|
Name |
Accession |
Description |
Interval |
E-value |
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
1-239 |
9.17e-163 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 449.44 E-value: 9.17e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 1 MIEIENVRKSFSSLEVLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGTDVHAKGTDLNRLRRKVG 80
Cdd:COG1126 1 MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKKDINKLRRKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 81 IVFQQWNAFPHLTVLENVMLAPRKVLGLPKDKAEEIAVKQLTHVGLGEKLKVYPNRMSGGQQQRMAIARALAMSPEYMLF 160
Cdd:COG1126 81 MVFQQFNLFPHLTVLENVTLAPIKVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKVMLF 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499282096 161 DEVTSALDPMLVGEVLDTLKMLAEEGMTMICVTHEMTFARDVSDRVAFFHQGIMAEIGSPDQIFASPQNPETQKFLASV 239
Cdd:COG1126 161 DEPTSALDPELVGEVLDVMRDLAKEGMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFENPQHERTRAFLSKV 239
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
2-212 |
2.27e-126 |
|
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: 356.45 E-value: 2.27e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 2 IEIENVRKSFSSLEVLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGTDVHAKGTDLNRLRRKVGI 81
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNINELRQKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 82 VFQQWNAFPHLTVLENVMLAPRKVLGLPKDKAEEIAVKQLTHVGLGEKLKVYPNRMSGGQQQRMAIARALAMSPEYMLFD 161
Cdd:cd03262 81 VFQQFNLFPHLTVLENITLAPIKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 499282096 162 EVTSALDPMLVGEVLDTLKMLAEEGMTMICVTHEMTFARDVSDRVAFFHQG 212
Cdd:cd03262 161 EPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDG 211
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
1-240 |
4.20e-123 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 349.87 E-value: 4.20e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 1 MIEIENVRKSFSSLEVLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGTDVHAKGT---------- 70
Cdd:COG4598 8 ALEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIRLKPDrdgelvpadr 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 71 -DLNRLRRKVGIVFQQWNAFPHLTVLENVMLAPRKVLGLPKDKAEEIAVKQLTHVGLGEKLKVYPNRMSGGQQQRMAIAR 149
Cdd:COG4598 88 rQLQRIRTRLGMVFQSFNLWSHMTVLENVIEAPVHVLGRPKAEAIERAEALLAKVGLADKRDAYPAHLSGGQQQRAAIAR 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 150 ALAMSPEYMLFDEVTSALDPMLVGEVLDTLKMLAEEGMTMICVTHEMTFARDVSDRVAFFHQGIMAEIGSPDQIFASPQN 229
Cdd:COG4598 168 ALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEEGRTMLVVTHEMGFARDVSSHVVFLHQGRIEEQGPPAEVFGNPKS 247
|
250
....*....|.
gi 499282096 230 PETQKFLASVR 240
Cdd:COG4598 248 ERLRQFLSSSL 258
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1-240 |
2.61e-109 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 314.34 E-value: 2.61e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 1 MIEIENVRKSFSSLEVLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGTDVHAKGTDLNRLRRKVG 80
Cdd:PRK09493 1 MIEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLIRQEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 81 IVFQQWNAFPHLTVLENVMLAPRKVLGLPKDKAEEIAVKQLTHVGLGEKLKVYPNRMSGGQQQRMAIARALAMSPEYMLF 160
Cdd:PRK09493 81 MVFQQFYLFPHLTALENVMFGPLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 161 DEVTSALDPMLVGEVLDTLKMLAEEGMTMICVTHEMTFARDVSDRVAFFHQGIMAEIGSPDQIFASPQNPETQKFLASVR 240
Cdd:PRK09493 161 DEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPPSQRLQEFLQHVS 240
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-236 |
2.36e-98 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 287.03 E-value: 2.36e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 1 MIEIENVRKSFSSLEVLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRI-----VIDGTDVHAKGTDLNR- 74
Cdd:PRK11264 3 AIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIrvgdiTIDTARSLSQQKGLIRq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 75 LRRKVGIVFQQWNAFPHLTVLENVMLAPRKVLGLPKDKAEEIAVKQLTHVGLGEKLKVYPNRMSGGQQQRMAIARALAMS 154
Cdd:PRK11264 83 LRQHVGFVFQNFNLFPHRTVLENIIEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 155 PEYMLFDEVTSALDPMLVGEVLDTLKMLAEEGMTMICVTHEMTFARDVSDRVAFFHQGIMAEIGSPDQIFASPQNPETQK 234
Cdd:PRK11264 163 PEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADPQQPRTRQ 242
|
..
gi 499282096 235 FL 236
Cdd:PRK11264 243 FL 244
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-236 |
3.05e-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: 258.37 E-value: 3.05e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 1 MIEIENVRKSFSSLEVLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGTDVH-AKGTDLNRLRRKV 79
Cdd:COG1127 5 MIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITgLSEKELYELRRRI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 80 GIVFQQwNA-FPHLTVLENVMLAPRKVLGLPKDKAEEIAVKQLTHVGLGEKLKVYPNRMSGGQQQRMAIARALAMSPEYM 158
Cdd:COG1127 85 GMLFQG-GAlFDSLTVFENVAFPLREHTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDPEIL 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499282096 159 LFDEVTSALDPMLVGEVLDTLKMLAEE-GMTMICVTHEMTFARDVSDRVAFFHQGIMAEIGSPDQIFASPqNPETQKFL 236
Cdd:COG1127 164 LYDEPTAGLDPITSAVIDELIRELRDElGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLASD-DPWVRQFL 241
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1-239 |
4.68e-87 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 261.17 E-value: 4.68e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 1 MIEIENVRKSFSS----LEVLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGTDVHA-KGTDLNRL 75
Cdd:COG1135 1 MIELENLSKTFPTkggpVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTAlSERELRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 76 RRKVGIVFQQWNAFPHLTVLENVMLaPRKVLGLPKDKAEEIAVKQLTHVGLGEKLKVYPNRMSGGQQQRMAIARALAMSP 155
Cdd:COG1135 81 RRKIGMIFQHFNLLSSRTVAENVAL-PLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 156 EYMLFDEVTSALDPMLVGEVLDTLKMLAEE-GMTMICVTHEMTFARDVSDRVAFFHQGIMAEIGSPDQIFASPQNPETQK 234
Cdd:COG1135 160 KVLLCDEATSALDPETTRSILDLLKDINRElGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVLDVFANPQSELTRR 239
|
....*
gi 499282096 235 FLASV 239
Cdd:COG1135 240 FLPTV 244
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
2-237 |
4.53e-86 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 256.05 E-value: 4.53e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 2 IEIENVRKSFSSLEVLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGTDVH-----------AKGT 70
Cdd:PRK10619 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgqlkvADKN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 71 DLNRLRRKVGIVFQQWNAFPHLTVLENVMLAPRKVLGLPKDKAEEIAVKQLTHVGLGEKLKV-YPNRMSGGQQQRMAIAR 149
Cdd:PRK10619 86 QLRLLRTRLTMVFQHFNLWSHMTVLENVMEAPIQVLGLSKQEARERAVKYLAKVGIDERAQGkYPVHLSGGQQQRVSIAR 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 150 ALAMSPEYMLFDEVTSALDPMLVGEVLDTLKMLAEEGMTMICVTHEMTFARDVSDRVAFFHQGIMAEIGSPDQIFASPQN 229
Cdd:PRK10619 166 ALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGNPQS 245
|
....*...
gi 499282096 230 PETQKFLA 237
Cdd:PRK10619 246 PRLQQFLK 253
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-216 |
5.34e-81 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 241.87 E-value: 5.34e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 1 MIEIENVRKSFSS----LEVLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGTDVHA-KGTDLNRL 75
Cdd:COG1136 4 LLELRNLTKSYGTgegeVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSlSERELARL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 76 RR-KVGIVFQQWNAFPHLTVLENVMLaPRKVLGLPKDKAEEIAVKQLTHVGLGEKLKVYPNRMSGGQQQRMAIARALAMS 154
Cdd:COG1136 84 RRrHIGFVFQFFNLLPELTALENVAL-PLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNR 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499282096 155 PEYMLFDEVTSALDPMLVGEVLDTLKMLAEE-GMTMICVTHEMTFARdVSDRVAFFHQGIMAE 216
Cdd:COG1136 163 PKLILADEPTGNLDSKTGEEVLELLRELNRElGTTIVMVTHDPELAA-RADRVIRLRDGRIVS 224
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1-228 |
3.66e-80 |
|
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: 240.18 E-value: 3.66e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 1 MIEIENVRKSFSS----LEVLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGTDVHA-KGTDLNRL 75
Cdd:cd03258 1 MIELKNVSKVFGDtggkVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLlSGKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 76 RRKVGIVFQQWNAFPHLTVLENVMLaPRKVLGLPKDKAEEIAVKQLTHVGLGEKLKVYPNRMSGGQQQRMAIARALAMSP 155
Cdd:cd03258 81 RRRIGMIFQHFNLLSSRTVFENVAL-PLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNP 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499282096 156 EYMLFDEVTSALDPMLVGEVLDTLKMLAEE-GMTMICVTHEMTFARDVSDRVAFFHQGIMAEIGSPDQIFASPQ 228
Cdd:cd03258 160 KVLLCDEATSALDPETTQSILALLRDINRElGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFANPQ 233
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
2-212 |
7.59e-80 |
|
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: 238.93 E-value: 7.59e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 2 IEIENVRKSFSS----LEVLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGTDVH-AKGTDLNRLR 76
Cdd:cd03255 1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISkLSEKELAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 77 RK-VGIVFQQWNAFPHLTVLENVMLAPRkVLGLPKDKAEEIAVKQLTHVGLGEKLKVYPNRMSGGQQQRMAIARALAMSP 155
Cdd:cd03255 81 RRhIGFVFQSFNLLPDLTALENVELPLL-LAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDP 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 499282096 156 EYMLFDEVTSALDPMLVGEVLDTLKMLAEE-GMTMICVTHEMTFARDvSDRVAFFHQG 212
Cdd:cd03255 160 KIILADEPTGNLDSETGKEVMELLRELNKEaGTTIVVVTHDPELAEY-ADRIIELRDG 216
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-236 |
7.95e-80 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 243.47 E-value: 7.95e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 1 MIEIENVRKSFSSLEVLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGTDVhakgTDLNRLRRKVG 80
Cdd:COG3842 5 ALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDV----TGLPPEKRNVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 81 IVFQQWNAFPHLTVLENVMLAPRkVLGLPKDKAEEIAVKQLTHVGLGEKLKVYPNRMSGGQQQRMAIARALAMSPEYMLF 160
Cdd:COG3842 81 MVFQDYALFPHLTVAENVAFGLR-MRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 161 DEVTSALDPMLVGEVLDTLK-MLAEEGMTMICVTH---E-MTfardVSDRVAFFHQGIMAEIGSPDQIFASPQNPETQKF 235
Cdd:COG3842 160 DEPLSALDAKLREEMREELRrLQRELGITFIYVTHdqeEaLA----LADRIAVMNDGRIEQVGTPEEIYERPATRFVADF 235
|
.
gi 499282096 236 L 236
Cdd:COG3842 236 I 236
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
2-235 |
1.34e-79 |
|
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: 238.56 E-value: 1.34e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 2 IEIENVRKSFSSLEVLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGTDVHA-KGTDLNRLRRKVG 80
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGlSEAELYRLRRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 81 IVFQQWNAFPHLTVLENVMLAPRKVLGLPKDKAEEIAVKQLTHVGLGEKLKVYPNRMSGGQQQRMAIARALAMSPEYMLF 160
Cdd:cd03261 81 MLFQSGALFDSLTVFENVAFPLREHTRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLY 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499282096 161 DEVTSALDPMLVGEVLDTLKMLAEE-GMTMICVTHEMTFARDVSDRVAFFHQGIMAEIGSPDQIFASpQNPETQKF 235
Cdd:cd03261 161 DEPTAGLDPIASGVIDDLIRSLKKElGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRAS-DDPLVRQF 235
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-239 |
8.95e-79 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 245.58 E-value: 8.95e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 1 MIEIENVRKSFSS-----LEVLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGTDV-HAKGTDLNR 74
Cdd:COG1123 260 LLEVRNLSKRYPVrgkggVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLtKLSRRSLRE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 75 LRRKVGIVFQQWNA--FPHLTVLENVMLAPRKVLGLPKDKAEEIAVKQLTHVGLGEKLK-VYPNRMSGGQQQRMAIARAL 151
Cdd:COG1123 340 LRRRVQMVFQDPYSslNPRMTVGDIIAEPLRLHGLLSRAERRERVAELLERVGLPPDLAdRYPHELSGGQRQRVAIARAL 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 152 AMSPEYMLFDEVTSALDPMLVGEVLDTLKMLAEE-GMTMICVTHEMTFARDVSDRVAFFHQGIMAEIGSPDQIFASPQNP 230
Cdd:COG1123 420 ALEPKLLILDEPTSALDVSVQAQILNLLRDLQRElGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVFANPQHP 499
|
....*....
gi 499282096 231 ETQKFLASV 239
Cdd:COG1123 500 YTRALLAAV 508
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
2-237 |
1.27e-77 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 234.14 E-value: 1.27e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 2 IEIENVRKSFSSLEVLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDG------TDVHAKgtDLNRL 75
Cdd:COG4161 3 IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGhqfdfsQKPSEK--AIRLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 76 RRKVGIVFQQWNAFPHLTVLENVMLAPRKVLGLPKDKAEEIAVKQLTHVGLGEKLKVYPNRMSGGQQQRMAIARALAMSP 155
Cdd:COG4161 81 RQKVGMVFQQYNLWPHLTVMENLIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 156 EYMLFDEVTSALDPMLVGEVLDTLKMLAEEGMTMICVTHEMTFARDVSDRVAFFHQGIMAEIGSPDqIFASPQNPETQKF 235
Cdd:COG4161 161 QVLLFDEPTAALDPEITAQVVEIIRELSQTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQGDAS-HFTQPQTEAFAHY 239
|
..
gi 499282096 236 LA 237
Cdd:COG4161 240 LS 241
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2-236 |
6.43e-77 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 232.62 E-value: 6.43e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 2 IEIENVRKSFSSLEVLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGL-EPID----SGRIVIDGTDVHAKGTDLNRLR 76
Cdd:COG1117 12 IEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMnDLIPgarvEGEILLDGEDIYDPDVDVVELR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 77 RKVGIVFQQWNAFPHlTVLENVMLAPRKVLGLPKDKAEEIAVKQLTHVGLGE----KLKVYPNRMSGGQQQRMAIARALA 152
Cdd:COG1117 92 RRVGMVFQKPNPFPK-SIYDNVAYGLRLHGIKSKSELDEIVEESLRKAALWDevkdRLKKSALGLSGGQQQRLCIARALA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 153 MSPEYMLFDEVTSALDPMLVGEVLDTLKMLAEEgMTMICVTHEMTFARDVSDRVAFFHQGIMAEIGSPDQIFASPQNPET 232
Cdd:COG1117 171 VEPEVLLMDEPTSALDPISTAKIEELILELKKD-YTIVIVTHNMQQAARVSDYTAFFYLGELVEFGPTEQIFTNPKDKRT 249
|
....
gi 499282096 233 QKFL 236
Cdd:COG1117 250 EDYI 253
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
2-225 |
3.68e-75 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 227.22 E-value: 3.68e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 2 IEIENVrkSFS---SLEVLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGTDVHAKgtDLNRLRRK 78
Cdd:COG1122 1 IELENL--SFSypgGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKK--NLRELRRK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 79 VGIVFQqwnaFP-----HLTVLENVMLAPRKvLGLPKDKAEEIAVKQLTHVGLGEKLKVYPNRMSGGQQQRMAIARALAM 153
Cdd:COG1122 77 VGLVFQ----NPddqlfAPTVEEDVAFGPEN-LGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAM 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499282096 154 SPEYMLFDEVTSALDPMLVGEVLDTLKMLAEEGMTMICVTHEMTFARDVSDRVAFFHQGIMAEIGSPDQIFA 225
Cdd:COG1122 152 EPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFS 223
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
1-206 |
3.72e-75 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 228.02 E-value: 3.72e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 1 MIEIENVRKSF-SSLEVLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGTDV-HAKGTDLNRLRRK 78
Cdd:COG3638 2 MLELRNLSKRYpGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVtALRGRALRRLRRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 79 VGIVFQQWNAFPHLTVLENVML-------APRKVLGL--PKDKaeEIAVKQLTHVGLGEKLKVYPNRMSGGQQQRMAIAR 149
Cdd:COG3638 82 IGMIFQQFNLVPRLSVLTNVLAgrlgrtsTWRSLLGLfpPEDR--ERALEALERVGLADKAYQRADQLSGGQQQRVAIAR 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 499282096 150 ALAMSPEYMLFDEVTSALDPMLVGEVLDTLKMLAEE-GMTMICVTHEMTFARDVSDRV 206
Cdd:COG3638 160 ALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREdGITVVVNLHQVDLARRYADRI 217
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-240 |
1.51e-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: 226.22 E-value: 1.51e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 1 MIEIENVRKSFSS----LEVLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGTDVHAKgtDLNRLR 76
Cdd:COG1124 1 MLEVRNLSVSYGQggrrVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRR--RRKAFR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 77 RKVGIVFQQ-WNAF-PHLTVLEnVMLAPRKVLGLPkDKAEEIAvKQLTHVGLGEK-LKVYPNRMSGGQQQRMAIARALAM 153
Cdd:COG1124 79 RRVQMVFQDpYASLhPRHTVDR-ILAEPLRIHGLP-DREERIA-ELLEQVGLPPSfLDRYPHQLSGGQRQRVAIARALIL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 154 SPEYMLFDEVTSALDPMLVGEVLDTLKML-AEEGMTMICVTHEMTFARDVSDRVAFFHQGIMAEIGSPDQIFASPQNPET 232
Cdd:COG1124 156 EPELLLLDEPTSALDVSVQAEILNLLKDLrEERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAGPKHPYT 235
|
....*...
gi 499282096 233 QKFLASVR 240
Cdd:COG1124 236 RELLAASL 243
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
2-223 |
8.81e-74 |
|
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: 223.60 E-value: 8.81e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 2 IEIENVRKSFSSLEVLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPI-----DSGRIVIDGTDVHAKGTDLNRLR 76
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLipgapDEGEVLLDGKDIYDLDVDVLELR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 77 RKVGIVFQQWNAFPhLTVLENVMLAPRKVLGLPKDKAEEIAVKQLTHVGLGEKLK--VYPNRMSGGQQQRMAIARALAMS 154
Cdd:cd03260 81 RRVGMVFQKPNPFP-GSIYDNVAYGLRLHGIKLKEELDERVEEALRKAALWDEVKdrLHALGLSGGQQQRLCLARALANE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499282096 155 PEYMLFDEVTSALDPMLVGEVLDTLKMLAEEgMTMICVTHEMTFARDVSDRVAFFHQGIMAEIGSPDQI 223
Cdd:cd03260 160 PEVLLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
2-237 |
7.63e-73 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 221.81 E-value: 7.63e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 2 IEIENVRKSFSSLEVLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDG------TDVHAKgtDLNRL 75
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGnhfdfsKTPSDK--AIREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 76 RRKVGIVFQQWNAFPHLTVLENVMLAPRKVLGLPKDKAEEIAVKQLTHVGLGEKLKVYPNRMSGGQQQRMAIARALAMSP 155
Cdd:PRK11124 81 RRNVGMVFQQYNLWPHLTVQQNLIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 156 EYMLFDEVTSALDPMLVGEVLDTLKMLAEEGMTMICVTHEMTFARDVSDRVAFFHQGIMAEIGSPDQiFASPQNPETQKF 235
Cdd:PRK11124 161 QVLLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTHEVEVARKTASRVVYMENGHIVEQGDASC-FTQPQTEAFKNY 239
|
..
gi 499282096 236 LA 237
Cdd:PRK11124 240 LS 241
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1-239 |
3.33e-72 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 223.52 E-value: 3.33e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 1 MIEIENVRKSFS----SLEVLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGTDVHA-KGTDLNRL 75
Cdd:PRK11153 1 MIELKNISKVFPqggrTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTAlSEKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 76 RRKVGIVFQQWNAFPHLTVLENVMLaPRKVLGLPKDKAEEIAVKQLTHVGLGEKLKVYPNRMSGGQQQRMAIARALAMSP 155
Cdd:PRK11153 81 RRQIGMIFQHFNLLSSRTVFDNVAL-PLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 156 EYMLFDEVTSALDPMLVGEVLDTLKMLAEE-GMTMICVTHEMTFARDVSDRVAFFHQGIMAEIGSPDQIFASPQNPETQK 234
Cdd:PRK11153 160 KVLLCDEATSALDPATTRSILELLKDINRElGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHPKHPLTRE 239
|
....*
gi 499282096 235 FLASV 239
Cdd:PRK11153 240 FIQST 244
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
2-218 |
7.32e-72 |
|
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: 218.16 E-value: 7.32e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 2 IEIENVRKSFSSLEVLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGTDVhakgTDLNRLRRKVGI 81
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDV----TGVPPERRNIGM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 82 VFQQWNAFPHLTVLENVMLAPRkVLGLPKDKAEEIAVKQLTHVGLGEKLKVYPNRMSGGQQQRMAIARALAMSPEYMLFD 161
Cdd:cd03259 77 VFQDYALFPHLTVAENIAFGLK-LRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 499282096 162 EVTSALDPMLVGEVLDTLK-MLAEEGMTMICVTHEMTFARDVSDRVAFFHQGIMAEIG 218
Cdd:cd03259 156 EPLSALDAKLREELREELKeLQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
2-236 |
8.58e-71 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 220.02 E-value: 8.58e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 2 IEIENVRKSFSSLEVLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGTDVHakgTDLNRLRRKVGI 81
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLF---TNLPPRERRVGF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 82 VFQQWNAFPHLTVLENVMLAPRkVLGLPKDKAEEIAVKQLTHVGLGEKLKVYPNRMSGGQQQRMAIARALAMSPEYMLFD 161
Cdd:COG1118 80 VFQHYALFPHMTVAENIAFGLR-VRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLLLD 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499282096 162 EVTSALDPMLVGEVLDTL-KMLAEEGMTMICVTHEMTFARDVSDRVAFFHQGIMAEIGSPDQIFASPQNPETQKFL 236
Cdd:COG1118 159 EPFGALDAKVRKELRRWLrRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDRPATPFVARFL 234
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-206 |
1.09e-70 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 216.88 E-value: 1.09e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 1 MIEIENVRKSFSS----LEVLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGTDVHAKGTDlnrlr 76
Cdd:COG1116 7 ALELRGVSKRFPTggggVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPD----- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 77 rkVGIVFQQWNAFPHLTVLENVMLAPRkVLGLPKDKAEEIAVKQLTHVGLGEKLKVYPNRMSGGQQQRMAIARALAMSPE 156
Cdd:COG1116 82 --RGVVFQEPALLPWLTVLDNVALGLE-LRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPE 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 499282096 157 YMLFDEVTSALDPMLVGEVLDTL-KMLAEEGMTMICVTHemtfarDV------SDRV 206
Cdd:COG1116 159 VLLMDEPFGALDALTRERLQDELlRLWQETGKTVLFVTH------DVdeavflADRV 209
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-229 |
2.89e-70 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 218.79 E-value: 2.89e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 1 MIEIENVRKSFSSLEVLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGTDVhakgTDLNRLRRKVG 80
Cdd:COG3839 3 SLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDV----TDLPPKDRNIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 81 IVFQQWNAFPHLTVLENvMLAPRKVLGLPKDKAEEIAVKQLTHVGLGEKLKVYPNRMSGGQQQRMAIARALAMSPEYMLF 160
Cdd:COG3839 79 MVFQSYALYPHMTVYEN-IAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFLL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499282096 161 DEVTSALDPMLVGEVLDTLKML-AEEGMTMICVTHE----MTFArdvsDRVAFFHQGIMAEIGSPDQIFASPQN 229
Cdd:COG3839 158 DEPLSNLDAKLRVEMRAEIKRLhRRLGTTTIYVTHDqveaMTLA----DRIAVMNDGRIQQVGTPEELYDRPAN 227
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
2-212 |
5.28e-69 |
|
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: 209.74 E-value: 5.28e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 2 IEIENVRKSFSSLEVLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGTDVHAKGTDLNRLRRKVGI 81
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPPLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 82 VFQQWNAFPHLTVLENVMLAprkvlglpkdkaeeiavkqlthvglgeklkvypnrMSGGQQQRMAIARALAMSPEYMLFD 161
Cdd:cd03229 81 VFQDFALFPHLTVLENIALG-----------------------------------LSGGQQQRVALARALAMDPDVLLLD 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 499282096 162 EVTSALDPMLVGEVLDTLKMLAEE-GMTMICVTHEMTFARDVSDRVAFFHQG 212
Cdd:cd03229 126 EPTSALDPITRREVRALLKSLQAQlGITVVLVTHDLDEAARLADRVVVLRDG 177
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1-218 |
1.39e-68 |
|
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: 210.44 E-value: 1.39e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 1 MIEIENVRKSF----SSLEVLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGTDVHAKGTDLNRLR 76
Cdd:cd03257 1 LLEVKNLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 77 RK-VGIVFQqwNAF----PHLTVLENVMLAPRKVLGLPKDKAEEIAVKQ-LTHVGLGEK-LKVYPNRMSGGQQQRMAIAR 149
Cdd:cd03257 81 RKeIQMVFQ--DPMsslnPRMTIGEQIAEPLRIHGKLSKKEARKEAVLLlLVGVGLPEEvLNRYPHELSGGQRQRVAIAR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 150 ALAMSPEYMLFDEVTSALDPMLVGEVLDTLKMLAEE-GMTMICVTHEMTFARDVSDRVAFFHQGIMAEIG 218
Cdd:cd03257 159 ALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEElGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
3-212 |
1.98e-67 |
|
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: 206.93 E-value: 1.98e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 3 EIENVRKSFSSLE--VLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGTDVHAkgTDLNRLRRKVG 80
Cdd:cd03225 1 ELKNLSFSYPDGArpALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTK--LSLKELRRKVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 81 IVFQqwNA---FPHLTVLENVMLAPRKvLGLPKDKAEEIAVKQLTHVGLGEKLKVYPNRMSGGQQQRMAIARALAMSPEY 157
Cdd:cd03225 79 LVFQ--NPddqFFGPTVEEEVAFGLEN-LGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDI 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 499282096 158 MLFDEVTSALDPMLVGEVLDTLKMLAEEGMTMICVTHEMTFARDVSDRVAFFHQG 212
Cdd:cd03225 156 LLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDG 210
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
2-223 |
3.93e-67 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 206.84 E-value: 3.93e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 2 IEIENVRKSFSSLEVLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGTDVHakgTDLNRLRRKVGI 81
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVA---RDPAEVRRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 82 VFQQWNAFPHLTVLENVMLApRKVLGLPKDKAEEIAVKQLTHVGLGEKLKVYPNRMSGGQQQRMAIARALAMSPEYMLFD 161
Cdd:COG1131 78 VPQEPALYPDLTVRENLRFF-ARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILD 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499282096 162 EVTSALDPMLVGEVLDTLKMLAEEGMTMICVTHEMTFARDVSDRVAFFHQGIMAEIGSPDQI 223
Cdd:COG1131 157 EPTSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDEL 218
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
2-240 |
6.36e-67 |
|
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: 206.77 E-value: 6.36e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 2 IEIENVRKSFSSLE-VLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGL-EPiDSGRIVIDGTDVHAkgTDLNRLRRKV 79
Cdd:cd03295 1 IEFENVTKRYGGGKkAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLiEP-TSGEIFIDGEDIRE--QDPVELRRKI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 80 GIVFQQWNAFPHLTVLENVMLAPrKVLGLPKDKAEEIAVKQLTHVGLGEK--LKVYPNRMSGGQQQRMAIARALAMSPEY 157
Cdd:cd03295 78 GYVIQQIGLFPHMTVEENIALVP-KLLKWPKEKIRERADELLALVGLDPAefADRYPHELSGGQQQRVGVARALAADPPL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 158 MLFDEVTSALDPMLVGEVLDTLKMLAEE-GMTMICVTHEMTFARDVSDRVAFFHQGIMAEIGSPDQIFASPQNPETQKFL 236
Cdd:cd03295 157 LLMDEPFGALDPITRDQLQEEFKRLQQElGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDFVAEFV 236
|
....
gi 499282096 237 ASVR 240
Cdd:cd03295 237 GADR 240
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1-216 |
5.85e-66 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 203.75 E-value: 5.85e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 1 MIEIENVRKSFS-SLEVLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGTDVHA-KGTDLNRLRRK 78
Cdd:COG2884 1 MIRFENVSKRYPgGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRlKRREIPYLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 79 VGIVFQQWNAFPHLTVLENVMLaPRKVLGLPKDKAEEIAVKQLTHVGLGEKLKVYPNRMSGGQQQRMAIARALAMSPEYM 158
Cdd:COG2884 81 IGVVFQDFRLLPDRTVYENVAL-PLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 499282096 159 LFDEVTSALDPMLVGEVLDTLKMLAEEGMTMICVTHEMTFARDVSDRVAFFHQGIMAE 216
Cdd:COG2884 160 LADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLELVDRMPKRVLELEDGRLVR 217
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
2-229 |
3.21e-65 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 202.08 E-value: 3.21e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 2 IEIENVRKSFSSLEVLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGTDVHakgtDLNRLRRKVGI 81
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDIT----NLPPHKRPVNT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 82 VFQQWNAFPHLTVLENVMLaPRKVLGLPKDKAEEIAVKQLTHVGLGEKLKVYPNRMSGGQQQRMAIARALAMSPEYMLFD 161
Cdd:cd03300 77 VFQNYALFPHLTVFENIAF-GLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLD 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499282096 162 EVTSALDPMLVGEVLDTLKMLAEE-GMTMICVTHEMTFARDVSDRVAFFHQGIMAEIGSPDQIFASPQN 229
Cdd:cd03300 156 EPLGALDLKLRKDMQLELKRLQKElGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPAN 224
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
2-206 |
3.86e-65 |
|
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: 202.03 E-value: 3.86e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 2 IEIENVRKSFSSL-EVLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGTDVHA-KGTDLNRLRRKV 79
Cdd:cd03256 1 IEVENLSKTYPNGkKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKlKGKALRQLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 80 GIVFQQWNAFPHLTVLENVMLAP-------RKVLGLPKDKAEEIAVKQLTHVGLGEKLKVYPNRMSGGQQQRMAIARALA 152
Cdd:cd03256 81 GMIFQQFNLIERLSVLENVLSGRlgrrstwRSLFGLFPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIARALM 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 499282096 153 MSPEYMLFDEVTSALDPMLVGEVLDTLKMLA-EEGMTMICVTHEMTFARDVSDRV 206
Cdd:cd03256 161 QQPKLILADEPVASLDPASSRQVMDLLKRINrEEGITVIVSLHQVDLAREYADRI 215
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
2-207 |
1.30e-64 |
|
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: 200.01 E-value: 1.30e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 2 IEIENVRKSFSS----LEVLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGTDVhakgtdlNRLRR 77
Cdd:cd03293 1 LEVRNVSKTYGGgggaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPV-------TGPGP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 78 KVGIVFQQWNAFPHLTVLENVMLAPrKVLGLPKDKAEEIAVKQLTHVGLGEKLKVYPNRMSGGQQQRMAIARALAMSPEY 157
Cdd:cd03293 74 DRGYVFQQDALLPWLTVLDNVALGL-ELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDV 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 499282096 158 MLFDEVTSALDPM---LVGEVLdtLKMLAEEGMTMICVTHEMTFARDVSDRVA 207
Cdd:cd03293 153 LLLDEPFSALDALtreQLQEEL--LDIWRETGKTVLLVTHDIDEAVFLADRVV 203
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
5-239 |
1.39e-63 |
|
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: 199.02 E-value: 1.39e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 5 ENVRKSFSSLEVLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGTDVHA-KGTDLNRLRRK-VGIV 82
Cdd:cd03294 28 EEILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAmSRKELRELRRKkISMV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 83 FQQWNAFPHLTVLENVMLaPRKVLGLPKDKAEEIAVKQLTHVGLGEKLKVYPNRMSGGQQQRMAIARALAMSPEYMLFDE 162
Cdd:cd03294 108 FQSFALLPHRTVLENVAF-GLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDE 186
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499282096 163 VTSALDPMLVGEVLDT-LKMLAEEGMTMICVTHEMTFARDVSDRVAFFHQGIMAEIGSPDQIFASPQNPETQKFLASV 239
Cdd:cd03294 187 AFSALDPLIRREMQDElLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDYVREFFRGV 264
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1-236 |
3.23e-63 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 196.90 E-value: 3.23e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 1 MIEIENVRKSFSSLevLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGTDVhakgTDLNRLRRKVG 80
Cdd:COG3840 1 MLRLDDLTYRYGDF--PLRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDL----TALPPAERPVS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 81 IVFQQWNAFPHLTVLENVMLAPRKVLGL---PKDKAEEIAVKqlthVGLGEKLKVYPNRMSGGQQQRMAIARALAMSPEY 157
Cdd:COG3840 75 MLFQENNLFPHLTVAQNIGLGLRPGLKLtaeQRAQVEQALER----VGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 158 MLFDEVTSALDPMLVGEVLDTLKMLAEE-GMTMICVTHEMTFARDVSDRVAFFHQGIMAEIGSPDQIFASPQNPETQKFL 236
Cdd:COG3840 151 LLLDEPFSALDPALRQEMLDLVDELCRErGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPPALAAYL 230
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-239 |
4.59e-63 |
|
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: 199.51 E-value: 4.59e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 1 MIEIENVRKSFSS----LEVLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEP---IDSGRIVIDGTDV-HAKGTDL 72
Cdd:COG0444 1 LLEVRNLKVYFPTrrgvVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPppgITSGEILFDGEDLlKLSEKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 73 NRLR-RKVGIVFQqwNAF----PHLTVLENVMLAPRKVLGLPKDKAEEIAVKQLTHVGL---GEKLKVYPNRMSGGQQQR 144
Cdd:COG0444 81 RKIRgREIQMIFQ--DPMtslnPVMTVGDQIAEPLRIHGGLSKAEARERAIELLERVGLpdpERRLDRYPHELSGGMRQR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 145 MAIARALAMSPEYMLFDEVTSALDPMLVGEVLDTLKMLAEE-GMTMICVTHEMTFARDVSDRVAFFHQGIMAEIGSPDQI 223
Cdd:COG0444 159 VMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRElGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGPVEEL 238
|
250
....*....|....*.
gi 499282096 224 FASPQNPETQKFLASV 239
Cdd:COG0444 239 FENPRHPYTRALLSSI 254
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
1-223 |
5.69e-62 |
|
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: 194.05 E-value: 5.69e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 1 MIEIENVRKSFSS-LEVLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGTDV-HAKGTDLNRLRRK 78
Cdd:TIGR02315 1 MLEVENLSKVYPNgKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDItKLRGKKLRKLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 79 VGIVFQQWNAFPHLTVLENVMLAP-------RKVLGLPKDKAEEIAVKQLTHVGLGEKLKVYPNRMSGGQQQRMAIARAL 151
Cdd:TIGR02315 81 IGMIFQHYNLIERLTVLENVLHGRlgykptwRSLLGRFSEEDKERALSALERVGLADKAYQRADQLSGGQQQRVAIARAL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499282096 152 AMSPEYMLFDEVTSALDPMLVGEVLDTLKMLAEE-GMTMICVTHEMTFARDVSDRVAFFHQGIMAEIGSPDQI 223
Cdd:TIGR02315 161 AQQPDLILADEPIASLDPKTSKQVMDYLKRINKEdGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSEL 233
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
2-228 |
4.79e-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: 4.79e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 2 IEIENVRKSFSSLEVLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGTDVHAKGTDLnRLRRKVGI 81
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHE-IARLGIGR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 82 VFQQWNAFPHLTVLENVMLAPRKVLGLP---------KDKAEEIAVKQLTHVGLGEKLKVYPNRMSGGQQQRMAIARALA 152
Cdd:cd03219 80 TFQIPRLFPELTVLENVMVAAQARTGSGlllararreEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499282096 153 MSPEYMLFDEVTSALDPMLVGEVLDTLKMLAEEGMTMICVTHEMTFARDVSDRVAFFHQG-IMAEiGSPDQIFASPQ 228
Cdd:cd03219 160 TDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGrVIAE-GTPDEVRNNPR 235
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-228 |
1.18e-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: 198.59 E-value: 1.18e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 1 MIEIENVRKSFSS--LEVLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPID---SGRIVIDGTDVhaKGTDLNRL 75
Cdd:COG1123 4 LLEVRDLSVRYPGgdVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDL--LELSEALR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 76 RRKVGIVFQQ-WNAFPHLTVLENVMLAPRkVLGLPKDKAEEIAVKQLTHVGLGEKLKVYPNRMSGGQQQRMAIARALAMS 154
Cdd:COG1123 82 GRRIGMVFQDpMTQLNPVTVGDQIAEALE-NLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALD 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499282096 155 PEYMLFDEVTSALDPMLVGEVLDTLKML-AEEGMTMICVTHEMTFARDVSDRVAFFHQGIMAEIGSPDQIFASPQ 228
Cdd:COG1123 161 PDLLIADEPTTALDVTTQAEILDLLRELqRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAPQ 235
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
2-228 |
2.50e-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 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: 191.13 E-value: 2.50e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 2 IEIENVrkSF-----SSLEV--LKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGTDVHA-KGTDLN 73
Cdd:TIGR04521 1 IKLKNV--SYiyqpgTPFEKkaLDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAkKKKKLK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 74 RLRRKVGIVFQqwnaFPH-----LTVLENVMLAPRKvLGLPKDKAEEIAVKQLTHVGLGEKLK-VYPNRMSGGQQQRMAI 147
Cdd:TIGR04521 79 DLRKKVGLVFQ----FPEhqlfeETVYKDIAFGPKN-LGLSEEEAEERVKEALELVGLDEEYLeRSPFELSGGQMRRVAI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 148 ARALAMSPEYMLFDEVTSALDPMLVGEVLDTLKMLA-EEGMTMICVTHEMTFARDVSDRVAFFHQGIMAEIGSPDQIFAS 226
Cdd:TIGR04521 154 AGVLAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHkEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVFSD 233
|
..
gi 499282096 227 PQ 228
Cdd:TIGR04521 234 VD 235
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
2-238 |
8.16e-60 |
|
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: 188.70 E-value: 8.16e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 2 IEIENVRKSFSSLEVLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGTDVhakgTDLNRLRRKVGI 81
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDA----TDVPVQERNVGF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 82 VFQQWNAFPHLTVLENVM--LAPRKVLGLP-KDKAEEIAVKQLTHVGLGEKLKVYPNRMSGGQQQRMAIARALAMSPEYM 158
Cdd:cd03296 79 VFQHYALFRHMTVFDNVAfgLRVKPRSERPpEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 159 LFDEVTSALDPMLVGEVLDTLKMLAEE-GMTMICVTHEMTFARDVSDRVAFFHQGIMAEIGSPDQIFASPQNPETQKFLA 237
Cdd:cd03296 159 LLDEPFGALDAKVRKELRRWLRRLHDElHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPASPFVYSFLG 238
|
.
gi 499282096 238 S 238
Cdd:cd03296 239 E 239
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1-224 |
7.74e-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: 186.40 E-value: 7.74e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 1 MIEIENVRKSFSSLEVLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGTDVHAKGTdlNRLRRKVG 80
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSR--RELARRIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 81 IVFQQWNAFPHLTVLENVML--AP-RKVLGLPKDKAEEIAVKQLTHVGLGEKLKVYPNRMSGGQQQRMAIARALAMSPEY 157
Cdd:COG1120 79 YVPQEPPAPFGLTVRELVALgrYPhLGLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499282096 158 MLFDEVTSALDPMLVGEVLDTLKMLA-EEGMTMICVTHEMTFARDVSDRVAFFHQGIMAEIGSPDQIF 224
Cdd:COG1120 159 LLLDEPTSHLDLAHQLEVLELLRRLArERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEVL 226
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-228 |
3.05e-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: 184.86 E-value: 3.05e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 1 MIEIENVRKSFSSLEVLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGTDVHAKGTD-LNRLrrkv 79
Cdd:COG0411 4 LLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHrIARL---- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 80 GIV--FQQWNAFPHLTVLENVMLA---------PRKVLGLPKDKAEEIAVKQ-----LTHVGLGEKLKVYPNRMSGGQQQ 143
Cdd:COG0411 80 GIArtFQNPRLFPELTVLENVLVAaharlgrglLAALLRLPRARREEREAREraeelLERVGLADRADEPAGNLSYGQQR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 144 RMAIARALAMSPEYMLFDEVTSALDPMLVGEVLDTLKML-AEEGMTMICVTHEMTFARDVSDRVAFFHQG-IMAEiGSPD 221
Cdd:COG0411 160 RLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLrDERGITILLIEHDMDLVMGLADRIVVLDFGrVIAE-GTPA 238
|
....*..
gi 499282096 222 QIFASPQ 228
Cdd:COG0411 239 EVRADPR 245
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
2-236 |
3.27e-58 |
|
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: 184.46 E-value: 3.27e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 2 IEIENVRKSFSSLEvLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGTDVhakgTDLNRLRRKVGI 81
Cdd:cd03299 1 LKVENLSKDWKEFK-LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDI----TNLPPEKRDISY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 82 VFQQWNAFPHLTVLENVMLAPRKVLGLPKDKAEEiaVKQLTHV-GLGEKLKVYPNRMSGGQQQRMAIARALAMSPEYMLF 160
Cdd:cd03299 76 VPQNYALFPHMTVYKNIAYGLKKRKVDKKEIERK--VLEIAEMlGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499282096 161 DEVTSALDPMLVGEVLDTLKMLAEE-GMTMICVTHEMTFARDVSDRVAFFHQGIMAEIGSPDQIFASPQNPETQKFL 236
Cdd:cd03299 154 DEPFSALDVRTKEKLREELKKIRKEfGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPKNEFVAEFL 230
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-200 |
5.14e-58 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 183.79 E-value: 5.14e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 1 MIEIENVRKSFSS----LEVLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGTDVHAKGTD-LNRL 75
Cdd:COG4181 8 IIELRGLTKTVGTgageLTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDaRARL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 76 R-RKVGIVFQQWNAFPHLTVLENVMLaPRKVLGLPkdKAEEIAVKQLTHVGLGEKLKVYPNRMSGGQQQRMAIARALAMS 154
Cdd:COG4181 88 RaRHVGFVFQSFQLLPTLTALENVML-PLELAGRR--DARARARALLERVGLGHRLDHYPAQLSGGEQQRVALARAFATE 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 499282096 155 PEYMLFDEVTSALDPMLVGEVLDTL-KMLAEEGMTMICVTHEMTFAR 200
Cdd:COG4181 165 PAILFADEPTGNLDAATGEQIIDLLfELNRERGTTLVLVTHDPALAA 211
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
2-225 |
1.38e-57 |
|
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: 183.79 E-value: 1.38e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 2 IEIENVRKSF--SSLEVLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGTDVhAKGTDLNRLRRKV 79
Cdd:TIGR04520 1 IEVENVSFSYpeSEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDT-LDEENLWEIRKKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 80 GIVFQQW-NAFPHLTVLENVMLAPRKvLGLPKDKAEEIAVKQLTHVGLGEKLKVYPNRMSGGQQQRMAIARALAMSPEYM 158
Cdd:TIGR04520 80 GMVFQNPdNQFVGATVEDDVAFGLEN-LGVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLAMRPDII 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499282096 159 LFDEVTSALDPMLVGEVLDTLKML-AEEGMTMICVTHEMTFARDvSDRVAFFHQGIMAEIGSPDQIFA 225
Cdd:TIGR04520 159 ILDEATSMLDPKGRKEVLETIRKLnKEEGITVISITHDMEEAVL-ADRVIVMNKGKIVAEGTPREIFS 225
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
2-218 |
2.29e-57 |
|
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: 181.30 E-value: 2.29e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 2 IEIENVRKSFSSLEVLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGTDVhakgTDLNRLRRKVGI 81
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDV----TDLPPKDRDIAM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 82 VFQQWNAFPHLTVLENvMLAPRKVLGLPKDKAEEiAVKQLTHV-GLGEKLKVYPNRMSGGQQQRMAIARALAMSPEYMLF 160
Cdd:cd03301 77 VFQNYALYPHMTVYDN-IAFGLKLRKVPKDEIDE-RVREVAELlQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLM 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 499282096 161 DEVTSALDPMLVGEVLDTLKMLAEE-GMTMICVTHEMTFARDVSDRVAFFHQGIMAEIG 218
Cdd:cd03301 155 DEPLSNLDAKLRVQMRAELKRLQQRlGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
2-235 |
8.31e-56 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 182.45 E-value: 8.31e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 2 IEIENVRKSFSSLEVLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGTDVhakgTDLNRLRRKVGI 81
Cdd:PRK09452 15 VELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDI----THVPAENRHVNT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 82 VFQQWNAFPHLTVLENVMLAPR--KVlglPKDKAEEIAVKQLTHVGLGEKLKVYPNRMSGGQQQRMAIARALAMSPEYML 159
Cdd:PRK09452 91 VFQSYALFPHMTVFENVAFGLRmqKT---PAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLL 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499282096 160 FDEVTSALDPMLVGEVLDTLKMLAEE-GMTMICVTHEMTFARDVSDRVAFFHQGIMAEIGSPDQIFASPQNPETQKF 235
Cdd:PRK09452 168 LDESLSALDYKLRKQMQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNLFVARF 244
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-227 |
5.40e-55 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 176.43 E-value: 5.40e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 1 MIEIENVRKSFSSLEVLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGTDVHAKgtdlnrlRRKVG 80
Cdd:COG1121 6 AIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRA-------RRRIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 81 IVFQQ----WNaFPhLTVLENVML---APRKVLGLPKDKAEEIAVKQLTHVGLGEKLKVYPNRMSGGQQQRMAIARALAM 153
Cdd:COG1121 79 YVPQRaevdWD-FP-ITVRDVVLMgryGRRGLFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQ 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499282096 154 SPEYMLFDEVTSALDPMLVGEVLDTLKMLAEEGMTMICVTHEMTFARDVSDRVAFFHQGIMAEiGSPDQIFASP 227
Cdd:COG1121 157 DPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLLNRGLVAH-GPPEEVLTPE 229
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
2-212 |
9.04e-55 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 173.35 E-value: 9.04e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 2 IEIENVRKSFSSLEVLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGTDVHAKGTDlnrLRRKVGI 81
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEE---VKRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 82 VFQQWNAFPHLTVLENVMLaprkvlglpkdkaeeiavkqlthvglgeklkvypnrmSGGQQQRMAIARALAMSPEYMLFD 161
Cdd:cd03230 78 LPEEPSLYENLTVRENLKL-------------------------------------SGGMKQRLALAQALLHDPELLILD 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 499282096 162 EVTSALDPMLVGEVLDTLKMLAEEGMTMICVTHEMTFARDVSDRVAFFHQG 212
Cdd:cd03230 121 EPTSGLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNG 171
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
1-239 |
2.19e-54 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 179.14 E-value: 2.19e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 1 MIEIENVRKSF---------------SSLEVLK---------GIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSG 56
Cdd:COG4175 3 KIEVRNLYKIFgkrperalklldqgkSKDEILEktgqtvgvnDASFDVEEGEIFVIMGLSGSGKSTLVRCLNRLIEPTAG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 57 RIVIDGTDV-HAKGTDLNRLRR-KVGIVFQQWNAFPHLTVLENVMLaPRKVLGLPKDKAEEIAVKQLTHVGLGEKLKVYP 134
Cdd:COG4175 83 EVLIDGEDItKLSKKELRELRRkKMSMVFQHFALLPHRTVLENVAF-GLEIQGVPKAERRERAREALELVGLAGWEDSYP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 135 NRMSGGQQQRMAIARALAMSPEYMLFDEVTSALDPMLVGEVLDTLKML-AEEGMTMICVTHEMTFARDVSDRVAFFHQGI 213
Cdd:COG4175 162 DELSGGMQQRVGLARALATDPDILLMDEAFSALDPLIRREMQDELLELqAKLKKTIVFITHDLDEALRLGDRIAIMKDGR 241
|
250 260
....*....|....*....|....*.
gi 499282096 214 MAEIGSPDQIFASPQNPETQKFLASV 239
Cdd:COG4175 242 IVQIGTPEEILTNPANDYVADFVEDV 267
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
2-239 |
2.19e-54 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 178.35 E-value: 2.19e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 2 IEIENVRKSFSSLEVLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGTDV---HAKgtdlnrlRRK 78
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVsrlHAR-------DRK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 79 VGIVFQQWNAFPHLTVLENV-----MLAPRKvlglpKDKAEEIAVK--------QLTHvgLGEKlkvYPNRMSGGQQQRM 145
Cdd:PRK10851 76 VGFVFQHYALFRHMTVFDNIafgltVLPRRE-----RPNAAAIKAKvtqllemvQLAH--LADR---YPAQLSGGQKQRV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 146 AIARALAMSPEYMLFDEVTSALDPMLVGEVLDTLKMLAEE-GMTMICVTHEMTFARDVSDRVAFFHQGIMAEIGSPDQIF 224
Cdd:PRK10851 146 ALARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEElKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVW 225
|
250
....*....|....*
gi 499282096 225 ASPQNPETQKFLASV 239
Cdd:PRK10851 226 REPATRFVLEFMGEV 240
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
2-223 |
4.64e-54 |
|
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: 173.39 E-value: 4.64e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 2 IEIENVRKSFSSLEVLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGTDVHAKGTDLnRLRRKVGI 81
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHE-RARAGIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 82 VFQQWNAFPHLTVLENVMLAprkVLGLPKDKAEEI--AVKQLTHVgLGEKLKVYPNRMSGGQQQRMAIARALAMSPEYML 159
Cdd:cd03224 80 VPEGRRIFPELTVEENLLLG---AYARRRAKRKARleRVYELFPR-LKERRKQLAGTLSGGEQQMLAIARALMSRPKLLL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499282096 160 FDEVTSALDPMLVGEVLDTLKMLAEEGMTMICVTHEMTFARDVSDRVAFFHQGIMAEIGSPDQI 223
Cdd:cd03224 156 LDEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAEL 219
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
17-240 |
1.58e-53 |
|
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: 176.20 E-value: 1.58e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 17 LKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGTDVHAKGTDLNR--LRRKVGIVFQQWNAFPHLTV 94
Cdd:TIGR01186 9 VNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEPTAGQIFIDGENIMKQSPVELRevRRKKIGMVFQQFALFPHMTI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 95 LENVMLAPrKVLGLPKDKAEEIAVKQLTHVGLGEKLKVYPNRMSGGQQQRMAIARALAMSPEYMLFDEVTSALDPMLVGE 174
Cdd:TIGR01186 89 LQNTSLGP-ELLGWPEQERKEKALELLKLVGLEEYEHRYPDELSGGMQQRVGLARALAAEPDILLMDEAFSALDPLIRDS 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499282096 175 VLDTLKML-AEEGMTMICVTHEMTFARDVSDRVAFFHQGIMAEIGSPDQIFASPQNPETQKFLASVR 240
Cdd:TIGR01186 168 MQDELKKLqATLQKTIVFITHDLDEAIRIGDRIVIMKAGEIVQVGTPDEILRNPANEYVEEFIGKVD 234
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1-223 |
2.18e-53 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 172.35 E-value: 2.18e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 1 MIEIENVRKSFSSLEVLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGTDVHakgTDLNRLRRKVG 80
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVR---KEPREARRQIG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 81 IVFQQWNAFPHLTVLENV-MLAPrkVLGLPKDKAEEIAVKQLTHVGLGEKLKVYPNRMSGGQQQRMAIARALAMSPEYML 159
Cdd:COG4555 78 VLPDERGLYDRLTVRENIrYFAE--LYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499282096 160 FDEVTSALDPMLVGEVLDTLKMLAEEGMTMICVTHEMTFARDVSDRVAFFHQGIMAEIGSPDQI 223
Cdd:COG4555 156 LDEPTNGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDEL 219
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
2-212 |
8.37e-52 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 166.92 E-value: 8.37e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 2 IEIENVRKSFSSLEVLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGTDVHAkgTDLNRLRRKVGI 81
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSA--MPPPEWRRQVAY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 82 VFQQwnafPHL---TVLENvMLAPRKVLGLPKDkaEEIAVKQLTHVGLGEKLKVYP-NRMSGGQQQRMAIARALAMSPEY 157
Cdd:COG4619 79 VPQE----PALwggTVRDN-LPFPFQLRERKFD--RERALELLERLGLPPDILDKPvERLSGGERQRLALIRALLLQPDV 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 499282096 158 MLFDEVTSALDPMLVGEVLDTLK-MLAEEGMTMICVTHEMTFARDVSDRVAFFHQG 212
Cdd:COG4619 152 LLLDEPTSALDPENTRRVEELLReYLAEEGRAVLWVSHDPEQIERVADRVLTLEAG 207
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-236 |
1.12e-51 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 168.03 E-value: 1.12e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 1 MIEIENVRKSFSSLEVLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGL-----EPIDSGRIVIDGTDVHAKGTDLNRL 75
Cdd:PRK14239 5 ILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndlnpEVTITGSIVYNGHNIYSPRTDTVDL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 76 RRKVGIVFQQWNAFPhLTVLENVMLAPRkvLGLPKDKA--EEIAVKQLTHVGLGEKLKvypNRM-------SGGQQQRMA 146
Cdd:PRK14239 85 RKEIGMVFQQPNPFP-MSIYENVVYGLR--LKGIKDKQvlDEAVEKSLKGASIWDEVK---DRLhdsalglSGGQQQRVC 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 147 IARALAMSPEYMLFDEVTSALDPMLVGEVLDTLKMLAEEgMTMICVTHEMTFARDVSDRVAFFHQGIMAEIGSPDQIFAS 226
Cdd:PRK14239 159 IARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDD-YTMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQMFMN 237
|
250
....*....|
gi 499282096 227 PQNPETQKFL 236
Cdd:PRK14239 238 PKHKETEDYI 247
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
2-239 |
1.12e-51 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 170.30 E-value: 1.12e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 2 IEIENVRKSF---SSL-----EVLK---GIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGTDV-HAKG 69
Cdd:COG4608 8 LEVRDLKKHFpvrGGLfgrtvGVVKavdGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDItGLSG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 70 TDLNRLRRKVGIVFQqwNAF----PHLTVLENVMlAPRKVLGL-PKDKAEEIAVKQLTHVGLG-EKLKVYPNRMSGGQQQ 143
Cdd:COG4608 88 RELRPLRRRMQMVFQ--DPYaslnPRMTVGDIIA-EPLRIHGLaSKAERRERVAELLELVGLRpEHADRYPHEFSGGQRQ 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 144 RMAIARALAMSPEYMLFDEVTSALDPMLVGEVLDTLKMLAEE-GMTMICVTHEMTFARDVSDRVAFFHQGIMAEIGSPDQ 222
Cdd:COG4608 165 RIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDElGLTYLFISHDLSVVRHISDRVAVMYLGKIVEIAPRDE 244
|
250
....*....|....*..
gi 499282096 223 IFASPQNPETQKFLASV 239
Cdd:COG4608 245 LYARPLHPYTQALLSAV 261
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-228 |
2.75e-51 |
|
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: 166.70 E-value: 2.75e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 1 MIEIENVRKSFSSLEVLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGTDVHAKGTDlNRLRRKVG 80
Cdd:COG0410 3 MLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPH-RIARLGIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 81 IVFQQWNAFPHLTVLENVMLA--PRKVLGLPKDKAEEIAvkQLTHVgLGEKLKVYPNRMSGGQQQRMAIARALAMSPEYM 158
Cdd:COG0410 82 YVPEGRRIFPSLTVEENLLLGayARRDRAEVRADLERVY--ELFPR-LKERRRQRAGTLSGGEQQMLAIGRALMSRPKLL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 159 LFDEVTSALDPMLVGEVLDTLKMLAEEGMTMICVTHEMTFARDVSDRVAFFHQGIMAEIGSPDQIFASPQ 228
Cdd:COG0410 159 LLDEPSLGLAPLIVEEIFEIIRRLNREGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLADPE 228
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
3-212 |
5.24e-50 |
|
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: 160.87 E-value: 5.24e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 3 EIENVRKSFSSLEVLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGTDVHAKgtDLNRLRRKVGIV 82
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKL--PLEELRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 83 FQqwnafphltvlenvmlaprkvlglpkdkaeeiavkqlthvglgeklkvypnrMSGGQQQRMAIARALAMSPEYMLFDE 162
Cdd:cd00267 79 PQ----------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDE 106
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 499282096 163 VTSALDPMLVGEVLDTLKMLAEEGMTMICVTHEMTFARDVSDRVAFFHQG 212
Cdd:cd00267 107 PTSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDG 156
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-236 |
5.97e-50 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 163.86 E-value: 5.97e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 2 IEIENVRKSFSSLEVLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPID-----SGRIVIDGTDVHAKGTDLNRLR 76
Cdd:PRK14267 5 IETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNeearvEGEVRLFGRNIYSPDVDPIEVR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 77 RKVGIVFQQWNAFPHLTVLENVMLApRKVLGLPKDKAE--EIAVKQLTHVGLGE----KLKVYPNRMSGGQQQRMAIARA 150
Cdd:PRK14267 85 REVGMVFQYPNPFPHLTIYDNVAIG-VKLNGLVKSKKEldERVEWALKKAALWDevkdRLNDYPSNLSGGQRQRLVIARA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 151 LAMSPEYMLFDEVTSALDPMLVGEVLDTLKMLAEEgMTMICVTHEMTFARDVSDRVAFFHQGIMAEIGSPDQIFASPQNP 230
Cdd:PRK14267 164 LAMKPKILLMDEPTANIDPVGTAKIEELLFELKKE-YTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENPEHE 242
|
....*.
gi 499282096 231 ETQKFL 236
Cdd:PRK14267 243 LTEKYV 248
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1-228 |
4.14e-49 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 162.08 E-value: 4.14e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 1 MIEIENVRKSFSSLE--VLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGTDVHAKgtDLNRLRRK 78
Cdd:PRK13632 7 MIKVENVSFSYPNSEnnALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKE--NLKEIRKK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 79 VGIVFQQW-NAFPHLTV-------LENVMLAPRKVlglpKDKAEEIAVKqlthVGLGEKLKVYPNRMSGGQQQRMAIARA 150
Cdd:PRK13632 85 IGIIFQNPdNQFIGATVeddiafgLENKKVPPKKM----KDIIDDLAKK----VGMEDYLDKEPQNLSGGQKQRVAIASV 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499282096 151 LAMSPEYMLFDEVTSALDPMLVGEVLDTLKMLAEEGM-TMICVTHEMTFARdVSDRVAFFHQGIMAEIGSPDQIFASPQ 228
Cdd:PRK13632 157 LALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKkTLISITHDMDEAI-LADKVIVFSEGKLIAQGKPKEILNNKE 234
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
21-218 |
1.32e-48 |
|
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: 158.81 E-value: 1.32e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 21 DLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGTDVhakgTDLNRLRRKVGIVFQQWNAFPHLTVLENVML 100
Cdd:cd03298 18 DLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDV----TAAPPADRPVSMLFQENNLFAHLTVEQNVGL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 101 APRKVLGLPKDKAEEIAvKQLTHVGLGEKLKVYPNRMSGGQQQRMAIARALAMSPEYMLFDEVTSALDPMLVGEVLD-TL 179
Cdd:cd03298 94 GLSPGLKLTAEDRQAIE-VALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDlVL 172
|
170 180 190
....*....|....*....|....*....|....*....
gi 499282096 180 KMLAEEGMTMICVTHEMTFARDVSDRVAFFHQGIMAEIG 218
Cdd:cd03298 173 DLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
2-239 |
1.50e-48 |
|
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: 167.17 E-value: 1.50e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 2 IEIENVRKSF-----------SSLEVLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPiDSGRIVIDGTDVHA-KG 69
Cdd:COG4172 276 LEARDLKVWFpikrglfrrtvGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIP-SEGEIRFDGQDLDGlSR 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 70 TDLNRLRRKVGIVFQqwNAF----PHLTVLENVMlAPRKVLGLPKDKAE--EIAVKQLTHVGL-GEKLKVYPNRMSGGQQ 142
Cdd:COG4172 355 RALRPLRRRMQVVFQ--DPFgslsPRMTVGQIIA-EGLRVHGPGLSAAErrARVAEALEEVGLdPAARHRYPHEFSGGQR 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 143 QRMAIARALAMSPEYMLFDEVTSALDpMLV-GEVLDTLKML-AEEGMTMICVTHEMTFARDVSDRVAFFHQGIMAEIGSP 220
Cdd:COG4172 432 QRIAIARALILEPKLLVLDEPTSALD-VSVqAQILDLLRDLqREHGLAYLFISHDLAVVRALAHRVMVMKDGKVVEQGPT 510
|
250
....*....|....*....
gi 499282096 221 DQIFASPQNPETQKFLASV 239
Cdd:COG4172 511 EQVFDAPQHPYTRALLAAA 529
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-238 |
1.85e-48 |
|
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: 166.78 E-value: 1.85e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 1 MIEIENVRKSF----SSLEVLKGIDLTVEKGEVVTIIGGSGSGKS-TLLTcINGLEP----IDSGRIVIDGTD-VHAKGT 70
Cdd:COG4172 6 LLSVEDLSVAFgqggGTVEAVKGVSFDIAAGETLALVGESGSGKSvTALS-ILRLLPdpaaHPSGSILFDGQDlLGLSER 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 71 DLNRLR-RKVGIVFQQ----WNafPHLTVLENVMLAPRKVLGLPKDKAEEIAVKQLTHVGLGE---KLKVYPNRMSGGQQ 142
Cdd:COG4172 85 ELRRIRgNRIAMIFQEpmtsLN--PLHTIGKQIAEVLRLHRGLSGAAARARALELLERVGIPDperRLDAYPHQLSGGQR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 143 QRMAIARALAMSPEYMLFDEVTSALDPMLVGEVLDTLKML-AEEGMTMICVTHEMTFARDVSDRVAFFHQGIMAEIGSPD 221
Cdd:COG4172 163 QRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLqRELGMALLLITHDLGVVRRFADRVAVMRQGEIVEQGPTA 242
|
250
....*....|....*..
gi 499282096 222 QIFASPQNPETQKFLAS 238
Cdd:COG4172 243 ELFAAPQHPYTRKLLAA 259
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
2-238 |
2.05e-48 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 162.58 E-value: 2.05e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 2 IEIENVRKSFSSLEVLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGTDVhakgTDLNRLRRKVGI 81
Cdd:PRK11432 7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDV----THRSIQQRDICM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 82 VFQQWNAFPHLTVLENVMLApRKVLGLPKdkaEEIA--VKQ-LTHVGLGEKLKVYPNRMSGGQQQRMAIARALAMSPEYM 158
Cdd:PRK11432 83 VFQSYALFPHMSLGENVGYG-LKMLGVPK---EERKqrVKEaLELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 159 LFDEVTSALDPMLVGEVLDTLKMLAEE-GMTMICVTHEMTFARDVSDRVAFFHQGIMAEIGSPDQIFASPQNpetqKFLA 237
Cdd:PRK11432 159 LFDEPLSNLDANLRRSMREKIRELQQQfNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPAS----RFMA 234
|
.
gi 499282096 238 S 238
Cdd:PRK11432 235 S 235
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-236 |
3.71e-48 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 159.31 E-value: 3.71e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 2 IEIENVRKSFSSLEVLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGL-----EPIDSGRIVIDGTDVHAkgTDLNRLR 76
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQDIFK--MDVIELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 77 RKVGIVFQQWNAFPHLTVLENVMLAPrKVLGLPKDKAE-EIAVKQ-LTHVGLGEKLKVYPN----RMSGGQQQRMAIARA 150
Cdd:PRK14247 82 RRVQMVFQIPNPIPNLSIFENVALGL-KLNRLVKSKKElQERVRWaLEKAQLWDEVKDRLDapagKLSGGQQQRLCIARA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 151 LAMSPEYMLFDEVTSALDPMLVGEvLDTLKMLAEEGMTMICVTHEMTFARDVSDRVAFFHQGIMAEIGSPDQIFASPQNP 230
Cdd:PRK14247 161 LAFQPEVLLADEPTANLDPENTAK-IESLFLELKKDMTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTNPRHE 239
|
....*.
gi 499282096 231 ETQKFL 236
Cdd:PRK14247 240 LTEKYV 245
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
2-225 |
1.22e-47 |
|
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: 166.93 E-value: 1.22e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 2 IEIENVRKSFSSLE--VLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGTDVhaKGTDLNRLRRKV 79
Cdd:COG2274 474 IELENVSFRYPGDSppVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDL--RQIDPASLRRQI 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 80 GIVFQQwnafPHL---TVLENVMLAprkVLGLPKDKAEEIA--------VKQL-----THVG-LGEKLkvypnrmSGGQQ 142
Cdd:COG2274 552 GVVLQD----VFLfsgTIRENITLG---DPDATDEEIIEAArlaglhdfIEALpmgydTVVGeGGSNL-------SGGQR 617
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 143 QRMAIARALAMSPEYMLFDEVTSALDPMLVGEVLDTLKMLAeEGMTMICVTHEMTFARDVsDRVAFFHQGIMAEIGSPDQ 222
Cdd:COG2274 618 QRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLL-KGRTVIIIAHRLSTIRLA-DRIIVLDKGRIVEDGTHEE 695
|
...
gi 499282096 223 IFA 225
Cdd:COG2274 696 LLA 698
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
32-239 |
1.52e-47 |
|
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: 159.58 E-value: 1.52e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 32 IIGGSGSGKSTLLTCINGLEPIDSGRIVIDGTDVhakgTDLNRLRRKVGIVFQQWNAFPHLTVLENVMLaPRKVLGLPKD 111
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDV----TNVPPHLRHINMVFQSYALFPHMTVEENVAF-GLKMRKVPRA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 112 KAEEIAVKQLTHVGLGEKLKVYPNRMSGGQQQRMAIARALAMSPEYMLFDEVTSALDPMLVGEVLDTLKMLAEE-GMTMI 190
Cdd:TIGR01187 76 EIKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQlGITFV 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 499282096 191 CVTHEMTFARDVSDRVAFFHQGIMAEIGSPDQIFASPQNPETQKFLASV 239
Cdd:TIGR01187 156 FVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFVARFIGEI 204
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
20-218 |
1.73e-47 |
|
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: 156.30 E-value: 1.73e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 20 IDLTVEkGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGT--DVHAKGTDLNRLRRKVGIVFQQWNAFPHLTVLEN 97
Cdd:cd03297 17 IDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTvlFDSRKKINLPPQQRKIGLVFQQYALFPHLNVREN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 98 VMLA-PRKVLGLPKDKAEEIavkqLTHVGLGEKLKVYPNRMSGGQQQRMAIARALAMSPEYMLFDEVTSALDPMLVGEVL 176
Cdd:cd03297 96 LAFGlKRKRNREDRISVDEL----LDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLL 171
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 499282096 177 DTL-KMLAEEGMTMICVTHEMTFARDVSDRVAFFHQGIMAEIG 218
Cdd:cd03297 172 PELkQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
2-223 |
1.74e-47 |
|
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: 156.51 E-value: 1.74e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 2 IEIENVRKSFSSLE--VLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGTDVHakgTDLNRLRRKV 79
Cdd:cd03263 1 LQIRNLTKTYKKGTkpAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIR---TDRKAARQSL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 80 GIVFQQWNAFPHLTVLENVMLAPRkVLGLPKDKAEEIAVKQLTHVGLGEKLKVYPNRMSGGQQQRMAIARALAMSPEYML 159
Cdd:cd03263 78 GYCPQFDALFDELTVREHLRFYAR-LKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499282096 160 FDEVTSALDPMLVGEVLDTLKMLAeEGMTMICVTHEMTFARDVSDRVAFFHQGIMAEIGSPDQI 223
Cdd:cd03263 157 LDEPTSGLDPASRRAIWDLILEVR-KGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQEL 219
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
20-230 |
3.79e-47 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 159.51 E-value: 3.79e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 20 IDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGTDVH--AKGTDLNRLRRKVGIVFQQWNAFPHLTVLEN 97
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFdsRKGIFLPPEKRRIGYVFQEARLFPHLSVRGN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 98 VMLAPRKVLGlPKDKAEEIAVKQLthVGLGEKLKVYPNRMSGGQQQRMAIARALAMSPEYMLFDEVTSALDPMLVGEVLD 177
Cdd:TIGR02142 96 LRYGMKRARP-SERRISFERVIEL--LGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILP 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 499282096 178 TLKMLAEE-GMTMICVTHEMTFARDVSDRVAFFHQGIMAEIGSPDQIFASPQNP 230
Cdd:TIGR02142 173 YLERLHAEfGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPDLP 226
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
17-165 |
5.95e-47 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 152.80 E-value: 5.95e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 17 LKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGTDVHAKgtDLNRLRRKVGIVFQQWNAFPHLTVLE 96
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDD--ERKSLRKEIGYVFQDPQLFPRLTVRE 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499282096 97 NVMLAPRkVLGLPKDKAEEIAVKQLTHVGLGEKLK----VYPNRMSGGQQQRMAIARALAMSPEYMLFDEVTS 165
Cdd:pfam00005 79 NLRLGLL-LKGLSKREKDARAEEALEKLGLGDLADrpvgERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1-228 |
7.00e-47 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 156.39 E-value: 7.00e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 1 MIEIENVRKSF-SSLEVLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGTDVHAKGTDLNRLRRKV 79
Cdd:PRK13639 1 ILETRDLKYSYpDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSLLEVRKTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 80 GIVFQqwNAFPHL---TVLENVMLAPRKvLGLPKDKAEEIAVKQLTHVGLGEKLKVYPNRMSGGQQQRMAIARALAMSPE 156
Cdd:PRK13639 81 GIVFQ--NPDDQLfapTVEEDVAFGPLN-LGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPE 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499282096 157 YMLFDEVTSALDPMLVGEVLDTLKMLAEEGMTMICVTHEMTFARDVSDRVAFFHQGIMAEIGSPDQIFASPQ 228
Cdd:PRK13639 158 IIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDIE 229
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
1-227 |
1.43e-46 |
|
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: 157.96 E-value: 1.43e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 1 MIEIeNVRKSFSS--LEVlkgiDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGTDV--HAKGTDLNRLR 76
Cdd:COG4148 2 MLEV-DFRLRRGGftLDV----DFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLqdSARGIFLPPHR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 77 RKVGIVFQQWNAFPHLTVLENVMLA-PRKVLGLPKDKAEEIaVKQLthvGLGEKLKVYPNRMSGGQQQRMAIARALAMSP 155
Cdd:COG4148 77 RRIGYVFQEARLFPHLSVRGNLLYGrKRAPRAERRISFDEV-VELL---GIGHLLDRRPATLSGGERQRVAIGRALLSSP 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499282096 156 EYMLFDEVTSALDPMLVGEVLDTLKMLAEE-GMTMICVTHEMTFARDVSDRVAFFHQGIMAEIGSPDQIFASP 227
Cdd:COG4148 153 RLLLMDEPLAALDLARKAEILPYLERLRDElDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRP 225
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
2-212 |
2.15e-46 |
|
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: 151.77 E-value: 2.15e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 2 IEIENVrkSFS----SLEVLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGTDVhaKGTDLNRLRR 77
Cdd:cd03228 1 IEFKNV--SFSypgrPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDL--RDLDLESLRK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 78 KVGIVFQQwnafPHL---TVLENVmlaprkvlglpkdkaeeiavkqlthvglgeklkvypnrMSGGQQQRMAIARALAMS 154
Cdd:cd03228 77 NIAYVPQD----PFLfsgTIRENI--------------------------------------LSGGQRQRIAIARALLRD 114
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 499282096 155 PEYMLFDEVTSALDPMLVGEVLDTLKMLAeEGMTMICVTHEMTFARDVsDRVAFFHQG 212
Cdd:cd03228 115 PPILILDEATSALDPETEALILEALRALA-KGKTVIVIAHRLSTIRDA-DRIIVLDDG 170
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1-234 |
4.26e-46 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 162.20 E-value: 4.26e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 1 MIEIENVRKSFSS----LEVLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGTDVHAKGTD-LNRL 75
Cdd:PRK10535 4 LLELKDIRRSYPSgeeqVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADaLAQL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 76 RRK-VGIVFQQWNAFPHLTVLENVMLaPRKVLGLPKDKAEEIAVKQLTHVGLGEKLKVYPNRMSGGQQQRMAIARALAMS 154
Cdd:PRK10535 84 RREhFGFIFQRYHLLSHLTAAQNVEV-PAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 155 PEYMLFDEVTSALDPMLVGEVLDTLKMLAEEGMTMICVTHEMTFARDvSDRVAFFHQG-IMAEIGS-PDQIFASPQNPET 232
Cdd:PRK10535 163 GQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHDPQVAAQ-AERVIEIRDGeIVRNPPAqEKVNVAGGTEPVV 241
|
..
gi 499282096 233 QK 234
Cdd:PRK10535 242 NT 243
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
3-215 |
4.57e-46 |
|
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: 152.30 E-value: 4.57e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 3 EIENVRKSFSSLEVLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGTDVHakgtdlnRLRRKVGIV 82
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLE-------KERKRIGYV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 83 FQQWNA---FPhLTVLENVMLA--PRKVLGLPKDKAEEIAVKQ-LTHVGLGEKLKVYPNRMSGGQQQRMAIARALAMSPE 156
Cdd:cd03235 74 PQRRSIdrdFP-ISVRDVVLMGlyGHKGLFRRLSKADKAKVDEaLERVGLSELADRQIGELSGGQQQRVLLARALVQDPD 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 499282096 157 YMLFDEVTSALDPMLVGEVLDTLKMLAEEGMTMICVTHEMTFARDVSDRVAFFHQGIMA 215
Cdd:cd03235 153 LLLLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRVLLLNRTVVA 211
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
2-237 |
5.17e-46 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 154.17 E-value: 5.17e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 2 IEIENVRKSFSSLEVLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGL-EPIDS----GRIVIDGTDVHAKGTDLNRLR 76
Cdd:PRK14243 11 LRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLnDLIPGfrveGKVTFHGKNLYAPDVDPVEVR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 77 RKVGIVFQQWNAFPHlTVLENVMLAPRkVLGLPKDkAEEIAVKQLTHVGL----GEKLKVYPNRMSGGQQQRMAIARALA 152
Cdd:PRK14243 91 RRIGMVFQKPNPFPK-SIYDNIAYGAR-INGYKGD-MDELVERSLRQAALwdevKDKLKQSGLSLSGGQQQRLCIARAIA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 153 MSPEYMLFDEVTSALDPMLVGEVLDTLKMLAEEgMTMICVTHEMTFARDVSDRVAFFH---------QGIMAEIGSPDQI 223
Cdd:PRK14243 168 VQPEVILMDEPCSALDPISTLRIEELMHELKEQ-YTIIIVTHNMQQAARVSDMTAFFNveltegggrYGYLVEFDRTEKI 246
|
250
....*....|....
gi 499282096 224 FASPQNPETQKFLA 237
Cdd:PRK14243 247 FNSPQQQATRDYVS 260
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
17-235 |
5.18e-46 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 154.79 E-value: 5.18e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 17 LKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGTDVHA--KGTDLNRLRRKVGIVFQqwnaFPHL-- 92
Cdd:PRK13634 23 LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAgkKNKKLKPLRKKVGIVFQ----FPEHql 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 93 ---TVLENVMLAPRKvLGLPKDKAEEIAVKQLTHVGLGEK-LKVYPNRMSGGQQQRMAIARALAMSPEYMLFDEVTSALD 168
Cdd:PRK13634 99 feeTVEKDICFGPMN-FGVSEEDAKQKAREMIELVGLPEElLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLD 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499282096 169 PMLVGEVLDTLKML-AEEGMTMICVTHEMTFARDVSDRVAFFHQGIMAEIGSPDQIFASPQN--------PETQKF 235
Cdd:PRK13634 178 PKGRKEMMEMFYKLhKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADPDEleaigldlPETVKF 253
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-212 |
9.24e-46 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 153.32 E-value: 9.24e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 1 MIEIENVRKSF---SSLE--VLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGTDVhakgTDLNRL 75
Cdd:COG1101 1 MLELKNLSKTFnpgTVNEkrALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDV----TKLPEY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 76 RR--KVGIVFQ--QWNAFPHLTVLENVMLAPRK------VLGLPKDKAEEIAvKQLTHVGLG-EklkvypNRM------- 137
Cdd:COG1101 77 KRakYIGRVFQdpMMGTAPSMTIEENLALAYRRgkrrglRRGLTKKRRELFR-ELLATLGLGlE------NRLdtkvgll 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 138 SGGQQQrmaiARALAMS----PEYMLFDEVTSALDPMLVGEVLD-TLKMLAEEGMTMICVTHEMTFARDVSDRVAFFHQG 212
Cdd:COG1101 150 SGGQRQ----ALSLLMAtltkPKLLLLDEHTAALDPKTAALVLElTEKIVEENNLTTLMVTHNMEQALDYGNRLIMMHEG 225
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
2-214 |
1.07e-44 |
|
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: 149.10 E-value: 1.07e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 2 IEIENVRKSF-SSLEVLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGTDV-HAKGTDLNRLRRKV 79
Cdd:cd03292 1 IEFINVTKTYpNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVsDLRGRAIPYLRRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 80 GIVFQQWNAFPHLTVLENVMLAPRKVLGLPKDKAEEIAvKQLTHVGLGEKLKVYPNRMSGGQQQRMAIARALAMSPEYML 159
Cdd:cd03292 81 GVVFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVP-AALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILI 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 499282096 160 FDEVTSALDPMLVGEVLDTLKMLAEEGMTMICVTHEMTFARDVSDRVAFFHQGIM 214
Cdd:cd03292 160 ADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
17-218 |
1.44e-44 |
|
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: 149.15 E-value: 1.44e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 17 LKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGTDVHAKGTDlnRLrrkvgIVFQQWNAFPHLTVLE 96
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPD--RM-----VVFQNYSLLPWLTVRE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 97 NVMLAPRKVL-GLPKDKAEEIAVKQLTHVGLGEKLKVYPNRMSGGQQQRMAIARALAMSPEYMLFDEVTSALDPMLVGEV 175
Cdd:TIGR01184 74 NIALAVDRVLpDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNL 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 499282096 176 LDTLKMLAEE-GMTMICVTHEMTFARDVSDRVAFFHQGIMAEIG 218
Cdd:TIGR01184 154 QEELMQIWEEhRVTVLMVTHDVDEALLLSDRVVMLTNGPAANIG 197
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1-239 |
2.19e-44 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 152.68 E-value: 2.19e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 1 MIEIENVRKSFSSLEVLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGTDVhakgTDLNRLRRKVG 80
Cdd:PRK11607 19 LLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDL----SHVPPYQRPIN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 81 IVFQQWNAFPHLTVLENVmlaprkVLGLPKDK--AEEIAVK---QLTHVGLGEKLKVYPNRMSGGQQQRMAIARALAMSP 155
Cdd:PRK11607 95 MMFQSYALFPHMTVEQNI------AFGLKQDKlpKAEIASRvneMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRP 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 156 EYMLFDEVTSALDPMLVGEV-LDTLKMLAEEGMTMICVTHEMTFARDVSDRVAFFHQGIMAEIGSPDQIFASPQNPETQK 234
Cdd:PRK11607 169 KLLLLDEPMGALDKKLRDRMqLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAE 248
|
....*
gi 499282096 235 FLASV 239
Cdd:PRK11607 249 FIGSV 253
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-238 |
2.80e-44 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 149.42 E-value: 2.80e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 2 IEIENVRKSFSSLEVLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDS-----GRIVIDGTDVHAKGTDLNRLR 76
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNIYERRVNLNRLR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 77 RKVGIVFQQWNAFPhLTVLENVMLAPRKVLGLPKDKAEEIAVKQLTHVGLGEKLKVYPNR----MSGGQQQRMAIARALA 152
Cdd:PRK14258 88 RQVSMVHPKPNLFP-MSVYDNVAYGVKIVGWRPKLEIDDIVESALKDADLWDEIKHKIHKsaldLSGGQQQRLCIARALA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 153 MSPEYMLFDEVTSALDP---MLVGEVLDTLKMLAEegMTMICVTHEMTFARDVSDRVAFFHQ-----GIMAEIGSPDQIF 224
Cdd:PRK14258 167 VKPKVLLMDEPCFGLDPiasMKVESLIQSLRLRSE--LTMVIVSHNLHQVSRLSDFTAFFKGnenriGQLVEFGLTKKIF 244
|
250
....*....|....
gi 499282096 225 ASPQNPETQKFLAS 238
Cdd:PRK14258 245 NSPHDSRTREYVLS 258
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
3-218 |
6.44e-44 |
|
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: 146.04 E-value: 6.44e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 3 EIENVRKSFSSLEVLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGTDVHAkgTDLNRLRRKVGIV 82
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLAS--LSPKELARKIAYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 83 FQqwnafphltVLENvmlaprkvlglpkdkaeeiavkqlthVGLGEKLKVYPNRMSGGQQQRMAIARALAMSPEYMLFDE 162
Cdd:cd03214 79 PQ---------ALEL--------------------------LGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDE 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 499282096 163 VTSALDPMLVGEVLDTLKMLA-EEGMTMICVTHEMTFARDVSDRVAFFHQGIMAEIG 218
Cdd:cd03214 124 PTSHLDIAHQIELLELLRRLArERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
2-224 |
1.43e-43 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 148.27 E-value: 1.43e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 2 IEIENV-----RKSFSSLEVLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGTDVHAKGTDLNRLR 76
Cdd:PRK13637 3 IKIENLthiymEGTPFEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKLSDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 77 RKVGIVFQ--QWNAFPHlTVLENVMLAPRKvLGLPKDKAEEIAVKQLTHVGLG-EKLK-VYPNRMSGGQQQRMAIARALA 152
Cdd:PRK13637 83 KKVGLVFQypEYQLFEE-TIEKDIAFGPIN-LGLSEEEIENRVKRAMNIVGLDyEDYKdKSPFELSGGQKRRVAIAGVVA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499282096 153 MSPEYMLFDEVTSALDPMLVGEVLDTLKMLAEE-GMTMICVTHEMTFARDVSDRVAFFHQGIMAEIGSPDQIF 224
Cdd:PRK13637 161 MEPKILILDEPTAGLDPKGRDEILNKIKELHKEyNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVF 233
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-206 |
2.19e-43 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 152.48 E-value: 2.19e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 1 MIEIENVRKSFSSLEVLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGTDVHAKGTdLNRLRRKVG 80
Cdd:COG1129 4 LLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSP-RDAQAAGIA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 81 IVFQQWNAFPHLTVLENVMLA--PRKVLGLPKDKAEEIAVKQLTHVGLGEKLKVYPNRMSGGQQQRMAIARALAMSPEYM 158
Cdd:COG1129 83 IIHQELNLVPNLSVAENIFLGrePRRGGLIDWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRDARVL 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 499282096 159 LFDEVTSALDPMLVGEVLDTLKMLAEEGMTMICVTHEMTFARDVSDRV 206
Cdd:COG1129 163 ILDEPTASLTEREVERLFRIIRRLKAQGVAIIYISHRLDEVFEIADRV 210
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
2-223 |
4.74e-43 |
|
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: 144.82 E-value: 4.74e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 2 IEIENVRKSFSSLEVLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGTDVHAKGTDlnrLRRKVGI 81
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPRE---VRRRIGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 82 VFQQWNAFPHLTVLENVMLAPRkVLGLPKDKAEEIAVKQLTHVGLGEKLKVYPNRMSGGQQQRMAIARALAMSPEYMLFD 161
Cdd:cd03265 78 VFQDLSVDDELTGWENLYIHAR-LYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLD 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499282096 162 EVTSALDPMLVGEVLDTL-KMLAEEGMTMICVTHEMTFARDVSDRVAFFHQGIMAEIGSPDQI 223
Cdd:cd03265 157 EPTIGLDPQTRAHVWEYIeKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
17-239 |
1.01e-42 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 149.03 E-value: 1.01e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 17 LKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGTDVhAKGTD--LNRLRRK-VGIVFQQWNAFPHLT 93
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDI-AKISDaeLREVRRKkIAMVFQSFALMPHMT 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 94 VLENVMLApRKVLGLPKDKAEEIAVKQLTHVGLGEKLKVYPNRMSGGQQQRMAIARALAMSPEYMLFDEVTSALDPMLVG 173
Cdd:PRK10070 123 VLDNTAFG-MELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRT 201
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499282096 174 EVLDTL-KMLAEEGMTMICVTHEMTFARDVSDRVAFFHQGIMAEIGSPDQIFASPQNPETQKFLASV 239
Cdd:PRK10070 202 EMQDELvKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFFRGV 268
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
2-222 |
2.32e-42 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 151.09 E-value: 2.32e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 2 IEIENVrkSFS---SLEVLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGTDVhaKGTDLNRLRRK 78
Cdd:COG1132 340 IEFENV--SFSypgDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDI--RDLTLESLRRQ 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 79 VGIVFQQwnafPHL---TVLENVMlaprkvLGLPKDKAEEI--AVKQL--------------THVG-LGEKLkvypnrmS 138
Cdd:COG1132 416 IGVVPQD----TFLfsgTIRENIR------YGRPDATDEEVeeAAKAAqahefiealpdgydTVVGeRGVNL-------S 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 139 GGQQQRMAIARALAMSPEYMLFDEVTSALDP---MLVGEVLDTLKmlaeEGMTMICVTHEMTFARDVsDRVAFFHQGIMA 215
Cdd:COG1132 479 GGQRQRIAIARALLKDPPILILDEATSALDTeteALIQEALERLM----KGRTTIVIAHRLSTIRNA-DRILVLDDGRIV 553
|
....*..
gi 499282096 216 EIGSPDQ 222
Cdd:COG1132 554 EQGTHEE 560
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
2-212 |
4.55e-42 |
|
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: 140.64 E-value: 4.55e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 2 IEIENVRKSFSSLEVLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGTDVHAKGTDlNRLRRKVGI 81
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPR-DARRAGIAM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 82 VFQqwnafphltvlenvmlaprkvlglpkdkaeeiavkqlthvglgeklkvypnrMSGGQQQRMAIARALAMSPEYMLFD 161
Cdd:cd03216 80 VYQ----------------------------------------------------LSVGERQMVEIARALARNARLLILD 107
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 499282096 162 EVTSALDPMLVGEVLDTLKMLAEEGMTMICVTHEMTFARDVSDRVAFFHQG 212
Cdd:cd03216 108 EPTAALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDG 158
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
3-223 |
9.94e-42 |
|
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: 141.89 E-value: 9.94e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 3 EIENVRKSFSSLEVLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGTDVHAKGTDlNRLRRKVGIV 82
Cdd:TIGR03410 2 EVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPH-ERARAGIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 83 FQQWNAFPHLTVLENVML----APRKVLGLPKDKAEEIAVkqlthvglgekLKVYPNR----MSGGQQQRMAIARALAMS 154
Cdd:TIGR03410 81 PQGREIFPRLTVEENLLTglaaLPRRSRKIPDEIYELFPV-----------LKEMLGRrggdLSGGQQQQLAIARALVTR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 155 PEYMLFDEVTSALDPMLVGEVLDTLKMLAEE-GMTMICVTHEMTFARDVSDRVAFFHQGIMAEIGSPDQI 223
Cdd:TIGR03410 150 PKLLLLDEPTEGIQPSIIKDIGRVIRRLRAEgGMAILLVEQYLDFARELADRYYVMERGRVVASGAGDEL 219
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
17-226 |
1.72e-41 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 142.85 E-value: 1.72e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 17 LKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGTDVHAKgtDLNRLRRKVGIVFQQW-NAFPHLTV- 94
Cdd:PRK13635 23 LKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEE--TVWDVRRQVGMVFQNPdNQFVGATVq 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 95 ------LENVmlaprkvlGLPKDKAEEIAVKQLTHVGLGEKLKVYPNRMSGGQQQRMAIARALAMSPEYMLFDEVTSALD 168
Cdd:PRK13635 101 ddvafgLENI--------GVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLD 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 499282096 169 PMLVGEVLDTLKMLAEEGM-TMICVTHEMTFARDvSDRVAFFHQGIMAEIGSPDQIFAS 226
Cdd:PRK13635 173 PRGRREVLETVRQLKEQKGiTVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEIFKS 230
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-222 |
2.06e-41 |
|
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: 148.38 E-value: 2.06e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 2 IEIENVRKSF--SSLEVLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGTDVHAkgTDLNRLRRKV 79
Cdd:COG4987 334 LELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRD--LDEDDLRRRI 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 80 GIVFQQwnafPHL---TVLENVMLAprkvlglpKDKAEEIAVKQ-LTHVGLGEKLKVYPN-----------RMSGGQQQR 144
Cdd:COG4987 412 AVVPQR----PHLfdtTLRENLRLA--------RPDATDEELWAaLERVGLGDWLAALPDgldtwlgeggrRLSGGERRR 479
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499282096 145 MAIARALAMSPEYMLFDEVTSALDPMLVGEVLDTLKMLAeEGMTMICVTHEMTFARDVsDRVAFFHQGIMAEIGSPDQ 222
Cdd:COG4987 480 LALARALLRDAPILLLDEPTEGLDAATEQALLADLLEAL-AGRTVLLITHRLAGLERM-DRILVLEDGRIVEQGTHEE 555
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
6-238 |
2.42e-41 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 144.79 E-value: 2.42e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 6 NVRKSFSSLEVLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGTDVHakgtDLNRLRRKVGIVFQQ 85
Cdd:PRK11000 8 NVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMN----DVPPAERGVGMVFQS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 86 WNAFPHLTVLENVMLAprkvLGLPKDKAEEIAvKQLTHVG----LGEKLKVYPNRMSGGQQQRMAIARALAMSPEYMLFD 161
Cdd:PRK11000 84 YALYPHLSVAENMSFG----LKLAGAKKEEIN-QRVNQVAevlqLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLD 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499282096 162 EVTSALDPML-VGEVLDTLKMLAEEGMTMICVTHEMTFARDVSDRVAFFHQGIMAEIGSPDQIFASPQNPETQKFLAS 238
Cdd:PRK11000 159 EPLSNLDAALrVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPANRFVAGFIGS 236
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
6-239 |
2.77e-41 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 142.16 E-value: 2.77e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 6 NVRKSFSSLEVLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGL-EPID----SGRIVIDGTDVHaKGTDLNRLRRKVG 80
Cdd:PRK14271 26 NLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMnDKVSgyrySGDVLLGGRSIF-NYRDVLEFRRRVG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 81 IVFQQWNAFPhLTVLENVMLAPRKVLGLPKDKAEEIAVKQLTHVGL----GEKLKVYPNRMSGGQQQRMAIARALAMSPE 156
Cdd:PRK14271 105 MLFQRPNPFP-MSIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLwdavKDRLSDSPFRLSGGQQQLLCLARTLAVNPE 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 157 YMLFDEVTSALDPMLVGEVLDTLKMLAEEgMTMICVTHEMTFARDVSDRVAFFHQGIMAEIGSPDQIFASPQNPETQKFL 236
Cdd:PRK14271 184 VLLLDEPTSALDPTTTEKIEEFIRSLADR-LTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKHAETARYV 262
|
...
gi 499282096 237 ASV 239
Cdd:PRK14271 263 AGL 265
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
2-212 |
3.22e-41 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 142.92 E-value: 3.22e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 2 IEIENVRKSFSS-----LEVLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGTDVHAK-------- 68
Cdd:PRK13651 3 IKVKNIVKIFNKklpteLKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKkktkekek 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 69 -GTDL-------------NRLRRKVGIVFQ--QWNAFPHlTVLENVMLAPRKvLGLPKDKAEEIAVKQLTHVGLGEK-LK 131
Cdd:PRK13651 83 vLEKLviqktrfkkikkiKEIRRRVGVVFQfaEYQLFEQ-TIEKDIIFGPVS-MGVSKEEAKKRAAKYIELVGLDESyLQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 132 VYPNRMSGGQQQRMAIARALAMSPEYMLFDEVTSALDPMLVGEVLDTLKMLAEEGMTMICVTHEMTFARDVSDRVAFFHQ 211
Cdd:PRK13651 161 RSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTKRTIFFKD 240
|
.
gi 499282096 212 G 212
Cdd:PRK13651 241 G 241
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
17-224 |
3.79e-41 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 141.81 E-value: 3.79e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 17 LKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGTDV--HAKGTDLNRLRRKVGIVFQqwnaFPHL-- 92
Cdd:PRK13649 23 LFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLItsTSKNKDIKQIRKKVGLVFQ----FPESql 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 93 ---TVLENVMLAPRKvLGLPKDKAEEIAVKQLTHVGLGEKL-KVYPNRMSGGQQQRMAIARALAMSPEYMLFDEVTSALD 168
Cdd:PRK13649 99 feeTVLKDVAFGPQN-FGVSQEEAEALAREKLALVGISESLfEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLD 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 499282096 169 PMLVGEVLDTLKMLAEEGMTMICVTHEMTFARDVSDRVAFFHQGIMAEIGSPDQIF 224
Cdd:PRK13649 178 PKGRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIF 233
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
16-236 |
1.81e-40 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 139.41 E-value: 1.81e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 16 VLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGTDVHAkGTDLNR-----LRRKVGIVFQQWNAFP 90
Cdd:PRK14246 25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYF-GKDIFQidaikLRKEVGMVFQQPNPFP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 91 HLTVLENVMLaPRKVLGLpKDKAE--EIAVKQLTHVGLG----EKLKVYPNRMSGGQQQRMAIARALAMSPEYMLFDEVT 164
Cdd:PRK14246 104 HLSIYDNIAY-PLKSHGI-KEKREikKIVEECLRKVGLWkevyDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPT 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499282096 165 SALDPMLVGEVLDTLKMLAEEgMTMICVTHEMTFARDVSDRVAFFHQGIMAEIGSPDQIFASPQNPETQKFL 236
Cdd:PRK14246 182 SMIDIVNSQAIEKLITELKNE-IAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNELTEKYV 252
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1-227 |
2.58e-40 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 139.74 E-value: 2.58e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 1 MIEIENVRKSF-SSLEVLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGTDVhAKGTDLNRLRRKV 79
Cdd:PRK13644 1 MIRLENVSYSYpDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDT-GDFSKLQGIRKLV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 80 GIVFQQ-WNAFPHLTVLENVMLAPRKvLGLPKDKAEEIAVKQLTHVGLGEKLKVYPNRMSGGQQQRMAIARALAMSPEYM 158
Cdd:PRK13644 80 GIVFQNpETQFVGRTVEEDLAFGPEN-LCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499282096 159 LFDEVTSALDPMLVGEVLDTLKMLAEEGMTMICVTHEMTFARDvSDRVAFFHQGIMAEIGSPDQIFASP 227
Cdd:PRK13644 159 IFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEELHD-ADRIIVMDRGKIVLEGEPENVLSDV 226
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-194 |
2.17e-39 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 136.92 E-value: 2.17e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 1 MIEIENVRKSF----SSLEVLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGTDVHAKGTDlnrlr 76
Cdd:COG4525 3 MLTVRHVSVRYpgggQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGAD----- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 77 RkvGIVFQQWNAFPHLTVLENVMLaPRKVLGLPKDKAEEIAVKQLTHVGLGEKLKVYPNRMSGGQQQRMAIARALAMSPE 156
Cdd:COG4525 78 R--GVVFQKDALLPWLNVLDNVAF-GLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPR 154
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 499282096 157 YMLFDEVTSALDPML---VGEVLdtLKMLAEEGMTMICVTH 194
Cdd:COG4525 155 FLLMDEPFGALDALTreqMQELL--LDVWQRTGKGVFLITH 193
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-206 |
3.10e-39 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 141.70 E-value: 3.10e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 1 MIEIENVRKSFSSLEVLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGTDVHAKGTdlnR--LRRK 78
Cdd:COG3845 5 ALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSP---RdaIALG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 79 VGIVFQQWNAFPHLTVLENVMLA--PRKVLGLPKDKAEEIAVKqlthvgLGEK--LKVYPNR----MSGGQQQRMAIARA 150
Cdd:COG3845 82 IGMVHQHFMLVPNLTVAENIVLGlePTKGGRLDRKAARARIRE------LSERygLDVDPDAkvedLSVGEQQRVEILKA 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 499282096 151 LAMSPEYMLFDEVTSALDPMLVGEVLDTLKMLAEEGMTMICVTHEMTFARDVSDRV 206
Cdd:COG3845 156 LYRGARILILDEPTAVLTPQEADELFEILRRLAAEGKSIIFITHKLREVMAIADRV 211
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
2-239 |
5.46e-39 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 136.50 E-value: 5.46e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 2 IEIENVRKSFS---SLEV--LKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGTDVHAKGTD--LNR 74
Cdd:PRK13641 3 IKFENVDYIYSpgtPMEKkgLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNknLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 75 LRRKVGIVFQqwnaFPHL-----TVLENVMLAPRKvLGLPKDKAEEIAVKQLTHVGLGEKL-KVYPNRMSGGQQQRMAIA 148
Cdd:PRK13641 83 LRKKVSLVFQ----FPEAqlfenTVLKDVEFGPKN-FGFSEDEAKEKALKWLKKVGLSEDLiSKSPFELSGGQMRRVAIA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 149 RALAMSPEYMLFDEVTSALDPMLVGEVLDTLKMLAEEGMTMICVTHEMTFARDVSDRVAFFHQGIMAEIGSPDQIFASPQ 228
Cdd:PRK13641 158 GVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDKE 237
|
250
....*....|....*....
gi 499282096 229 --------NPETQKFLASV 239
Cdd:PRK13641 238 wlkkhyldEPATSRFASKL 256
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
9-227 |
9.00e-39 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 136.90 E-value: 9.00e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 9 KSFSSLEVLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGTDVHAKGT--------------DLNR 74
Cdd:PRK13631 34 KQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIGDKKNnhelitnpyskkikNFKE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 75 LRRKVGIVFQqwnaFPHL-----TVLENVMLAPrKVLGLPKDKAEEIAVKQLTHVGLGEK-LKVYPNRMSGGQQQRMAIA 148
Cdd:PRK13631 114 LRRRVSMVFQ----FPEYqlfkdTIEKDIMFGP-VALGVKKSEAKKLAKFYLNKMGLDDSyLERSPFGLSGGQKRRVAIA 188
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499282096 149 RALAMSPEYMLFDEVTSALDPMLVGEVLDTLKMLAEEGMTMICVTHEMTFARDVSDRVAFFHQGIMAEIGSPDQIFASP 227
Cdd:PRK13631 189 GILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTGTPYEIFTDQ 267
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-226 |
9.93e-39 |
|
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: 141.05 E-value: 9.93e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 2 IEIENVrkSFSSLE---VLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGTDVHAkgTDLNRLRRK 78
Cdd:COG4988 337 IELEDV--SFSYPGgrpALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSD--LDPASWRRQ 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 79 VGIVFQQwnafPHL---TVLENVMLAprkvlglpKDKAEEIAVKQ-LTHVGLGEKLKVYPN-----------RMSGGQQQ 143
Cdd:COG4988 413 IAWVPQN----PYLfagTIRENLRLG--------RPDASDEELEAaLEAAGLDEFVAALPDgldtplgeggrGLSGGQAQ 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 144 RMAIARALAMSPEYMLFDEVTSALDPMLVGEVLDTLKMLAeEGMTMICVTHEMTFARDvSDRVAFFHQGIMAEIGSPDQI 223
Cdd:COG4988 481 RLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLA-KGRTVILITHRLALLAQ-ADRILVLDDGRIVEQGTHEEL 558
|
...
gi 499282096 224 FAS 226
Cdd:COG4988 559 LAK 561
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1-223 |
1.01e-38 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 134.83 E-value: 1.01e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 1 MIEIENVRKSFSSLEVLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGTDVHAkgTDLNRLRRKVG 80
Cdd:COG4604 1 MIEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVAT--TPSRELAKRLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 81 IVfQQWNAFPH-LTVLENVMLApR----KvlGLPKDKAEEIAVKQLTHVGLGEKLKVYPNRMSGGQQQRMAIARALAMSP 155
Cdd:COG4604 79 IL-RQENHINSrLTVRELVAFG-RfpysK--GRLTAEDREIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQDT 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499282096 156 EYMLFDEVTSALDPMLVGEVLDTLKMLAEE-GMTMICVTHEMTFARDVSDRVAFFHQGIMAEIGSPDQI 223
Cdd:COG4604 155 DYVLLDEPLNNLDMKHSVQMMKLLRRLADElGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEI 223
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-227 |
1.50e-38 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 136.90 E-value: 1.50e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 1 MIEIENVRKSFS-SLEVLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGTDVhakgTDLNRLRRKV 79
Cdd:PRK11650 3 GLKLQAVRKSYDgKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVV----NELEPADRDI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 80 GIVFQQWNAFPHLTVLENvMLAPRKVLGLPKDKAEEIAVKQLTHVGLGEKLKVYPNRMSGGQQQRMAIARALAMSPEYML 159
Cdd:PRK11650 79 AMVFQNYALYPHMSVREN-MAYGLKIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499282096 160 FDEVTSALDPML-VGEVLDTLKMLAEEGMTMICVTHE----MTFArdvsDRVAFFHQGIMAEIGSPDQIFASP 227
Cdd:PRK11650 158 FDEPLSNLDAKLrVQMRLEIQRLHRRLKTTSLYVTHDqveaMTLA----DRVVVMNGGVAEQIGTPVEVYEKP 226
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-224 |
2.12e-38 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 134.09 E-value: 2.12e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 1 MIEIENVRKSFSSLEVLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCING-LEPiDSGRIVIDGTDVHA-KGTDLNRLRrk 78
Cdd:COG4559 1 MLEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGeLTP-SSGEVRLNGRPLAAwSPWELARRR-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 79 vGIVFQQWN-AFPhLTVLENVMLApRKVLGLPKDKAEEIAVKQLTHVG---LGEKLkvYPnRMSGGQQQRMAIARALA-- 152
Cdd:COG4559 78 -AVLPQHSSlAFP-FTVEEVVALG-RAPHGSSAAQDRQIVREALALVGlahLAGRS--YQ-TLSGGEQQRVQLARVLAql 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499282096 153 -----MSPEYMLFDEVTSALDPMLVGEVLDTLKMLAEEGMTMICVTHEMTFARDVSDRVAFFHQG-IMAEiGSPDQIF 224
Cdd:COG4559 152 wepvdGGPRWLFLDEPTSALDLAHQHAVLRLARQLARRGGGVVAVLHDLNLAAQYADRILLLHQGrLVAQ-GTPEEVL 228
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-206 |
6.40e-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: 132.17 E-value: 6.40e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 1 MIEIENVRKSFS-------SLEVLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGTD-----VHAK 68
Cdd:COG4778 4 LLEVENLSKTFTlhlqggkRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDGgwvdlAQAS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 69 GTDLNRLRRK-VGIVFQQWNAFPHLTVLENVMlAPRKVLGLPKDKAEEIAVKQLTHVGLGEKL-KVYPNRMSGGQQQRMA 146
Cdd:COG4778 84 PREILALRRRtIGYVSQFLRVIPRVSALDVVA-EPLLERGVDREEARARARELLARLNLPERLwDLPPATFSGGEQQRVN 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499282096 147 IARALAMSPEYMLFDEVTSALDP---MLVGEVLDTLKmlaEEGMTMICVTHEMTFARDVSDRV 206
Cdd:COG4778 163 IARGFIADPPLLLLDEPTASLDAanrAVVVELIEEAK---ARGTAIIGIFHDEEVREAVADRV 222
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1-222 |
8.17e-38 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 132.59 E-value: 8.17e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 1 MIEIENVRKSFSSLEVLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGTDVHA-KGTDLNRLRrkv 79
Cdd:PRK13548 2 MLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADwSPAELARRR--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 80 GIVFQQWN-AFPhLTVLENVMLApRKVLGLPKDKAEEIAVKQLTHVGLGEklkvYPNR----MSGGQQQRMAIARALA-- 152
Cdd:PRK13548 79 AVLPQHSSlSFP-FTVEEVVAMG-RAPHGLSRAEDDALVAAALAQVDLAH----LAGRdypqLSGGEQQRVQLARVLAql 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499282096 153 ----MSPEYMLFDEVTSALDPMLVGEVLDTLKMLA-EEGMTMICVTHEMTFARDVSDRVAFFHQGIMAEIGSPDQ 222
Cdd:PRK13548 153 wepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAhERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAE 227
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
2-225 |
1.07e-37 |
|
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: 131.51 E-value: 1.07e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 2 IEIENVRKSFSS---LEVLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGTDVhaKGTDLNRLRRK 78
Cdd:cd03249 1 IEFKNVSFRYPSrpdVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDI--RDLNLRWLRSQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 79 VGIVFQQwnafPHL---TVLENVmlaprkVLGLPKDKAEEI--AVKQL--------------THVG-LGEKLkvypnrmS 138
Cdd:cd03249 79 IGLVSQE----PVLfdgTIAENI------RYGKPDATDEEVeeAAKKAnihdfimslpdgydTLVGeRGSQL-------S 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 139 GGQQQRMAIARALAMSPEYMLFDEVTSALD---PMLVGEVLDTLKmlaeEGMTMICVTHEMTFARDvSDRVAFFHQGIMA 215
Cdd:cd03249 142 GGQKQRIAIARALLRNPKILLLDEATSALDaesEKLVQEALDRAM----KGRTTIVIAHRLSTIRN-ADLIAVLQNGQVV 216
|
250
....*....|
gi 499282096 216 EIGSPDQIFA 225
Cdd:cd03249 217 EQGTHDELMA 226
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
1-224 |
1.47e-37 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 132.94 E-value: 1.47e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 1 MIEIENVRKSFS-----SLEVLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGL-EP----IDSGRIVIDGTdvhAKGT 70
Cdd:PRK13643 1 MIKFEKVNYTYQpnspfASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLlQPtegkVTVGDIVVSST---SKQK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 71 DLNRLRRKVGIVFQqwnaFPHL-----TVLENVMLAPRKvLGLPKDKAEEIAVKQLTHVGLGEKL-KVYPNRMSGGQQQR 144
Cdd:PRK13643 78 EIKPVRKKVGVVFQ----FPESqlfeeTVLKDVAFGPQN-FGIPKEKAEKIAAEKLEMVGLADEFwEKSPFELSGGQMRR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 145 MAIARALAMSPEYMLFDEVTSALDPMLVGEVLDTLKMLAEEGMTMICVTHEMTFARDVSDRVAFFHQGIMAEIGSPDQIF 224
Cdd:PRK13643 153 VAIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVF 232
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-228 |
1.61e-37 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 131.30 E-value: 1.61e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 1 MIEIENVRKSFSSLEVLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGTDVhakgTDL---NRLRR 77
Cdd:COG1137 3 TLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDI----THLpmhKRARL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 78 KVGIVFQQWNAFPHLTVLENVMlAPRKVLGLPKDKAEEIAVKQLTHVGLGEKLKVYPNRMSGGQQQRMAIARALAMSPEY 157
Cdd:COG1137 79 GIGYLPQEASIFRKLTVEDNIL-AVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKF 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499282096 158 MLFDEVTSALDPMLVGEVLDTLKMLAEEGMTmICVT----HEmTFarDVSDRVAFFHQG-IMAEiGSPDQIFASPQ 228
Cdd:COG1137 158 ILLDEPFAGVDPIAVADIQKIIRHLKERGIG-VLITdhnvRE-TL--GICDRAYIISEGkVLAE-GTPEEILNNPL 228
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1-224 |
1.76e-37 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 132.52 E-value: 1.76e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 1 MIEIENVRKSFSSLE------VLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGTDVhAKGTDLNR 74
Cdd:PRK13633 4 MIKCKNVSYKYESNEesteklALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDT-SDEENLWD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 75 LRRKVGIVFQQW-NAFPHLTVLENVMLAPRKvLGLPKDKAEEIAVKQLTHVGLGEKLKVYPNRMSGGQQQRMAIARALAM 153
Cdd:PRK13633 83 IRNKAGMVFQNPdNQIVATIVEEDVAFGPEN-LGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAM 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499282096 154 SPEYMLFDEVTSALDPMLVGEVLDTLKML-AEEGMTMICVTHEMTFARDvSDRVAFFHQGIMAEIGSPDQIF 224
Cdd:PRK13633 162 RPECIIFDEPTAMLDPSGRREVVNTIKELnKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIF 232
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
2-225 |
1.80e-37 |
|
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: 131.20 E-value: 1.80e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 2 IEIENVRKSFS-SLEVLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGTDVhaKGTDLNRLRRKVG 80
Cdd:cd03253 1 IEFENVTFAYDpGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDI--REVTLDSLRRAIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 81 IVFQQ---WNAfphlTVLENVMLaprkvlGLPKDKAEEI--AVKQlthVGLGEKLKVYPN-----------RMSGGQQQR 144
Cdd:cd03253 79 VVPQDtvlFND----TIGYNIRY------GRPDATDEEVieAAKA---AQIHDKIMRFPDgydtivgerglKLSGGEKQR 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 145 MAIARALAMSPEYMLFDEVTSALDPMLVGEVLDTLKMLAeEGMTMICVTHEMTFARDvSDRVAFFHQGIMAEIGSPDQIF 224
Cdd:cd03253 146 VAIARAILKNPPILLLDEATSALDTHTEREIQAALRDVS-KGRTTIVIAHRLSTIVN-ADKIIVLKDGRIVERGTHEELL 223
|
.
gi 499282096 225 A 225
Cdd:cd03253 224 A 224
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
2-212 |
1.94e-37 |
|
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: 130.03 E-value: 1.94e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 2 IEIENVRKSFSSLEVLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGTDVhakgTDLNRLRRKVGI 81
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSY----QKNIEALRRIGA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 82 VFQQWNAFPHLTVLENVMLApRKVLGLPKDKAEEIavkqLTHVGLGEKLKVYPNRMSGGQQQRMAIARALAMSPEYMLFD 161
Cdd:cd03268 77 LIEAPGFYPNLTARENLRLL-ARLLGIRKKRIDEV----LDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILD 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 499282096 162 EVTSALDPMLVGEVLDTLKMLAEEGMTMICVTHEMTFARDVSDRVAFFHQG 212
Cdd:cd03268 152 EPTNGLDPDGIKELRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKG 202
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1-212 |
2.00e-37 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 131.67 E-value: 2.00e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 1 MIEIENVRKSFSSLEVLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGL---EPIDSGRIVIDGTDVHAKGT---DLNR 74
Cdd:PRK09984 4 IIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgDKSAGSHIELLGRTVQREGRlarDIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 75 LRRKVGIVFQQWNAFPHLTVLENVMLAP-------RKVLGLPKDKAEEIAVKQLTHVGLGEKLKVYPNRMSGGQQQRMAI 147
Cdd:PRK09984 84 SRANTGYIFQQFNLVNRLSVLENVLIGAlgstpfwRTCFSWFTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAI 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499282096 148 ARALAMSPEYMLFDEVTSALDPMLVGEVLDTLKMLAE-EGMTMICVTHEMTFARDVSDRVAFFHQG 212
Cdd:PRK09984 164 ARALMQQAKVILADEPIASLDPESARIVMDTLRDINQnDGITVVVTLHQVDYALRYCERIVALRQG 229
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
2-225 |
2.11e-37 |
|
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: 130.81 E-value: 2.11e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 2 IEIENVRKSFSSLE--VLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGTDVhaKGTDLNRLRRKV 79
Cdd:cd03251 1 VEFKNVTFRYPGDGppVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDV--RDYTLASLRRQI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 80 GIVFQQWNAFpHLTVLENVMLAPRKVlglpkDKAEEIAVKQLTHV---------GLGEKLKVYPNRMSGGQQQRMAIARA 150
Cdd:cd03251 79 GLVSQDVFLF-NDTVAENIAYGRPGA-----TREEVEEAARAANAhefimelpeGYDTVIGERGVKLSGGQRQRIAIARA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499282096 151 LAMSPEYMLFDEVTSALD---PMLVGEVLDTLKmlaeEGMTMICVTHEMTFARDvSDRVAFFHQGIMAEIGSPDQIFA 225
Cdd:cd03251 153 LLKDPPILILDEATSALDtesERLVQAALERLM----KNRTTFVIAHRLSTIEN-ADRIVVLEDGKIVERGTHEELLA 225
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
17-238 |
6.84e-37 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 132.01 E-value: 6.84e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 17 LKGIDLTVEKGEVVTIIGGSGSGKSTL---LTCInglEPIDSGRIVIDGTDV-HAKGTDLNRLRRKVGIVFQqwNAFPHL 92
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTLarlLTMI---ETPTGGELYYQGQDLlKADPEAQKLLRQKIQIVFQ--NPYGSL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 93 TvlenvmlaPRKVLG------------LPKDKAEEIAVKQLTHVGL-GEKLKVYPNRMSGGQQQRMAIARALAMSPEYML 159
Cdd:PRK11308 106 N--------PRKKVGqileepllintsLSAAERREKALAMMAKVGLrPEHYDRYPHMFSGGQRQRIAIARALMLDPDVVV 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 160 FDEVTSALDPMLVGEVLDTLKMLAEE-GMTMICVTHEMTFARDVSDRVAFFHQGIMAEIGSPDQIFASPQNPETQKFLAS 238
Cdd:PRK11308 178 ADEPVSALDVSVQAQVLNLMMDLQQElGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFNNPRHPYTQALLSA 257
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1-205 |
7.27e-37 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 129.32 E-value: 7.27e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 1 MIEIENVRKSFSSLEVLkgIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGTDvHAKGTDLnrlRRKVG 80
Cdd:PRK10771 1 MLKLTDITWLYHHLPMR--FDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQD-HTTTPPS---RRPVS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 81 IVFQQWNAFPHLTVLENVMLAPRKVLGL---PKDKAEEIAVKqlthVGLGEKLKVYPNRMSGGQQQRMAIARALAMSPEY 157
Cdd:PRK10771 75 MLFQENNLFSHLTVAQNIGLGLNPGLKLnaaQREKLHAIARQ----MGIEDLLARLPGQLSGGQRQRVALARCLVREQPI 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 499282096 158 MLFDEVTSALDPMLVGEVLDTLKML-AEEGMTMICVTHEMTFARDVSDR 205
Cdd:PRK10771 151 LLLDEPFSALDPALRQEMLTLVSQVcQERQLTLLMVSHSLEDAARIAPR 199
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1-225 |
1.19e-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: 134.93 E-value: 1.19e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 1 MIEIENVRKSFSSLE--VLK---GIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSG----RIVIDGTDVHAKGTD 71
Cdd:TIGR03269 279 IIKVRNVSKRYISVDrgVVKavdNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGevnvRVGDEWVDMTKPGPD 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 72 LN-RLRRKVGIVFQQWNAFPHLTVLENVMLAPRkvLGLPKDKAEEIAVKQLTHVGLGEK-----LKVYPNRMSGGQQQRM 145
Cdd:TIGR03269 359 GRgRAKRYIGILHQEYDLYPHRTVLDNLTEAIG--LELPDELARMKAVITLKMVGFDEEkaeeiLDKYPDELSEGERHRV 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 146 AIARALAMSPEYMLFDEVTSALDPMLVGEVLDT-LKMLAEEGMTMICVTHEMTFARDVSDRVAFFHQGIMAEIGSPDQIF 224
Cdd:TIGR03269 437 ALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSiLKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEEIV 516
|
.
gi 499282096 225 A 225
Cdd:TIGR03269 517 E 517
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
2-227 |
2.79e-36 |
|
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: 128.04 E-value: 2.79e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 2 IEIENVRKSFSSLEVLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGTDVhakgTDL---NRLRRK 78
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDI----TKLpmhKRARLG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 79 VGIVFQQWNAFPHLTVLENVMLAPRkVLGLPKDKAEEIAVKQLTHVGLGEKLKVYPNRMSGGQQQRMAIARALAMSPEYM 158
Cdd:cd03218 77 IGYLPQEASIFRKLTVEENILAVLE-IRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 159 LFDEVTSALDPMLVGEVLDTLKMLAEEGMTMICVTHEMTFARDVSDRVAFFHQG-IMAEiGSPDQIFASP 227
Cdd:cd03218 156 LLDEPFAGVDPIAVQDIQKIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGkVLAE-GTPEEIAANE 224
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1-218 |
4.02e-36 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 127.10 E-value: 4.02e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 1 MIEIENVRKSFSSLE----VLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGTDVHakgTDLNRLR 76
Cdd:cd03266 1 MITADALTKRFRDVKktvqAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVV---KEPAEAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 77 RKVGIVFQQWNAFPHLTVLENVMLAPRkVLGLPKDKAEEiAVKQLTHV-GLGEKLKVYPNRMSGGQQQRMAIARALAMSP 155
Cdd:cd03266 78 RRLGFVSDSTGLYDRLTARENLEYFAG-LYGLKGDELTA-RLEELADRlGMEELLDRRVGGFSTGMRQKVAIARALVHDP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499282096 156 EYMLFDEVTSALDPMLVGEVLDTLKMLAEEGMTMICVTHEMTFARDVSDRVAFFHQGIMAEIG 218
Cdd:cd03266 156 PVLLLDEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-195 |
4.56e-36 |
|
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: 126.44 E-value: 4.56e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 1 MIEIENVRKSFSSLEVLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGTDVHAKGTDlnrLRRKVG 80
Cdd:COG4133 2 MLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDARED---YRRRLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 81 IVFQQWNAFPHLTVLENVMLApRKVLGLPKDKAEEIAVkqLTHVGLGEKLKVYPNRMSGGQQQRMAIARALAMSPEYMLF 160
Cdd:COG4133 79 YLGHADGLKPELTVRENLRFW-AALYGLRADREAIDEA--LEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLL 155
|
170 180 190
....*....|....*....|....*....|....*
gi 499282096 161 DEVTSALDPMLVGEVLDTLKMLAEEGMTMICVTHE 195
Cdd:COG4133 156 DEPFTALDAAGVALLAELIAAHLARGGAVLLTTHQ 190
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
15-226 |
1.30e-35 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 127.59 E-value: 1.30e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 15 EVLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGTDVHAKGTD--LNRLRRKVGIVFQqwnaFPHL 92
Cdd:PRK13646 21 QAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDkyIRPVRKRIGMVFQ----FPES 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 93 TVLEN-----VMLAPrKVLGLPKDKAEEIAVKQLTHVGLGEK-LKVYPNRMSGGQQQRMAIARALAMSPEYMLFDEVTSA 166
Cdd:PRK13646 97 QLFEDtvereIIFGP-KNFKMNLDEVKNYAHRLLMDLGFSRDvMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAG 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499282096 167 LDPMLVGEVLDTLKMLA-EEGMTMICVTHEMTFARDVSDRVAFFHQGIMAEIGSPDQIFAS 226
Cdd:PRK13646 176 LDPQSKRQVMRLLKSLQtDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFKD 236
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1-225 |
1.83e-35 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 127.27 E-value: 1.83e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 1 MIEIENVRKSFSS-LEVLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGTDVHAKGTDLNRLRRKV 79
Cdd:PRK13636 5 ILKVEELNYNYSDgTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRKGLMKLRESV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 80 GIVFQQW-NAFPHLTVLENVMLAPRKvLGLPKDKAEEIAVKQLTHVGLgEKLKVYPNR-MSGGQQQRMAIARALAMSPEY 157
Cdd:PRK13636 85 GMVFQDPdNQLFSASVYQDVSFGAVN-LKLPEDEVRKRVDNALKRTGI-EHLKDKPTHcLSFGQKKRVAIAGVLVMEPKV 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499282096 158 MLFDEVTSALDPMLVGEVLDTLKMLAEE-GMTMICVTHEMTFARDVSDRVAFFHQGIMAEIGSPDQIFA 225
Cdd:PRK13636 163 LVLDEPTAGLDPMGVSEIMKLLVEMQKElGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFA 231
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-225 |
4.38e-35 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 126.00 E-value: 4.38e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 1 MIEIENVRKSFSSLE---VLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGTDVHAKgtDLNRLRR 77
Cdd:PRK13650 4 IIEVKNLTFKYKEDQekyTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEE--NVWDIRH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 78 KVGIVFQQW-NAFPHLTVLENVMLAPRKVlGLPKDKAEEIAVKQLTHVGLGEKLKVYPNRMSGGQQQRMAIARALAMSPE 156
Cdd:PRK13650 82 KIGMVFQNPdNQFVGATVEDDVAFGLENK-GIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPK 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 157 YMLFDEVTSALDPMLVGEVLDTLKMLAEE-GMTMICVTHEMTFARdVSDRVAFFHQGIMAEIGSPDQIFA 225
Cdd:PRK13650 161 IIILDEATSMLDPEGRLELIKTIKGIRDDyQMTVISITHDLDEVA-LSDRVLVMKNGQVESTSTPRELFS 229
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
2-227 |
5.86e-35 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 131.62 E-value: 5.86e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 2 IEIENV--RKSFSSLEVLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGTDVhaKGTDLNRLRRKV 79
Cdd:TIGR03797 452 IEVDRVtfRYRPDGPLILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDL--AGLDVQAVRRQL 529
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 80 GIVFQQWNAFPHlTVLENVMLAPRkvlgLPKDKAEEIAvkqlTHVGLGEKLKVYPNRM-----------SGGQQQRMAIA 148
Cdd:TIGR03797 530 GVVLQNGRLMSG-SIFENIAGGAP----LTLDEAWEAA----RMAGLAEDIRAMPMGMhtvisegggtlSGGQRQRLLIA 600
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 149 RALAMSPEYMLFDEVTSALD---PMLVGEVLDTLKmlaeegMTMICVTHEMTFARDvSDRVAFFHQGIMAEIGSPDQIFA 225
Cdd:TIGR03797 601 RALVRKPRILLFDEATSALDnrtQAIVSESLERLK------VTRIVIAHRLSTIRN-ADRIYVLDAGRVVQQGTYDELMA 673
|
..
gi 499282096 226 SP 227
Cdd:TIGR03797 674 RE 675
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
2-238 |
9.59e-35 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 124.43 E-value: 9.59e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 2 IEIENVRKSfSSLEVLKGIDLTVEKGEVVTIIGGSGSGKStlLTCINGLEPID------SGRIVIDGTDVHAkgtdlNRL 75
Cdd:PRK10418 5 IELRNIALQ-AAQPLVHGVSLTLQRGRVLALVGGSGSGKS--LTCAAALGILPagvrqtAGRVLLDGKPVAP-----CAL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 76 R-RKVGIVFQQ-WNAFPHLTVLENVMLAPRKVLGLPKDKAEEIAVkqLTHVGLGEK---LKVYPNRMSGGQQQRMAIARA 150
Cdd:PRK10418 77 RgRKIATIMQNpRSAFNPLHTMHTHARETCLALGKPADDATLTAA--LEAVGLENAarvLKLYPFEMSGGMLQRMMIALA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 151 LAMSPEYMLFDEVTSALDPMLVGEVLDTL-KMLAEEGMTMICVTHEMTFARDVSDRVAFFHQGIMAEIGSPDQIFASPQN 229
Cdd:PRK10418 155 LLCEAPFIIADEPTTDLDVVAQARILDLLeSIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPKH 234
|
....*....
gi 499282096 230 PETQKFLAS 238
Cdd:PRK10418 235 AVTRSLVSA 243
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
1-199 |
1.30e-34 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 123.35 E-value: 1.30e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 1 MIEIENVRKSF----SSLEVLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGTDVHAKGTDLN-RL 75
Cdd:PRK10584 6 IVEVHHLKKSVgqgeHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARaKL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 76 R-RKVGIVFQQWNAFPHLTVLENVMLaPRKVLGLPKDKAEEIAVKQLTHVGLGEKLKVYPNRMSGGQQQRMAIARALAMS 154
Cdd:PRK10584 86 RaKHVGFVFQSFMLIPTLNALENVEL-PALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGR 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 499282096 155 PEYMLFDEVTSALDPMLVGEVLDTLKMLAEE-GMTMICVTHEMTFA 199
Cdd:PRK10584 165 PDVLFADEPTGNLDRQTGDKIADLLFSLNREhGTTLILVTHDLQLA 210
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
3-206 |
1.47e-34 |
|
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: 122.75 E-value: 1.47e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 3 EIENVRKSFS-SLEVLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGTDVHAKgtdlnRLRRKVGI 81
Cdd:cd03226 1 RIENISFSYKkGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAK-----ERRKSIGY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 82 VFQqwNAFPHL---TVLENVMLaprkvlGLP-KDKAEEIAVKQLTHVGLGEKLKVYPNRMSGGQQQRMAIARALAMSPEY 157
Cdd:cd03226 76 VMQ--DVDYQLftdSVREELLL------GLKeLDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDL 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 499282096 158 MLFDEVTSALDPMLVGEVLDTLKMLAEEGMTMICVTHEMTFARDVSDRV 206
Cdd:cd03226 148 LIFDEPTSGLDYKNMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRV 196
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
2-226 |
3.51e-34 |
|
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: 122.59 E-value: 3.51e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 2 IEIENVRKSF--SSLEVLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGTDVHAkgTDLNRLRRKV 79
Cdd:cd03252 1 ITFEHVRFRYkpDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLAL--ADPAWLRRQV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 80 GIVFQQwNAFPHLTVLENVMLAPRkvlGLPKDKAEEIAVKQLTHVGLGEKLKVYPN-------RMSGGQQQRMAIARALA 152
Cdd:cd03252 79 GVVLQE-NVLFNRSIRDNIALADP---GMSMERVIEAAKLAGAHDFISELPEGYDTivgeqgaGLSGGQRQRIAIARALI 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499282096 153 MSPEYMLFDEVTSALDPMLVGEVLDTLKMLAeEGMTMICVTHEMTFARDvSDRVAFFHQGIMAEIGSPDQIFAS 226
Cdd:cd03252 155 HNPRILIFDEATSALDYESEHAIMRNMHDIC-AGRTVIIIAHRLSTVKN-ADRIIVMEKGRIVEQGSHDELLAE 226
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
4-218 |
4.22e-34 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 122.86 E-value: 4.22e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 4 IENVRKSFSSLEVLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVidgtdvhAKGTDLNRLRRKVGIVF 83
Cdd:PRK11247 15 LNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELL-------AGTAPLAEAREDTRLMF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 84 QQWNAFPHLTVLENVMLAPRkvlGLPKDKAEEiavkQLTHVGLGEKLKVYPNRMSGGQQQRMAIARALAMSPEYMLFDEV 163
Cdd:PRK11247 88 QDARLLPWKKVIDNVGLGLK---GQWRDAALQ----ALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 499282096 164 TSALDPMLVGEVLDTLKML-AEEGMTMICVTHEMTFARDVSDRVAFFHQGimaEIG 218
Cdd:PRK11247 161 LGALDALTRIEMQDLIESLwQQHGFTVLLVTHDVSEAVAMADRVLLIEEG---KIG 213
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
2-225 |
5.11e-34 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 127.61 E-value: 5.11e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 2 IEIENVRKSFSSLEVLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLE--PIDSGRIVI----------------DGT 63
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDqyEPTSGRIIYhvalcekcgyverpskVGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 64 DVHAKGTDLN---------------RLRRKVGIVFQQWNA-FPHLTVLENVMLAPRKvLGLPKDKAEEIAVKQLTHVGLG 127
Cdd:TIGR03269 81 PCPVCGGTLEpeevdfwnlsdklrrRIRKRIAIMLQRTFAlYGDDTVLDNVLEALEE-IGYEGKEAVGRAVDLIEMVQLS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 128 EKLKVYPNRMSGGQQQRMAIARALAMSPEYMLFDEVTSALDPMLVGEVLDTLKMLA-EEGMTMICVTHEMTFARDVSDRV 206
Cdd:TIGR03269 160 HRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVkASGISMVLTSHWPEVIEDLSDKA 239
|
250
....*....|....*....
gi 499282096 207 AFFHQGIMAEIGSPDQIFA 225
Cdd:TIGR03269 240 IWLENGEIKEEGTPDEVVA 258
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1-228 |
5.91e-34 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 122.94 E-value: 5.91e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 1 MIEIENVRKSFSSLE--VLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGTDVHAKgtDLNRLRRK 78
Cdd:PRK13648 7 IIVFKNVSFQYQSDAsfTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDD--NFEKLRKH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 79 VGIVFQQ-WNAFPHLTV-------LENVMLaprkvlglPKDKAEEIAVKQLTHVGLGEKLKVYPNRMSGGQQQRMAIARA 150
Cdd:PRK13648 85 IGIVFQNpDNQFVGSIVkydvafgLENHAV--------PYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGV 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499282096 151 LAMSPEYMLFDEVTSALDPMLVGEVLDTLKMLAEE-GMTMICVTHEMTFARDvSDRVAFFHQGIMAEIGSPDQIFASPQ 228
Cdd:PRK13648 157 LALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEhNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIFDHAE 234
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
2-212 |
6.23e-34 |
|
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: 121.23 E-value: 6.23e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 2 IEIENVRKSFSSLEVLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGTDVHAKGtdlnrlRRKVGI 81
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAA------RNRIGY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 82 VFQQWNAFPHLTVLENVM-LAPRKvlGLPKDKAEEIAVKQLTHVGLGEKLKVYPNRMSGGQQQRMAIARALAMSPEYMLF 160
Cdd:cd03269 75 LPEERGLYPKMKVIDQLVyLAQLK--GLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLIL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 499282096 161 DEVTSALDPMLVGEVLDTLKMLAEEGMTMICVTHEMTFARDVSDRVAFFHQG 212
Cdd:cd03269 153 DEPFSGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKG 204
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
2-226 |
1.19e-33 |
|
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: 120.79 E-value: 1.19e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 2 IEIENVrkSFSSLE---VLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGTDVhaKGTDLNRLRRK 78
Cdd:cd03254 3 IEFENV--NFSYDEkkpVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDI--RDISRKSLRSM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 79 VGIVFQQwnafPHL---TVLENVMLAPRkvlgLPKDKAEEIAVKQLTHVGLGEKLK------VYPN--RMSGGQQQRMAI 147
Cdd:cd03254 79 IGVVLQD----TFLfsgTIMENIRLGRP----NATDEEVIEAAKEAGAHDFIMKLPngydtvLGENggNLSQGERQLLAI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 148 ARALAMSPEYMLFDEVTSALDP---MLVGEVLDTLKmlaeEGMTMICVTHEMTFARDvSDRVAFFHQGIMAEIGSPDQIF 224
Cdd:cd03254 151 ARAMLRDPKILILDEATSNIDTeteKLIQEALEKLM----KGRTSIIIAHRLSTIKN-ADKILVLDDGKIIEEGTHDELL 225
|
..
gi 499282096 225 AS 226
Cdd:cd03254 226 AK 227
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
12-239 |
1.47e-33 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 123.28 E-value: 1.47e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 12 SSLEVLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGTDVHAKGTDLNRLRRK-VGIVFQQWNAF- 89
Cdd:PRK15079 32 KTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRAVRSdIQMIFQDPLASl 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 90 -PHLTVLEnVMLAPRKVLgLPKDKAEEIA--VKQ-LTHVGLGEKL-KVYPNRMSGGQQQRMAIARALAMSPEYMLFDEVT 164
Cdd:PRK15079 112 nPRMTIGE-IIAEPLRTY-HPKLSRQEVKdrVKAmMLKVGLLPNLiNRYPHEFSGGQCQRIGIARALILEPKLIICDEPV 189
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499282096 165 SALDPMLVGEVLDTLKMLAEE-GMTMICVTHEMTFARDVSDRVAFFHQGIMAEIGSPDQIFASPQNPETQKFLASV 239
Cdd:PRK15079 190 SALDVSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNPLHPYTKALMSAV 265
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-223 |
1.65e-33 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 122.52 E-value: 1.65e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 1 MIEIENVRKSFSSLEVLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGTDVHAKgtdlnrLRRKVG 80
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPE------DRRRIG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 81 -------IvfqqwnaFPHLTVLENVM-LAPRKvlGLPKDKAEEIAVKQLTHVGLGEKLKVYPNRMSGGQQQRMAIARALA 152
Cdd:COG4152 75 ylpeergL-------YPKMKVGEQLVyLARLK--GLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALL 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499282096 153 MSPEYMLFDEVTSALDPMLVGEVLDTLKMLAEEGMTMICVTHEMTFARDVSDRVAFFHQGIMAEIGSPDQI 223
Cdd:COG4152 146 HDPELLILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEI 216
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
2-228 |
2.07e-33 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 121.83 E-value: 2.07e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 2 IEIENVRKSF--SSLEVLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGL---EPIDSGRIVIDGTDVHAKgtDLNRLR 76
Cdd:PRK13640 6 VEFKHVSFTYpdSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLllpDDNPNSKITVDGITLTAK--TVWDIR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 77 RKVGIVFQQW-NAFPHLTVLENVM--LAPRKVlglPKDKAEEIAVKQLTHVGLGEKLKVYPNRMSGGQQQRMAIARALAM 153
Cdd:PRK13640 84 EKVGIVFQNPdNQFVGATVGDDVAfgLENRAV---PRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAV 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499282096 154 SPEYMLFDEVTSALDPMLVGEVLDTLKMLAEE-GMTMICVTHEMTFArDVSDRVAFFHQGIMAEIGSPDQIFASPQ 228
Cdd:PRK13640 161 EPKIIILDESTSMLDPAGKEQILKLIRKLKKKnNLTVISITHDIDEA-NMADQVLVLDDGKLLAQGSPVEIFSKVE 235
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-225 |
5.47e-33 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 119.80 E-value: 5.47e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 1 MIEIENVRKSF-------SSL---------------EVLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRI 58
Cdd:COG1134 4 MIEVENVSKSYrlyhepsRSLkelllrrrrtrreefWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 59 VIDGTdVHAKgtdLNrlrrkVGIVFQqwnafPHLTVLENVMLAPRkVLGLPKD----KAEEI---AvkqlthvGLGE--- 128
Cdd:COG1134 84 EVNGR-VSAL---LE-----LGAGFH-----PELTGRENIYLNGR-LLGLSRKeideKFDEIvefA-------ELGDfid 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 129 -KLKVYpnrmSGGQQQRMAIARALAMSPEYMLFDEVTSALDPMLVGEVLDTLKMLAEEGMTMICVTHEMTFARDVSDRVA 207
Cdd:COG1134 142 qPVKTY----SSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRESGRTVIFVSHSMGAVRRLCDRAI 217
|
250
....*....|....*...
gi 499282096 208 FFHQGIMAEIGSPDQIFA 225
Cdd:COG1134 218 WLEKGRLVMDGDPEEVIA 235
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
13-227 |
6.23e-33 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 120.18 E-value: 6.23e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 13 SLEVLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGTDVHA-KGTDLNRLRRKVGIVFQQ-WNAF- 89
Cdd:PRK10419 24 HQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKlNRAQRKAFRRDIQMVFQDsISAVn 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 90 PHLTVLENVMLAPRKVLGLpkDKAEEIAVKQ--LTHVGLG-EKLKVYPNRMSGGQQQRMAIARALAMSPEYMLFDEVTSA 166
Cdd:PRK10419 104 PRKTVREIIREPLRHLLSL--DKAERLARASemLRAVDLDdSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSN 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499282096 167 LDPMLVGEVLDTLKMLAEE-GMTMICVTHEMTFARDVSDRVAFFHQGIMAEIG--SPDQIFASP 227
Cdd:PRK10419 182 LDLVLQAGVIRLLKKLQQQfGTACLFITHDLRLVERFCQRVMVMDNGQIVETQpvGDKLTFSSP 245
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
2-212 |
1.49e-32 |
|
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: 116.55 E-value: 1.49e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 2 IEIENVRKSFSSLE--VLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGTDVHAkgTDLNRLRRKV 79
Cdd:cd03246 1 LEVENVSFRYPGAEppVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQ--WDPNELGDHV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 80 GIVFQQWNAFPHlTVLENVmlaprkvlglpkdkaeeiavkqlthvglgeklkvypnrMSGGQQQRMAIARALAMSPEYML 159
Cdd:cd03246 79 GYLPQDDELFSG-SIAENI--------------------------------------LSGGQRQRLGLARALYGNPRILV 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 499282096 160 FDEVTSALDPMLVGEVLDTLKMLAEEGMTMICVTHEMTFARDVsDRVAFFHQG 212
Cdd:cd03246 120 LDEPNSHLDVEGERALNQAIAALKAAGATRIVIAHRPETLASA-DRILVLEDG 171
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1-196 |
2.69e-32 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 118.26 E-value: 2.69e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 1 MIEIENVRKSFSSLEVLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGTDVHAKGTDLnrlrrkvG 80
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAER-------G 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 81 IVFQQWNAFPHLTVLENVMLAPRkVLGLPKDKAEEIAVKQLTHVGLGEKLKVYPNRMSGGQQQRMAIARALAMSPEYMLF 160
Cdd:PRK11248 74 VVFQNEGLLPWRNVQDNVAFGLQ-LAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLL 152
|
170 180 190
....*....|....*....|....*....|....*...
gi 499282096 161 DEVTSALDpMLVGEVLDT--LKMLAEEGMTMICVTHEM 196
Cdd:PRK11248 153 DEPFGALD-AFTREQMQTllLKLWQETGKQVLLITHDI 189
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
5-228 |
3.03e-32 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 117.69 E-value: 3.03e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 5 ENVRKSFSSLEVLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGTDV-----HAkgtdlnRLRRKV 79
Cdd:PRK10895 7 KNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDIsllplHA------RARRGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 80 GIVFQQWNAFPHLTVLENVM--LAPRKVLGLP--KDKAEEIAVK-QLTHV--GLGEKLkvypnrmSGGQQQRMAIARALA 152
Cdd:PRK10895 81 GYLPQEASIFRRLSVYDNLMavLQIRDDLSAEqrEDRANELMEEfHIEHLrdSMGQSL-------SGGERRRVEIARALA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499282096 153 MSPEYMLFDEVTSALDPMLVGEVLDTLKMLAEEGMTMICVTHEMTFARDVSDRVAFFHQGIMAEIGSPDQIFASPQ 228
Cdd:PRK10895 154 ANPKFILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDEH 229
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1-214 |
5.42e-32 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 116.51 E-value: 5.42e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 1 MIEIENVRKSF-SSLEVLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGTDV-HAKGTDLNRLRRK 78
Cdd:PRK10908 1 MIRFEHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDItRLKNREVPFLRRQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 79 VGIVFQQWNAFPHLTVLENVMLaPRKVLGLPKDKAEEIAVKQLTHVGLGEKLKVYPNRMSGGQQQRMAIARALAMSPEYM 158
Cdd:PRK10908 81 IGMIFQDHHLLMDRTVYDNVAI-PLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 499282096 159 LFDEVTSALDPMLVGEVLDTLKMLAEEGMTMICVTHEMTFARDVSDRVAFFHQGIM 214
Cdd:PRK10908 160 LADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1-236 |
1.12e-31 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 116.79 E-value: 1.12e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 1 MIEIENVRKSFSSLEVLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGTDVHAKG-TDLNRLRRKV 79
Cdd:PRK11831 7 LVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSrSRLYTVRKRM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 80 GIVFQQWNAFPHLTVLENVMLAPRKVLGLPKDKAEEIAVKQLTHVGLGEKLKVYPNRMSGGQQQRMAIARALAMSPEYML 159
Cdd:PRK11831 87 SMLFQSGALFTDMNVFDNVAYPLREHTQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIM 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 160 FDEVTSALDPMLVGeVLdtLKMLAE----EGMTMICVTHEMTFARDVSDR---VAffHQGIMAEiGSPDQIFASPqNPET 232
Cdd:PRK11831 167 FDEPFVGQDPITMG-VL--VKLISElnsaLGVTCVVVSHDVPEVLSIADHayiVA--DKKIVAH-GSAQALQANP-DPRV 239
|
....
gi 499282096 233 QKFL 236
Cdd:PRK11831 240 RQFL 243
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-194 |
2.50e-31 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 115.57 E-value: 2.50e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 1 MIEIENVRKSFSSLEVLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLE-PIDSGRIVIDGTDVhaKGTDLNRLRRKV 79
Cdd:COG1119 3 LLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLpPTYGNDVRLFGERR--GGEDVWELRKRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 80 GIV--FQQWNAFPHLTVLENVMLAPRKVLGL---PKDKAEEIAVKQLTHVGLGEKLKVYPNRMSGGQQQRMAIARALAMS 154
Cdd:COG1119 81 GLVspALQLRFPRDETVLDVVLSGFFDSIGLyrePTDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIARALVKD 160
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 499282096 155 PEYMLFDEVTSALDPMLVGEVLDTLKMLAEEG-MTMICVTH 194
Cdd:COG1119 161 PELLILDEPTAGLDLGARELLLALLDKLAAEGaPTLVLVTH 201
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
2-220 |
2.57e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 115.99 E-value: 2.57e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 2 IEIENVRKSF-SSLEVLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGTDVHAKgtDLNRLRRKVG 80
Cdd:PRK13647 5 IEVEDLHFRYkDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAE--NEKWVRSKVG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 81 IVFQQWN--AFPhLTVLENVMLAPRKvLGLPKDKAEEIAVKQLTHVGLGEKLKVYPNRMSGGQQQRMAIARALAMSPEYM 158
Cdd:PRK13647 83 LVFQDPDdqVFS-STVWDDVAFGPVN-MGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499282096 159 LFDEVTSALDPMLVGEVLDTLKMLAEEGMTMICVTHEMTFARDVSDRVAFFHQGIMAEIGSP 220
Cdd:PRK13647 161 VLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDK 222
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
10-194 |
2.98e-31 |
|
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: 113.80 E-value: 2.98e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 10 SFSSLEVLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGL--EPIDSGRIVIDGTDVHakgtdLNRLRRKVGIVFQQWN 87
Cdd:cd03213 18 SKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRrtGLGVSGEVLINGRPLD-----KRSFRKIIGYVPQDDI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 88 AFPHLTVLENVMLAPrkvlglpkdkaeeiavkqlthvglgeKLKvypnRMSGGQQQRMAIARALAMSPEYMLFDEVTSAL 167
Cdd:cd03213 93 LHPTLTVRETLMFAA--------------------------KLR----GLSGGERKRVSIALELVSNPSLLFLDEPTSGL 142
|
170 180
....*....|....*....|....*..
gi 499282096 168 DPMLVGEVLDTLKMLAEEGMTMICVTH 194
Cdd:cd03213 143 DSSSALQVMSLLRRLADTGRTIICSIH 169
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
15-194 |
3.15e-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: 3.15e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 15 EVLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGTDVHAkgTDLNRLRRKVGIVFQQwnafPHL-- 92
Cdd:TIGR02868 349 PVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSS--LDQDEVRRRVSVCAQD----AHLfd 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 93 -TVLENVMLAprkvlglPKDKAEEIAVKQLTHVGLGEKLKVYPN-----------RMSGGQQQRMAIARALAMSPEYMLF 160
Cdd:TIGR02868 423 tTVRENLRLA-------RPDATDEELWAALERVGLADWLRALPDgldtvlgeggaRLSGGERQRLALARALLADAPILLL 495
|
170 180 190
....*....|....*....|....*....|....
gi 499282096 161 DEVTSALDPMLVGEVLDTLkMLAEEGMTMICVTH 194
Cdd:TIGR02868 496 DEPTEHLDAETADELLEDL-LAALSGRTVVLITH 528
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
13-206 |
4.42e-31 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 114.53 E-value: 4.42e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 13 SLEVLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIdgtdvhaKGTDLNRL---------RRKVGIVF 83
Cdd:PRK11629 21 QTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIF-------NGQPMSKLssaakaelrNQKLGFIY 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 84 QQWNAFPHLTVLENVMLaPRKVLGLPKDKAEEIAVKQLTHVGLGEKLKVYPNRMSGGQQQRMAIARALAMSPEYMLFDEV 163
Cdd:PRK11629 94 QFHHLLPDFTALENVAM-PLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEP 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 499282096 164 TSALDPMLVGEVLDTLKML-AEEGMTMICVTHEMTFARDVSDRV 206
Cdd:PRK11629 173 TGNLDARNADSIFQLLGELnRLQGTAFLVVTHDLQLAKRMSRQL 216
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
2-212 |
1.51e-30 |
|
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: 112.29 E-value: 1.51e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 2 IEIENVRKSFSSLEVLKGIDLTVEKGeVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGTDVHAKGtdlNRLRRKVGI 81
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQP---QKLRRRIGY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 82 VFQQWNAFPHLTVLEnvMLAPRKVL-GLPKDKAEEIAVKQLTHVGLGEKLKVYPNRMSGGQQQRMAIARALAMSPEYMLF 160
Cdd:cd03264 77 LPQEFGVYPNFTVRE--FLDYIAWLkGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIV 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 499282096 161 DEVTSALDPmlvGEVLDTLKMLAE--EGMTMICVTHEMTFARDVSDRVAFFHQG 212
Cdd:cd03264 155 DEPTAGLDP---EERIRFRNLLSElgEDRIVILSTHIVEDVESLCNQVAVLNKG 205
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1-227 |
2.37e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 113.74 E-value: 2.37e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 1 MIEIENVRKSFS-SLEVLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGTDVHAKgtDLNRLRRKV 79
Cdd:PRK13652 3 LIETRDLCYSYSgSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKE--NIREVRKFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 80 GIVFQQWN-AFPHLTVLENVMLAPRKvLGLPKDKAEEIAVKQLTHVGLGEKLKVYPNRMSGGQQQRMAIARALAMSPEYM 158
Cdd:PRK13652 81 GLVFQNPDdQIFSPTVEQDIAFGPIN-LGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 159 LFDEVTSALDPMLVGEVLDTLKMLAEE-GMTMICVTHEMTFARDVSDRVAFFHQGIMAEIGSPDQIFASP 227
Cdd:PRK13652 160 VLDEPTAGLDPQGVKELIDFLNDLPETyGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
16-237 |
2.98e-30 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 117.50 E-value: 2.98e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 16 VLKGIDLTVEKGEVVTIIGGSGSGKST----LLTCINGlepidSGRIVIDGTDVHakgtDLNR-----LRRKVGIVFQQW 86
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLINS-----QGEIWFDGQPLH----NLNRrqllpVRHRIQVVFQDP 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 87 NAF--PHLTVLENVMLAPR---KVLGLPKDKAEEIAVkqLTHVGLG-EKLKVYPNRMSGGQQQRMAIARALAMSPEYMLF 160
Cdd:PRK15134 372 NSSlnPRLNVLQIIEEGLRvhqPTLSAAQREQQVIAV--MEEVGLDpETRHRYPAEFSGGQRQRIAIARALILKPSLIIL 449
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499282096 161 DEVTSALDPMLVGEVLDTLKMLAEE-GMTMICVTHEMTFARDVSDRVAFFHQGIMAEIGSPDQIFASPQNPETQKFLA 237
Cdd:PRK15134 450 DEPTSSLDKTVQAQILALLKSLQQKhQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERVFAAPQQEYTRQLLA 527
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
2-226 |
3.50e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 113.56 E-value: 3.50e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 2 IEIENVRKSFS-----SLEVLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGTDVHA---KGTDLN 73
Cdd:PRK13645 7 IILDNVSYTYAkktpfEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPAnlkKIKEVK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 74 RLRRKVGIVFQqwnaFPHL-----TVLENVMLAPRKvLGLPKDKAEEIAVKQLTHVGLGEK-LKVYPNRMSGGQQQRMAI 147
Cdd:PRK13645 87 RLRKEIGLVFQ----FPEYqlfqeTIEKDIAFGPVN-LGENKQEAYKKVPELLKLVQLPEDyVKRSPFELSGGQKRRVAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 148 ARALAMSPEYMLFDEVTSALDPMLVGEVLDT-LKMLAEEGMTMICVTHEMTFARDVSDRVAFFHQGIMAEIGSPDQIFAS 226
Cdd:PRK13645 162 AGIIAMDGNTLVLDEPTGGLDPKGEEDFINLfERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFSN 241
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
7-218 |
2.31e-29 |
|
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: 109.67 E-value: 2.31e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 7 VRKSFSSLEVLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGL---EPIDSGRIVIDGTDVHAKgtdlnRLRRKVGIVF 83
Cdd:cd03234 13 AKNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRvegGGTTSGQILFNGQPRKPD-----QFQKCVAYVR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 84 QQWNAFPHLTVLENVMLAPRKVLGLPKDKA---EEIAVKQLTHVGLGEKLKVYPNRMSGGQQQRMAIARALAMSPEYMLF 160
Cdd:cd03234 88 QDDILLPGLTVRETLTYTAILRLPRKSSDAirkKRVEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLIL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499282096 161 DEVTSALDPMLVGEVLDTLKMLAEEGMTMICVTHEMT---FarDVSDRVAFFHQGIMAEIG 218
Cdd:cd03234 168 DEPTSGLDSFTALNLVSTLSQLARRNRIVILTIHQPRsdlF--RLFDRILLLSSGEIVYSG 226
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
10-206 |
3.17e-29 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 108.48 E-value: 3.17e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 10 SFSSLEVLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGTdvhakgtdlnrlrRKVGIVFQQW--- 86
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGG-------------ARVAYVPQRSevp 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 87 NAFPhLTVLENVML---APRKVLGLPKDKAEEIAVKQLTHVGLGEKLKVYPNRMSGGQQQRMAIARALAMSPEYMLFDEV 163
Cdd:NF040873 68 DSLP-LTVRDLVAMgrwARRGLWRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEP 146
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 499282096 164 TSALDPMLVGEVLDTLKMLAEEGMTMICVTHEMTFARDVSDRV 206
Cdd:NF040873 147 TTGLDAESRERIIALLAEEHARGATVVVVTHDLELVRRADPCV 189
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1-229 |
3.35e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 110.57 E-value: 3.35e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 1 MIEIENVRKSF---SSLEVLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGTDVHAKgtDLNRLRR 77
Cdd:PRK13642 4 ILEVENLVFKYekeSDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAE--NVWNLRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 78 KVGIVFQQW-NAFPHLTVLENVMLAPRKvLGLPKDKAEEIAVKQLTHVGLGEKLKVYPNRMSGGQQQRMAIARALAMSPE 156
Cdd:PRK13642 82 KIGMVFQNPdNQFVGATVEDDVAFGMEN-QGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPE 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499282096 157 YMLFDEVTSALDPMLVGEVLDTLKMLAEE-GMTMICVTHEMTFARDvSDRVAFFHQGIMAEIGSPDQIFASPQN 229
Cdd:PRK13642 161 IIILDESTSMLDPTGRQEIMRVIHEIKEKyQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELFATSED 233
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
2-212 |
3.52e-29 |
|
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: 109.22 E-value: 3.52e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 2 IEIENVRKSF--SSLEVLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGTDVhaKGTDLNRLRRKV 79
Cdd:cd03245 3 IEFRNVSFSYpnQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDI--RQLDPADLRRNI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 80 GIVFQQwnafPHL---TVLENVMlaprkvLGLPKDKAEEIaVKQLTHVGLGEKLKVYPNRM-----------SGGQQQRM 145
Cdd:cd03245 81 GYVPQD----VTLfygTLRDNIT------LGAPLADDERI-LRAAELAGVTDFVNKHPNGLdlqigergrglSGGQRQAV 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499282096 146 AIARALAMSPEYMLFDEVTSALDPMLVGEVLDTLKMLAeEGMTMICVTHEMTFArDVSDRVAFFHQG 212
Cdd:cd03245 150 ALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLL-GDKTLIIITHRPSLL-DLVDRIIVMDSG 214
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
20-239 |
4.49e-29 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 111.37 E-value: 4.49e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 20 IDLTVEKGEVVTIIGGSGSGKSTLLTCINGLepID-SGRIVIDGTDVHakGTDLNRL----RRK-----VGIVFQQ--WN 87
Cdd:PRK11022 26 ISYSVKQGEVVGIVGESGSGKSVSSLAIMGL--IDyPGRVMAEKLEFN--GQDLQRIsekeRRNlvgaeVAMIFQDpmTS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 88 AFPHLTVLENVMLAPRKVLGLPKDKAEEIAVKQLTHVGL---GEKLKVYPNRMSGGQQQRMAIARALAMSPEYMLFDEVT 164
Cdd:PRK11022 102 LNPCYTVGFQIMEAIKVHQGGNKKTRRQRAIDLLNQVGIpdpASRLDVYPHQLSGGMSQRVMIAMAIACRPKLLIADEPT 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499282096 165 SALDPMLVGEVLDTLKMLAE-EGMTMICVTHEMTFARDVSDRVAFFHQGIMAEIGSPDQIFASPQNPETQKFLASV 239
Cdd:PRK11022 182 TALDVTIQAQIIELLLELQQkENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDIFRAPRHPYTQALLRAL 257
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
1-228 |
4.51e-29 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 111.89 E-value: 4.51e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 1 MIEIeNVRKSFSSLeVLKgIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGT---DVHaKGTDLNRLRR 77
Cdd:PRK11144 1 MLEL-NFKQQLGDL-CLT-VNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRvlfDAE-KGICLPPEKR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 78 KVGIVFQQWNAFPHLTVLENVMLAPRKvlglpKDKAEEIAVKQLthVGLGEKLKVYPNRMSGGQQQRMAIARALAMSPEY 157
Cdd:PRK11144 77 RIGYVFQDARLFPHYKVRGNLRYGMAK-----SMVAQFDKIVAL--LGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPEL 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499282096 158 MLFDEVTSALDPMLVGEVLDTLKMLAEE-GMTMICVTHEMTFARDVSDRVAFFHQGIMAEIGSPDQIFASPQ 228
Cdd:PRK11144 150 LLMDEPLASLDLPRKRELLPYLERLAREiNIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVWASSA 221
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
27-239 |
5.00e-29 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 114.57 E-value: 5.00e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 27 GEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGTDVHA-KGTDLNRLRRKVGIVFQQWNAF--PHLTVLENVMlAPR 103
Cdd:PRK10261 350 GETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTlSPGKLQALRRDIQFIFQDPYASldPRQTVGDSIM-EPL 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 104 KVLGL-PKDKAEEIAVKQLTHVGL-GEKLKVYPNRMSGGQQQRMAIARALAMSPEYMLFDEVTSALDPMLVGEVLDTLKM 181
Cdd:PRK10261 429 RVHGLlPGKAAAARVAWLLERVGLlPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLD 508
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 499282096 182 LAEE-GMTMICVTHEMTFARDVSDRVAFFHQGIMAEIGSPDQIFASPQNPETQKFLASV 239
Cdd:PRK10261 509 LQRDfGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENPQHPYTRKLMAAV 567
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
2-194 |
6.06e-29 |
|
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: 113.54 E-value: 6.06e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 2 IEIENVRKSFS-SLEVLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGTDVhaKGTDLNRLRRKVG 80
Cdd:TIGR02857 322 LEFSGVSVAYPgRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPL--ADADADSWRDQIA 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 81 IVFQQwnafPHL---TVLENVMLAprkvlgLPKDKAEEIAvKQLTHVGLGEKLKVYP-----------NRMSGGQQQRMA 146
Cdd:TIGR02857 400 WVPQH----PFLfagTIAENIRLA------RPDASDAEIR-EALERAGLDEFVAALPqgldtpigeggAGLSGGQAQRLA 468
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 499282096 147 IARALAMSPEYMLFDEVTSALDPMLVGEVLDTLKMLAeEGMTMICVTH 194
Cdd:TIGR02857 469 LARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALA-QGRTVLLVTH 515
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1-227 |
8.65e-29 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 108.92 E-value: 8.65e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 1 MIEIENVRKSFSSLEVLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGTdvHAKGTDLNRLRRKvG 80
Cdd:PRK11300 5 LLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQ--HIEGLPGHQIARM-G 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 81 IV--FQQWNAFPHLTVLENVMLAPRKVL------GLPK--------DKAEEIAVKQLTHVGLGEklkvYPNRMSG----G 140
Cdd:PRK11300 82 VVrtFQHVRLFREMTVIENLLVAQHQQLktglfsGLLKtpafrraeSEALDRAATWLERVGLLE----HANRQAGnlayG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 141 QQQRMAIARALAMSPEYMLFDEVTSALDPMLVGEVLDTLKMLAEE-GMTMICVTHEMTFARDVSDRVAFFHQGIMAEIGS 219
Cdd:PRK11300 158 QQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEhNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGT 237
|
....*...
gi 499282096 220 PDQIFASP 227
Cdd:PRK11300 238 PEEIRNNP 245
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1-223 |
8.93e-29 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 113.22 E-value: 8.93e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 1 MIEIENVRKSFSSLEVLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGTD-VHAKGTdlnrLRRKV 79
Cdd:PRK15439 11 LLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPcARLTPA----KAHQL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 80 GI--VFQQWNAFPHLTVLENVMlaprkvLGLPKDKAEEIAVKQL-THVGLGEKLKVYPNRMSGGQQQRMAIARALAMSPE 156
Cdd:PRK15439 87 GIylVPQEPLLFPNLSVKENIL------FGLPKRQASMQKMKQLlAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSR 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499282096 157 YMLFDEVTSALDPMLVGEVLDTLKMLAEEGMTMICVTHEMTFARDVSDRVAFFHQGIMAEIGSPDQI 223
Cdd:PRK15439 161 ILILDEPTASLTPAETERLFSRIRELLAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTADL 227
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-238 |
1.37e-28 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 112.88 E-value: 1.37e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 1 MIEIENVRKSFSS----LEVLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPID-----SGRIVIDGTDV-HAKGT 70
Cdd:PRK15134 5 LLAIENLSVAFRQqqtvRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPSPpvvypSGDIRFHGESLlHASEQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 71 DLNRLR-RKVGIVFQQwnAFPHLTVLENVMLAPRKVL----GLPKDKAEEIAVKQLTHVGL---GEKLKVYPNRMSGGQQ 142
Cdd:PRK15134 85 TLRGVRgNKIAMIFQE--PMVSLNPLHTLEKQLYEVLslhrGMRREAARGEILNCLDRVGIrqaAKRLTDYPHQLSGGER 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 143 QRMAIARALAMSPEYMLFDEVTSALDPMLVGEVLDTLKMLAEE-GMTMICVTHEMTFARDVSDRVAFFHQGIMAEIGSPD 221
Cdd:PRK15134 163 QRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQElNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAA 242
|
250
....*....|....*..
gi 499282096 222 QIFASPQNPETQKFLAS 238
Cdd:PRK15134 243 TLFSAPTHPYTQKLLNS 259
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
17-239 |
3.16e-28 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 112.26 E-value: 3.16e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 17 LKGIDLTVEKGEVVTIIGGSGSGKS-TLLTCINGLEPidsgriviDGTDVHAKGTDLNRLRRKV---------------- 79
Cdd:PRK10261 32 VRNLSFSLQRGETLAIVGESGSGKSvTALALMRLLEQ--------AGGLVQCDKMLLRRRSRQVielseqsaaqmrhvrg 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 80 ---GIVFQQ--WNAFPHLTVLENVMLAPRKVLGLPKDKAEEIAVKQLTHVGLGEK---LKVYPNRMSGGQQQRMAIARAL 151
Cdd:PRK10261 104 admAMIFQEpmTSLNPVFTVGEQIAESIRLHQGASREEAMVEAKRMLDQVRIPEAqtiLSRYPHQLSGGMRQRVMIAMAL 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 152 AMSPEYMLFDEVTSALDPMLVGEVLDTLKMLAEE-GMTMICVTHEMTFARDVSDRVAFFHQGIMAEIGSPDQIFASPQNP 230
Cdd:PRK10261 184 SCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEmSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQIFHAPQHP 263
|
....*....
gi 499282096 231 ETQKFLASV 239
Cdd:PRK10261 264 YTRALLAAV 272
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-205 |
4.31e-28 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 106.89 E-value: 4.31e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 1 MIEIENVRKSFSSLEVLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGTDVHAKGTDlNRLRRKVG 80
Cdd:PRK11614 5 MLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTA-KIMREAVA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 81 IVFQQWNAFPHLTVLENVMLAprkvlGLPKDKA---EEIAVKQLTHVGLGEKLKVYPNRMSGGQQQRMAIARALAMSPEY 157
Cdd:PRK11614 84 IVPEGRRVFSRMTVEENLAMG-----GFFAERDqfqERIKWVYELFPRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRL 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 499282096 158 MLFDEVTSALDPMLVGEVLDTLKMLAEEGMTMICVTHEMTFARDVSDR 205
Cdd:PRK11614 159 LLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADR 206
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
2-218 |
5.36e-28 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 106.08 E-value: 5.36e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 2 IEIENVRKSFSS----------------------LEVLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIV 59
Cdd:cd03220 1 IELENVSKSYPTykggssslkklgilgrkgevgeFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 60 IDGTDVHAKGtdlnrlrrkVGIVFQqwnafPHLTVLENVMLAPRkVLGLPKD--KAEEIAVKQLThvGLGE----KLKVY 133
Cdd:cd03220 81 VRGRVSSLLG---------LGGGFN-----PELTGRENIYLNGR-LLGLSRKeiDEKIDEIIEFS--ELGDfidlPVKTY 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 134 pnrmSGGQQQRMAIARALAMSPEYMLFDEVTSALDPMLVGEVLDTLKMLAEEGMTMICVTHEMTFARDVSDRVAFFHQGI 213
Cdd:cd03220 144 ----SSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGK 219
|
....*
gi 499282096 214 MAEIG 218
Cdd:cd03220 220 IRFDG 224
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-223 |
7.05e-28 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 108.38 E-value: 7.05e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 2 IEIENVRKSFSSLEVLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGTDVHAKGtdlnRL-RRKVG 80
Cdd:PRK13536 42 IDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARA----RLaRARIG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 81 IVFQQWNAFPHLTVLENVMLAPRkVLGLPKDKAEEIAVKQLTHVGLGEKLKVYPNRMSGGQQQRMAIARALAMSPEYMLF 160
Cdd:PRK13536 118 VVPQFDNLDLEFTVRENLLVFGR-YFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLIL 196
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499282096 161 DEVTSALDPMLVGEVLDTLKMLAEEGMTMICVTHEMTFARDVSDRVAFFHQGIMAEIGSPDQI 223
Cdd:PRK13536 197 DEPTTGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHAL 259
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
2-227 |
8.48e-28 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 110.97 E-value: 8.48e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 2 IEIENVrkSFS-----SLEVLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGTDVhaKGTDLNRLR 76
Cdd:TIGR00958 479 IEFQDV--SFSypnrpDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPL--VQYDHHYLH 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 77 RKVGIVFQQwnafPHL---TVLENVMLAPRKVlglPKDKAEEIAVKQLTHVGLGEKLKVYP-------NRMSGGQQQRMA 146
Cdd:TIGR00958 555 RQVALVGQE----PVLfsgSVRENIAYGLTDT---PDEEIMAAAKAANAHDFIMEFPNGYDtevgekgSQLSGGQKQRIA 627
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 147 IARALAMSPEYMLFDEVTSALDpmlvGEVLDTLKMLAE-EGMTMICVTHEMTFARDvSDRVAFFHQGIMAEIGSPDQIFA 225
Cdd:TIGR00958 628 IARALVRKPRVLILDEATSALD----AECEQLLQESRSrASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQLME 702
|
..
gi 499282096 226 SP 227
Cdd:TIGR00958 703 DQ 704
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
2-226 |
1.76e-27 |
|
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: 110.22 E-value: 1.76e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 2 IEIENVRKSFS--SLEVLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGTDVHAkgTDLNRLRRKV 79
Cdd:TIGR01846 456 ITFENIRFRYApdSPEVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAI--ADPAWLRRQM 533
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 80 GIVFQQwNAFPHLTVLENVMLA-PrkvlGLPKDK---------AEE--IAVKQLTHVGLGEKlkvyPNRMSGGQQQRMAI 147
Cdd:TIGR01846 534 GVVLQE-NVLFSRSIRDNIALCnP----GAPFEHvihaaklagAHDfiSELPQGYNTEVGEK----GANLSGGQRQRIAI 604
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499282096 148 ARALAMSPEYMLFDEVTSALDPMLVGEVLDTLKMLAeEGMTMICVTHEMTFARDvSDRVAFFHQGIMAEIGSPDQIFAS 226
Cdd:TIGR01846 605 ARALVGNPRILIFDEATSALDYESEALIMRNMREIC-RGRTVIIIAHRLSTVRA-CDRIIVLEKGQIAESGRHEELLAL 681
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-227 |
2.92e-27 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 107.62 E-value: 2.92e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 1 MIEIENVRKSFSSLEVLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGTDVHAkgTDLNRLRRKVG 80
Cdd:PRK09536 3 MIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEA--LSARAASRRVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 81 IVFQQWN-AF-------------PHLTVLEnvmlaprkvlglPKDKAEEIAVKQ-LTHVGLGEKLKVYPNRMSGGQQQRM 145
Cdd:PRK09536 81 SVPQDTSlSFefdvrqvvemgrtPHRSRFD------------TWTETDRAAVERaMERTGVAQFADRPVTSLSGGERQRV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 146 AIARALAMSPEYMLFDEVTSALDPMLVGEVLDTLKMLAEEGMTMICVTHEMTFARDVSDRVAFFHQGIMAEIGSPDQIFA 225
Cdd:PRK09536 149 LLARALAQATPVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVLT 228
|
..
gi 499282096 226 SP 227
Cdd:PRK09536 229 AD 230
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
16-212 |
4.60e-27 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 102.51 E-value: 4.60e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 16 VLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGTDVHAKGTdlnRLRRKVGIVF-----QQWNAFP 90
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSP---RDAIRAGIAYvpedrKREGLVL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 91 HLTVLENVMLaprkvlglpkdkaeeiavkqlthvglgeklkvyPNRMSGGQQQRMAIARALAMSPEYMLFDEVTSALDpm 170
Cdd:cd03215 92 DLSVAENIAL---------------------------------SSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVD-- 136
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 499282096 171 lVG---EVLDTLKMLAEEGMTMICVTHEMTFARDVSDRVAFFHQG 212
Cdd:cd03215 137 -VGakaEIYRLIRELADAGKAVLLISSELDELLGLCDRILVMYEG 180
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-239 |
5.48e-27 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 104.24 E-value: 5.48e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 1 MIEIENVRKSFSSLEVLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGTDvhAKGTDLNRL----R 76
Cdd:PRK11701 6 LLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRD--GQLRDLYALseaeR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 77 RKV-----GIVFQqwNAFPHL--------TVLENVMLAPRKVLGlpkdKAEEIAVKQLTHVGLG-EKLKVYPNRMSGGQQ 142
Cdd:PRK11701 84 RRLlrtewGFVHQ--HPRDGLrmqvsaggNIGERLMAVGARHYG----DIRATAGDWLERVEIDaARIDDLPTTFSGGMQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 143 QRMAIARALAMSPEYMLFDEVTSALDPMLVGEVLDTLKML-AEEGMTMICVTHEMTFARDVSDRVAFFHQGIMAEIGSPD 221
Cdd:PRK11701 158 QRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLvRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVVESGLTD 237
|
250
....*....|....*...
gi 499282096 222 QIFASPQNPETQKFLASV 239
Cdd:PRK11701 238 QVLDDPQHPYTQLLVSSV 255
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-226 |
3.31e-26 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 103.35 E-value: 3.31e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 2 IEIENVRKSFSSLEVLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGTDVHAKGtdlNRLRRKVGI 81
Cdd:PRK13537 8 IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRA---RHARQRVGV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 82 VFQQWNAFPHLTVLENVMLAPRkVLGLPKDKAEEIAVKQLTHVGLGEKLKVYPNRMSGGQQQRMAIARALAMSPEYMLFD 161
Cdd:PRK13537 85 VPQFDNLDPDFTVRENLLVFGR-YFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLD 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499282096 162 EVTSALDPMLVGEVLDTLKMLAEEGMTMICVTHEMTFARDVSDRVAFFHQGIMAEIGSPDQIFAS 226
Cdd:PRK13537 164 EPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIES 228
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
16-233 |
9.69e-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: 104.83 E-value: 9.69e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 16 VLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGTDVHAkgTDLNRLRRKVGIVFQQWNAFPHlTVL 95
Cdd:COG4618 347 ILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQ--WDREELGRHIGYLPQDVELFDG-TIA 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 96 EN-----------VMLAPRK------VLGLPK--DkaeeiavkqlTHVGLGeklkvyPNRMSGGQQQRMAIARALAMSPE 156
Cdd:COG4618 424 ENiarfgdadpekVVAAAKLagvhemILRLPDgyD----------TRIGEG------GARLSGGQRQRIGLARALYGDPR 487
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499282096 157 YMLFDEVTSALDPmlVGE--VLDTLKMLAEEGMTMICVTHEMTFARDVsDRVAFFHQGIMAEIGSPDQIFASPQNPETQ 233
Cdd:COG4618 488 LVVLDEPNSNLDD--EGEaaLAAAIRALKARGATVVVITHRPSLLAAV-DKLLVLRDGRVQAFGPRDEVLARLARPAAA 563
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
15-222 |
9.74e-26 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 104.74 E-value: 9.74e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 15 EVLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPID---SGRIVIDGTDVHAKgtdlnRLRRKVGIVFQQWNAFPH 91
Cdd:TIGR00955 39 HLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGMPIDAK-----EMRAISAYVQQDDLFIPT 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 92 LTVLENVMLAPRKVLG--LPKDKAEEIaVKQ-LTHVGLGE--KLKV-YPNRM---SGGQQQRMAIARALAMSPEYMLFDE 162
Cdd:TIGR00955 114 LTVREHLMFQAHLRMPrrVTKKEKRER-VDEvLQALGLRKcaNTRIgVPGRVkglSGGERKRLAFASELLTDPPLLFCDE 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499282096 163 VTSALDPMLVGEVLDTLKMLAEEGMTMICVTHEMT---FarDVSDRVAFFHQGIMAEIGSPDQ 222
Cdd:TIGR00955 193 PTSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQPSselF--ELFDKIILMAEGRVAYLGSPDQ 253
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
15-225 |
1.08e-25 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 104.82 E-value: 1.08e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 15 EVLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGTDVhaKGTDLNRLRRKVGIVFQQWNAFPHlTV 94
Cdd:TIGR01193 488 NILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSL--KDIDRHTLRQFINYLPQEPYIFSG-SI 564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 95 LENVMLAPRKVLGLPK-DKAEEIA-----VKQLThVGLGEKLKVYPNRMSGGQQQRMAIARALAMSPEYMLFDEVTSALD 168
Cdd:TIGR01193 565 LENLLLGAKENVSQDEiWAACEIAeikddIENMP-LGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLD 643
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 499282096 169 PMLVGEVLDTLKMLAEEgmTMICVTHEMTFARDvSDRVAFFHQGIMAEIGSPDQIFA 225
Cdd:TIGR01193 644 TITEKKIVNNLLNLQDK--TIIFVAHRLSVAKQ-SDKIIVLDHGKIIEQGSHDELLD 697
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1-238 |
3.41e-25 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 99.86 E-value: 3.41e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 1 MIEIENVRKSF---------SSLEVLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGTDVHAKgtD 71
Cdd:PRK15112 4 LLEVRNLSKTFryrtgwfrrQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFG--D 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 72 LNRLRRKVGIVFQQwnafphltvlENVMLAPRKVLG------------LPKDKAEEIAVKQLTHVGL-GEKLKVYPNRMS 138
Cdd:PRK15112 82 YSYRSQRIRMIFQD----------PSTSLNPRQRISqildfplrlntdLEPEQREKQIIETLRQVGLlPDHASYYPHMLA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 139 GGQQQRMAIARALAMSPEYMLFDEVTSALDPMLVGEVLDTLKMLAEE-GMTMICVTHEMTFARDVSDRVAFFHQGIMAEI 217
Cdd:PRK15112 152 PGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKqGISYIYVTQHLGMMKHISDQVLVMHQGEVVER 231
|
250 260
....*....|....*....|.
gi 499282096 218 GSPDQIFASPQNPETQKFLAS 238
Cdd:PRK15112 232 GSTADVLASPLHELTKRLIAG 252
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
2-220 |
3.73e-25 |
|
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: 98.33 E-value: 3.73e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 2 IEIENVRKSFSSLE--VLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGTDVhaKGTDLNRLRRKV 79
Cdd:cd03244 3 IEFKNVSLRYRPNLppVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDI--SKIGLHDLRSRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 80 GIVFQQwnafPHL---TVLENvmLAPrkvLGLPKDkaEEIaVKQLTHVGLGEKLKVYPNRM-----------SGGQQQRM 145
Cdd:cd03244 81 SIIPQD----PVLfsgTIRSN--LDP---FGEYSD--EEL-WQALERVGLKEFVESLPGGLdtvveeggenlSVGQRQLL 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499282096 146 AIARALAMSPEYMLFDEVTSALDP---MLVGEVLDTlkmlAEEGMTMICVTHEMTFARDvSDRVAFFHQGIMAEIGSP 220
Cdd:cd03244 149 CLARALLRKSKILVLDEATASVDPetdALIQKTIRE----AFKDCTVLTIAHRLDTIID-SDRILVLDKGRVVEFDSP 221
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
2-221 |
4.81e-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: 97.60 E-value: 4.81e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 2 IEIENVRKSFSSLEVLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLE--PIDSGRIVIDGTDVhakgTDLN---RLR 76
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKGEDI----TDLPpeeRAR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 77 RKVGIVFQQWNAFPHLTVLENVmlapRKVlglpkdkaeeiavkqltHVGLgeklkvypnrmSGGQQQRMAIARALAMSPE 156
Cdd:cd03217 77 LGIFLAFQYPPEIPGVKNADFL----RYV-----------------NEGF-----------SGGEKKRNEILQLLLLEPD 124
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499282096 157 YMLFDEVTSALDPMLVGEVLDTLKMLAEEGMTMICVTH-EMTFARDVSDRVAFFHQGIMAEIGSPD 221
Cdd:cd03217 125 LAILDEPDSGLDIDALRLVAEVINKLREEGKSVLIITHyQRLLDYIKPDRVHVLYDGRIVKSGDKE 190
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
2-226 |
7.59e-25 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 102.35 E-value: 7.59e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 2 IEIENVRKSF-SSLEVLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGTDVhakgTDLNR--LRRK 78
Cdd:PRK13657 335 VEFDDVSFSYdNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDI----RTVTRasLRRN 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 79 VGIVFQQWNAFPHlTVLENVMLaprkvlGLPKDKAEE-------------IAVKQL---THVGlgEKlkvyPNRMSGGQQ 142
Cdd:PRK13657 411 IAVVFQDAGLFNR-SIEDNIRV------GRPDATDEEmraaaeraqahdfIERKPDgydTVVG--ER----GRQLSGGER 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 143 QRMAIARALAMSPEYMLFDEVTSALDPML---VGEVLDTLKmlaeEGMTMICVTHEMTFARDvSDRVAFFHQGIMAEIGS 219
Cdd:PRK13657 478 QRLAIARALLKDPPILILDEATSALDVETeakVKAALDELM----KGRTTFIIAHRLSTVRN-ADRILVFDNGRVVESGS 552
|
....*..
gi 499282096 220 PDQIFAS 226
Cdd:PRK13657 553 FDELVAR 559
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
3-217 |
7.84e-25 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 102.02 E-value: 7.84e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 3 EIENVrksfSSLEVLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGTDVHAKGT------------ 70
Cdd:COG1129 258 EVEGL----SVGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPrdairagiayvp 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 71 -DlnrlRRKVGIvfqqwnaFPHLTVLENVMLAPRKVL---GLPKDKAEEIAVKQLThvglgEKLKVYPNRM-------SG 139
Cdd:COG1129 334 eD----RKGEGL-------VLDLSIRENITLASLDRLsrgGLLDRRRERALAEEYI-----KRLRIKTPSPeqpvgnlSG 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 140 GQQQRMAIARALAMSPEYMLFDEVTSALDpmlVG---EVLDTLKMLAEEGMTMICVTHEMTFARDVSDRVAFFHQG-IMA 215
Cdd:COG1129 398 GNQQKVVLAKWLATDPKVLILDEPTRGID---VGakaEIYRLIRELAAEGKAVIVISSELPELLGLSDRILVMREGrIVG 474
|
..
gi 499282096 216 EI 217
Cdd:COG1129 475 EL 476
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
2-225 |
1.07e-24 |
|
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: 101.72 E-value: 1.07e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 2 IEIENVRKSF--SSLEVLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGTDVhaKGTDLNRLRRKV 79
Cdd:TIGR02203 331 VEFRNVTFRYpgRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDL--ADYTLASLRRQV 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 80 GIVFQQWNAFPHlTVLENVMLAPRKvlGLPKDKAEEIA--------VKQLTHvGLGEKLKVYPNRMSGGQQQRMAIARAL 151
Cdd:TIGR02203 409 ALVSQDVVLFND-TIANNIAYGRTE--QADRAEIERALaaayaqdfVDKLPL-GLDTPIGENGVLLSGGQRQRLAIARAL 484
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499282096 152 AMSPEYMLFDEVTSALD---PMLVGEVLDTLKmlaeEGMTMICVTHEMTFARDvSDRVAFFHQGIMAEIGSPDQIFA 225
Cdd:TIGR02203 485 LKDAPILILDEATSALDnesERLVQAALERLM----QGRTTLVIAHRLSTIEK-ADRIVVMDDGRIVERGTHNELLA 556
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-212 |
1.12e-24 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 101.40 E-value: 1.12e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 1 MIEIENVRKSFSSLEVLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIdgtdvhaKGTDLNRLRRK-- 78
Cdd:PRK09700 5 YISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITI-------NNINYNKLDHKla 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 79 ----VGIVFQQWNAFPHLTVLENVM---LAPRKVLGLPK---DKAEEIAVKQLTHVGLGEKLKVYPNRMSGGQQQRMAIA 148
Cdd:PRK09700 78 aqlgIGIIYQELSVIDELTVLENLYigrHLTKKVCGVNIidwREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499282096 149 RALAMSPEYMLFDEVTSALDPMLVGEVLDTLKMLAEEGMTMICVTHEMTFARDVSDRVAFFHQG 212
Cdd:PRK09700 158 KTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDG 221
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1-216 |
1.48e-24 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 101.29 E-value: 1.48e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 1 MIEIENVRKSFSSLEVLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIdGTDVhakgtdlnrlrrKVG 80
Cdd:COG0488 315 VLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETV------------KIG 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 81 IVFQQWNAF-PHLTVLENVMLAprkvlglpKDKAEEIAVKQLthvgL------GEKLKVYPNRMSGGQQQRMAIARALAM 153
Cdd:COG0488 382 YFDQHQEELdPDKTVLDELRDG--------APGGTEQEVRGY----LgrflfsGDDAFKPVGVLSGGEKARLALAKLLLS 449
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499282096 154 SPEYMLFDEVTSALDpmlvgevLDTLKMLAE-----EGmTMICVTHEMTFARDVSDRVAFFHQGIMAE 216
Cdd:COG0488 450 PPNVLLLDEPTNHLD-------IETLEALEEalddfPG-TVLLVSHDRYFLDRVATRILEFEDGGVRE 509
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
2-216 |
5.67e-24 |
|
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: 94.30 E-value: 5.67e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 2 IEIENVrkSFSSLE----VLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCING-LEPiDSGRIVIDGTDVHAKGtdlNRLR 76
Cdd:cd03247 1 LSINNV--SFSYPEqeqqVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGdLKP-QQGEITLDGVPVSDLE---KALS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 77 RKVGIVFQQwnafPHL---TVLENvmlaprkvlglpkdkaeeiavkqlthvgLGEklkvypnRMSGGQQQRMAIARALAM 153
Cdd:cd03247 75 SLISVLNQR----PYLfdtTLRNN----------------------------LGR-------RFSGGERQRLALARILLQ 115
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499282096 154 SPEYMLFDEVTSALDPMLVGEVLDTLkMLAEEGMTMICVTHEMTFARDVsDRVAFFHQG-IMAE 216
Cdd:cd03247 116 DAPIVLLDEPTVGLDPITERQLLSLI-FEVLKDKTLIWITHHLTGIEHM-DKILFLENGkIIMQ 177
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
16-211 |
9.09e-24 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 99.11 E-value: 9.09e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 16 VLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVI-DGTDVhakgtdlnrlrrkvgiVF--QQwnafPHL 92
Cdd:COG4178 378 LLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARpAGARV----------------LFlpQR----PYL 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 93 TV--LENVMLAPRKVLGLPKDKAEEIavkqLTHVGLG---EKLKV---YPNRMSGGQQQRMAIARALAMSPEYMLFDEVT 164
Cdd:COG4178 438 PLgtLREALLYPATAEAFSDAELREA----LEAVGLGhlaERLDEeadWDQVLSLGEQQRLAFARLLLHKPDWLFLDEAT 513
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 499282096 165 SALDPMLVGEVldtLKMLAEE--GMTMICVTHEMTFARdvsdrvafFHQ 211
Cdd:COG4178 514 SALDEENEAAL---YQLLREElpGTTVISVGHRSTLAA--------FHD 551
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
15-225 |
1.07e-23 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 95.84 E-value: 1.07e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 15 EVLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGTDVHAKGTDLNRLRRKVGIVFQQWNAFPHLTV 94
Cdd:PRK13638 15 PVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKRGLLALRQQVATVFQDPEQQIFYTD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 95 LENVMLAPRKVLGLPKDKAEEIAVKQLTHVGlGEKLKVYPNR-MSGGQQQRMAIARALAMSPEYMLFDEVTSALDPMLVG 173
Cdd:PRK13638 95 IDSDIAFSLRNLGVPEAEITRRVDEALTLVD-AQHFRHQPIQcLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRT 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 499282096 174 EVLDTLKMLAEEGMTMICVTHEMTFARDVSDRVAFFHQGIMAEIGSPDQIFA 225
Cdd:PRK13638 174 QMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVFA 225
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
2-212 |
1.26e-23 |
|
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: 94.71 E-value: 1.26e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 2 IEIENVRKSFS---------------------SLEVLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVI 60
Cdd:cd03267 1 IEVSNLSKSYRvyskepgligslkslfkrkyrEVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 61 DGTDvhaKGTDLNRLRRKVGIVFQQ-----WNafphLTVLENVMLApRKVLGLPKDKAEEiAVKQLTH-VGLGEKLKVYP 134
Cdd:cd03267 81 AGLV---PWKRRKKFLRRIGVVFGQktqlwWD----LPVIDSFYLL-AAIYDLPPARFKK-RLDELSElLDLEELLDTPV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 135 NRMSGGQQQRMAIARALAMSPEYMLFDEVTSALDPMLVGEVLDTLKML-AEEGMTMICVTHEMtfaRDV---SDRVAFFH 210
Cdd:cd03267 152 RQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYnRERGTTVLLTSHYM---KDIealARRVLVID 228
|
..
gi 499282096 211 QG 212
Cdd:cd03267 229 KG 230
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
2-194 |
1.33e-23 |
|
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: 98.74 E-value: 1.33e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 2 IEIENVrkSFS---SLEVLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGTDVhakgTDLNR--LR 76
Cdd:COG5265 358 VRFENV--SFGydpERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDI----RDVTQasLR 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 77 RKVGIVfqqwnafPHLTVLENVMLAPRKVLGLPK-DKAEEIAVKQLTHVG-------------LGEK-LKVypnrmSGGQ 141
Cdd:COG5265 432 AAIGIV-------PQDTVLFNDTIAYNIAYGRPDaSEEEVEAAARAAQIHdfieslpdgydtrVGERgLKL-----SGGE 499
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 499282096 142 QQRMAIARALAMSPEYMLFDEVTSALDPMLVGEVLDTLKMLAeEGMTMICVTH 194
Cdd:COG5265 500 KQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVA-RGRTTLVIAH 551
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1-239 |
4.33e-23 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 95.18 E-value: 4.33e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 1 MIEIENVRKSFSS----LEVLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGL---EPIDSGRIVIDGTDV-HAKGTDL 72
Cdd:PRK09473 12 LLDVKDLRVTFSTpdgdVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLlaaNGRIGGSATFNGREIlNLPEKEL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 73 NRLR-RKVGIVFQ----QWNafPHLTVLENVMlaprKVLGLPK--DKAE--EIAVKQLTHVGLGE---KLKVYPNRMSGG 140
Cdd:PRK09473 92 NKLRaEQISMIFQdpmtSLN--PYMRVGEQLM----EVLMLHKgmSKAEafEESVRMLDAVKMPEarkRMKMYPHEFSGG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 141 QQQRMAIARALAMSPEYMLFDEVTSALDPMLVGEVLDTLKMLAEE-GMTMICVTHEMTFARDVSDRVAFFHQGIMAEIGS 219
Cdd:PRK09473 166 MRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGN 245
|
250 260
....*....|....*....|
gi 499282096 220 PDQIFASPQNPETQKFLASV 239
Cdd:PRK09473 246 ARDVFYQPSHPYSIGLLNAV 265
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-206 |
6.08e-23 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 96.54 E-value: 6.08e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 1 MIEIENVRKSFSSLEVLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDS--GRIVIDGTDVHAKG---TDlnrl 75
Cdd:PRK13549 5 LLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGTyeGEIIFEGEELQASNirdTE---- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 76 RRKVGIVFQQWNAFPHLTVLENVMLA----PRKVLGLPKDKAEeiAVKQLTHVGLG--EKLKVYpnRMSGGQQQRMAIAR 149
Cdd:PRK13549 81 RAGIAIIHQELALVKELSVLENIFLGneitPGGIMDYDAMYLR--AQKLLAQLKLDinPATPVG--NLGLGQQQLVEIAK 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 499282096 150 ALAMSPEYMLFDEVTSALDPMLVGEVLDTLKMLAEEGMTMICVTHEMTFARDVSDRV 206
Cdd:PRK13549 157 ALNKQARLLILDEPTASLTESETAVLLDIIRDLKAHGIACIYISHKLNEVKAISDTI 213
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-212 |
1.75e-22 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 95.13 E-value: 1.75e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 4 IENVRKSFSSLEVLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIdgtdvhAKGTdlnrlrrKVGIVF 83
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSI------PKGL-------RIGYLP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 84 QQWNAFPHLTVLENVMLAPRKVLGLPKDKAE-------------EIAVKQ------------------LTHVGLGEKL-- 130
Cdd:COG0488 68 QEPPLDDDLTVLDTVLDGDAELRALEAELEEleaklaepdedleRLAELQeefealggweaearaeeiLSGLGFPEEDld 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 131 -KVypNRMSGGQQQRMAIARALAMSPEYMLFDEVTSALDpmlvgevLDTL----KMLAEEGMTMICVTHEMTFARDVSDR 205
Cdd:COG0488 148 rPV--SELSGGWRRRVALARALLSEPDLLLLDEPTNHLD-------LESIewleEFLKNYPGTVLVVSHDRYFLDRVATR 218
|
....*..
gi 499282096 206 VAFFHQG 212
Cdd:COG0488 219 ILELDRG 225
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
20-220 |
2.80e-22 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 95.47 E-value: 2.80e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 20 IDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGTDVHakgTDLNRLRRKVGIVFQQWNAFPHLTVLENVM 99
Cdd:TIGR01257 949 LNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIE---TNLDAVRQSLGMCPQHNILFHHLTVAEHIL 1025
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 100 LAPrKVLGLPKDKAEEIAVKQLTHVGLGEKLKVYPNRMSGGQQQRMAIARALAMSPEYMLFDEVTSALDPMLVGEVLDTL 179
Cdd:TIGR01257 1026 FYA-QLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLL 1104
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 499282096 180 kMLAEEGMTMICVTHEMTFARDVSDRVAFFHQGIMAEIGSP 220
Cdd:TIGR01257 1105 -LKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTP 1144
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-225 |
8.37e-22 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 93.35 E-value: 8.37e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 2 IEIENVrkSFS----SLEVLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGTDVHAKGTDlnRLRR 77
Cdd:PRK11160 339 LTLNNV--SFTypdqPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEA--ALRQ 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 78 KVGIVFQQWNAFPHlTVLENVMLAprkvlglpKDKA-EEIAVKQLTHVGLgEKLKVYPNRM-----------SGGQQQRM 145
Cdd:PRK11160 415 AISVVSQRVHLFSA-TLRDNLLLA--------APNAsDEALIEVLQQVGL-EKLLEDDKGLnawlgeggrqlSGGEQRRL 484
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 146 AIARALAMSPEYMLFDEVTSALDPMLVGEVLDTLKMLAeEGMTMICVTHEMTfARDVSDRVAFFHQGIMAEIGSPDQIFA 225
Cdd:PRK11160 485 GIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHA-QNKTVLMITHRLT-GLEQFDRICVMDNGQIIEQGTHQELLA 562
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
3-212 |
1.14e-21 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 93.05 E-value: 1.14e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 3 EIENVRKSFSSLEVLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGTDVHAKGTdLNRLRRKVGIV 82
Cdd:PRK11288 6 SFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFAST-TAALAAGVAII 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 83 FQQWNAFPHLTVLENVMLA--PRKVLGLPKDKAEEIAVKQLTHVGL----GEKLKvypnRMSGGQQQRMAIARALAMSPE 156
Cdd:PRK11288 85 YQELHLVPEMTVAENLYLGqlPHKGGIVNRRLLNYEAREQLEHLGVdidpDTPLK----YLSIGQRQMVEIAKALARNAR 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 499282096 157 YMLFDEVTSALDPMLVGEVLDTLKMLAEEGMTMICVTHEMTFARDVSDRVAFFHQG 212
Cdd:PRK11288 161 VIAFDEPTSSLSAREIEQLFRVIRELRAEGRVILYVSHRMEEIFALCDAITVFKDG 216
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-212 |
2.15e-21 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 90.53 E-value: 2.15e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 1 MIEIENVRKSF-------------SSL--------EVLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCING-LEPiDSGRI 58
Cdd:COG4586 1 IIEVENLSKTYrvyekepglkgalKGLfrreyrevEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGiLVP-TSGEV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 59 VIDGTDVHAkgtDLNRLRRKVGIVFQQ-----WnafpHLTVLENVMLApRKVLGLPKDKAEEiAVKQLTHV-GLGEKLKV 132
Cdd:COG4586 80 RVLGYVPFK---RRKEFARRIGVVFGQrsqlwW----DLPAIDSFRLL-KAIYRIPDAEYKK-RLDELVELlDLGELLDT 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 133 yPNR-MSGGQQQRMAIARALAMSPEYMLFDEVTSALDPMLVGEVLDTLKML-AEEGMTMICVTHEMtfaRDV---SDRVA 207
Cdd:COG4586 151 -PVRqLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYnRERGTTILLTSHDM---DDIealCDRVI 226
|
....*
gi 499282096 208 FFHQG 212
Cdd:COG4586 227 VIDHG 231
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1-212 |
4.01e-21 |
|
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: 91.42 E-value: 4.01e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 1 MIEIENVRKSFSSLEVLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDS--GRIVIDGTDVHAKGTDlNRLRRK 78
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTwdGEIYWSGSPLKASNIR-DTERAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 79 VGIVFQQWNAFPHLTVLENVMLAPRkvLGLPKDKAEEIAVKQLTHVGLGE-KLKVYPN-----RMSGGQQQRMAIARALA 152
Cdd:TIGR02633 80 IVIIHQELTLVPELSVAENIFLGNE--ITLPGGRMAYNAMYLRAKNLLRElQLDADNVtrpvgDYGGGQQQLVEIAKALN 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 153 MSPEYMLFDEVTSALDPMLVGEVLDTLKMLAEEGMTMICVTHEMTFARDVSDRVAFFHQG 212
Cdd:TIGR02633 158 KQARLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDG 217
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
2-217 |
4.19e-21 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 91.57 E-value: 4.19e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 2 IEIENVR-----KSFSslevLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGTDVHAKgtDLNRLR 76
Cdd:PRK10522 323 LELRNVTfayqdNGFS----VGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAE--QPEDYR 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 77 RKVGIVFQQWNAFPHLtvlenvmLAPRKvlglpKDKAEEIAVKQLTHVGLGEKLKVYPNR-----MSGGQQQRMAIARAL 151
Cdd:PRK10522 397 KLFSAVFTDFHLFDQL-------LGPEG-----KPANPALVEKWLERLKMAHKLELEDGRisnlkLSKGQKKRLALLLAL 464
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499282096 152 AMSPEYMLFDEVTSALDPMLVGEV-LDTLKMLAEEGMTMICVTHEMTFArDVSDRVAFFHQGIMAEI 217
Cdd:PRK10522 465 AEERDILLLDEWAADQDPHFRREFyQVLLPLLQEMGKTIFAISHDDHYF-IHADRLLEMRNGQLSEL 530
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
2-220 |
4.29e-21 |
|
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: 87.47 E-value: 4.29e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 2 IEIEN--VRKSFSSLEVLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGTDVhaKGTDLNRLRRKV 79
Cdd:cd03369 7 IEVENlsVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDI--STIPLEDLRSSL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 80 GIVFQQwnafPHL---TVLENVmlaprkvlglpkDKAEEIAVKQLThvglgEKLKVYP--NRMSGGQQQRMAIARALAMS 154
Cdd:cd03369 85 TIIPQD----PTLfsgTIRSNL------------DPFDEYSDEEIY-----GALRVSEggLNLSQGQRQLLCLARALLKR 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499282096 155 PEYMLFDEVTSALDPMLVGEVLDTLKmlaEE--GMTMICVTHEMTFARDVsDRVAFFHQGIMAEIGSP 220
Cdd:cd03369 144 PRVLVLDEATASIDYATDALIQKTIR---EEftNSTILTIAHRLRTIIDY-DKILVMDAGEVKEYDHP 207
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1-239 |
4.94e-21 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 88.53 E-value: 4.94e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 1 MIEIENVRKSFSSLEVLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGTDVHAKGTdlNRLRRKVG 80
Cdd:PRK11231 2 TLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSS--RQLARRLA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 81 IVFQQWNAFPHLTVLENVMLAPRKVLGL-----PKDKAE-EIAVKQLTHVGLGEKLKvypNRMSGGQQQRMAIARALAMS 154
Cdd:PRK11231 80 LLPQHHLTPEGITVRELVAYGRSPWLSLwgrlsAEDNARvNQAMEQTRINHLADRRL---TDLSGGQRQRAFLAMVLAQD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 155 PEYMLFDEVTSALDPMLVGEVLDTLKMLAEEGMTMICVTHEMTFARDVSDRVAFFHQGIMAEIGSPDQIFaspqnpeTQK 234
Cdd:PRK11231 157 TPVVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVM-------TPG 229
|
....*
gi 499282096 235 FLASV 239
Cdd:PRK11231 230 LLRTV 234
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
2-212 |
9.66e-21 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 86.37 E-value: 9.66e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 2 IEIENV-----RKSFSSLEVLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGTdvhakgtdlnrlr 76
Cdd:cd03250 1 ISVEDAsftwdSGEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 77 rkVGIVFQQ-W--NAfphlTVLENVmlaprkVLGLPKDKAEEIAVkqLTHVGLGEKLKVYPNR-----------MSGGQQ 142
Cdd:cd03250 68 --IAYVSQEpWiqNG----TIRENI------LFGKPFDEERYEKV--IKACALEPDLEILPDGdlteigekginLSGGQK 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499282096 143 QRMAIARALAMSPEYMLFDEVTSALDP----MLVGEVLdtLKMLAeEGMTMICVTHEMTFARDVsDRVAFFHQG 212
Cdd:cd03250 134 QRISLARAVYSDADIYLLDDPLSAVDAhvgrHIFENCI--LGLLL-NNKTRILVTHQLQLLPHA-DQIVVLDNG 203
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
2-168 |
1.70e-20 |
|
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: 86.37 E-value: 1.70e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 2 IEIENVRKSF---SSLEVLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGTDVHAkgTDLNRLRRK 78
Cdd:cd03248 12 VKFQNVTFAYptrPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQ--YEHKYLHSK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 79 VGIVFQQWNAFPHlTVLENVMLAprkVLGLPKDKAEEIAVKQLTH-----------VGLGEKlkvyPNRMSGGQQQRMAI 147
Cdd:cd03248 90 VSLVGQEPVLFAR-SLQDNIAYG---LQSCSFECVKEAAQKAHAHsfiselasgydTEVGEK----GSQLSGGQKQRVAI 161
|
170 180
....*....|....*....|.
gi 499282096 148 ARALAMSPEYMLFDEVTSALD 168
Cdd:cd03248 162 ARALIRNPQVLILDEATSALD 182
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
2-194 |
3.49e-20 |
|
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: 84.13 E-value: 3.49e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 2 IEIENVrkSFSSLE---VLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIvidgtdvhakgtdlnrlrrk 78
Cdd:cd03223 1 IELENL--SLATPDgrvLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI-------------------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 79 vgivfqqwnafpHLTVLENVMLAPRK---VLGLPKDkaeeiavkQLthvglgeklkVYP--NRMSGGQQQRMAIARALAM 153
Cdd:cd03223 59 ------------GMPEGEDLLFLPQRpylPLGTLRE--------QL----------IYPwdDVLSGGEQQRLAFARLLLH 108
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 499282096 154 SPEYMLFDEVTSALDPmlvgEVLDTL-KMLAEEGMTMICVTH 194
Cdd:cd03223 109 KPKFVFLDEATSALDE----ESEDRLyQLLKELGITVISVGH 146
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
2-212 |
4.07e-20 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 83.27 E-value: 4.07e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 2 IEIENVRKSFSSLEVLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGTDVHAkgtdlnrlrrkvgi 81
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVKIG-------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 82 VFQQwnafphltvlenvmlaprkvlglpkdkaeeiavkqlthvglgeklkvypnrMSGGQQQRMAIARALAMSPEYMLFD 161
Cdd:cd03221 67 YFEQ---------------------------------------------------LSGGEKMRLALAKLLLENPNLLLLD 95
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 499282096 162 EVTSALDpmlvgevLDTLKMLAE-----EGmTMICVTHEMTFARDVSDRVAFFHQG 212
Cdd:cd03221 96 EPTNHLD-------LESIEALEEalkeyPG-TVILVSHDRYFLDQVATKIIELEDG 143
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
17-229 |
5.07e-20 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 85.66 E-value: 5.07e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 17 LKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPiDSGRIVIDGTDV-HAKGTDLNRLRrkvGIVFQQWNAFPHLTVL 95
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLLP-GQGEILLNGRPLsDWSAAELARHR---AYLSQQQSPPFAMPVF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 96 EnvMLAprkvLGLPK---DKAEEIAVKQLTH-VGLGEKLKVYPNRMSGGQQQRMAIARAL-----AMSPE--YMLFDEVT 164
Cdd:COG4138 88 Q--YLA----LHQPAgasSEAVEQLLAQLAEaLGLEDKLSRPLTQLSGGEWQRVRLAAVLlqvwpTINPEgqLLLLDEPM 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499282096 165 SALDpmlVGE--VLDTL-KMLAEEGMTMICVTHEMTFARDVSDRVAFFHQGIMAEIGSPDQIFaSPQN 229
Cdd:COG4138 162 NSLD---VAQqaALDRLlRELCQQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEVM-TPEN 225
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
16-213 |
9.32e-20 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 84.24 E-value: 9.32e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 16 VLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEP--IDSGRIVIDgtdvhakgtdlnrlrrkvgivfqqWNAFPH-L 92
Cdd:COG2401 45 VLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKgtPVAGCVDVP------------------------DNQFGReA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 93 TVLENVmlaprkvlGLPKDKAEeiAVKQLTHVGLGEK--LKVYPNRMSGGQQQRMAIARALAMSPEYMLFDEVTSALDPM 170
Cdd:COG2401 101 SLIDAI--------GRKGDFKD--AVELLNAVGLSDAvlWLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQ 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 499282096 171 LVGEVLDTLKMLAEE-GMTMICVTHEMTFARDVS-DRVAFFHQGI 213
Cdd:COG2401 171 TAKRVARNLQKLARRaGITLVVATHHYDVIDDLQpDLLIFVGYGG 215
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
2-168 |
1.72e-19 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 86.61 E-value: 1.72e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 2 IEIENVRKSFSSLEV--LKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGTDVhaKGTDLNRLRRKV 79
Cdd:PRK11176 342 IEFRNVTFTYPGKEVpaLRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDL--RDYTLASLRNQV 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 80 GIVFQQWNAFpHLTVLENVMLAPRKvlglpKDKAEEI--AVKQLTHVGLGEKLKVYPNRM--------SGGQQQRMAIAR 149
Cdd:PRK11176 420 ALVSQNVHLF-NDTIANNIAYARTE-----QYSREQIeeAARMAYAMDFINKMDNGLDTVigengvllSGGQRQRIAIAR 493
|
170
....*....|....*....
gi 499282096 150 ALAMSPEYMLFDEVTSALD 168
Cdd:PRK11176 494 ALLRDSPILILDEATSALD 512
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
4-227 |
1.79e-19 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 84.45 E-value: 1.79e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 4 IENVRKSFSSLEVLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGTDVHAKGTDLnrLRRKVGIVF 83
Cdd:PRK10575 14 LRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKA--FARKVAYLP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 84 QQWNAFPHLTVLENVMLA--P-RKVLGLPKDKAEEIAVKQLTHVGlgekLKVYPNR----MSGGQQQRMAIARALAMSPE 156
Cdd:PRK10575 92 QQLPAAEGMTVRELVAIGryPwHGALGRFGAADREKVEEAISLVG----LKPLAHRlvdsLSGGERQRAWIAMLVAQDSR 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499282096 157 YMLFDEVTSALDPMLVGEVLDTLKMLAEE-GMTMICVTHEMTFARDVSDRVAFFHQGIMAEIGSPDQIFASP 227
Cdd:PRK10575 168 CLLLDEPTSALDIAHQVDVLALVHRLSQErGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRGE 239
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
3-217 |
6.64e-19 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 85.08 E-value: 6.64e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 3 EIENVR-KSFSSLEVLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGTDVHAKGTdlnRLRRKVGI 81
Cdd:COG3845 259 EVENLSvRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSP---RERRRLGV 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 82 VF-----QQWNAFPHLTVLENVML-----APRKVLG-LPKDKAEEIAVKQLthvglgEKLKV-YPN------RMSGGQQQ 143
Cdd:COG3845 336 AYipedrLGRGLVPDMSVAENLILgryrrPPFSRGGfLDRKAIRAFAEELI------EEFDVrTPGpdtparSLSGGNQQ 409
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499282096 144 RMAIARALAMSPEYMLFDEVTSALDpmlVG---EVLDTLKMLAEEGMTMICVTHEMTFARDVSDRVAFFHQG-IMAEI 217
Cdd:COG3845 410 KVILARELSRDPKLLIAAQPTRGLD---VGaieFIHQRLLELRDAGAAVLLISEDLDEILALSDRIAVMYEGrIVGEV 484
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
18-217 |
8.66e-19 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 84.84 E-value: 8.66e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 18 KGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGTDVHAKgTDLNRLRRKVGIVFQQWNA---FPHLTV 94
Cdd:PRK09700 280 RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPR-SPLDAVKKGMAYITESRRDngfFPNFSI 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 95 LENVMLAP-------RKVLGLPKDKAEE-IAVKQLTHVGLG-EKLKVYPNRMSGGQQQRMAIARALAMSPEYMLFDEVTS 165
Cdd:PRK09700 359 AQNMAISRslkdggyKGAMGLFHEVDEQrTAENQRELLALKcHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTR 438
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 499282096 166 ALDPMLVGEVLDTLKMLAEEGMTMICVTHEMTFARDVSDRVAFFHQGIMAEI 217
Cdd:PRK09700 439 GIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRLTQI 490
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1-202 |
1.70e-18 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 80.91 E-value: 1.70e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 1 MIEIENVRKSFSSLEVLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGTDVhakgTDLN--RLRRK 78
Cdd:PRK10247 7 LLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDI----STLKpeIYRQQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 79 VGIVFQQwnafPHL---TVLENVMLaPRKVLGLPKDkaEEIAVKQLTHVGLGEK-LKVYPNRMSGGQQQRMAIARALAMS 154
Cdd:PRK10247 83 VSYCAQT----PTLfgdTVYDNLIF-PWQIRNQQPD--PAIFLDDLERFALPDTiLTKNIAELSGGEKQRISLIRNLQFM 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 499282096 155 PEYMLFDEVTSALDPMLVGEVLDTLKMLAEE-GMTMICVTH---EMTFARDV 202
Cdd:PRK10247 156 PKVLLLDEITSALDESNKHNVNEIIHRYVREqNIAVLWVTHdkdEINHADKV 207
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
2-226 |
2.90e-18 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 83.23 E-value: 2.90e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 2 IEIENVrkSFSSLE---VLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGTDV----HAKgtdlnr 74
Cdd:PRK10790 341 IDIDNV--SFAYRDdnlVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLsslsHSV------ 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 75 LRRKVGIVfQQWNAFPHLTVLENVMLAprkvlglpKDKAEEIAVKQLTHVGLGEKLKVYP-----------NRMSGGQQQ 143
Cdd:PRK10790 413 LRQGVAMV-QQDPVVLADTFLANVTLG--------RDISEEQVWQALETVQLAELARSLPdglytplgeqgNNLSVGQKQ 483
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 144 RMAIARALAMSPEYMLFDEVTSALDPMLVGEVLDTLKMLAEEgMTMICVTHEMTFARDvSDRVAFFHQGIMAEIGSPDQI 223
Cdd:PRK10790 484 LLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREH-TTLVVIAHRLSTIVE-ADTILVLHRGQAVEQGTHQQL 561
|
...
gi 499282096 224 FAS 226
Cdd:PRK10790 562 LAA 564
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1-194 |
2.12e-17 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 78.53 E-value: 2.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 1 MIEIENVRKSFSSLEVLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGlEP---IDSGRIVIDGTDVhakgTDLN-RLR 76
Cdd:CHL00131 7 ILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG-HPaykILEGDILFKGESI----LDLEpEER 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 77 RKVGI--VFQQWNAFPHLTVLENVMLA---PRKVLGLPK-DKAE--EIAVKQLTHVGLGEK-LKVYPNR-MSGGQQQRMA 146
Cdd:CHL00131 82 AHLGIflAFQYPIEIPGVSNADFLRLAynsKRKFQGLPElDPLEflEIINEKLKLVGMDPSfLSRNVNEgFSGGEKKRNE 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 499282096 147 IARALAMSPEYMLFDEVTSALDPMLVGEVLDTLKMLAEEGMTMICVTH 194
Cdd:CHL00131 162 ILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIILITH 209
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1-194 |
4.56e-17 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 76.84 E-value: 4.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 1 MIEIENVRKSFSSLEVLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGtdvhaKGTDLNRLRRKVG 80
Cdd:PRK13539 2 MLEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDG-----GDIDDPDVAEACH 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 81 IVFQQwNAF-PHLTVLENVMLApRKVLGLPKDKAEEiavkQLTHVGLGEKLKVYPNRMSGGQQQRMAIARALAM-SPEYM 158
Cdd:PRK13539 77 YLGHR-NAMkPALTVAENLEFW-AAFLGGEELDIAA----ALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSnRPIWI 150
|
170 180 190
....*....|....*....|....*....|....*.
gi 499282096 159 LfDEVTSALDPMLVGEVLDTLKMLAEEGMTMICVTH 194
Cdd:PRK13539 151 L-DEPTAALDAAAVALFAELIRAHLAQGGIVIAATH 185
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
5-223 |
7.35e-17 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 77.33 E-value: 7.35e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 5 ENVRKSFSSLEVLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGTDVHAKGTdlNRLRRKVGIVFQ 84
Cdd:PRK10253 11 EQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYAS--KEVARRIGLLAQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 85 QWNAFPHLTVLENVMLA--PRKVLGLPKDKAEEIAV-KQLTHVGLGEKLKVYPNRMSGGQQQRMAIARALAMSPEYMLFD 161
Cdd:PRK10253 89 NATTPGDITVQELVARGryPHQPLFTRWRKEDEEAVtKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLD 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499282096 162 EVTSALDpmlVGEVLDTLKMLAE----EGMTMICVTHEMTFA-RDVSDRVAFFHQGIMAEiGSPDQI 223
Cdd:PRK10253 169 EPTTWLD---ISHQIDLLELLSElnreKGYTLAAVLHDLNQAcRYASHLIALREGKIVAQ-GAPKEI 231
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
20-217 |
7.47e-17 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 79.07 E-value: 7.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 20 IDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGTDVHAkgTDLNRLRRKVGIVFQQWNAFPHLtvlenvm 99
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTA--DNREAYRQLFSAVFSDFHLFDRL------- 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 100 laprkvLGLPKDKAEEIAVKQLTHVGLGEKLKVYPNR-----MSGGQQQRMAIARALAMSPEYMLFDEVTSALDPML--- 171
Cdd:COG4615 422 ------LGLDGEADPARARELLERLELDHKVSVEDGRfsttdLSQGQRKRLALLVALLEDRPILVFDEWAADQDPEFrrv 495
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 499282096 172 -VGEVLDTLKmlaEEGMTMICVTH-EMTFarDVSDRVAFFHQGIMAEI 217
Cdd:COG4615 496 fYTELLPELK---ARGKTVIAISHdDRYF--DLADRVLKMDYGKLVEL 538
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
1-206 |
1.05e-16 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 78.68 E-value: 1.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 1 MIEIENVRKSFSSLEVLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDS--GRIVIDGTDVHAKGTdlnRLRRK 78
Cdd:NF040905 1 ILEMRGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGSyeGEILFDGEVCRFKDI---RDSEA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 79 VGIVF--QQWNAFPHLTVLENVML----APRKVLGLPKDKAEeiAVKQLTHVGLGEKLKVYPNRMSGGQQQRMAIARALA 152
Cdd:NF040905 78 LGIVIihQELALIPYLSIAENIFLgnerAKRGVIDWNETNRR--ARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALS 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 499282096 153 MSPEYMLFDEVTSALDPMLVGEVLDTLKMLAEEGMTMICVTHEMTFARDVSDRV 206
Cdd:NF040905 156 KDVKLLILDEPTAALNEEDSAALLDLLLELKAQGITSIIISHKLNEIRRVADSI 209
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
20-227 |
1.62e-16 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 77.96 E-value: 1.62e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 20 IDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIdSGRIVIDGTDVHAkgTDLNRLRRKVGIVFQQwnafPHL---TVLE 96
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPY-QGSLKINGIELRE--LDPESWRKHLSWVGQN----PQLphgTLRD 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 97 NVMLAprkvlglpKDKAEEIAVKQ-LTHVGLGEKLKVYPN-----------RMSGGQQQRMAIARALAMSPEYMLFDEVT 164
Cdd:PRK11174 442 NVLLG--------NPDASDEQLQQaLENAWVSEFLPLLPQgldtpigdqaaGLSVGQAQRLALARALLQPCQLLLLDEPT 513
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499282096 165 SALDPMLVGEVLDTLKmLAEEGMTMICVTHEMTFARDVsDRVAFFHQGIMAEIGSPDQIFASP 227
Cdd:PRK11174 514 ASLDAHSEQLVMQALN-AASRRQTTLMVTHQLEDLAQW-DQIWVMQDGQIVQQGDYAELSQAG 574
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
16-194 |
2.20e-16 |
|
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: 74.84 E-value: 2.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 16 VLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGTDVHAKGTDLNRLRRKVGivfQQWNAFPHLTVL 95
Cdd:cd03231 15 LFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLG---HAPGIKTTLSVL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 96 ENVMLaprkvlgLPKDKAEEIAVKQLTHVGLGEKLKVYPNRMSGGQQQRMAIARALAMSPEYMLFDEVTSALDPMLVGEV 175
Cdd:cd03231 92 ENLRF-------WHADHSDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARF 164
|
170
....*....|....*....
gi 499282096 176 LDTLKMLAEEGMTMICVTH 194
Cdd:cd03231 165 AEAMAGHCARGGMVVLTTH 183
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
16-220 |
2.32e-16 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 76.02 E-value: 2.32e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 16 VLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCING--LEPIDS------GRIVIDGTDVHAkgTDLNRLRRKVGIVFQQWN 87
Cdd:PRK13547 16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGdlTGGGAPrgarvtGDVTLNGEPLAA--IDAPRLARLRAVLPQAAQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 88 -AFPhLTVLENVML-----APRKvlGLPKDKAEEIAVKQLTHVGLGEKLKVYPNRMSGGQQQRMAIARALAM-------- 153
Cdd:PRK13547 94 pAFA-FSAREIVLLgryphARRA--GALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLAQlwpphdaa 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499282096 154 -SPEYMLFDEVTSALDPMLVGEVLDTLKMLAEE-GMTMICVTHEMTFARDVSDRVAFFHQGIMAEIGSP 220
Cdd:PRK13547 171 qPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDwNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAP 239
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1-212 |
3.36e-16 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 76.97 E-value: 3.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 1 MIEIENVRKSFSSLEVLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGTDVHAKGTDLNRlRRKVG 80
Cdd:PRK10762 4 LLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQ-EAGIG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 81 IVFQQWNAFPHLTVLENVMLAPRKVLGLPK---DKAEEIAVKQLTHVGLGEKLKVYPNRMSGGQQQRMAIARALAMSPEY 157
Cdd:PRK10762 83 IIHQELNLIPQLTIAENIFLGREFVNRFGRidwKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKV 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 499282096 158 MLFDEVTSALDPMLVGEVLDTLKMLAEEGMTMICVTHEMTFARDVSDRVAFFHQG 212
Cdd:PRK10762 163 IIMDEPTDALTDTETESLFRVIRELKSQGRGIVYISHRLKEIFEICDDVTVFRDG 217
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
2-226 |
3.66e-16 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 77.32 E-value: 3.66e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 2 IEIENVRKSFSSL---EVLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCING-LEPIDSGRIVIDGTDVHAKgtdlnrlrr 77
Cdd:PLN03232 615 ISIKNGYFSWDSKtskPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGeLSHAETSSVVIRGSVAYVP--------- 685
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 78 KVGIVFqqwNAfphlTVLENVMLAPRKVlglPKDKAEEIAVKQLTHvglgeKLKVYPNR-----------MSGGQQQRMA 146
Cdd:PLN03232 686 QVSWIF---NA----TVRENILFGSDFE---SERYWRAIDVTALQH-----DLDLLPGRdlteigergvnISGGQKQRVS 750
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 147 IARALAMSPEYMLFDEVTSALDPMLVGEVLDTLKMLAEEGMTMICVTHEMTFARDVsDRVAFFHQGIMAEIGSPDQIFAS 226
Cdd:PLN03232 751 MARAVYSNSDIYIFDDPLSALDAHVAHQVFDSCMKDELKGKTRVLVTNQLHFLPLM-DRIILVSEGMIKEEGTFAELSKS 829
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
4-195 |
3.89e-16 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 77.23 E-value: 3.89e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 4 IENVRKSFSSLEVLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCInglepidSGRI---VIDGTDVHAKGTDLNRLRRKVG 80
Cdd:PLN03211 71 ISDETRQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNAL-------AGRIqgnNFTGTILANNRKPTKQILKRTG 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 81 IVFQQWNAFPHLTVLENVMLAprKVLGLPKD--KAEEIAVKQ--LTHVGLGE-KLKVYPNR----MSGGQQQRMAIARAL 151
Cdd:PLN03211 144 FVTQDDILYPHLTVRETLVFC--SLLRLPKSltKQEKILVAEsvISELGLTKcENTIIGNSfirgISGGERKRVSIAHEM 221
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 499282096 152 AMSPEYMLFDEVTSALDPMLVGEVLDTLKMLAEEGMTMICVTHE 195
Cdd:PLN03211 222 LINPSLLILDEPTSGLDATAAYRLVLTLGSLAQKGKTIVTSMHQ 265
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
4-212 |
5.86e-16 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 76.31 E-value: 5.86e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 4 IENVRKSFSSLEVLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGTDVHAKgTDLNRLRRKVGIVF 83
Cdd:PRK10982 1 MSNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFK-SSKEALENGISMVH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 84 QQWNAFPHLTVLENVMLA--PRKVLGLPKDKA--EEIAVKQLTHVGLGEKLKVypNRMSGGQQQRMAIARALAMSPEYML 159
Cdd:PRK10982 80 QELNLVLQRSVMDNMWLGryPTKGMFVDQDKMyrDTKAIFDELDIDIDPRAKV--ATLSVSQMQMIEIAKAFSYNAKIVI 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 499282096 160 FDEVTSALDPMLVGEVLDTLKMLAEEGMTMICVTHEMTFARDVSDRVAFFHQG 212
Cdd:PRK10982 158 MDEPTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDG 210
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
17-226 |
7.91e-16 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 76.32 E-value: 7.91e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 17 LKGIDLTVEKGEVVTIIGGSGSGKSTLLTCING-LEPIDSGRIVIDGTdvhakgtdlnrlrrkVGIVFQ-QW--NAfphl 92
Cdd:PLN03130 633 LSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGeLPPRSDASVVIRGT---------------VAYVPQvSWifNA---- 693
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 93 TVLENVMLaprkvlGLPKDKA---EEIAVKQLTHvglgeKLKVYPNR-----------MSGGQQQRMAIARALAMSPEYM 158
Cdd:PLN03130 694 TVRDNILF------GSPFDPEryeRAIDVTALQH-----DLDLLPGGdlteigergvnISGGQKQRVSMARAVYSNSDVY 762
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499282096 159 LFDEVTSALDPMLVGEVLDTLKMLAEEGMTMICVTHEMTFARDVsDRVAFFHQGIMAEIGSPDQIFAS 226
Cdd:PLN03130 763 IFDDPLSALDAHVGRQVFDKCIKDELRGKTRVLVTNQLHFLSQV-DRIILVHEGMIKEEGTYEELSNN 829
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
23-223 |
2.94e-15 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 72.66 E-value: 2.94e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 23 TVEKGEVVTIIGGSGSGKSTLLTCINGLEPiDSGRIVIDGTDV-HAKGTDLNRLRrkvGIVFQQWNAFPHLTVLEnvMLA 101
Cdd:PRK03695 18 EVRAGEILHLVGPNGAGKSTLLARMAGLLP-GSGSIQFAGQPLeAWSAAELARHR---AYLSQQQTPPFAMPVFQ--YLT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 102 prkvLGLPKDKAEEIAVKQLTHV----GLGEKLKVYPNRMSGGQQQRMAIARA-LAMSPE------YMLFDEVTSALDpm 170
Cdd:PRK03695 92 ----LHQPDKTRTEAVASALNEVaealGLDDKLGRSVNQLSGGEWQRVRLAAVvLQVWPDinpagqLLLLDEPMNSLD-- 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 499282096 171 lVGEV--LDTL-KMLAEEGMTMICVTHEMTFARDVSDRVAFFHQGIMAEIGSPDQI 223
Cdd:PRK03695 166 -VAQQaaLDRLlSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEV 220
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
16-239 |
5.00e-15 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 73.02 E-value: 5.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 16 VLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPiDSGRIVIDgtDVHAKGTDLNRL----RRKV-----GIVFQQW 86
Cdd:COG4170 22 AVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITK-DNWHVTAD--RFRWNGIDLLKLspreRRKIigreiAMIFQEP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 87 NAF--PHLTVLENVMLA-PRKVLG-----LPKDKAEEiaVKQLTH-VGLGEK---LKVYPNRMSGGQQQRMAIARALAMS 154
Cdd:COG4170 99 SSCldPSAKIGDQLIEAiPSWTFKgkwwqRFKWRKKR--AIELLHrVGIKDHkdiMNSYPHELTEGECQKVMIAMAIANQ 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 155 PEYMLFDEVTSALDPMLVGEVLDTL-KMLAEEGMTMICVTHEMTFARDVSDRVAFFHQGIMAEIGSPDQIFASPQNPETQ 233
Cdd:COG4170 177 PRLLIADEPTNAMESTTQAQIFRLLaRLNQLQGTSILLISHDLESISQWADTITVLYCGQTVESGPTEQILKSPHHPYTK 256
|
....*.
gi 499282096 234 KFLASV 239
Cdd:COG4170 257 ALLRSM 262
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
16-227 |
5.35e-15 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 73.59 E-value: 5.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 16 VLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGTDVHAkgTDLNRLRRKVGIVFQQwnafPHL--- 92
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTK--LQLDSWRSRLAVVSQT----PFLfsd 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 93 TVLENVmlaprkVLGLPKDKAEEI-AVKQLTHVG-------------LGEKLKVypnrMSGGQQQRMAIARALAMSPEYM 158
Cdd:PRK10789 404 TVANNI------ALGRPDATQQEIeHVARLASVHddilrlpqgydteVGERGVM----LSGGQKQRISIARALLLNAEIL 473
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499282096 159 LFDEVTSALDPMLVGEVLDTLKMLAeEGMTMICVTHEMTfARDVSDRVAFFHQGIMAEIGSPDQIFASP 227
Cdd:PRK10789 474 ILDDALSAVDGRTEHQILHNLRQWG-EGRTVIISAHRLS-ALTEASEILVMQHGHIAQRGNHDQLAQQS 540
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
14-169 |
5.91e-15 |
|
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: 70.85 E-value: 5.91e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 14 LEVLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGTDVHAKGTDLNR----LRRKVGIVfqqwnaf 89
Cdd:TIGR01189 13 RMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHEnilyLGHLPGLK------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 90 PHLTVLENVMLAPRkvLGLPKDKAEEIAvkqLTHVGLGEKLKVYPNRMSGGQQQRMAIARALAMSPEYMLFDEVTSALDP 169
Cdd:TIGR01189 86 PELSALENLHFWAA--IHGGAQRTIEDA---LAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDK 160
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
15-212 |
1.73e-14 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 72.01 E-value: 1.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 15 EVLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGTDVHAKGTdLNRLRRkvGIVF-----QQWNAF 89
Cdd:PRK15439 277 EGFRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALST-AQRLAR--GLVYlpedrQSSGLY 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 90 PHLTVLENVMLAPRKVLGLPKDKAEEIAVKQLTHVGLGEKL--KVYPNR-MSGGQQQRMAIARALAMSPEYMLFDEVTSA 166
Cdd:PRK15439 354 LDAPLAWNVCALTHNRRGFWIKPARENAVLERYRRALNIKFnhAEQAARtLSGGNQQKVLIAKCLEASPQLLIVDEPTRG 433
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 499282096 167 LDPMLVGEVLDTLKMLAEEGMTMICVTHEMTFARDVSDRVAFFHQG 212
Cdd:PRK15439 434 VDVSARNDIYQLIRSIAAQNVAVLFISSDLEEIEQMADRVLVMHQG 479
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
17-223 |
2.93e-14 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 71.46 E-value: 2.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 17 LKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGT-DVHAKGTDLNRlrrkvgivfqqwnafpHLTVL 95
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSaALIAISSGLNG----------------QLTGI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 96 ENVMLAPRkVLGLPKDKAEEIAVKQLTHVGLGEKLKVYPNRMSGGQQQRMAIARALAMSPEYMLFDEVTSALDPMLVGEV 175
Cdd:PRK13545 104 ENIELKGL-MMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKC 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 499282096 176 LDTLKMLAEEGMTMICVTHEMTFARDVSDRVAFFHQGIMAEIGSPDQI 223
Cdd:PRK13545 183 LDKMNEFKEQGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEV 230
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
20-212 |
6.29e-14 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 70.24 E-value: 6.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 20 IDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPID-SGRIVIDGTDVHAKgTDLNRLRRKVGIV---FQQWNAFPHLTVL 95
Cdd:TIGR02633 279 VSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKPVDIR-NPAQAIRAGIAMVpedRKRHGIVPILGVG 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 96 ENVMLAPRK---VLGLPKDKAEE----IAVKQLTHVGLGEKLKVypNRMSGGQQQRMAIARALAMSPEYMLFDEVTSALD 168
Cdd:TIGR02633 358 KNITLSVLKsfcFKMRIDAAAELqiigSAIQRLKVKTASPFLPI--GRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVD 435
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 499282096 169 PMLVGEVLDTLKMLAEEGMTMICVTHEMTFARDVSDRVAFFHQG 212
Cdd:TIGR02633 436 VGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEG 479
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
16-226 |
7.19e-14 |
|
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: 70.74 E-value: 7.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 16 VLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGTDVHAKGtdLNRLRRKVGIV------------- 82
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIG--LHDLRFKITIIpqdpvlfsgslrm 1378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 83 ----FQQWNAFPHLTVLEnvmLAPRK--VLGLPKDKAEEIAVKqlthvglGEKLKVypnrmsgGQQQRMAIARALAMSPE 156
Cdd:TIGR00957 1379 nldpFSQYSDEEVWWALE---LAHLKtfVSALPDKLDHECAEG-------GENLSV-------GQRQLVCLARALLRKTK 1441
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 157 YMLFDEVTSALDPMLVGEVLDTLKMLAEEgMTMICVTHEMTFARDVSdRVAFFHQGIMAEIGSPDQIFAS 226
Cdd:TIGR00957 1442 ILVLDEATAAVDLETDNLIQSTIRTQFED-CTVLTIAHRLNTIMDYT-RVIVLDKGEVAEFGAPSNLLQQ 1509
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
16-228 |
9.14e-14 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 70.19 E-value: 9.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 16 VLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGTDVHAKGtdLNRLRRKVGIVFQQwnafPHL--- 92
Cdd:PTZ00243 1325 VLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYG--LRELRRQFSMIPQD----PVLfdg 1398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 93 TVLENVmlAPRkvlgLPKDKAEEIAVKQLthVGLGEKLKVYP-----------NRMSGGQQQRMAIARA-LAMSPEYMLF 160
Cdd:PTZ00243 1399 TVRQNV--DPF----LEASSAEVWAALEL--VGLRERVASESegidsrvleggSNYSVGQRQLMCMARAlLKKGSGFILM 1470
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499282096 161 DEVTSALDPMLVGEVLDTLkMLAEEGMTMICVTHEM-TFARdvSDRVAFFHQGIMAEIGSPDQIFASPQ 228
Cdd:PTZ00243 1471 DEATANIDPALDRQIQATV-MSAFSAYTVITIAHRLhTVAQ--YDKIIVMDHGAVAEMGSPRELVMNRQ 1536
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
1-218 |
1.24e-13 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 68.28 E-value: 1.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 1 MIEIENVRKSFSSLEVLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDsgrivIDGTDVHAKGTDL------NR 74
Cdd:PRK09580 1 MLSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDYE-----VTGGTVEFKGKDLlelspeDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 75 LRRKVGIVFQQWNAFPHLT---VLENVMLAPRKVLGL-PKDK-------AEEIAVKQLTHVGLGEKLKVypnRMSGGQQQ 143
Cdd:PRK09580 76 AGEGIFMAFQYPVEIPGVSnqfFLQTALNAVRSYRGQePLDRfdfqdlmEEKIALLKMPEDLLTRSVNV---GFSGGEKK 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 144 RMAIARALAMSPEYMLFDEVTSALDpmlvgevLDTLKMLAE-------EGMTMICVTHEMTFARDVS-DRVAFFHQGIMA 215
Cdd:PRK09580 153 RNDILQMAVLEPELCILDESDSGLD-------IDALKIVADgvnslrdGKRSFIIVTHYQRILDYIKpDYVHVLYQGRIV 225
|
...
gi 499282096 216 EIG 218
Cdd:PRK09580 226 KSG 228
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
17-196 |
1.35e-13 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 68.37 E-value: 1.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 17 LKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGTDVhakgtdlNRLRRK--VGIVFQQ----WnAFP 90
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPT-------RQALQKnlVAYVPQSeevdW-SFP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 91 HLtvLENVMLAPR----KVLGLPKDKAEEIAVKQLTHVGLGEKLKVYPNRMSGGQQQRMAIARALAMSPEYMLFDEVTSA 166
Cdd:PRK15056 95 VL--VEDVVMMGRyghmGWLRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTG 172
|
170 180 190
....*....|....*....|....*....|
gi 499282096 167 LDPMLVGEVLDTLKMLAEEGMTMICVTHEM 196
Cdd:PRK15056 173 VDVKTEARIISLLRELRDEGKTMLVSTHNL 202
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
1-194 |
1.43e-13 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 67.14 E-value: 1.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 1 MIEIENV------RKSFSslevlkGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGTDVHAKGTDLNR 74
Cdd:PRK13538 1 MLEARNLacerdeRILFS------GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 75 ----LRRKVGIVfqqwnafPHLTVLENVmlapRKVLGLPKDKAEEIAVKQLTHVGLGEKLKVYPNRMSGGQQQRMAIARA 150
Cdd:PRK13538 75 dllyLGHQPGIK-------TELTALENL----RFYQRLHGPGDDEALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARL 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 499282096 151 LAMSPEYMLFDEVTSALDPMLVGEVLDTLKMLAEEGMTMICVTH 194
Cdd:PRK13538 144 WLTRAPLWILDEPFTAIDKQGVARLEALLAQHAEQGGMVILTTH 187
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
1-239 |
1.66e-13 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 68.68 E-value: 1.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 1 MIEIENVRKSFSSLE-VLKGID---LTVEKGEVVTIIGGSGSGKSTLLTCINGLEPiDSGRIVIDG---TDVhakgtDLN 73
Cdd:PRK15093 3 LLDIRNLTIEFKTSDgWVKAVDrvsMTLTEGEIRGLVGESGSGKSLIAKAICGVTK-DNWRVTADRmrfDDI-----DLL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 74 RL----RRK-----VGIVFQQWNAF--PHLTVLENVMLA-P--------RKVLGLPKDKAEEIavkqLTHVGLGEK---L 130
Cdd:PRK15093 77 RLspreRRKlvghnVSMIFQEPQSCldPSERVGRQLMQNiPgwtykgrwWQRFGWRKRRAIEL----LHRVGIKDHkdaM 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 131 KVYPNRMSGGQQQRMAIARALAMSPEYMLFDEVTSALDPMLVGEVLDTLKMLAE-EGMTMICVTHEMTFARDVSDRVAFF 209
Cdd:PRK15093 153 RSFPYELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQnNNTTILLISHDLQMLSQWADKINVL 232
|
250 260 270
....*....|....*....|....*....|
gi 499282096 210 HQGIMAEIGSPDQIFASPQNPETQKFLASV 239
Cdd:PRK15093 233 YCGQTVETAPSKELVTTPHHPYTQALIRAI 262
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
13-212 |
1.74e-13 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 69.26 E-value: 1.74e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 13 SLEV-------LKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGTDVHAKGTD---------LNRLR 76
Cdd:PRK10762 257 RLKVdnlsgpgVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQdglangivyISEDR 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 77 RKVGIVFQqwnafphLTVLENVMLAP----RKVLGLPKDKAEEIAVkqlthvglGEKLKVY----PNR------MSGGQQ 142
Cdd:PRK10762 337 KRDGLVLG-------MSVKENMSLTAlryfSRAGGSLKHADEQQAV--------SDFIRLFniktPSMeqaiglLSGGNQ 401
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499282096 143 QRMAIARALAMSPEYMLFDEVTSALDpmlVG---EVLDTLKMLAEEGMTMICVTHEMTFARDVSDRVAFFHQG 212
Cdd:PRK10762 402 QKVAIARGLMTRPKVLILDEPTRGVD---VGakkEIYQLINQFKAEGLSIILVSSEMPEVLGMSDRILVMHEG 471
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1-206 |
3.52e-13 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 68.44 E-value: 3.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 1 MIEIENVRKSFSSLEVLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDgTDV-----------HAKG 69
Cdd:PRK11147 3 LISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYE-QDLivarlqqdpprNVEG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 70 TDLNRLRRKVGIVFQQWNAFPHLTVLenVMLAPR-KVLglpkDKAEEIAvKQLTHVGLG----------EKLKVYPNR-- 136
Cdd:PRK11147 82 TVYDFVAEGIEEQAEYLKRYHDISHL--VETDPSeKNL----NELAKLQ-EQLDHHNLWqlenrinevlAQLGLDPDAal 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499282096 137 --MSGGQQQRMAIARALAMSPEYMLFDEVTSALDpmlvgevLDTLKMLaeEGM------TMICVTHEMTFARDVSDRV 206
Cdd:PRK11147 155 ssLSGGWLRKAALGRALVSNPDVLLLDEPTNHLD-------IETIEWL--EGFlktfqgSIIFISHDRSFIRNMATRI 223
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-228 |
4.83e-13 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 66.29 E-value: 4.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 1 MIEIENVRKSFSSLEVLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGtdvhakgtdlnRLRrkVG 80
Cdd:PRK09544 4 LVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNG-----------KLR--IG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 81 IVFQQWNAFPH--LTVLENVMLAP--RKVLGLPKdkaeeiavkqLTHVGLGEKLKVYPNRMSGGQQQRMAIARALAMSPE 156
Cdd:PRK09544 71 YVPQKLYLDTTlpLTVNRFLRLRPgtKKEDILPA----------LKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQ 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499282096 157 YMLFDEVTSALDpmLVGEV--LDTLKMLAEE-GMTMICVTHEMTFARDVSDRVAFFHQGIMAEiGSPDQIFASPQ 228
Cdd:PRK09544 141 LLVLDEPTQGVD--VNGQValYDLIDQLRRElDCAVLMVSHDLHLVMAKTDEVLCLNHHICCS-GTPEVVSLHPE 212
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
12-198 |
6.32e-13 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 65.82 E-value: 6.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 12 SSLEVLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGTDVHAKGTDLNRLRRKVGIVF---QQW-- 86
Cdd:cd03290 12 SGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRNRYSVAYaaqKPWll 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 87 NAfphlTVLENVmlaprkVLGLPKDKAEEIAVkqLTHVGLGEKLKVYPN-----------RMSGGQQQRMAIARALAMSP 155
Cdd:cd03290 92 NA----TVEENI------TFGSPFNKQRYKAV--TDACSLQPDIDLLPFgdqteigergiNLSGGQRQRICVARALYQNT 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 499282096 156 EYMLFDEVTSALDPMLVGEVLDT--LKMLAEEGMTMICVTHEMTF 198
Cdd:cd03290 160 NIVFLDDPFSALDIHLSDHLMQEgiLKFLQDDKRTLVLVTHKLQY 204
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
4-190 |
9.57e-13 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 64.98 E-value: 9.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 4 IENVRKSFSSLEVLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPidsGRIVIDGtDVHAKGTDL----NRLRRKV 79
Cdd:cd03233 10 SFTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTE---GNVSVEG-DIHYNGIPYkefaEKYPGEI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 80 GIVFQQWNAFPHLTVLENVMLAprkvlglpkdkaeeiavkqlthvglgekLKVYPNRM----SGGQQQRMAIARALAMSP 155
Cdd:cd03233 86 IYVSEEDVHFPTLTVRETLDFA----------------------------LRCKGNEFvrgiSGGERKRVSIAEALVSRA 137
|
170 180 190
....*....|....*....|....*....|....*.
gi 499282096 156 EYMLFDEVTSALDPMLVGEVLDTLKMLA-EEGMTMI 190
Cdd:cd03233 138 SVLCWDNSTRGLDSSTALEILKCIRTMAdVLKTTTF 173
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
2-200 |
1.42e-12 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 66.98 E-value: 1.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 2 IEIENVRKSFSS---LEVLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDgtDVH-AKGTDLNRLRR 77
Cdd:PTZ00265 383 IQFKNVRFHYDTrkdVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIIN--DSHnLKDINLKWWRS 460
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 78 KVGIVFQQWNAFPH------------LTVLE-------------------------------NVMLAPRKVLGLPKDKAE 114
Cdd:PTZ00265 461 KIGVVSQDPLLFSNsiknnikyslysLKDLEalsnyynedgndsqenknkrnscrakcagdlNDMSNTTDSNELIEMRKN 540
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 115 EIAVKQLTHVGLGEKLKVY-----------------PNRMSGGQQQRMAIARALAMSPEYMLFDEVTSALD---PMLVGE 174
Cdd:PTZ00265 541 YQTIKDSEVVDVSKKVLIHdfvsalpdkyetlvgsnASKLSGGQKQRISIARAIIRNPKILILDEATSSLDnksEYLVQK 620
|
250 260
....*....|....*....|....*.
gi 499282096 175 VLDTLKmlAEEGMTMICVTHEMTFAR 200
Cdd:PTZ00265 621 TINNLK--GNENRITIIIAHRLSTIR 644
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
2-230 |
1.67e-12 |
|
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: 64.93 E-value: 1.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 2 IEIEN--VRKSFSSLEVLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGTDVHAkgTDLNRLRRKV 79
Cdd:cd03288 20 IKIHDlcVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISK--LPLHTLRSRL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 80 GIVFQ---------QWNAFPHLTVLENVMLaprkvlglpkdKAEEIA-----VKQLTHvGLGEKLKVYPNRMSGGQQQRM 145
Cdd:cd03288 98 SIILQdpilfsgsiRFNLDPECKCTDDRLW-----------EALEIAqlknmVKSLPG-GLDAVVTEGGENFSVGQRQLF 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 146 AIARALAMSPEYMLFDEVTSALDpMLVGEVLDTLKMLAEEGMTMICVTHEMTFARDvSDRVAFFHQGIMAEIGSPDQIFA 225
Cdd:cd03288 166 CLARAFVRKSSILIMDEATASID-MATENILQKVVMTAFADRTVVTIAHRVSTILD-ADLVLVLSRGILVECDTPENLLA 243
|
....*
gi 499282096 226 SPQNP 230
Cdd:cd03288 244 QEDGV 248
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
16-225 |
3.79e-12 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 65.53 E-value: 3.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 16 VLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGTDVHAKGtdLNRLRRKVGIVFQ---------QW 86
Cdd:PLN03130 1254 VLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFG--LMDLRKVLGIIPQapvlfsgtvRF 1331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 87 NAFP---HLTV-----LENVMLAP---RKVLGLPKDKAEEiavkqlthvglGEKLKVypnrmsgGQQQRMAIARALAMSP 155
Cdd:PLN03130 1332 NLDPfneHNDAdlwesLERAHLKDvirRNSLGLDAEVSEA-----------GENFSV-------GQRQLLSLARALLRRS 1393
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499282096 156 EYMLFDEVTSALDpmlVGEvlDTL--KMLAEE--GMTMICVTHEMTFARDvSDRVAFFHQGIMAEIGSPDQIFA 225
Cdd:PLN03130 1394 KILVLDEATAAVD---VRT--DALiqKTIREEfkSCTMLIIAHRLNTIID-CDRILVLDAGRVVEFDTPENLLS 1461
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
16-225 |
4.10e-12 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 65.38 E-value: 4.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 16 VLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGTDVHAKGtdLNRLRRKVGIVFQQWNAFPHlTVL 95
Cdd:PLN03232 1251 VLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFG--LTDLRRVLSIIPQSPVLFSG-TVR 1327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 96 ENV-MLAPRKVLGLPK--DKAEEIAVKQLTHVGLGEKLKVYPNRMSGGQQQRMAIARALAMSPEYMLFDEVTSALDPMLV 172
Cdd:PLN03232 1328 FNIdPFSEHNDADLWEalERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTD 1407
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 499282096 173 GEVLDTLKmlaEE--GMTMICVTHEMTFARDVsDRVAFFHQGIMAEIGSPDQIFA 225
Cdd:PLN03232 1408 SLIQRTIR---EEfkSCTMLVIAHRLNTIIDC-DKILVLSSGQVLEYDSPQELLS 1458
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
24-219 |
4.19e-12 |
|
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: 65.42 E-value: 4.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 24 VEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGTDVHakgTDLNRLRRKVGIVfQQWNAFPHL-TVLENVMLAP 102
Cdd:TIGR01257 1962 VRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSIL---TNISDVHQNMGYC-PQFDAIDDLlTGREHLYLYA 2037
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 103 RkVLGLPKDKAEEIAVKQLTHVGLgeklKVYPNRM----SGGQQQRMAIARALAMSPEYMLFDEVTSALDPMLVGEVLDT 178
Cdd:TIGR01257 2038 R-LRGVPAEEIEKVANWSIQSLGL----SLYADRLagtySGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNT 2112
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 499282096 179 LKMLAEEGMTMICVTHEMTFARDVSDRVAFFHQGIMAEIGS 219
Cdd:TIGR01257 2113 IVSIIREGRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGT 2153
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
17-219 |
4.44e-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: 65.35 E-value: 4.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 17 LKGIDLTVEKGEVVTIIGGSGSGKSTLLTCIngLEPIDSgrivIDGtDVHAKGTdlnrlrrkVGIVFQQ-WnaFPHLTVL 95
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSAL--LAEMDK----VEG-HVHMKGS--------VAYVPQQaW--IQNDSLR 716
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 96 ENVMLAprKVLGLPKDKAEEIAVKQLTHVGL---GEKLKVYPN--RMSGGQQQRMAIARALAMSPEYMLFDEVTSALDPM 170
Cdd:TIGR00957 717 ENILFG--KALNEKYYQQVLEACALLPDLEIlpsGDRTEIGEKgvNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAH 794
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 499282096 171 LVGEVLDtlKMLAEEGM----TMICVTHEMTFARDVsDRVAFFHQGIMAEIGS 219
Cdd:TIGR00957 795 VGKHIFE--HVIGPEGVlknkTRILVTHGISYLPQV-DVIIVMSGGKISEMGS 844
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
20-226 |
8.17e-12 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 64.38 E-value: 8.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 20 IDLTVEKGEVVTIIGGSGSGKST---LLTcinGLEPIDSGRIVIDGTDVHAKgtDLNrLRRKVGIVFQQWNAFPHLTVLE 96
Cdd:NF033858 285 VSFRIRRGEIFGFLGSNGCGKSTtmkMLT---GLLPASEGEAWLFGQPVDAG--DIA-TRRRVGYMSQAFSLYGELTVRQ 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 97 NVMLAPRkVLGLPKDKAEEiAVKQLTH-VGLGEKLKVYPNRMSGGQQQRMAIARALAMSPEYMLFDEVTSALDP------ 169
Cdd:NF033858 359 NLELHAR-LFHLPAAEIAA-RVAEMLErFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPvardmf 436
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499282096 170 --MLVGevldtlkmLA-EEGMTMICVTHEMTFA-RdvSDRVAFFHQGIMAEIGSPDQIFAS 226
Cdd:NF033858 437 wrLLIE--------LSrEDGVTIFISTHFMNEAeR--CDRISLMHAGRVLASDTPAALVAA 487
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
16-169 |
1.15e-11 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 62.17 E-value: 1.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 16 VLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGTdvHAKGTDLNRLrrkVGIVFQQWNAFPHLTVL 95
Cdd:PRK13543 26 VFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGK--TATRGDRSRF---MAYLGHLPGLKADLSTL 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499282096 96 ENVMLaprkVLGLPKDKAEEIAVKQLTHVGLGEKLKVYPNRMSGGQQQRMAIARaLAMSPEYM-LFDEVTSALDP 169
Cdd:PRK13543 101 ENLHF----LCGLHGRRAKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALAR-LWLSPAPLwLLDEPYANLDL 170
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
20-215 |
1.25e-11 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 63.78 E-value: 1.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 20 IDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGTDVHAKGT-DLNRL--------RRKVGIVfqqwnafP 90
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPrDAIRAgimlcpedRKAEGII-------P 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 91 HLTVLENVMLAPR----KVLGLPKDKAE-EIAVKQLthvglgEKLKV-YPNR------MSGGQQQRMAIARALAMSPEYM 158
Cdd:PRK11288 345 VHSVADNINISARrhhlRAGCLINNRWEaENADRFI------RSLNIkTPSReqlimnLSGGNQQKAILGRWLSEDMKVI 418
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 159 LFDEVTSALDpmlVG---EVLDTLKMLAEEGMTMICVTHEMTFARDVSDRVAFFHQGIMA 215
Cdd:PRK11288 419 LLDEPTRGID---VGakhEIYNVIYELAAQGVAVLFVSSDLPEVLGVADRIVVMREGRIA 475
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
16-195 |
1.89e-11 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 63.59 E-value: 1.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 16 VLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINglEPIDSGriVIDGTDVHAKGTDLNR-LRRKVGIVFQQWNAFPHLTV 94
Cdd:TIGR00956 778 ILNNVDGWVKPGTLTALMGASGAGKTTLLNVLA--ERVTTG--VITGGDRLVNGRPLDSsFQRSIGYVQQQDLHLPTSTV 853
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 95 LENVMLA-----PRKVLGLPKDKAEEIAVKQLTH-------VGL-GEKLKVYpnrmsggQQQRMAIARALAMSPEYMLF- 160
Cdd:TIGR00956 854 RESLRFSaylrqPKSVSKSEKMEYVEEVIKLLEMesyadavVGVpGEGLNVE-------QRKRLTIGVELVAKPKLLLFl 926
|
170 180 190
....*....|....*....|....*....|....*
gi 499282096 161 DEVTSALDPMLVGEVLDTLKMLAEEGMTMICVTHE 195
Cdd:TIGR00956 927 DEPTSGLDSQTAWSICKLMRKLADHGQAILCTIHQ 961
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
54-240 |
2.88e-11 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 62.74 E-value: 2.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 54 DSGRIVIDGTDVHakGTDLNRLRRKVGIVFQQWNAFpHLTVLENVMLAprkvlglpKDKAEEIAVKQLTH-VGLGEKLKV 132
Cdd:PTZ00265 1275 NSGKILLDGVDIC--DYNLKDLRNLFSIVSQEPMLF-NMSIYENIKFG--------KEDATREDVKRACKfAAIDEFIES 1343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 133 YPNR-----------MSGGQQQRMAIARALAMSPEYMLFDEVTSALDP---MLVGEVLDTLKMLAEEgmTMICVTHEMTF 198
Cdd:PTZ00265 1344 LPNKydtnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSnseKLIEKTIVDIKDKADK--TIITIAHRIAS 1421
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 499282096 199 ARDvSDRVAFFHqgimaeigSPDQIFASPQNPETQKFLASVR 240
Cdd:PTZ00265 1422 IKR-SDKIVVFN--------NPDRTGSFVQAHGTHEELLSVQ 1454
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
2-206 |
6.08e-11 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 61.45 E-value: 6.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 2 IEIENVRKSFSSLEVLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIV-IDGTDV------HAK--GTDL 72
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKwSENANIgyyaqdHAYdfENDL 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 73 NrlrrkvgiVFQ---QWNAFPHLTvlenvmLAPRKVLGLPKDKAEEIavkqlthvglGEKLKVypnrMSGGQQQRMAIAR 149
Cdd:PRK15064 400 T--------LFDwmsQWRQEGDDE------QAVRGTLGRLLFSQDDI----------KKSVKV----LSGGEKGRMLFGK 451
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 499282096 150 ALAMSPEYMLFDEVTSALDpMlvgEVLDTLKMLAE--EGmTMICVTHEMTFARDVSDRV 206
Cdd:PRK15064 452 LMMQKPNVLVMDEPTNHMD-M---ESIESLNMALEkyEG-TLIFVSHDREFVSSLATRI 505
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
23-212 |
8.60e-11 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 61.10 E-value: 8.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 23 TVEKGEVVTIIGGSGSGKSTLLTCINGLEP-IDSGRIVIDGTDVHAKG-TDLNRL--------RRKVGIVfqqwnafPHL 92
Cdd:PRK13549 284 SLRRGEILGIAGLVGAGRTELVQCLFGAYPgRWEGEIFIDGKPVKIRNpQQAIAQgiamvpedRKRDGIV-------PVM 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 93 TVLENVMLA--PRKVLGLPKDKAEEI-----AVKQLTHVGLGEKLKVypNRMSGGQQQRMAIARALAMSPEYMLFDEVTS 165
Cdd:PRK13549 357 GVGKNITLAalDRFTGGSRIDDAAELktileSIQRLKVKTASPELAI--ARLSGGNQQKAVLAKCLLLNPKILILDEPTR 434
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 499282096 166 ALDpmlVG---EVLDTLKMLAEEGMTMICVTHEMTFARDVSDRVAFFHQG 212
Cdd:PRK13549 435 GID---VGakyEIYKLINQLVQQGVAIIVISSELPEVLGLSDRVLVMHEG 481
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
16-212 |
1.10e-10 |
|
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: 61.08 E-value: 1.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 16 VLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCING-LEPID-----SGRIVIDgtdvhakgtdlnrlrrkvgivfQQWNAF 89
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGeLEPSEgkikhSGRISFS----------------------PQTSWI 498
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 90 PHLTVLENVmlaprkVLGLPKDKAEEIAVkqLTHVGLGEKLKVYPNR-----------MSGGQQQRMAIARALAMSPEYM 158
Cdd:TIGR01271 499 MPGTIKDNI------IFGLSYDEYRYTSV--IKACQLEEDIALFPEKdktvlgeggitLSGGQRARISLARAVYKDADLY 570
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 499282096 159 LFDEVTSALDPMLVGEVLDT--LKMLAEEgmTMICVTHEMTFARDvSDRVAFFHQG 212
Cdd:TIGR01271 571 LLDSPFTHLDVVTEKEIFESclCKLMSNK--TRILVTSKLEHLKK-ADKILLLHEG 623
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
12-195 |
1.17e-10 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 58.79 E-value: 1.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 12 SSLEVLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPID--SGRIVIDGtdvhaKGTDLNrLRRKVGIVFQQWNAF 89
Cdd:cd03232 18 GKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAGviTGEILING-----RPLDKN-FQRSTGYVEQQDVHS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 90 PHLTVLENVMLAPrKVLGLpkdkaeeiavkqlthvglgeklkvypnrmSGGQQQRMAIARALAMSPEYMLFDEVTSALDP 169
Cdd:cd03232 92 PNLTVREALRFSA-LLRGL-----------------------------SVEQRKRLTIGVELAAKPSILFLDEPTSGLDS 141
|
170 180
....*....|....*....|....*.
gi 499282096 170 MLVGEVLDTLKMLAEEGMTMICVTHE 195
Cdd:cd03232 142 QAAYNIVRFLKKLADSGQAILCTIHQ 167
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
17-240 |
1.30e-10 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 59.83 E-value: 1.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 17 LKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDG-TDVHAKGTDLNrlrrkvgivfqqwnafPHLTVL 95
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGeVSVIAISAGLS----------------GQLTGI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 96 ENV---MLaprkVLGLPKDKAEEIAVKQLTHVGLGEKLKVYPNRMSGGQQQRMAIARALAMSPEYMLFDEVTSALDPMLV 172
Cdd:PRK13546 104 ENIefkML----CMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFA 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499282096 173 GEVLDTLKMLAEEGMTMICVTHEMTFARDVSDRVAFFHQGIMAEIGSPDQIFaspqnPETQKFLASVR 240
Cdd:PRK13546 180 QKCLDKIYEFKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDVL-----PKYEAFLNDFK 242
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
2-223 |
1.38e-10 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 60.13 E-value: 1.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 2 IEIENVRKSFSSLEVLKGIDLTVEKGEVVTIIG--GSGSGKSTLLTCINGlePiDSGRiviDGTDVHAKGTDLNRLRRKV 79
Cdd:NF000106 14 VEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGp*GAA**RGALPAHV*G--P-DAGR---RPWRF*TWCANRRALRRTI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 80 G----IVFQQWNAFphlTVLENVMLAPRKvLGLPKDKAEEIAVKQLTHVGLGEKLKVYPNRMSGGQQQRMAIARALAMSP 155
Cdd:NF000106 88 G*hrpVR*GRRESF---SGRENLYMIGR*-LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499282096 156 EYMLFDEVTSALDPMLVGEVLDTLKMLAEEGMTMICVTHEMTFARDVSDRVAFFHQGIMAEIGSPDQI 223
Cdd:NF000106 164 AVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDEL 231
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
16-180 |
1.51e-10 |
|
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: 60.69 E-value: 1.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 16 VLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDsGRIVIDGtdVHAKGTDLNRLRRKVGIVFQQwnafphLTVL 95
Cdd:TIGR01271 1234 VLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTE-GEIQIDG--VSWNSVTLQTWRKAFGVIPQK------VFIF 1304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 96 ENVMlapRKVLGLPKDKAEEIAVKQLTHVGLGEKLKVYPNR-----------MSGGQQQRMAIARALAMSPEYMLFDEVT 164
Cdd:TIGR01271 1305 SGTF---RKNLDPYEQWSDEEIWKVAEEVGLKSVIEQFPDKldfvlvdggyvLSNGHKQLMCLARSILSKAKILLLDEPS 1381
|
170
....*....|....*.
gi 499282096 165 SALDPMLVGEVLDTLK 180
Cdd:TIGR01271 1382 AHLDPVTLQIIRKTLK 1397
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
15-202 |
1.87e-10 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 60.33 E-value: 1.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 15 EVLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGlepIDSGrivIDGTDVHAKGtdlnrlrRKVGIVFQQWNAFPHLTV 94
Cdd:TIGR03719 19 EILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAG---VDKD---FNGEARPQPG-------IKVGYLPQEPQLDPTKTV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 95 LENVMLAPRKVLGL-------------PKDKAEEIAVKQ------LTHVGL----------GEKLKVYP-----NRMSGG 140
Cdd:TIGR03719 86 RENVEEGVAEIKDAldrfneisakyaePDADFDKLAAEQaelqeiIDAADAwdldsqleiaMDALRCPPwdadvTKLSGG 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499282096 141 QQQRMAIARALAMSPEYMLFDEVTSALDpmlvGEVLDTL-KMLAEEGMTMICVTHEMTFARDV 202
Cdd:TIGR03719 166 ERRRVALCRLLLSKPDMLLLDEPTNHLD----AESVAWLeRHLQEYPGTVVAVTHDRYFLDNV 224
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
2-207 |
2.13e-10 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 59.95 E-value: 2.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 2 IEIENVRKSFSSLEVLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIdGTDVhakgtdlnrlrrKVGI 81
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETV------------KLAY 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 82 VFQQWNAF-PHLTVLE------------NVMLAPRKVLGL--PKDKAEEIAVKQLthvglgeklkvypnrmSGGQQQRMA 146
Cdd:TIGR03719 390 VDQSRDALdPNKTVWEeisggldiiklgKREIPSRAYVGRfnFKGSDQQKKVGQL----------------SGGERNRVH 453
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499282096 147 IARALAMSPEYMLFDEVTSALDpmlvgevLDTLKMLAEE-----GMTMIcVTHEMTFArdvsDRVA 207
Cdd:TIGR03719 454 LAKTLKSGGNVLLLDEPTNDLD-------VETLRALEEAllnfaGCAVV-ISHDRWFL----DRIA 507
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
10-212 |
4.34e-10 |
|
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: 58.33 E-value: 4.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 10 SFSSLE-----VLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCING-LEPiDSGRIVIDGtdvhakgtdlnrlrrKVGIVF 83
Cdd:cd03291 41 FFSNLClvgapVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGeLEP-SEGKIKHSG---------------RISFSS 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 84 QQWNAFPHlTVLENVmlaprkVLGLPKDKAEEIAVKQLTHvgLGEKLKVYPNR-----------MSGGQQQRMAIARALA 152
Cdd:cd03291 105 QFSWIMPG-TIKENI------IFGVSYDEYRYKSVVKACQ--LEEDITKFPEKdntvlgeggitLSGGQRARISLARAVY 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499282096 153 MSPEYMLFDEVTSALDPMLVGEVLDT--LKMLAEEgmTMICVTHEMTFARdVSDRVAFFHQG 212
Cdd:cd03291 176 KDADLYLLDSPFGYLDVFTEKEIFEScvCKLMANK--TRILVTSKMEHLK-KADKILILHEG 234
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
17-209 |
5.16e-10 |
|
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: 56.95 E-value: 5.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 17 LKGIDLTVEKGEVVTIIGGSGSGKSTLltCINGLEPIDSGRIVIDGTdvhakgtdlnrlrrkvgivfqqwNAFPHLTVle 96
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTL--VNEGLYASGKARLISFLP-----------------------KFSRNKLI-- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 97 nvMLAPRKVLglpkdkaeeIAVKqLTHVGLGEKLkvypNRMSGGQQQRMAIARALAMSPEYMLF--DEVTSALDPMLVGE 174
Cdd:cd03238 64 --FIDQLQFL---------IDVG-LGYLTLGQKL----STLSGGELQRVKLASELFSEPPGTLFilDEPSTGLHQQDINQ 127
|
170 180 190
....*....|....*....|....*....|....*
gi 499282096 175 VLDTLKMLAEEGMTMICVTHEMTFArDVSDRVAFF 209
Cdd:cd03238 128 LLEVIKGLIDLGNTVILIEHNLDVL-SSADWIIDF 161
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
2-201 |
1.11e-09 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 57.72 E-value: 1.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 2 IEIENVRKSFSSLEVLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPID-SGRIVIDGTDvHAKGTDLNRLRRKVG 80
Cdd:PRK10938 261 IVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDHPQGySNDLTLFGRR-RGSGETIWDIKKHIG 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 81 IVFQQWnafpHL-----TVLENVMLAP--------RKVlglpKDKAEEIAVKQLTHVGLGEKLKVYPNR-MSGGQQQRMA 146
Cdd:PRK10938 340 YVSSSL----HLdyrvsTSVRNVILSGffdsigiyQAV----SDRQQKLAQQWLDILGIDKRTADAPFHsLSWGQQRLAL 411
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 147 IARALAMSPEYMLFDEVTSALDPM---LVGEVLDtlkMLAEEGMTMI------------CVTHEMTFARD 201
Cdd:PRK10938 412 IVRALVKHPTLLILDEPLQGLDPLnrqLVRRFVD---VLISEGETQLlfvshhaedapaCITHRLEFVPD 478
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
2-60 |
1.81e-09 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 57.05 E-value: 1.81e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 499282096 2 IEIENVRKSFSSLEVLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVI 60
Cdd:PRK11819 325 IEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI 383
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
13-239 |
2.44e-09 |
|
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: 55.88 E-value: 2.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 13 SLEVLKGidlTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGTDVHAK---------GTDLNRLRRKVGIVF 83
Cdd:cd03237 14 TLEVEGG---SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSYKpqyikadyeGTVRDLLSSITKDFY 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 84 Q--QWNAfphltvleNVMlaprKVLGLpkdkaEEIAVKQLthvglgeklkvypNRMSGGQQQRMAIARALAMSPEYMLFD 161
Cdd:cd03237 91 ThpYFKT--------EIA----KPLQI-----EQILDREV-------------PELSGGELQRVAIAACLSKDADIYLLD 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 162 EVTSALDP---MLVGEVLDTLKMLAEEgmTMICVTHEMTFARDVSDRVAFFhQGIMAE--IGSPDQIFASPQNpetqKFL 236
Cdd:cd03237 141 EPSAYLDVeqrLMASKVIRRFAENNEK--TAFVVEHDIIMIDYLADRLIVF-EGEPSVngVANPPQSLRSGMN----RFL 213
|
...
gi 499282096 237 ASV 239
Cdd:cd03237 214 KNL 216
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
16-239 |
5.57e-09 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 55.89 E-value: 5.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 16 VLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCI----NGLEPIDSGRIVIDGTDVHakgtDL-NRLRRKVGIVFQQWNAFP 90
Cdd:TIGR00956 76 ILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIasntDGFHIGVEGVITYDGITPE----EIkKHYRGDVVYNAETDVHFP 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 91 HLTVLENVMLAPR------KVLGLPKDK-AEEIAVKQLTHVGLGE-KLKVYPNRM----SGGQQQRMAIARALAMSPEYM 158
Cdd:TIGR00956 152 HLTVGETLDFAARcktpqnRPDGVSREEyAKHIADVYMATYGLSHtRNTKVGNDFvrgvSGGERKRVSIAEASLGGAKIQ 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 159 LFDEVTSALDPMLVGEVLDTLKMLAEEGMTMICVT----HEMTFarDVSDRVAFFHQGIMAEIGSPDQI--------FAS 226
Cdd:TIGR00956 232 CWDNATRGLDSATALEFIRALKTSANILDTTPLVAiyqcSQDAY--ELFDKVIVLYEGYQIYFGPADKAkqyfekmgFKC 309
|
250
....*....|...
gi 499282096 227 PQNPETQKFLASV 239
Cdd:TIGR00956 310 PDRQTTADFLTSL 322
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
1-194 |
7.42e-09 |
|
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: 55.53 E-value: 7.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 1 MIEIENVRKSFSSLEVL-KGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDgtdvhAKGtdlnrlrrKV 79
Cdd:TIGR00954 451 GIKFENIPLVTPNGDVLiESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKP-----AKG--------KL 517
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 80 GIVFQQwnafPHLTV--LENVMLAPRKVL-----GLPKDKAEEIAVK-QLTHV----GLGEKLKVYPNRMSGGQQQRMAI 147
Cdd:TIGR00954 518 FYVPQR----PYMTLgtLRDQIIYPDSSEdmkrrGLSDKDLEQILDNvQLTHIlereGGWSAVQDWMDVLSGGEKQRIAM 593
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 499282096 148 ARALAMSPEYMLFDEVTSALDPmlvgEVLDTLKMLAEE-GMTMICVTH 194
Cdd:TIGR00954 594 ARLFYHKPQFAILDECTSAVSV----DVEGYMYRLCREfGITLFSVSH 637
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
16-196 |
8.50e-09 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 54.48 E-value: 8.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 16 VLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDsGRIVIDGtdVHAKGTDLNRLRRKVGIVFQQWNAFPHlTVL 95
Cdd:cd03289 19 VLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GDIQIDG--VSWNSVPLQKWRKAFGVIPQKVFIFSG-TFR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 96 ENvmLAPRKvlglpKDKAEEIaVKQLTHVGLGEKLKVYPNR-----------MSGGQQQRMAIARALAMSPEYMLFDEVT 164
Cdd:cd03289 95 KN--LDPYG-----KWSDEEI-WKVAEEVGLKSVIEQFPGQldfvlvdggcvLSHGHKQLMCLARSVLSKAKILLLDEPS 166
|
170 180 190
....*....|....*....|....*....|..
gi 499282096 165 SALDPMLVGEVLDTLKMlAEEGMTMICVTHEM 196
Cdd:cd03289 167 AHLDPITYQVIRKTLKQ-AFADCTVILSEHRI 197
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
26-211 |
4.71e-08 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 50.83 E-value: 4.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 26 KGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGTDVHAKGTDLNRLRRKVGIvfqqwnafphltvlenvmlaprkv 105
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGG------------------------ 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 106 lglpkdkaeeiavkqlthvglgeklkvYPNRMSGGQQQRMAIARALAMSPEYMLFDEVTSALDPMLVGEVLD------TL 179
Cdd:smart00382 57 ---------------------------KKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLleelrlLL 109
|
170 180 190
....*....|....*....|....*....|..
gi 499282096 180 KMLAEEGMTMICVTHEMTFARDVSDRVAFFHQ 211
Cdd:smart00382 110 LLKSEKNLTVILTTNDEKDLGPALLRRRFDRR 141
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
23-197 |
5.54e-08 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 52.86 E-value: 5.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 23 TVEKGEVVTIIGGSGSGKSTLLTcinglepIDSGRIVIDGTDVHAKGTDLNRLRRKVGIVFQQwnafpHLTVLEN----- 97
Cdd:COG1245 95 VPKKGKVTGILGPNGIGKSTALK-------ILSGELKPNLGDYDEEPSWDEVLKRFRGTELQD-----YFKKLANgeikv 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 98 ------VMLAPRKVLGLPKD---------KAEEIaVKQLthvGLGEKLKVYPNRMSGGQQQRMAIARALAMSPEYMLFDE 162
Cdd:COG1245 163 ahkpqyVDLIPKVFKGTVREllekvdergKLDEL-AEKL---GLENILDRDISELSGGELQRVAIAAALLRDADFYFFDE 238
|
170 180 190
....*....|....*....|....*....|....*...
gi 499282096 163 VTSALDpmlVGE---VLDTLKMLAEEGMTMICVTHEMT 197
Cdd:COG1245 239 PSSYLD---IYQrlnVARLIRELAEEGKYVLVVEHDLA 273
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
15-196 |
7.58e-08 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 52.47 E-value: 7.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 15 EVLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDgtdvhakgtdlnrlrRKVGIVFQQ-W--NAfph 91
Cdd:PTZ00243 674 VLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAE---------------RSIAYVPQQaWimNA--- 735
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 92 lTVLENVMLAPRKVlglPKDKAEEIAVKQLT----------HVGLGEKlkvyPNRMSGGQQQRMAIARALAMSPEYMLFD 161
Cdd:PTZ00243 736 -TVRGNILFFDEED---AARLADAVRVSQLEadlaqlggglETEIGEK----GVNLSGGQKARVSLARAVYANRDVYLLD 807
|
170 180 190
....*....|....*....|....*....|....*.
gi 499282096 162 EVTSALDPMlVGE-VLDTLKMLAEEGMTMICVTHEM 196
Cdd:PTZ00243 808 DPLSALDAH-VGErVVEECFLGALAGKTRVLATHQV 842
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
3-198 |
1.23e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 51.87 E-value: 1.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 3 EIENVRKSFSSLEVLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCING-LEPiDSGRIVIdgtdvhakGTDLnrlrrKVGi 81
Cdd:PRK11147 321 EMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGqLQA-DSGRIHC--------GTKL-----EVA- 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 82 VFQQWNAF--PHLTVLEN-------VML--APRKVLGLPKD-----KAEEIAVKQLthvglgeklkvypnrmSGGQQQRM 145
Cdd:PRK11147 386 YFDQHRAEldPEKTVMDNlaegkqeVMVngRPRHVLGYLQDflfhpKRAMTPVKAL----------------SGGERNRL 449
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 499282096 146 AIARALAMSPEYMLFDEVTSALDPmlvgEVLDTLK-MLAEEGMTMICVTHEMTF 198
Cdd:PRK11147 450 LLARLFLKPSNLLILDEPTNDLDV----ETLELLEeLLDSYQGTVLLVSHDRQF 499
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
1-209 |
1.36e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 51.73 E-value: 1.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 1 MIEIENVRKSFS--SLEVLKGidlTVEKGEVVTIIGGSGSGKSTLLTCING-LEPiDSGRIVIDgtdvhakgtdlnrlrr 77
Cdd:PRK13409 340 LVEYPDLTKKLGdfSLEVEGG---EIYEGEVIGIVGPNGIGKTTFAKLLAGvLKP-DEGEVDPE---------------- 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 78 kVGIVF--QQWNAFPHLTVLENVMLAPRKVLGLPKDkaEEIaVKQLthvGLGEKLKVYPNRMSGGQQQRMAIARALAMSP 155
Cdd:PRK13409 400 -LKISYkpQYIKPDYDGTVEDLLRSITDDLGSSYYK--SEI-IKPL---QLERLLDKNVKDLSGGELQRVAIAACLSRDA 472
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 499282096 156 EYMLFDEVTSALDpmlVGE---VLDTLKMLAEE-GMTMICVTHEMTFARDVSDRVAFF 209
Cdd:PRK13409 473 DLYLLDEPSAHLD---VEQrlaVAKAIRRIAEErEATALVVDHDIYMIDYISDRLMVF 527
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
15-194 |
1.95e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 51.27 E-value: 1.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 15 EVLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPidsgriVIDGTDVHAKGTdlnrlrrKVGIVFQQwnafPHL-- 92
Cdd:PRK11819 21 QILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDK------EFEGEARPAPGI-------KVGYLPQE----PQLdp 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 93 --TVLENVMLAPRKVLGLpKDKAEEIAVK--------------------QLTHVGLGE---KL--------------KVy 133
Cdd:PRK11819 84 ekTVRENVEEGVAEVKAA-LDRFNEIYAAyaepdadfdalaaeqgelqeIIDAADAWDldsQLeiamdalrcppwdaKV- 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499282096 134 pNRMSGGQQQRMAIARALAMSPEYMLFDEVTSALDpmlvGEVLDTL-KMLAEEGMTMICVTH 194
Cdd:PRK11819 162 -TKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLD----AESVAWLeQFLHDYPGTVVAVTH 218
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
1-195 |
5.68e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 48.41 E-value: 5.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 1 MIEIENVRKSFSSLEVLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGTDVHakgTDLNRLRRKVG 80
Cdd:PRK13540 1 MLDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIK---KDLCTYQKQLC 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 81 IVFQQWNAFPHLTVLENVMLAPRKVLGlpkdkaeEIAVKQLTHVGLGEKLKVYP-NRMSGGQQQRMAIARALAMSPEYML 159
Cdd:PRK13540 78 FVGHRSGINPYLTLRENCLYDIHFSPG-------AVGITELCRLFSLEHLIDYPcGLLSSGQKRQVALLRLWMSKAKLWL 150
|
170 180 190
....*....|....*....|....*....|....*.
gi 499282096 160 FDEVTSALDPMLVGEVLDTLKMLAEEGMTMICVTHE 195
Cdd:PRK13540 151 LDEPLVALDELSLLTIITKIQEHRAKGGAVLLTSHQ 186
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
2-169 |
2.96e-06 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 47.81 E-value: 2.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 2 IEIENVRKSFSSLEVLKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGTDVHAKgtdlnRLRRKVG- 80
Cdd:NF033858 2 ARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMADA-----RHRRAVCp 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 81 -IVFQ-QW---NAFPHLTVLENVMLAPRkVLGLpkDKAE-EIAVKQLTH-VGLGEklkvYPNR----MSGGQQQRMAIAR 149
Cdd:NF033858 77 rIAYMpQGlgkNLYPTLSVFENLDFFGR-LFGQ--DAAErRRRIDELLRaTGLAP----FADRpagkLSGGMKQKLGLCC 149
|
170 180
....*....|....*....|
gi 499282096 150 ALAMSPEYMLFDEVTSALDP 169
Cdd:NF033858 150 ALIHDPDLLILDEPTTGVDP 169
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
17-195 |
3.21e-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: 46.48 E-value: 3.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 17 LKGIDLTVEKGEVVTIIGGSGSGKSTL--------------------------------LTCINGLEPIdsgrIVIDgtd 64
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSSLafdtiyaegqrryveslsayarqflgqmdkpdVDSIEGLSPA----IAID--- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 65 vhAKGTDLNRlRRKVGIVFQQWNafpHLTVL-ENVMLAPRkvlglpkdkaeeiaVKQLTHVGLGEklkVYPNR----MSG 139
Cdd:cd03270 84 --QKTTSRNP-RSTVGTVTEIYD---YLRLLfARVGIRER--------------LGFLVDVGLGY---LTLSRsaptLSG 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 499282096 140 GQQQRMAIARALAMSPEYML--FDEVTSALDPMLVGEVLDTLKMLAEEGMTMICVTHE 195
Cdd:cd03270 141 GEAQRIRLATQIGSGLTGVLyvLDEPSIGLHPRDNDRLIETLKRLRDLGNTVLVVEHD 198
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
23-197 |
3.25e-06 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 47.50 E-value: 3.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 23 TVEKGEVVTIIGGSGSGKSTLLTcinglepIDSGRIVIDGTDVHAKGTDLNRLRRKVGIVFQQwnafpHLTVLEN----- 97
Cdd:PRK13409 95 IPKEGKVTGILGPNGIGKTTAVK-------ILSGELIPNLGDYEEEPSWDEVLKRFRGTELQN-----YFKKLYNgeikv 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 98 ------VMLAPRKVLGLPKD---------KAEEIaVKQLthvGLGEKLKVYPNRMSGGQQQRMAIARALAMSPEYMLFDE 162
Cdd:PRK13409 163 vhkpqyVDLIPKVFKGKVREllkkvdergKLDEV-VERL---GLENILDRDISELSGGELQRVAIAAALLRDADFYFFDE 238
|
170 180 190
....*....|....*....|....*....|....*..
gi 499282096 163 VTSALDpmlVGEVLDTLKMLAE--EGMTMICVTHEMT 197
Cdd:PRK13409 239 PTSYLD---IRQRLNVARLIRElaEGKYVLVVEHDLA 272
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
23-206 |
4.32e-06 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 46.59 E-value: 4.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 23 TVEKGEVVTIIGGSGSGKSTLLTCING-LEP-------IDSGRIVID---GTDVHAKGTDLNRLRRKVGIVFQqwnafph 91
Cdd:cd03236 22 VPREGQVLGLVGPNGIGKSTALKILAGkLKPnlgkfddPPDWDEILDefrGSELQNYFTKLLEGDVKVIVKPQ------- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 92 ltvleNVMLAPR----KVLGLPKDKAE----EIAVKQLthvGLGEKLKVYPNRMSGGQQQRMAIARALAMSPEYMLFDEV 163
Cdd:cd03236 95 -----YVDLIPKavkgKVGELLKKKDErgklDELVDQL---ELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEP 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 499282096 164 TSALDpmlVGEVLD---TLKMLAEEGMTMICVTHEMTFARDVSDRV 206
Cdd:cd03236 167 SSYLD---IKQRLNaarLIRELAEDDNYVLVVEHDLAVLDYLSDYI 209
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
2-209 |
4.76e-06 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 47.09 E-value: 4.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 2 IEIENVRKSFS--SLEVLKGidlTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGriVIDGtdvhakgtdlnrlrrKV 79
Cdd:COG1245 342 VEYPDLTKSYGgfSLEVEGG---EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEG--EVDE---------------DL 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 80 GIVF--QQWNAFPHLTVLENVMLAPRKVLGLPKDKaEEIaVKQLthvGLGEKLKVYPNRMSGGQQQRMAIARALAMSPEY 157
Cdd:COG1245 402 KISYkpQYISPDYDGTVEEFLRSANTDDFGSSYYK-TEI-IKPL---GLEKLLDKNVKDLSGGELQRVAIAACLSRDADL 476
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 499282096 158 MLFDEVTSALD---PMLVGEVldtLKMLAEE-GMTMICVTHEMTFARDVSDRVAFF 209
Cdd:COG1245 477 YLLDEPSAHLDveqRLAVAKA---IRRFAENrGKTAMVVDHDIYLIDYISDRLMVF 529
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
17-217 |
1.22e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 45.49 E-value: 1.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 17 LKGIDLTVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGTDVHAKGTD---------LNRLRRKVGIvfqqwn 87
Cdd:PRK10982 264 IRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANeainhgfalVTEERRSTGI------ 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 88 aFPHLTVLENVMLAPRKV----LGLPKDKA---------EEIAVK---QLTHVGlgeklkvypnRMSGGQQQRMAIARAL 151
Cdd:PRK10982 338 -YAYLDIGFNSLISNIRNyknkVGLLDNSRmksdtqwviDSMRVKtpgHRTQIG----------SLSGGNQQKVIIGRWL 406
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499282096 152 AMSPEYMLFDEVTSALDPMLVGEVLDTLKMLAEEGMTMICVTHEMTFARDVSDRVAFFHQGIMAEI 217
Cdd:PRK10982 407 LTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNGLVAGI 472
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
24-210 |
3.90e-05 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 42.94 E-value: 3.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 24 VEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGTDVHAKgtdlnrlrrkvgivfqqwnafphltvlenvmlaPR 103
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITPVYK---------------------------------PQ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 104 KVlglpkdkaeeiavkqlthvglgeklkvypnRMSGGQQQRMAIARALAMSPEYMLFDEVTSALDPMLVGEVLDTLKMLA 183
Cdd:cd03222 69 YI------------------------------DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLS 118
|
170 180
....*....|....*....|....*...
gi 499282096 184 EEGM-TMICVTHEMTFARDVSDRVAFFH 210
Cdd:cd03222 119 EEGKkTALVVEHDLAVLDYLSDRIHVFE 146
|
|
| ABC_SMC3_euk |
cd03272 |
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ... |
118-193 |
1.73e-04 |
|
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: 41.48 E-value: 1.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 118 VKQLTHVGLGEKLKVypNRMSGGQQQRMAIARALAM-----SPEYmLFDEVTSALDPMLVGEVLDTLKMLAeEGMTMICV 192
Cdd:cd03272 142 INSLTNMKQDEQQEM--QQLSGGQKSLVALALIFAIqkcdpAPFY-LFDEIDAALDAQYRTAVANMIKELS-DGAQFITT 217
|
.
gi 499282096 193 T 193
Cdd:cd03272 218 T 218
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
11-216 |
1.87e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 42.08 E-value: 1.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 11 FSSLEVLKGIDL-------TVEKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRIVIDGT-------------DVHAKG- 69
Cdd:PRK10636 4 FSSLQIRRGVRVlldnataTINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNwqlawvnqetpalPQPALEy 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 70 -TDLNRLRRKVGIVFQQWNAfphltvlENVMLAPRKVLG-LPKDKAEEIAVK--QLTHvGLG---EKLKVYPNRMSGGQQ 142
Cdd:PRK10636 84 vIDGDREYRQLEAQLHDANE-------RNDGHAIATIHGkLDAIDAWTIRSRaaSLLH-GLGfsnEQLERPVSDFSGGWR 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499282096 143 QRMAIARALAMSPEYMLFDEVTSALDpmlvgevLDTL----KMLAEEGMTMICVTHEMTFARDVSDRVAFFHQGIMAE 216
Cdd:PRK10636 156 MRLNLAQALICRSDLLLLDEPTNHLD-------LDAViwleKWLKSYQGTLILISHDRDFLDPIVDKIIHIEQQSLFE 226
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
2-78 |
5.07e-04 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 39.79 E-value: 5.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 2 IEIENVRkSFSSLEvlkgIDLtvEKGevVTIIGG-SGSGKSTLLTCI--------NGLEPIDSGRIVIDGTDVHAKGTDL 72
Cdd:pfam13476 1 LTIENFR-SFRDQT----IDF--SKG--LTLITGpNGSGKTTILDAIklalygktSRLKRKSGGGFVKGDIRIGLEGKGK 71
|
....*.
gi 499282096 73 NRLRRK 78
Cdd:pfam13476 72 AYVEIT 77
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
2-183 |
5.21e-04 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 39.99 E-value: 5.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 2 IEIENVRkSFSSLEVlkgIDLTvekGEVVTIIGGSGSGKSTLLTCIN---GLEPIDSGRIVIDGTDVHAKGT--DLN--- 73
Cdd:COG0419 5 LRLENFR-SYRDTET---IDFD---DGLNLIVGPNGAGKSTILEAIRyalYGKARSRSKLRSDLINVGSEEAsvELEfeh 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 74 -----RLRRKVGIVFQQWNAFP-----------HLTVLENVMLAPRKVLGLPKDKAEEIAVKQLTHVGLGEKLKVY--PN 135
Cdd:COG0419 78 ggkryRIERRQGEFAEFLEAKPserkealkrllGLEIYEELKERLKELEEALESALEELAELQKLKQEILAQLSGLdpIE 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 499282096 136 RMSGGQQQRMAIARALAmspeyMLFDevTSALDPMLVGEVLDTLKMLA 183
Cdd:COG0419 158 TLSGGERLRLALADLLS-----LILD--FGSLDEERLERLLDALEELA 198
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
137-213 |
7.63e-04 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 40.34 E-value: 7.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 137 MSGGQQQRMAIARALAM-----SPEYmLFDEVTSALDPMLVGEVLDTLKMLAEEgMTMICVTH--EMTFARDVSDRVAFF 209
Cdd:pfam02463 1078 LSGGEKTLVALALIFAIqkykpAPFY-LLDEIDAALDDQNVSRVANLLKELSKN-AQFIVISLreEMLEKADKLVGVTMV 1155
|
....
gi 499282096 210 HQGI 213
Cdd:pfam02463 1156 ENGV 1159
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
17-43 |
8.75e-04 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 40.01 E-value: 8.75e-04
10 20
....*....|....*....|....*..
gi 499282096 17 LKGIDLTVEKGEVVTIIGGSGSGKSTL 43
Cdd:COG0178 16 LKNIDVDIPRNKLVVITGLSGSGKSSL 42
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
136-199 |
1.23e-03 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 38.49 E-value: 1.23e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499282096 136 RMSGGQQQRMAIARALAM-----SPEYmLFDEVTSALDPMLVGEVLDTLKMLAEEGMTMICVTHEMTFA 199
Cdd:cd03227 77 QLSGGEKELSALALILALaslkpRPLY-ILDEIDRGLDPRDGQALAEAILEHLVKGAQVIVITHLPELA 144
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
135-202 |
1.66e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 39.46 E-value: 1.66e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499282096 135 NRMSGGQQQRMAIARALAMSPEYMLFDEVTSALDpmlVGEVLDTLKMLAEEGMTMICVTHEMTFARDV 202
Cdd:PLN03073 343 KTFSGGWRMRIALARALFIEPDLLLLDEPTNHLD---LHAVLWLETYLLKWPKTFIVVSHAREFLNTV 407
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
134-206 |
1.70e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 39.43 E-value: 1.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 134 PNR----MSGGQQQRMAIARALA---MSPEYMLfDEVTSALDPMLVGEVLDTLKMLAEEGMTMICVTHE---MTFArdvs 203
Cdd:PRK00635 470 PERalatLSGGEQERTALAKHLGaelIGITYIL-DEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEHDeqmISLA---- 544
|
...
gi 499282096 204 DRV 206
Cdd:PRK00635 545 DRI 547
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
30-168 |
1.84e-03 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 38.31 E-value: 1.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 30 VTII-GGSGSGKSTLLTCINGLEPIDSGRIVIdgtdvhaKGTDLNRLRRK-VGIVFQQWNAFPHLTVLENVmlaprKVLG 107
Cdd:PRK13541 28 ITYIkGANGCGKSSLLRMIAGIMQPSSGNIYY-------KNCNINNIAKPyCTYIGHNLGLKLEMTVFENL-----KFWS 95
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499282096 108 LPKDKAEEIAVKqLTHVGLGEKL--KVYpnRMSGGQQQRMAIARALAMSPEYMLFDEVTSALD 168
Cdd:PRK13541 96 EIYNSAETLYAA-IHYFKLHDLLdeKCY--SLSSGMQKIVAIARLIACQSDLWLLDEVETNLS 155
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
103-194 |
3.39e-03 |
|
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: 38.14 E-value: 3.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 103 RKVLGLPKDKAEEIAVKQLTHVGLGEKLKVYPNRMSGGQQQ---RMAIARALAMSPEYMLFDEVTSALDPMLVGEVLDTL 179
Cdd:pfam13304 203 GEGIEKSLLVDDRLRERGLILLENGGGGELPAFELSDGTKRllaLLAALLSALPKGGLLLIDEPESGLHPKLLRRLLELL 282
|
90
....*....|....*
gi 499282096 180 KMLAEEGMTMICVTH 194
Cdd:pfam13304 283 KELSRNGAQLILTTH 297
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
2-48 |
3.49e-03 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 37.67 E-value: 3.49e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 499282096 2 IEIENVRkSFSSLEvlkgIDLTVEKGevVTIIGGS-GSGKSTLLTCIN 48
Cdd:COG3950 6 LTIENFR-GFEDLE----IDFDNPPR--LTVLVGEnGSGKTTLLEAIA 46
|
|
| NACHT |
COG5635 |
Predicted NTPase, NACHT family domain [Signal transduction mechanisms]; |
6-44 |
4.09e-03 |
|
Predicted NTPase, NACHT family domain [Signal transduction mechanisms];
Pssm-ID: 444362 [Multi-domain] Cd Length: 935 Bit Score: 38.25 E-value: 4.09e-03
10 20 30
....*....|....*....|....*....|....*....
gi 499282096 6 NVRKSFSSLEVLKGIDLtveKGEVVTIIGGSGSGKSTLL 44
Cdd:COG5635 162 NLLERIESLKRLELLEA---KKKRLLILGEPGSGKTTLL 197
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
17-43 |
4.63e-03 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 37.74 E-value: 4.63e-03
10 20
....*....|....*....|....*..
gi 499282096 17 LKGIDLTVEKGEVVTIIGGSGSGKSTL 43
Cdd:PRK00349 16 LKNIDLDIPRDKLVVFTGLSGSGKSSL 42
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
2-203 |
4.93e-03 |
|
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: 37.67 E-value: 4.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 2 IEIENVRkSFSSLEvlkgIDLtveKGEVVTIIGGSGSGKSTLLTCINGLEPIDSGRiVIDGTDVHaKGTDLNRLRRKVGI 81
Cdd:COG3593 6 IKIKNFR-SIKDLS----IEL---SDDLTVLVGENNSGKSSILEALRLLLGPSSSR-KFDEEDFY-LGDDPDLPEIEIEL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 82 VFQQW-----NAFPHLTVLENVMLAPRKV-----------------------------LGLPKDKAEEIAvkQLTHVGLG 127
Cdd:COG3593 76 TFGSLlsrllRLLLKEEDKEELEEALEELneelkealkalnellseylkelldgldleLELSLDELEDLL--KSLSLRIE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 128 EKLKVYPNRMSGGQQQR--MAIARALA---MSPEY--MLFDEVTSALDPMLVGEVLDTLKMLAEEGMTMICVTHEMTFAR 200
Cdd:COG3593 154 DGKELPLDRLGSGFQRLilLALLSALAelkRAPANpiLLIEEPEAHLHPQAQRRLLKLLKELSEKPNQVIITTHSPHLLS 233
|
...
gi 499282096 201 DVS 203
Cdd:COG3593 234 EVP 236
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
17-196 |
5.94e-03 |
|
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: 37.21 E-value: 5.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 17 LKGIDLTVEKGEVVTIIGGSGSGKSTLL----------------------TCINGLEPIDSgRIVIDGTDV--------- 65
Cdd:cd03271 11 LKNIDVDIPLGVLTCVTGVSGSGKSSLIndtlypalarrlhlkkeqpgnhDRIEGLEHIDK-VIVIDQSPIgrtprsnpa 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 66 ---------------HAKGTDLNRLRRKVgivfqqwnAFPHLTVLEnvmlaprkVLGLPKDKAEE-------IAVK-QLT 122
Cdd:cd03271 90 tytgvfdeirelfceVCKGKRYNRETLEV--------RYKGKSIAD--------VLDMTVEEALEffenipkIARKlQTL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499282096 123 H-VGLGE-KLKVYPNRMSGGQQQRMAIARALAMSPE----YMLfDEVTSALDPMLVGEVLDTLKMLAEEGMTMICVTHEM 196
Cdd:cd03271 154 CdVGLGYiKLGQPATTLSGGEAQRIKLAKELSKRSTgktlYIL-DEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIEHNL 232
|
|
| fliI |
PRK07721 |
flagellar protein export ATPase FliI; |
14-47 |
6.73e-03 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181092 [Multi-domain] Cd Length: 438 Bit Score: 37.39 E-value: 6.73e-03
10 20 30
....*....|....*....|....*....|....*..
gi 499282096 14 LEV-LKGID--LTVEKGEVVTIIGGSGSGKSTLLTCI 47
Cdd:PRK07721 142 MEVgVRAIDslLTVGKGQRVGIFAGSGVGKSTLMGMI 178
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
17-44 |
8.39e-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: 37.30 E-value: 8.39e-03
10 20
....*....|....*....|....*...
gi 499282096 17 LKGIDLTVEKGEVVTIIGGSGSGKSTLL 44
Cdd:TIGR00630 624 LKNITVSIPLGLFTCITGVSGSGKSTLI 651
|
|
| |
