|
Name |
Accession |
Description |
Interval |
E-value |
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
4-241 |
5.96e-167 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 460.23 E-value: 5.96e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 4 MIEIKHLNKYFGDLHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPLT-KKNHLEMARKYSS 82
Cdd:COG1126 1 MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTdSKKDINKLRRKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 83 MVFQQFNLYPNMTVLGNLTLAPIKLQKKSKEEATEIAIAALKRVGMAHKAGEYPQNLSGGQQQRIAIARALCTKQPIILF 162
Cdd:COG1126 81 MVFQQFNLFPHLTVLENVTLAPIKVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKVMLF 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1469315281 163 DEPTSALDPEMVQEVLDVMIELAQEDITMICVTHEMGFARQVADRVIFMEDGRILEEGTPEHFFDNPENPRCREFLSKI 241
Cdd:COG1126 161 DEPTSALDPELVGEVLDVMRDLAKEGMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFENPQHERTRAFLSKV 239
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
5-216 |
8.40e-136 |
|
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: 380.34 E-value: 8.40e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 5 IEIKHLNKYFGDLHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPLTK-KNHLEMARKYSSM 83
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDdKKNINELRQKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 84 VFQQFNLYPNMTVLGNLTLAPIKLQKKSKEEATEIAIAALKRVGMAHKAGEYPQNLSGGQQQRIAIARALCTKQPIILFD 163
Cdd:cd03262 81 VFQQFNLFPHLTVLENITLAPIKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1469315281 164 EPTSALDPEMVQEVLDVMIELAQEDITMICVTHEMGFARQVADRVIFMEDGRI 216
Cdd:cd03262 161 EPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
2-243 |
1.46e-117 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 336.00 E-value: 1.46e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 2 ADMIEIKHLNKYFGDLHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPL----TKKNHLEMA 77
Cdd:COG4598 6 PPALEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIrlkpDRDGELVPA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 78 --------RKYSSMVFQQFNLYPNMTVLGNLTLAPIKLQKKSKEEATEIAIAALKRVGMAHKAGEYPQNLSGGQQQRIAI 149
Cdd:COG4598 86 drrqlqriRTRLGMVFQSFNLWSHMTVLENVIEAPVHVLGRPKAEAIERAEALLAKVGLADKRDAYPAHLSGGQQQRAAI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 150 ARALCTKQPIILFDEPTSALDPEMVQEVLDVMIELAQEDITMICVTHEMGFARQVADRVIFMEDGRILEEGTPEHFFDNP 229
Cdd:COG4598 166 ARALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEEGRTMLVVTHEMGFARDVSSHVVFLHQGRIEEQGPPAEVFGNP 245
|
250
....*....|....
gi 1469315281 230 ENPRCREFLSKILH 243
Cdd:COG4598 246 KSERLRQFLSSSLK 259
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
4-238 |
1.42e-111 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 320.12 E-value: 1.42e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 4 MIEIKHLNKYFGDLHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPLTKKNHLE-MARKYSS 82
Cdd:PRK09493 1 MIEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDErLIRQEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 83 MVFQQFNLYPNMTVLGNLTLAPIKLQKKSKEEATEIAIAALKRVGMAHKAGEYPQNLSGGQQQRIAIARALCTKQPIILF 162
Cdd:PRK09493 81 MVFQQFYLFPHLTALENVMFGPLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLF 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1469315281 163 DEPTSALDPEMVQEVLDVMIELAQEDITMICVTHEMGFARQVADRVIFMEDGRILEEGTPEHFFDNPENPRCREFL 238
Cdd:PRK09493 161 DEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPPSQRLQEFL 236
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
4-242 |
5.05e-94 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 276.25 E-value: 5.05e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 4 MIEIKHLNKYFGDLHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSG-----EVLIDGT-PLTK-KNHLEM 76
Cdd:PRK11264 3 AIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGtirvgDITIDTArSLSQqKGLIRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 77 ARKYSSMVFQQFNLYPNMTVLGNLTLAPIKLQKKSKEEATEIAIAALKRVGMAHKAGEYPQNLSGGQQQRIAIARALCTK 156
Cdd:PRK11264 83 LRQHVGFVFQNFNLFPHRTVLENIIEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 157 QPIILFDEPTSALDPEMVQEVLDVMIELAQEDITMICVTHEMGFARQVADRVIFMEDGRILEEGTPEHFFDNPENPRCRE 236
Cdd:PRK11264 163 PEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADPQQPRTRQ 242
|
....*.
gi 1469315281 237 FLSKIL 242
Cdd:PRK11264 243 FLEKFL 248
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
4-243 |
6.69e-94 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 278.88 E-value: 6.69e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 4 MIEIKHLNKYF----GDLHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPLTK--KNHLEMA 77
Cdd:COG1135 1 MIELENLSKTFptkgGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTAlsERELRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 78 RKYSSMVFQQFNLYPNMTVLGNLTLaPIKLQKKSKEEATEIAIAALKRVGMAHKAGEYPQNLSGGQQQRIAIARALCTKQ 157
Cdd:COG1135 81 RRKIGMIFQHFNLLSSRTVAENVAL-PLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 158 PIILFDEPTSALDPEMVQEVLDVMIELAQE-DITMICVTHEMGFARQVADRVIFMEDGRILEEGTPEHFFDNPENPRCRE 236
Cdd:COG1135 160 KVLLCDEATSALDPETTRSILDLLKDINRElGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVLDVFANPQSELTRR 239
|
....*..
gi 1469315281 237 FLSKILH 243
Cdd:COG1135 240 FLPTVLN 246
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
5-239 |
1.19e-91 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 269.58 E-value: 1.19e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 5 IEIKHLNKYFGDLHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDG------TPLTKKNHLEMAR 78
Cdd:COG4161 3 IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGhqfdfsQKPSEKAIRLLRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 79 KYSsMVFQQFNLYPNMTVLGNLTLAPIKLQKKSKEEATEIAIAALKRVGMAHKAGEYPQNLSGGQQQRIAIARALCTKQP 158
Cdd:COG4161 83 KVG-MVFQQYNLWPHLTVMENLIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 159 IILFDEPTSALDPEMVQEVLDVMIELAQEDITMICVTHEMGFARQVADRVIFMEDGRILEEGTPEHfFDNPENPRCREFL 238
Cdd:COG4161 162 VLLFDEPTAALDPEITAQVVEIIRELSQTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQGDASH-FTQPQTEAFAHYL 240
|
.
gi 1469315281 239 S 239
Cdd:COG4161 241 S 241
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
5-239 |
4.53e-90 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 265.72 E-value: 4.53e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 5 IEIKHLNKYFGDLHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDG------TPLTKKNHLEMAR 78
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGnhfdfsKTPSDKAIRELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 79 KYSsMVFQQFNLYPNMTVLGNLTLAPIKLQKKSKEEATEIAIAALKRVGMAHKAGEYPQNLSGGQQQRIAIARALCTKQP 158
Cdd:PRK11124 83 NVG-MVFQQYNLWPHLTVQQNLIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 159 IILFDEPTSALDPEMVQEVLDVMIELAQEDITMICVTHEMGFARQVADRVIFMEDGRILEEGTPEHfFDNPENPRCREFL 238
Cdd:PRK11124 162 VLLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTHEVEVARKTASRVVYMENGHIVEQGDASC-FTQPQTEAFKNYL 240
|
.
gi 1469315281 239 S 239
Cdd:PRK11124 241 S 241
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-219 |
1.32e-89 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 263.83 E-value: 1.32e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 1 MADMIEIKHLNKYFGD----LHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPLTKKNHLEM 76
Cdd:COG1136 1 MSPLLELRNLTKSYGTgegeVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSEREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 77 A---RKYSSMVFQQFNLYPNMTVLGNLTLaPIKLQKKSKEEATEIAIAALKRVGMAHKAGEYPQNLSGGQQQRIAIARAL 153
Cdd:COG1136 81 ArlrRRHIGFVFQFFNLLPELTALENVAL-PLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARAL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1469315281 154 CTKQPIILFDEPTSALDPEMVQEVLDVMIELAQE-DITMICVTHEMGFARQvADRVIFMEDGRILEE 219
Cdd:COG1136 160 VNRPKLILADEPTGNLDSKTGEEVLELLRELNRElGTTIVMVTHDPELAAR-ADRVIRLRDGRIVSD 225
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
4-230 |
2.23e-88 |
|
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: 260.98 E-value: 2.23e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 4 MIEIKHLNKYFGD----LHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPLTKKNHLEM--A 77
Cdd:cd03258 1 MIELKNVSKVFGDtggkVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELrkA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 78 RKYSSMVFQQFNLYPNMTVLGNLTLaPIKLQKKSKEEATEIAIAALKRVGMAHKAGEYPQNLSGGQQQRIAIARALCTKQ 157
Cdd:cd03258 81 RRRIGMIFQHFNLLSSRTVFENVAL-PLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNP 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1469315281 158 PIILFDEPTSALDPEMVQEVLDVMIELAQE-DITMICVTHEMGFARQVADRVIFMEDGRILEEGTPEHFFDNPE 230
Cdd:cd03258 160 KVLLCDEATSALDPETTQSILALLRDINRElGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFANPQ 233
|
|
| ectoine_ehuA |
TIGR03005 |
ectoine/hydroxyectoine ABC transporter, ATP-binding protein; Members of this family are the ... |
5-242 |
2.96e-85 |
|
ectoine/hydroxyectoine ABC transporter, ATP-binding protein; Members of this family are the ATP-binding protein of a conserved four gene ABC transporter operon found next to ectoine unilization operons and ectoine biosynthesis operons. Ectoine is a compatible solute that protects enzymes from high osmolarity. It is released by some species in response to hypoosmotic shock, and it is taken up by a number of bacteria as a compatible solute or for consumption. This family shows strong sequence similiarity to a number of amino acid ABC transporter ATP-binding proteins.
Pssm-ID: 132050 [Multi-domain] Cd Length: 252 Bit Score: 253.98 E-value: 2.96e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 5 IEIKHLNKYFGDLHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPLT------------KKN 72
Cdd:TIGR03005 1 VRFSDVTKRFGILTVLDGLNFSVAAGEKVALIGPSGSGKSTILRILMTLEPIDEGQIQVEGEQLYhmpgrngplvpaDEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 73 HLEMARKYSSMVFQQFNLYPNMTVLGNLTLAPIKLQKKSKEEATEIAIAALKRVGMAHKAGEYPQNLSGGQQQRIAIARA 152
Cdd:TIGR03005 81 HLRQMRNKIGMVFQSFNLFPHKTVLDNVTEAPVLVLGMARAEAEKRAMELLDMVGLADKADHMPAQLSGGQQQRVAIARA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 153 LCTKQPIILFDEPTSALDPEMVQEVLDVMIELAQE-DITMICVTHEMGFARQVADRVIFMEDGRILEEGTPEHFFDNPEN 231
Cdd:TIGR03005 161 LAMRPKVMLFDEVTSALDPELVGEVLNVIRRLASEhDLTMLLVTHEMGFAREFADRVCFFDKGRIVEQGKPDEIFRQPKE 240
|
250
....*....|.
gi 1469315281 232 PRCREFLSKIL 242
Cdd:TIGR03005 241 ERTREFLSKVI 251
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-238 |
3.86e-83 |
|
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: 247.97 E-value: 3.86e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 1 MADMIEIKHLNKYFGDLHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPLTK--KNHLEMAR 78
Cdd:COG1127 2 SEPMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGlsEKELYELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 79 KYSSMVFQQFNLYPNMTVLGNLTLAPIKLQKKSKEEATEIAIAALKRVGMAHKAGEYPQNLSGGQQQRIAIARALCTKQP 158
Cdd:COG1127 82 RRIGMLFQGGALFDSLTVFENVAFPLREHTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDPE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 159 IILFDEPTSALDPEMVQEVLDVMIELAQE-DITMICVTHEMGFARQVADRVIFMEDGRILEEGTPEHFFDNpENPRCREF 237
Cdd:COG1127 162 ILLYDEPTAGLDPITSAVIDELIRELRDElGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLAS-DDPWVRQF 240
|
.
gi 1469315281 238 L 238
Cdd:COG1127 241 L 241
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
5-216 |
9.94e-83 |
|
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: 246.25 E-value: 9.94e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 5 IEIKHLNKYFGD----LHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPLTKKNHLEMA--- 77
Cdd:cd03255 1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 78 RKYSSMVFQQFNLYPNMTVLGNLTLaPIKLQKKSKEEATEIAIAALKRVGMAHKAGEYPQNLSGGQQQRIAIARALCTKQ 157
Cdd:cd03255 81 RRHIGFVFQSFNLLPDLTALENVEL-PLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 158 PIILFDEPTSALDPEMVQEVLDVMIELAQED-ITMICVTHEMGFARQvADRVIFMEDGRI 216
Cdd:cd03255 160 KIILADEPTGNLDSETGKEVMELLRELNKEAgTTIVVVTHDPELAEY-ADRIIELRDGKI 218
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
4-223 |
2.44e-82 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 246.12 E-value: 2.44e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 4 MIEIKHLNK-YFGDLHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPLTKKNH--LEMARKY 80
Cdd:COG3638 2 MLELRNLSKrYPGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGraLRRLRRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 81 SSMVFQQFNLYPNMTVLGNL---------TLAPIkLQKKSKEEaTEIAIAALKRVGMAHKAGEYPQNLSGGQQQRIAIAR 151
Cdd:COG3638 82 IGMIFQQFNLVPRLSVLTNVlagrlgrtsTWRSL-LGLFPPED-RERALEALERVGLADKAYQRADQLSGGQQQRVAIAR 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1469315281 152 ALCTKQPIILFDEPTSALDPEMVQEVLDVMIELAQED-ITMICVTHEMGFARQVADRVIFMEDGRILEEGTPE 223
Cdd:COG3638 160 ALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDgITVVVNLHQVDLARRYADRIIGLRDGRVVFDGPPA 232
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
5-242 |
1.97e-81 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 244.49 E-value: 1.97e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 5 IEIKHLNKYFGDLHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPLT------------KKN 72
Cdd:PRK10619 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgqlkvaDKN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 73 HLEMARKYSSMVFQQFNLYPNMTVLGNLTLAPIKLQKKSKEEATEIAIAALKRVGMAHKA-GEYPQNLSGGQQQRIAIAR 151
Cdd:PRK10619 86 QLRLLRTRLTMVFQHFNLWSHMTVLENVMEAPIQVLGLSKQEARERAVKYLAKVGIDERAqGKYPVHLSGGQQQRVSIAR 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 152 ALCTKQPIILFDEPTSALDPEMVQEVLDVMIELAQEDITMICVTHEMGFARQVADRVIFMEDGRILEEGTPEHFFDNPEN 231
Cdd:PRK10619 166 ALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGNPQS 245
|
250
....*....|.
gi 1469315281 232 PRCREFLSKIL 242
Cdd:PRK10619 246 PRLQQFLKGSL 256
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
4-243 |
4.98e-81 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 246.25 E-value: 4.98e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 4 MIEIKHLNKYF----GDLHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPLTK--KNHLEMA 77
Cdd:PRK11153 1 MIELKNISKVFpqggRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTAlsEKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 78 RKYSSMVFQQFNLYPNMTVLGNLTLaPIKLQKKSKEEATEIAIAALKRVGMAHKAGEYPQNLSGGQQQRIAIARALCTKQ 157
Cdd:PRK11153 81 RRQIGMIFQHFNLLSSRTVFDNVAL-PLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 158 PIILFDEPTSALDPEMVQEVLDVMIELAQE-DITMICVTHEMGFARQVADRVIFMEDGRILEEGTPEHFFDNPENPRCRE 236
Cdd:PRK11153 160 KVLLCDEATSALDPATTRSILELLKDINRElGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHPKHPLTRE 239
|
....*..
gi 1469315281 237 FLSKILH 243
Cdd:PRK11153 240 FIQSTLH 246
|
|
| 3a0107s01c2 |
TIGR00972 |
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein ... |
5-240 |
5.64e-80 |
|
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein of a family of ABC transporters for inorganic phosphate. In the model species Escherichia coli, a constitutive transporter for inorganic phosphate, with low affinity, is also present. The high affinity transporter that includes this polypeptide is induced when extracellular phosphate concentrations are low. The proteins most similar to the members of this family but not included appear to be amino acid transporters. [Transport and binding proteins, Anions]
Pssm-ID: 273372 [Multi-domain] Cd Length: 247 Bit Score: 240.27 E-value: 5.64e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 5 IEIKHLNKYFGDLHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEE-----PTSGEVLIDGTPLT-KKNHLEMAR 78
Cdd:TIGR00972 2 IEIENLNLFYGEKEALKNINLDIPKNQVTALIGPSGCGKSTLLRSLNRMNDlvpgvRIEGKVLFDGQDIYdKKIDVVELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 79 KYSSMVFQQFNLYPnMTVLGNLTLAPiKLQK-KSKEEATEIAIAALKRVGM----AHKAGEYPQNLSGGQQQRIAIARAL 153
Cdd:TIGR00972 82 RRVGMVFQKPNPFP-MSIYDNIAYGP-RLHGiKDKKELDEIVEESLKKAALwdevKDRLHDSALGLSGGQQQRLCIARAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 154 CTKQPIILFDEPTSALDPEMVQEVLDVMIELAqEDITMICVTHEMGFARQVADRVIFMEDGRILEEGTPEHFFDNPENPR 233
Cdd:TIGR00972 160 AVEPEVLLLDEPTSALDPIATGKIEELIQELK-KKYTIVIVTHNMQQAARISDRTAFFYDGELVEYGPTEQIFTNPKEKR 238
|
....*..
gi 1469315281 234 CREFLSK 240
Cdd:TIGR00972 239 TEDYISG 245
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-232 |
2.14e-79 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 242.31 E-value: 2.14e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 1 MAD-MIEIKHLNKYFGDLHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPLTkknHLEMARK 79
Cdd:COG3842 1 MAMpALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVT---GLPPEKR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 80 YSSMVFQQFNLYPNMTVLGNLTLaPIKLQKKSKEEATEIAIAALKRVGMAHKAGEYPQNLSGGQQQRIAIARALCTKQPI 159
Cdd:COG3842 78 NVGMVFQDYALFPHLTVAENVAF-GLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRV 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1469315281 160 ILFDEPTSALDP----EMVQEVLDVmieLAQEDITMICVTHEMGFARQVADRVIFMEDGRILEEGTPEHFFDNPENP 232
Cdd:COG3842 157 LLLDEPLSALDAklreEMREELRRL---QRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEIYERPATR 230
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
5-220 |
3.58e-79 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 237.03 E-value: 3.58e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 5 IEIKHLNKYFGDLHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPLTkknHLEMARKYSSMV 84
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVT---GVPPERRNIGMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 85 FQQFNLYPNMTVLGNLTLaPIKLQKKSKEEATEIAIAALKRVGMAHKAGEYPQNLSGGQQQRIAIARALCTKQPIILFDE 164
Cdd:cd03259 78 FQDYALFPHLTVAENIAF-GLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1469315281 165 PTSALDPEMVQEVLDVMIEL-AQEDITMICVTHEMGFARQVADRVIFMEDGRILEEG 220
Cdd:cd03259 157 PLSALDAKLREELREELKELqRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
5-230 |
1.19e-78 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 236.07 E-value: 1.19e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 5 IEIKHLN-KYFGDLHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPLTKKNHLEMARKySSM 83
Cdd:COG1122 1 IELENLSfSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRK-VGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 84 VFQqfnlYP-----NMTVLGNLTLAPIKLqKKSKEEATEIAIAALKRVGMAHKAGEYPQNLSGGQQQRIAIARALCTKQP 158
Cdd:COG1122 80 VFQ----NPddqlfAPTVEEDVAFGPENL-GLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPE 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1469315281 159 IILFDEPTSALDPEMVQEVLDVMIELAQEDITMICVTHEMGFARQVADRVIFMEDGRILEEGTPEHFFDNPE 230
Cdd:COG1122 155 VLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDYE 226
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
4-232 |
6.98e-78 |
|
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: 243.27 E-value: 6.98e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 4 MIEIKHLNKYF-----GDLHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPLTKKNHLEMA- 77
Cdd:COG1123 260 LLEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLRe 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 78 -RKYSSMVFQ----QFNlyPNMTVLGNLTLAPIKLQKKSKEEATEIAIAALKRVGM-AHKAGEYPQNLSGGQQQRIAIAR 151
Cdd:COG1123 340 lRRRVQMVFQdpysSLN--PRMTVGDIIAEPLRLHGLLSRAERRERVAELLERVGLpPDLADRYPHELSGGQRQRVAIAR 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 152 ALCTKQPIILFDEPTSALDPeMVQ-EVLDVMIELAQE-DITMICVTHEMGFARQVADRVIFMEDGRILEEGTPEHFFDNP 229
Cdd:COG1123 418 ALALEPKLLILDEPTSALDV-SVQaQILNLLRDLQRElGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVFANP 496
|
...
gi 1469315281 230 ENP 232
Cdd:COG1123 497 QHP 499
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
5-225 |
1.13e-77 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 234.00 E-value: 1.13e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 5 IEIKHLNKYFGDL-HVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPLTKKNH--LEMARKYS 81
Cdd:cd03256 1 IEVENLSKTYPNGkKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGkaLRQLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 82 SMVFQQFNLYPNMTVLGNLTLApiKLQKKS---------KEEATEIAIAALKRVGMAHKAGEYPQNLSGGQQQRIAIARA 152
Cdd:cd03256 81 GMIFQQFNLIERLSVLENVLSG--RLGRRStwrslfglfPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIARA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1469315281 153 LCTKQPIILFDEPTSALDPEMVQEVLDVMIELAQED-ITMICVTHEMGFARQVADRVIFMEDGRILEEGTPEHF 225
Cdd:cd03256 159 LMQQPKLILADEPVASLDPASSRQVMDLLKRINREEgITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAEL 232
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-219 |
1.81e-77 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 234.21 E-value: 1.81e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 1 MADMIEIKHLNKYF----GDLHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPLTKKNHlEM 76
Cdd:COG1116 4 AAPALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGP-DR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 77 ArkyssMVFQQFNLYPNMTVLGNLTLAPiKLQKKSKEEATEIAIAALKRVGMAHKAGEYPQNLSGGQQQRIAIARALCTK 156
Cdd:COG1116 83 G-----VVFQEPALLPWLTVLDNVALGL-ELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALAND 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1469315281 157 QPIILFDEPTSALDP----EMVQEVLDVmieLAQEDITMICVTHEMGFARQVADRVIFMED--GRILEE 219
Cdd:COG1116 157 PEVLLMDEPFGALDAltreRLQDELLRL---WQETGKTVLFVTHDVDEAVFLADRVVVLSArpGRIVEE 222
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-231 |
3.49e-76 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 234.20 E-value: 3.49e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 1 MAdMIEIKHLNKYFGDLHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPLtkkNHLEMARKY 80
Cdd:COG3839 1 MA-SLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDV---TDLPPKDRN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 81 SSMVFQQFNLYPNMTVLGNLTLaPIKLQKKSKEEATEIAIAALKRVGMAHKAGEYPQNLSGGQQQRIAIARALCTKQPII 160
Cdd:COG3839 77 IAMVFQSYALYPHMTVYENIAF-PLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 161 LFDEPTSALDP----EMVQEVLDVMIELaqeDITMICVTHEmgfarQV-----ADRVIFMEDGRILEEGTPEHFFDNPEN 231
Cdd:COG3839 156 LLDEPLSNLDAklrvEMRAEIKRLHRRL---GTTTIYVTHD-----QVeamtlADRIAVMNDGRIQQVGTPEELYDRPAN 227
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
5-215 |
2.82e-75 |
|
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: 225.91 E-value: 2.82e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 5 IEIKHLNKYFGDLHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPLTKKN-HLEMARKYSSM 83
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEdELPPLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 84 VFQQFNLYPNMTVLGNLTLApiklqkkskeeateiaiaalkrvgmahkageypqnLSGGQQQRIAIARALCTKQPIILFD 163
Cdd:cd03229 81 VFQDFALFPHLTVLENIALG-----------------------------------LSGGQQQRVALARALAMDPDVLLLD 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1469315281 164 EPTSALDPEMVQEVLDVMIELAQED-ITMICVTHEMGFARQVADRVIFMEDGR 215
Cdd:cd03229 126 EPTSALDPITRREVRALLKSLQAQLgITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
5-237 |
1.93e-74 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 225.84 E-value: 1.93e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 5 IEIKHLNKYFGDLHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPLTK--KNHLEMARKYSS 82
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGlsEAELYRLRRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 83 MVFQQFNLYPNMTVLGNLTLaPIK-LQKKSKEEATEIAIAALKRVGMAHKAGEYPQNLSGGQQQRIAIARALCTKQPIIL 161
Cdd:cd03261 81 MLFQSGALFDSLTVFENVAF-PLReHTRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1469315281 162 FDEPTSALDPEMVQEVLDVMIELAQE-DITMICVTHEMGFARQVADRVIFMEDGRILEEGTPEHFFDNPeNPRCREF 237
Cdd:cd03261 160 YDEPTAGLDPIASGVIDDLIRSLKKElGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRASD-DPLVRQF 235
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
4-227 |
1.97e-74 |
|
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: 226.03 E-value: 1.97e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 4 MIEIKHLNK-YFGDLHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPLTK--KNHLEMARKY 80
Cdd:TIGR02315 1 MLEVENLSKvYPNGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKlrGKKLRKLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 81 SSMVFQQFNLYPNMTVLGNL---------TLAPIkLQKKSKEEaTEIAIAALKRVGMAHKAGEYPQNLSGGQQQRIAIAR 151
Cdd:TIGR02315 81 IGMIFQHYNLIERLTVLENVlhgrlgykpTWRSL-LGRFSEED-KERALSALERVGLADKAYQRADQLSGGQQQRVAIAR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1469315281 152 ALCTKQPIILFDEPTSALDPEMVQEVLDVMIELAQED-ITMICVTHEMGFARQVADRVIFMEDGRILEEGTPEHFFD 227
Cdd:TIGR02315 159 ALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDgITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSELDD 235
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
5-223 |
4.41e-73 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 222.25 E-value: 4.41e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 5 IEIKHLNKYFGDLHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPLTKknHLEMARKYSSMV 84
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVAR--DPAEVRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 85 FQQFNLYPNMTVLGNLTLApIKLQKKSKEEATEIAIAALKRVGMAHKAGEYPQNLSGGQQQRIAIARALCTKQPIILFDE 164
Cdd:COG1131 79 PQEPALYPDLTVRENLRFF-ARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDE 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1469315281 165 PTSALDPEMVQEVLDVMIELAQEDITMICVTHEMGFARQVADRVIFMEDGRILEEGTPE 223
Cdd:COG1131 158 PTSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPD 216
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
4-220 |
1.06e-72 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 220.69 E-value: 1.06e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 4 MIEIKHLNK-YFGDLHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVdYLEE-PTSGEVLIDGTPLT--KKNHLEMARK 79
Cdd:COG2884 1 MIRFENVSKrYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLL-YGEErPTSGQVLVNGQDLSrlKRREIPYLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 80 YSSMVFQQFNLYPNMTVLGNLTLaPIKLQKKSKEEATEIAIAALKRVGMAHKAGEYPQNLSGGQQQRIAIARALCTKQPI 159
Cdd:COG2884 80 RIGVVFQDFRLLPDRTVYENVAL-PLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPEL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1469315281 160 ILFDEPTSALDPEMVQEVLDVMIELAQEDITMICVTHEMGFARQVADRVIFMEDGRILEEG 220
Cdd:COG2884 159 LLADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLELVDRMPKRVLELEDGRLVRDE 219
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
4-242 |
1.08e-72 |
|
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: 221.60 E-value: 1.08e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 4 MIEIKHLNKYFG----DLHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPLTKKNHLEMARK 79
Cdd:COG1124 1 MLEVRNLSVSYGqggrRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 80 ySSMVFQQ----FNlyPNMTVLGnlTLA-PIKLQKKSKEEAtEIAiAALKRVGM-AHKAGEYPQNLSGGQQQRIAIARAL 153
Cdd:COG1124 81 -VQMVFQDpyasLH--PRHTVDR--ILAePLRIHGLPDREE-RIA-ELLEQVGLpPSFLDRYPHQLSGGQRQRVAIARAL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 154 CTKQPIILFDEPTSALDPeMVQ-EVLDVMIEL-AQEDITMICVTHEMGFARQVADRVIFMEDGRILEEGTPEHFFDNPEN 231
Cdd:COG1124 154 ILEPELLLLDEPTSALDV-SVQaEILNLLKDLrEERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAGPKH 232
|
250
....*....|.
gi 1469315281 232 PRCREFLSKIL 242
Cdd:COG1124 233 PYTRELLAASL 243
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
20-237 |
2.54e-71 |
|
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: 219.05 E-value: 2.54e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 20 LKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPLTKKNH---LEMARKYSSMVFQQFNLYPNMTV 96
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRkelRELRRKKISMVFQSFALLPHRTV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 97 LGNLTLaPIKLQKKSKEEATEIAIAALKRVGMAHKAGEYPQNLSGGQQQRIAIARALCTKQPIILFDEPTSALDP----E 172
Cdd:cd03294 120 LENVAF-GLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPlirrE 198
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1469315281 173 MVQEVLDVMIELAqedITMICVTHEMGFARQVADRVIFMEDGRILEEGTPEHFFDNPENPRCREF 237
Cdd:cd03294 199 MQDELLRLQAELQ---KTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDYVREF 260
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
4-220 |
7.71e-71 |
|
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: 216.22 E-value: 7.71e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 4 MIEIKHLNKYF----GDLHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPLTKKNHLEMA-- 77
Cdd:cd03257 1 LLEVKNLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKir 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 78 RKYSSMVFQ--QFNLYPNMTVLGNLTLAPIKLQKKSKEEATEIAIAA-LKRVGMAHK-AGEYPQNLSGGQQQRIAIARAL 153
Cdd:cd03257 81 RKEIQMVFQdpMSSLNPRMTIGEQIAEPLRIHGKLSKKEARKEAVLLlLVGVGLPEEvLNRYPHELSGGQRQRVAIARAL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1469315281 154 CTKQPIILFDEPTSALDPEMVQEVLDVMIELAQE-DITMICVTHEMGFARQVADRVIFMEDGRILEEG 220
Cdd:cd03257 161 ALNPKLLIADEPTSALDVSVQAQILDLLKKLQEElGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
4-238 |
2.26e-70 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 217.65 E-value: 2.26e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 4 MIEIKHLNKYFGDLHV-LKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPLTKKNHLEMARK--Y 80
Cdd:COG1125 1 MIEFENVTKRYPDGTVaVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRDLDPVELRRRigY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 81 ssmVFQQFNLYPNMTVLGNLTLAPiKLQKKSKEEATEIAIAALKRVGMAHK--AGEYPQNLSGGQQQRIAIARALCTKQP 158
Cdd:COG1125 81 ---VIQQIGLFPHMTVAENIATVP-RLLGWDKERIRARVDELLELVGLDPEeyRDRYPHELSGGQQQRVGVARALAADPP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 159 IILFDEPTSALDPeMVQEVL-DVMIELaQEDI--TMICVTHEMGFARQVADRVIFMEDGRILEEGTPEHFFDNPENPRCR 235
Cdd:COG1125 157 ILLMDEPFGALDP-ITREQLqDELLRL-QRELgkTIVFVTHDIDEALKLGDRIAVMREGRIVQYDTPEEILANPANDFVA 234
|
...
gi 1469315281 236 EFL 238
Cdd:COG1125 235 DFV 237
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
5-225 |
3.40e-70 |
|
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: 214.74 E-value: 3.40e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 5 IEIKHLNKYFGDLHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEE-----PTSGEVLIDGTPLTKKNHLEMA-R 78
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIYDLDVDVLElR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 79 KYSSMVFQQFNLYPnMTVLGNLTLAPIKLQKKSKEEATEIAIAALKRVGMAHKAGE--YPQNLSGGQQQRIAIARALCTK 156
Cdd:cd03260 81 RRVGMVFQKPNPFP-GSIYDNVAYGLRLHGIKLKEELDERVEEALRKAALWDEVKDrlHALGLSGGQQQRLCLARALANE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1469315281 157 QPIILFDEPTSALDPEMVQEVLDVMIELAQEdITMICVTHEMGFARQVADRVIFMEDGRILEEGTPEHF 225
Cdd:cd03260 160 PEVLLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
4-237 |
6.72e-70 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 219.20 E-value: 6.72e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 4 MIEIKHLNKYFGD-----LHVLK-------------------DINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSG 59
Cdd:COG4175 3 KIEVRNLYKIFGKrperaLKLLDqgkskdeilektgqtvgvnDASFDVEEGEIFVIMGLSGSGKSTLVRCLNRLIEPTAG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 60 EVLIDGTPLTKKNH---LEMARKYSSMVFQQFNLYPNMTVLGNLTLaPIKLQKKSKEEATEIAIAALKRVGMAHKAGEYP 136
Cdd:COG4175 83 EVLIDGEDITKLSKkelRELRRKKMSMVFQHFALLPHRTVLENVAF-GLEIQGVPKAERRERAREALELVGLAGWEDSYP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 137 QNLSGGQQQRIAIARALCTKQPIILFDEPTSALDP----EMvQEVLdvmIELaQEDI--TMICVTHEMGFARQVADRVIF 210
Cdd:COG4175 162 DELSGGMQQRVGLARALATDPDILLMDEAFSALDPlirrEM-QDEL---LEL-QAKLkkTIVFITHDLDEALRLGDRIAI 236
|
250 260
....*....|....*....|....*..
gi 1469315281 211 MEDGRILEEGTPEHFFDNPENPRCREF 237
Cdd:COG4175 237 MKDGRIVQIGTPEEILTNPANDYVADF 263
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
5-240 |
2.62e-68 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 210.23 E-value: 2.62e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 5 IEIKHLNKYFGDLH-VLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPLTKKNHLEMARK--Ys 81
Cdd:cd03295 1 IEFENVTKRYGGGKkAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKigY- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 82 smVFQQFNLYPNMTVLGNLTLAPiKLQKKSKEEATEIAIAALKRVGM--AHKAGEYPQNLSGGQQQRIAIARALCTKQPI 159
Cdd:cd03295 80 --VIQQIGLFPHMTVEENIALVP-KLLKWPKEKIRERADELLALVGLdpAEFADRYPHELSGGQQQRVGVARALAADPPL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 160 ILFDEPTSALDPEMVQEVLDVMIELAQE-DITMICVTHEMGFARQVADRVIFMEDGRILEEGTPEHFFDNPENPRCREFL 238
Cdd:cd03295 157 LLMDEPFGALDPITRDQLQEEFKRLQQElGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDFVAEFV 236
|
..
gi 1469315281 239 SK 240
Cdd:cd03295 237 GA 238
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
5-239 |
3.17e-68 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 210.66 E-value: 3.17e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 5 IEIKHLNKYFGDLHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYL--EEP---TSGEVLIDGTP-LTKKNHLEMAR 78
Cdd:COG1117 12 IEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMndLIPgarVEGEILLDGEDiYDPDVDVVELR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 79 KYSSMVFQQFNLYPnMTVLGNLTLAPIKLQKKSKEEATEIAIAALKRVGM----AHKAGEYPQNLSGGQQQRIAIARALC 154
Cdd:COG1117 92 RRVGMVFQKPNPFP-KSIYDNVAYGLRLHGIKSKSELDEIVEESLRKAALwdevKDRLKKSALGLSGGQQQRLCIARALA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 155 TKQPIILFDEPTSALDPEMVQEVLDVMIELAqEDITMICVTHEMGFARQVADRVIFMEDGRILEEGTPEHFFDNPENPRC 234
Cdd:COG1117 171 VEPEVLLMDEPTSALDPISTAKIEELILELK-KDYTIVIVTHNMQQAARVSDYTAFFYLGELVEFGPTEQIFTNPKDKRT 249
|
....*
gi 1469315281 235 REFLS 239
Cdd:COG1117 250 EDYIT 254
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
4-238 |
6.20e-68 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 209.23 E-value: 6.20e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 4 MIEIKHLNKYFGDLHvlKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPLTkknHLEMARKYSSM 83
Cdd:COG3840 1 MLRLDDLTYRYGDFP--LRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLT---ALPPAERPVSM 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 84 VFQQFNLYPNMTVLGN--LTLAP-IKLqkkSKEEATEIAiAALKRVGMAHKAGEYPQNLSGGQQQRIAIARALCTKQPII 160
Cdd:COG3840 76 LFQENNLFPHLTVAQNigLGLRPgLKL---TAEQRAQVE-QALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPIL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1469315281 161 LFDEPTSALDPEMVQEVLDVMIELAQE-DITMICVTHEMGFARQVADRVIFMEDGRILEEGTPEHFFDNPENPRCREFL 238
Cdd:COG3840 152 LLDEPFSALDPALRQEMLDLVDELCRErGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPPALAAYL 230
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
5-219 |
1.41e-67 |
|
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: 207.71 E-value: 1.41e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 5 IEIKHLNKYFGD----LHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPLTKKNHlemARky 80
Cdd:cd03293 1 LEVRNVSKTYGGgggaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGP---DR-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 81 sSMVFQQFNLYPNMTVLGNLTLaPIKLQKKSKEEATEIAIAALKRVGMAHKAGEYPQNLSGGQQQRIAIARALCTKQPII 160
Cdd:cd03293 76 -GYVFQQDALLPWLTVLDNVAL-GLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1469315281 161 LFDEPTSALDP----EMVQEVLDVmieLAQEDITMICVTHEMGFARQVADRVIFME--DGRILEE 219
Cdd:cd03293 154 LLDEPFSALDAltreQLQEELLDI---WRETGKTVLLVTHDIDEAVFLADRVVVLSarPGRIVAE 215
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
5-232 |
2.89e-66 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 208.46 E-value: 2.89e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 5 IEIKHLNKYFGDLHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPLTkkNHLEMARKYSSMV 84
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLF--TNLPPRERRVGFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 85 FQQFNLYPNMTVLGNLTLAPiKLQKKSKEEATEIAIAALKRVGMAHKAGEYPQNLSGGQQQRIAIARALCTKQPIILFDE 164
Cdd:COG1118 81 FQHYALFPHMTVAENIAFGL-RVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLLLDE 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1469315281 165 PTSALD----PEMVQEVLDVmieLAQEDITMICVTHEMGFARQVADRVIFMEDGRILEEGTPEHFFDNPENP 232
Cdd:COG1118 160 PFGALDakvrKELRRWLRRL---HDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDRPATP 228
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
6-215 |
4.13e-66 |
|
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: 203.85 E-value: 4.13e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 6 EIKHLNKYFGDLH--VLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPLTKKNHLEMARKySSM 83
Cdd:cd03225 1 ELKNLSFSYPDGArpALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRK-VGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 84 VFQ----QFNlypNMTVLGNLTLAPiKLQKKSKEEATEIAIAALKRVGMAHKAGEYPQNLSGGQQQRIAIARALCTKQPI 159
Cdd:cd03225 80 VFQnpddQFF---GPTVEEEVAFGL-ENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDI 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1469315281 160 ILFDEPTSALDPEMVQEVLDVMIELAQEDITMICVTHEMGFARQVADRVIFMEDGR 215
Cdd:cd03225 156 LLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
5-230 |
6.27e-66 |
|
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: 204.21 E-value: 6.27e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 5 IEIKHLNKYFGDLHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPLTKKNHLEMARKYSSMV 84
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARLGIGRT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 85 FQQFNLYPNMTVLGNLTLAPIKLQK---------KSKEEATEIAIAALKRVGMAHKAGEYPQNLSGGQQQRIAIARALCT 155
Cdd:cd03219 81 FQIPRLFPELTVLENVMVAAQARTGsglllararREEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALAT 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1469315281 156 KQPIILFDEPTSALDPEMVQEVLDVMIELAQEDITMICVTHEMGFARQVADRVIFMEDGRILEEGTPEHFFDNPE 230
Cdd:cd03219 161 DPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRNNPR 235
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
4-223 |
1.17e-65 |
|
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: 204.12 E-value: 1.17e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 4 MIEIKHLNKYFGDLHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPLTKKNHLEMARKYsSM 83
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRI-AY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 84 VFQQFNLYPNMTV-----LGnltLAP-IKLQKKSKEEATEIAIAALKRVGMAHKAGEYPQNLSGGQQQRIAIARALCTKQ 157
Cdd:COG1120 80 VPQEPPAPFGLTVrelvaLG---RYPhLGLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1469315281 158 PIILFDEPTSALDPEMVQEVLDVMIELAQE-DITMICVTHEMGFARQVADRVIFMEDGRILEEGTPE 223
Cdd:COG1120 157 PLLLLDEPTSHLDLAHQLEVLELLRRLARErGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPE 223
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-230 |
1.23e-65 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 211.69 E-value: 1.23e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 1 MADMIEIKHLNKYF--GDLHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPT---SGEVLIDGTPLTKKNHLE 75
Cdd:COG1123 1 MTPLLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 76 MARKYSsMVFQQFNLYPNMTVLGNLTLAPIKLQKKSKEEATEIAIAALKRVGMAHKAGEYPQNLSGGQQQRIAIARALCT 155
Cdd:COG1123 81 RGRRIG-MVFQDPMTQLNPVTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALAL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1469315281 156 KQPIILFDEPTSALDPEMVQEVLDVMIELAQE-DITMICVTHEMGFARQVADRVIFMEDGRILEEGTPEHFFDNPE 230
Cdd:COG1123 160 DPDLLIADEPTTALDVTTQAEILDLLRELQRErGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAPQ 235
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
4-223 |
4.43e-64 |
|
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: 199.20 E-value: 4.43e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 4 MIEIKHLNKYFGD----LHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPLTKKNHLEMAR- 78
Cdd:COG4181 8 IIELRGLTKTVGTgageLTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDARARl 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 79 --KYSSMVFQQFNLYPNMTVLGNLTLaPIKLqkKSKEEATEIAIAALKRVGMAHKAGEYPQNLSGGQQQRIAIARALCTk 156
Cdd:COG4181 88 raRHVGFVFQSFQLLPTLTALENVML-PLEL--AGRRDARARARALLERVGLGHRLDHYPAQLSGGEQQRVALARAFAT- 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1469315281 157 QPIILF-DEPTSALDPEMVQEVLDVMIELAQE-DITMICVTHEMGFARQvADRVIFMEDGRILEEGTPE 223
Cdd:COG4181 164 EPAILFaDEPTGNLDAATGEQIIDLLFELNRErGTTLVLVTHDPALAAR-CDRVLRLRAGRLVEDTAAT 231
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
4-232 |
1.73e-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: 200.66 E-value: 1.73e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 4 MIEIKHLNKYF----GDLHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEP---TSGEVLIDGTPLTKKNHLEM 76
Cdd:COG0444 1 LLEVRNLKVYFptrrGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 77 aRKYS----SMVFQQ----FNlyPNMTVLGNLTLAPIKLQKKSKEEATEIAIAALKRVGM---AHKAGEYPQNLSGGQQQ 145
Cdd:COG0444 81 -RKIRgreiQMIFQDpmtsLN--PVMTVGDQIAEPLRIHGGLSKAEARERAIELLERVGLpdpERRLDRYPHELSGGMRQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 146 RIAIARALCTKQPIILFDEPTSALDPEMVQEVLDVMIELAQE-DITMICVTHEMGFARQVADRVIFMEDGRILEEGTPEH 224
Cdd:COG0444 158 RVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRElGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGPVEE 237
|
....*...
gi 1469315281 225 FFDNPENP 232
Cdd:COG0444 238 LFENPRHP 245
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-230 |
3.70e-63 |
|
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: 197.57 E-value: 3.70e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 1 MADMIEIKHLNKYFGDLHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPLTKK-----NHLE 75
Cdd:COG0411 1 SDPLLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLpphriARLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 76 MARKyssmvFQQFNLYPNMTVLGNLTLA--------------PIKLQKKSKEEATEIAIAALKRVGMAHKAGEYPQNLSG 141
Cdd:COG0411 81 IART-----FQNPRLFPELTVLENVLVAaharlgrgllaallRLPRARREEREARERAEELLERVGLADRADEPAGNLSY 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 142 GQQQRIAIARALCTKQPIILFDEPTSALDPEMVQEVLDVMIELAQE-DITMICVTHEMGFARQVADRVIFMEDGRILEEG 220
Cdd:COG0411 156 GQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDErGITILLIEHDMDLVMGLADRIVVLDFGRVIAEG 235
|
250
....*....|
gi 1469315281 221 TPEHFFDNPE 230
Cdd:COG0411 236 TPAEVRADPR 245
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
5-231 |
5.18e-63 |
|
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: 196.69 E-value: 5.18e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 5 IEIKHLNKYFGDLHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPLTkknHLEMARKYSSMV 84
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDIT---NLPPHKRPVNTV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 85 FQQFNLYPNMTVLGNLTLaPIKLQKKSKEEATEIAIAALKRVGMAHKAGEYPQNLSGGQQQRIAIARALCTKQPIILFDE 164
Cdd:cd03300 78 FQNYALFPHLTVFENIAF-GLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDE 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1469315281 165 PTSALDPEMVQEVLDVMIELAQE-DITMICVTHEMGFARQVADRVIFMEDGRILEEGTPEHFFDNPEN 231
Cdd:cd03300 157 PLGALDLKLRKDMQLELKRLQKElGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPAN 224
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
20-241 |
3.18e-62 |
|
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: 198.92 E-value: 3.18e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 20 LKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPLTKKNHLEMA---RKYSSMVFQQFNLYPNMTV 96
Cdd:TIGR01186 9 VNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEPTAGQIFIDGENIMKQSPVELRevrRKKIGMVFQQFALFPHMTI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 97 LGNLTLAPiKLQKKSKEEATEIAIAALKRVGMAHKAGEYPQNLSGGQQQRIAIARALCTKQPIILFDEPTSALDP----E 172
Cdd:TIGR01186 89 LQNTSLGP-ELLGWPEQERKEKALELLKLVGLEEYEHRYPDELSGGMQQRVGLARALAAEPDILLMDEAFSALDPlirdS 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1469315281 173 MVQEVLDVMIELAQediTMICVTHEMGFARQVADRVIFMEDGRILEEGTPEHFFDNPENPRCREFLSKI 241
Cdd:TIGR01186 168 MQDELKKLQATLQK---TIVFITHDLDEAIRIGDRIVIMKAGEIVQVGTPDEILRNPANEYVEEFIGKV 233
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-231 |
8.37e-61 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 191.46 E-value: 8.37e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 1 MADMIEIKHLNKYFGDLHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPLTKKNHLeMArkY 80
Cdd:COG1121 3 MMPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARRR-IG--Y 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 81 ssmVFQQFNLYPN--MTV-----LGnlTLAPIKLQKKSKEEATEIAIAALKRVGMAHKAGEYPQNLSGGQQQRIAIARAL 153
Cdd:COG1121 80 ---VPQRAEVDWDfpITVrdvvlMG--RYGRRGLFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARAL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1469315281 154 CTKQPIILFDEPTSALDPEMVQEVLDVMIELAQEDITMICVTHEMGFARQVADRVIFMeDGRILEEGTPEHFFdNPEN 231
Cdd:COG1121 155 AQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLL-NRGLVAHGPPEEVL-TPEN 230
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
1-241 |
1.87e-60 |
|
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ATP-binding protein is found in a number of genomes in operon-like contexts strongly suggesting a substrate specificity for 2-aminoethylphosphonate (2-AEP). The characterized PhnSTUV system is absent in the genomes in which this system is found. These genomes encode systems for the catabolism of 2-AEP, making the need for a 2-AEP-specific transporter likely. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274496 [Multi-domain] Cd Length: 353 Bit Score: 194.10 E-value: 1.87e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 1 MADMIEIKHLNKYFGDLHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPLTkknHLEMARKY 80
Cdd:TIGR03265 1 SSPYLSIDNIRKRFGAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDIT---RLPPQKRD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 81 SSMVFQQFNLYPNMTVLGNLTLApIKLQKKSKEEATEIAIAALKRVGMAHKAGEYPQNLSGGQQQRIAIARALCTKQPII 160
Cdd:TIGR03265 78 YGIVFQSYALFPNLTVADNIAYG-LKNRGMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALATSPGLL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 161 LFDEPTSALDPEmVQEVLDVMIELAQED--ITMICVTHEMGFARQVADRVIFMEDGRILEEGTPEHFFDNPENPRCREFL 238
Cdd:TIGR03265 157 LLDEPLSALDAR-VREHLRTEIRQLQRRlgVTTIMVTHDQEEALSMADRIVVMNHGVIEQVGTPQEIYRHPATPFVADFV 235
|
...
gi 1469315281 239 SKI 241
Cdd:TIGR03265 236 GEV 238
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
7-211 |
1.92e-59 |
|
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly wide distribution consists of a polypeptide related to the lactococcin 972 (see TIGR01653) and multiple-membrane-spanning putative immunity protein (see TIGR01654). This model represents a small clade within the ABC transporters that regularly are found adjacent to these bacteriocin system gene pairs and are likely serve as export proteins. [Cellular processes, Toxin production and resistance, Transport and binding proteins, Unknown substrate]
Pssm-ID: 188353 [Multi-domain] Cd Length: 206 Bit Score: 186.67 E-value: 1.92e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 7 IKHLNKYFGDLHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGT---PLTKKNHLEMARKYSSM 83
Cdd:TIGR03608 1 LKNISKKFGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQetpPLNSKKASKFRREKLGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 84 VFQQFNLYPNMTVLGNLTLaPIKLQKKSKEEATEIAIAALKRVGMAHKAGEYPQNLSGGQQQRIAIARALCTKQPIILFD 163
Cdd:TIGR03608 81 LFQNFALIENETVEENLDL-GLKYKKLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLILAD 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1469315281 164 EPTSALDPEMVQEVLDVMIELAQEDITMICVTHEMGFARQvADRVIFM 211
Cdd:TIGR03608 160 EPTGSLDPKNRDEVLDLLLELNDEGKTIIIVTHDPEVAKQ-ADRVIEL 206
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
5-216 |
4.35e-59 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 184.52 E-value: 4.35e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 5 IEIKHLNKYFGDLHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPLTKKNHLemARKYSSMV 84
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEE--VKRRIGYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 85 FQQFNLYPNMTVLGNLtlapiklqkkskeeateiaiaalkrvgmahkageypqNLSGGQQQRIAIARALCTKQPIILFDE 164
Cdd:cd03230 79 PEEPSLYENLTVRENL-------------------------------------KLSGGMKQRLALAQALLHDPELLILDE 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1469315281 165 PTSALDPEMVQEVLDVMIELAQEDITMICVTHEMGFARQVADRVIFMEDGRI 216
Cdd:cd03230 122 PTSGLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
4-225 |
1.40e-58 |
|
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: 185.45 E-value: 1.40e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 4 MIEIKHLNKYFGDLHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPLTKKNhlEMARKYSSM 83
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEP--REARRQIGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 84 VFQQFNLYPNMTVLGNLTLApIKLQKKSKEEATEIAIAALKRVGMAHKAGEYPQNLSGGQQQRIAIARALCTKQPIILFD 163
Cdd:COG4555 79 LPDERGLYDRLTVRENIRYF-AELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLD 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1469315281 164 EPTSALDPEMVQEVLDVMIELAQEDITMICVTHEMGFARQVADRVIFMEDGRILEEGTPEHF 225
Cdd:COG4555 158 EPTNGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDEL 219
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
5-230 |
4.17e-58 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the 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: 185.33 E-value: 4.17e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 5 IEIKHLN-KYFG-DLHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDG-TPLTKKNHLEMaRKYS 81
Cdd:TIGR04520 1 IEVENVSfSYPEsEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGlDTLDEENLWEI-RKKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 82 SMVFQ----QFnlyPNMTV-------LGNLTLAPIKLQKKSKEeateiaiaALKRVGMAHKAGEYPQNLSGGQQQRIAIA 150
Cdd:TIGR04520 80 GMVFQnpdnQF---VGATVeddvafgLENLGVPREEMRKRVDE--------ALKLVGMEDFRDREPHLLSGGQKQRVAIA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 151 RALCTKQPIILFDEPTSALDPEMVQEVLDVMIEL-AQEDITMICVTHEMGFARQvADRVIFMEDGRILEEGTPEHFFDNP 229
Cdd:TIGR04520 149 GVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLnKEEGITVISITHDMEEAVL-ADRVIVMNKGKIVAEGTPREIFSQV 227
|
.
gi 1469315281 230 E 230
Cdd:TIGR04520 228 E 228
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
5-223 |
4.74e-58 |
|
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: 183.40 E-value: 4.74e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 5 IEIKHLNKYFGDLHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPLTKKNHLEMARKYSSMV 84
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARAGIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 85 FQQFNLYPNMTVLGNLTLAPIKLQKKSKEEATEIAIA---ALKRVgMAHKAGeypqNLSGGQQQRIAIARALCTKQPIIL 161
Cdd:cd03224 81 PEGRRIFPELTVEENLLLGAYARRRAKRKARLERVYElfpRLKER-RKQLAG----TLSGGEQQMLAIARALMSRPKLLL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1469315281 162 FDEPTSALDPEMVQEVLDVMIELAQEDITMICVTHEMGFARQVADRVIFMEDGRILEEGTPE 223
Cdd:cd03224 156 LDEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAA 217
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
4-215 |
5.56e-58 |
|
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC transporter ATP-binding protein family. This protein, and its permease partner FtsX, localize to the division site. In a number of species, the ftsEX gene pair is located next to FtsY, the signal recognition particle-docking protein. [Cellular processes, Cell division]
Pssm-ID: 131721 [Multi-domain] Cd Length: 214 Bit Score: 183.22 E-value: 5.56e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 4 MIEIKHLNK-YFGDLHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPLTKKNHLEMA--RKY 80
Cdd:TIGR02673 1 MIEFHNVSKaYPGGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLRGRQLPllRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 81 SSMVFQQFNLYPNMTVLGNLTLaPIKLQKKSKEEATEIAIAALKRVGMAHKAGEYPQNLSGGQQQRIAIARALCTKQPII 160
Cdd:TIGR02673 81 IGVVFQDFRLLPDRTVYENVAL-PLEVRGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPPLL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1469315281 161 LFDEPTSALDPEMVQEVLDVMIELAQEDITMICVTHEMGFARQVADRVIFMEDGR 215
Cdd:TIGR02673 160 LADEPTGNLDPDLSERILDLLKRLNKRGTTVIVATHDLSLVDRVAHRVIILDDGR 214
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
5-216 |
1.49e-57 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 181.94 E-value: 1.49e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 5 IEIKHLNKYFGDLHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPLTKKNhLEMARKYSSMV 84
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMP-PPEWRRQVAYV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 85 FQQFNLYPNmTVLGNLTLApikLQKKSKEEATEIAIAALKRVGMAHKAGEYP-QNLSGGQQQRIAIARALCTKQPIILFD 163
Cdd:COG4619 80 PQEPALWGG-TVRDNLPFP---FQLRERKFDRERALELLERLGLPPDILDKPvERLSGGERQRLALIRALLLQPDVLLLD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1469315281 164 EPTSALDPEMVQEVLDVMIEL-AQEDITMICVTHEMGFARQVADRVIFMEDGRI 216
Cdd:COG4619 156 EPTSALDPENTRRVEELLREYlAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
5-220 |
4.51e-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: 180.91 E-value: 4.51e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 5 IEIKHLNKYFGDLHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPLTKknhLEMARKYSSMV 84
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTD---LPPKDRDIAMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 85 FQQFNLYPNMTVLGNLTLaPIKLQKKSKEEATEIAIAALKRVGMAHKAGEYPQNLSGGQQQRIAIARALCTKQPIILFDE 164
Cdd:cd03301 78 FQNYALYPHMTVYDNIAF-GLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1469315281 165 PTSALDPEMVQEVLDVMIELAQE-DITMICVTHEMGFARQVADRVIFMEDGRILEEG 220
Cdd:cd03301 157 PLSNLDAKLRVQMRAELKRLQQRlGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
5-231 |
9.89e-57 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 184.77 E-value: 9.89e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 5 IEIKHLNKYFGDLHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPLTkknHLEMARKYSSMV 84
Cdd:PRK09452 15 VELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDIT---HVPAENRHVNTV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 85 FQQFNLYPNMTVLGNLTLApIKLQKKSKEEATEIAIAALKRVGMAHKAGEYPQNLSGGQQQRIAIARALCTKQPIILFDE 164
Cdd:PRK09452 92 FQSYALFPHMTVFENVAFG-LRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDE 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1469315281 165 PTSALDPEMVQEvldVMIELA----QEDITMICVTHEMGFARQVADRVIFMEDGRILEEGTPEHFFDNPEN 231
Cdd:PRK09452 171 SLSALDYKLRKQ---MQNELKalqrKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKN 238
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
6-220 |
1.25e-56 |
|
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: 178.40 E-value: 1.25e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 6 EIKHLNKYFGDLHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPLTKKNHLEMARKYSSMvf 85
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYV-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 86 qqfnlypnmtvlgnltlapikLQkkskeeateiaiaALKRVGMAHKAGEYPQNLSGGQQQRIAIARALCTKQPIILFDEP 165
Cdd:cd03214 79 ---------------------PQ-------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEP 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1469315281 166 TSALDPEMVQEVLDVMIELAQE-DITMICVTHEMGFARQVADRVIFMEDGRILEEG 220
Cdd:cd03214 125 TSHLDIAHQIELLELLRRLARErGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
5-239 |
1.92e-56 |
|
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: 188.82 E-value: 1.92e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 5 IEIKHLN-KYFGDLH-VLKDINLTVKRGEKLVMIGPSGSGKSTLI----RcvdyLEEPTSGEVLIDGTPLTKKNhLEMAR 78
Cdd:COG4987 334 LELEDVSfRYPGAGRpVLDGLSLTLPPGERVAIVGPSGSGKSTLLalllR----FLDPQSGSITLGGVDLRDLD-EDDLR 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 79 KYSSMVFQQFNLYpNMTVLGNLTLApiklqkksKEEATEIAI-AALKRVGMAH-----------KAGEYPQNLSGGQQQR 146
Cdd:COG4987 409 RRIAVVPQRPHLF-DTTLRENLRLA--------RPDATDEELwAALERVGLGDwlaalpdgldtWLGEGGRRLSGGERRR 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 147 IAIARALCTKQPIILFDEPTSALDPEMVQEVLDVMIELAQEDiTMICVTHEM-GFARqvADRVIFMEDGRILEEGTPEHF 225
Cdd:COG4987 480 LALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGR-TVLLITHRLaGLER--MDRILVLEDGRIVEQGTHEEL 556
|
250
....*....|....
gi 1469315281 226 FDNpeNPRCREFLS 239
Cdd:COG4987 557 LAQ--NGRYRQLYQ 568
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
6-215 |
1.36e-55 |
|
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: 175.13 E-value: 1.36e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 6 EIKHLNKYFGDLHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPLTKKNHLEmARKYSSMVF 85
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEE-LRRRIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 86 QqfnlypnmtvlgnltlapiklqkkskeeateiaiaalkrvgmahkageypqnLSGGQQQRIAIARALCTKQPIILFDEP 165
Cdd:cd00267 80 Q----------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEP 107
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1469315281 166 TSALDPEMVQEVLDVMIELAQEDITMICVTHEMGFARQVADRVIFMEDGR 215
Cdd:cd00267 108 TSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
1-232 |
1.48e-55 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 180.70 E-value: 1.48e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 1 MADMIEIKHLNKYF-----------GDLHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPLT 69
Cdd:COG4608 4 AEPLLEVRDLKKHFpvrgglfgrtvGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDIT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 70 KKNHLEMA--RKYSSMVFQ--QFNLYPNMTVlGNLTLAPIKLQK-KSKEEATEIAIAALKRVGM--AHkAGEYPQNLSGG 142
Cdd:COG4608 84 GLSGRELRplRRRMQMVFQdpYASLNPRMTV-GDIIAEPLRIHGlASKAERRERVAELLELVGLrpEH-ADRYPHEFSGG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 143 QQQRIAIARALCTKQPIILFDEPTSALDPEmVQ-EVLDVMIELAQE-DITMICVTHEMGFARQVADRVIFMEDGRILEEG 220
Cdd:COG4608 162 QRQRIGIARALALNPKLIVCDEPVSALDVS-IQaQVLNLLEDLQDElGLTYLFISHDLSVVRHISDRVAVMYLGKIVEIA 240
|
250
....*....|..
gi 1469315281 221 TPEHFFDNPENP 232
Cdd:COG4608 241 PRDELYARPLHP 252
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
3-229 |
2.95e-55 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 180.30 E-value: 2.95e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 3 DMIEIKHLNKYFGDLHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPLTKKNhleMARKYSS 82
Cdd:PRK11432 5 NFVVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRS---IQQRDIC 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 83 MVFQQFNLYPNMTVLGNLTLApIKLQKKSKEEATEIAIAALKRVGMAHKAGEYPQNLSGGQQQRIAIARALCTKQPIILF 162
Cdd:PRK11432 82 MVFQSYALFPHMSLGENVGYG-LKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLF 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1469315281 163 DEPTSALDPEMVQEVLDVMIELAQE-DITMICVTHEMGFARQVADRVIFMEDGRILEEGTPEHFFDNP 229
Cdd:PRK11432 161 DEPLSNLDANLRRSMREKIRELQQQfNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQP 228
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
5-223 |
1.09e-54 |
|
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: 186.58 E-value: 1.09e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 5 IEIKHLN-KYFGDLH-VLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPLtkkNHLEMA--RKY 80
Cdd:COG2274 474 IELENVSfRYPGDSPpVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDL---RQIDPAslRRQ 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 81 SSMVFQQFNLYpNMTVLGNLTLApiklqkksKEEAT-EIAIAALKRVG-----MAHKAG------EYPQNLSGGQQQRIA 148
Cdd:COG2274 551 IGVVLQDVFLF-SGTIRENITLG--------DPDATdEEIIEAARLAGlhdfiEALPMGydtvvgEGGSNLSGGQRQRLA 621
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1469315281 149 IARALCTKQPIILFDEPTSALDPEMVQEVLDVMIELAQeDITMICVTHEMGFARQvADRVIFMEDGRILEEGTPE 223
Cdd:COG2274 622 IARALLRNPRILILDEATSALDAETEAIILENLRRLLK-GRTVIIIAHRLSTIRL-ADRIIVLDKGRIVEDGTHE 694
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
5-224 |
6.08e-54 |
|
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: 181.88 E-value: 6.08e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 5 IEIKHLN-KYFGDLHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPLTkknHLEMA--RKYS 81
Cdd:COG4988 337 IELEDVSfSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLS---DLDPAswRRQI 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 82 SMVFQQFNLyPNMTVLGNLTLApiklqkksKEEATEIAI-AALKRVGMAH-----------KAGEYPQNLSGGQQQRIAI 149
Cdd:COG4988 414 AWVPQNPYL-FAGTIRENLRLG--------RPDASDEELeAALEAAGLDEfvaalpdgldtPLGEGGRGLSGGQAQRLAL 484
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1469315281 150 ARALCTKQPIILFDEPTSALDPEMVQEVLDVMIELAQeDITMICVTHEMGFARQvADRVIFMEDGRILEEGTPEH 224
Cdd:COG4988 485 ARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAK-GRTVILITHRLALLAQ-ADRILVLDDGRIVEQGTHEE 557
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
5-223 |
9.84e-54 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 181.90 E-value: 9.84e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 5 IEIKHLN-KYFGDLHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPLTKKNhLEMARKYSSM 83
Cdd:COG1132 340 IEFENVSfSYPGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLT-LESLRRQIGV 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 84 VFQQFNLYpNMTVLGNLTLApiklqkksKEEATEIAI-AALKRV-----------GMAHKAGEYPQNLSGGQQQRIAIAR 151
Cdd:COG1132 419 VPQDTFLF-SGTIRENIRYG--------RPDATDEEVeEAAKAAqahefiealpdGYDTVVGERGVNLSGGQRQRIAIAR 489
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1469315281 152 ALCTKQPIILFDEPTSALDPEMVQEVLDVMIELAQeDITMICVTHEMGFARQvADRVIFMEDGRILEEGTPE 223
Cdd:COG1132 490 ALLKDPPILILDEATSALDTETEALIQEALERLMK-GRTTIVIAHRLSTIRN-ADRILVLDDGRIVEQGTHE 559
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
5-238 |
1.08e-53 |
|
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: 172.91 E-value: 1.08e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 5 IEIKHLNKYFGDLHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPLTKKNhleMARKYSSMV 84
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVP---VQERNVGFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 85 FQQFNLYPNMTVLGN----LTLAPIKlQKKSKEEATEIAIAALKRVGMAHKAGEYPQNLSGGQQQRIAIARALCTKQPII 160
Cdd:cd03296 80 FQHYALFRHMTVFDNvafgLRVKPRS-ERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1469315281 161 LFDEPTSALDPEMVQEVLDVMIELAQE-DITMICVTHEMGFARQVADRVIFMEDGRILEEGTPEHFFDNPENPRCREFL 238
Cdd:cd03296 159 LLDEPFGALDAKVRKELRRWLRRLHDElHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPASPFVYSFL 237
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
5-216 |
1.33e-53 |
|
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: 171.82 E-value: 1.33e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 5 IEIKHLNK-YFGDLHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPLT--KKNHLEMARKYS 81
Cdd:cd03292 1 IEFINVTKtYPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSdlRGRAIPYLRRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 82 SMVFQQFNLYPNMTVLGNLTLAPIKLQKKSKEEATEIAiAALKRVGMAHKAGEYPQNLSGGQQQRIAIARALCTKQPIIL 161
Cdd:cd03292 81 GVVFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVP-AALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILI 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1469315281 162 FDEPTSALDPEMVQEVLDVMIELAQEDITMICVTHEMGFARQVADRVIFMEDGRI 216
Cdd:cd03292 160 ADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
5-239 |
1.87e-53 |
|
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: 172.13 E-value: 1.87e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 5 IEIKHLNKYFGDLHvLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPLTkknHLEMARKYSSMV 84
Cdd:cd03299 1 LKVENLSKDWKEFK-LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDIT---NLPPEKRDISYV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 85 FQQFNLYPNMTVLGNLTLApIKLQKKSKEEATEIAIAALKRVGMAHKAGEYPQNLSGGQQQRIAIARALCTKQPIILFDE 164
Cdd:cd03299 77 PQNYALFPHMTVYKNIAYG-LKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDE 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1469315281 165 PTSALDPEmVQEVLDVMIELAQE--DITMICVTHEMGFARQVADRVIFMEDGRILEEGTPEHFFDNPENPRCREFLS 239
Cdd:cd03299 156 PFSALDVR-TKEKLREELKKIRKefGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPKNEFVAEFLG 231
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
5-215 |
2.94e-53 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 169.49 E-value: 2.94e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 5 IEIKHLN-KYFGDLH-VLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPLTKKNHLEMaRKYSS 82
Cdd:cd03228 1 IEFKNVSfSYPGRPKpVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESL-RKNIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 83 MVFQQFNLYpNMTVLGNLtlapiklqkkskeeateiaiaalkrvgmahkageypqnLSGGQQQRIAIARALCTKQPIILF 162
Cdd:cd03228 80 YVPQDPFLF-SGTIRENI--------------------------------------LSGGQRQRIAIARALLRDPPILIL 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1469315281 163 DEPTSALDPEMVQEVLDVMIELAQeDITMICVTHEMGFARQvADRVIFMEDGR 215
Cdd:cd03228 121 DEATSALDPETEALILEALRALAK-GKTVIVIAHRLSTIRD-ADRIIVLDDGR 171
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
10-220 |
5.39e-53 |
|
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: 170.37 E-value: 5.39e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 10 LNKYFGDLHVLK-DINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPLTkknHLEMARKYSSMVFQQF 88
Cdd:cd03298 3 LDKIRFSYGEQPmHFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVT---AAPPADRPVSMLFQEN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 89 NLYPNMTVLGNLTLAPIKLQKKSKEEATEIAiAALKRVGMAHKAGEYPQNLSGGQQQRIAIARALCTKQPIILFDEPTSA 168
Cdd:cd03298 80 NLFAHLTVEQNVGLGLSPGLKLTAEDRQAIE-VALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAA 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1469315281 169 LDPEMVQEVLDVMIEL-AQEDITMICVTHEMGFARQVADRVIFMEDGRILEEG 220
Cdd:cd03298 159 LDPALRAEMLDLVLDLhAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
5-243 |
9.70e-53 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 174.12 E-value: 9.70e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 5 IEIKHLNKYFGDLHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPLTkknHLEMARKYSSMV 84
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVS---RLHARDRKVGFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 85 FQQFNLYPNMTVLGNLTLAPIKLQKKSKEEATEI---AIAALKRVGMAHKAGEYPQNLSGGQQQRIAIARALCTKQPIIL 161
Cdd:PRK10851 80 FQHYALFRHMTVFDNIAFGLTVLPRRERPNAAAIkakVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 162 FDEPTSALDPEMVQEVLDVMIELAQE-DITMICVTHEMGFARQVADRVIFMEDGRILEEGTPEHFFDNPENPRCREFLSK 240
Cdd:PRK10851 160 LDEPFGALDAQVRKELRRWLRQLHEElKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREPATRFVLEFMGE 239
|
...
gi 1469315281 241 ILH 243
Cdd:PRK10851 240 VNR 242
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
4-223 |
9.99e-53 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 171.07 E-value: 9.99e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 4 MIEIKHLNKYFGDLHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCV-DYLEePTSGEVLIDGTPLTKKNHLEMARK--- 79
Cdd:COG4559 1 MLEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLtGELT-PSSGEVRLNGRPLAAWSPWELARRrav 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 80 ---YSSMVFQqFnlypnmTV-----LGnltLAPiklQKKSKEEATEIAIAALKRVGMAHKAG-EYPQnLSGGQQQRIAIA 150
Cdd:COG4559 80 lpqHSSLAFP-F------TVeevvaLG---RAP---HGSSAAQDRQIVREALALVGLAHLAGrSYQT-LSGGEQQRVQLA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 151 RALC------TKQPIILF-DEPTSALDPEMVQEVLDVMIELAQEDITMICVTHEMGFARQVADRVIFMEDGRILEEGTPE 223
Cdd:COG4559 146 RVLAqlwepvDGGPRWLFlDEPTSALDLAHQHAVLRLARQLARRGGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPE 225
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
5-230 |
3.41e-52 |
|
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: 170.32 E-value: 3.41e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 5 IEIKHLNKYFG-----DLHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPLT--KKNHLEMA 77
Cdd:TIGR04521 1 IKLKNVSYIYQpgtpfEKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITakKKKKLKDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 78 RKYSSMVFQqfnlYPNM-----TVLGNLTLAPIKLqKKSKEEATEIAIAALKRVGMAHKAGEY-PQNLSGGQQQRIAIAR 151
Cdd:TIGR04521 81 RKKVGLVFQ----FPEHqlfeeTVYKDIAFGPKNL-GLSEEEAEERVKEALELVGLDEEYLERsPFELSGGQMRRVAIAG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 152 ALCTKQPIILFDEPTSALDPEMVQEVLDVMIELAQE-DITMICVTHEMGFARQVADRVIFMEDGRILEEGTPEHFFDNPE 230
Cdd:TIGR04521 156 VLAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEkGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVFSDVD 235
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
1-235 |
9.92e-52 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 168.86 E-value: 9.92e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 1 MADMIEIKHLNKYF---------GDLHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPLTKK 71
Cdd:COG4167 1 MSALLEVRNLSKTFkyrtglfrrQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 72 NhlemaRKYSS----MVFQQFN--LYPNMTVlGNLTLAPIKLQKKSKEEATEIAIAA-LKRVGM-AHKAGEYPQNLSGGQ 143
Cdd:COG4167 81 D-----YKYRCkhirMIFQDPNtsLNPRLNI-GQILEEPLRLNTDLTAEEREERIFAtLRLVGLlPEHANFYPHMLSSGQ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 144 QQRIAIARALCTKQPIILFDEPTSALDPEMVQEVLDVMIELaQED--ITMICVTHEMGFARQVADRVIFMEDGRILEEGT 221
Cdd:COG4167 155 KQRVALARALILQPKIIIADEALAALDMSVRSQIINLMLEL-QEKlgISYIYVSQHLGIVKHISDKVLVMHQGEVVEYGK 233
|
250
....*....|....
gi 1469315281 222 PEHFFDNPENPRCR 235
Cdd:COG4167 234 TAEVFANPQHEVTK 247
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
5-232 |
7.62e-51 |
|
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: 173.33 E-value: 7.62e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 5 IEIKHLNKYF-----------GDLHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEePTSGEVLIDGTPLTKKNH 73
Cdd:COG4172 276 LEARDLKVWFpikrglfrrtvGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLI-PSEGEIRFDGQDLDGLSR 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 74 LEMARKYSSM--VFQQ-FN-LYPNMTVL-----GNLTLAPiklqKKSKEEATEIAIAALKRVG----MAHKageYPQNLS 140
Cdd:COG4172 355 RALRPLRRRMqvVFQDpFGsLSPRMTVGqiiaeGLRVHGP----GLSAAERRARVAEALEEVGldpaARHR---YPHEFS 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 141 GGQQQRIAIARALCTKQPIILFDEPTSALDpeM-VQ-EVLDVMIELAQE-DITMICVTHEMGFARQVADRVIFMEDGRIL 217
Cdd:COG4172 428 GGQRQRIAIARALILEPKLLVLDEPTSALD--VsVQaQILDLLRDLQREhGLAYLFISHDLAVVRALAHRVMVMKDGKVV 505
|
250
....*....|....*
gi 1469315281 218 EEGTPEHFFDNPENP 232
Cdd:COG4172 506 EQGPTEQVFDAPQHP 520
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
4-230 |
1.66e-50 |
|
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: 164.77 E-value: 1.66e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 4 MIEIKHLNKYFGDLHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPLTKKNHLEMARKYSSM 83
Cdd:COG0410 3 MLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIARLGIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 84 VFQQFNLYPNMTVLGNLTLAPIKLQKKSKEEATEIAIAAL-----KRvgMAHKAGeypqNLSGGQQQRIAIARALCTKQP 158
Cdd:COG0410 83 VPEGRRIFPSLTVEENLLLGAYARRDRAEVRADLERVYELfprlkER--RRQRAG----TLSGGEQQMLAIGRALMSRPK 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1469315281 159 IILFDEPTSALDPEMVQEVLDVMIELAQEDITMICVTHEMGFARQVADRVIFMEDGRILEEGTPEHFFDNPE 230
Cdd:COG0410 157 LLLLDEPSLGLAPLIVEEIFEIIRRLNREGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLADPE 228
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
20-167 |
1.86e-50 |
|
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: 161.66 E-value: 1.86e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 20 LKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPLTKKNHlEMARKYSSMVFQQFNLYPNMTVLGN 99
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDER-KSLRKEIGYVFQDPQLFPRLTVREN 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1469315281 100 LTLAPIkLQKKSKEEATEIAIAALKRVGMAHKA----GEYPQNLSGGQQQRIAIARALCTKQPIILFDEPTS 167
Cdd:pfam00005 80 LRLGLL-LKGLSKREKDARAEEALEKLGLGDLAdrpvGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
4-223 |
2.75e-49 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 162.25 E-value: 2.75e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 4 MIEIKHLNKYFGDLHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRC-VDYLeEPTSGEVLIDGTPLTKKNHLEMARK--- 79
Cdd:PRK13548 2 MLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRAlSGEL-SPDSGEVRLNGRPLADWSPAELARRrav 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 80 ---YSSMVFqqfnlyPnMTV-----LGnltLAPIKLqkkSKEEATEIAIAALKRVGMAHKAG-EYPQnLSGGQQQRIAIA 150
Cdd:PRK13548 81 lpqHSSLSF------P-FTVeevvaMG---RAPHGL---SRAEDDALVAAALAQVDLAHLAGrDYPQ-LSGGEQQRVQLA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 151 RALC------TKQPIILFDEPTSALDPEMVQEVLDVMIELAQED-ITMICVTHEMGFARQVADRVIFMEDGRILEEGTPE 223
Cdd:PRK13548 147 RVLAqlwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERgLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPA 226
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
35-241 |
1.11e-48 |
|
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: 162.66 E-value: 1.11e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 35 MIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPLTkknHLEMARKYSSMVFQQFNLYPNMTVLGNLTLaPIKLQKKSKEE 114
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVT---NVPPHLRHINMVFQSYALFPHMTVEENVAF-GLKMRKVPRAE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 115 ATEIAIAALKRVGMAHKAGEYPQNLSGGQQQRIAIARALCTKQPIILFDEPTSALD----PEMVQEVLDVMIELAqedIT 190
Cdd:TIGR01187 77 IKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDkklrDQMQLELKTIQEQLG---IT 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1469315281 191 MICVTHEMGFARQVADRVIFMEDGRILEEGTPEHFFDNPENPRCREFLSKI 241
Cdd:TIGR01187 154 FVFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFVARFIGEI 204
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
20-241 |
2.41e-48 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 164.05 E-value: 2.41e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 20 LKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPLTKKNHLEMA---RKYSSMVFQQFNLYPNMTV 96
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELRevrRKKIAMVFQSFALMPHMTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 97 LGNLTLApIKLQKKSKEEATEIAIAALKRVGMAHKAGEYPQNLSGGQQQRIAIARALCTKQPIILFDEPTSALDPEMVQE 176
Cdd:PRK10070 124 LDNTAFG-MELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTE 202
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1469315281 177 VLDVMIEL-AQEDITMICVTHEMGFARQVADRVIFMEDGRILEEGTPEHFFDNPENPRCREFLSKI 241
Cdd:PRK10070 203 MQDELVKLqAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFFRGV 268
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-226 |
2.52e-48 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 160.57 E-value: 2.52e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 1 MADMIEIKHLN-KYFG-DLHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPLTKKNHLEMaR 78
Cdd:PRK13635 2 KEEIIRVEHISfRYPDaATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDV-R 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 79 KYSSMVFQQ-FNLYPNMTVLGNLTLApIKLQKKSKEEATEIAIAALKRVGMAHKAGEYPQNLSGGQQQRIAIARALCTKQ 157
Cdd:PRK13635 81 RQVGMVFQNpDNQFVGATVQDDVAFG-LENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQP 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 158 PIILFDEPTSALDPEMVQEVLDVMIEL-AQEDITMICVTHEMGFARQvADRVIFMEDGRILEEGTPEHFF 226
Cdd:PRK13635 160 DIIILDEATSMLDPRGRREVLETVRQLkEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEIF 228
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
16-216 |
4.82e-48 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 157.72 E-value: 4.82e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 16 DLHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGtpltkKNHLEMA--RKYSSMVFQQFNLYPN 93
Cdd:TIGR01277 10 YEHLPMEFDLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVND-----QSHTGLApyQRPVSMLFQENNLFAH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 94 MTVLGNLTLA---PIKLQKKSKEEATEIAiaalKRVGMAHKAGEYPQNLSGGQQQRIAIARALCTKQPIILFDEPTSALD 170
Cdd:TIGR01277 85 LTVRQNIGLGlhpGLKLNAEQQEKVVDAA----QQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALD 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1469315281 171 PEMVQEVLDVMIELAQE-DITMICVTHEMGFARQVADRVIFMEDGRI 216
Cdd:TIGR01277 161 PLLREEMLALVKQLCSErQRTLLMVTHHLSDARAIASQIAVVSQGKI 207
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
6-209 |
5.03e-48 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 157.70 E-value: 5.03e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 6 EIKHLNKYFGDLHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPLTKKnhlemaRKYSSMVF 85
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKE------RKRIGYVP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 86 QQFNL---YPnMTV-----LGNLtlAPIKLQKKSKEEATEIAIAALKRVGMAHKAGEYPQNLSGGQQQRIAIARALCTKQ 157
Cdd:cd03235 75 QRRSIdrdFP-ISVrdvvlMGLY--GHKGLFRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDP 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1469315281 158 PIILFDEPTSALDPEMVQEVLDVMIELAQEDITMICVTHEMGFARQVADRVI 209
Cdd:cd03235 152 DLLLLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRVL 203
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1-231 |
1.14e-47 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 161.35 E-value: 1.14e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 1 MADmIEIKHLNKYFGDLHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGtplTKKNHLEMARKY 80
Cdd:PRK11000 1 MAS-VTLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGE---KRMNDVPPAERG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 81 SSMVFQQFNLYPNMTVLGNLTLApIKLQKKSKEEATEIAIAALKRVGMAHKAGEYPQNLSGGQQQRIAIARALCTKQPII 160
Cdd:PRK11000 77 VGMVFQSYALYPHLSVAENMSFG-LKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVF 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1469315281 161 LFDEPTSALDPEM-VQevldVMIELA----QEDITMICVTHEMGFARQVADRVIFMEDGRILEEGTPEHFFDNPEN 231
Cdd:PRK11000 156 LLDEPLSNLDAALrVQ----MRIEISrlhkRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPAN 227
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
4-230 |
5.20e-47 |
|
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: 159.11 E-value: 5.20e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 4 MIEIkHLNKYFGDLHVlkDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPLtkknhLEMARKYS-- 81
Cdd:COG4148 2 MLEV-DFRLRRGGFTL--DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVL-----QDSARGIFlp 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 82 ------SMVFQQFNLYPNMTVLGNLTLApiklQKKSKEEATEIAIAAL-KRVGMAHKAGEYPQNLSGGQQQRIAIARALC 154
Cdd:COG4148 74 phrrriGYVFQEARLFPHLSVRGNLLYG----RKRAPRAERRISFDEVvELLGIGHLLDRRPATLSGGERQRVAIGRALL 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1469315281 155 TkQP-IILFDEPTSALDPEMVQEVLDVMIELAQE-DITMICVTHEMGFARQVADRVIFMEDGRILEEGTPEHFFDNPE 230
Cdd:COG4148 150 S-SPrLLLMDEPLAALDLARKAEILPYLERLRDElDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRPD 226
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-221 |
7.46e-47 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 157.19 E-value: 7.46e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 4 MIEIKHLNKYFGDLHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPLTKKNHlemarkyssm 83
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDR---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 84 vfQQF-------NLYPNMTVLGNLT-LApiKLQKKSKEEATEIAIAALKRVGMAHKAGEYPQNLSGGQQQRIAIARALCT 155
Cdd:COG4152 71 --RRIgylpeerGLYPKMKVGEQLVyLA--RLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLH 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1469315281 156 KQPIILFDEPTSALDPEMVQEVLDVMIELAQEDITMICVTHEMGFARQVADRVIFMEDGRILEEGT 221
Cdd:COG4152 147 DPELLILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGS 212
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
5-231 |
1.02e-46 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 155.46 E-value: 1.02e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 5 IEIKHLNKYFGDLHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVD-----YLEEPTSGEVLIDGTPLTKKNHLEMaRK 79
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNrlielYPEARVSGEVYLDGQDIFKMDVIEL-RR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 80 YSSMVFQQFNLYPNMTVLGNLTLAPiKLQK--KSKEEATEIAIAALKRVGM----AHKAGEYPQNLSGGQQQRIAIARAL 153
Cdd:PRK14247 83 RVQMVFQIPNPIPNLSIFENVALGL-KLNRlvKSKKELQERVRWALEKAQLwdevKDRLDAPAGKLSGGQQQRLCIARAL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1469315281 154 CTKQPIILFDEPTSALDPEMVQEVLDVMIELaQEDITMICVTHEMGFARQVADRVIFMEDGRILEEGTPEHFFDNPEN 231
Cdd:PRK14247 162 AFQPEVLLADEPTANLDPENTAKIESLFLEL-KKDMTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTNPRH 238
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
4-215 |
1.24e-46 |
|
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: 153.79 E-value: 1.24e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 4 MIEIKHLNKYFGDLHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPLTKknHLEMARKYSSM 83
Cdd:COG4133 2 MLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRD--AREDYRRRLAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 84 VFQQFNLYPNMTVLGNLTLapikLQKKSKEEATEIAI-AALKRVGMAHKAGEYPQNLSGGQQQRIAIARALCTKQPIILF 162
Cdd:COG4133 80 LGHADGLKPELTVRENLRF----WAALYGLRADREAIdEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1469315281 163 DEPTSALDPEMVQEVLDVMIELAQEDITMICVTH-EMGFArqvADRVIFMEDGR 215
Cdd:COG4133 156 DEPFTALDAAGVALLAELIAAHLARGGAVLLTTHqPLELA---AARVLDLGDFK 206
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-242 |
1.49e-46 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 155.00 E-value: 1.49e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 1 MADMIEIKHLNKYFGDLHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYL-----EEPTSGEVLIDGTPL--TKKNH 73
Cdd:PRK14267 1 MKFAIETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLlelneEARVEGEVRLFGRNIysPDVDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 74 LEMaRKYSSMVFQQFNLYPNMTVLGNLTLApIKLQK--KSKEEATEIAIAALKRVGM----AHKAGEYPQNLSGGQQQRI 147
Cdd:PRK14267 81 IEV-RREVGMVFQYPNPFPHLTIYDNVAIG-VKLNGlvKSKKELDERVEWALKKAALwdevKDRLNDYPSNLSGGQRQRL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 148 AIARALCTKQPIILFDEPTSALDPEMVQEVLDVMIELaQEDITMICVTHEMGFARQVADRVIFMEDGRILEEGTPEHFFD 227
Cdd:PRK14267 159 VIARALAMKPKILLMDEPTANIDPVGTAKIEELLFEL-KKEYTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFE 237
|
250
....*....|....*
gi 1469315281 228 NPENPRCREFLSKIL 242
Cdd:PRK14267 238 NPEHELTEKYVTGAL 252
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-220 |
2.69e-46 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 160.57 E-value: 2.69e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 1 MADMIEIKHLNKYFGDLHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPLTKKNHLEMARKY 80
Cdd:COG1129 1 AEPLLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDAQAAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 81 SSMVFQQFNLYPNMTVLGNLTLA--PIKL----QKKSKEEATEIaiaaLKRVGMAHKAGEYPQNLSGGQQQRIAIARALC 154
Cdd:COG1129 81 IAIIHQELNLVPNLSVAENIFLGrePRRGglidWRAMRRRAREL----LARLGLDIDPDTPVGDLSVAQQQLVEIARALS 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1469315281 155 TKQPIILFDEPTSALDPEMVQEVLDVMIELAQEDITMICVTHEMGFARQVADRVIFMEDGRILEEG 220
Cdd:COG1129 157 RDARVLILDEPTASLTEREVERLFRIIRRLKAQGVAIIYISHRLDEVFEIADRVTVLRDGRLVGTG 222
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
4-233 |
5.11e-46 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 154.47 E-value: 5.11e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 4 MIEIKHLN-KYFGDLHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPLT-KKNHLEMARKYS 81
Cdd:PRK13639 1 ILETRDLKySYPDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKyDKKSLLEVRKTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 82 SMVFQQFN---LYPnmTVLGNLTLAPIKLqKKSKEEATEIAIAALKRVGMAHKAGEYPQNLSGGQQQRIAIARALCTKQP 158
Cdd:PRK13639 81 GIVFQNPDdqlFAP--TVEEDVAFGPLNL-GLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPE 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1469315281 159 IILFDEPTSALDPEMVQEVLDVMIELAQEDITMICVTHEMGFARQVADRVIFMEDGRILEEGTPEHFFDNPENPR 233
Cdd:PRK13639 158 IIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDIETIR 232
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
4-241 |
5.70e-46 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 157.30 E-value: 5.70e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 4 MIEIKHLNKYFGDLHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPLTkknHLEMARKYSSM 83
Cdd:PRK11607 19 LLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLS---HVPPYQRPINM 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 84 VFQQFNLYPNMTVLGNLTLApIKLQKKSKEEATEIAIAALKRVGMAHKAGEYPQNLSGGQQQRIAIARALCTKQPIILFD 163
Cdd:PRK11607 96 MFQSYALFPHMTVEQNIAFG-LKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLD 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 164 EPTSALDPE----MVQEVLDVmieLAQEDITMICVTHEMGFARQVADRVIFMEDGRILEEGTPEHFFDNPENPRCREFLS 239
Cdd:PRK11607 175 EPMGALDKKlrdrMQLEVVDI---LERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAEFIG 251
|
..
gi 1469315281 240 KI 241
Cdd:PRK11607 252 SV 253
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
11-220 |
6.54e-46 |
|
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: 152.06 E-value: 6.54e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 11 NKYFGDLHVlkDINLTVKrGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPL---TKKNHLEMARKYSSMVFQQ 87
Cdd:cd03297 7 EKRLPDFTL--KIDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLfdsRKKINLPPQQRKIGLVFQQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 88 FNLYPNMTVLGNLTLA-PIKLQKKSKEEATEIaiaaLKRVGMAHKAGEYPQNLSGGQQQRIAIARALCTKQPIILFDEPT 166
Cdd:cd03297 84 YALFPHLNVRENLAFGlKRKRNREDRISVDEL----LDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPF 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1469315281 167 SALDPEMVQEVLDVMIELAQE-DITMICVTHEMGFARQVADRVIFMEDGRILEEG 220
Cdd:cd03297 160 SALDRALRLQLLPELKQIKKNlNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
6-216 |
6.99e-46 |
|
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: 152.03 E-value: 6.99e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 6 EIKHLN-KYFGDLHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPLTKKnhleMARKYSSMV 84
Cdd:cd03226 1 RIENISfSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAK----ERRKSIGYV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 85 FQ--QFNLYPNmTVLGNLTLApiklqKKSKEEATEIAIAALKRVGMAHKAGEYPQNLSGGQQQRIAIARALCTKQPIILF 162
Cdd:cd03226 77 MQdvDYQLFTD-SVREELLLG-----LKELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIF 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1469315281 163 DEPTSALDPEMVQEVLDVMIELAQEDITMICVTHEMGFARQVADRVIFMEDGRI 216
Cdd:cd03226 151 DEPTSGLDYKNMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAI 204
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
4-223 |
1.07e-45 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 152.43 E-value: 1.07e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 4 MIEIKHLNKYFGDLHVLkdINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGtpltkKNHLEM--ARKYS 81
Cdd:PRK10771 1 MLKLTDITWLYHHLPMR--FDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNG-----QDHTTTppSRRPV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 82 SMVFQQFNLYPNMTVLGN--LTLAP-IKLQKKSKEEATEIAiaalKRVGMAHKAGEYPQNLSGGQQQRIAIARALCTKQP 158
Cdd:PRK10771 74 SMLFQENNLFSHLTVAQNigLGLNPgLKLNAAQREKLHAIA----RQMGIEDLLARLPGQLSGGQRQRVALARCLVREQP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1469315281 159 IILFDEPTSALDPEMVQEVLDVMIELAQE-DITMICVTHEMGFARQVADRVIFMEDGRILEEGTPE 223
Cdd:PRK10771 150 ILLLDEPFSALDPALRQEMLTLVSQVCQErQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTD 215
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
7-216 |
2.21e-45 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 152.14 E-value: 2.21e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 7 IKHLNKYFGDLHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPLTKknhlemARKYSSMVFQ 86
Cdd:PRK11247 15 LNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAE------AREDTRLMFQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 87 QFNLYPNMTVLGNLTLApikLQKKSKEEATEiaiaALKRVGMAHKAGEYPQNLSGGQQQRIAIARALCTKQPIILFDEPT 166
Cdd:PRK11247 89 DARLLPWKKVIDNVGLG---LKGQWRDAALQ----ALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1469315281 167 SALDP----EMVQevldvMIE-LAQE-DITMICVTHEMGFARQVADRVIFMEDGRI 216
Cdd:PRK11247 162 GALDAltriEMQD-----LIEsLWQQhGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-232 |
3.35e-45 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 158.31 E-value: 3.35e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 1 MADM--IEIKHLNKYFGD----LHVLKDINLTVKRGEKLVMIGPSGSGKS----TLIRCVDYLEEPTSGEVLIDGTPLTK 70
Cdd:COG4172 1 MMSMplLSVEDLSVAFGQgggtVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 71 KNHLEMaRKYS----SMVFQQ----FNlyPNMTVlGNLTLAPIKLQKK-SKEEATEIAIAALKRVGM---AHKAGEYPQN 138
Cdd:COG4172 81 LSEREL-RRIRgnriAMIFQEpmtsLN--PLHTI-GKQIAEVLRLHRGlSGAAARARALELLERVGIpdpERRLDAYPHQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 139 LSGGQQQRIAIARALCTKQPIILFDEPTSALDPeMVQ-EVLDVMIELAQE-DITMICVTHEMGFARQVADRVIFMEDGRI 216
Cdd:COG4172 157 LSGGQRQRVMIAMALANEPDLLIADEPTTALDV-TVQaQILDLLKDLQRElGMALLLITHDLGVVRRFADRVAVMRQGEI 235
|
250
....*....|....*.
gi 1469315281 217 LEEGTPEHFFDNPENP 232
Cdd:COG4172 236 VEQGPTAELFAAPQHP 251
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1-228 |
3.82e-45 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 151.70 E-value: 3.82e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 1 MADMIEIKHLNKYFGDLHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVdyleeptSGEVLIDGTPltkKNHLEM---- 76
Cdd:PRK09984 1 MQTIIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHL-------SGLITGDKSA---GSHIELlgrt 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 77 -------------ARKYSSMVFQQFNLYPNMTVLGNLTLAPIK--------LQKKSKEEATEiAIAALKRVGMAHKAGEY 135
Cdd:PRK09984 71 vqregrlardirkSRANTGYIFQQFNLVNRLSVLENVLIGALGstpfwrtcFSWFTREQKQR-ALQALTRVGMVHFAHQR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 136 PQNLSGGQQQRIAIARALCTKQPIILFDEPTSALDPEMVQEVLDVMIELAQED-ITMICVTHEMGFARQVADRVIFMEDG 214
Cdd:PRK09984 150 VSTLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDgITVVVTLHQVDYALRYCERIVALRQG 229
|
250
....*....|....
gi 1469315281 215 RILEEGTPEHfFDN 228
Cdd:PRK09984 230 HVFYDGSSQQ-FDN 242
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
5-224 |
6.39e-45 |
|
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: 149.96 E-value: 6.39e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 5 IEIKHLNKYFGDL--HVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPLTKknHLEMARKYSS 82
Cdd:cd03263 1 LQIRNLTKTYKKGtkPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT--DRKAARQSLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 83 MVFQQFNLYPNMTVLGNLTL-APIKlqKKSKEEATEIAIAALKRVGMAHKAGEYPQNLSGGQQQRIAIARALCTKQPIIL 161
Cdd:cd03263 79 YCPQFDALFDELTVREHLRFyARLK--GLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1469315281 162 FDEPTSALDPEMVQEVLDvMIELAQEDITMICVTHEMGFARQVADRVIFMEDGRILEEGTPEH 224
Cdd:cd03263 157 LDEPTSGLDPASRRAIWD-LILEVRKGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQE 218
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
5-216 |
7.30e-45 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 147.96 E-value: 7.30e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 5 IEIKHLNKYFGDLHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPLTKKNHLEMARKYSSMV 84
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDARRAGIAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 85 FQqfnlypnmtvlgnltlapiklqkkskeeateiaiaalkrvgmahkageypqnLSGGQQQRIAIARALCTKQPIILFDE 164
Cdd:cd03216 81 YQ----------------------------------------------------LSVGERQMVEIARALARNARLLILDE 108
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1469315281 165 PTSALDPEMVQEVLDVMIELAQEDITMICVTHEMGFARQVADRVIFMEDGRI 216
Cdd:cd03216 109 PTAALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRV 160
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
4-218 |
8.52e-45 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 150.78 E-value: 8.52e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 4 MIEIKHLNKYFG----DLHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPLTKKNhlemARK 79
Cdd:COG4525 3 MLTVRHVSVRYPgggqPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPG----ADR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 80 ysSMVFQQFNLYPNMTVLGNLTLaPIKLQKKSKEEATEIAIAALKRVGMAHKAGEYPQNLSGGQQQRIAIARALCTKQPI 159
Cdd:COG4525 79 --GVVFQKDALLPWLNVLDNVAF-GLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRF 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1469315281 160 ILFDEPTSALDP---EMVQE-VLDVMielAQEDITMICVTHEMGFARQVADRVIFMED--GRILE 218
Cdd:COG4525 156 LLMDEPFGALDAltrEQMQElLLDVW---QRTGKGVFLITHSVEEALFLATRLVVMSPgpGRIVE 217
|
|
| ABC_ATP_DarD |
NF038007 |
darobactin export ABC transporter ATP-binding protein; |
4-216 |
9.95e-45 |
|
darobactin export ABC transporter ATP-binding protein;
Pssm-ID: 411600 [Multi-domain] Cd Length: 218 Bit Score: 149.48 E-value: 9.95e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 4 MIEIKHLNKYFG----DLHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDG---TPLTKKNHLEM 76
Cdd:NF038007 1 MLNMQNAEKCYItktiKTKVLNHLNFSVEKGDFVSIMGPSGSGKSTLLNIIGMFDSLDSGSLTLAGkevTNLSYSQKIIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 77 ARKYSSMVFQQFNLYPNMTVLGNLTLaPIKLQKKSKEEATEIAIAALKRVGMAHKAGEYPQNLSGGQQQRIAIARALCTK 156
Cdd:NF038007 81 RRELIGYIFQSFNLIPHLSIFDNVAL-PLKYRGVAKKERIERVNQVLNLFGIDNRRNHKPMQLSGGQQQRVAIARAMVSN 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 157 QPIILFDEPTSALDPEMVQEVLDVMIELAQEDITMICVTHEMGfARQVADRVIFMEDGRI 216
Cdd:NF038007 160 PALLLADEPTGNLDSKNARAVLQQLKYINQKGTTIIMVTHSDE-ASTYGNRIINMKDGKL 218
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
6-221 |
1.14e-44 |
|
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: 149.60 E-value: 1.14e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 6 EIKHLNKYFGDLHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPLTKKNHLEMARKYSSMVF 85
Cdd:TIGR03410 2 EVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERARAGIAYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 86 QQFNLYPNMTVLGNLTLAPIKLQKKSKEEATEI--AIAALKRVgMAHKAGeypqNLSGGQQQRIAIARALCTKQPIILFD 163
Cdd:TIGR03410 82 QGREIFPRLTVEENLLTGLAALPRRSRKIPDEIyeLFPVLKEM-LGRRGG----DLSGGQQQQLAIARALVTRPKLLLLD 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1469315281 164 EPTSALDPEMVQEVLDVMIELAQE-DITMICVTHEMGFARQVADRVIFMEDGRILEEGT 221
Cdd:TIGR03410 157 EPTEGIQPSIIKDIGRVIRRLRAEgGMAILLVEQYLDFARELADRYYVMERGRVVASGA 215
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-230 |
1.82e-44 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 152.69 E-value: 1.82e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 1 MAdMIEIKHLNK-YFGDLHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPLtkkNHLEMARK 79
Cdd:PRK11650 1 MA-GLKLQAVRKsYDGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVV---NELEPADR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 80 YSSMVFQQFNLYPNMTVLGNLTLApIKLQKKSKEeatEIAiaalKRVGMAHKA---GEY----PQNLSGGQQQRIAIARA 152
Cdd:PRK11650 77 DIAMVFQNYALYPHMSVRENMAYG-LKIRGMPKA---EIE----ERVAEAARIlelEPLldrkPRELSGGQRQRVAMGRA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 153 LCTKQPIILFDEPTSALDPEM-VQ---EVLDVMIELAQediTMICVTHEMGFARQVADRVIFMEDGRILEEGTPEHFFDN 228
Cdd:PRK11650 149 IVREPAVFLFDEPLSNLDAKLrVQmrlEIQRLHRRLKT---TSLYVTHDQVEAMTLADRVVVMNGGVAEQIGTPVEVYEK 225
|
..
gi 1469315281 229 PE 230
Cdd:PRK11650 226 PA 227
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1-224 |
7.71e-44 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 156.04 E-value: 7.71e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 1 MADMIEIKHLNKYF----GDLHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPLTKKNHLEM 76
Cdd:PRK10535 1 MTALLELKDIRRSYpsgeEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 77 A---RKYSSMVFQQFNLYPNMTVLGNLTLaPIKLQKKSKEEATEIAIAALKRVGMAHKAGEYPQNLSGGQQQRIAIARAL 153
Cdd:PRK10535 81 AqlrREHFGFIFQRYHLLSHLTAAQNVEV-PAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARAL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1469315281 154 CTKQPIILFDEPTSALDPEMVQEVLDVMIELAQEDITMICVTHEMGFARQvADRVIFMEDGRILEEGTPEH 224
Cdd:PRK10535 160 MNGGQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHDPQVAAQ-AERVIEIRDGEIVRNPPAQE 229
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
5-220 |
8.70e-44 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 146.59 E-value: 8.70e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 5 IEIKHLNKYFGDLHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGtPLTKKNHlEMARKYSSMV 84
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDG-KSYQKNI-EALRRIGALI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 85 FQQfNLYPNMTVLGNLTLAPiKLQKKSKEEATEIaiaaLKRVGMAHKAGEYPQNLSGGQQQRIAIARALCTKQPIILFDE 164
Cdd:cd03268 79 EAP-GFYPNLTARENLRLLA-RLLGIRKKRIDEV----LDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDE 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1469315281 165 PTSALDPEMVQEVLDVMIELAQEDITMICVTHEMGFARQVADRVIFMEDGRILEEG 220
Cdd:cd03268 153 PTNGLDPDGIKELRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1-230 |
1.96e-43 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 147.93 E-value: 1.96e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 1 MADMIEIKHLN-KYFGD-----LHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPLTKKNHL 74
Cdd:PRK13633 1 MNEMIKCKNVSyKYESNeesteKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 75 EMARKYSSMVFQQfnlyPNMTVLG------------NLTLAPIKLQKKSKEeateiaiaALKRVGMAHKAGEYPQNLSGG 142
Cdd:PRK13633 81 WDIRNKAGMVFQN----PDNQIVAtiveedvafgpeNLGIPPEEIRERVDE--------SLKKVGMYEYRRHAPHLLSGG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 143 QQQRIAIARALCTKQPIILFDEPTSALDPEMVQEVLDVMIELAQED-ITMICVTHEMGFARQvADRVIFMEDGRILEEGT 221
Cdd:PRK13633 149 QKQRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYgITIILITHYMEEAVE-ADRIIVMDSGKVVMEGT 227
|
....*....
gi 1469315281 222 PEHFFDNPE 230
Cdd:PRK13633 228 PKEIFKEVE 236
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
4-241 |
2.32e-43 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 147.44 E-value: 2.32e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 4 MIEIKHLN-KYFGD-LHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPLTKKNhLEMARKYS 81
Cdd:PRK13632 7 MIKVENVSfSYPNSeNNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKEN-LKEIRKKI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 82 SMVFQQ-FNLYPNMTV-------LGNLTLAPIKLQKKSKEEAteiaiaalKRVGMAHKAGEYPQNLSGGQQQRIAIARAL 153
Cdd:PRK13632 86 GIIFQNpDNQFIGATVeddiafgLENKKVPPKKMKDIIDDLA--------KKVGMEDYLDKEPQNLSGGQKQRVAIASVL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 154 CTKQPIILFDEPTSALDPEMVQEVLDVMIELAQE-DITMICVTHEMGFARQvADRVIFMEDGRILEEGTPEHFFDNpenp 232
Cdd:PRK13632 158 ALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTrKKTLISITHDMDEAIL-ADKVIVFSEGKLIAQGKPKEILNN---- 232
|
....*....
gi 1469315281 233 rcREFLSKI 241
Cdd:PRK13632 233 --KEILEKA 239
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
4-239 |
4.03e-43 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 146.46 E-value: 4.03e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 4 MIEIKHLNKYFGDLHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYL-----EEPTSGEVLIDG----TPLTKKNHL 74
Cdd:PRK14239 5 ILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndlnpEVTITGSIVYNGhniySPRTDTVDL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 75 emaRKYSSMVFQQFNLYPnMTVLGN----LTLAPIKlQKKSKEEATEiaiAALKRVGMAHKAGEYPQN----LSGGQQQR 146
Cdd:PRK14239 85 ---RKEIGMVFQQPNPFP-MSIYENvvygLRLKGIK-DKQVLDEAVE---KSLKGASIWDEVKDRLHDsalgLSGGQQQR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 147 IAIARALCTKQPIILFDEPTSALDPEMVQEVLDVMIELaQEDITMICVTHEMGFARQVADRVIFMEDGRILEEGTPEHFF 226
Cdd:PRK14239 157 VCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGL-KDDYTMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQMF 235
|
250
....*....|...
gi 1469315281 227 DNPENPRCREFLS 239
Cdd:PRK14239 236 MNPKHKETEDYIS 248
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
17-239 |
4.21e-43 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 148.19 E-value: 4.21e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 17 LHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPLTKKNHLEMA--RKYSSMVFQqfNLY--- 91
Cdd:PRK11308 28 VKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAQKllRQKIQIVFQ--NPYgsl 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 92 -PNMTVlGNLTLAPIKLQKK-SKEEATEIAIAALKRVGM-AHKAGEYPQNLSGGQQQRIAIARALCTKQPIILFDEPTSA 168
Cdd:PRK11308 106 nPRKKV-GQILEEPLLINTSlSAAERREKALAMMAKVGLrPEHYDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSA 184
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1469315281 169 LDPEMVQEVLDVMIELAQE-DITMICVTHEMGFARQVADRVIFMEDGRILEEGTPEHFFDNPENPRCREFLS 239
Cdd:PRK11308 185 LDVSVQAQVLNLMMDLQQElGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFNNPRHPYTQALLS 256
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
12-223 |
7.14e-43 |
|
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin resistance ABC transporter, ATP binding subunit in bacteria and archaea. This model is restricted in its scope to preferentially recognize the ATP binding subunit associated with effux of the drug, daunorubicin. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. In eukaryotes proteins of similar function include p-gyco proteins, multidrug resistance protein etc. [Transport and binding proteins, Other]
Pssm-ID: 130256 [Multi-domain] Cd Length: 302 Bit Score: 147.15 E-value: 7.14e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 12 KYFGDLHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPLTKKNhlEMARKYSSMVFQQFNLY 91
Cdd:TIGR01188 1 KVYGDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVVREP--RKVRRSIGIVPQYASVD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 92 PNMTVLGNLTLAPiKLQKKSKEEATEIAIAALKRVGMAHKAGEYPQNLSGGQQQRIAIARALCTkQPIILF-DEPTSALD 170
Cdd:TIGR01188 79 EDLTGRENLEMMG-RLYGLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIH-QPDVLFlDEPTTGLD 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1469315281 171 PEMVQEVLDVMIELAQEDITMICVTHEMGFARQVADRVIFMEDGRILEEGTPE 223
Cdd:TIGR01188 157 PRTRRAIWDYIRALKEEGVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPE 209
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-223 |
7.91e-43 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 151.33 E-value: 7.91e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 1 MADMIEIKHLNKYFGDLHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVdY-LEEPTSGEVLIDGTPLTKKNHLEmARK 79
Cdd:COG3845 2 MPPALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKIL-YgLYQPDSGEILIDGKPVRIRSPRD-AIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 80 YS-SMVFQQFNLYPNMTVLGNLTLA--PIKLQKKSKEEATEIAIAALKRVGMAHKAGEYPQNLSGGQQQRIAIARALCTK 156
Cdd:COG3845 80 LGiGMVHQHFMLVPNLTVAENIVLGlePTKGGRLDRKAARARIRELSERYGLDVDPDAKVEDLSVGEQQRVEILKALYRG 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1469315281 157 QPIILFDEPTSALDPEMVQEVLDVMIELAQEDITMICVTHEMGFARQVADRVIFMEDGRILEEGTPE 223
Cdd:COG3845 160 ARILILDEPTAVLTPQEADELFEILRRLAAEGKSIIFITHKLREVMAIADRVTVLRRGKVVGTVDTA 226
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
3-219 |
9.74e-43 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 144.54 E-value: 9.74e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 3 DMIEIKHLNKYFGD----LHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPLTKKNHLEMAR 78
Cdd:PRK10584 5 NIVEVHHLKKSVGQgeheLSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 79 ---KYSSMVFQQFNLYPNMTVLGNLTLaPIKLQKKSKEEATEIAIAALKRVGMAHKAGEYPQNLSGGQQQRIAIARALCT 155
Cdd:PRK10584 85 lraKHVGFVFQSFMLIPTLNALENVEL-PALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNG 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1469315281 156 kQPIILF-DEPTSALDPEMVQEVLDVMIELAQE-DITMICVTHEMGFARQvADRVIFMEDGRILEE 219
Cdd:PRK10584 164 -RPDVLFaDEPTGNLDRQTGDKIADLLFSLNREhGTTLILVTHDLQLAAR-CDRRLRLVNGQLQEE 227
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
5-227 |
1.60e-42 |
|
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: 143.91 E-value: 1.60e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 5 IEIKHLN-KYFGDLHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPLTKKNHLEMaRKYSSM 83
Cdd:cd03254 3 IEFENVNfSYDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSL-RSMIGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 84 VFQQFNLYPNmTVLGNLTLapiklqkkSKEEAT-EIAIAALKRVGMAH-----------KAGEYPQNLSGGQQQRIAIAR 151
Cdd:cd03254 82 VLQDTFLFSG-TIMENIRL--------GRPNATdEEVIEAAKEAGAHDfimklpngydtVLGENGGNLSQGERQLLAIAR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1469315281 152 ALCTKQPIILFDEPTSALDPEMVQEVLDVMIELaQEDITMICVTHEMGFARQvADRVIFMEDGRILEEGTPEHFFD 227
Cdd:cd03254 153 AMLRDPKILILDEATSNIDTETEKLIQEALEKL-MKGRTSIIIAHRLSTIKN-ADKILVLDDGKIIEEGTHDELLA 226
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-215 |
2.82e-42 |
|
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: 143.34 E-value: 2.82e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 1 MADMIEIKHLNKYFgDLH--------VLKDINLTVKRGEKLVMIGPSGSGKSTLIRCV--DYLeePTSGEVLIDgtplTK 70
Cdd:COG4778 1 MTTLLEVENLSKTF-TLHlqggkrlpVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIygNYL--PDSGSILVR----HD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 71 KNHLEMA----------RK----YSSmvfqQF-NLYPNMTVLgNLTLAPIKLQKKSKEEATEIAIAALKRVGMAHK-AGE 134
Cdd:COG4778 74 GGWVDLAqaspreilalRRrtigYVS----QFlRVIPRVSAL-DVVAEPLLERGVDREEARARARELLARLNLPERlWDL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 135 YPQNLSGGQQQRIAIARALCTKQPIILFDEPTSALDPEMVQEVLDVMIELAQEDITMICVTHEMGFARQVADRVIFMEDG 214
Cdd:COG4778 149 PPATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVREAVADRVVDVTPF 228
|
.
gi 1469315281 215 R 215
Cdd:COG4778 229 S 229
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1-230 |
8.55e-42 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 142.82 E-value: 8.55e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 1 MADMIEIKHLNKYFGDLHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPLTKKNHLEMARKY 80
Cdd:PRK11300 2 SQPLLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIARMG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 81 SSMVFQQFNLYPNMTVLGNLTLAP------------IKLQ--KKSKEEATEIAIAALKRVGMAHKAGEYPQNLSGGQQQR 146
Cdd:PRK11300 82 VVRTFQHVRLFREMTVIENLLVAQhqqlktglfsglLKTPafRRAESEALDRAATWLERVGLLEHANRQAGNLAYGQQRR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 147 IAIARALCTKQPIILFDEPTSALDPEMVQEVLDVMIELAQE-DITMICVTHEMGFARQVADRVIFMEDGRILEEGTPEHF 225
Cdd:PRK11300 162 LEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEhNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEI 241
|
....*
gi 1469315281 226 FDNPE 230
Cdd:PRK11300 242 RNNPD 246
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
22-232 |
1.40e-41 |
|
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: 144.87 E-value: 1.40e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 22 DINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPL---TKKNHLEMARKYSSMVFQQFNLYPNMTVLG 98
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLfdsRKGIFLPPEKRRIGYVFQEARLFPHLSVRG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 99 NLTLApiklQKKSKEEATEIAIAALKRV-GMAHKAGEYPQNLSGGQQQRIAIARALCTKQPIILFDEPTSALDPEMVQEV 177
Cdd:TIGR02142 95 NLRYG----MKRARPSERRISFERVIELlGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEI 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1469315281 178 LDVMIELAQE-DITMICVTHEMGFARQVADRVIFMEDGRILEEGTPEHFFDNPENP 232
Cdd:TIGR02142 171 LPYLERLHAEfGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPDLP 226
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-226 |
1.68e-41 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 142.95 E-value: 1.68e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 1 MADMIEIKHLN-KYFGDL--HVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPLTKKNHLEMA 77
Cdd:PRK13650 1 MSNIIEVKNLTfKYKEDQekYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 78 RKYsSMVFQQ-FNLYPNMTVLGNLTLApikLQKK--SKEEATEIAIAALKRVGMAHKAGEYPQNLSGGQQQRIAIARALC 154
Cdd:PRK13650 81 HKI-GMVFQNpDNQFVGATVEDDVAFG---LENKgiPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1469315281 155 TKQPIILFDEPTSALDPEMVQEVLDVMIELAQE-DITMICVTHEMGfarQVA--DRVIFMEDGRILEEGTPEHFF 226
Cdd:PRK13650 157 MRPKIIILDEATSMLDPEGRLELIKTIKGIRDDyQMTVISITHDLD---EVAlsDRVLVMKNGQVESTSTPRELF 228
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
20-214 |
6.93e-41 |
|
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: 139.91 E-value: 6.93e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 20 LKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPLTKKNHLEMarkyssMVFQQFNLYPNMTVLGN 99
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRM------VVFQNYSLLPWLTVREN 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 100 LTLAPIK-LQKKSKEEATEIAIAALKRVGMAHKAGEYPQNLSGGQQQRIAIARALCTKQPIILFDEPTSALDPEMVQEVL 178
Cdd:TIGR01184 75 IALAVDRvLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQ 154
|
170 180 190
....*....|....*....|....*....|....*..
gi 1469315281 179 DVMIELAQED-ITMICVTHEMGFARQVADRVIFMEDG 214
Cdd:TIGR01184 155 EELMQIWEEHrVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
5-223 |
7.18e-41 |
|
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: 140.06 E-value: 7.18e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 5 IEIKHLN-KYFGDLHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPLTKKNhLEMARKYSSM 83
Cdd:cd03253 1 IEFENVTfAYDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVT-LDSLRRAIGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 84 VFQQFNLYpNMTVLGNLtlapiklqKKSKEEATEIAIAALKRVGMAH------------KAGEYPQNLSGGQQQRIAIAR 151
Cdd:cd03253 80 VPQDTVLF-NDTIGYNI--------RYGRPDATDEEVIEAAKAAQIHdkimrfpdgydtIVGERGLKLSGGEKQRVAIAR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1469315281 152 ALCTKQPIILFDEPTSALDPEMVQEVLDVMIELAQeDITMICVTHEMgfaRQV--ADRVIFMEDGRILEEGTPE 223
Cdd:cd03253 151 AILKNPPILLLDEATSALDTHTEREIQAALRDVSK-GRTTIVIAHRL---STIvnADKIIVLKDGRIVERGTHE 220
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
20-230 |
9.09e-41 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 141.31 E-value: 9.09e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 20 LKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPLT--KKN-HLEMARKYSSMVFQ--QFNLYPNm 94
Cdd:PRK13634 23 LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITagKKNkKLKPLRKKVGIVFQfpEHQLFEE- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 95 TVLGNLTLAPIKLqKKSKEEATEIAIAALKRVGMAHKAGEY-PQNLSGGQQQRIAIARALCTKQPIILFDEPTSALDPEM 173
Cdd:PRK13634 102 TVEKDICFGPMNF-GVSEEDAKQKAREMIELVGLPEELLARsPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKG 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1469315281 174 VQEVLDVMIELAQE-DITMICVTHEMGFARQVADRVIFMEDGRILEEGTPEHFFDNPE 230
Cdd:PRK13634 181 RKEMMEMFYKLHKEkGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADPD 238
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
5-220 |
9.43e-41 |
|
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: 138.95 E-value: 9.43e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 5 IEIKHLNKYFGDLHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPLTkknhlEMARKYSSMV 84
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLD-----IAARNRIGYL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 85 FQQFNLYPNMTVLGNLT-LApiKLQKKSKEEATEIAIAALKRVGMAHKAGEYPQNLSGGQQQRIAIARALCTKQPIILFD 163
Cdd:cd03269 76 PEERGLYPKMKVIDQLVyLA--QLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILD 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1469315281 164 EPTSALDPEMVQEVLDVMIELAQEDITMICVTHEMGFARQVADRVIFMEDGRILEEG 220
Cdd:cd03269 154 EPFSGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
5-220 |
1.50e-40 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 138.48 E-value: 1.50e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 5 IEIKHLNKYFGDLHVLKDINLTVKRGeKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPLTKknHLEMARKYSSMV 84
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLK--QPQKLRRRIGYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 85 FQQFNLYPNMTVLGNLTLAPIkLQKKSKEEATEIAIAALKRVGMAHKAGEYPQNLSGGQQQRIAIARALCTKQPIILFDE 164
Cdd:cd03264 78 PQEFGVYPNFTVREFLDYIAW-LKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1469315281 165 PTSALDPEMVQEVLDVMIELAQEDITMICvTHEMGFARQVADRVIFMEDGRILEEG 220
Cdd:cd03264 157 PTAGLDPEERIRFRNLLSELGEDRIVILS-THIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
4-230 |
1.80e-40 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 140.32 E-value: 1.80e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 4 MIEIKHL-NKYFGDLHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPLTKKNHLEMaRKYSS 82
Cdd:PRK13652 3 LIETRDLcYSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREV-RKFVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 83 MVFQQFN---LYPnmTVLGNLTLAPIKLQKKSKEEATEIAiAALKRVGMAHKAGEYPQNLSGGQQQRIAIARALCTKQPI 159
Cdd:PRK13652 82 LVFQNPDdqiFSP--TVEQDIAFGPINLGLDEETVAHRVS-SALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQV 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1469315281 160 ILFDEPTSALDPEMVQEVLDVMIELAQE-DITMICVTHEMGFARQVADRVIFMEDGRILEEGTPEHFFDNPE 230
Cdd:PRK13652 159 LVLDEPTAGLDPQGVKELIDFLNDLPETyGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQPD 230
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
5-221 |
2.12e-40 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 138.52 E-value: 2.12e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 5 IEIKHLN-KYFGDLH-VLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPLtKKNHLEMARKYSS 82
Cdd:cd03251 1 VEFKNVTfRYPGDGPpVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDV-RDYTLASLRRQIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 83 MVFQQFNLYpNMTVLGNLTLApiklqkksKEEATEIAIAALKRVGMAH------------KAGEYPQNLSGGQQQRIAIA 150
Cdd:cd03251 80 LVSQDVFLF-NDTVAENIAYG--------RPGATREEVEEAARAANAHefimelpegydtVIGERGVKLSGGQRQRIAIA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1469315281 151 RALCTKQPIILFDEPTSALDPE---MVQEVLDvmiELaQEDITMICVTHEMGFARQvADRVIFMEDGRILEEGT 221
Cdd:cd03251 151 RALLKDPPILILDEATSALDTEserLVQAALE---RL-MKNRTTFVIAHRLSTIEN-ADRIVVLEDGKIVERGT 219
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
5-223 |
4.30e-40 |
|
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: 137.50 E-value: 4.30e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 5 IEIKHLNKYFGDLHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPLTKKNhlEMARKYSSMV 84
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREP--REVRRRIGIV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 85 FQQFNLYPNMTVLGNLTLAPiKLQKKSKEEATEIAIAALKRVGMAHKAGEYPQNLSGGQQQRIAIARALcTKQPIILF-D 163
Cdd:cd03265 79 FQDLSVDDELTGWENLYIHA-RLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSL-VHRPEVLFlD 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1469315281 164 EPTSALDPEMVQEVLDVMIEL-AQEDITMICVTHEMGFARQVADRVIFMEDGRILEEGTPE 223
Cdd:cd03265 157 EPTIGLDPQTRAHVWEYIEKLkEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPE 217
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
15-221 |
1.34e-39 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 136.48 E-value: 1.34e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 15 GDLH--VLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPLTK---KNHLEMARKYSSMVFQQFN 89
Cdd:PRK11629 18 GSVQtdVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKlssAAKAELRNQKLGFIYQFHH 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 90 LYPNMTVLGNLTLaPIKLQKKSKEEATEIAIAALKRVGMAHKAGEYPQNLSGGQQQRIAIARALCTKQPIILFDEPTSAL 169
Cdd:PRK11629 98 LLPDFTALENVAM-PLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNL 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1469315281 170 DPEMVQEVLDVMIEL-AQEDITMICVTHEMGFARQVaDRVIFMEDGRILEEGT 221
Cdd:PRK11629 177 DARNADSIFQLLGELnRLQGTAFLVVTHDLQLAKRM-SRQLEMRDGRLTAELS 228
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
19-223 |
3.72e-39 |
|
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: 135.74 E-value: 3.72e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 19 VLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPLtKKNHLEMARKYSSMVFQQFNLYpNMTVLG 98
Cdd:cd03249 18 ILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDI-RDLNLRWLRSQIGLVSQEPVLF-DGTIAE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 99 NLTLapiklqkkSKEEATEIAIAALKRVGMAHK------------AGEYPQNLSGGQQQRIAIARALCTKQPIILFDEPT 166
Cdd:cd03249 96 NIRY--------GKPDATDEEVEEAAKKANIHDfimslpdgydtlVGERGSQLSGGQKQRIAIARALLRNPKILLLDEAT 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 167 SALDPE---MVQEVLDvmieLAQEDITMICVTHEMGfARQVADRVIFMEDGRILEEGTPE 223
Cdd:cd03249 168 SALDAEsekLVQEALD----RAMKGRTTIVIAHRLS-TIRNADLIAVLQNGQVVEQGTHD 222
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
20-230 |
5.31e-39 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 136.72 E-value: 5.31e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 20 LKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPLTKKN-HLEMARKYSSMVFQqfnlYPNM---- 94
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKvKLSDIRKKVGLVFQ----YPEYqlfe 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 95 -TVLGNLTLAPIKLqKKSKEEATEIAIAALKRVGMAHK--AGEYPQNLSGGQQQRIAIARALCTKQPIILFDEPTSALDP 171
Cdd:PRK13637 99 eTIEKDIAFGPINL-GLSEEEIENRVKRAMNIVGLDYEdyKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDP 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 172 EMVQEVLDVMIELAQE-DITMICVTHEMGFARQVADRVIFMEDGRILEEGTPEHFFDNPE 230
Cdd:PRK13637 178 KGRDEILNKIKELHKEyNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVFKEVE 237
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
4-241 |
9.16e-39 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 137.14 E-value: 9.16e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 4 MIEIKHLNKYFG-------------DLHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPLTK 70
Cdd:PRK15079 8 LLEVADLKVHFDikdgkqwfwqppkTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 71 KNHLEM--ARKYSSMVFQQ--FNLYPNMTVlGNLTLAPIKL--QKKSKEEATEIAIAALKRVGM-AHKAGEYPQNLSGGQ 143
Cdd:PRK15079 88 MKDDEWraVRSDIQMIFQDplASLNPRMTI-GEIIAEPLRTyhPKLSRQEVKDRVKAMMLKVGLlPNLINRYPHEFSGGQ 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 144 QQRIAIARALCTKQPIILFDEPTSALDPEMVQEVLDVMIELAQE-DITMICVTHEMGFARQVADRVIFMEDGRILEEGTP 222
Cdd:PRK15079 167 CQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTY 246
|
250
....*....|....*....
gi 1469315281 223 EHFFDNPENPRCREFLSKI 241
Cdd:PRK15079 247 DEVYHNPLHPYTKALMSAV 265
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
3-230 |
1.27e-38 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 135.70 E-value: 1.27e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 3 DMIEIKHLNKYFGDLH--VLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGE---VLIDGTPLTKKNHLEMa 77
Cdd:PRK13640 4 NIVEFKHVSFTYPDSKkpALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPnskITVDGITLTAKTVWDI- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 78 RKYSSMVFQQ-FNLYPNMTVLGNLTLApIKLQKKSKEEATEIAIAALKRVGMAHKAGEYPQNLSGGQQQRIAIARALCTK 156
Cdd:PRK13640 83 REKVGIVFQNpDNQFVGATVGDDVAFG-LENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVE 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1469315281 157 QPIILFDEPTSALDPEMVQEVLDVMIELAQE-DITMICVTHEMGFARQvADRVIFMEDGRILEEGTPEHFFDNPE 230
Cdd:PRK13640 162 PKIIILDESTSMLDPAGKEQILKLIRKLKKKnNLTVISITHDIDEANM-ADQVLVLDDGKLLAQGSPVEIFSKVE 235
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
4-223 |
1.39e-38 |
|
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: 134.44 E-value: 1.39e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 4 MIEIKHLNKYFGDLHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSG-EVLIDGTPLTKKNHLEMARK--Y 80
Cdd:COG1119 3 LLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRGGEDVWELRKRigL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 81 SSMVFQQfNLYPNMTVLgNLTL----APIKLQKKSKEEATEIAIAALKRVGMAHKAGEYPQNLSGGQQQRIAIARALCTK 156
Cdd:COG1119 83 VSPALQL-RFPRDETVL-DVVLsgffDSIGLYREPTDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIARALVKD 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1469315281 157 QPIILFDEPTSALDPEMVQEVLDVMIELAQE-DITMICVTH---EM--GFarqvaDRVIFMEDGRILEEGTPE 223
Cdd:COG1119 161 PELLILDEPTAGLDLGARELLLALLDKLAAEgAPTLVLVTHhveEIppGI-----THVLLLKDGRVVAAGPKE 228
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
18-220 |
2.23e-38 |
|
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: 133.10 E-value: 2.23e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 18 HVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPLTKKNHLEMaRKYSSMVFQQFNLYpNMTVL 97
Cdd:cd03245 18 PALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADL-RRNIGYVPQDVTLF-YGTLR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 98 GNLTLAPIKLQKKSKEEATEIA----IAALKRVGMAHKAGEYPQNLSGGQQQRIAIARALCTKQPIILFDEPTSALDPEM 173
Cdd:cd03245 96 DNITLGAPLADDERILRAAELAgvtdFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPPILLLDEPTSAMDMNS 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1469315281 174 VQEVLDVMIELAqEDITMICVTHEMGFArQVADRVIFMEDGRILEEG 220
Cdd:cd03245 176 EERLKERLRQLL-GDKTLIIITHRPSLL-DLVDRIIVMDSGRIVADG 220
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
4-233 |
2.31e-38 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 134.98 E-value: 2.31e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 4 MIEIKHLNKYFGD-LHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPL--TKKNHLEMaRKY 80
Cdd:PRK13636 5 ILKVEELNYNYSDgTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIdySRKGLMKL-RES 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 81 SSMVFQQ-FNLYPNMTVLGNLTLAPIKLQKkSKEEATEIAIAALKRVGMAHKAGEYPQNLSGGQQQRIAIARALCTKQPI 159
Cdd:PRK13636 84 VGMVFQDpDNQLFSASVYQDVSFGAVNLKL-PEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKV 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1469315281 160 ILFDEPTSALDPEMVQEVLDVMIELAQE-DITMICVTHEMGFARQVADRVIFMEDGRILEEGTPEHFFDNPENPR 233
Cdd:PRK13636 163 LVLDEPTAGLDPMGVSEIMKLLVEMQKElGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFAEKEMLR 237
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
5-230 |
2.38e-38 |
|
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: 133.44 E-value: 2.38e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 5 IEIKHLNKYFGDLHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPLTKKNHLEMARKYSSMV 84
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRARLGIGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 85 FQQFNLYPNMTVLGNLtLAPIKLQKKSKEEATEIAIAALKRVGMAHKAGEYPQNLSGGQQQRIAIARALCTKQPIILFDE 164
Cdd:cd03218 81 PQEASIFRKLTVEENI-LAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1469315281 165 PTSALDPEMVQEVLDVMIELAQEDITMICVTHEMGFARQVADRVIFMEDGRILEEGTPEHFFDNPE 230
Cdd:cd03218 160 PFAGVDPIAVQDIQKIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANEL 225
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
3-223 |
2.46e-38 |
|
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: 139.55 E-value: 2.46e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 3 DMIEIKHLNKYF-----GDLHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLI----DGTPLTKKNH 73
Cdd:TIGR03269 278 PIIKVRNVSKRYisvdrGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdEWVDMTKPGP 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 74 LEMAR--KYSSMVFQQFNLYPNMTVLGNLTLApIKLQKkSKEEATEIAIAALKRVGMAHKAGE-----YPQNLSGGQQQR 146
Cdd:TIGR03269 358 DGRGRakRYIGILHQEYDLYPHRTVLDNLTEA-IGLEL-PDELARMKAVITLKMVGFDEEKAEeildkYPDELSEGERHR 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 147 IAIARALCTKQPIILFDEPTSALDP----EMVQEVLDVMIELAQediTMICVTHEMGFARQVADRVIFMEDGRILEEGTP 222
Cdd:TIGR03269 436 VALAQVLIKEPRIVILDEPTGTMDPitkvDVTHSILKAREEMEQ---TFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDP 512
|
.
gi 1469315281 223 E 223
Cdd:TIGR03269 513 E 513
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
4-213 |
2.46e-38 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 132.61 E-value: 2.46e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 4 MIEIKHLNKYFGDLHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCV-DYLEEP--TSGEVLIDGTPLTkknHLEMARKY 80
Cdd:COG4136 1 MLSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIaGTLSPAfsASGEVLLNGRRLT---ALPAEQRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 81 SSMVFQQFNLYPNMTVLGNLTLA-PIKLQKKSKEEAteiAIAALKRVGMAHKAGEYPQNLSGGQQQRIAIARALCTKQPI 159
Cdd:COG4136 78 IGILFQDDLLFPHLSVGENLAFAlPPTIGRAQRRAR---VEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRA 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1469315281 160 ILFDEPTSALDPEMVQEVLD-VMIELAQEDITMICVTHEMGfARQVADRVIFMED 213
Cdd:COG4136 155 LLLDEPFSKLDAALRAQFREfVFEQIRQRGIPALLVTHDEE-DAPAAGRVLDLGN 208
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
15-221 |
3.88e-38 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 139.57 E-value: 3.88e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 15 GDLHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPLTKKNhlEMA-RKYSSMVFQQFNLYpN 93
Cdd:PRK11160 351 QPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYS--EAAlRQAISVVSQRVHLF-S 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 94 MTVLGNLTLApiklqkksKEEAT-EIAIAALKRVGMAHKA----------GEYPQNLSGGQQQRIAIARALCTKQPIILF 162
Cdd:PRK11160 428 ATLRDNLLLA--------APNASdEALIEVLQQVGLEKLLeddkglnawlGEGGRQLSGGEQRRLGIARALLHDAPLLLL 499
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1469315281 163 DEPTSALDPEMVQEVLDVMIELAQeDITMICVTHemgfaRQVA----DRVIFMEDGRILEEGT 221
Cdd:PRK11160 500 DEPTEGLDAETERQILELLAEHAQ-NKTVLMITH-----RLTGleqfDRICVMDNGQIIEQGT 556
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
1-223 |
8.31e-38 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 133.32 E-value: 8.31e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 1 MADMIEIKHLNKYFGD-LHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPLTKKNHLEMaRK 79
Cdd:PRK13647 1 MDNIIEVEDLHFRYKDgTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWV-RS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 80 YSSMVFQQfnlyPN-----MTVLGNLTLAPIKLqKKSKEEATEIAIAALKRVGM---AHKAgeyPQNLSGGQQQRIAIAR 151
Cdd:PRK13647 80 KVGLVFQD----PDdqvfsSTVWDDVAFGPVNM-GLDKDEVERRVEEALKAVRMwdfRDKP---PYHLSYGQKKRVAIAG 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1469315281 152 ALCTKQPIILFDEPTSALDPEMVQEVLDVMIELAQEDITMICVTHEMGFARQVADRVIFMEDGRILEEGTPE 223
Cdd:PRK13647 152 VLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKS 223
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
13-201 |
8.45e-38 |
|
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 130234 [Multi-domain] Cd Length: 190 Bit Score: 130.62 E-value: 8.45e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 13 YFGDLHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPL--TKKNHLEmARKYSSMVFQQFN- 89
Cdd:TIGR01166 1 YPGGPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPLdySRKGLLE-RRQRVGLVFQDPDd 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 90 --LYPnmTVLGNLTLAPIKLqKKSKEEATEIAIAALKRVGMAHKAGEYPQNLSGGQQQRIAIARALCTKQPIILFDEPTS 167
Cdd:TIGR01166 80 qlFAA--DVDQDVAFGPLNL-GLSEAEVERRVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTA 156
|
170 180 190
....*....|....*....|....*....|....
gi 1469315281 168 ALDPEMVQEVLDVMIELAQEDITMICVTHEMGFA 201
Cdd:TIGR01166 157 GLDPAGREQMLAILRRLRAEGMTVVISTHDVDLA 190
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
5-220 |
8.58e-38 |
|
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: 130.13 E-value: 8.58e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 5 IEIKHLNKYFG--DLHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPLTkkNHLEMARKYSS 82
Cdd:cd03247 1 LSINNVSFSYPeqEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVS--DLEKALSSLIS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 83 MVFQQFNLYpNMTVLGNLtlapiklqkkskeeateiaiaalkrvgmahkaGEypqNLSGGQQQRIAIARALCTKQPIILF 162
Cdd:cd03247 79 VLNQRPYLF-DTTLRNNL--------------------------------GR---RFSGGERQRLALARILLQDAPIVLL 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1469315281 163 DEPTSALDPEMVQEVLDVMIELAqEDITMICVTHEM-GFARqvADRVIFMEDGRILEEG 220
Cdd:cd03247 123 DEPTVGLDPITERQLLSLIFEVL-KDKTLIWITHHLtGIEH--MDKILFLENGKIIMQG 178
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
16-221 |
1.02e-37 |
|
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ATP transporter that exports lipid A and to eukaryotic P-glycoproteins.
Pssm-ID: 131259 [Multi-domain] Cd Length: 576 Bit Score: 138.68 E-value: 1.02e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 16 DLHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPLTKKNHLEMaRKYSSMVFQQFNLYPNmT 95
Cdd:TIGR02204 352 DQPALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDGVDLRQLDPAEL-RARMALVPQDPVLFAA-S 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 96 VLGNLTLAPIKLQKKSKEEATEIA-----IAALKRvGMAHKAGEYPQNLSGGQQQRIAIARALCTKQPIILFDEPTSALD 170
Cdd:TIGR02204 430 VMENIRYGRPDATDEEVEAAARAAhahefISALPE-GYDTYLGERGVTLSGGQRQRIAIARAILKDAPILLLDEATSALD 508
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1469315281 171 PEMVQEVLDVMIELAQEDITMIcVTHEMGFArQVADRVIFMEDGRILEEGT 221
Cdd:TIGR02204 509 AESEQLVQQALETLMKGRTTLI-IAHRLATV-LKADRIVVMDQGRIVAQGT 557
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
4-223 |
1.63e-37 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 135.35 E-value: 1.63e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 4 MIEIKHLNKYFGDLHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPLTKKNHLEMARKYSSm 83
Cdd:PRK09536 3 MIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVAS- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 84 VFQQFNLYPNMTVLGNLTLA--PIKLQKKSKEEATEIAI-AALKRVGMAHKAGEYPQNLSGGQQQRIAIARALCTKQPII 160
Cdd:PRK09536 82 VPQDTSLSFEFDVRQVVEMGrtPHRSRFDTWTETDRAAVeRAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1469315281 161 LFDEPTSALDPEMVQEVLDVMIELAQEDITMICVTHEMGFARQVADRVIFMEDGRILEEGTPE 223
Cdd:PRK09536 162 LLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPA 224
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
19-223 |
1.84e-37 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 138.55 E-value: 1.84e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 19 VLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPLTKKNhLEMARKYSSMVFQQFNLYPNmTVLG 98
Cdd:TIGR03797 468 ILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAGLD-VQAVRRQLGVVLQNGRLMSG-SIFE 545
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 99 NLTL-APIKLqkkskEEATEiaiaALKRVGMAHKAGEYP-----------QNLSGGQQQRIAIARALCTKQPIILFDEPT 166
Cdd:TIGR03797 546 NIAGgAPLTL-----DEAWE----AARMAGLAEDIRAMPmgmhtviseggGTLSGGQRQRLLIARALVRKPRILLFDEAT 616
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1469315281 167 SALDPEMvQEVldVMIELAQEDITMICVTHEMGFARQvADRVIFMEDGRILEEGTPE 223
Cdd:TIGR03797 617 SALDNRT-QAI--VSESLERLKVTRIVIAHRLSTIRN-ADRIYVLDAGRVVQQGTYD 669
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
5-221 |
2.98e-37 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 137.16 E-value: 2.98e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 5 IEIKHLNKYFG--DLHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPLTkknHLEMA--RKY 80
Cdd:TIGR02203 331 VEFRNVTFRYPgrDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLA---DYTLAslRRQ 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 81 SSMVFQQFNLYpNMTVLGNLTLApiKLQKKSKEEATEIAIAA-LKRV------GMAHKAGEYPQNLSGGQQQRIAIARAL 153
Cdd:TIGR02203 408 VALVSQDVVLF-NDTIANNIAYG--RTEQADRAEIERALAAAyAQDFvdklplGLDTPIGENGVLLSGGQRQRLAIARAL 484
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1469315281 154 CTKQPIILFDEPTSALDPE---MVQEVLDvmiELAQEDITMIcVTHEMGfARQVADRVIFMEDGRILEEGT 221
Cdd:TIGR02203 485 LKDAPILILDEATSALDNEserLVQAALE---RLMQGRTTLV-IAHRLS-TIEKADRIVVMDDGRIVERGT 550
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
4-216 |
3.15e-37 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 130.38 E-value: 3.15e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 4 MIEIKHLNK-YFGDLHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPLT--KKNHLEMARKY 80
Cdd:PRK10908 1 MIRFEHVSKaYLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITrlKNREVPFLRRQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 81 SSMVFQQFNLYPNMTVLGNLTLaPIKLQKKSKEEATEIAIAALKRVGMAHKAGEYPQNLSGGQQQRIAIARALCTKQPII 160
Cdd:PRK10908 81 IGMIFQDHHLLMDRTVYDNVAI-PLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1469315281 161 LFDEPTSALDPEMVQEVLDVMIELAQEDITMICVTHEMGFARQVADRVIFMEDGRI 216
Cdd:PRK10908 160 LADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1-241 |
3.31e-37 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 131.43 E-value: 3.31e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 1 MADMIEIKHLNKYFGDLHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDG--TPLTKKNHLEMAR 78
Cdd:PRK11831 4 VANLVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGenIPAMSRSRLYTVR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 79 KYSSMVFQQFNLYPNMTVLGNLTLaPIKLQKKSKEEATE-IAIAALKRVGMAHKAGEYPQNLSGGQQQRIAIARALCTKQ 157
Cdd:PRK11831 84 KRMSMLFQSGALFTDMNVFDNVAY-PLREHTQLPAPLLHsTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 158 PIILFDEPTSALDPemvqEVLDVMIELAQE-----DITMICVTHEMGFARQVADRVIFMEDGRILEEGTPEHFFDNPEnP 232
Cdd:PRK11831 163 DLIMFDEPFVGQDP----ITMGVLVKLISElnsalGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQANPD-P 237
|
....*....
gi 1469315281 233 RCREFLSKI 241
Cdd:PRK11831 238 RVRQFLDGI 246
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
4-223 |
6.09e-37 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 130.20 E-value: 6.09e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 4 MIEIKHLNKYFGDLHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPLTKKNHLEMARKYSsm 83
Cdd:COG4604 1 MIEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLA-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 84 VFQQFN-LYPNMTV--L----------GNLTlapiklqkKSKEEATEIAIAALKRVGMAHKageYPQNLSGGQQQRIAIA 150
Cdd:COG4604 79 ILRQENhINSRLTVreLvafgrfpyskGRLT--------AEDREIIDEAIAYLDLEDLADR---YLDELSGGQRQRAFIA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1469315281 151 RALCTKQPIILFDEPTSALDPEMVQEVLDVMIELAQE-DITMICVTHEMGFARQVADRVIFMEDGRILEEGTPE 223
Cdd:COG4604 148 MVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADElGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPE 221
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
4-242 |
7.47e-37 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 130.31 E-value: 7.47e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 4 MIEIKHLNKYF---------GDLHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPLTKKNHL 74
Cdd:TIGR02769 2 LLEVRDVTHTYrtgglfgakQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 75 EMA--RKYSSMVFQQ----FNlyPNMTVlGNLTLAPIK-LQKKSKEEATEIAIAALKRVGM-AHKAGEYPQNLSGGQQQR 146
Cdd:TIGR02769 82 QRRafRRDVQLVFQDspsaVN--PRMTV-RQIIGEPLRhLTSLDESEQKARIAELLDMVGLrSEDADKLPRQLSGGQLQR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 147 IAIARALCTKQPIILFDEPTSALDPEMVQEVLDVMIELAQE-DITMICVTHEMGFARQVADRVIFMEDGRILEEGTPEHF 225
Cdd:TIGR02769 159 INIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAfGTAYLFITHDLRLVQSFCQRVAVMDKGQIVEECDVAQL 238
|
250
....*....|....*..
gi 1469315281 226 FDNpENPRCREFLSKIL 242
Cdd:TIGR02769 239 LSF-KHPAGRNLQSAVL 254
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
20-230 |
8.62e-37 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 130.72 E-value: 8.62e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 20 LKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDG---TPLTKKNHLEMARKYSSMVFQ--QFNLYPNm 94
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGyhiTPETGNKNLKKLRKKVSLVFQfpEAQLFEN- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 95 TVLGNLTLAPIKLqKKSKEEATEIAIAALKRVGMAHK-AGEYPQNLSGGQQQRIAIARALCTKQPIILFDEPTSALDPEM 173
Cdd:PRK13641 102 TVLKDVEFGPKNF-GFSEDEAKEKALKWLKKVGLSEDlISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEG 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1469315281 174 VQEVLDVMIELAQEDITMICVTHEMGFARQVADRVIFMEDGRILEEGTPEHFFDNPE 230
Cdd:PRK13641 181 RKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDKE 237
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
4-230 |
9.67e-37 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 131.51 E-value: 9.67e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 4 MIEIKHLNKYFGD-----LHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLI--------------D 64
Cdd:PRK13631 21 ILRVKNLYCVFDEkqeneLVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVgdiyigdkknnhelI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 65 GTPLTKK-NHLEMARKYSSMVFQ--QFNLYPNmTVLGNLTLAPIKLqKKSKEEATEIAIAALKRVGMAHKAGEY-PQNLS 140
Cdd:PRK13631 101 TNPYSKKiKNFKELRRRVSMVFQfpEYQLFKD-TIEKDIMFGPVAL-GVKKSEAKKLAKFYLNKMGLDDSYLERsPFGLS 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 141 GGQQQRIAIARALCTKQPIILFDEPTSALDPEMVQEVLDVMIELAQEDITMICVTHEMGFARQVADRVIFMEDGRILEEG 220
Cdd:PRK13631 179 GGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTG 258
|
250
....*....|
gi 1469315281 221 TPEHFFDNPE 230
Cdd:PRK13631 259 TPYEIFTDQH 268
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
19-220 |
1.28e-36 |
|
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: 127.67 E-value: 1.28e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 19 VLKDINLTVKRGEKLVMIGPSGSGKSTLIRCV-DYLEEP-TSGEVLIDGTPLTKKNHlemaRKYSSMVFQQFNLYPNMTV 96
Cdd:cd03213 24 LLKNVSGKAKPGELTAIMGPSGAGKSTLLNALaGRRTGLgVSGEVLINGRPLDKRSF----RKIIGYVPQDDILHPTLTV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 97 lgnltlapiklqkkskEEATEIAiAALKrvgmahkageypqNLSGGQQQRIAIARALCTKQPIILFDEPTSALDPEMVQE 176
Cdd:cd03213 100 ----------------RETLMFA-AKLR-------------GLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQ 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1469315281 177 VLDVMIELAQEDITMICVTH----EMgFarQVADRVIFMEDGRILEEG 220
Cdd:cd03213 150 VMSLLRRLADTGRTIICSIHqpssEI-F--ELFDKLLLLSQGRVIYFG 194
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
16-229 |
2.16e-36 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 135.62 E-value: 2.16e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 16 DLHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPLTKKNHLEMARKYSSmVFQQFNLYpNMT 95
Cdd:TIGR00958 493 DVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVAL-VGQEPVLF-SGS 570
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 96 VLGNLTLApikLQKKSKEEATEIAIAALKR---VGMAH----KAGEYPQNLSGGQQQRIAIARALCTKQPIILFDEPTSA 168
Cdd:TIGR00958 571 VRENIAYG---LTDTPDEEIMAAAKAANAHdfiMEFPNgydtEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSA 647
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1469315281 169 LDPEMVQEVLDVMielAQEDITMICVTHEMGFARQvADRVIFMEDGRILEEGTPEHFFDNP 229
Cdd:TIGR00958 648 LDAECEQLLQESR---SRASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQLMEDQ 704
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
5-211 |
2.84e-36 |
|
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: 133.95 E-value: 2.84e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 5 IEIKHLN-KYFGDLHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPLTkknHLEMA--RKYS 81
Cdd:TIGR02857 322 LEFSGVSvAYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLA---DADADswRDQI 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 82 SMVFQQFNLYPNmTVLGNLTLApiklqkksKEEATEIAIA-ALKRVGMAH-----------KAGEYPQNLSGGQQQRIAI 149
Cdd:TIGR02857 399 AWVPQHPFLFAG-TIAENIRLA--------RPDASDAEIReALERAGLDEfvaalpqgldtPIGEGGAGLSGGQAQRLAL 469
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1469315281 150 ARALCTKQPIILFDEPTSALDPEMVQEVLDVMIELAQeDITMICVTHEMGFARqVADRVIFM 211
Cdd:TIGR02857 470 ARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQ-GRTVLLVTHRLALAA-LADRIVVL 529
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
5-223 |
5.88e-36 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 133.00 E-value: 5.88e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 5 IEIKHLNKYFGDLHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLE--EPTSGEVLI----------------DGT 66
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDqyEPTSGRIIYhvalcekcgyverpskVGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 67 P-----------------LTKKNHLEMARKYSSMVFQQFNLYPNMTVLGNLTLAPIKLQKKSKEeATEIAIAALKRVGMA 129
Cdd:TIGR03269 81 PcpvcggtlepeevdfwnLSDKLRRRIRKRIAIMLQRTFALYGDDTVLDNVLEALEEIGYEGKE-AVGRAVDLIEMVQLS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 130 HKAGEYPQNLSGGQQQRIAIARALcTKQPIILF-DEPTSALDPEMVQEVLDVMIELAQE-DITMICVTHEMGFARQVADR 207
Cdd:TIGR03269 160 HRITHIARDLSGGEKQRVVLARQL-AKEPFLFLaDEPTGTLDPQTAKLVHNALEEAVKAsGISMVLTSHWPEVIEDLSDK 238
|
250
....*....|....*.
gi 1469315281 208 VIFMEDGRILEEGTPE 223
Cdd:TIGR03269 239 AIWLENGEIKEEGTPD 254
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-216 |
7.76e-36 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 127.51 E-value: 7.76e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 4 MIEIKHLNKYFG-----DLHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPLTKKNhlEMAR 78
Cdd:COG1101 1 MLELKNLSKTFNpgtvnEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLP--EYKR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 79 -KYSSMVFQ--QFNLYPNMTVLGNLTLAPIK---------LQKKSKEEATEIaiaaLKRVG------MAHKAGeypqNLS 140
Cdd:COG1101 79 aKYIGRVFQdpMMGTAPSMTIEENLALAYRRgkrrglrrgLTKKRRELFREL----LATLGlglenrLDTKVG----LLS 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1469315281 141 GGQQQRIAIARALCTKQPIILFDEPTSALDPEMVQEVLDVMIELAQED-ITMICVTHEMGFARQVADRVIFMEDGRI 216
Cdd:COG1101 151 GGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENnLTTLMVTHNMEQALDYGNRLIMMHEGRI 227
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
3-231 |
1.61e-35 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 126.70 E-value: 1.61e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 3 DMIEIKHLNKYFGDLHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEE------PTSGEVLIDGTPLTKKNHLEM 76
Cdd:PRK14246 9 DVFNISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiydskiKVDGKVLYFGKDIFQIDAIKL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 77 aRKYSSMVFQQFNLYPNMTVLGNLTLaPIKLQK-KSKEEATEIAIAALKRVGM---AHKAGEYP-QNLSGGQQQRIAIAR 151
Cdd:PRK14246 89 -RKEVGMVFQQPNPFPHLSIYDNIAY-PLKSHGiKEKREIKKIVEECLRKVGLwkeVYDRLNSPaSQLSGGQQQRLTIAR 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 152 ALCTKQPIILFDEPTSALDPEMVQEVLDVMIELAQEdITMICVTHEMGFARQVADRVIFMEDGRILEEGTPEHFFDNPEN 231
Cdd:PRK14246 167 ALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNE-IAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKN 245
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
19-221 |
2.10e-35 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 126.73 E-value: 2.10e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 19 VLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPLTKKNHLEMA--RKYSSMVFQQ----FNlyP 92
Cdd:PRK10419 27 VLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQRKafRRDIQMVFQDsisaVN--P 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 93 NMTVlGNLTLAPIK-LQKKSKEEATEIAIAALKRVGMAHK-AGEYPQNLSGGQQQRIAIARALCTKQPIILFDEPTSALD 170
Cdd:PRK10419 105 RKTV-REIIREPLRhLLSLDKAERLARASEMLRAVDLDDSvLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLD 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1469315281 171 PEMVQEVLDVMIELAQE-DITMICVTHEMGFARQVADRVIFMEDGRILEEGT 221
Cdd:PRK10419 184 LVLQAGVIRLLKKLQQQfGTACLFITHDLRLVERFCQRVMVMDNGQIVETQP 235
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
4-220 |
2.26e-35 |
|
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: 125.17 E-value: 2.26e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 4 MIEIKHLNKYFGDL----HVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPlTKKNHLEMARK 79
Cdd:cd03266 1 MITADALTKRFRDVkktvQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFD-VVKEPAEARRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 80 YSsMVFQQFNLYPNMTVLGNLT-------LAPIKLQKKSKEEAteiaiaalKRVGMAHKAGEYPQNLSGGQQQRIAIARA 152
Cdd:cd03266 80 LG-FVSDSTGLYDRLTARENLEyfaglygLKGDELTARLEELA--------DRLGMEELLDRRVGGFSTGMRQKVAIARA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1469315281 153 LCTKQPIILFDEPTSALDPEMVQEVLDVMIELAQEDITMICVTHEMGFARQVADRVIFMEDGRILEEG 220
Cdd:cd03266 151 LVHDPPVLLLDEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
4-229 |
3.04e-35 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 126.64 E-value: 3.04e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 4 MIEIKHLNKYFGD-LHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPLTKKNHLEMARKYSS 82
Cdd:PRK13644 1 MIRLENVSYSYPDgTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKLQGIRKLVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 83 MVFQQfnlyPNMTVLG------------NLTLAPIKLQKKSKEeateiaiaALKRVGMAHKAGEYPQNLSGGQQQRIAIA 150
Cdd:PRK13644 81 IVFQN----PETQFVGrtveedlafgpeNLCLPPIEIRKRVDR--------ALAEIGLEKYRHRSPKTLSGGQGQCVALA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1469315281 151 RALCTKQPIILFDEPTSALDPEMVQEVLDVMIELAQEDITMICVTHEMGfARQVADRVIFMEDGRILEEGTPEHFFDNP 229
Cdd:PRK13644 149 GILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLE-ELHDADRIIVMDRGKIVLEGEPENVLSDV 226
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
4-230 |
5.03e-35 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 125.63 E-value: 5.03e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 4 MIEIKHLN-KYFGDL-HVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPLTKKNhLEMARKYS 81
Cdd:PRK13648 7 IIVFKNVSfQYQSDAsFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDN-FEKLRKHI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 82 SMVFQQfnlyPNMTVLGNLTLAPIKL----QKKSKEEATEIAIAALKRVGMAHKAGEYPQNLSGGQQQRIAIARALCTKQ 157
Cdd:PRK13648 86 GIVFQN----PDNQFVGSIVKYDVAFglenHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNP 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1469315281 158 PIILFDEPTSALDPEMVQEVLDVMIELAQE-DITMICVTHEMGFARQvADRVIFMEDGRILEEGTPEHFFDNPE 230
Cdd:PRK13648 162 SVIILDEATSMLDPDARQNLLDLVRKVKSEhNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIFDHAE 234
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
5-227 |
5.92e-35 |
|
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: 124.91 E-value: 5.92e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 5 IEIKHLN-KYFGD-LHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPLTKKNhLEMARKYSS 82
Cdd:cd03252 1 ITFEHVRfRYKPDgPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALAD-PAWLRRQVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 83 MVFQQfNLYPNMTVLGNLTLAPIKLQKKSKEEATEIA-----IAALkRVGMAHKAGEYPQNLSGGQQQRIAIARALCTKQ 157
Cdd:cd03252 80 VVLQE-NVLFNRSIRDNIALADPGMSMERVIEAAKLAgahdfISEL-PEGYDTIVGEQGAGLSGGQRQRIAIARALIHNP 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1469315281 158 PIILFDEPTSALDPEMVQEVLDVMielaqEDI----TMICVTHEMGFARQvADRVIFMEDGRILEEGTPEHFFD 227
Cdd:cd03252 158 RILIFDEATSALDYESEHAIMRNM-----HDIcagrTVIIIAHRLSTVKN-ADRIIVMEKGRIVEQGSHDELLA 225
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
18-223 |
8.09e-35 |
|
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274550 [Multi-domain] Cd Length: 694 Bit Score: 131.14 E-value: 8.09e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 18 HVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPLTkknHLEMA--RKYSSMVFQQFNLYpNMT 95
Cdd:TIGR03375 479 PALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIR---QIDPAdlRRNIGYVPQDPRLF-YGT 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 96 VLGNLTLAPIKLQKKSKEEATEIA----IAALKRVGMAHKAGEYPQNLSGGQQQRIAIARALCTKQPIILFDEPTSALDP 171
Cdd:TIGR03375 555 LRDNIALGAPYADDEEILRAAELAgvteFVRRHPDGLDMQIGERGRSLSGGQRQAVALARALLRDPPILLLDEPTSAMDN 634
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1469315281 172 EMVQEVLDVMIELAqEDITMICVTHEMGFARQVaDRVIFMEDGRILEEGTPE 223
Cdd:TIGR03375 635 RSEERFKDRLKRWL-AGKTLVLVTHRTSLLDLV-DRIIVMDNGRIVADGPKD 684
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
5-238 |
8.44e-35 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 125.15 E-value: 8.44e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 5 IEIKHLNKYFGDLHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEpTSGEVLIDG-------TPLTKKNHLEMA 77
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNE-LESEVRVEGrveffnqNIYERRVNLNRL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 78 RKYSSMVFQQFNLYPnMTVLGNLTLAPIKLQKKSKEEATEIAIAALKRVGM----AHKAGEYPQNLSGGQQQRIAIARAL 153
Cdd:PRK14258 87 RRQVSMVHPKPNLFP-MSVYDNVAYGVKIVGWRPKLEIDDIVESALKDADLwdeiKHKIHKSALDLSGGQQQRLCIARAL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 154 CTKQPIILFDEPTSALDPEMVQEVLDVMIELA-QEDITMICVTHEMGFARQVADRVIFMED-----GRILEEGTPEHFFD 227
Cdd:PRK14258 166 AVKPKVLLMDEPCFGLDPIASMKVESLIQSLRlRSELTMVIVSHNLHQVSRLSDFTAFFKGnenriGQLVEFGLTKKIFN 245
|
250
....*....|.
gi 1469315281 228 NPENPRCREFL 238
Cdd:PRK14258 246 SPHDSRTREYV 256
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
4-230 |
9.54e-35 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 123.99 E-value: 9.54e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 4 MIEIKHLNKYFGDLHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPLTkknHLEM---ARK- 79
Cdd:COG1137 3 TLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDIT---HLPMhkrARLg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 80 --Y----SSmVFQqfnlypNMTVLGNLtLAPIKLQKKSKEEATEIAIAALKRVGMAHKAGEYPQNLSGGQQQRIAIARAL 153
Cdd:COG1137 80 igYlpqeAS-IFR------KLTVEDNI-LAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARAL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 154 CTKQPIILFDEPTSALDPEMVQEVLDVMIELAQEDITmICVT----HEMgfaRQVADRVIFMEDGRILEEGTPEHFFDNP 229
Cdd:COG1137 152 ATNPKFILLDEPFAGVDPIAVADIQKIIRHLKERGIG-VLITdhnvRET---LGICDRAYIISEGKVLAEGTPEEILNNP 227
|
.
gi 1469315281 230 E 230
Cdd:COG1137 228 L 228
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
19-216 |
9.55e-35 |
|
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: 122.32 E-value: 9.55e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 19 VLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPLTKKnHLEMARKYSSMVFQQFNLYPNmTVLG 98
Cdd:cd03246 17 VLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQW-DPNELGDHVGYLPQDDELFSG-SIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 99 NLtlapiklqkkskeeateiaiaalkrvgmahkageypqnLSGGQQQRIAIARALcTKQP-IILFDEPTSALDPEMVQEV 177
Cdd:cd03246 95 NI--------------------------------------LSGGQRQRLGLARAL-YGNPrILVLDEPNSHLDVEGERAL 135
|
170 180 190
....*....|....*....|....*....|....*....
gi 1469315281 178 LDVMIELAQEDITMICVTHEMGFARQvADRVIFMEDGRI 216
Cdd:cd03246 136 NQAIAALKAAGATRIVIAHRPETLAS-ADRILVLEDGRV 173
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
19-223 |
9.88e-35 |
|
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: 131.02 E-value: 9.88e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 19 VLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPLTKKNHLEMARKYSsmVFQQFNLYPNMTVLG 98
Cdd:TIGR01846 472 VLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPAWLRRQMG--VVLQENVLFSRSIRD 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 99 NLTLAPIKLQKKSKEEATEIA-----IAALKRvGMAHKAGEYPQNLSGGQQQRIAIARALCTKQPIILFDEPTSALDPEM 173
Cdd:TIGR01846 550 NIALCNPGAPFEHVIHAAKLAgahdfISELPQ-GYNTEVGEKGANLSGGQRQRIAIARALVGNPRILIFDEATSALDYES 628
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1469315281 174 VQEVLDVMIELAQEDiTMICVTHEMGFARQvADRVIFMEDGRILEEGTPE 223
Cdd:TIGR01846 629 EALIMRNMREICRGR-TVIIIAHRLSTVRA-CDRIIVLEKGQIAESGRHE 676
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
5-222 |
1.23e-34 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 125.58 E-value: 1.23e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 5 IEIKHLNKYFG-----DLHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEV---LIDGTPLTKKNHLEM 76
Cdd:PRK13651 3 IKVKNIVKIFNkklptELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewiFKDEKNKKKTKEKEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 77 A--------------------RKYSSMVFQ--QFNLYPNmTVLGNLTLAPIKLqKKSKEEATEIAIAALKRVGMAHkagE 134
Cdd:PRK13651 83 VleklviqktrfkkikkikeiRRRVGVVFQfaEYQLFEQ-TIEKDIIFGPVSM-GVSKEEAKKRAAKYIELVGLDE---S 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 135 Y----PQNLSGGQQQRIAIARALCTKQPIILFDEPTSALDPEMVQEVLDVMIELAQEDITMICVTHEMGFARQVADRVIF 210
Cdd:PRK13651 158 YlqrsPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTKRTIF 237
|
250
....*....|..
gi 1469315281 211 MEDGRILEEGTP 222
Cdd:PRK13651 238 FKDGKIIKDGDT 249
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1-221 |
1.66e-34 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 124.52 E-value: 1.66e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 1 MADMIEIKHLNKYF---------GDLHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPLTKK 71
Cdd:PRK15112 1 VETLLEVRNLSKTFryrtgwfrrQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 72 NHlemarKYSS----MVFQ--QFNLYPNMTVlGNLTLAPIKLQKKSKEEATEIAI-AALKRVGM-AHKAGEYPQNLSGGQ 143
Cdd:PRK15112 81 DY-----SYRSqrirMIFQdpSTSLNPRQRI-SQILDFPLRLNTDLEPEQREKQIiETLRQVGLlPDHASYYPHMLAPGQ 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1469315281 144 QQRIAIARALCTKQPIILFDEPTSALDPEMVQEVLDVMIELAQED-ITMICVTHEMGFARQVADRVIFMEDGRILEEGT 221
Cdd:PRK15112 155 KQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQgISYIYVTQHLGMMKHISDQVLVMHQGEVVERGS 233
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
4-223 |
1.70e-34 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 123.97 E-value: 1.70e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 4 MIEIKHLNKYFGDLHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPLTKKNHLEMARKYS-- 81
Cdd:PRK11231 2 TLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLAll 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 82 --------SMVFQQFNLY---PNMTVLGNLTLAPIKLQKKSKEEaTEIAIAALKRVgmahkageypQNLSGGQQQRIAIA 150
Cdd:PRK11231 82 pqhhltpeGITVRELVAYgrsPWLSLWGRLSAEDNARVNQAMEQ-TRINHLADRRL----------TDLSGGQRQRAFLA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1469315281 151 RALCTKQPIILFDEPTSALDPEMVQEVLDVMIELAQEDITMICVTHEMGFARQVADRVIFMEDGRILEEGTPE 223
Cdd:PRK11231 151 MVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPE 223
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
5-221 |
2.65e-34 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 129.31 E-value: 2.65e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 5 IEIKHLN-KYFGDLHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPLTKKNhLEMARKYSSM 83
Cdd:PRK13657 335 VEFDDVSfSYDNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVT-RASLRRNIAV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 84 VFQQFNLYpNMTVLGNLTLApiklqkksKEEATEIAI-AALKRV-----------GMAHKAGEYPQNLSGGQQQRIAIAR 151
Cdd:PRK13657 414 VFQDAGLF-NRSIEDNIRVG--------RPDATDEEMrAAAERAqahdfierkpdGYDTVVGERGRQLSGGERQRLAIAR 484
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1469315281 152 ALCTKQPIILFDEPTSALDPEM---VQEVLDvmiELAQEDITMIcVTHEMGFARQvADRVIFMEDGRILEEGT 221
Cdd:PRK13657 485 ALLKDPPILILDEATSALDVETeakVKAALD---ELMKGRTTFI-IAHRLSTVRN-ADRILVFDNGRVVESGS 552
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
20-226 |
3.41e-34 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 124.09 E-value: 3.41e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 20 LKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPLT---KKNHLEMARKYSSMVFQ--QFNLYPNm 94
Cdd:PRK13649 23 LFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITstsKNKDIKQIRKKVGLVFQfpESQLFEE- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 95 TVLGNLTLAPIKLqKKSKEEATEIAIAALKRVGMAHKAGEY-PQNLSGGQQQRIAIARALCTKQPIILFDEPTSALDPEM 173
Cdd:PRK13649 102 TVLKDVAFGPQNF-GVSQEEAEALAREKLALVGISESLFEKnPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKG 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1469315281 174 VQEVLDVMIELAQEDITMICVTHEMGFARQVADRVIFMEDGRILEEGTPEHFF 226
Cdd:PRK13649 181 RKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIF 233
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
1-239 |
3.79e-34 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 123.27 E-value: 3.79e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 1 MADMIEIKHLNKYfGDLHVLKDINLTVKRGEKLVMIGPSGSGKStlIRCVDYLE------EPTSGEVLIDGTPLtkknHL 74
Cdd:PRK10418 1 MPQQIELRNIALQ-AAQPLVHGVSLTLQRGRVLALVGGSGSGKS--LTCAAALGilpagvRQTAGRVLLDGKPV----AP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 75 EMAR-KYSSMVFQQ----FNLYPNMTVLGNLTLAPIklqkkSKEEATEIAIAALKRVGMAHKA---GEYPQNLSGGQQQR 146
Cdd:PRK10418 74 CALRgRKIATIMQNprsaFNPLHTMHTHARETCLAL-----GKPADDATLTAALEAVGLENAArvlKLYPFEMSGGMLQR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 147 IAIARALCTKQPIILFDEPTSALDPEMVQEVLDVMIELAQE-DITMICVTHEMGFARQVADRVIFMEDGRILEEGTPEHF 225
Cdd:PRK10418 149 MMIALALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKrALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETL 228
|
250
....*....|....
gi 1469315281 226 FDNPENPRCREFLS 239
Cdd:PRK10418 229 FNAPKHAVTRSLVS 242
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
5-239 |
6.51e-34 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 122.58 E-value: 6.51e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 5 IEIKHLNKYFGDLHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEE--PT---SGEVLIDGTPLTKK--NHLEMA 77
Cdd:PRK14243 11 LRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDliPGfrvEGKVTFHGKNLYAPdvDPVEVR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 78 RKYSsMVFQQFNLYPNmTVLGNLTLAP-IKLQKKSKEEATEiaiAALKRVGM----AHKAGEYPQNLSGGQQQRIAIARA 152
Cdd:PRK14243 91 RRIG-MVFQKPNPFPK-SIYDNIAYGArINGYKGDMDELVE---RSLRQAALwdevKDKLKQSGLSLSGGQQQRLCIARA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 153 LCTKQPIILFDEPTSALDPEMVQEVLDVMIELaQEDITMICVTHEMGFARQVADRVIFM---------EDGRILEEGTPE 223
Cdd:PRK14243 166 IAVQPEVILMDEPCSALDPISTLRIEELMHEL-KEQYTIIIVTHNMQQAARVSDMTAFFnveltegggRYGYLVEFDRTE 244
|
250
....*....|....*.
gi 1469315281 224 HFFDNPENPRCREFLS 239
Cdd:PRK14243 245 KIFNSPQQQATRDYVS 260
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
5-222 |
7.88e-34 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 121.45 E-value: 7.88e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 5 IEIKHLN-KYFGDLH-VLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPLTKKnHLEMARKYSS 82
Cdd:cd03244 3 IEFKNVSlRYRPNLPpVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKI-GLHDLRSRIS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 83 MVFQQFNLYPNmTVLGNltLAPikLQKKSKEEateiAIAALKRVGMAHKAGEYP-----------QNLSGGQQQRIAIAR 151
Cdd:cd03244 82 IIPQDPVLFSG-TIRSN--LDP--FGEYSDEE----LWQALERVGLKEFVESLPggldtvveeggENLSVGQRQLLCLAR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1469315281 152 ALCTKQPIILFDEPTSALDPE---MVQEVldvmIELAQEDITMICVTHE----MGFarqvaDRVIFMEDGRILEEGTP 222
Cdd:cd03244 153 ALLRKSKILVLDEATASVDPEtdaLIQKT----IREAFKDCTVLTIAHRldtiIDS-----DRILVLDKGRVVEFDSP 221
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
18-239 |
1.68e-33 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 126.36 E-value: 1.68e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 18 HVLKDINLTVKRGEKLVMIGPSGSGKST----LIRCVdyleePTSGEVLIDGTPLTKKNHLEM--ARKYSSMVFQQFN-- 89
Cdd:PRK15134 300 VVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLI-----NSQGEIWFDGQPLHNLNRRQLlpVRHRIQVVFQDPNss 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 90 LYPNMTVLgNLTLAPIKLQKK--SKEEATEIAIAALKRVGM-AHKAGEYPQNLSGGQQQRIAIARALCTKQPIILFDEPT 166
Cdd:PRK15134 375 LNPRLNVL-QIIEEGLRVHQPtlSAAQREQQVIAVMEEVGLdPETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPT 453
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1469315281 167 SALDPEMVQEVLDVMIELAQE-DITMICVTHEMGFARQVADRVIFMEDGRILEEGTPEHFFDNPENPRCREFLS 239
Cdd:PRK15134 454 SSLDKTVQAQILALLKSLQQKhQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERVFAAPQQEYTRQLLA 527
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
5-196 |
4.94e-33 |
|
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: 125.17 E-value: 4.94e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 5 IEIKHLN-KYFGDLHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPLTKKNHLEMARKYSsM 83
Cdd:TIGR02868 335 LELRDLSaGYPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVS-V 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 84 VFQQFNLYpNMTVLGNLTLApiklqkksKEEATEIAI-AALKRVGMAH-----------KAGEYPQNLSGGQQQRIAIAR 151
Cdd:TIGR02868 414 CAQDAHLF-DTTVRENLRLA--------RPDATDEELwAALERVGLADwlralpdgldtVLGEGGARLSGGERQRLALAR 484
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1469315281 152 ALCTKQPIILFDEPTSALDPEMVQEVLDVMIElAQEDITMICVTH 196
Cdd:TIGR02868 485 ALLADAPILLLDEPTEHLDAETADELLEDLLA-ALSGRTVVLITH 528
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-223 |
6.99e-33 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 119.42 E-value: 6.99e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 1 MADMIEIKHLNKYF----------------------GDLHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTS 58
Cdd:COG1134 1 MSSMIEVENVSKSYrlyhepsrslkelllrrrrtrrEEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 59 GEVLIDG--TPLtkknhLEMArkyssMVFQQF-----NLYPNMTVLGnLTLAPIklqkKSKEEatEI-AIAALkrvgmah 130
Cdd:COG1134 81 GRVEVNGrvSAL-----LELG-----AGFHPEltgreNIYLNGRLLG-LSRKEI----DEKFD--EIvEFAEL------- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 131 kaGEY---P-QNLSGGQQQRIAIARALCTKQPIILFDEPTSALDPEMVQEVLDVMIELAQEDITMICVTHEMGFARQVAD 206
Cdd:COG1134 137 --GDFidqPvKTYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRESGRTVIFVSHSMGAVRRLCD 214
|
250
....*....|....*..
gi 1469315281 207 RVIFMEDGRILEEGTPE 223
Cdd:COG1134 215 RAIWLEKGRLVMDGDPE 231
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
16-216 |
1.11e-32 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 118.34 E-value: 1.11e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 16 DLHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPLTKKNHLEMARKYsSMVFQQFNLYPNmT 95
Cdd:cd03248 26 DTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSKV-SLVGQEPVLFAR-S 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 96 VLGNLTLApikLQKKSKEEATEIAIAA-------LKRVGMAHKAGEYPQNLSGGQQQRIAIARALCTKQPIILFDEPTSA 168
Cdd:cd03248 104 LQDNIAYG---LQSCSFECVKEAAQKAhahsfisELASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSA 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1469315281 169 LDPEMVQEVLDVMIElAQEDITMICVTHEMGFARQvADRVIFMEDGRI 216
Cdd:cd03248 181 LDAESEQQVQQALYD-WPERRTVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
19-220 |
1.35e-32 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 118.14 E-value: 1.35e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 19 VLKDINLTVKRGEKLVMIGPSGSGKSTL---IRCVDYLEEPTSGEVLIDGTPLTKKnhleMARKYSSMVFQQFNLYPNMT 95
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTLldaISGRVEGGGTTSGQILFNGQPRKPD----QFQKCVAYVRQDDILLPGLT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 96 VLGNLTL-APIKLQKKSKEEAT--EIAIAALKRVGMAHKAGEYPQNLSGGQQQRIAIARALcTKQPIILF-DEPTSALDP 171
Cdd:cd03234 98 VRETLTYtAILRLPRKSSDAIRkkRVEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQL-LWDPKVLIlDEPTSGLDS 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1469315281 172 EMVQEVLDVMIELAQEDITMICVTHEMG---FarQVADRVIFMEDGRILEEG 220
Cdd:cd03234 177 FTALNLVSTLSQLARRNRIVILTIHQPRsdlF--RLFDRILLLSSGEIVYSG 226
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
4-218 |
1.65e-32 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 118.65 E-value: 1.65e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 4 MIEIKHLNKYFGDLHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPLTKKNhlemARKysSM 83
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPG----AER--GV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 84 VFQQFNLYPNMTVLGNLTLApIKLQKKSKEEATEIAIAALKRVGMAHKAGEYPQNLSGGQQQRIAIARALCTKQPIILFD 163
Cdd:PRK11248 75 VFQNEGLLPWRNVQDNVAFG-LQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLD 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1469315281 164 EPTSALDP---EMVQEVLdvmIELAQEDITMI-CVTHEMGFARQVADRVIFME--DGRILE 218
Cdd:PRK11248 154 EPFGALDAftrEQMQTLL---LKLWQETGKQVlLITHDIEEAVFMATELVLLSpgPGRVVE 211
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
35-239 |
1.72e-32 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 119.43 E-value: 1.72e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 35 MIGPSGSGKSTLIRCVDYLEEPTSG-----EVLIDGTPLTKKNHLEMARKYSSMVFQQFNLYPnMTVLGNLtLAPIKLQK 109
Cdd:PRK14271 52 LMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIFNYRDVLEFRRRVGMLFQRPNPFP-MSIMDNV-LAGVRAHK 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 110 -KSKEEATEIAIAALKRVGM----AHKAGEYPQNLSGGQQQRIAIARALCTKQPIILFDEPTSALDPEMVQEVLDVMIEL 184
Cdd:PRK14271 130 lVPRKEFRGVAQARLTEVGLwdavKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSL 209
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1469315281 185 AqEDITMICVTHEMGFARQVADRVIFMEDGRILEEGTPEHFFDNPENPRCREFLS 239
Cdd:PRK14271 210 A-DRLTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKHAETARYVA 263
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
20-226 |
2.69e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 119.07 E-value: 2.69e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 20 LKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDG---TPLTKKNHLEMARKYSSMVFQ--QFNLYPNm 94
Cdd:PRK13643 22 LFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDivvSSTSKQKEIKPVRKKVGVVFQfpESQLFEE- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 95 TVLGNLTLAPIKLqKKSKEEATEIAIAALKRVGMAHKAGE-YPQNLSGGQQQRIAIARALCTKQPIILFDEPTSALDPEM 173
Cdd:PRK13643 101 TVLKDVAFGPQNF-GIPKEKAEKIAAEKLEMVGLADEFWEkSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKA 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1469315281 174 VQEVLDVMIELAQEDITMICVTHEMGFARQVADRVIFMEDGRILEEGTPEHFF 226
Cdd:PRK13643 180 RIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVF 232
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-214 |
6.49e-32 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 121.82 E-value: 6.49e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 1 MADMIEIKHLNKYFGDLHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPLTKKNHLEMARKY 80
Cdd:PRK09700 2 ATPYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 81 SSMVFQQFNLYPNMTVLGNLTLA----------PIKLQKKSKEEATEIaiaaLKRVGMAHKAGEYPQNLSGGQQQRIAIA 150
Cdd:PRK09700 82 IGIIYQELSVIDELTVLENLYIGrhltkkvcgvNIIDWREMRVRAAMM----LLRVGLKVDLDEKVANLSISHKQMLEIA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1469315281 151 RALCTKQPIILFDEPTSALDPEMVQEVLDVMIELAQEDITMICVTHEMGFARQVADRVIFMEDG 214
Cdd:PRK09700 158 KTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDG 221
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
14-209 |
1.24e-31 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 114.64 E-value: 1.24e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 14 FGDLHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEV----------------LIDGTPLTKKNHLEMA 77
Cdd:NF040873 2 YGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVrraggarvayvpqrseVPDSLPLTVRDLVAMG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 78 RkyssmvfqqfnlYPNMTVLGNLTlapiklqkkskEEATEIAIAALKRVGMAHKAGEYPQNLSGGQQQRIAIARALCTKQ 157
Cdd:NF040873 82 R------------WARRGLWRRLT-----------RDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEA 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1469315281 158 PIILFDEPTSALDPEMVQEVLDVMIELAQEDITMICVTHEMGFARQvADRVI 209
Cdd:NF040873 139 DLLLLDEPTTGLDAESRERIIALLAEEHARGATVVVVTHDLELVRR-ADPCV 189
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
19-221 |
1.39e-31 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 121.47 E-value: 1.39e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 19 VLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPLTkknHLEMA--RKYSSMVfqqfnlyPNMTV 96
Cdd:COG5265 373 ILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIR---DVTQAslRAAIGIV-------PQDTV 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 97 LGNLTLA-------PiklqkkskeEATEIAIAALKRvgMAH--------------KAGEYPQNLSGGQQQRIAIARALCT 155
Cdd:COG5265 443 LFNDTIAyniaygrP---------DASEEEVEAAAR--AAQihdfieslpdgydtRVGERGLKLSGGEKQRVAIARTLLK 511
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1469315281 156 KQPIILFDEPTSALDPEMVQEVLDVMIELAQEDITMI------CVTHemgfarqvADRVIFMEDGRILEEGT 221
Cdd:COG5265 512 NPPILIFDEATSALDSRTERAIQAALREVARGRTTLViahrlsTIVD--------ADEILVLEAGRIVERGT 575
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
4-242 |
1.53e-31 |
|
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated complex. This protein (PhnK) and the adjacent-encoded PhnL resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this complex rather than part of a transporter per se. [Central intermediary metabolism, Phosphorus compounds]
Pssm-ID: 188208 [Multi-domain] Cd Length: 253 Bit Score: 116.47 E-value: 1.53e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 4 MIEIKHLNKYFGDLHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEV---LIDGTP-----LTKKNHLE 75
Cdd:TIGR02323 3 LLQVSGLSKSYGGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTAtyiMRSGAElelyqLSEAERRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 76 MARKYSSMVFQQFNLYPNMTVL--GNLTLAPIKLQKKSKEEATEIAIAALKRVGM-AHKAGEYPQNLSGGQQQRIAIARA 152
Cdd:TIGR02323 83 LMRTEWGFVHQNPRDGLRMRVSagANIGERLMAIGARHYGNIRATAQDWLEEVEIdPTRIDDLPRAFSGGMQQRLQIARN 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 153 LCTKQPIILFDEPTSALDPEMVQEVLDVMIELAQE-DITMICVTHEMGFARQVADRVIFMEDGRILEEGTPEHFFDNPEN 231
Cdd:TIGR02323 163 LVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDlGLAVIIVTHDLGVARLLAQRLLVMQQGRVVESGLTDQVLDDPQH 242
|
250
....*....|.
gi 1469315281 232 PRCREFLSKIL 242
Cdd:TIGR02323 243 PYTQLLVSSIL 253
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
20-221 |
2.72e-31 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 120.89 E-value: 2.72e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 20 LKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPLtKKNHLEMARKYSSMVFQQFNLYpNMTVLGN 99
Cdd:PRK11176 359 LRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDL-RDYTLASLRNQVALVSQNVHLF-NDTIANN 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 100 LTLAPI-KLQKKSKEEATEIA-----IAALKRvGMAHKAGEYPQNLSGGQQQRIAIARALCTKQPIILFDEPTSALDPE- 172
Cdd:PRK11176 437 IAYARTeQYSREQIEEAARMAyamdfINKMDN-GLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTEs 515
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1469315281 173 --MVQEVLDvmiELaQEDITMICVTHEMGFARQvADRVIFMEDGRILEEGT 221
Cdd:PRK11176 516 erAIQAALD---EL-QKNRTSLVIAHRLSTIEK-ADEILVVEDGEIVERGT 561
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
20-226 |
3.46e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 116.03 E-value: 3.46e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 20 LKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDG---TPLTKKNHLEMARKYSSMVFQ--QFNLYPNm 94
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDitiTHKTKDKYIRPVRKRIGMVFQfpESQLFED- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 95 TVLGNLTLAPiKLQKKSKEEATEIAIAALKRVGMAHKAGEY-PQNLSGGQQQRIAIARALCTKQPIILFDEPTSALDPEM 173
Cdd:PRK13646 102 TVEREIIFGP-KNFKMNLDEVKNYAHRLLMDLGFSRDVMSQsPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQS 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1469315281 174 VQEVLDVMIELAQED-ITMICVTHEMGFARQVADRVIFMEDGRILEEGTPEHFF 226
Cdd:PRK13646 181 KRQVMRLLKSLQTDEnKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELF 234
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
3-218 |
3.89e-31 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 119.78 E-value: 3.89e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 3 DMIEIKHLNKYFGDLHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIdGTpltkknHLEMArkYss 82
Cdd:COG0488 314 KVLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GE------TVKIG--Y-- 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 83 mvFQQFN--LYPNMTVLGNLtlapiklqKKSKEEATEIAIAAL------------KRVGmahkageypqNLSGGQQQRIA 148
Cdd:COG0488 383 --FDQHQeeLDPDKTVLDEL--------RDGAPGGTEQEVRGYlgrflfsgddafKPVG----------VLSGGEKARLA 442
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 149 IARALCTKQPIILFDEPTSALDPEMVQEVLDVmieLAQEDITMICVTHEMGFARQVADRVIFMEDGRILE 218
Cdd:COG0488 443 LAKLLLSPPNVLLLDEPTNHLDIETLEALEEA---LDDFPGTVLLVSHDRYFLDRVATRILEFEDGGVRE 509
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
5-221 |
6.09e-31 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 120.23 E-value: 6.09e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 5 IEIKHLN-KY-FGDlHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPLTKKNHLEMaRKYSS 82
Cdd:TIGR01193 474 IVINDVSySYgYGS-NILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTL-RQFIN 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 83 MVFQQFNLYPNmTVLGNLTL-APIKLQKKSKEEATEIA-----IAALKrVGMAHKAGEYPQNLSGGQQQRIAIARALCTK 156
Cdd:TIGR01193 552 YLPQEPYIFSG-SILENLLLgAKENVSQDEIWAACEIAeikddIENMP-LGYQTELSEEGSSISGGQKQRIALARALLTD 629
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1469315281 157 QPIILFDEPTSALDPEMVQEVLDVMIELaqEDITMICVTHEMGFARQVaDRVIFMEDGRILEEGT 221
Cdd:TIGR01193 630 SKVLILDESTSNLDTITEKKIVNNLLNL--QDKTIIFVAHRLSVAKQS-DKIIVLDHGKIIEQGS 691
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
3-241 |
1.74e-30 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 118.80 E-value: 1.74e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 3 DMIEIKHLNKYF----GDLHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPLTKKNH--LEM 76
Cdd:PRK10261 11 DVLAVENLNIAFmqeqQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRRRSRqvIEL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 77 ARKYSS-----------MVFQQ--FNLYPNMTVlGNLTLAPIKL-QKKSKEEATEIAIAALKRVGMAHKA---GEYPQNL 139
Cdd:PRK10261 91 SEQSAAqmrhvrgadmaMIFQEpmTSLNPVFTV-GEQIAESIRLhQGASREEAMVEAKRMLDQVRIPEAQtilSRYPHQL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 140 SGGQQQRIAIARALCTKQPIILFDEPTSALDPEMVQEVLDvMIELAQEDITM--ICVTHEMGFARQVADRVIFMEDGRIL 217
Cdd:PRK10261 170 SGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQ-LIKVLQKEMSMgvIFITHDMGVVAEIADRVLVMYQGEAV 248
|
250 260
....*....|....*....|....
gi 1469315281 218 EEGTPEHFFDNPENPRCREFLSKI 241
Cdd:PRK10261 249 ETGSVEQIFHAPQHPYTRALLAAV 272
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
5-220 |
3.23e-30 |
|
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 represents the family of all lantibiotics related to gallidermin, including epidermin, mutatin, and nisin. This protein family describes the ATP-binding subunit of a gallidermin/epidermin class lantibiotic protection transporter. It is largely restricted to gallidermin-family lantibiotic biosynthesis and export cassettes, but also occurs in orphan transporter cassettes in species that lack candidate lantibiotic precursor and synthetase genes.
Pssm-ID: 163452 [Multi-domain] Cd Length: 223 Bit Score: 112.11 E-value: 3.23e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 5 IEIKHLNKYFGDLHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPLTKKnhleMARKYSSMV 84
Cdd:TIGR03740 1 LETKNLSKRFGKQTAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGHPWTRK----DLHKIGSLI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 85 fQQFNLYPNMTVLGNLTLApIKLQKKSKEEATEIaiaaLKRVGMAHKAGEYPQNLSGGQQQRIAIARALCTKQPIILFDE 164
Cdd:TIGR03740 77 -ESPPLYENLTARENLKVH-TTLLGLPDSRIDEV----LNIVDLTNTGKKKAKQFSLGMKQRLGIAIALLNHPKLLILDE 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1469315281 165 PTSALDPEMVQEVLDVMIELAQEDITMICVTHEMGFARQVADRVIFMEDGRILEEG 220
Cdd:TIGR03740 151 PTNGLDPIGIQELRELIRSFPEQGITVILSSHILSEVQQLADHIGIISEGVLGYQG 206
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
19-238 |
3.80e-30 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 117.11 E-value: 3.80e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 19 VLKDINLTVKRGEKLVMIGPSGSGKS-TLIRCVDYLEEP----TSGEVLIDGTPLTKKNHLEMAR---KYSSMVFQQ--F 88
Cdd:PRK15134 24 VVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPpvvyPSGDIRFHGESLLHASEQTLRGvrgNKIAMIFQEpmV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 89 NLYPNMTVLGNLTLApIKLQKKSKEEA--TEIaIAALKRVGMAHKAG---EYPQNLSGGQQQRIAIARALCTKQPIILFD 163
Cdd:PRK15134 104 SLNPLHTLEKQLYEV-LSLHRGMRREAarGEI-LNCLDRVGIRQAAKrltDYPHQLSGGERQRVMIAMALLTRPELLIAD 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1469315281 164 EPTSALDPEMVQEVLDVMIELAQE-DITMICVTHEMGFARQVADRVIFMEDGRILEEGTPEHFFDNPENPRCREFL 238
Cdd:PRK15134 182 EPTTALDVSVQAQILQLLRELQQElNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAATLFSAPTHPYTQKLL 257
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
18-242 |
4.66e-30 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 117.46 E-value: 4.66e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 18 HVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEP---TSGEVLIDGTPLTKKnhleMARKYSSMVfQQFNLY-PN 93
Cdd:TIGR00955 39 HLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKgvkGSGSVLLNGMPIDAK----EMRAISAYV-QQDDLFiPT 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 94 MTVLGNLTL-APIKLQ----KKSKEEATEIAIAALKRVGMAHK---AGEYPQNLSGGQQQRIAIARALCTKQPIILFDEP 165
Cdd:TIGR00955 114 LTVREHLMFqAHLRMPrrvtKKEKRERVDEVLQALGLRKCANTrigVPGRVKGLSGGERKRLAFASELLTDPPLLFCDEP 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 166 TSALDPEMVQEVLDVMIELAQEDITMICVTH-------EMgFarqvaDRVIFMEDGRILEEGTPEH---FFDN-----PE 230
Cdd:TIGR00955 194 TSGLDSFMAYSVVQVLKGLAQKGKTIICTIHqpsselfEL-F-----DKIILMAEGRVAYLGSPDQavpFFSDlghpcPE 267
|
250
....*....|..
gi 1469315281 231 NPRCREFLSKIL 242
Cdd:TIGR00955 268 NYNPADFYVQVL 279
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
19-216 |
8.88e-30 |
|
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: 109.44 E-value: 8.88e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 19 VLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPLTKKNHLEMARKYSSMV---FQQFNLYPNMT 95
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAGIAYVpedRKREGLVLDLS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 96 VLGNLTLAPIklqkkskeeateiaiaalkrvgmahkageypqnLSGGQQQRIAIARALCTKQPIILFDEPTSALDPEMVQ 175
Cdd:cd03215 95 VAENIALSSL---------------------------------LSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKA 141
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1469315281 176 EVLDVMIELAQEDITMICVTHEMGFARQVADRVIFMEDGRI 216
Cdd:cd03215 142 EIYRLIRELADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
14-223 |
2.44e-29 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 110.85 E-value: 2.44e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 14 FGDLHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPLTKKNHLEMARKYSSmvfqqfnLYPN 93
Cdd:PRK10253 17 YGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGL-------LAQN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 94 MTVLGNLTLAPI---------KLQKKSKEEATEIAIAALKRVGMAHKAGEYPQNLSGGQQQRIAIARALCTKQPIILFDE 164
Cdd:PRK10253 90 ATTPGDITVQELvargryphqPLFTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDE 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 165 PTSALDPEMVQEVLDVMIELAQED-ITMICVTHEMGFARQVADRVIFMEDGRILEEGTPE 223
Cdd:PRK10253 170 PTTWLDISHQIDLLELLSELNREKgYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPK 229
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1-232 |
4.82e-29 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 111.35 E-value: 4.82e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 1 MADMIEIKHLNKYF----GDLHVLKDINLTVKRGEKLVMIGPSGSGKS-TLIRCVDYLEEP--TSGEVLIDGTPLTKKNH 73
Cdd:PRK09473 9 ADALLDVKDLRVTFstpdGDVTAVNDLNFSLRAGETLGIVGESGSGKSqTAFALMGLLAANgrIGGSATFNGREILNLPE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 74 LEMARKYS---SMVFQQ--FNLYPNMTVlGNLTLAPIKLQKK-SKEEATEIAIAALKRVGM--AHK-AGEYPQNLSGGQQ 144
Cdd:PRK09473 89 KELNKLRAeqiSMIFQDpmTSLNPYMRV-GEQLMEVLMLHKGmSKAEAFEESVRMLDAVKMpeARKrMKMYPHEFSGGMR 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 145 QRIAIARALCTKQPIILFDEPTSALDPEMVQEVLDVMIELAQE-DITMICVTHEMGFARQVADRVIFMEDGRILEEGTPE 223
Cdd:PRK09473 168 QRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNAR 247
|
....*....
gi 1469315281 224 HFFDNPENP 232
Cdd:PRK09473 248 DVFYQPSHP 256
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
19-216 |
6.08e-29 |
|
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: 114.07 E-value: 6.08e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 19 VLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPLtkknhlemaRKYSSMVF--------QQFNL 90
Cdd:COG4618 347 ILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADL---------SQWDREELgrhigylpQDVEL 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 91 YPNmTVlgnltlapiklqkksKE------EAT-EIAIAALKRVGmAHKA------------GEYPQNLSGGQQQRIAIAR 151
Cdd:COG4618 418 FDG-TI---------------AEniarfgDADpEKVVAAAKLAG-VHEMilrlpdgydtriGEGGARLSGGQRQRIGLAR 480
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1469315281 152 ALCTKQPIILFDEPTSALDPEMVQEVLDVMIELAQEDITMICVTHEMGfARQVADRVIFMEDGRI 216
Cdd:COG4618 481 ALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKARGATVVVITHRPS-LLAAVDKLLVLRDGRV 544
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1-231 |
7.59e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 109.80 E-value: 7.59e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 1 MADMIEIKHLNKYF---GDLHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPLTKKNHLEMA 77
Cdd:PRK13642 1 MNKILEVENLVFKYekeSDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 78 RKYSsMVFQQ-FNLYPNMTVLGNLTLApIKLQKKSKEEATEIAIAALKRVGMAHKAGEYPQNLSGGQQQRIAIARALCTK 156
Cdd:PRK13642 81 RKIG-MVFQNpDNQFVGATVEDDVAFG-MENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1469315281 157 QPIILFDEPTSALDPEMVQEVLDVMIELAQE-DITMICVTHEMGFARQvADRVIFMEDGRILEEGTPEHFFDNPEN 231
Cdd:PRK13642 159 PEIIILDESTSMLDPTGRQEIMRVIHEIKEKyQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELFATSED 233
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
10-241 |
8.59e-29 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 113.80 E-value: 8.59e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 10 LNKYFGDLHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPLT--KKNHLEMARKYSSMVFQQ 87
Cdd:PRK10261 330 LNRVTREVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDtlSPGKLQALRRDIQFIFQD 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 88 --FNLYPNMTVlGNLTLAPIKLQKKSKEEATEIAIA-ALKRVGM-AHKAGEYPQNLSGGQQQRIAIARALCTKQPIILFD 163
Cdd:PRK10261 410 pyASLDPRQTV-GDSIMEPLRVHGLLPGKAAAARVAwLLERVGLlPEHAWRYPHEFSGGQRQRICIARALALNPKVIIAD 488
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1469315281 164 EPTSALDPEMVQEVLDVMIELAQE-DITMICVTHEMGFARQVADRVIFMEDGRILEEGTPEHFFDNPENPRCREFLSKI 241
Cdd:PRK10261 489 EAVSALDVSIRGQIINLLLDLQRDfGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENPQHPYTRKLMAAV 567
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
5-215 |
1.08e-28 |
|
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: 105.61 E-value: 1.08e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 5 IEIKHLNKYFGDLHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDgtpltkknhlemarkyssmv 84
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWG-------------------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 85 fqqfnlypnmtvlgnltlapiklqkkskeeateiaiaalKRVGMAHkageYPQnLSGGQQQRIAIARALCTKQPIILFDE 164
Cdd:cd03221 61 ---------------------------------------STVKIGY----FEQ-LSGGEKMRLALAKLLLENPNLLLLDE 96
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1469315281 165 PTSALDPEMVQEVLDvmiELAQEDITMICVTHEMGFARQVADRVIFMEDGR 215
Cdd:cd03221 97 PTNHLDLESIEALEE---ALKEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
4-219 |
1.42e-28 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 110.73 E-value: 1.42e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 4 MIEIkHLNKYFGDLHVlkDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPL---TKKNHLEMARKY 80
Cdd:PRK11144 1 MLEL-NFKQQLGDLCL--TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLfdaEKGICLPPEKRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 81 SSMVFQQFNLYPNMTVLGNLTLApikLQKKSKEEATEIaiaaLKRVGMAHKAGEYPQNLSGGQQQRIAIARALCTKQPII 160
Cdd:PRK11144 78 IGYVFQDARLFPHYKVRGNLRYG---MAKSMVAQFDKI----VALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELL 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1469315281 161 LFDEPTSALDPEMVQEVLDVMIELAQE-DITMICVTHEMGFARQVADRVIFMEDGRI-----LEE 219
Cdd:PRK11144 151 LMDEPLASLDLPRKRELLPYLERLAREiNIPILYVSHSLDEILRLADRVVVLEQGKVkafgpLEE 215
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-242 |
3.19e-28 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 107.70 E-value: 3.19e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 1 MADMIEIKHLNKYFGDLHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPLTKKNHLEMARKY 80
Cdd:PRK11701 3 DQPLLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYALSEAE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 81 SSMVF-------QQF---NLYPNMTVLGNLTLAPIKLQKKSKEEATEIAIAALKRVGM-AHKAGEYPQNLSGGQQQRIAI 149
Cdd:PRK11701 83 RRRLLrtewgfvHQHprdGLRMQVSAGGNIGERLMAVGARHYGDIRATAGDWLERVEIdAARIDDLPTTFSGGMQQRLQI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 150 ARALCTKQPIILFDEPTSALDPEMVQEVLDVMIELAQE-DITMICVTHEMGFARQVADRVIFMEDGRILEEGTPEHFFDN 228
Cdd:PRK11701 163 ARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRElGLAVVIVTHDLAVARLLAHRLLVMKQGRVVESGLTDQVLDD 242
|
250
....*....|....
gi 1469315281 229 PENPRCREFLSKIL 242
Cdd:PRK11701 243 PQHPYTQLLVSSVL 256
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
6-223 |
3.91e-28 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 107.08 E-value: 3.91e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 6 EIKHLNKYFGDLHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCV----DYleEPTSGEVLIDGTPLTKKNHLEMARKYS 81
Cdd:COG0396 2 EIKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLmghpKY--EVTSGSILLDGEDILELSPDERARAGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 82 SMVFQqfnlYP-------NMTVLgNLTLAPIKLQKKSKEEATEIAIAALKRVGMAHKAGEYPQN--LSGGQQQRIAIARA 152
Cdd:COG0396 80 FLAFQ----YPveipgvsVSNFL-RTALNARRGEELSAREFLKLLKEKMKELGLDEDFLDRYVNegFSGGEKKRNEILQM 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1469315281 153 LCTKQPIILFDEPTSALDPEMVQEVLDVMIELAQEDITMICVTHemgFAR----QVADRVIFMEDGRILEEGTPE 223
Cdd:COG0396 155 LLLEPKLAILDETDSGLDIDALRIVAEGVNKLRSPDRGILIITH---YQRildyIKPDFVHVLVDGRIVKSGGKE 226
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
19-215 |
4.93e-28 |
|
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: 105.63 E-value: 4.93e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 19 VLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVdyLEE--PTSGEVLIDGTpltkknhleMArkYSSmvfQQfnlyP---N 93
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSAL--LGEleKLSGSVSVPGS---------IA--YVS---QE----PwiqN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 94 MTVLGNLTL-AP---------IK-------LQKKSKEEATEIaiaalkrvgmahkaGEYPQNLSGGQQQRIAIARALCTK 156
Cdd:cd03250 80 GTIRENILFgKPfdeeryekvIKacalepdLEILPDGDLTEI--------------GEKGINLSGGQKQRISLARAVYSD 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 157 QPIILFDEPTSALDPEMVQEVLD-VMIELAQEDITMICVTHEMGFARQvADRVIFMEDGR 215
Cdd:cd03250 146 ADIYLLDDPLSAVDAHVGRHIFEnCILGLLLNNKTRILVTHQLQLLPH-ADQIVVLDNGR 204
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1-232 |
6.21e-28 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 108.29 E-value: 6.21e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 1 MAdMIEIKHLNKYFGD----LHVLKDINLTVKRGEKLVMIGPSGSGKS----TLIRCVDYLEEPTSGEVLIDGTPLTK-- 70
Cdd:PRK11022 1 MA-LLNVDKLSVHFGDesapFRAVDRISYSVKQGEVVGIVGESGSGKSvsslAIMGLIDYPGRVMAEKLEFNGQDLQRis 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 71 -KNHLEMARKYSSMVFQQ--FNLYPNMTVlGNLTLAPIKL-QKKSKEEATEIAIAALKRVGMAHKAGE---YPQNLSGGQ 143
Cdd:PRK11022 80 eKERRNLVGAEVAMIFQDpmTSLNPCYTV-GFQIMEAIKVhQGGNKKTRRQRAIDLLNQVGIPDPASRldvYPHQLSGGM 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 144 QQRIAIARALCTKQPIILFDEPTSALDPEMVQEVLDVMIELAQ-EDITMICVTHEMGFARQVADRVIFMEDGRILEEGTP 222
Cdd:PRK11022 159 SQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQkENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKA 238
|
250
....*....|
gi 1469315281 223 EHFFDNPENP 232
Cdd:PRK11022 239 HDIFRAPRHP 248
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
19-223 |
1.65e-27 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 109.74 E-value: 1.65e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 19 VLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPLTKKNHLEMARKYSSMVfQQFNLYPNmTVLG 98
Cdd:TIGR01842 333 TLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGKHIGYLP-QDVELFPG-TVAE 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 99 NLTLAPIKLQKKSKEEATEIA-----IAALKRvGMAHKAGEYPQNLSGGQQQRIAIARALCTKQPIILFDEPTSALDPEM 173
Cdd:TIGR01842 411 NIARFGENADPEKIIEAAKLAgvhelILRLPD-GYDTVIGPGGATLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEG 489
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1469315281 174 VQEVLDVMIELAQEDITMICVTHEMGfARQVADRVIFMEDGRILEEGTPE 223
Cdd:TIGR01842 490 EQALANAIKALKARGITVVVITHRPS-LLGCVDKILVLQDGRIARFGERD 538
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
6-216 |
1.90e-27 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 109.34 E-value: 1.90e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 6 EIKHLNkyfgDLHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPLTKKNHLEMARKysSMVF 85
Cdd:COG1129 258 EVEGLS----VGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDAIRA--GIAY 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 86 -----QQFNLYPNMTVLGNLTLAPIK-------LQKKSKEEATEIAIAAL--KRVGMAHKAGeypqNLSGGQQQRIAIAR 151
Cdd:COG1129 332 vpedrKGEGLVLDLSIRENITLASLDrlsrgglLDRRRERALAEEYIKRLriKTPSPEQPVG----NLSGGNQQKVVLAK 407
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1469315281 152 ALCTKQPIILFDEPTSALDpemV---QEVLDVMIELAQEDITMICVTHEMGFARQVADRVIFMEDGRI 216
Cdd:COG1129 408 WLATDPKVLILDEPTRGID---VgakAEIYRLIRELAAEGKAVIVISSELPELLGLSDRILVMREGRI 472
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
5-227 |
4.37e-27 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 106.45 E-value: 4.37e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 5 IEIKHLNKYFGDLHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPLTKKNHLemARKYSSMV 84
Cdd:PRK13536 42 IDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARL--ARARIGVV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 85 FQQFNLYPNMTVLGNLTLAPIKLQKKSKEeaTEIAIAALKRVG-MAHKAGEYPQNLSGGQQQRIAIARALCTKQPIILFD 163
Cdd:PRK13536 120 PQFDNLDLEFTVRENLLVFGRYFGMSTRE--IEAVIPSLLEFArLESKADARVSDLSGGMKRRLTLARALINDPQLLILD 197
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1469315281 164 EPTSALDPEMVQEVLDVMIELAQEDITMICVTHEMGFARQVADRVIFMEDGRILEEGTPEHFFD 227
Cdd:PRK13536 198 EPTTGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHALID 261
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-228 |
4.60e-27 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 104.19 E-value: 4.60e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 1 MADMIEIKHLNKYFGDLHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPLTKKNHLEMARKY 80
Cdd:PRK11614 2 EKVMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMREA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 81 SSMVFQQFNLYPNMTVLGNLTLAPIKLQKKSKEEATEIAIAALKRVG--MAHKAGeypqNLSGGQQQRIAIARALCTKQP 158
Cdd:PRK11614 82 VAIVPEGRRVFSRMTVEENLAMGGFFAERDQFQERIKWVYELFPRLHerRIQRAG----TMSGGEQQMLAIGRALMSQPR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 159 IILFDEPTSALDPEMVQEVLDVMIELAQEDITMICVTHEMGFARQVADRVIFMEDGRILEEGTPEHFFDN 228
Cdd:PRK11614 158 LLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHVVLEDTGDALLAN 227
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-215 |
7.05e-27 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 107.71 E-value: 7.05e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 1 MADMIEIKHLNKYFGDLHVLKDINLTVKRGEKLVMIGPSGSGKSTLIR--CVDYLEEPTSGEVLIDGTPLTKKNHLEMAR 78
Cdd:PRK13549 2 MEYLLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKvlSGVYPHGTYEGEIIFEGEELQASNIRDTER 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 79 KYSSMVFQQFNLYPNMTVLGNLTLA--PIKLQKKSKEEATEIAIAALKRVGMAHKAGEYPQNLSGGQQQRIAIARALCTK 156
Cdd:PRK13549 82 AGIAIIHQELALVKELSVLENIFLGneITPGGIMDYDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQ 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1469315281 157 QPIILFDEPTSALDPEMVQEVLDVMIELAQEDITMICVTHEMGFARQVADRVIFMEDGR 215
Cdd:PRK13549 162 ARLLILDEPTASLTESETAVLLDIIRDLKAHGIACIYISHKLNEVKAISDTICVIRDGR 220
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
4-209 |
1.74e-26 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 102.10 E-value: 1.74e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 4 MIEIKHLNKYFGDLHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPLTKKNHlEMARKYSSM 83
Cdd:PRK10247 7 LLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKP-EIYRQQVSY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 84 VFQQFNLYPNmTVLGNLTLaPIKLQKKSKEEAteIAIAALKRVGMAHKAGEYPQN-LSGGQQQRIAIARALCTKQPIILF 162
Cdd:PRK10247 86 CAQTPTLFGD-TVYDNLIF-PWQIRNQQPDPA--IFLDDLERFALPDTILTKNIAeLSGGEKQRISLIRNLQFMPKVLLL 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1469315281 163 DEPTSALDPEMVQEVLDVMIELAQE-DITMICVTHEMGFARQvADRVI 209
Cdd:PRK10247 162 DEITSALDESNKHNVNEIIHRYVREqNIAVLWVTHDKDEINH-ADKVI 208
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
4-196 |
2.66e-26 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 101.10 E-value: 2.66e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 4 MIEIKHLNKYFGDLHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGtpltKKNHLEMARKYSSM 83
Cdd:PRK13539 2 MLEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDG----GDIDDPDVAEACHY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 84 VFQQFNLYPNMTVLGNLTL-APIKLQkkskeEATEIAiAALKRVGMAHKAGEYPQNLSGGQQQRIAIARALCTKQPIILF 162
Cdd:PRK13539 78 LGHRNAMKPALTVAENLEFwAAFLGG-----EELDIA-AALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWIL 151
|
170 180 190
....*....|....*....|....*....|....*
gi 1469315281 163 DEPTSALDPEMVQEVLDVMIE-LAQEDItMICVTH 196
Cdd:PRK13539 152 DEPTAALDAAAVALFAELIRAhLAQGGI-VIAATH 185
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
16-241 |
4.39e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 102.78 E-value: 4.39e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 16 DLHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDG----TPLTKKNHLEMARKYSSMVFQ--QFN 89
Cdd:PRK13645 23 EFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDyaipANLKKIKEVKRLRKEIGLVFQfpEYQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 90 LYPNmTVLGNLTLAPIKLqKKSKEEATEIAIAALKRVGMAHK-AGEYPQNLSGGQQQRIAIARALCTKQPIILFDEPTSA 168
Cdd:PRK13645 103 LFQE-TIEKDIAFGPVNL-GENKQEAYKKVPELLKLVQLPEDyVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGG 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1469315281 169 LDPEMVQEVLDVMIELAQE-DITMICVTHEMGFARQVADRVIFMEDGRILEEGTPEHFFDNpenprcREFLSKI 241
Cdd:PRK13645 181 LDPKGEEDFINLFERLNKEyKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFSN------QELLTKI 248
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
20-218 |
4.50e-26 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 105.82 E-value: 4.50e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 20 LKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPLTKKNhLEMARKYSSMVFQQFNLYPNMtvlgn 99
Cdd:PRK10522 339 VGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQ-PEDYRKLFSAVFTDFHLFDQL----- 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 100 ltlapikLQKKSKEEATEIAIAALKRVGMAHK---AGEYPQN--LSGGQQQRIAIARALCTKQPIILFDEPTSALDPEMV 174
Cdd:PRK10522 413 -------LGPEGKPANPALVEKWLERLKMAHKlelEDGRISNlkLSKGQKKRLALLLALAEERDILLLDEWAADQDPHFR 485
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1469315281 175 QEVLDVMIELAQE-DITMICVTHEMGFARQvADRVIFMEDGRILE 218
Cdd:PRK10522 486 REFYQVLLPLLQEmGKTIFAISHDDHYFIH-ADRLLEMRNGQLSE 529
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
5-223 |
6.46e-26 |
|
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: 99.91 E-value: 6.46e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 5 IEIKHLNKYFGDLHVLKDINLTVKRGEKLVMIGPSGSGKSTLIR----CVDYleEPTSGEVLIDGTPLTKKNHLEMARKY 80
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKtimgHPKY--EVTEGEILFKGEDITDLPPEERARLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 81 SSMVFQqfnlYPnmtvlgnltlapiklqkkskEEATEIAIAALKR-VGMahkageypqNLSGGQQQRIAIARALCTKQPI 159
Cdd:cd03217 79 IFLAFQ----YP--------------------PEIPGVKNADFLRyVNE---------GFSGGEKKRNEILQLLLLEPDL 125
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1469315281 160 ILFDEPTSALDPEMVQEVLDVMIELAQEDITMICVTH-EMGFARQVADRVIFMEDGRILEEGTPE 223
Cdd:cd03217 126 AILDEPDSGLDIDALRLVAEVINKLREEGKSVLIITHyQRLLDYIKPDRVHVLYDGRIVKSGDKE 190
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
5-227 |
9.56e-26 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 102.19 E-value: 9.56e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 5 IEIKHLNKYFGDLHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPLTKKNHLemARKYSSMV 84
Cdd:PRK13537 8 IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARH--ARQRVGVV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 85 FQQFNLYPNMTVLGNLtLAPIKLQKKSKEEATEIAIAALKRVGMAHKAGEYPQNLSGGQQQRIAIARALCTKQPIILFDE 164
Cdd:PRK13537 86 PQFDNLDPDFTVRENL-LVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDE 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1469315281 165 PTSALDPEMVQEVLDVMIELAQEDITMICVTHEMGFARQVADRVIFMEDGRILEEGTPEHFFD 227
Cdd:PRK13537 165 PTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIE 227
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
5-221 |
1.33e-25 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 104.54 E-value: 1.33e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 5 IEIKHLNKYFGDLHVLKD-INLTVKRGEKLVMIGPSGSGKSTLIRCV-DYLeePTSGEVLIDGTPLtkkNHLEMA--RKY 80
Cdd:PRK11174 350 IEAEDLEILSPDGKTLAGpLNFTLPAGQRIALVGPSGAGKTSLLNALlGFL--PYQGSLKINGIEL---RELDPEswRKH 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 81 SSMVFQQFNLyPNMTVLGNLTLApiklqkksKEEATEIAI-AALKRV-----------GMAHKAGEYPQNLSGGQQQRIA 148
Cdd:PRK11174 425 LSWVGQNPQL-PHGTLRDNVLLG--------NPDASDEQLqQALENAwvseflpllpqGLDTPIGDQAAGLSVGQAQRLA 495
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1469315281 149 IARALCTKQPIILFDEPTSALDPEMVQEVLDVMIELAQeDITMICVTHEMGFARQVaDRVIFMEDGRILEEGT 221
Cdd:PRK11174 496 LARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASR-RQTTLMVTHQLEDLAQW-DQIWVMQDGQIVQQGD 566
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
23-222 |
1.72e-25 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 104.71 E-value: 1.72e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 23 INLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPLtkKNHLEMARKYSSMVFQQFNLYPNMTVLGNLtL 102
Cdd:TIGR01257 949 LNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI--ETNLDAVRQSLGMCPQHNILFHHLTVAEHI-L 1025
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 103 APIKLQKKSKEEATEIAIAALKRVGMAHKAGEYPQNLSGGQQQRIAIARALCTKQPIILFDEPTSALDPEMVQEVLDVMI 182
Cdd:TIGR01257 1026 FYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLL 1105
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1469315281 183 ELaQEDITMICVTHEMGFARQVADRVIFMEDGRILEEGTP 222
Cdd:TIGR01257 1106 KY-RSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTP 1144
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
5-220 |
1.77e-25 |
|
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: 99.53 E-value: 1.77e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 5 IEIKHLNKYF----------------------GDLHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVL 62
Cdd:cd03220 1 IELENVSKSYptykggssslkklgilgrkgevGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 63 IDGTPltkknhlemarkySSMVFQQFNLYPNMTVLGNLTL-APIKLQKKSKEEATEIAIAALKRVGmahKAGEYP-QNLS 140
Cdd:cd03220 81 VRGRV-------------SSLLGLGGGFNPELTGRENIYLnGRLLGLSRKEIDEKIDEIIEFSELG---DFIDLPvKTYS 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 141 GGQQQRIAIARALCTKQPIILFDEPTSALDPEMVQEVLDVMIELAQEDITMICVTHEMGFARQVADRVIFMEDGRILEEG 220
Cdd:cd03220 145 SGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
16-223 |
2.66e-25 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 99.53 E-value: 2.66e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 16 DLHV---LKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLeEPTSGEVLIDGTPLTKKNHLEMARkYSSMVFQQFNLYP 92
Cdd:COG4138 5 DVAVagrLGPISAQVNAGELIHLIGPNGAGKSTLLARMAGL-LPGQGEILLNGRPLSDWSAAELAR-HRAYLSQQQSPPF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 93 NMTVLGNLTLApikLQKKSKEEATEIAIAAL-KRVGMAHKAGEYPQNLSGGQQQRIAIARALCTKQP-------IILFDE 164
Cdd:COG4138 83 AMPVFQYLALH---QPAGASSEAVEQLLAQLaEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLQVWPtinpegqLLLLDE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1469315281 165 PTSALDpeMVQEV-LDVMI-ELAQEDITMICVTHEMGFARQVADRVIFMEDGRILEEGTPE 223
Cdd:COG4138 160 PMNSLD--VAQQAaLDRLLrELCQQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETA 218
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
4-215 |
2.68e-25 |
|
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: 103.37 E-value: 2.68e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 4 MIEIKHLNKYFGDLHVLKDINLTVKRGEKLVMIGPSGSGKSTLIR--CVDYLEEPTSGEVLIDGTPLTKKNHLEMARKYS 81
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKilSGVYPHGTWDGEIYWSGSPLKASNIRDTERAGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 82 SMVFQQFNLYPNMTVLGNLTLA---PIKLQKKSKEEATEIAIAALKRVGMAHKAGEYP-QNLSGGQQQRIAIARALCTKQ 157
Cdd:TIGR02633 81 VIIHQELTLVPELSVAENIFLGneiTLPGGRMAYNAMYLRAKNLLRELQLDADNVTRPvGDYGGGQQQLVEIAKALNKQA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1469315281 158 PIILFDEPTSALDPEMVQEVLDVMIELAQEDITMICVTHEMGFARQVADRVIFMEDGR 215
Cdd:TIGR02633 161 RLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQ 218
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
7-216 |
3.49e-25 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 103.22 E-value: 3.49e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 7 IKHLNKYFGDLHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVlidgtplTKKNHLEMArkyssMVFQ 86
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEV-------SIPKGLRIG-----YLPQ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 87 QFNLYPNMTVL-----GNLTLAPIKLQKKSKEEATEIAIAALKRVGMAH----KAGEY---------------------- 135
Cdd:COG0488 69 EPPLDDDLTVLdtvldGDAELRALEAELEELEAKLAEPDEDLERLAELQeefeALGGWeaearaeeilsglgfpeedldr 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 136 -PQNLSGGQQQRIAIARALCTKQPIILFDEPTSALDPEmvqevldvMIE-----LAQEDITMICVTHEMGFARQVADRVI 209
Cdd:COG0488 149 pVSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLE--------SIEwleefLKNYPGTVLVVSHDRYFLDRVATRIL 220
|
....*..
gi 1469315281 210 FMEDGRI 216
Cdd:COG0488 221 ELDRGKL 227
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1-215 |
1.37e-24 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 101.14 E-value: 1.37e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 1 MADMIEIKHLNKYFGDLHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPLTKKNHLEMARKY 80
Cdd:PRK11288 1 SSPYLSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAALAAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 81 SSMVFQQFNLYPNMTVLGNLTLA--PIKLQKKSKEEATEIAIAALKRVGMAHKAGEYPQNLSGGQQQRIAIARALCTKQP 158
Cdd:PRK11288 81 VAIIYQELHLVPEMTVAENLYLGqlPHKGGIVNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNAR 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1469315281 159 IILFDEPTSALDPEMVQEVLDVMIELAQEDITMICVTHEMGFARQVADRVIFMEDGR 215
Cdd:PRK11288 161 VIAFDEPTSSLSAREIEQLFRVIRELRAEGRVILYVSHRMEEIFALCDAITVFKDGR 217
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
2-196 |
2.65e-24 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 100.65 E-value: 2.65e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 2 ADMIEIKHLNKYFGDLHVL-KDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEV----------------LID 64
Cdd:COG4178 360 DGALALEDLTLRTPDGRPLlEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIarpagarvlflpqrpyLPL 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 65 GTpLtkKNHLemarkyssmvfqqfnLYPNmtvlgnltlapiklqkkSKEEATEIAI-AALKRVGMAHKAG------EYPQ 137
Cdd:COG4178 440 GT-L--REAL---------------LYPA-----------------TAEAFSDAELrEALEAVGLGHLAErldeeaDWDQ 484
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1469315281 138 NLSGGQQQRIAIARALCTKQPIILFDEPTSALDPEMVQEVLDvMIELAQEDITMICVTH 196
Cdd:COG4178 485 VLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQ-LLREELPGTTVISVGH 542
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
19-224 |
6.59e-24 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 96.40 E-value: 6.59e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 19 VLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPLTKKNHLEMARKYSSMVfQQFNLYPNMTV-- 96
Cdd:PRK10575 26 LLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLP-QQLPAAEGMTVre 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 97 ------------LGNLTLApiklQKKSKEEAteIAIAALKRvgMAHKAGEypqNLSGGQQQRIAIARALCTKQPIILFDE 164
Cdd:PRK10575 105 lvaigrypwhgaLGRFGAA----DREKVEEA--ISLVGLKP--LAHRLVD---SLSGGERQRAWIAMLVAQDSRCLLLDE 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1469315281 165 PTSALDPEMVQEVLDVMIELAQE-DITMICVTHEMGFARQVADRVIFMEDGRILEEGTPEH 224
Cdd:PRK10575 174 PTSALDIAHQVDVLALVHRLSQErGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAE 234
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
6-219 |
1.93e-23 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 98.32 E-value: 1.93e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 6 EIKHLNKYfgDLHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPLTKKNHLEMARKYSSMV- 84
Cdd:PRK09700 267 EVRNVTSR--DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDAVKKGMAYIt 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 85 --------FQQFNLYPNMTVLGNLTLAPIKLQKKSKEEATEIAIAALKRVGMAHKAGEYPQN---LSGGQQQRIAIARAL 153
Cdd:PRK09700 345 esrrdngfFPNFSIAQNMAISRSLKDGGYKGAMGLFHEVDEQRTAENQRELLALKCHSVNQNiteLSGGNQQKVLISKWL 424
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1469315281 154 CTKQPIILFDEPTSALDPEMVQEVLDVMIELAQEDITMICVTHEMGFARQVADRVIFMEDGRILEE 219
Cdd:PRK09700 425 CCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRLTQI 490
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
23-223 |
5.11e-23 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 93.46 E-value: 5.11e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 23 INLTVKRGEKLVMIGPSGSGKSTLIRCVDYLeEPTSGEVLIDGTPLTKKNHLEMARkYSSMVFQQFNLYPNMTVLGNLTL 102
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGL-LPGSGSIQFAGQPLEAWSAAELAR-HRAYLSQQQTPPFAMPVFQYLTL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 103 ApikLQKKSKEEATEIAIAAL-KRVGMAHKAGEYPQNLSGGQQQRIAIARALCTKQPII-------LFDEPTSALDpeMV 174
Cdd:PRK03695 93 H---QPDKTRTEAVASALNEVaEALGLDDKLGRSVNQLSGGEWQRVRLAAVVLQVWPDInpagqllLLDEPMNSLD--VA 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1469315281 175 QEV-LDVMI-ELAQEDITMICVTHEMGFARQVADRVIFMEDGRILEEGTPE 223
Cdd:PRK03695 168 QQAaLDRLLsELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRD 218
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-230 |
7.24e-23 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 93.25 E-value: 7.24e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 1 MADMIEIKHLNKYFGDLHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLidgtpltKKNHLEMArky 80
Cdd:PRK09544 1 MTSLVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK-------RNGKLRIG--- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 81 ssMVFQQFNLYPNM--TVLGNLTLAPiklQKKSKEeateiAIAALKRVGMAHKAGEYPQNLSGGQQQRIAIARALCTKQP 158
Cdd:PRK09544 71 --YVPQKLYLDTTLplTVNRFLRLRP---GTKKED-----ILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQ 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1469315281 159 IILFDEPTSALDPEMVQEVLDVMIELAQE-DITMICVTHEMGFARQVADRVIFMeDGRILEEGTPEHFFDNPE 230
Cdd:PRK09544 141 LLVLDEPTQGVDVNGQVALYDLIDQLRRElDCAVLMVSHDLHLVMAKTDEVLCL-NHHICCSGTPEVVSLHPE 212
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1-228 |
1.20e-22 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 95.89 E-value: 1.20e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 1 MADMIEIKHLNKYFGDLHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPLTKKNHLEmARKY 80
Cdd:PRK15439 8 APPLLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAK-AHQL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 81 S-SMVFQQFNLYPNMTVLGNLTLAPIKLQkKSKEEATEIaIAALK-RVGMAHKAGeypqNLSGGQQQRIAIARALCTKQP 158
Cdd:PRK15439 87 GiYLVPQEPLLFPNLSVKENILFGLPKRQ-ASMQKMKQL-LAALGcQLDLDSSAG----SLEVADRQIVEILRGLMRDSR 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 159 IILFDEPTSALDPEMVQEVLDVMIELAQEDITMICVTHEMGFARQVADRVIFMEDGRILEEGTPEHFFDN 228
Cdd:PRK15439 161 ILILDEPTASLTPAETERLFSRIRELLAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTADLSTD 230
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
23-224 |
1.22e-22 |
|
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: 96.02 E-value: 1.22e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 23 INLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPLTKKNhLEMARKYSSMVFQQFNLYPNMTVLGNLTL 102
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADN-REAYRQLFSAVFSDFHLFDRLLGLDGEAD 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 103 ApiklqkkskEEATEIaiaaLKRVGMAHK----AGEY-PQNLSGGQQQRIAIARALCTKQPIILFDEPTSALDPE----M 173
Cdd:COG4615 430 P---------ARAREL----LERLELDHKvsveDGRFsTTDLSQGQRKRLALLVALLEDRPILVFDEWAADQDPEfrrvF 496
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1469315281 174 VQEVLdvmIELAQEDITMICVTH-EMGFarQVADRVIFMEDGRILEEGTPEH 224
Cdd:COG4615 497 YTELL---PELKARGKTVIAISHdDRYF--DLADRVLKMDYGKLVELTGPAA 543
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1-233 |
2.19e-22 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 91.88 E-value: 2.19e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 1 MADMIEiKHLNKYFGDLHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPLTKKNHLEMARKY 80
Cdd:PRK10895 1 MATLTA-KNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 81 SSMVFQQFNLYPNMTVLGNLtLAPIKLQKK-SKEEATEIAIAALKRVGMAHKAGEYPQNLSGGQQQRIAIARALCTKQPI 159
Cdd:PRK10895 80 IGYLPQEASIFRRLSVYDNL-MAVLQIRDDlSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKF 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1469315281 160 ILFDEPTSALDPEMVQEVLDVMIELAQEDITMICVTHEMGFARQVADRVIFMEDGRILEEGTPEHFFDNPENPR 233
Cdd:PRK10895 159 ILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDEHVKR 232
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
5-222 |
3.78e-22 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 90.55 E-value: 3.78e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 5 IEIKHLN-KYFGDL-HVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPlTKKNHLEMARKYSS 82
Cdd:cd03369 7 IEVENLSvRYAPDLpPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGID-ISTIPLEDLRSSLT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 83 MVFQQFNLYPNmTVLGNLtlapiklqkKSKEEATEIAIAALKRVGmahkagEYPQNLSGGQQQRIAIARALCTKQPIILF 162
Cdd:cd03369 86 IIPQDPTLFSG-TIRSNL---------DPFDEYSDEEIYGALRVS------EGGLNLSQGQRQLLCLARALLKRPRVLVL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1469315281 163 DEPTSALDPEMVQEVLDVMIELAQeDITMICVTHEMgfaRQVA--DRVIFMEDGRILEEGTP 222
Cdd:cd03369 150 DEATASIDYATDALIQKTIREEFT-NSTILTIAHRL---RTIIdyDKILVMDAGEVKEYDHP 207
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
15-174 |
6.70e-22 |
|
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: 89.34 E-value: 6.70e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 15 GDLHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPLTK-KNHLEMARKYSSmvfQQFNLYPN 93
Cdd:TIGR01189 11 GERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEqRDEPHENILYLG---HLPGLKPE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 94 MTVLGNLT-LAPIKlqkkskEEATEIAIAALKRVGMAHKAGEYPQNLSGGQQQRIAIARALCTKQPIILFDEPTSALDPE 172
Cdd:TIGR01189 88 LSALENLHfWAAIH------GGAQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKA 161
|
..
gi 1469315281 173 MV 174
Cdd:TIGR01189 162 GV 163
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
14-230 |
8.92e-22 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 90.84 E-value: 8.92e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 14 FGDLHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPLT-KKNHLEMARKYSSMVFQ---QFN 89
Cdd:PRK13638 11 YQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDySKRGLLALRQQVATVFQdpeQQI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 90 LYPNMTV-----LGNLTLAPIKLQKKSKEeateiaiaALKRVGMAHKAGEYPQNLSGGQQQRIAIARALCTKQPIILFDE 164
Cdd:PRK13638 91 FYTDIDSdiafsLRNLGVPEAEITRRVDE--------ALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1469315281 165 PTSALDPEMVQEVLDVMIELAQEDITMICVTHEMGFARQVADRVIFMEDGRILEEGTPEHFFDNPE 230
Cdd:PRK13638 163 PTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVFACTE 228
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
5-228 |
1.07e-21 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 93.65 E-value: 1.07e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 5 IEIKhlNKYF-----GDLHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVdyLEE--PTS-GEVLIDGTPltkknhlem 76
Cdd:PLN03130 615 ISIK--NGYFswdskAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAM--LGElpPRSdASVVIRGTV--------- 681
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 77 arKYSSMVFQQFNlypnMTVLGNLTL-APIKLQKKSKEeateIAIAALKRV------GMAHKAGEYPQNLSGGQQQRIAI 149
Cdd:PLN03130 682 --AYVPQVSWIFN----ATVRDNILFgSPFDPERYERA----IDVTALQHDldllpgGDLTEIGERGVNISGGQKQRVSM 751
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1469315281 150 ARALCTKQPIILFDEPTSALDPEMVQEVLDVMIELAQEDITMICVTHEMGFARQVaDRVIFMEDGRILEEGTPEHFFDN 228
Cdd:PLN03130 752 ARAVYSNSDVYIFDDPLSALDAHVGRQVFDKCIKDELRGKTRVLVTNQLHFLSQV-DRIILVHEGMIKEEGTYEELSNN 829
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
5-223 |
1.61e-21 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 92.88 E-value: 1.61e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 5 IEIKHLNKYFGDLHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPLTKKNhLEMARK--YSS 82
Cdd:NF033858 267 IEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDAGD-IATRRRvgYMS 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 83 mvfQQFNLYPNMTVLGNLTL-ApiKLQKKSKEEATEIAIAALKRVGMAHKAGEYPQNLSGGQQQRIAIARALCTKQPIIL 161
Cdd:NF033858 346 ---QAFSLYGELTVRQNLELhA--RLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLI 420
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1469315281 162 FDEPTSALDPEMVQEVLDVMIELAQED-ITMICVTHEMGFArQVADRVIFMEDGRILEEGTPE 223
Cdd:NF033858 421 LDEPTSGVDPVARDMFWRLLIELSREDgVTIFISTHFMNEA-ERCDRISLMHAGRVLASDTPA 482
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
12-222 |
1.95e-21 |
|
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: 92.70 E-value: 1.95e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 12 KYFGDLH-VLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPLTKKNhLEMARkyssmvfQQFNL 90
Cdd:TIGR00957 1293 RYREDLDlVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIG-LHDLR-------FKITI 1364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 91 YPNMTVL--GNLTLAPIKLQKKSKEEA-TEIAIAALKRV------GMAHKAGEYPQNLSGGQQQRIAIARALCTKQPIIL 161
Cdd:TIGR00957 1365 IPQDPVLfsGSLRMNLDPFSQYSDEEVwWALELAHLKTFvsalpdKLDHECAEGGENLSVGQRQLVCLARALLRKTKILV 1444
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1469315281 162 FDEPTSALDPEmVQEVLDVMIELAQEDITMICVTHEMgfaRQVAD--RVIFMEDGRILEEGTP 222
Cdd:TIGR00957 1445 LDEATAAVDLE-TDNLIQSTIRTQFEDCTVLTIAHRL---NTIMDytRVIVLDKGEVAEFGAP 1503
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
15-196 |
4.76e-21 |
|
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: 87.16 E-value: 4.76e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 15 GDLHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPLtkknHLEMARKYSSMVF--QQFNLYP 92
Cdd:cd03231 11 DGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPL----DFQRDSIARGLLYlgHAPGIKT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 93 NMTVLGNLT-LAPIklqkkskeEATEIAIAALKRVGMA---HKAGEYpqnLSGGQQQRIAIARALCTKQPIILFDEPTSA 168
Cdd:cd03231 87 TLSVLENLRfWHAD--------HSDEQVEEALARVGLNgfeDRPVAQ---LSAGQQRRVALARLLLSGRPLWILDEPTTA 155
|
170 180
....*....|....*....|....*...
gi 1469315281 169 LDPEMVQEVLDVMIELAQEDITMICVTH 196
Cdd:cd03231 156 LDKAGVARFAEAMAGHCARGGMVVLTTH 183
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
4-222 |
7.31e-21 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 88.35 E-value: 7.31e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 4 MIEIKHLNKYFGDLHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCV--DYLEEPTS------GEVLIDGTPLTKKNHLE 75
Cdd:PRK13547 1 MLTADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALagDLTGGGAPrgarvtGDVTLNGEPLAAIDAPR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 76 MARKYSSMVFQQFNLYP----NMTVLGNLTLApiKLQKKSKEEATEIAIAALKRVGMAHKAGEYPQNLSGGQQQRIAIAR 151
Cdd:PRK13547 81 LARLRAVLPQAAQPAFAfsarEIVLLGRYPHA--RRAGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFAR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 152 ALCTKQP---------IILFDEPTSALDPEMVQEVLDVMIELAQE-DITMICVTHEMGFARQVADRVIFMEDGRILEEGT 221
Cdd:PRK13547 159 VLAQLWPphdaaqpprYLLLDEPTAALDLAHQHRLLDTVRRLARDwNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGA 238
|
.
gi 1469315281 222 P 222
Cdd:PRK13547 239 P 239
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
19-196 |
1.45e-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: 84.90 E-value: 1.45e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 19 VLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIdgtpLTKKNHLEMARKyssmvfqqfnlyPNMTvLG 98
Cdd:cd03223 16 LLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGM----PEGEDLLFLPQR------------PYLP-LG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 99 NLtlapiklqkksKEeateiAIAalkrvgmahkageYP--QNLSGGQQQRIAIARALCTKQPIILFDEPTSALDPEMVQE 176
Cdd:cd03223 79 TL-----------RE-----QLI-------------YPwdDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDR 129
|
170 180
....*....|....*....|
gi 1469315281 177 VLDVmieLAQEDITMICVTH 196
Cdd:cd03223 130 LYQL---LKELGITVISVGH 146
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
5-229 |
2.38e-20 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 89.39 E-value: 2.38e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 5 IEIKHLNKYFGDLHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPLTKKnHLEMARKYSSMV 84
Cdd:PRK10789 316 VNIRQFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKL-QLDSWRSRLAVV 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 85 FQQFNLYPNmTVLGNLTLAPIKLQKKSKEEATEIA-----IAALKRvGMAHKAGEYPQNLSGGQQQRIAIARALCTKQPI 159
Cdd:PRK10789 395 SQTPFLFSD-TVANNIALGRPDATQQEIEHVARLAsvhddILRLPQ-GYDTEVGERGVMLSGGQKQRISIARALLLNAEI 472
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 160 ILFDEPTSALDPEMVQEVLDVMIELAQEDiTMICVTHEMGfARQVADRVIFMEDGRILEEGTPEHFFDNP 229
Cdd:PRK10789 473 LILDDALSAVDGRTEHQILHNLRQWGEGR-TVIISAHRLS-ALTEASEILVMQHGHIAQRGNHDQLAQQS 540
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
4-216 |
2.51e-20 |
|
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: 89.11 E-value: 2.51e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 4 MIEIKHLNKYFGDLHVLK---DINLTVKRGEKLVMIGPSGSGKSTLIRCV-DYLEEPTSGEVLIDGTPLTKKNHLEMARK 79
Cdd:TIGR02633 257 ILEARNLTCWDVINPHRKrvdDVSFSLRRGEILGVAGLVGAGRTELVQALfGAYPGKFEGNVFINGKPVDIRNPAQAIRA 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 80 YSSMV---FQQFNLYPNMTVLGNLTLAPI-KLQKKSK--EEATEIAI-AALKRVGMAHKAGEYP-QNLSGGQQQRIAIAR 151
Cdd:TIGR02633 337 GIAMVpedRKRHGIVPILGVGKNITLSVLkSFCFKMRidAAAELQIIgSAIQRLKVKTASPFLPiGRLSGGNQQKAVLAK 416
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1469315281 152 ALCTKQPIILFDEPTSALDPEMVQEVLDVMIELAQEDITMICVTHEMGFARQVADRVIFMEDGRI 216
Cdd:TIGR02633 417 MLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGKL 481
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
19-220 |
2.97e-20 |
|
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: 85.85 E-value: 2.97e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 19 VLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDG-TPLTKKNhlEMARKYSSMVFQQFNLYPNMTVL 97
Cdd:cd03267 36 ALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGlVPWKRRK--KFLRRIGVVFGQKTQLWWDLPVI 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 98 GNLTL-------APIKLQKKSKEEATEIAIAALKRVGMahkageypQNLSGGQQQRIAIARALCTKQPIILFDEPTSALD 170
Cdd:cd03267 114 DSFYLlaaiydlPPARFKKRLDELSELLDLEELLDTPV--------RQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLD 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1469315281 171 ---PEMVQEVLDvmIELAQEDITMICVTHEMGFARQVADRVIFMEDGRILEEG 220
Cdd:cd03267 186 vvaQENIRNFLK--EYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
5-221 |
3.83e-20 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 88.62 E-value: 3.83e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 5 IEIKHLN-KYFGDLHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPLTKKNHlEMARKYSSM 83
Cdd:PRK10790 341 IDIDNVSfAYRDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSH-SVLRQGVAM 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 84 VfQQfnlypNMTVLGNLTLAPIKLQKKSKEEAT-----EIAIAALKRV---GMAHKAGEYPQNLSGGQQQRIAIARALCT 155
Cdd:PRK10790 420 V-QQ-----DPVVLADTFLANVTLGRDISEEQVwqaleTVQLAELARSlpdGLYTPLGEQGNNLSVGQKQLLALARVLVQ 493
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1469315281 156 KQPIILFDEPTSALDP---EMVQEVLdvmiELAQEDITMICVTHEMGFARQvADRVIFMEDGRILEEGT 221
Cdd:PRK10790 494 TPQILILDEATANIDSgteQAIQQAL----AAVREHTTLVVIAHRLSTIVE-ADTILVLHRGQAVEQGT 557
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
10-215 |
4.90e-20 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 88.25 E-value: 4.90e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 10 LNKYFGDLHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPLTKKNHLEMARKYSSMVFQQFN 89
Cdd:PRK10982 4 ISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEALENGISMVHQELN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 90 LYPNMTVLGNLTLA--PI--------KLQKKSKEEATEIAIAALKRVGMAhkageypqNLSGGQQQRIAIARALCTKQPI 159
Cdd:PRK10982 84 LVLQRSVMDNMWLGryPTkgmfvdqdKMYRDTKAIFDELDIDIDPRAKVA--------TLSVSQMQMIEIAKAFSYNAKI 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1469315281 160 ILFDEPTSALDPEMVQEVLDVMIELAQEDITMICVTHEMGFARQVADRVIFMEDGR 215
Cdd:PRK10982 156 VIMDEPTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQ 211
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
20-226 |
6.89e-20 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 85.70 E-value: 6.89e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 20 LKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPLTK--KNHLEMARKYSSMVFQQFN-LYPNMTV 96
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQalQKNLVAYVPQSEEVDWSFPvLVEDVVM 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 97 LGNLtlAPIKLQKKSKEEATEIAIAALKRVGMAHKAGEYPQNLSGGQQQRIAIARALCTKQPIILFDEPTSALDPEMVQE 176
Cdd:PRK15056 103 MGRY--GHMGWLRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEAR 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1469315281 177 VLDVMIELAQEDITMICVTHEMGFARQVADRVIfMEDGRILEEGTPEHFF 226
Cdd:PRK15056 181 IISLLRELRDEGKTMLVSTHNLGSVTEFCDYTV-MVKGTVLASGPTETTF 229
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
4-218 |
2.62e-19 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 86.00 E-value: 2.62e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 4 MIEIKHLNKYFGDLHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCV-------DYleeptSGEVLIDGTPLTKKN---- 72
Cdd:NF040905 1 ILEMRGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLsgvyphgSY-----EGEILFDGEVCRFKDirds 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 73 --------HLEMArkyssmvfqqfnLYPNMTV-----LGNltlapiklqKKSK------EEATEIAIAALKRVGMAhkag 133
Cdd:NF040905 76 ealgiviiHQELA------------LIPYLSIaenifLGN---------ERAKrgvidwNETNRRARELLAKVGLD---- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 134 EYPQNLSG----GQQQRIAIARALCTKQPIILFDEPTSALDPEMVQEVLDVMIELAQEDITMICVTHEMGFARQVADRVI 209
Cdd:NF040905 131 ESPDTLVTdigvGKQQLVEIAKALSKDVKLLILDEPTAALNEEDSAALLDLLLELKAQGITSIIISHKLNEIRRVADSIT 210
|
....*....
gi 1469315281 210 FMEDGRILE 218
Cdd:NF040905 211 VLRDGRTIE 219
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
7-214 |
3.70e-18 |
|
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: 80.07 E-value: 3.70e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 7 IKHLNKYF---GDLHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGT-PLTKKNHLEMAR-KYS 81
Cdd:cd03290 1 VQVTNGYFswgSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKnESEPSFEATRSRnRYS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 82 SMVFQQFNLYPNMTVLGNLTL-APIKLQK-KSKEEATEIA--IAALKrVGMAHKAGEYPQNLSGGQQQRIAIARALCTKQ 157
Cdd:cd03290 81 VAYAAQKPWLLNATVEENITFgSPFNKQRyKAVTDACSLQpdIDLLP-FGDQTEIGERGINLSGGQRQRICVARALYQNT 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1469315281 158 PIILFDEPTSALDPEMVQEVLDV-MIELAQEDI-TMICVTHEMGFARQvADRVIFMEDG 214
Cdd:cd03290 160 NIVFLDDPFSALDIHLSDHLMQEgILKFLQDDKrTLVLVTHKLQYLPH-ADWIIAMKDG 217
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
19-229 |
3.82e-18 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 83.29 E-value: 3.82e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 19 VLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLidgtpltkknhlemARKYSSMVFQQFNLYpNMTVLG 98
Cdd:PTZ00243 675 LLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVW--------------AERSIAYVPQQAWIM-NATVRG 739
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 99 NLTL----APIKLQKKSKEEATEIAIAALKRvGMAHKAGEYPQNLSGGQQQRIAIARALCTKQPIILFDEPTSALDPEMV 174
Cdd:PTZ00243 740 NILFfdeeDAARLADAVRVSQLEADLAQLGG-GLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVG 818
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1469315281 175 QEVLDVMIELAQEDITMICVTHEMGFARQvADRVIFMEDGRILEEGTPEHFFDNP 229
Cdd:PTZ00243 819 ERVVEECFLGALAGKTRVLATHQVHVVPR-ADYVVALGDGRVEFSGSSADFMRTS 872
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
5-230 |
7.01e-18 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 82.33 E-value: 7.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 5 IEIKhlNKYFG-DLHV----LKDINLTVKRGEKLVMIGPSGSGKSTLIRC-VDYLEEPTSGEVLIDGTPltkknhlemar 78
Cdd:PLN03232 615 ISIK--NGYFSwDSKTskptLSDINLEIPVGSLVAIVGGTGEGKTSLISAmLGELSHAETSSVVIRGSV----------- 681
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 79 KYSSMVFQQFNlypnMTVLGNLTLAPiklQKKSKEEATEIAIAALKR---VGMAH---KAGEYPQNLSGGQQQRIAIARA 152
Cdd:PLN03232 682 AYVPQVSWIFN----ATVRENILFGS---DFESERYWRAIDVTALQHdldLLPGRdltEIGERGVNISGGQKQRVSMARA 754
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1469315281 153 LCTKQPIILFDEPTSALDPEMVQEVLDVMIELAQEDITMICVTHEMGFARQVaDRVIFMEDGRILEEGTPEHFFDNPE 230
Cdd:PLN03232 755 VYSNSDIYIFDDPLSALDAHVAHQVFDSCMKDELKGKTRVLVTNQLHFLPLM-DRIILVSEGMIKEEGTFAELSKSGS 831
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
22-216 |
7.46e-18 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 81.90 E-value: 7.46e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 22 DINLTVKRGEKLVMIGPSGSGKSTLIRCV--DYlEEPTSGEVLIDGTPLTKKNHLEMARKYSSMVFQ---QFNLYPNMTV 96
Cdd:PRK13549 280 DVSFSLRRGEILGIAGLVGAGRTELVQCLfgAY-PGRWEGEIFIDGKPVKIRNPQQAIAQGIAMVPEdrkRDGIVPVMGV 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 97 LGNLTLApiKLQKKSK----EEATEIAIA--ALKRVGMAHKAGEYP-QNLSGGQQQRIAIARALCTKQPIILFDEPTSAL 169
Cdd:PRK13549 359 GKNITLA--ALDRFTGgsriDDAAELKTIleSIQRLKVKTASPELAiARLSGGNQQKAVLAKCLLLNPKILILDEPTRGI 436
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1469315281 170 DPEMVQEVLDVMIELAQEDITMICVTHEMGFARQVADRVIFMEDGRI 216
Cdd:PRK13549 437 DVGAKYEIYKLINQLVQQGVAIIVISSELPEVLGLSDRVLVMHEGKL 483
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
18-196 |
8.54e-18 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 79.23 E-value: 8.54e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 18 HVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCV--DYLEEPTSGEVlidgtpltkknhlemarkyssmVFQQFNLYPNMT 95
Cdd:COG2401 44 YVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLagALKGTPVAGCV----------------------DVPDNQFGREAS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 96 VLGNLtlapikLQKKSKEEATEIaiaaLKRVGMAhKAGEY---PQNLSGGQQQRIAIARALCTKQPIILFDEPTSALDPE 172
Cdd:COG2401 102 LIDAI------GRKGDFKDAVEL----LNAVGLS-DAVLWlrrFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQ 170
|
170 180
....*....|....*....|....*
gi 1469315281 173 MVQEVLDVMIELAQE-DITMICVTH 196
Cdd:COG2401 171 TAKRVARNLQKLARRaGITLVVATH 195
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-228 |
1.45e-17 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 80.13 E-value: 1.45e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 4 MIEIKHLNKYF----------GDL-----------HVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVL 62
Cdd:COG4586 1 IIEVENLSKTYrvyekepglkGALkglfrreyrevEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 63 IDG-TPLtkKNHLEMARKYsSMVFQQFN-LYPNMTVLGNLTLA------PIKLQKKSKEEATEI-AIAALKRVgmahkag 133
Cdd:COG4586 81 VLGyVPF--KRRKEFARRI-GVVFGQRSqLWWDLPAIDSFRLLkaiyriPDAEYKKRLDELVELlDLGELLDT------- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 134 eyP-QNLSGGQQQRIAIARALCTKQPIILFDEPTSALDPEMVQEVLDVMIELAQE-DITMICVTHEMGFARQVADRVIFM 211
Cdd:COG4586 151 --PvRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRErGTTILLTSHDMDDIEALCDRVIVI 228
|
250
....*....|....*..
gi 1469315281 212 EDGRILEEGTPEHFFDN 228
Cdd:COG4586 229 DHGRIIYDGSLEELKER 245
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
30-220 |
1.89e-17 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 81.08 E-value: 1.89e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 30 GEKLVMIGPSGSGKSTLIRCVDYLEEPTS--GEVLIDGTPLTKKnhlemARKYSSMVFQQFNLYPNMTVLGNLTL-APIK 106
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRKPTKQ-----ILKRTGFVTQDDILYPHLTVRETLVFcSLLR 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 107 LQKK-SKEEATEIAIAALKRVGMAH-----KAGEYPQNLSGGQQQRIAIARALCTKQPIILFDEPTSALDPEMVQEVLDV 180
Cdd:PLN03211 169 LPKSlTKQEKILVAESVISELGLTKcentiIGNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLT 248
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1469315281 181 MIELAQEDITMICVTHE-MGFARQVADRVIFMEDGRILEEG 220
Cdd:PLN03211 249 LGSLAQKGKTIVTSMHQpSSRVYQMFDSVLVLSEGRCLFFG 289
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
16-196 |
2.34e-17 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 77.54 E-value: 2.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 16 DLHVL-KDINLTVKRGEkLVMI-GPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPLTKKNHlemarkyssmVFQQFNLY-- 91
Cdd:PRK13538 12 DERILfSGLSFTLNAGE-LVQIeGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRD----------EYHQDLLYlg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 92 ------PNMTVLGNLTLApiklQKKSKEEATEIAIAALKRVGMAHKAgEYP-QNLSGGQQQRIAIARALCTKQPIILFDE 164
Cdd:PRK13538 81 hqpgikTELTALENLRFY----QRLHGPGDDEALWEALAQVGLAGFE-DVPvRQLSAGQQRRVALARLWLTRAPLWILDE 155
|
170 180 190
....*....|....*....|....*....|..
gi 1469315281 165 PTSALDPEMVQEVLDVMIELAQEDITMICVTH 196
Cdd:PRK13538 156 PFTAIDKQGVARLEALLAQHAEQGGMVILTTH 187
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
26-212 |
8.43e-17 |
|
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: 76.68 E-value: 8.43e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 26 TVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPLTKKNHlEMARKYSSMVfQQFnLYPNMTVLGNLT---- 101
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSYKPQ-YIKADYEGTV-RDL-LSSITKDFYTHPyfkt 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 102 --LAPIKLQKKSKEEATEiaiaalkrvgmahkageypqnLSGGQQQRIAIARALCTKQPIILFDEPTSALDPE---MVQE 176
Cdd:cd03237 98 eiAKPLQIEQILDREVPE---------------------LSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEqrlMASK 156
|
170 180 190
....*....|....*....|....*....|....*.
gi 1469315281 177 VLDVMIELAQEdiTMICVTHEMGFARQVADRVIFME 212
Cdd:cd03237 157 VIRRFAENNEK--TAFVVEHDIIMIDYLADRLIVFE 190
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
7-222 |
2.79e-16 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 77.28 E-value: 2.79e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 7 IKHLNKYF-GDLHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDgtPLTKKNHLEmarkyssmvf 85
Cdd:TIGR03719 7 MNRVSKVVpPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQ--PGIKVGYLP---------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 86 QQFNLYPNMTVLGN--LTLAPIK--LQK----------------KSKEEATEI--AIAALK------RVGMAHKAGEYP- 136
Cdd:TIGR03719 75 QEPQLDPTKTVRENveEGVAEIKdaLDRfneisakyaepdadfdKLAAEQAELqeIIDAADawdldsQLEIAMDALRCPp 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 137 -----QNLSGGQQQRIAIARALCTKQPIILFDEPTSALDPEMVQevldvMIE--LAQEDITMICVTHEMGFARQVAdrvi 209
Cdd:TIGR03719 155 wdadvTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVA-----WLErhLQEYPGTVVAVTHDRYFLDNVA---- 225
|
250
....*....|....*..
gi 1469315281 210 fmedGRILE----EGTP 222
Cdd:TIGR03719 226 ----GWILEldrgRGIP 238
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
20-216 |
3.14e-16 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 77.35 E-value: 3.14e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 20 LKDINLTVKRGEKLVMIGPSGSGKSTLIRcVDYLEEP-TSGEVLIDGTPLTKKN----------HLEMARKYSSMVFQqF 88
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMK-VLYGALPrTSGYVTLDGHEVVTRSpqdglangivYISEDRKRDGLVLG-M 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 89 NLYPNM--TVLGNLTLAPIKLQKKSKEEATE--IAIAALKRVGMAHKAGeypqNLSGGQQQRIAIARALCTKQPIILFDE 164
Cdd:PRK10762 346 SVKENMslTALRYFSRAGGSLKHADEQQAVSdfIRLFNIKTPSMEQAIG----LLSGGNQQKVAIARGLMTRPKVLILDE 421
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1469315281 165 PTSALDPEMVQEVLDVMIELAQEDITMICVTHEMGFARQVADRVIFMEDGRI 216
Cdd:PRK10762 422 PTRGVDVGAKKEIYQLINQFKAEGLSIILVSSEMPEVLGMSDRILVMHEGRI 473
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
15-227 |
4.58e-16 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 77.29 E-value: 4.58e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 15 GDLHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGT----PLT--------KKNHL---EMARK 79
Cdd:TIGR00957 649 DLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSvayvPQQawiqndslRENILfgkALNEK 728
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 80 YSSMVFQQFNLYPNMTVLgnltlapiklqkkSKEEATEIaiaalkrvgmahkaGEYPQNLSGGQQQRIAIARALCTKQPI 159
Cdd:TIGR00957 729 YYQQVLEACALLPDLEIL-------------PSGDRTEI--------------GEKGVNLSGGQKQRVSLARAVYSNADI 781
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 160 ILFDEPTSALDPEMVQEVLDVMI--ELAQEDITMICVTHEMGFARQVaDRVIFMEDGRILEEGTPEHFFD 227
Cdd:TIGR00957 782 YLFDDPLSAVDAHVGKHIFEHVIgpEGVLKNKTRILVTHGISYLPQV-DVIIVMSGGKISEMGSYQELLQ 850
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
19-226 |
5.59e-16 |
|
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: 74.95 E-value: 5.59e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 19 VLKDINLTVKRGEKLVMIGPSGSGKSTL----IRCVDYLEeptsGEVLIDGTPLTKKNhLEMARKYSSMVFQ-------- 86
Cdd:cd03288 36 VLKHVKAYIKPGQKVGICGRTGSGKSSLslafFRMVDIFD----GKIVIDGIDISKLP-LHTLRSRLSIILQdpilfsgs 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 87 -QFNLYPNMtvlgnltlapiKLQKKSKEEATEIAiaALKRVGMAHKAG------EYPQNLSGGQQQRIAIARALCTKQPI 159
Cdd:cd03288 111 iRFNLDPEC-----------KCTDDRLWEALEIA--QLKNMVKSLPGGldavvtEGGENFSVGQRQLFCLARAFVRKSSI 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1469315281 160 ILFDEPTSALDpeMVQE-VLDVMIELAQEDITMICVTHEMGFARQvADRVIFMEDGRILEEGTPEHFF 226
Cdd:cd03288 178 LIMDEATASID--MATEnILQKVVMTAFADRTVVTIAHRVSTILD-ADLVLVLSRGILVECDTPENLL 242
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1-219 |
2.38e-15 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 74.65 E-value: 2.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 1 MADMIEIKHLNKYFGDLHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPLTKKNHLEMARKY 80
Cdd:PRK10762 1 MQALLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 81 SSMVFQQFNLYPNMTVLGNLTLA--------PIKLQKKSKEeateiAIAALKRVGMAHKAGEYPQNLSGGQQQRIAIARA 152
Cdd:PRK10762 81 IGIIHQELNLIPQLTIAENIFLGrefvnrfgRIDWKKMYAE-----ADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKV 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1469315281 153 LCTKQPIILFDEPTSALDPEMVQEVLDVMIELAQEDITMICVTHEMGFARQVADRVIFMEDGRILEE 219
Cdd:PRK10762 156 LSFESKVIIMDEPTDALTDTETESLFRVIRELKSQGRGIVYISHRLKEIFEICDDVTVFRDGQFIAE 222
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
6-216 |
3.80e-15 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 74.22 E-value: 3.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 6 EIKHLNKYFGDLHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIdGTpltkknHLEMArkYssmvF 85
Cdd:PRK11147 321 EMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHC-GT------KLEVA--Y----F 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 86 QQF--NLYPNMTVLGNLTlapiklqkkskEEATEIAIAALKRvgmaHKAGeYPQN--------------LSGGQQQRIAI 149
Cdd:PRK11147 388 DQHraELDPEKTVMDNLA-----------EGKQEVMVNGRPR----HVLG-YLQDflfhpkramtpvkaLSGGERNRLLL 451
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1469315281 150 ARALCTKQPIILFDEPTSALDPEMVqEVLDVMIELAQEdiTMICVTHEmgfaRQVADRV-----IFMEDGRI 216
Cdd:PRK11147 452 ARLFLKPSNLLILDEPTNDLDVETL-ELLEELLDSYQG--TVLLVSHD----RQFVDNTvtecwIFEGNGKI 516
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
23-225 |
7.57e-15 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 73.02 E-value: 7.57e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 23 INLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPLTKKNHLEMARkySSMVF-----QQFNLYPNMTVL 97
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRDAIR--AGIMLcpedrKAEGIIPVHSVA 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 98 GNLTL--------APIKLQKKSKEEATEIAIAALKrvgMAHKAGEYP-QNLSGGQQQRIAIARALCTKQPIILFDEPTSA 168
Cdd:PRK11288 350 DNINIsarrhhlrAGCLINNRWEAENADRFIRSLN---IKTPSREQLiMNLSGGNQQKAILGRWLSEDMKVILLDEPTRG 426
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1469315281 169 LDPEMVQEVLDVMIELAQEDITMICVTHE----MGfarqVADRVIFMEDGRILEEGTPEHF 225
Cdd:PRK11288 427 IDVGAKHEIYNVIYELAAQGVAVLFVSSDlpevLG----VADRIVVMREGRIAGELAREQA 483
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
16-172 |
7.84e-15 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 71.03 E-value: 7.84e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 16 DLHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPLTKKnhlEMARkYSSMVFQQFNLYPNMT 95
Cdd:PRK13543 23 EEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRG---DRSR-FMAYLGHLPGLKADLS 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1469315281 96 VLGNLTLapikLQKKSKEEATEIAIAALKRVGMAHKAGEYPQNLSGGQQQRIAIARALCTKQPIILFDEPTSALDPE 172
Cdd:PRK13543 99 TLENLHF----LCGLHGRRAKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLE 171
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
4-223 |
8.37e-15 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 71.60 E-value: 8.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 4 MIEIKHLNKYFGDLHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCV----DYleEPTSGEVLIDGTPLTKKNHLEMARK 79
Cdd:CHL00131 7 ILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIaghpAY--KILEGDILFKGESILDLEPEERAHL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 80 YSSMVFQqfnlYP-------NMTVLGNLTLAPIKLQKKSKEEAT---EIAIAALKRVGMAHKAGEYPQN--LSGGQQQRI 147
Cdd:CHL00131 85 GIFLAFQ----YPieipgvsNADFLRLAYNSKRKFQGLPELDPLeflEIINEKLKLVGMDPSFLSRNVNegFSGGEKKRN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 148 AIAR-ALCTKQPIILfDEPTSALDPEMVQEVLDVMIELAQEDITMICVTHemgFARQ----VADRVIFMEDGRILEEGTP 222
Cdd:CHL00131 161 EILQmALLDSELAIL-DETDSGLDIDALKIIAEGINKLMTSENSIILITH---YQRLldyiKPDYVHVMQNGKIIKTGDA 236
|
.
gi 1469315281 223 E 223
Cdd:CHL00131 237 E 237
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
17-223 |
2.00e-14 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 71.98 E-value: 2.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 17 LHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPLTKKNHLEMARKysSMVF-----QQFNLY 91
Cdd:COG3845 271 VPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRL--GVAYipedrLGRGLV 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 92 PNMTVLGNLTLAPIKLQKKSK------EEATEIAIAALKR-----VGMAHKAGeypqNLSGGQQQRIAIARALCTKQPII 160
Cdd:COG3845 349 PDMSVAENLILGRYRRPPFSRggfldrKAIRAFAEELIEEfdvrtPGPDTPAR----SLSGGNQQKVILARELSRDPKLL 424
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1469315281 161 LFDEPTSALDPEMVQEVLDVMIELAQEDITMICVTHEMGFARQVADRVIFMEDGRILEEGTPE 223
Cdd:COG3845 425 IAAQPTRGLDVGAIEFIHQRLLELRDAGAAVLLISEDLDEILALSDRIAVMYEGRIVGEVPAA 487
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
20-216 |
2.63e-14 |
|
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: 69.21 E-value: 2.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 20 LKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPT---SGEVLIDGTPLtkknhLEMARKY---SSMVFQQFNLYPN 93
Cdd:cd03233 23 LKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPY-----KEFAEKYpgeIIYVSEEDVHFPT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 94 MTVlgnltlapiklqkkskEEATEIAIAAlkrvgmahKAGEYPQNLSGGQQQRIAIARALCTKQPIILFDEPTSALDPEM 173
Cdd:cd03233 98 LTV----------------RETLDFALRC--------KGNEFVRGISGGERKRVSIAEALVSRASVLCWDNSTRGLDSST 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1469315281 174 VQEVLDVMIELAQE--DITMICVTHEMGFARQVADRVIFMEDGRI 216
Cdd:cd03233 154 ALEILKCIRTMADVlkTTTFVSLYQASDEIYDLFDKVLVLYEGRQ 198
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
19-228 |
2.83e-14 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 71.69 E-value: 2.83e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 19 VLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPLTKKNHLEMaRKYSSMVFQQFNLYPNmTVLG 98
Cdd:PLN03130 1254 VLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDL-RKVLGIIPQAPVLFSG-TVRF 1331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 99 NLTlaPIKLQKKSK-EEATEIAiaALKRV------GMAHKAGEYPQNLSGGQQQRIAIARALCTKQPIILFDEPTSALDP 171
Cdd:PLN03130 1332 NLD--PFNEHNDADlWESLERA--HLKDVirrnslGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDV 1407
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1469315281 172 EMvqevlDVMIelaQEDI-------TMICVTHEMGFARQvADRVIFMEDGRILEEGTPEHFFDN 228
Cdd:PLN03130 1408 RT-----DALI---QKTIreefkscTMLIIAHRLNTIID-CDRILVLDAGRVVEFDTPENLLSN 1462
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
20-216 |
1.18e-13 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 69.76 E-value: 1.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 20 LKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPLTKKNHLEMARKYSSMVFQ---QFNLYPNMTV 96
Cdd:PRK10982 264 IRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANEAINHGFALVTEerrSTGIYAYLDI 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 97 LGNLTLAPIK--------LQKKSKEEATEIAIAALKRVGMAHKAgeYPQNLSGGQQQRIAIARALCTKQPIILFDEPTSA 168
Cdd:PRK10982 344 GFNSLISNIRnyknkvglLDNSRMKSDTQWVIDSMRVKTPGHRT--QIGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRG 421
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1469315281 169 LDPEMVQEVLDVMIELAQEDITMICVTHEMGFARQVADRVIFMEDGRI 216
Cdd:PRK10982 422 IDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNGLV 469
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
58-226 |
1.82e-13 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 69.67 E-value: 1.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 58 SGEVLIDGTPLTKKNhLEMARKYSSMVFQQFNLYpNMTVLGNL-------TLAPIKlqKKSKEEATEIAIAALKRvGMAH 130
Cdd:PTZ00265 1276 SGKILLDGVDICDYN-LKDLRNLFSIVSQEPMLF-NMSIYENIkfgkedaTREDVK--RACKFAAIDEFIESLPN-KYDT 1350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 131 KAGEYPQNLSGGQQQRIAIARALCTKQPIILFDEPTSALDPEMVQEVLDVMIELAQE-DITMICVTHEMGFARQVADRVI 209
Cdd:PTZ00265 1351 NVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKaDKTIITIAHRIASIKRSDKIVV 1430
|
170 180
....*....|....*....|.
gi 1469315281 210 FMEDGR----ILEEGTPEHFF 226
Cdd:PTZ00265 1431 FNNPDRtgsfVQAHGTHEELL 1451
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
19-228 |
2.26e-13 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 69.23 E-value: 2.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 19 VLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPLTKKNhLEMARKYSSMVFQQFNLYPNmTVLG 98
Cdd:PLN03232 1251 VLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFG-LTDLRRVLSIIPQSPVLFSG-TVRF 1328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 99 NLTlaPIKLQK-----KSKEEATEIAIAALKRVGMAHKAGEYPQNLSGGQQQRIAIARALCTKQPIILFDEPTSALDPEm 173
Cdd:PLN03232 1329 NID--PFSEHNdadlwEALERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVR- 1405
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1469315281 174 VQEVLDVMIELAQEDITMICVTHEMGFARQvADRVIFMEDGRILEEGTPEHFFDN 228
Cdd:PLN03232 1406 TDSLIQRTIREEFKSCTMLVIAHRLNTIID-CDKILVLSSGQVLEYDSPQELLSR 1459
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
3-220 |
2.48e-13 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 68.22 E-value: 2.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 3 DMIEIKHLNKYFGDLHVLKDINLTVKRGEKLVMIGPSGSG--KSTL---IRCVDYLEEPTSGEVLIDGTPLTKKNhLEMA 77
Cdd:NF000106 12 NAVEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RGALpahV*GPDAGRRPWRF*TWCANRRALRRT-IG*H 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 78 RKYSSMVFQQFNLYPNMTVLGnltlapiKLQKKSKEEATEIAIAALKRVGMAHKAGEYPQNLSGGQQQRIAIARALCTKQ 157
Cdd:NF000106 91 RPVR*GRRESFSGRENLYMIG-------R*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1469315281 158 PIILFDEPTSALDPEMVQEVLDVMIELAQEDITMICVTHEMGFARQVADRVIFMEDGRILEEG 220
Cdd:NF000106 164 AVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADG 226
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
15-197 |
3.56e-13 |
|
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: 65.73 E-value: 3.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 15 GDLHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEP--TSGEVLIDGTPLTKKnhlemARKYSSMVFQQFNLYP 92
Cdd:cd03232 18 GKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAgvITGEILINGRPLDKN-----FQRSTGYVEQQDVHSP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 93 NMTVlgnltlapiklqkkskEEATEIAiAALKrvgmahkageypqNLSGGQQQRIAIARALCTKqPIILF-DEPTSALDP 171
Cdd:cd03232 93 NLTV----------------REALRFS-ALLR-------------GLSVEQRKRLTIGVELAAK-PSILFlDEPTSGLDS 141
|
170 180
....*....|....*....|....*.
gi 1469315281 172 EMVQEVLDVMIELAQEDITMICVTHE 197
Cdd:cd03232 142 QAAYNIVRFLKKLADSGQAILCTIHQ 167
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
5-232 |
6.94e-13 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 67.75 E-value: 6.94e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 5 IEIKHLNKYFG---DLHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPLTKKNHLEMARKYS 81
Cdd:PTZ00265 383 IQFKNVRFHYDtrkDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDSHNLKDINLKWWRSKI 462
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 82 SMVFQQFNLYPNmTVLGNL--TLAPIK----LQKKSKEEATE--------------------IAIAALKRVGMAHKAGEY 135
Cdd:PTZ00265 463 GVVSQDPLLFSN-SIKNNIkySLYSLKdleaLSNYYNEDGNDsqenknkrnscrakcagdlnDMSNTTDSNELIEMRKNY 541
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 136 -----------------------------------PQNLSGGQQQRIAIARALCTKQPIILFDEPTSALDPE---MVQEV 177
Cdd:PTZ00265 542 qtikdsevvdvskkvlihdfvsalpdkyetlvgsnASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKseyLVQKT 621
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1469315281 178 LDVMieLAQEDITMICVTHEMGFARQVadRVIFMEDGRilEEGTPEHFFDNPENP 232
Cdd:PTZ00265 622 INNL--KGNENRITIIIAHRLSTIRYA--NTIFVLSNR--ERGSTVDVDIIGEDP 670
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
18-220 |
7.63e-13 |
|
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: 64.65 E-value: 7.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 18 HVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYleepTSGEV-LIDGTPLTKKNHLEMARKYSSMVfqqfnlypNMTv 96
Cdd:cd03238 9 HNLQNLDVSIPLNVLVVVTGVSGSGKSTLVNEGLY----ASGKArLISFLPKFSRNKLIFIDQLQFLI--------DVG- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 97 LGNLTLapiklqkkskeeateiaiaalkrvgmahkaGEYPQNLSGGQQQRIAIARALC--TKQPIILFDEPTSALDPEMV 174
Cdd:cd03238 76 LGYLTL------------------------------GQKLSTLSGGELQRVKLASELFsePPGTLFILDEPSTGLHQQDI 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1469315281 175 QEVLDVMIELAQEDITMICVTHEMGFARQvADRVIFM------EDGRILEEG 220
Cdd:cd03238 126 NQLLEVIKGLIDLGNTVILIEHNLDVLSS-ADWIIDFgpgsgkSGGKVVFSG 176
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
19-230 |
9.75e-13 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 67.50 E-value: 9.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 19 VLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPLTKKNHLEMARKYsSMVFQQFNLYpNMTVLG 98
Cdd:PTZ00243 1325 VLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQF-SMIPQDPVLF-DGTVRQ 1402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 99 NLTlaPIkLQKKSKEeateiAIAALKRVGMAHKAG-----------EYPQNLSGGQQQRIAIARALCTK-QPIILFDEPT 166
Cdd:PTZ00243 1403 NVD--PF-LEASSAE-----VWAALELVGLRERVAsesegidsrvlEGGSNYSVGQRQLMCMARALLKKgSGFILMDEAT 1474
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1469315281 167 SALDPemvqeVLDVMIEL----AQEDITMICVTHEMGFARQVaDRVIFMEDGRILEEGTPEHFFDNPE 230
Cdd:PTZ00243 1475 ANIDP-----ALDRQIQAtvmsAFSAYTVITIAHRLHTVAQY-DKIIVMDHGAVAEMGSPRELVMNRQ 1536
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
5-216 |
1.09e-12 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 66.96 E-value: 1.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 5 IEIKHLNKYFGDLHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVD------YLEEPT-------SGEVLIDgtplTKK 71
Cdd:PRK10938 261 IVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITgdhpqgYSNDLTlfgrrrgSGETIWD----IKK 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 72 ------NHLEMARKYSSMV--------FQQFNLYpnmtvlgnlTLAPIKLQKKSKEeateiaiaALKRVGMAHKAGEYP- 136
Cdd:PRK10938 337 higyvsSSLHLDYRVSTSVrnvilsgfFDSIGIY---------QAVSDRQQKLAQQ--------WLDILGIDKRTADAPf 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 137 QNLSGGQQQRIAIARALCTKQPIILFDEPTSALDP---EMVQEVLDVMIelAQEDITMICVTHEMGFARQ-VADRVIFME 212
Cdd:PRK10938 400 HSLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPlnrQLVRRFVDVLI--SEGETQLLFVSHHAEDAPAcITHRLEFVP 477
|
....
gi 1469315281 213 DGRI 216
Cdd:PRK10938 478 DGDI 481
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
5-216 |
1.21e-12 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 66.84 E-value: 1.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 5 IEIKHLNKYFGDLHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVlidgtPLTKKNHL-EMARKYSSM 83
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV-----KWSENANIgYYAQDHAYD 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 84 VFQQFNLYPNMTvlgnltlapiklQKKsKEEATEIAI-AALKRVGM-AHKAGEYPQNLSGGQQQRIAIARALCTKQPIIL 161
Cdd:PRK15064 395 FENDLTLFDWMS------------QWR-QEGDDEQAVrGTLGRLLFsQDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLV 461
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1469315281 162 FDEPTSALDPEMVqEVLDVMIELAQEdiTMICVTHEMGFARQVADRVIFMEDGRI 216
Cdd:PRK15064 462 MDEPTNHMDMESI-ESLNMALEKYEG--TLIFVSHDREFVSSLATRIIEITPDGV 513
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
4-232 |
1.97e-12 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 65.59 E-value: 1.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 4 MIEIKHLNKYF----GDLHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEP----TSGEVL---IDGTPLTKKN 72
Cdd:PRK15093 3 LLDIRNLTIEFktsdGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDnwrvTADRMRfddIDLLRLSPRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 73 HLEMARKYSSMVFQ--QFNLYPNMTVLGNLTLAPIKLQKKS---------KEEATEIaiaaLKRVGM-AHKA--GEYPQN 138
Cdd:PRK15093 83 RRKLVGHNVSMIFQepQSCLDPSERVGRQLMQNIPGWTYKGrwwqrfgwrKRRAIEL----LHRVGIkDHKDamRSFPYE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 139 LSGGQQQRIAIARALCTKQPIILFDEPTSALDPEMVQEVLDVMIELAQED-ITMICVTHEMGFARQVADRVIFMEDGRIL 217
Cdd:PRK15093 159 LTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNnTTILLISHDLQMLSQWADKINVLYCGQTV 238
|
250
....*....|....*
gi 1469315281 218 EEGTPEHFFDNPENP 232
Cdd:PRK15093 239 ETAPSKELVTTPHHP 253
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
13-224 |
2.20e-12 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 66.04 E-value: 2.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 13 YFGDLHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVL--------------IDGTPLTKKNHLEMAR 78
Cdd:PLN03073 518 YPGGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFrsakvrmavfsqhhVDGLDLSSNPLLYMMR 597
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 79 KYSSMVFQQFNLY-PNMTVLGNLTLAPIklqkkskeeateiaiaalkrvgmahkageypQNLSGGQQQRIAIARALCTKQ 157
Cdd:PLN03073 598 CFPGVPEQKLRAHlGSFGVTGNLALQPM-------------------------------YTLSGGQKSRVAFAKITFKKP 646
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1469315281 158 PIILFDEPTSALDPEMVQEVLDVMIeLAQEDITMicVTHEMGFARQVADRVIFMEDGRIleegTPEH 224
Cdd:PLN03073 647 HILLLDEPSNHLDLDAVEALIQGLV-LFQGGVLM--VSHDEHLISGSVDELWVVSEGKV----TPFH 706
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
5-185 |
3.80e-12 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 65.34 E-value: 3.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 5 IEIKHLNKYFGDLHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTplTKKNHLEMARKyssmv 84
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGET--VKLAYVDQSRD----- 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 85 fqqfNLYPNMTVLGNLT--LAPIKLQKksKEEATEIAIAAL--------KRVGMahkageypqnLSGGQQQRIAIARALC 154
Cdd:TIGR03719 396 ----ALDPNKTVWEEISggLDIIKLGK--REIPSRAYVGRFnfkgsdqqKKVGQ----------LSGGERNRVHLAKTLK 459
|
170 180 190
....*....|....*....|....*....|.
gi 1469315281 155 TKQPIILFDEPTSALDPEMVQEVLDVMIELA 185
Cdd:TIGR03719 460 SGGNVLLLDEPTNDLDVETLRALEEALLNFA 490
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
8-218 |
5.69e-12 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 64.75 E-value: 5.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 8 KHLNKYFG-DLHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIdgTPLTKKNHLEmarkyssmvfQ 86
Cdd:PRK11819 10 NRVSKVVPpKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARP--APGIKVGYLP----------Q 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 87 QFNLYPNMTVLGNLT--LAPIKLQKKSKEE-----ATEIA---------------IAAL------KRVGMAHKA-----G 133
Cdd:PRK11819 78 EPQLDPEKTVRENVEegVAEVKAALDRFNEiyaayAEPDAdfdalaaeqgelqeiIDAAdawdldSQLEIAMDAlrcppW 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 134 EYP-QNLSGGQQQRIAIARALCTKQPIILFDEPTSALDPEMVQevldvMIE--LAQEDITMICVTHEMGFARQVAdrvif 210
Cdd:PRK11819 158 DAKvTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVA-----WLEqfLHDYPGTVVAVTHDRYFLDNVA----- 227
|
....*...
gi 1469315281 211 medGRILE 218
Cdd:PRK11819 228 ---GWILE 232
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
27-225 |
7.02e-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: 65.03 E-value: 7.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 27 VKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDG-TPLTKKNHLEMARKYSSmvfqQFNLYPNMTVLGNLTLAPI 105
Cdd:TIGR01257 1962 VRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGkSILTNISDVHQNMGYCP----QFDAIDDLLTGREHLYLYA 2037
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 106 KLQKKSKEEATEIAIAALKRVGMAHKAGEYPQNLSGGQQQRIAIARALCTKQPIILFDEPTSALDPEMVQEVLDVMIELA 185
Cdd:TIGR01257 2038 RLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSII 2117
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1469315281 186 QEDITMICVTHEMGFARQVADRVIFMEDGRILEEGTPEHF 225
Cdd:TIGR01257 2118 REGRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGTIQHL 2157
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
18-196 |
8.81e-12 |
|
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: 61.61 E-value: 8.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 18 HVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYleeptsgeVLIDGTPLTKKNHLEMARKYSsmvfqqfnlypnmtvl 97
Cdd:cd03227 9 SYFVPNDVTFGEGSLTIITGPNGSGKSTILDAIGL--------ALGGAQSATRRRSGVKAGCIV---------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 98 gnltlapiklqkkskeeATEIAIAALKRVGmahkageypqnLSGGQQQRIAIAR--ALCTKQ--PIILFDEPTSALDPEM 173
Cdd:cd03227 65 -----------------AAVSAELIFTRLQ-----------LSGGEKELSALALilALASLKprPLYILDEIDRGLDPRD 116
|
170 180
....*....|....*....|...
gi 1469315281 174 VQEVLDVMIELAQEDITMICVTH 196
Cdd:cd03227 117 GQALAEAILEHLVKGAQVIVITH 139
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
19-198 |
1.03e-11 |
|
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: 64.16 E-value: 1.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 19 VLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEpTSGEVLIDGTPLTKKNhLEMARKYSSMVFQQFNLYPNmTVLG 98
Cdd:TIGR01271 1234 VLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVSWNSVT-LQTWRKAFGVIPQKVFIFSG-TFRK 1310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 99 NLTlapiKLQKKSKEEATEIAiaalKRVGMAHKAGEYPQNL-----------SGGQQQRIAIARALCTKQPIILFDEPTS 167
Cdd:TIGR01271 1311 NLD----PYEQWSDEEIWKVA----EEVGLKSVIEQFPDKLdfvlvdggyvlSNGHKQLMCLARSILSKAKILLLDEPSA 1382
|
170 180 190
....*....|....*....|....*....|.
gi 1469315281 168 ALDPEMVQeVLDVMIELAQEDITMICVTHEM 198
Cdd:TIGR01271 1383 HLDPVTLQ-IIRKTLKQSFSNCTVILSEHRV 1412
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
21-216 |
6.19e-11 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 61.61 E-value: 6.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 21 KDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPLTK---KNHLEMARKYSSMVFQQFNLYPNMTVL 97
Cdd:PRK15439 280 RNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINAlstAQRLARGLVYLPEDRQSSGLYLDAPLA 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 98 GN---LTLAPIKLQKKSKEEAteiaiAALKR----VGMAHKAGEYP-QNLSGGQQQRIAIARALCTKQPIILFDEPTSAL 169
Cdd:PRK15439 360 WNvcaLTHNRRGFWIKPAREN-----AVLERyrraLNIKFNHAEQAaRTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGV 434
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1469315281 170 DPEMVQEVLDVMIELAQEDITMICVTHEMGFARQVADRVIFMEDGRI 216
Cdd:PRK15439 435 DVSARNDIYQLIRSIAAQNVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
29-215 |
1.45e-10 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 57.77 E-value: 1.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 29 RGEKLVMIGPSGSGKSTLIRCV-DYLEEPTSGEVLIDGTPLTKKNHLEMARKYSsmvfqqfnlypnmtvlgnltlapikl 107
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALaRELGPPGGGVIYIDGEDILEEVLDQLLLIIV-------------------------- 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 108 qkkskeeateiaiaalkrvgmahkaGEYPQNLSGGQQQRIAIARALCTKQPIILFDEPTSALDPEMVQEVLD------VM 181
Cdd:smart00382 55 -------------------------GGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLleelrlLL 109
|
170 180 190
....*....|....*....|....*....|....*....
gi 1469315281 182 IELAQEDITMICVTHEMGF-----ARQVADRVIFMEDGR 215
Cdd:smart00382 110 LLKSEKNLTVILTTNDEKDlgpalLRRRFDRRIVLLLIL 148
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
5-216 |
1.96e-10 |
|
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: 59.48 E-value: 1.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 5 IEIKHLN-KYFGDLH-VLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEpTSGEVLIDGTPLTKKNhLEMARKYSS 82
Cdd:cd03289 3 MTVKDLTaKYTEGGNaVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVP-LQKWRKAFG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 83 MVFQQFNLYPNmTVLGNLTlapiKLQKKSKEEATEIAiaalKRVGMAHKAGEYPQNL-----------SGGQQQRIAIAR 151
Cdd:cd03289 81 VIPQKVFIFSG-TFRKNLD----PYGKWSDEEIWKVA----EEVGLKSVIEQFPGQLdfvlvdggcvlSHGHKQLMCLAR 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1469315281 152 ALCTKQPIILFDEPTSALDPEMVQeVLDVMIELAQEDITMICVTHEMGfARQVADRVIFMEDGRI 216
Cdd:cd03289 152 SVLSKAKILLLDEPSAHLDPITYQ-VIRKTLKQAFADCTVILSEHRIE-AMLECQRFLVIEENKV 214
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
19-242 |
2.13e-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: 59.49 E-value: 2.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 19 VLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPltkknhlemarKYSSmvfqQFNLYPNMTVLG 98
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGRI-----------SFSS----QFSWIMPGTIKE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 99 NLT--LAPIKLQKKSKEEATEIAIAALKrvgMAHK----AGEYPQNLSGGQQQRIAIARALCTKQPIILFDEPTSALDPE 172
Cdd:cd03291 117 NIIfgVSYDEYRYKSVVKACQLEEDITK---FPEKdntvLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVF 193
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 173 MVQEVLDVMIELAQEDITMICVTHEMGFARQvADRVIFMEDGRILEEGTpehfFDNPENPRcREFLSKIL 242
Cdd:cd03291 194 TEKEIFESCVCKLMANKTRILVTSKMEHLKK-ADKILILHEGSSYFYGT----FSELQSLR-PDFSSKLM 257
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
10-212 |
2.26e-10 |
|
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: 57.97 E-value: 2.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 10 LNKYFGDLHVLKDINlTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPLTKKnhlemarkyssmvfqqfn 89
Cdd:cd03222 6 CVKRYGVFFLLVELG-VVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITPVYK------------------ 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 90 lypnmtvlgnltlapiklqkkskeeateiaiaalkrvgmahkageyPQ--NLSGGQQQRIAIARALCTKQPIILFDEPTS 167
Cdd:cd03222 67 ----------------------------------------------PQyiDLSGGELQRVAIAAALLRNATFYLFDEPSA 100
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1469315281 168 ALDPEMVQEVLDVMIELAQEDI-TMICVTHEMGFARQVADRVIFME 212
Cdd:cd03222 101 YLDIEQRLNAARAIRRLSEEGKkTALVVEHDLAVLDYLSDRIHVFE 146
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
5-172 |
4.73e-10 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 58.98 E-value: 4.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 5 IEIKHLNKYFGDLHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTplTKKNHLEMARKyssmv 84
Cdd:PRK11819 325 IEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGET--VKLAYVDQSRD----- 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 85 fqqfNLYPNMTVLGNLT--LAPIKLQKKskeeatEIA----IAAL--------KRVGMahkageypqnLSGGQQQRIAIA 150
Cdd:PRK11819 398 ----ALDPNKTVWEEISggLDIIKVGNR------EIPsrayVGRFnfkggdqqKKVGV----------LSGGERNRLHLA 457
|
170 180
....*....|....*....|....
gi 1469315281 151 RALctKQP--IILFDEPTSALDPE 172
Cdd:PRK11819 458 KTL--KQGgnVLLLDEPTNDLDVE 479
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
26-209 |
5.03e-10 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 59.05 E-value: 5.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 26 TVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPLTKKNHLEMArkyssmvfqqfnlyPNMTVlgNLTLAPI 105
Cdd:PRK13409 361 EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELKISYKPQYIKPD--------------YDGTV--EDLLRSI 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 106 KLQKKSKEEATEIAiaalKRVGMAHKAGEYPQNLSGGQQQRIAIARALCTKQPIILFDEPTSALDPE---MVQEVLDVMI 182
Cdd:PRK13409 425 TDDLGSSYYKSEII----KPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEqrlAVAKAIRRIA 500
|
170 180
....*....|....*....|....*..
gi 1469315281 183 ElaQEDITMICVTHEMGFARQVADRVI 209
Cdd:PRK13409 501 E--EREATALVVDHDIYMIDYISDRLM 525
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
34-212 |
6.45e-10 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 56.85 E-value: 6.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 34 VMIGPSGSGKSTLIRCVDYleePTSGEvlidgTPLTKK--NHL-EMARKYSsmvfqqfnlypnmtvlgnlTLAPIKLQKK 110
Cdd:cd03240 26 LIVGQNGAGKTTIIEALKY---ALTGE-----LPPNSKggAHDpKLIREGE-------------------VRAQVKLAFE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 111 SKEEATEIA---IAALKRVGMAHKAG------EYPQNLSGGQQQ------RIAIARALCTKQPIILFDEPTSALDPEMVQ 175
Cdd:cd03240 79 NANGKKYTItrsLAILENVIFCHQGEsnwpllDMRGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENIE 158
|
170 180 190
....*....|....*....|....*....|....*....
gi 1469315281 176 EVLDVMIE--LAQEDITMICVTHEMGFaRQVADRVIFME 212
Cdd:cd03240 159 ESLAEIIEerKSQKNFQLIVITHDEEL-VDAADHIYRVE 196
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
15-214 |
8.47e-10 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 58.58 E-value: 8.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 15 GDLHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCvdyLEEPTSGEVLIDGTPLTKKNHLEMARKYSSMVFQQFNLY-PN 93
Cdd:TIGR00956 774 EKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNV---LAERVTTGVITGGDRLVNGRPLDSSFQRSIGYVQQQDLHlPT 850
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 94 MTVLGNLTLA-----PIKLQKKSKEEATEIAIaalKRVGMAHKA----GEYPQNLSGGQQQRIAIARALCTKQPIILF-D 163
Cdd:TIGR00956 851 STVRESLRFSaylrqPKSVSKSEKMEYVEEVI---KLLEMESYAdavvGVPGEGLNVEQRKRLTIGVELVAKPKLLLFlD 927
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1469315281 164 EPTSALDPEMVQEVLDVMIELAQEDITMICVTHE---MGFARqvADRVIFMEDG 214
Cdd:TIGR00956 928 EPTSGLDSQTAWSICKLMRKLADHGQAILCTIHQpsaILFEE--FDRLLLLQKG 979
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
4-183 |
9.64e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 56.50 E-value: 9.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 4 MIEIKHLNKYFGDLHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPLTKKnhLEMARKYSSM 83
Cdd:PRK13540 1 MLDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKD--LCTYQKQLCF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 84 VFQQFNLYPNMTVLGNLTLapiKLQKKSkeeaTEIAIAALKRVGMAHKAGEYPQN-LSGGQQQRIAIARALCTKQPIILF 162
Cdd:PRK13540 79 VGHRSGINPYLTLRENCLY---DIHFSP----GAVGITELCRLFSLEHLIDYPCGlLSSGQKRQVALLRLWMSKAKLWLL 151
|
170 180
....*....|....*....|.
gi 1469315281 163 DEPTSALDpEMVQEVLDVMIE 183
Cdd:PRK13540 152 DEPLVALD-ELSLLTIITKIQ 171
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
1-220 |
1.50e-09 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 56.75 E-value: 1.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 1 MADMIEIKHLNKYFgdlHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTpltkknhlemarky 80
Cdd:PRK13546 24 MKDALIPKHKNKTF---FALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGE-------------- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 81 SSMVFQQFNLYPNMTVLGNLTLAPIKLQKKSKEeateiaIAALK-RVGMAHKAGEY----PQNLSGGQQQRIAIARALCT 155
Cdd:PRK13546 87 VSVIAISAGLSGQLTGIENIEFKMLCMGFKRKE------IKAMTpKIIEFSELGEFiyqpVKKYSSGMRAKLGFSINITV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1469315281 156 KQPIILFDEPTSALDPEMVQEVLDVMIELAQEDITMICVTHEMGFARQVADRVIFMEDGRILEEG 220
Cdd:PRK13546 161 NPDILVIDEALSVGDQTFAQKCLDKIYEFKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYG 225
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
19-214 |
1.94e-09 |
|
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: 57.61 E-value: 1.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 19 VLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDG-----------TPLTKKNHLEMARKYS----SM 83
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGrisfspqtswiMPGTIKDNIIFGLSYDeyryTS 520
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 84 VFQQFNLYPNMTVLGNLTLAPIklqkkskeeateiaiaalkrvgmahkaGEYPQNLSGGQQQRIAIARALCTKQPIILFD 163
Cdd:TIGR01271 521 VIKACQLEEDIALFPEKDKTVL---------------------------GEGGITLSGGQRARISLARAVYKDADLYLLD 573
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1469315281 164 EPTSALDPEMVQEVLDVMIELAQEDITMICVTHEMGFARQvADRVIFMEDG 214
Cdd:TIGR01271 574 SPFTHLDVVTEKEIFESCLCKLMSNKTRILVTSKLEHLKK-ADKILLLHEG 623
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
10-224 |
2.37e-09 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 57.04 E-value: 2.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 10 LNKYFGDLH-----VLKDINLTVKRGEKLVMIGPSGSGKSTLIRCV----DYLEEPTSGEVLIDGTPLTK-KNHLEMARK 79
Cdd:TIGR00956 62 FRKLKKFRDtktfdILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIasntDGFHIGVEGVITYDGITPEEiKKHYRGDVV 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 80 YSSmvfQQFNLYPNMTVLGNLTLApIKLQKK-------SKEE-ATEIAIAALKRVGMAH----KAG-EYPQNLSGGQQQR 146
Cdd:TIGR00956 142 YNA---ETDVHFPHLTVGETLDFA-ARCKTPqnrpdgvSREEyAKHIADVYMATYGLSHtrntKVGnDFVRGVSGGERKR 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 147 IAIARALCTKQPIILFDEPTSALDPEMVQEVLDVMIELAqeDITMICVTHEMGFARQVA----DRVIFMEDGRILEEGTP 222
Cdd:TIGR00956 218 VSIAEASLGGAKIQCWDNATRGLDSATALEFIRALKTSA--NILDTTPLVAIYQCSQDAyelfDKVIVLYEGYQIYFGPA 295
|
..
gi 1469315281 223 EH 224
Cdd:TIGR00956 296 DK 297
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
14-216 |
2.82e-09 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 56.72 E-value: 2.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 14 FGDLHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEV-LIDGTPLT--KKNHLEMARkyssmvfqqfnl 90
Cdd:PRK10636 322 YGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIgLAKGIKLGyfAQHQLEFLR------------ 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 91 yPNMTVLGNLT-LAPIKLQKKSKEeateiaiaALKRVGM-AHKAGEYPQNLSGGQQQRIAIARALCTKQPIILFDEPTSA 168
Cdd:PRK10636 390 -ADESPLQHLArLAPQELEQKLRD--------YLGGFGFqGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNH 460
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1469315281 169 LDPEMVQEVLDVMIELaqeDITMICVTHEMGFARQVADRVIFMEDGRI 216
Cdd:PRK10636 461 LDLDMRQALTEALIDF---EGALVVVSHDRHLLRSTTDDLYLVHDGKV 505
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
18-220 |
3.17e-09 |
|
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: 55.34 E-value: 3.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 18 HVLKDINLTVKRGEKLVMIGPSGSGKSTLirCVDYLeeptsgevlidgtpltkknHLEMARKYS---SMVFQQF--NLY- 91
Cdd:cd03270 9 HNLKNVDVDIPRNKLVVITGVSGSGKSSL--AFDTI-------------------YAEGQRRYVeslSAYARQFlgQMDk 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 92 PNMTVLGNLTLApIKLQKKSKEE--------ATEI---------------AIAALKRVGMAH-KAGEYPQNLSGGQQQRI 147
Cdd:cd03270 68 PDVDSIEGLSPA-IAIDQKTTSRnprstvgtVTEIydylrllfarvgireRLGFLVDVGLGYlTLSRSAPTLSGGEAQRI 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 148 AIARALCTKQPIIL--FDEPTSALDPEMVQEVLDVMIELAQEDITMICVTHEMGFARQvADRVIFM------EDGRILEE 219
Cdd:cd03270 147 RLATQIGSGLTGVLyvLDEPSIGLHPRDNDRLIETLKRLRDLGNTVLVVEHDEDTIRA-ADHVIDIgpgagvHGGEIVAQ 225
|
.
gi 1469315281 220 G 220
Cdd:cd03270 226 G 226
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
26-198 |
3.77e-09 |
|
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: 55.45 E-value: 3.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 26 TVKRGEKLVMIGPSGSGKSTLIRCV---------DYLEEPTSGEVL--IDGTPLtkKNHLEMAR--KYSSMVFQQF-NLY 91
Cdd:cd03236 22 VPREGQVLGLVGPNGIGKSTALKILagklkpnlgKFDDPPDWDEILdeFRGSEL--QNYFTKLLegDVKVIVKPQYvDLI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 92 PNmTVLGNLTLApikLQKKSKEEATEIAIaalKRVGMAHKAGEYPQNLSGGQQQRIAIARALCTKQPIILFDEPTSALDP 171
Cdd:cd03236 100 PK-AVKGKVGEL---LKKKDERGKLDELV---DQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDI 172
|
170 180
....*....|....*....|....*..
gi 1469315281 172 EMVQEVLDVMIELAQEDITMICVTHEM 198
Cdd:cd03236 173 KQRLNAARLIRELAEDDNYVLVVEHDL 199
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
4-220 |
5.91e-09 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 54.80 E-value: 5.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 4 MIEIKHLNKYFGDLHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCV----DYleEPTSGEVLIDGTPLTKKNHLEMARK 79
Cdd:PRK09580 1 MLSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLagreDY--EVTGGTVEFKGKDLLELSPEDRAGE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 80 YSSMVFQ----------QFNLYPNMTVLGNLTLAPiKLQKKSKEEATEIAIAALKrvgmahkageYPQNL---------S 140
Cdd:PRK09580 79 GIFMAFQypveipgvsnQFFLQTALNAVRSYRGQE-PLDRFDFQDLMEEKIALLK----------MPEDLltrsvnvgfS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 141 GGQQQRIAIARALCTKQPIILFDEPTSALDPEMVQEVLDVMIELAQEDITMICVTHEMGFARQVA-DRVIFMEDGRILEE 219
Cdd:PRK09580 148 GGEKKRNDILQMAVLEPELCILDESDSGLDIDALKIVADGVNSLRDGKRSFIIVTHYQRILDYIKpDYVHVLYQGRIVKS 227
|
.
gi 1469315281 220 G 220
Cdd:PRK09580 228 G 228
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
19-196 |
8.52e-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: 8.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 19 VLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEePTSGEVLidgtplTKKNHLEM----ARKYSSM-VFQQFNLYPN 93
Cdd:TIGR00954 467 LIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELW-PVYGGRL------TKPAKGKLfyvpQRPYMTLgTLRDQIIYPD 539
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 94 mtvlgnltlAPIKLQKKSKEEATEIAIAA-------LKRVGMAHKAGEYPQNLSGGQQQRIAIARALCTKQPIILFDEPT 166
Cdd:TIGR00954 540 ---------SSEDMKRRGLSDKDLEQILDnvqlthiLEREGGWSAVQDWMDVLSGGEKQRIAMARLFYHKPQFAILDECT 610
|
170 180 190
....*....|....*....|....*....|.
gi 1469315281 167 SALDPEMVqevlDVMIELAQE-DITMICVTH 196
Cdd:TIGR00954 611 SAVSVDVE----GYMYRLCREfGITLFSVSH 637
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
18-223 |
9.83e-09 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 55.18 E-value: 9.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 18 HVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCV---DYLEEpTSGEVLIDGTPLTKKNHLEMARK---YSSMVFQQFNLY 91
Cdd:NF040905 274 KVVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVfgrSYGRN-ISGTVFKDGKEVDVSTVSDAIDAglaYVTEDRKGYGLN 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 92 PNMTVLGNLTLApiKLQKKSK----EEATEIAIAALKRVGMAHKAGEYPQ---NLSGGQQQRIAIARALCTKQPIILFDE 164
Cdd:NF040905 353 LIDDIKRNITLA--NLGKVSRrgviDENEEIKVAEEYRKKMNIKTPSVFQkvgNLSGGNQQKVVLSKWLFTDPDVLILDE 430
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1469315281 165 PTSALDPEMVQEVLDVMIELAQEDITMICVTHEMGFARQVADRVIFMEDGRIL-----EEGTPE 223
Cdd:NF040905 431 PTRGIDVGAKYEIYTIINELAAEGKGVIVISSELPELLGMCDRIYVMNEGRITgelprEEASQE 494
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
120-222 |
1.79e-08 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 53.39 E-value: 1.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 120 IAALKRVGMAH-KAGEYPQNLSGGQQQRIAIARAL---CTKQPIILFDEPTSALDPEMVQEVLDVMIELAQEDITMICVT 195
Cdd:cd03271 150 LQTLCDVGLGYiKLGQPATTLSGGEAQRIKLAKELskrSTGKTLYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIE 229
|
90 100 110
....*....|....*....|....*....|...
gi 1469315281 196 HEMGFARqVADRVIFM------EDGRILEEGTP 222
Cdd:cd03271 230 HNLDVIK-CADWIIDLgpeggdGGGQVVASGTP 261
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
26-198 |
2.30e-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: 54.02 E-value: 2.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 26 TVKRGEKLVMIGPSGSGKSTLIRCV---------DYLEEPTSGEVL--IDGTPLtkKNHLEM--------ARK--YSSMV 84
Cdd:COG1245 95 VPKKGKVTGILGPNGIGKSTALKILsgelkpnlgDYDEEPSWDEVLkrFRGTEL--QDYFKKlangeikvAHKpqYVDLI 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 85 FQQFNlypnmtvlGNltlaPIKLQKKSKEE--ATEIAiaalKRVGMAHKAGEYPQNLSGGQQQRIAIARALCTKQPIILF 162
Cdd:COG1245 173 PKVFK--------GT----VRELLEKVDERgkLDELA----EKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFF 236
|
170 180 190
....*....|....*....|....*....|....*....
gi 1469315281 163 DEPTSALDpemVQE---VLDVMIELAQEDITMICVTHEM 198
Cdd:COG1245 237 DEPSSYLD---IYQrlnVARLIRELAEEGKYVLVVEHDL 272
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
26-209 |
2.41e-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: 54.02 E-value: 2.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 26 TVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEV------------LIDGTPLTKKNHLEMARK--YSSMVFQQfnly 91
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVdedlkisykpqyISPDYDGTVEEFLRSANTddFGSSYYKT---- 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 92 pnmTVLGNLTLAPIkLQKKSKEeateiaiaalkrvgmahkageypqnLSGGQQQRIAIARALCTKQPIILFDEPTSALDP 171
Cdd:COG1245 438 ---EIIKPLGLEKL-LDKNVKD-------------------------LSGGELQRVAIAACLSRDADLYLLDEPSAHLDV 488
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1469315281 172 E---MVQEVLDVMIElaQEDITMICVTHEMGFARQVADRVI 209
Cdd:COG1245 489 EqrlAVAKAIRRFAE--NRGKTAMVVDHDIYLIDYISDRLM 527
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
19-172 |
1.50e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 50.26 E-value: 1.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 19 VLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPLTKknhleMARKYSSMVFQQFNLYPNMTVLG 98
Cdd:PRK13541 15 NLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINN-----IAKPYCTYIGHNLGLKLEMTVFE 89
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1469315281 99 NLtlapiKLQKKSKEEATEIAiAALKRVGMAHKAGEYPQNLSGGQQQRIAIARALCTKQPIILFDEPTSALDPE 172
Cdd:PRK13541 90 NL-----KFWSEIYNSAETLY-AAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKE 157
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
113-223 |
2.46e-07 |
|
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: 51.17 E-value: 2.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 113 EEATEI--AIAALKR-------VGMAH-KAGEYPQNLSGGQQQRIAIARAL---CTKQPIILFDEPTSALDPEMVQEVLD 179
Cdd:TIGR00630 794 EEAYEFfeAVPSISRklqtlcdVGLGYiRLGQPATTLSGGEAQRIKLAKELskrSTGRTLYILDEPTTGLHFDDIKKLLE 873
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1469315281 180 VMIELAQEDITMICVTHEMGFARQvADRVIFM------EDGRILEEGTPE 223
Cdd:TIGR00630 874 VLQRLVDKGNTVVVIEHNLDVIKT-ADYIIDLgpeggdGGGTVVASGTPE 922
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
17-197 |
4.49e-07 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 50.23 E-value: 4.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 17 LHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCV------DYLEeptsGEVLIDGTPltkKNHLEMARkySSMVFQQFNL 90
Cdd:PLN03140 893 LQLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLagrktgGYIE----GDIRISGFP---KKQETFAR--ISGYCEQNDI 963
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 91 Y-PNMTVLGNLTLA-----PIKLQKKSK----EEATE-IAIAALKR--VGMAHKAGeypqnLSGGQQQRIAIARALCTKQ 157
Cdd:PLN03140 964 HsPQVTVRESLIYSaflrlPKEVSKEEKmmfvDEVMElVELDNLKDaiVGLPGVTG-----LSTEQRKRLTIAVELVANP 1038
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1469315281 158 PIILFDEPTSALDPEMVQEVLDVMIELAQEDITMICVTHE 197
Cdd:PLN03140 1039 SIIFMDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQ 1078
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
26-198 |
1.28e-06 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 48.65 E-value: 1.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 26 TVKRGEKLVMIGPSGSGKSTLIRCV---------DYLEEPTSGEVL--IDGTPL------TKKNHLEMARKyssmvFQQF 88
Cdd:PRK13409 95 IPKEGKVTGILGPNGIGKTTAVKILsgelipnlgDYEEEPSWDEVLkrFRGTELqnyfkkLYNGEIKVVHK-----PQYV 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 89 NLYPnMTVLGNLtlapIKLQKKSKEeaTEIAIAALKRVGMAHKAGEYPQNLSGGQQQRIAIARALCTKQPIILFDEPTSA 168
Cdd:PRK13409 170 DLIP-KVFKGKV----RELLKKVDE--RGKLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSY 242
|
170 180 190
....*....|....*....|....*....|...
gi 1469315281 169 LDpemVQE---VLDVMIELAqEDITMICVTHEM 198
Cdd:PRK13409 243 LD---IRQrlnVARLIRELA-EGKYVLVVEHDL 271
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
130-196 |
4.23e-06 |
|
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: 46.61 E-value: 4.23e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 130 HKAGEYPQNLSGGQQQ---RIAIARALCTKQPIILFDEPTSALDPEMVQEVLDVMIELAQEDITMICVTH 196
Cdd:pfam13304 228 GGGELPAFELSDGTKRllaLLAALLSALPKGGLLLIDEPESGLHPKLLRRLLELLKELSRNGAQLILTTH 297
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
139-228 |
1.02e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 46.36 E-value: 1.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 139 LSGGQQQRIAIARALCTKQPIILF--DEPTSALDPEMVQEVLDVMIELAQEDITMICVTHEMGFArQVADRVIFME---- 212
Cdd:PRK00635 477 LSGGEQERTALAKHLGAELIGITYilDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEHDEQMI-SLADRIIDIGpgag 555
|
90
....*....|....*...
gi 1469315281 213 --DGRILEEGTPEHFFDN 228
Cdd:PRK00635 556 ifGGEVLFNGSPREFLAK 573
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
15-220 |
1.60e-05 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 45.27 E-value: 1.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 15 GDLH-VLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTpltkknhlemarkySSMVFQQFNLYPN 93
Cdd:PRK13545 34 GEYHyALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGS--------------AALIAISSGLNGQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 94 MTVLGNLTLAPIKLQKKsKEEATEIAIAALKRVGMAHKAGEYPQNLSGGQQQRIAIARALCTKQPIILFDEPTSALDPEM 173
Cdd:PRK13545 100 LTGIENIELKGLMMGLT-KEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTF 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1469315281 174 VQEVLDVMIELAQEDITMICVTHEMGFARQVADRVIFMEDGRILEEG 220
Cdd:PRK13545 179 TKKCLDKMNEFKEQGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYG 225
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
1-46 |
2.14e-05 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 45.02 E-value: 2.14e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1469315281 1 MADMIEIK----HlNkyfgdlhvLKDINLTVKRGeKLVMI-GPSGSGKSTL 46
Cdd:COG0178 2 MMDKIRIRgareH-N--------LKNIDVDIPRN-KLVVItGLSGSGKSSL 42
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
24-204 |
3.09e-05 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 44.50 E-value: 3.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 24 NLTVKRGE--KLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLID-GTPLTKKNHlemarkyssmvfQQFNlYPNMTVL--- 97
Cdd:PRK15064 19 NISVKFGGgnRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLDpNERLGKLRQ------------DQFA-FEEFTVLdtv 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 98 --GNLTLAPIKLQKK---SKEEATE---IAIAALKrVGMAH--------KAGE------YP--------QNLSGGQQQRI 147
Cdd:PRK15064 86 imGHTELWEVKQERDriyALPEMSEedgMKVADLE-VKFAEmdgytaeaRAGElllgvgIPeeqhyglmSEVAPGWKLRV 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1469315281 148 AIARALCTKQPIILFDEPTSALDPEMVQEVLDVmieLAQEDITMICVTHEMGFARQV 204
Cdd:PRK15064 165 LLAQALFSNPDILLLDEPTNNLDINTIRWLEDV---LNERNSTMIIISHDRHFLNSV 218
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
139-216 |
3.30e-05 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 44.56 E-value: 3.30e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1469315281 139 LSGGQQQRIAIARALCTKQPIILFDEPTSALDPEMVqEVLDVMIELAQEDITMIcvTHEMGFARQVADRVIFMEDGRI 216
Cdd:PRK11147 157 LSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETI-EWLEGFLKTFQGSIIFI--SHDRSFIRNMATRIVDLDRGKL 231
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
5-222 |
4.93e-05 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 43.96 E-value: 4.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 5 IEIKHLNKYFGDLHVLKDINLTVKRGEKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVLIDGTPLTKKNHLEMAR------ 78
Cdd:NF033858 2 ARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMADARHRRAVCpriaym 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 79 -----KyssmvfqqfNLYPNMTVLGNLTL-ApiKLQKKSKEEaTEIAIAAL-KRVGMA----HKAGeypqNLSGGQQQRI 147
Cdd:NF033858 82 pqglgK---------NLYPTLSVFENLDFfG--RLFGQDAAE-RRRRIDELlRATGLApfadRPAG----KLSGGMKQKL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 148 AIARALctkqpI------ILfDEPTSALDP-------EMVQEvldvmIELAQEDITMICVTHEMGFARQVaDRVIFMEDG 214
Cdd:NF033858 146 GLCCAL-----IhdpdllIL-DEPTTGVDPlsrrqfwELIDR-----IRAERPGMSVLVATAYMEEAERF-DWLVAMDAG 213
|
....*...
gi 1469315281 215 RILEEGTP 222
Cdd:NF033858 214 RVLATGTP 221
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
120-240 |
5.13e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 44.05 E-value: 5.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 120 IAALKRVGMAH-KAGEYPQNLSGGQQQRIAIARALCT---KQPIILFDEPTSALDPEMVQEVLDVMIELAQEDITMICVT 195
Cdd:PRK00635 790 IHALCSLGLDYlPLGRPLSSLSGGEIQRLKLAYELLApskKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVVIIE 869
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1469315281 196 HEMGFARqVADRVIFM------EDGRILEEGTPEHFF--DNPENPRCREFLSK 240
Cdd:PRK00635 870 HNMHVVK-VADYVLELgpeggnLGGYLLASCSPEELIhlHTPTAKALRPYLSS 921
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
128-216 |
5.56e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 43.70 E-value: 5.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 128 MAHKAgeyPQNLSGGQQQRIAIARALCTKQPIILFDEPTSALDpemVQEVLDVMIELAQEDITMICVTHEMGFARQVADR 207
Cdd:PLN03073 337 MQVKA---TKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLD---LHAVLWLETYLLKWPKTFIVVSHAREFLNTVVTD 410
|
....*....
gi 1469315281 208 VIFMEDGRI 216
Cdd:PLN03073 411 ILHLHGQKL 419
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
139-242 |
5.60e-05 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 43.86 E-value: 5.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 139 LSGGQQQRIAIARALC---TKQPIILFDEPTSALDPEMVQEVLDVMIELAQEDITMICVTHEMGFARqVADRVIfmeD-- 213
Cdd:COG0178 827 LSGGEAQRVKLASELSkrsTGKTLYILDEPTTGLHFHDIRKLLEVLHRLVDKGNTVVVIEHNLDVIK-TADWII---Dlg 902
|
90 100 110
....*....|....*....|....*....|....*.
gi 1469315281 214 -------GRILEEGTPEHFFDNPENPRCReFLSKIL 242
Cdd:COG0178 903 peggdggGEIVAEGTPEEVAKVKASYTGR-YLKEYL 937
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
20-214 |
1.41e-04 |
|
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: 42.30 E-value: 1.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 20 LKDINLTVKRGeKLVMIGPSGSGKSTLIRCVDYLEEPTSGEVL------IDGTPLTKKNHLEMarKYSSMVFQQFNLYPN 93
Cdd:COG3593 14 IKDLSIELSDD-LTVLVGENNSGKSSILEALRLLLGPSSSRKFdeedfyLGDDPDLPEIEIEL--TFGSLLSRLLRLLLK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 94 MTVLGNLTLAPIKLQKKSKEEATEI---------------------------AIAALKRVGMAHKAGEYPQNLSGGQQQR 146
Cdd:COG3593 91 EEDKEELEEALEELNEELKEALKALnellseylkelldgldlelelsldeleDLLKSLSLRIEDGKELPLDRLGSGFQRL 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1469315281 147 I------AIARALCTKQ-PIILFDEPTSALDPEMVQEVLDVMIELAQEDITMICVTHEMGFARQV-ADRVIFMEDG 214
Cdd:COG3593 171 IllallsALAELKRAPAnPILLIEEPEAHLHPQAQRRLLKLLKELSEKPNQVIITTHSPHLLSEVpLENIRRLRRD 246
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
140-218 |
1.46e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 42.46 E-value: 1.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 140 SGGQQQRIAIARALCTKQPIILFDEPTSALDpemvqevLDVMIELAQ----EDITMICVTHEMGFARQVADRVIFMEDGR 215
Cdd:PRK10636 151 SGGWRMRLNLAQALICRSDLLLLDEPTNHLD-------LDAVIWLEKwlksYQGTLILISHDRDFLDPIVDKIIHIEQQS 223
|
...
gi 1469315281 216 ILE 218
Cdd:PRK10636 224 LFE 226
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
1-46 |
1.77e-04 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 42.37 E-value: 1.77e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1469315281 1 MADMIEIK----HlNkyfgdlhvLKDINLTVKRgEKLVMI-GPSGSGKSTL 46
Cdd:PRK00349 2 MMDKIIIRgareH-N--------LKNIDLDIPR-DKLVVFtGLSGSGKSSL 42
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
139-230 |
2.47e-04 |
|
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: 41.92 E-value: 2.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 139 LSGGQQQRIAIARALCTKQPIILF--DEPTSALDPEMVQEVLDVMIELAQEDITMICVTHEMGFARqVADRVIFM----- 211
Cdd:TIGR00630 489 LSGGEAQRIRLATQIGSGLTGVLYvlDEPSIGLHQRDNRRLINTLKRLRDLGNTLIVVEHDEDTIR-AADYVIDIgpgag 567
|
90 100
....*....|....*....|
gi 1469315281 212 -EDGRILEEGTPEHFFDNPE 230
Cdd:TIGR00630 568 eHGGEVVASGTPEEILANPD 587
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
93-242 |
4.96e-04 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 40.83 E-value: 4.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 93 NMTVlgnltlapiklqkkskEEATEI--AIAALKR-------VGMAH-KAGeypQN---LSGGQQQRIAIARAL---CTK 156
Cdd:PRK00349 791 DMTV----------------EEALEFfeAIPKIARklqtlvdVGLGYiKLG---QPattLSGGEAQRVKLAKELskrSTG 851
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 157 QPIILFDEPTSALDPEMVQEVLDVMIELAQEDITMICVTHEMGFARQvADRVIFM------EDGRILEEGTPEHFFDNPE 230
Cdd:PRK00349 852 KTLYILDEPTTGLHFEDIRKLLEVLHRLVDKGNTVVVIEHNLDVIKT-ADWIIDLgpeggdGGGEIVATGTPEEVAKVEA 930
|
170
....*....|..
gi 1469315281 231 NPRCReFLSKIL 242
Cdd:PRK00349 931 SYTGR-YLKPVL 941
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
5-185 |
6.73e-04 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 39.61 E-value: 6.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 5 IEIKHLNKYFGDLHVLKDINLTVkrgeklvMIGPSGSGKSTLIRCVDY-LEEPTSG--------------------EVLI 63
Cdd:COG0419 5 LRLENFRSYRDTETIDFDDGLNL-------IVGPNGAGKSTILEAIRYaLYGKARSrsklrsdlinvgseeasvelEFEH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 64 DGTPLT-KKNHLEMAR-------KYSSMVFQQFNLYPNMTVLGNLTLAPIKLQKKsKEEATEIAIAALKRVGMAHKAGEY 135
Cdd:COG0419 78 GGKRYRiERRQGEFAEfleakpsERKEALKRLLGLEIYEELKERLKELEEALESA-LEELAELQKLKQEILAQLSGLDPI 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1469315281 136 PQnLSGGQQQRIAIARALctkqPIILfDepTSALDPEMVQEVLDVMIELA 185
Cdd:COG0419 157 ET-LSGGERLRLALADLL----SLIL-D--FGSLDEERLERLLDALEELA 198
|
|
| IcmF |
COG3523 |
Type VI protein secretion system component VasK [Intracellular trafficking, secretion, and ... |
6-49 |
7.16e-04 |
|
Type VI protein secretion system component VasK [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 442745 [Multi-domain] Cd Length: 1192 Bit Score: 40.71 E-value: 7.16e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1469315281 6 EIKHLNKYFGD-LHVLKDINLTVKRGEK----L---VMIGPSGSGKSTLIRC 49
Cdd:COG3523 94 EIEALRERFQEaLATLKKSRLGQGGGRRalyeLpwyLIIGPPGAGKTTALVN 145
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
18-46 |
1.75e-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: 39.23 E-value: 1.75e-03
10 20
....*....|....*....|....*....
gi 1469315281 18 HVLKDINLTVKRGEKLVMIGPSGSGKSTL 46
Cdd:TIGR00630 10 HNLKNIDVEIPRDKLVVITGLSGSGKSSL 38
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
105-200 |
2.90e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 38.87 E-value: 2.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 105 IKLQKKSKEEATEIAIAALKRVGMAHKAGEYPQNLSG----GQQQ------RIAIARALCTKQPIILFDEPTSALDPEMV 174
Cdd:TIGR00606 1162 IEIRSDADENVSASDKRRNYNYRVVMLKGDTALDMRGrcsaGQKVlasliiRLALAETFCLNCGIIALDEPTTNLDRENI 1241
|
90 100 110
....*....|....*....|....*....|.
gi 1469315281 175 QEVLDVMIEL-----AQEDITMICVTHEMGF 200
Cdd:TIGR00606 1242 ESLAHALVEIiksrsQQRNFQLLVITHDEDF 1272
|
|
| COG4639 |
COG4639 |
Predicted kinase [General function prediction only]; |
34-48 |
2.91e-03 |
|
Predicted kinase [General function prediction only];
Pssm-ID: 443677 [Multi-domain] Cd Length: 145 Bit Score: 37.12 E-value: 2.91e-03
|
| ABC_ATPase |
pfam09818 |
ATPase of the ABC class; This is the C-terminal ATPase domain from bacterial ABC class ATPases. ... |
137-218 |
2.92e-03 |
|
ATPase of the ABC class; This is the C-terminal ATPase domain from bacterial ABC class ATPases. This entry also includes MRB1590 from Trypanosoma brucei brucei has a central ATPase domain homologous to this domain.
Pssm-ID: 462914 Cd Length: 282 Bit Score: 37.96 E-value: 2.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 137 QNLSGGQQQRIAIARALCTKQPIILFDEPTSA-----LDPEM------VQEVLDVMIELAQED-----ITMICVTHEMGF 200
Cdd:pfam09818 156 EDASGSTSQAANIMEALEAGASLLLIDEDTSAtnfmiRDERMqalvskDKEPITPFVDRVRSLyddlgVSTILVVGGSGD 235
|
90
....*....|....*...
gi 1469315281 201 ARQVADRVIFMEDGRILE 218
Cdd:pfam09818 236 YLDVADTVILMDEYRPSD 253
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
20-47 |
6.01e-03 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 37.74 E-value: 6.01e-03
10 20
....*....|....*....|....*....
gi 1469315281 20 LKDINLTVKRGeKLVMI-GPSGSGKSTLI 47
Cdd:PRK00349 625 LKNVDVEIPLG-KFTCVtGVSGSGKSTLI 652
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
123-214 |
7.45e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 37.50 E-value: 7.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469315281 123 LKRVGMAH-KAGEYPQNLSGGQQQRIAIARALCTK--QPIILFDEPTSALDPEMVQEVLDVMIELAQEDITMIcVTHEMG 199
Cdd:PRK00635 1371 IDKVGLSYiTLGQEQDTLSDGEHYRLHLAKKISSNltDIIYLLEDPLSGLHPQDAPTLLQLIKELVTNNNTVI-ATDRSG 1449
|
90
....*....|....*
gi 1469315281 200 FARQVADRVIFMEDG 214
Cdd:PRK00635 1450 SLAEHADHLIHLGPG 1464
|
|
| |
