|
Name |
Accession |
Description |
Interval |
E-value |
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
12-250 |
3.28e-175 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 481.42 E-value: 3.28e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 12 IISVAGVNKWYGAFQVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIELGQSENAAQAVRREVG 91
Cdd:COG1126 1 MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKKDINKLRRKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 92 MVFQHFNLFPHLDLVQNCILAPMSVRGMSRRAAEALAVGLLERVRLGEHAHKYPSQLSGGQQQRAAIARALCMEPRVMLF 171
Cdd:COG1126 81 MVFQQFNLFPHLTVLENVTLAPIKVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKVMLF 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 500071467 172 DEPTSALDPEMVGEVLDTMRGLAAEGMTMMIVTHEMGFARQVADRVVFMDRGQIVEQAPPAAFFGAPVHERTRRFLSQI 250
Cdd:COG1126 161 DEPTSALDPELVGEVLDVMRDLAKEGMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFENPQHERTRAFLSKV 239
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
13-225 |
1.45e-138 |
|
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: 387.66 E-value: 1.45e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 13 ISVAGVNKWYGAFQVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIELGQSENAAQAVRREVGM 92
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNINELRQKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 93 VFQHFNLFPHLDLVQNCILAPMSVRGMSRRAAEALAVGLLERVRLGEHAHKYPSQLSGGQQQRAAIARALCMEPRVMLFD 172
Cdd:cd03262 81 VFQQFNLFPHLTVLENITLAPIKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 500071467 173 EPTSALDPEMVGEVLDTMRGLAAEGMTMMIVTHEMGFARQVADRVVFMDRGQI 225
Cdd:cd03262 161 EPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
6-252 |
5.34e-118 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 337.54 E-value: 5.34e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 6 ASPAAPIISVAGVNKWYGAFQVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIEL-------GQ 78
Cdd:COG4598 2 TDTAPPALEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIrlkpdrdGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 79 SENA----AQAVRREVGMVFQHFNLFPHLDLVQNCILAPMSVRGMSRRAAEALAVGLLERVRLGEHAHKYPSQLSGGQQQ 154
Cdd:COG4598 82 LVPAdrrqLQRIRTRLGMVFQSFNLWSHMTVLENVIEAPVHVLGRPKAEAIERAEALLAKVGLADKRDAYPAHLSGGQQQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 155 RAAIARALCMEPRVMLFDEPTSALDPEMVGEVLDTMRGLAAEGMTMMIVTHEMGFARQVADRVVFMDRGQIVEQAPPAAF 234
Cdd:COG4598 162 RAAIARALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEEGRTMLVVTHEMGFARDVSSHVVFLHQGRIEEQGPPAEV 241
|
250
....*....|....*...
gi 500071467 235 FGAPVHERTRRFLSQILH 252
Cdd:COG4598 242 FGNPKSERLRQFLSSSLK 259
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
12-250 |
1.70e-110 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 317.81 E-value: 1.70e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 12 IISVAGVNKWYGAFQVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIELGQSENAAQAVRREVG 91
Cdd:PRK09493 1 MIEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLIRQEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 92 MVFQHFNLFPHLDLVQNCILAPMSVRGMSRRAAEALAVGLLERVRLGEHAHKYPSQLSGGQQQRAAIARALCMEPRVMLF 171
Cdd:PRK09493 81 MVFQQFYLFPHLTALENVMFGPLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLF 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 500071467 172 DEPTSALDPEMVGEVLDTMRGLAAEGMTMMIVTHEMGFARQVADRVVFMDRGQIVEQAPPAAFFGAPVHERTRRFLSQI 250
Cdd:PRK09493 161 DEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPPSQRLQEFLQHV 239
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
13-251 |
2.87e-100 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 292.42 E-value: 2.87e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 13 ISVAGVNKWYGAFQVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIE------LGQSENAAQAV 86
Cdd:PRK11264 4 IEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITidtarsLSQQKGLIRQL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 87 RREVGMVFQHFNLFPHLDLVQNCILAPMSVRGMSRRAAEALAVGLLERVRLGEHAHKYPSQLSGGQQQRAAIARALCMEP 166
Cdd:PRK11264 84 RQHVGFVFQNFNLFPHRTVLENIIEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 167 RVMLFDEPTSALDPEMVGEVLDTMRGLAAEGMTMMIVTHEMGFARQVADRVVFMDRGQIVEQAPPAAFFGAPVHERTRRF 246
Cdd:PRK11264 164 EVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADPQQPRTRQF 243
|
....*
gi 500071467 247 LSQIL 251
Cdd:PRK11264 244 LEKFL 248
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
13-248 |
7.34e-97 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 283.44 E-value: 7.34e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 13 ISVAGVNKWYGAFQVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEG--SIVVDGIELGQSENAAQ--AVRR 88
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGtlNIAGNHFDFSKTPSDKAirELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 89 EVGMVFQHFNLFPHLDLVQNCILAPMSVRGMSRRAAEALAVGLLERVRLGEHAHKYPSQLSGGQQQRAAIARALCMEPRV 168
Cdd:PRK11124 83 NVGMVFQQYNLWPHLTVQQNLIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 169 MLFDEPTSALDPEMVGEVLDTMRGLAAEGMTMMIVTHEMGFARQVADRVVFMDRGQIVEQApPAAFFGAPVHERTRRFLS 248
Cdd:PRK11124 163 LLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTHEVEVARKTASRVVYMENGHIVEQG-DASCFTQPQTEAFKNYLS 241
|
|
| ectoine_ehuA |
TIGR03005 |
ectoine/hydroxyectoine ABC transporter, ATP-binding protein; Members of this family are the ... |
13-251 |
1.10e-96 |
|
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: 283.26 E-value: 1.10e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 13 ISVAGVNKWYGAFQVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIEL-------GQ----SEN 81
Cdd:TIGR03005 1 VRFSDVTKRFGILTVLDGLNFSVAAGEKVALIGPSGSGKSTILRILMTLEPIDEGQIQVEGEQLyhmpgrnGPlvpaDEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 82 AAQAVRREVGMVFQHFNLFPHLDLVQNCILAPMSVRGMSRRAAEALAVGLLERVRLGEHAHKYPSQLSGGQQQRAAIARA 161
Cdd:TIGR03005 81 HLRQMRNKIGMVFQSFNLFPHKTVLDNVTEAPVLVLGMARAEAEKRAMELLDMVGLADKADHMPAQLSGGQQQRVAIARA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 162 LCMEPRVMLFDEPTSALDPEMVGEVLDTMRGLAAE-GMTMMIVTHEMGFARQVADRVVFMDRGQIVEQAPPAAFFGAPVH 240
Cdd:TIGR03005 161 LAMRPKVMLFDEVTSALDPELVGEVLNVIRRLASEhDLTMLLVTHEMGFAREFADRVCFFDKGRIVEQGKPDEIFRQPKE 240
|
250
....*....|.
gi 500071467 241 ERTRRFLSQIL 251
Cdd:TIGR03005 241 ERTREFLSKVI 251
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
13-248 |
9.02e-94 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 275.35 E-value: 9.02e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 13 ISVAGVNKWYGAFQVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIEL----GQSENAAQAVRR 88
Cdd:COG4161 3 IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFdfsqKPSEKAIRLLRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 89 EVGMVFQHFNLFPHLDLVQNCILAPMSVRGMSRRAAEALAVGLLERVRLGEHAHKYPSQLSGGQQQRAAIARALCMEPRV 168
Cdd:COG4161 83 KVGMVFQQYNLWPHLTVMENLIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 169 MLFDEPTSALDPEMVGEVLDTMRGLAAEGMTMMIVTHEMGFARQVADRVVFMDRGQIVEQApPAAFFGAPVHERTRRFLS 248
Cdd:COG4161 163 LLFDEPTAALDPEITAQVVEIIRELSQTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQG-DASHFTQPQTEAFAHYLS 241
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
12-252 |
4.02e-92 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 274.65 E-value: 4.02e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 12 IISVAGVNKWY----GAFQVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIELGQ-SENAAQAV 86
Cdd:COG1135 1 MIELENLSKTFptkgGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTAlSERELRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 87 RREVGMVFQHFNLFPHLDLVQNcILAPMSVRGMSRRAAEALAVGLLERVRLGEHAHKYPSQLSGGQQQRAAIARALCMEP 166
Cdd:COG1135 81 RRKIGMIFQHFNLLSSRTVAEN-VALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 167 RVMLFDEPTSALDPEMVGEVLDTMRGLAAE-GMTMMIVTHEMGFARQVADRVVFMDRGQIVEQAPPAAFFGAPVHERTRR 245
Cdd:COG1135 160 KVLLCDEATSALDPETTRSILDLLKDINRElGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVLDVFANPQSELTRR 239
|
....*..
gi 500071467 246 FLSQILH 252
Cdd:COG1135 240 FLPTVLN 246
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
10-228 |
1.11e-85 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 254.20 E-value: 1.11e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 10 APIISVAGVNKWYG----AFQVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIELGQ-SENAAQ 84
Cdd:COG1136 2 SPLLELRNLTKSYGtgegEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSlSERELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 85 AVRRE-VGMVFQHFNLFPHLDLVQNcILAPMSVRGMSRRAAEALAVGLLERVRLGEHAHKYPSQLSGGQQQRAAIARALC 163
Cdd:COG1136 82 RLRRRhIGFVFQFFNLLPELTALEN-VALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 500071467 164 MEPRVMLFDEPTSALDPEMVGEVLDTMRGLAAE-GMTMMIVTHEMGFARQvADRVVFMDRGQIVEQ 228
Cdd:COG1136 161 NRPKLILADEPTGNLDSKTGEEVLELLRELNRElGTTIVMVTHDPELAAR-ADRVIRLRDGRIVSD 225
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
13-251 |
6.37e-83 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 248.73 E-value: 6.37e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 13 ISVAGVNKWYGAFQVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIEL-------GQ----SEN 81
Cdd:PRK10619 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTInlvrdkdGQlkvaDKN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 82 AAQAVRREVGMVFQHFNLFPHLDLVQNCILAPMSVRGMSRRAAEALAVGLLERVRLGEHAH-KYPSQLSGGQQQRAAIAR 160
Cdd:PRK10619 86 QLRLLRTRLTMVFQHFNLWSHMTVLENVMEAPIQVLGLSKQEARERAVKYLAKVGIDERAQgKYPVHLSGGQQQRVSIAR 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 161 ALCMEPRVMLFDEPTSALDPEMVGEVLDTMRGLAAEGMTMMIVTHEMGFARQVADRVVFMDRGQIVEQAPPAAFFGAPVH 240
Cdd:PRK10619 166 ALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGNPQS 245
|
250
....*....|.
gi 500071467 241 ERTRRFLSQIL 251
Cdd:PRK10619 246 PRLQQFLKGSL 256
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
8-247 |
2.53e-81 |
|
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: 243.73 E-value: 2.53e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 8 PAAPIISVAGVNKWYGAFQVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIELGQ-SENAAQAV 86
Cdd:COG1127 1 MSEPMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGlSEKELYEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 87 RREVGMVFQHFNLFPHLDLVQNcILAPMSVRG-MSRRAAEALAVGLLERVRLGEHAHKYPSQLSGGQQQRAAIARALCME 165
Cdd:COG1127 81 RRRIGMLFQGGALFDSLTVFEN-VAFPLREHTdLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 166 PRVMLFDEPTSALDPEMVGEVLDTMRGLAAE-GMTMMIVTHEMGFARQVADRVVFMDRGQIVEQAPPAAFFGAPvHERTR 244
Cdd:COG1127 160 PEILLYDEPTAGLDPITSAVIDELIRELRDElGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLASD-DPWVR 238
|
...
gi 500071467 245 RFL 247
Cdd:COG1127 239 QFL 241
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
13-225 |
2.72e-81 |
|
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: 242.78 E-value: 2.72e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 13 ISVAGVNKWYGA----FQVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIELGQ-SENAAQAVR 87
Cdd:cd03255 1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKlSEKELAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 88 RE-VGMVFQHFNLFPHLDLVQNcILAPMSVRGMSRRAAEALAVGLLERVRLGEHAHKYPSQLSGGQQQRAAIARALCMEP 166
Cdd:cd03255 81 RRhIGFVFQSFNLLPDLTALEN-VELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 167 RVMLFDEPTSALDPEMVGEVLDTMRGLAAE-GMTMMIVTHEMGFARQvADRVVFMDRGQI 225
Cdd:cd03255 160 KIILADEPTGNLDSETGKEVMELLRELNKEaGTTIVVVTHDPELAEY-ADRIIELRDGKI 218
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
12-238 |
4.32e-80 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 240.56 E-value: 4.32e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 12 IISVAGVNKWYG----AFQVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIELGQ-SENAAQAV 86
Cdd:cd03258 1 MIELKNVSKVFGdtggKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLlSGKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 87 RREVGMVFQHFNLFPHLDLVQNcILAPMSVRGMSRRAAEALAVGLLERVRLGEHAHKYPSQLSGGQQQRAAIARALCMEP 166
Cdd:cd03258 81 RRRIGMIFQHFNLLSSRTVFEN-VALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNP 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 500071467 167 RVMLFDEPTSALDPEMVGEVLDTMRGLAAE-GMTMMIVTHEMGFARQVADRVVFMDRGQIVEQAPPAAFFGAP 238
Cdd:cd03258 160 KVLLCDEATSALDPETTQSILALLRDINRElGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFANP 232
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
2-250 |
5.26e-80 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 249.44 E-value: 5.26e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 2 PNPDASPAAPIISVAGVNKWY-----GAFQVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIEL 76
Cdd:COG1123 250 AAPAAAAAEPLLEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDL 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 77 -GQSENAAQAVRREVGMVFQH-FNLFPHLDLVQNCILAPMSVRG-MSRRAAEALAVGLLERVRLG-EHAHKYPSQLSGGQ 152
Cdd:COG1123 330 tKLSRRSLRELRRRVQMVFQDpYSSLNPRMTVGDIIAEPLRLHGlLSRAERRERVAELLERVGLPpDLADRYPHELSGGQ 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 153 QQRAAIARALCMEPRVMLFDEPTSALDPEMVGEVLDTMRGLAAE-GMTMMIVTHEMGFARQVADRVVFMDRGQIVEQAPP 231
Cdd:COG1123 410 RQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRElGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPT 489
|
250
....*....|....*....
gi 500071467 232 AAFFGAPVHERTRRFLSQI 250
Cdd:COG1123 490 EEVFANPQHPYTRALLAAV 508
|
|
| 3a0107s01c2 |
TIGR00972 |
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein ... |
12-248 |
5.10e-79 |
|
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: 238.35 E-value: 5.10e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 12 IISVAGVNKWYGAFQVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQL-----EQHQEGSIVVDGIELGQSENAAQAV 86
Cdd:TIGR00972 1 AIEIENLNLFYGEKEALKNINLDIPKNQVTALIGPSGCGKSTLLRSLNRMndlvpGVRIEGKVLFDGQDIYDKKIDVVEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 87 RREVGMVFQHFNLFPhLDLVQNCILAPMSVRGMSRRAAEALAVGLLERVRLGEH----AHKYPSQLSGGQQQRAAIARAL 162
Cdd:TIGR00972 81 RRRVGMVFQKPNPFP-MSIYDNIAYGPRLHGIKDKKELDEIVEESLKKAALWDEvkdrLHDSALGLSGGQQQRLCIARAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 163 CMEPRVMLFDEPTSALDPEMVGEVLDTMRGLaAEGMTMMIVTHEMGFARQVADRVVFMDRGQIVEQAPPAAFFGAPVHER 242
Cdd:TIGR00972 160 AVEPEVLLLDEPTSALDPIATGKIEELIQEL-KKKYTIVIVTHNMQQAARISDRTAFFYDGELVEYGPTEQIFTNPKEKR 238
|
....*.
gi 500071467 243 TRRFLS 248
Cdd:TIGR00972 239 TEDYIS 244
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
13-252 |
2.71e-78 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 239.70 E-value: 2.71e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 13 ISVAGVNKWY----GAFQVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIELGQ-SENAAQAVR 87
Cdd:PRK11153 2 IELKNISKVFpqggRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTAlSEKELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 88 REVGMVFQHFNLFPHLDLVQNCILaPMSVRGMSRRAAEALAVGLLERVRLGEHAHKYPSQLSGGQQQRAAIARALCMEPR 167
Cdd:PRK11153 82 RQIGMIFQHFNLLSSRTVFDNVAL-PLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 168 VMLFDEPTSALDPEMVGEVLDTMRGLAAE-GMTMMIVTHEMGFARQVADRVVFMDRGQIVEQAPPAAFFGAPVHERTRRF 246
Cdd:PRK11153 161 VLLCDEATSALDPATTRSILELLKDINRElGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHPKHPLTREF 240
|
....*.
gi 500071467 247 LSQILH 252
Cdd:PRK11153 241 IQSTLH 246
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
11-234 |
2.89e-78 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 236.11 E-value: 2.89e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 11 PIISVAGVNKWY-GAFQVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIELGQSENAA-QAVRR 88
Cdd:COG3638 1 PMLELRNLSKRYpGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRAlRRLRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 89 EVGMVFQHFNLFPHLDLVQNcILA--------PMSVRGMSRRAAEALAVGLLERVRLGEHAHKYPSQLSGGQQQRAAIAR 160
Cdd:COG3638 81 RIGMIFQQFNLVPRLSVLTN-VLAgrlgrtstWRSLLGLFPPEDRERALEALERVGLADKAYQRADQLSGGQQQRVAIAR 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 500071467 161 ALCMEPRVMLFDEPTSALDPEMVGEVLDTMRGLAAE-GMTMMIVTHEMGFARQVADRVVFMDRGQIVEQAPPAAF 234
Cdd:COG3638 160 ALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREdGITVVVNLHQVDLARRYADRIIGLRDGRVVFDGPPAEL 234
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
23-235 |
2.73e-75 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 227.99 E-value: 2.73e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 23 GAFQVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIELgqSENAAQAVRREVGMVFQhfnlFPH 102
Cdd:COG1122 12 GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDI--TKKNLRELRRKVGLVFQ----NPD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 103 LDLV-----QNCILAPMSvRGMSRRAAEALAVGLLERVRLGEHAHKYPSQLSGGQQQRAAIARALCMEPRVMLFDEPTSA 177
Cdd:COG1122 86 DQLFaptveEDVAFGPEN-LGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLVLDEPTAG 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 500071467 178 LDPEMVGEVLDTMRGLAAEGMTMMIVTHEMGFARQVADRVVFMDRGQIVEQAPPAAFF 235
Cdd:COG1122 165 LDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVF 222
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
9-247 |
1.53e-74 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 230.37 E-value: 1.53e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 9 AAPIISVAGVNKWYGAFQVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIELgqseNAAQAVRR 88
Cdd:COG3842 2 AMPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDV----TGLPPEKR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 89 EVGMVFQHFNLFPHLDLVQNcILAPMSVRGMSRRAAEALAVGLLERVRLGEHAHKYPSQLSGGQQQRAAIARALCMEPRV 168
Cdd:COG3842 78 NVGMVFQDYALFPHLTVAEN-VAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 169 MLFDEPTSALDPEMVGEVLDTMRGLAAE-GMTMMIVTHEMGFARQVADRVVFMDRGQIVEQAPPAAFFGAPVHERTRRFL 247
Cdd:COG3842 157 LLLDEPLSALDAKLREEMREELRRLQRElGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEIYERPATRFVADFI 236
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
7-227 |
1.07e-73 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 224.97 E-value: 1.07e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 7 SPAAPIISVAGVNKWY----GAFQVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIELgqsena 82
Cdd:COG1116 2 SAAAPALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPV------ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 83 aQAVRREVGMVFQHFNLFPHLDLVQNcILAPMSVRGMSRRAAEALAVGLLERVRLGEHAHKYPSQLSGGQQQRAAIARAL 162
Cdd:COG1116 76 -TGPGPDRGVVFQEPALLPWLTVLDN-VALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARAL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 500071467 163 CMEPRVMLFDEPTSALDP----EMVGEVLDTmrgLAAEGMTMMIVTHEMGFARQVADRVVFMDR--GQIVE 227
Cdd:COG1116 154 ANDPEVLLMDEPFGALDAltreRLQDELLRL---WQETGKTVLFVTHDVDEAVFLADRVVVLSArpGRIVE 221
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
13-234 |
8.82e-73 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 221.86 E-value: 8.82e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 13 ISVAGVNKWYGAFQVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIELGQsenAAQAVRREVGM 92
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVAR---DPAEVRRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 93 VFQHFNLFPHLDLVQNCILApMSVRGMSRRAAEALAVGLLERVRLGEHAHKYPSQLSGGQQQRAAIARALCMEPRVMLFD 172
Cdd:COG1131 78 VPQEPALYPDLTVRENLRFF-ARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILD 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 500071467 173 EPTSALDPEMVGEVLDTMRGLAAEGMTMMIVTHEMGFARQVADRVVFMDRGQIVEQAPPAAF 234
Cdd:COG1131 157 EPTSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDEL 218
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
13-229 |
3.90e-72 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 219.31 E-value: 3.90e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 13 ISVAGVNKWYGAFQVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGielgQSENAAQAVRREVGM 92
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDG----RDVTGVPPERRNIGM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 93 VFQHFNLFPHLDLVQNcILAPMSVRGMSRRAAEALAVGLLERVRLGEHAHKYPSQLSGGQQQRAAIARALCMEPRVMLFD 172
Cdd:cd03259 77 VFQDYALFPHLTVAEN-IAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 500071467 173 EPTSALDPEMVGEVLDTMRGLAAE-GMTMMIVTHEMGFARQVADRVVFMDRGQIVEQA 229
Cdd:cd03259 156 EPLSALDAKLREELREELKELQRElGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
13-247 |
5.56e-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: 220.44 E-value: 5.56e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 13 ISVAGVNKWYGA----FQVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIELGQSENAAQavRR 88
Cdd:COG1124 2 LEVRNLSVSYGQggrrVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAF--RR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 89 EVGMVFQHfnlfPHLDL-----VQNCILAPMSVRGMSRRAAEALAvgLLERVRLG-EHAHKYPSQLSGGQQQRAAIARAL 162
Cdd:COG1124 80 RVQMVFQD----PYASLhprhtVDRILAEPLRIHGLPDREERIAE--LLEQVGLPpSFLDRYPHQLSGGQRQRVAIARAL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 163 CMEPRVMLFDEPTSALDPEMVGEVLDTMRGLAAE-GMTMMIVTHEMGFARQVADRVVFMDRGQIVEQAPPAAFFGAPVHE 241
Cdd:COG1124 154 ILEPELLLLDEPTSALDVSVQAEILNLLKDLREErGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAGPKHP 233
|
....*.
gi 500071467 242 RTRRFL 247
Cdd:COG1124 234 YTRELL 239
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
12-229 |
4.85e-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: 217.37 E-value: 4.85e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 12 IISVAGVNKWY----GAFQVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIELGQSENAAQAVR 87
Cdd:cd03257 1 LLEVKNLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 88 R-EVGMVFQHfnlfPHLDL-----VQNCILAPMSVRGMSRRAAEALAVGLLERVRLG---EHAHKYPSQLSGGQQQRAAI 158
Cdd:cd03257 81 RkEIQMVFQD----PMSSLnprmtIGEQIAEPLRIHGKLSKKEARKEAVLLLLVGVGlpeEVLNRYPHELSGGQRQRVAI 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 500071467 159 ARALCMEPRVMLFDEPTSALDPEMVGEVLDTMRGLAAE-GMTMMIVTHEMGFARQVADRVVFMDRGQIVEQA 229
Cdd:cd03257 157 ARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEElGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
13-246 |
6.77e-71 |
|
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: 216.98 E-value: 6.77e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 13 ISVAGVNKWYGAFQVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIELGQ-SENAAQAVRREVG 91
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGlSEAELYRLRRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 92 MVFQHFNLFPHLDLVQNcILAPMSVRG-MSRRAAEALAVGLLERVRLGEHAHKYPSQLSGGQQQRAAIARALCMEPRVML 170
Cdd:cd03261 81 MLFQSGALFDSLTVFEN-VAFPLREHTrLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 500071467 171 FDEPTSALDPEMVGEVLDTMRGLAAE-GMTMMIVTHEMGFARQVADRVVFMDRGQIVEQAPPAAFFGAPvHERTRRF 246
Cdd:cd03261 160 YDEPTAGLDPIASGVIDDLIRSLKKElGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRASD-DPLVRQF 235
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
13-234 |
2.30e-70 |
|
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: 215.89 E-value: 2.30e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 13 ISVAGVNKWYGA-FQVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIELGQ-SENAAQAVRREV 90
Cdd:cd03256 1 IEVENLSKTYPNgKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKlKGKALRQLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 91 GMVFQHFNLFPHLDLVQNCI---LAPMS-VRGMSRRAAEA---LAVGLLERVRLGEHAHKYPSQLSGGQQQRAAIARALC 163
Cdd:cd03256 81 GMIFQQFNLIERLSVLENVLsgrLGRRStWRSLFGLFPKEekqRALAALERVGLLDKAYQRADQLSGGQQQRVAIARALM 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 500071467 164 MEPRVMLFDEPTSALDPEMVGEVLDTMRGLAAE-GMTMMIVTHEMGFARQVADRVVFMDRGQIVEQAPPAAF 234
Cdd:cd03256 161 QQPKLILADEPVASLDPASSRQVMDLLKRINREeGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAEL 232
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
13-247 |
6.32e-70 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 218.48 E-value: 6.32e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 13 ISVAGVNKWYGAFQVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIELgqseNAAQAVR-REVG 91
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDL----FTNLPPReRRVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 92 MVFQHFNLFPHLDLVQNcILAPMSVRGMSRRAAEALAVGLLERVRLGEHAHKYPSQLSGGQQQRAAIARALCMEPRVMLF 171
Cdd:COG1118 79 FVFQHYALFPHMTVAEN-IAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLLL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 172 DEPTSALD----PEM---VGEVLDTMRGlaaegmTMMIVTHEMGFARQVADRVVFMDRGQIVEQAPPAAFFGAPVHERTR 244
Cdd:COG1118 158 DEPFGALDakvrKELrrwLRRLHDELGG------TTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDRPATPFVA 231
|
...
gi 500071467 245 RFL 247
Cdd:COG1118 232 RFL 234
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
3-248 |
1.69e-69 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 214.13 E-value: 1.69e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 3 NPDASPAAPIISVAGVNKWYGAFQVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQL-----EQHQEGSIVVDGIE-L 76
Cdd:COG1117 2 TAPASTLEPKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMndlipGARVEGEILLDGEDiY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 77 GQSENAAQaVRREVGMVFQHFNLFPH--LDlvqNcILAPMSVRGMSRRAA------EAL-AVGLLERV--RLgehaHKYP 145
Cdd:COG1117 82 DPDVDVVE-LRRRVGMVFQKPNPFPKsiYD---N-VAYGLRLHGIKSKSEldeiveESLrKAALWDEVkdRL----KKSA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 146 SQLSGGQQQRAAIARALCMEPRVMLFDEPTSALDPEMVGEVLDTMRGLAAEgMTMMIVTHEMGFARQVADRVVFMDRGQI 225
Cdd:COG1117 153 LGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKD-YTIVIVTHNMQQAARVSDYTAFFYLGEL 231
|
250 260
....*....|....*....|...
gi 500071467 226 VEQAPPAAFFGAPVHERTRRFLS 248
Cdd:COG1117 232 VEFGPTEQIFTNPKDKRTEDYIT 254
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
13-234 |
1.82e-69 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 213.20 E-value: 1.82e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 13 ISVAGVNKWYGAFQVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQ-----EGSIVVDGIELGQSENAAQAVR 87
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIpgapdEGEVLLDGKDIYDLDVDVLELR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 88 REVGMVFQHFNLFPHLdlVQNCILAPMSVRGM-SRRAAEALAVGLLERVRLGEHAHK--YPSQLSGGQQQRAAIARALCM 164
Cdd:cd03260 81 RRVGMVFQKPNPFPGS--IYDNVAYGLRLHGIkLKEELDERVEEALRKAALWDEVKDrlHALGLSGGQQQRLCLARALAN 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 165 EPRVMLFDEPTSALDPEMVGEVLDTMRGLAAEgMTMMIVTHEMGFARQVADRVVFMDRGQIVEQAPPAAF 234
Cdd:cd03260 159 EPEVLLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
13-224 |
2.30e-69 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 211.28 E-value: 2.30e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 13 ISVAGVNKWYGAFQVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIELGQSENAAQAVRREVGM 92
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPPLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 93 VFQHFNLFPHLDLVQNCILApmsvrgmsrraaealavgllervrlgehahkypsqLSGGQQQRAAIARALCMEPRVMLFD 172
Cdd:cd03229 81 VFQDFALFPHLTVLENIALG-----------------------------------LSGGQQQRVALARALAMDPDVLLLD 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 500071467 173 EPTSALDPEMVGEVLDTMRGLAAE-GMTMMIVTHEMGFARQVADRVVFMDRGQ 224
Cdd:cd03229 126 EPTSALDPITRREVRALLKSLQAQlGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
12-227 |
3.16e-69 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 212.22 E-value: 3.16e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 12 IISVAGVNKWY-GAFQVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIELGQ-SENAAQAVRRE 89
Cdd:COG2884 1 MIRFENVSKRYpGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRlKRREIPYLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 90 VGMVFQHFNLFPHLDLVQNcILAPMSVRGMSRRAAEALAVGLLERVRLGEHAHKYPSQLSGGQQQRAAIARALCMEPRVM 169
Cdd:COG2884 81 IGVVFQDFRLLPDRTVYEN-VALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 500071467 170 LFDEPTSALDPEMVGEVLDTMRGLAAEGMTMMIVTHEMGFARQVADRVVFMDRGQIVE 227
Cdd:COG2884 160 LADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLELVDRMPKRVLELEDGRLVR 217
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
12-234 |
2.31e-67 |
|
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: 208.31 E-value: 2.31e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 12 IISVAGVNKWYG-AFQVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIELGQ-SENAAQAVRRE 89
Cdd:TIGR02315 1 MLEVENLSKVYPnGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKlRGKKLRKLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 90 VGMVFQHFNLFPHLDLVQNCI---LAPMS-VRGMSRRAAEA---LAVGLLERVRLGEHAHKYPSQLSGGQQQRAAIARAL 162
Cdd:TIGR02315 81 IGMIFQHYNLIERLTVLENVLhgrLGYKPtWRSLLGRFSEEdkeRALSALERVGLADKAYQRADQLSGGQQQRVAIARAL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 500071467 163 CMEPRVMLFDEPTSALDPEMVGEVLDTMRGLAAE-GMTMMIVTHEMGFARQVADRVVFMDRGQIVEQAPPAAF 234
Cdd:TIGR02315 161 AQQPDLILADEPIASLDPKTSKQVMDYLKRINKEdGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSEL 233
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
23-224 |
2.53e-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: 204.62 E-value: 2.53e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 23 GAFQVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIELgqSENAAQAVRREVGMVFQH-----F 97
Cdd:cd03225 12 GARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDL--TKLSLKELRRKVGLVFQNpddqfF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 98 NLFPHLDLVQNCILapmsvRGMSRRAAEALAVGLLERVRLGEHAHKYPSQLSGGQQQRAAIARALCMEPRVMLFDEPTSA 177
Cdd:cd03225 90 GPTVEEEVAFGLEN-----LGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAG 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 500071467 178 LDPEMVGEVLDTMRGLAAEGMTMMIVTHEMGFARQVADRVVFMDRGQ 224
Cdd:cd03225 165 LDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
13-228 |
2.70e-66 |
|
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: 205.01 E-value: 2.70e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 13 ISVAGVNKWYG----AFQVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIELgqsenaaQAVRR 88
Cdd:cd03293 1 LEVRNVSKTYGggggAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPV-------TGPGP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 89 EVGMVFQHFNLFPHLDLVQNcILAPMSVRGMSRRAAEALAVGLLERVRLGEHAHKYPSQLSGGQQQRAAIARALCMEPRV 168
Cdd:cd03293 74 DRGYVFQQDALLPWLTVLDN-VALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDV 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 500071467 169 MLFDEPTSALDP----EMVGEVLDTMRGlaaEGMTMMIVTHEMGFARQVADRVVFMDR--GQIVEQ 228
Cdd:cd03293 153 LLLDEPFSALDAltreQLQEELLDIWRE---TGKTVLLVTHDIDEAVFLADRVVVLSArpGRIVAE 215
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
10-238 |
3.45e-65 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 210.92 E-value: 3.45e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 10 APIISVAGVNKWY--GAFQVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQ---EGSIVVDGIELGQSENAAQ 84
Cdd:COG1123 2 TPLLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 85 AvrREVGMVFQHF--NLFPHLdlVQNCILAPMSVRGMSRRAAEALAVGLLERVRLGEHAHKYPSQLSGGQQQRAAIARAL 162
Cdd:COG1123 82 G--RRIGMVFQDPmtQLNPVT--VGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMAL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 500071467 163 CMEPRVMLFDEPTSALDPEMVGEVLDTMRGLAAE-GMTMMIVTHEMGFARQVADRVVFMDRGQIVEQAPPAAFFGAP 238
Cdd:COG1123 158 ALDPDLLIADEPTTALDVTTQAEILDLLRELQRErGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAP 234
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
12-240 |
4.98e-65 |
|
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: 204.90 E-value: 4.98e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 12 IISVAGVNKWY----GAFQVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQ---EGSIVVDGIELGQ-SENAA 83
Cdd:COG0444 1 LLEVRNLKVYFptrrGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPgitSGEILFDGEDLLKlSEKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 84 QAVR-REVGMVFQH----FN-LFPhldlVQNCILAPMSV-RGMSRRAAEALAVGLLERVRL---GEHAHKYPSQLSGGQQ 153
Cdd:COG0444 81 RKIRgREIQMIFQDpmtsLNpVMT----VGDQIAEPLRIhGGLSKAEARERAIELLERVGLpdpERRLDRYPHELSGGMR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 154 QRAAIARALCMEPRVMLFDEPTSALDPEMVGEVLDTMRGLAAE-GMTMMIVTHEMGFARQVADRVVFMDRGQIVEQAPPA 232
Cdd:COG0444 157 QRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRElGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGPVE 236
|
....*...
gi 500071467 233 AFFGAPVH 240
Cdd:COG0444 237 ELFENPRH 244
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
13-238 |
1.22e-63 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 202.23 E-value: 1.22e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 13 ISVAGVNKWYGAFQVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIELgqseNAAQAVRREVGM 92
Cdd:COG3839 4 LELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDV----TDLPPKDRNIAM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 93 VFQHFNLFPHLDLVQNcILAPMSVRGMSRRAAEALAVGLLERVRLGEHAHKYPSQLSGGQQQRAAIARALCMEPRVMLFD 172
Cdd:COG3839 80 VFQSYALYPHMTVYEN-IAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFLLD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 173 EPTSALDP----EMVGEVLDTMRGLaaeGMTMMIVTHEmgfarQV-----ADRVVFMDRGQIVEQAPP------------ 231
Cdd:COG3839 159 EPLSNLDAklrvEMRAEIKRLHRRL---GTTTIYVTHD-----QVeamtlADRIAVMNDGRIQQVGTPeelydrpanlfv 230
|
....*..
gi 500071467 232 AAFFGAP 238
Cdd:COG3839 231 AGFIGSP 237
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
6-233 |
1.49e-63 |
|
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: 198.43 E-value: 1.49e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 6 ASPAAPIISVAGVNKWY----GAFQVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIELGQ-SE 80
Cdd:COG4181 2 SSSSAPIIELRGLTKTVgtgaGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFAlDE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 81 NAAQAVRRE-VGMVFQHFNLFPHLDLVQNCILaPMSVRGmsRRAAEALAVGLLERVRLGEHAHKYPSQLSGGQQQRAAIA 159
Cdd:COG4181 82 DARARLRARhVGFVFQSFQLLPTLTALENVML-PLELAG--RRDARARARALLERVGLGHRLDHYPAQLSGGEQQRVALA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 500071467 160 RALCMEPRVMLFDEPTSALDPEMVGEVLDTMRGLAAE-GMTMMIVTHEMGFARQvADRVVFMDRGQIVEQAPPAA 233
Cdd:COG4181 159 RAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRErGTTLVLVTHDPALAAR-CDRVLRLRAGRLVEDTAATA 232
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
13-239 |
3.64e-61 |
|
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: 192.07 E-value: 3.64e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 13 ISVAGVNKWYGAFQVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIELgqseNAAQAVRREVGM 92
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDI----TNLPPHKRPVNT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 93 VFQHFNLFPHLDLVQNcILAPMSVRGMSRRAAEALAVGLLERVRLGEHAHKYPSQLSGGQQQRAAIARALCMEPRVMLFD 172
Cdd:cd03300 77 VFQNYALFPHLTVFEN-IAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLD 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 500071467 173 EPTSALDPEMVGEVLDTMRGLAAE-GMTMMIVTHEMGFARQVADRVVFMDRGQIVEQAPPAAFFGAPV 239
Cdd:cd03300 156 EPLGALDLKLRKDMQLELKRLQKElGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPA 223
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
30-246 |
2.24e-60 |
|
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: 191.32 E-value: 2.24e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 30 DVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIELGQ-SENAAQAVRRE-VGMVFQHFNLFPHLDLVQ 107
Cdd:cd03294 42 DVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAmSRKELRELRRKkISMVFQSFALLPHRTVLE 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 108 NcILAPMSVRGMSRRAAEALAVGLLERVRLGEHAHKYPSQLSGGQQQRAAIARALCMEPRVMLFDEPTSALDPEMVGEVL 187
Cdd:cd03294 122 N-VAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQ 200
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 188 DTMRGLAAE-GMTMMIVTHEMGFARQVADRVVFMDRGQIVEQAPPAAFFGAPVHERTRRF 246
Cdd:cd03294 201 DELLRLQAElQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDYVREF 260
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
13-225 |
4.05e-59 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 186.18 E-value: 4.05e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 13 ISVAGVNKWYGAFQVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIELgqSENAAQAVRREVGM 92
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPL--SAMPPPEWRRQVAY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 93 VFQHFNLFPhlDLVQNCILAPMSVRGmsRRAAEALAVGLLERVRLGEHAHKYP-SQLSGGQQQRAAIARALCMEPRVMLF 171
Cdd:COG4619 79 VPQEPALWG--GTVRDNLPFPFQLRE--RKFDRERALELLERLGLPPDILDKPvERLSGGERQRLALIRALLLQPDVLLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 500071467 172 DEPTSALDPEMVGEVLDTMRGLAAE-GMTMMIVTHEMGFARQVADRVVFMDRGQI 225
Cdd:COG4619 155 DEPTSALDPENTRRVEELLREYLAEeGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
13-249 |
4.32e-59 |
|
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: 187.12 E-value: 4.32e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 13 ISVAGVNKWYGA-FQVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIELgqSENAAQAVRREVG 91
Cdd:cd03295 1 IEFENVTKRYGGgKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDI--REQDPVELRRKIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 92 MVFQHFNLFPHLDLVQNCILAPmSVRGMSRRAAEALAVGLLERVRL--GEHAHKYPSQLSGGQQQRAAIARALCMEPRVM 169
Cdd:cd03295 79 YVIQQIGLFPHMTVEENIALVP-KLLKWPKEKIRERADELLALVGLdpAEFADRYPHELSGGQQQRVGVARALAADPPLL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 170 LFDEPTSALDPEMVGEVLDTMRGLAAE-GMTMMIVTHEMGFARQVADRVVFMDRGQIVEQAPPAAFFGAPVHERTRRFLS 248
Cdd:cd03295 158 LMDEPFGALDPITRDQLQEEFKRLQQElGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDFVAEFVG 237
|
.
gi 500071467 249 Q 249
Cdd:cd03295 238 A 238
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
15-226 |
8.92e-59 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 191.08 E-value: 8.92e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 15 VAGVNkwygafqvltDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIELGQ-SENAAQAVRRE-VGM 92
Cdd:COG4175 40 TVGVN----------DASFDVEEGEIFVIMGLSGSGKSTLVRCLNRLIEPTAGEVLIDGEDITKlSKKELRELRRKkMSM 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 93 VFQHFNLFPHLDLVQNCILaPMSVRGMSRRAAEALAVGLLERVRLGEHAHKYPSQLSGGQQQRAAIARALCMEPRVMLFD 172
Cdd:COG4175 110 VFQHFALLPHRTVLENVAF-GLEIQGVPKAERRERAREALELVGLAGWEDSYPDELSGGMQQRVGLARALATDPDILLMD 188
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 500071467 173 EPTSALDP----EMVGEVLDtmrgLAAE-GMTMMIVTHEMGFARQVADRVVFMDRGQIV 226
Cdd:COG4175 189 EAFSALDPlirrEMQDELLE----LQAKlKKTIVFITHDLDEALRLGDRIAIMKDGRIV 243
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
13-233 |
1.08e-58 |
|
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: 186.10 E-value: 1.08e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 13 ISVAGVNKWYGAFQVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIELGQsENAAQAVRREVGM 92
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITG-LPPHEIARLGIGR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 93 VFQHFNLFPHLDLVQNCILAPMSVRG---------MSRRAAEALAVGLLERVRLGEHAHKYPSQLSGGQQQRAAIARALC 163
Cdd:cd03219 80 TFQIPRLFPELTVLENVMVAAQARTGsglllararREEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 164 MEPRVMLFDEPTSALDPEMVGEVLDTMRGLAAEGMTMMIVTHEMGFARQVADRVVFMDRGQIVEQAPPAA 233
Cdd:cd03219 160 TDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDE 229
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
8-245 |
1.33e-58 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 186.06 E-value: 1.33e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 8 PAAPIISVAGVNKWYGAFQVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIELGQsenaaqaVR 87
Cdd:COG1121 2 MMMPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRR-------AR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 88 REVGMVFQHFNL---FPH--LDLVQNCILAPMSVRGMSRRAAEALAVGLLERVRLGEHAHKYPSQLSGGQQQRAAIARAL 162
Cdd:COG1121 75 RRIGYVPQRAEVdwdFPItvRDVVLMGRYGRRGLFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARAL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 163 CMEPRVMLFDEPTSALDPEMVGEVLDTMRGLAAEGMTMMIVTHEMGFARQVADRVVFMDRGQIVEqAPPAAFFGAPVHER 242
Cdd:COG1121 155 AQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLLNRGLVAH-GPPEEVLTPENLSR 233
|
...
gi 500071467 243 TRR 245
Cdd:COG1121 234 AYG 236
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
9-233 |
7.00e-58 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 184.47 E-value: 7.00e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 9 AAPIISVAGVNKWYGAFQVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIELgQSENAAQAVRR 88
Cdd:COG0411 1 SDPLLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDI-TGLPPHRIARL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 89 EVGMVFQHFNLFPHLDLVQNCILAPMSVRGMS--------------RRAAEALAVGLLERVRLGEHAHKYPSQLSGGQQQ 154
Cdd:COG0411 80 GIARTFQNPRLFPELTVLENVLVAAHARLGRGllaallrlprarreEREARERAEELLERVGLADRADEPAGNLSYGQQR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 155 RAAIARALCMEPRVMLFDEPTSALDPEMVGEVLDTMRGLAAE-GMTMMIVTHEMGFARQVADRVVFMDRGQIVEQAPPAA 233
Cdd:COG0411 160 RLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDErGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGTPAE 239
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
17-247 |
1.47e-57 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 185.29 E-value: 1.47e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 17 GVNKWY-GAFQVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIELgQSENAAQaVRREVGMVFQ 95
Cdd:COG1125 6 NVTKRYpDGTVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDI-RDLDPVE-LRRRIGYVIQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 96 HFNLFPHLDLVQNCILAPMsVRGMSRRAAEALAVGLLERVRL--GEHAHKYPSQLSGGQQQRAAIARALCMEPRVMLFDE 173
Cdd:COG1125 84 QIGLFPHMTVAENIATVPR-LLGWDKERIRARVDELLELVGLdpEEYRDRYPHELSGGQQQRVGVARALAADPPILLMDE 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 500071467 174 PTSALDPeMVGEVL-DTMRGLAAE-GMTMMIVTHEMGFARQVADRVVFMDRGQIVEQAPPAAFFGAPVHERTRRFL 247
Cdd:COG1125 163 PFGALDP-ITREQLqDELLRLQRElGKTIVFVTHDIDEALKLGDRIAVMREGRIVQYDTPEEILANPANDFVADFV 237
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
13-247 |
2.05e-57 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 182.92 E-value: 2.05e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 13 ISVAGVNKWYGAFQVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIELGQSEnaaqAVRREVGM 92
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVP----VQERNVGF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 93 VFQHFNLFPHLDLVQNcILAPMSVRGMSRRAAEAL----AVGLLERVRLGEHAHKYPSQLSGGQQQRAAIARALCMEPRV 168
Cdd:cd03296 79 VFQHYALFRHMTVFDN-VAFGLRVKPRSERPPEAEirakVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 169 MLFDEPTSALDPEMVGEVLDTMRGLAAE-GMTMMIVTHEMGFARQVADRVVFMDRGQIVEQAPPAAFFGAPVHERTRRFL 247
Cdd:cd03296 158 LLLDEPFGALDAKVRKELRRWLRRLHDElHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPASPFVYSFL 237
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
13-236 |
2.58e-57 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 183.40 E-value: 2.58e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 13 ISVAGVNKWY--GAFQVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIELGQSENAAQaVRREV 90
Cdd:TIGR04520 1 IEVENVSFSYpeSEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLDEENLWE-IRKKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 91 GMVFQHfnlfPhlDlvqNCILAPmSV----------RG-----MSRRAAEALavgllERVRLGEHAHKYPSQLSGGQQQR 155
Cdd:TIGR04520 80 GMVFQN----P--D---NQFVGA-TVeddvafglenLGvpreeMRKRVDEAL-----KLVGMEDFRDREPHLLSGGQKQR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 156 AAIARALCMEPRVMLFDEPTSALDPEMVGEVLDTMRGLAAE-GMTMMIVTHEMGFARQvADRVVFMDRGQIVEQAPPAAF 234
Cdd:TIGR04520 145 VAIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEeGITVISITHDMEEAVL-ADRVIVMNKGKIVAEGTPREI 223
|
..
gi 500071467 235 FG 236
Cdd:TIGR04520 224 FS 225
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
23-247 |
5.53e-57 |
|
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: 189.90 E-value: 5.53e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 23 GAFQVLTDVSLSVARGEKVVICGPSGSGKS----TLIRCLNQLEQHQEGSIVVDGIEL-GQSENAAQAVR-REVGMVFQH 96
Cdd:COG4172 21 GTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLlGLSERELRRIRgNRIAMIFQE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 97 fnlfphldlvqncilaPMSV------------------RGMSRRAAEALAVGLLERVRLGEHAHK---YPSQLSGGQQQR 155
Cdd:COG4172 101 ----------------PMTSlnplhtigkqiaevlrlhRGLSGAAARARALELLERVGIPDPERRldaYPHQLSGGQRQR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 156 AAIARALCMEPRVMLFDEPTSALDPEMVGEVLDTMRGLAAE-GMTMMIVTHEMGFARQVADRVVFMDRGQIVEQAPPAAF 234
Cdd:COG4172 165 VMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRElGMALLLITHDLGVVRRFADRVAVMRQGEIVEQGPTAEL 244
|
250
....*....|...
gi 500071467 235 FGAPVHERTRRFL 247
Cdd:COG4172 245 FAAPQHPYTRKLL 257
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
32-247 |
3.16e-56 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 179.57 E-value: 3.16e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 32 SLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIELGQSENAaqavRREVGMVFQHFNLFPHLDLVQNCIL 111
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPA----ERPVSMLFQENNLFPHLTVAQNIGL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 112 A--PmsvrGMSRRAAEALAV-GLLERVRLGEHAHKYPSQLSGGQQQRAAIARALCMEPRVMLFDEPTSALDPEMVGEVLD 188
Cdd:COG3840 95 GlrP----GLKLTAEQRAQVeQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDPALRQEMLD 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 189 TMRGLAAE-GMTMMIVTHEMGFARQVADRVVFMDRGQIVEQAPPAAFFGAPVHERTRRFL 247
Cdd:COG3840 171 LVDELCRErGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPPALAAYL 230
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
2-248 |
7.60e-56 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 186.81 E-value: 7.60e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 2 PNPDASPAAPIISVAGVNKWY-----------GAFQVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLeQHQEGSIV 70
Cdd:COG4172 265 PRPVPPDAPPLLEARDLKVWFpikrglfrrtvGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRL-IPSEGEIR 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 71 VDGIEL-GQSENAAQAVRREVGMVFQhfNLFPHLD---LVQNCILAPMSV--RGMSRRAAEALAVGLLERVRL-GEHAHK 143
Cdd:COG4172 344 FDGQDLdGLSRRALRPLRRRMQVVFQ--DPFGSLSprmTVGQIIAEGLRVhgPGLSAAERRARVAEALEEVGLdPAARHR 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 144 YPSQLSGGQQQRAAIARALCMEPRVMLFDEPTSALDPEMVGEVLDTMRGLAAE-GMTMMIVTHEMGFARQVADRVVFMDR 222
Cdd:COG4172 422 YPHEFSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREhGLAYLFISHDLAVVRALAHRVMVMKD 501
|
250 260
....*....|....*....|....*.
gi 500071467 223 GQIVEQAPPAAFFGAPVHERTRRFLS 248
Cdd:COG4172 502 GKVVEQGPTEQVFDAPQHPYTRALLA 527
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
12-232 |
1.30e-55 |
|
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: 178.70 E-value: 1.30e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 12 IISVAGVNKWYGAFQVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIELgqSENAAQAVRREVG 91
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDL--ASLSRRELARRIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 92 MVFQH----FNL----------FPHLDLvqnciLAPMSVRGMsRRAAEALavgllERVRLGEHAHKYPSQLSGGQQQRAA 157
Cdd:COG1120 79 YVPQEppapFGLtvrelvalgrYPHLGL-----FGRPSAEDR-EAVEEAL-----ERTGLEHLADRPVDELSGGERQRVL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 500071467 158 IARALCMEPRVMLFDEPTSALDPEMVGEVLDTMRGLAAE-GMTMMIVTHEMGFARQVADRVVFMDRGQIVEQAPPA 232
Cdd:COG1120 148 IARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARErGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPE 223
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
10-238 |
1.33e-55 |
|
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: 181.77 E-value: 1.33e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 10 APIISVAGVNKWYGAFQVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIELgqseNAAQAVRRE 89
Cdd:TIGR03265 2 SPYLSIDNIRKRFGAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDI----TRLPPQKRD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 90 VGMVFQHFNLFPHLDLVQNcILAPMSVRGMSRRAAEALAVGLLERVRLGEHAHKYPSQLSGGQQQRAAIARALCMEPRVM 169
Cdd:TIGR03265 78 YGIVFQSYALFPNLTVADN-IAYGLKNRGMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALATSPGLL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 500071467 170 LFDEPTSALDPEmVGEVLDT-MRGLAAE-GMTMMIVTHEMGFARQVADRVVFMDRGQIVEQAPPAAFFGAP 238
Cdd:TIGR03265 157 LLDEPLSALDAR-VREHLRTeIRQLQRRlGVTTIMVTHDQEEALSMADRIVVMNHGVIEQVGTPQEIYRHP 226
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
13-234 |
1.72e-55 |
|
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: 177.24 E-value: 1.72e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 13 ISVAGVNKWYGAFQVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIELGqSENAAQAVRREVGM 92
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDIT-GLPPHERARAGIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 93 VFQHFNLFPHLDLVQNcILAPMSVRGMSRRAAEalavglLERV-----RLGEHAHKYPSQLSGGQQQRAAIARALCMEPR 167
Cdd:cd03224 80 VPEGRRIFPELTVEEN-LLLGAYARRRAKRKAR------LERVyelfpRLKERRKQLAGTLSGGEQQMLAIARALMSRPK 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 500071467 168 VMLFDEPTSALDPEMVGEVLDTMRGLAAEGMTMMIVTHEMGFARQVADRVVFMDRGQIVEQAPPAAF 234
Cdd:cd03224 153 LLLLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAEL 219
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
6-250 |
2.99e-55 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 179.93 E-value: 2.99e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 6 ASPAAPIISVAGVNKWY----GAF-------QVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGI 74
Cdd:COG4608 1 AAMAEPLLEVRDLKKHFpvrgGLFgrtvgvvKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 75 ELGQ-SENAAQAVRREVGMVFQHfnlfPHLDL-----VQNCILAPMSVRGM-SRRAAEALAVGLLERVRLG-EHAHKYPS 146
Cdd:COG4608 81 DITGlSGRELRPLRRRMQMVFQD----PYASLnprmtVGDIIAEPLRIHGLaSKAERRERVAELLELVGLRpEHADRYPH 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 147 QLSGGQQQRAAIARALCMEPRVMLFDEPTSALDPEMVGEVLDTMRGLAAE-GMTMMIVTHEMGFARQVADRVVFMDRGQI 225
Cdd:COG4608 157 EFSGGQRQRIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDElGLTYLFISHDLSVVRHISDRVAVMYLGKI 236
|
250 260
....*....|....*....|....*
gi 500071467 226 VEQAPPAAFFGAPVHERTRRFLSQI 250
Cdd:COG4608 237 VEIAPRDELYARPLHPYTQALLSAV 261
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
13-234 |
2.02e-54 |
|
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: 175.43 E-value: 2.02e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 13 ISVAGVNKWYGAFQVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIELGQSENAAqavRREVGM 92
Cdd:COG4555 2 IEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREA---RRQIGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 93 VFQHFNLFPHLDLVQNcILAPMSVRGMSRRAAEALAVGLLERVRLGEHAHKYPSQLSGGQQQRAAIARALCMEPRVMLFD 172
Cdd:COG4555 79 LPDERGLYDRLTVREN-IRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLD 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 500071467 173 EPTSALDPEMVGEVLDTMRGLAAEGMTMMIVTHEMGFARQVADRVVFMDRGQIVEQAPPAAF 234
Cdd:COG4555 158 EPTNGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDEL 219
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
13-225 |
3.14e-54 |
|
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: 172.58 E-value: 3.14e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 13 ISVAGVNKWYGAFQVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIELGqseNAAQAVRREVGM 92
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIK---KEPEEVKRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 93 VFQHFNLFPHldlvqncilapMSVRgmsrraaEALavgllervrlgehahkypsQLSGGQQQRAAIARALCMEPRVMLFD 172
Cdd:cd03230 78 LPEEPSLYEN-----------LTVR-------ENL-------------------KLSGGMKQRLALAQALLHDPELLILD 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 500071467 173 EPTSALDPEMVGEVLDTMRGLAAEGMTMMIVTHEMGFARQVADRVVFMDRGQI 225
Cdd:cd03230 121 EPTSGLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
10-234 |
4.10e-54 |
|
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: 174.40 E-value: 4.10e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 10 APIISVAGVNKWYGAFQVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIELGQSEnAAQAVRRE 89
Cdd:COG0410 1 MPMLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLP-PHRIARLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 90 VGMVFQHFNLFPHLDLVQNCILAPMSVRGMSRRAAEalavglLERV-----RLGEHAHKYPSQLSGGQQQRAAIARALCM 164
Cdd:COG0410 80 IGYVPEGRRIFPSLTVEENLLLGAYARRDRAEVRAD------LERVyelfpRLKERRRQRAGTLSGGEQQMLAIGRALMS 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 165 EPRVMLFDEPTSALDPEMVGEVLDTMRGLAAEGMTMMIVTHEMGFARQVADRVVFMDRGQIVEQAPPAAF 234
Cdd:COG0410 154 RPKLLLLDEPSLGLAPLIVEEIFEIIRRLNREGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAEL 223
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
13-229 |
1.64e-53 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 176.43 E-value: 1.64e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 13 ISVAGVNKWYGAFQVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIELGQsenaAQAVRREVGM 92
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSR----LHARDRKVGF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 93 VFQHFNLFPHLDLVQNcILAPMSVrgMSRR------AAEALAVGLLERVRLGEHAHKYPSQLSGGQQQRAAIARALCMEP 166
Cdd:PRK10851 79 VFQHYALFRHMTVFDN-IAFGLTV--LPRRerpnaaAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 500071467 167 RVMLFDEPTSALDPEMVGEVLDTMRGLAAE-GMTMMIVTHEMGFARQVADRVVFMDRGQIvEQA 229
Cdd:PRK10851 156 QILLLDEPFGALDAQVRKELRRWLRQLHEElKFTSVFVTHDQEEAMEVADRVVVMSQGNI-EQA 218
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
24-235 |
1.65e-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: 171.48 E-value: 1.65e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 24 AFQVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIELGQSEN-AAQAVRREVGMVFQhfnlFPH 102
Cdd:TIGR04521 17 EKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKkKLKDLRKKVGLVFQ----FPE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 103 LDLVQNCIL-----APMSVrGMS-----RRAAEALA-VGLLErvrlgEHAHKYPSQLSGGQQQRAAIARALCMEPRVMLF 171
Cdd:TIGR04521 93 HQLFEETVYkdiafGPKNL-GLSeeeaeERVKEALElVGLDE-----EYLERSPFELSGGQMRRVAIAGVLAMEPEVLIL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 500071467 172 DEPTSALDPEMVGEVLDTMRGLAAE-GMTMMIVTHEMGFARQVADRVVFMDRGQIVEQAPPAAFF 235
Cdd:TIGR04521 167 DEPTAGLDPKGRKEILDLFKRLHKEkGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVF 231
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
13-227 |
3.92e-52 |
|
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: 168.59 E-value: 3.92e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 13 ISVAGVNKWYGAFQVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIELgqseNAAQAVRREVGM 92
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDV----TDLPPKDRDIAM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 93 VFQHFNLFPHLDLVQNcILAPMSVRGMSRRAAEALAVGLLERVRLGEHAHKYPSQLSGGQQQRAAIARALCMEPRVMLFD 172
Cdd:cd03301 77 VFQNYALYPHMTVYDN-IAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 500071467 173 EPTSALDP----EMVGEVLDTMRGLaaeGMTMMIVTHEMGFARQVADRVVFMDRGQIVE 227
Cdd:cd03301 156 EPLSNLDAklrvQMRAELKRLQQRL---GTTTIYVTHDQVEAMTMADRIAVMNDGQIQQ 211
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
14-224 |
1.73e-51 |
|
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: 164.73 E-value: 1.73e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 14 SVAGVNKWYGAFQVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIELGQSENaaQAVRREVGMV 93
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPL--EELRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 94 FQhfnlfphldlvqncilapmsvrgmsrraaealavgllervrlgehahkypsqLSGGQQQRAAIARALCMEPRVMLFDE 173
Cdd:cd00267 79 PQ----------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDE 106
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 500071467 174 PTSALDPEMVGEVLDTMRGLAAEGMTMMIVTHEMGFARQVADRVVFMDRGQ 224
Cdd:cd00267 107 PTSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
20-247 |
1.07e-50 |
|
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: 169.26 E-value: 1.07e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 20 KWYGAFQVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIELGQSENA--AQAVRREVGMVFQHF 97
Cdd:TIGR01186 1 KKTGGKKGVNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEPTAGQIFIDGENIMKQSPVelREVRRKKIGMVFQQF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 98 NLFPHLDLVQNCILAPmSVRGMSRRAAEALAVGLLERVRLGEHAHKYPSQLSGGQQQRAAIARALCMEPRVMLFDEPTSA 177
Cdd:TIGR01186 81 ALFPHMTILQNTSLGP-ELLGWPEQERKEKALELLKLVGLEEYEHRYPDELSGGMQQRVGLARALAAEPDILLMDEAFSA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 500071467 178 LDP----EMVGEVLDTMRGLaaeGMTMMIVTHEMGFARQVADRVVFMDRGQIVEQAPPAAFFGAPVHERTRRFL 247
Cdd:TIGR01186 160 LDPlirdSMQDELKKLQATL---QKTIVFITHDLDEAIRIGDRIVIMKAGEIVQVGTPDEILRNPANEYVEEFI 230
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
9-234 |
2.81e-50 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 171.35 E-value: 2.81e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 9 AAPIISVAGVNKWYGAFQVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIELgQSENAAQAVRR 88
Cdd:COG1129 1 AEPLLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPV-RFRSPRDAQAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 89 EVGMVFQHFNLFPHLDLVQNCILA--PMSVRGMSRRAAEALAVGLLERVRLGEHAHKYPSQLSGGQQQRAAIARALCMEP 166
Cdd:COG1129 80 GIAIIHQELNLVPNLSVAENIFLGrePRRGGLIDWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRDA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 500071467 167 RVMLFDEPTSALDPEMVGEVLDTMRGLAAEGMTMMIVTHEMGFARQVADRV-VFMDrGQIVEQAPPAAF 234
Cdd:COG1129 160 RVLILDEPTASLTEREVERLFRIIRRLKAQGVAIIYISHRLDEVFEIADRVtVLRD-GRLVGTGPVAEL 227
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
11-235 |
3.59e-50 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 165.57 E-value: 3.59e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 11 PIISVAGVNKWY--GAFQVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIELgqSENAAQAVRR 88
Cdd:PRK13635 4 EIIRVEHISFRYpdAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVL--SEETVWDVRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 89 EVGMVFQH-FNLFPHlDLVQNCILAPMSVRGMSR-----RAAEAlavglLERVRLGEHAHKYPSQLSGGQQQRAAIARAL 162
Cdd:PRK13635 82 QVGMVFQNpDNQFVG-ATVQDDVAFGLENIGVPReemveRVDQA-----LRQVGMEDFLNREPHRLSGGQKQRVAIAGVL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 500071467 163 CMEPRVMLFDEPTSALDPEMVGEVLDTMRGLAAEGM-TMMIVTHEMGFARQvADRVVFMDRGQIVEQAPPAAFF 235
Cdd:PRK13635 156 ALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGiTVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEIF 228
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
26-224 |
1.36e-49 |
|
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: 160.63 E-value: 1.36e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 26 QVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIELgqSENAAQAVRREVGMVFQHFNLFPhldl 105
Cdd:cd03228 16 PVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDL--RDLDLESLRKNIAYVPQDPFLFS---- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 106 vqncilapMSVRgmsrraaEALavgllervrlgehahkypsqLSGGQQQRAAIARALCMEPRVMLFDEPTSALDPEMVGE 185
Cdd:cd03228 90 --------GTIR-------ENI--------------------LSGGQRQRIAIARALLRDPPILILDEATSALDPETEAL 134
|
170 180 190
....*....|....*....|....*....|....*....
gi 500071467 186 VLDTMRGLaAEGMTMMIVTHEMGFARQvADRVVFMDRGQ 224
Cdd:cd03228 135 ILEALRAL-AKGKTVIVIAHRLSTIRD-ADRIIVLDDGR 171
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
11-250 |
4.03e-49 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 165.51 E-value: 4.03e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 11 PIISVAGVNKWYGAFQVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGielgQSENAAQAVRREV 90
Cdd:PRK09452 13 PLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDG----QDITHVPAENRHV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 91 GMVFQHFNLFPHLDLVQNCILA-PMSVRG---MSRRAAEALAVgllerVRLGEHAHKYPSQLSGGQQQRAAIARALCMEP 166
Cdd:PRK09452 89 NTVFQSYALFPHMTVFENVAFGlRMQKTPaaeITPRVMEALRM-----VQLEEFAQRKPHQLSGGQQQRVAIARAVVNKP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 167 RVMLFDEPTSALD----PEMVGEVLDTMRGLaaeGMTMMIVTHEMGFARQVADRVVFMDRGQIVEQAPPAAFFGAPVHER 242
Cdd:PRK09452 164 KVLLLDESLSALDyklrKQMQNELKALQRKL---GITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNLF 240
|
....*...
gi 500071467 243 TRRFLSQI 250
Cdd:PRK09452 241 VARFIGEI 248
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
9-245 |
9.62e-49 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 167.51 E-value: 9.62e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 9 AAPIISVAGVNKWYGAFQVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIELgQSENAAQAVRR 88
Cdd:COG3845 2 MPPALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPV-RIRSPRDAIAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 89 EVGMVFQHFNLFPHLDLVQNCILA--PMSVRGMSRRAAEALAVGLLERVRLGEHAHKYPSQLSGGQQQRAAIARALCMEP 166
Cdd:COG3845 81 GIGMVHQHFMLVPNLTVAENIVLGlePTKGGRLDRKAARARIRELSERYGLDVDPDAKVEDLSVGEQQRVEILKALYRGA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 167 RVMLFDEPTSALDPEMVGEVLDTMRGLAAEGMTMMIVTHEMGFARQVADRVVFMDRGQIVEQAPPAAF---------FGA 237
Cdd:COG3845 161 RILILDEPTAVLTPQEADELFEILRRLAAEGKSIIFITHKLREVMAIADRVTVLRRGKVVGTVDTAETseeelaelmVGR 240
|
....*...
gi 500071467 238 PVHERTRR 245
Cdd:COG3845 241 EVLLRVEK 248
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
22-228 |
1.19e-48 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 158.37 E-value: 1.19e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 22 YGAFQVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIELGQSENAAQAvrREVGMVFQhfnlfp 101
Cdd:cd03214 9 YGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELA--RKIAYVPQ------ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 102 hldlvqncilapmsvrgmsrraaealavgLLERVRLGEHAHKYPSQLSGGQQQRAAIARALCMEPRVMLFDEPTSALDPE 181
Cdd:cd03214 81 -----------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIA 131
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 500071467 182 MVGEVLDTMRGLAAE-GMTMMIVTHEMGFARQVADRVVFMDRGQIVEQ 228
Cdd:cd03214 132 HQIELLELLRRLARErGKTVVMVLHDLNLAARYADRVILLKDGRIVAQ 179
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
28-176 |
1.31e-48 |
|
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: 157.42 E-value: 1.31e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 28 LTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIELGQSEnaAQAVRREVGMVFQHFNLFPHLDLVQ 107
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDE--RKSLRKEIGYVFQDPQLFPRLTVRE 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 500071467 108 NcILAPMSVRGMSRRAAEALAVGLLERVRLG----EHAHKYPSQLSGGQQQRAAIARALCMEPRVMLFDEPTS 176
Cdd:pfam00005 79 N-LRLGLLLKGLSKREKDARAEEALEKLGLGdladRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
12-224 |
1.43e-48 |
|
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: 159.34 E-value: 1.43e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 12 IISVAGVNKWY-GAFQVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIELGQ-SENAAQAVRRE 89
Cdd:TIGR02673 1 MIEFHNVSKAYpGGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRlRGRQLPLLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 90 VGMVFQHFNLFPHLDLVQNCILaPMSVRGMSRRAAEALAVGLLERVRLGEHAHKYPSQLSGGQQQRAAIARALCMEPRVM 169
Cdd:TIGR02673 81 IGVVFQDFRLLPDRTVYENVAL-PLEVRGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPPLL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 500071467 170 LFDEPTSALDPEMVGEVLDTMRGLAAEGMTMMIVTHEMGFARQVADRVVFMDRGQ 224
Cdd:TIGR02673 160 LADEPTGNLDPDLSERILDLLKRLNKRGTTVIVATHDLSLVDRVAHRVIILDDGR 214
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
30-228 |
2.63e-48 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 158.81 E-value: 2.63e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 30 DVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIELGQSENAaqavRREVGMVFQHFNLFPHLDLVQNC 109
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPA----DRPVSMLFQENNLFAHLTVEQNV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 110 ILApmSVRGMSRRAAEALAV-GLLERVRLGEHAHKYPSQLSGGQQQRAAIARALCMEPRVMLFDEPTSALDPEMVGEVLD 188
Cdd:cd03298 92 GLG--LSPGLKLTAEDRQAIeVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLD 169
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 500071467 189 TMRGLAAE-GMTMMIVTHEMGFARQVADRVVFMDRGQIVEQ 228
Cdd:cd03298 170 LVLDLHAEtKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQ 210
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
22-223 |
1.13e-47 |
|
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: 156.92 E-value: 1.13e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 22 YGAFQVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIELGQSenaaqavRREVGMVFQHFNL-- 99
Cdd:cd03235 9 YGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKE-------RKRIGYVPQRRSIdr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 100 -FPH--LDLVQNCILAPMSVRGMSRRAAEALAVGLLERVRLGEHAHKYPSQLSGGQQQRAAIARALCMEPRVMLFDEPTS 176
Cdd:cd03235 82 dFPIsvRDVVLMGLYGHKGLFRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFA 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 500071467 177 ALDPEMVGEVLDTMRGLAAEGMTMMIVTHEMGFARQVADRVVFMDRG 223
Cdd:cd03235 162 GVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRVLLLNRT 208
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
22-238 |
4.84e-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: 159.50 E-value: 4.84e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 22 YGAFQVltDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGiELGQSENAAQAV---RREVGMVFQHFN 98
Cdd:COG4148 11 RGGFTL--DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGG-EVLQDSARGIFLpphRRRIGYVFQEAR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 99 LFPHLdlvqncilapmSVR-----GMSRRAAEALAVGLLERVRL---GEHAHKYPSQLSGGQQQRAAIARALCMEPRVML 170
Cdd:COG4148 88 LFPHL-----------SVRgnllyGRKRAPRAERRISFDEVVELlgiGHLLDRRPATLSGGERQRVAIGRALLSSPRLLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 500071467 171 FDEPTSALDPEMVGEVLDTMRGLAAE-GMTMMIVTHEMGFARQVADRVVFMDRGQIVEQAPPAAFFGAP 238
Cdd:COG4148 157 MDEPLAALDLARKAEILPYLERLRDElDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRP 225
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
27-233 |
4.91e-47 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 165.78 E-value: 4.91e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 27 VLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIELGQSENAAqaVRREVGMVFQHFNLF------ 100
Cdd:COG2274 490 VLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPAS--LRRQIGVVLQDVFLFsgtire 567
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 101 ------PHLDLVQncIlapmsvrgmsRRAAEAlaVGLLERVR---------LGEHAhkypSQLSGGQQQRAAIARALCME 165
Cdd:COG2274 568 nitlgdPDATDEE--I----------IEAARL--AGLHDFIEalpmgydtvVGEGG----SNLSGGQRQRLAIARALLRN 629
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 500071467 166 PRVMLFDEPTSALDPEMVGEVLDTMRGLAAeGMTMMIVTHEMGFARQvADRVVFMDRGQIVEQAPPAA 233
Cdd:COG2274 630 PRILILDEATSALDAETEAIILENLRRLLK-GRTVIIIAHRLSTIRL-ADRIIVLDKGRIVEDGTHEE 695
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
43-250 |
1.25e-46 |
|
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: 157.66 E-value: 1.25e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 43 ICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIELGQsenaAQAVRREVGMVFQHFNLFPHLDLVQNcILAPMSVRGMSRR 122
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTN----VPPHLRHINMVFQSYALFPHMTVEEN-VAFGLKMRKVPRA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 123 AAEALAVGLLERVRLGEHAHKYPSQLSGGQQQRAAIARALCMEPRVMLFDEPTSALD----PEMVGEVLDTMRGLaaeGM 198
Cdd:TIGR01187 76 EIKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDkklrDQMQLELKTIQEQL---GI 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 500071467 199 TMMIVTHEMGFARQVADRVVFMDRGQIVEQAPPAAFFGAPVHERTRRFLSQI 250
Cdd:TIGR01187 153 TFVFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFVARFIGEI 204
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
18-238 |
1.57e-46 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 158.34 E-value: 1.57e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 18 VNKWYGAFQVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIELgqSENAAQavRREVGMVFQHF 97
Cdd:PRK11432 12 ITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDV--THRSIQ--QRDICMVFQSY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 98 NLFPHLDLVQNcILAPMSVRGMSR-----RAAEALAVgllerVRLGEHAHKYPSQLSGGQQQRAAIARALCMEPRVMLFD 172
Cdd:PRK11432 88 ALFPHMSLGEN-VGYGLKMLGVPKeerkqRVKEALEL-----VDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 500071467 173 EPTSALDPEMVGEVLDTMRGLAAE-GMTMMIVTHEMGFARQVADRVVFMDRGQIVEQAPPAAFFGAP 238
Cdd:PRK11432 162 EPLSNLDANLRRSMREKIRELQQQfNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQP 228
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
18-225 |
9.54e-46 |
|
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: 152.18 E-value: 9.54e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 18 VNKWYGA-FQVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIEL-GQSENAAQAVRREVGMVFQ 95
Cdd:cd03292 6 VTKTYPNgTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVsDLRGRAIPYLRRKIGVVFQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 96 HFNLFPHLDLVQNCILApMSVRGMSRRAAEALAVGLLERVRLGEHAHKYPSQLSGGQQQRAAIARALCMEPRVMLFDEPT 175
Cdd:cd03292 86 DFRLLPDRNVYENVAFA-LEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPT 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 500071467 176 SALDPEMVGEVLDTMRGLAAEGMTMMIVTHEMGFARQVADRVVFMDRGQI 225
Cdd:cd03292 165 GNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
13-251 |
3.04e-45 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 152.30 E-value: 3.04e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 13 ISVAGVNKWYGAFQVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQL-----EQHQEGSIVVDGIELGQSENAAQAVR 87
Cdd:PRK14267 5 IETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLlelneEARVEGEVRLFGRNIYSPDVDPIEVR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 88 REVGMVFQHFNLFPHLDLVQNCILApMSVRGMSRRAAEalavgLLERVR-----------LGEHAHKYPSQLSGGQQQRA 156
Cdd:PRK14267 85 REVGMVFQYPNPFPHLTIYDNVAIG-VKLNGLVKSKKE-----LDERVEwalkkaalwdeVKDRLNDYPSNLSGGQRQRL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 157 AIARALCMEPRVMLFDEPTSALDPEMVGEVLDTMRGLAAEgMTMMIVTHEMGFARQVADRVVFMDRGQIVEQAPPAAFFG 236
Cdd:PRK14267 159 VIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKE-YTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFE 237
|
250
....*....|....*
gi 500071467 237 APVHERTRRFLSQIL 251
Cdd:PRK14267 238 NPEHELTEKYVTGAL 252
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
13-226 |
4.25e-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: 148.73 E-value: 4.25e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 13 ISVAGVNKWYGAFQVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIELgQSENAAQAVRREVGM 92
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEV-SFASPRDARRAGIAM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 93 VFQhfnlfphldlvqncilapmsvrgmsrraaealavgllervrlgehahkypsqLSGGQQQRAAIARALCMEPRVMLFD 172
Cdd:cd03216 80 VYQ----------------------------------------------------LSVGERQMVEIARALARNARLLILD 107
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 500071467 173 EPTSALDPEMVGEVLDTMRGLAAEGMTMMIVTHEMGFARQVADRVVFMDRGQIV 226
Cdd:cd03216 108 EPTAALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
13-252 |
1.10e-44 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 150.45 E-value: 1.10e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 13 ISVAGVNKWYGAFQVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQL-----EQHQEGSIVVDGIELGQSEnaAQAVR 87
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQDIFKMD--VIELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 88 REVGMVFQHFNLFPHLDLVQNCILAPM------SVRGMSRRAAEAL-AVGLLERV--RLGEHAHKypsqLSGGQQQRAAI 158
Cdd:PRK14247 82 RRVQMVFQIPNPIPNLSIFENVALGLKlnrlvkSKKELQERVRWALeKAQLWDEVkdRLDAPAGK----LSGGQQQRLCI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 159 ARALCMEPRVMLFDEPTSALDPEMVGEVLDTMRGLAAEgMTMMIVTHEMGFARQVADRVVFMDRGQIVEQAPPAAFFGAP 238
Cdd:PRK14247 158 ARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKD-MTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTNP 236
|
250
....*....|....
gi 500071467 239 VHERTRRFLSQILH 252
Cdd:PRK14247 237 RHELTEKYVTGRLY 250
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
17-220 |
1.23e-44 |
|
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: 148.92 E-value: 1.23e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 17 GVNKWYGAFQVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIELGQSENA-AQAVRRE-VGMVF 94
Cdd:TIGR03608 3 NISKKFGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLNSKkASKFRREkLGYLF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 95 QHFNLFPHLDLVQNCILAPMSVRGmSRRAAEALAVGLLERVRLGEHAHKYPSQLSGGQQQRAAIARALCMEPRVMLFDEP 174
Cdd:TIGR03608 83 QNFALIENETVEENLDLGLKYKKL-SKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLILADEP 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 500071467 175 TSALDPEMVGEVLDTMRGLAAEGMTMMIVTHEMGFARQvADRVVFM 220
Cdd:TIGR03608 162 TGSLDPKNRDEVLDLLLELNDEGKTIIIVTHDPEVAKQ-ADRVIEL 206
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-232 |
1.27e-44 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 157.62 E-value: 1.27e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 2 PNPDASPAAPIISVAGVN-KWYGA-FQVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIELgqS 79
Cdd:COG4987 323 AEPAPAPGGPSLELEDVSfRYPGAgRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDL--R 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 80 ENAAQAVRREVGMVFQHFNLFPhldlvqncilapMSVRGMSRRA------AEALAVglLERVRLGEHAHKYP-------- 145
Cdd:COG4987 401 DLDEDDLRRRIAVVPQRPHLFD------------TTLRENLRLArpdatdEELWAA--LERVGLGDWLAALPdgldtwlg 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 146 ---SQLSGGQQQRAAIARALCMEPRVMLFDEPTSALDPEMVGEVLDTMRGlAAEGMTMMIVTHEMGFARQvADRVVFMDR 222
Cdd:COG4987 467 eggRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLE-ALAGRTVLLITHRLAGLER-MDRILVLED 544
|
250
....*....|
gi 500071467 223 GQIVEQAPPA 232
Cdd:COG4987 545 GRIVEQGTHE 554
|
|
| ABC_ATP_DarD |
NF038007 |
darobactin export ABC transporter ATP-binding protein; |
26-225 |
2.41e-44 |
|
darobactin export ABC transporter ATP-binding protein;
Pssm-ID: 411600 [Multi-domain] Cd Length: 218 Bit Score: 148.71 E-value: 2.41e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 26 QVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIE-LGQSENAAQAVRRE-VGMVFQHFNLFPHL 103
Cdd:NF038007 19 KVLNHLNFSVEKGDFVSIMGPSGSGKSTLLNIIGMFDSLDSGSLTLAGKEvTNLSYSQKIILRRElIGYIFQSFNLIPHL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 104 DLVQNCILaPMSVRGMSRRAAEALAVGLLERVRLGEHAHKYPSQLSGGQQQRAAIARALCMEPRVMLFDEPTSALDPEMV 183
Cdd:NF038007 99 SIFDNVAL-PLKYRGVAKKERIERVNQVLNLFGIDNRRNHKPMQLSGGQQQRVAIARAMVSNPALLLADEPTGNLDSKNA 177
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 500071467 184 GEVLDTMRGLAAEGMTMMIVTHEMGfARQVADRVVFMDRGQI 225
Cdd:NF038007 178 RAVLQQLKYINQKGTTIIMVTHSDE-ASTYGNRIINMKDGKL 218
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
11-248 |
2.52e-44 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 149.54 E-value: 2.52e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 11 PIISVAGVNKWYGAFQVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQL-----EQHQEGSIVVDGIELGQSENAAQA 85
Cdd:PRK14239 4 PILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndlnpEVTITGSIVYNGHNIYSPRTDTVD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 86 VRREVGMVFQHFNLFPhLDLVQNCILApMSVRGMSRRAAEALAV-------GLLERVRlgEHAHKYPSQLSGGQQQRAAI 158
Cdd:PRK14239 84 LRKEIGMVFQQPNPFP-MSIYENVVYG-LRLKGIKDKQVLDEAVekslkgaSIWDEVK--DRLHDSALGLSGGQQQRVCI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 159 ARALCMEPRVMLFDEPTSALDPEMVGEVLDTMRGLaAEGMTMMIVTHEMGFARQVADRVVFMDRGQIVEQAPPAAFFGAP 238
Cdd:PRK14239 160 ARVLATSPKIILLDEPTSALDPISAGKIEETLLGL-KDDYTMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQMFMNP 238
|
250
....*....|
gi 500071467 239 VHERTRRFLS 248
Cdd:PRK14239 239 KHKETEDYIS 248
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
13-248 |
5.25e-44 |
|
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: 148.25 E-value: 5.25e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 13 ISVAGVNKWYGAFQvLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIELgqseNAAQAVRREVGM 92
Cdd:cd03299 1 LKVENLSKDWKEFK-LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDI----TNLPPEKRDISY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 93 VFQHFNLFPHLDlVQNCILAPMSVRGMSRRAAEALAVGLLERVRLGEHAHKYPSQLSGGQQQRAAIARALCMEPRVMLFD 172
Cdd:cd03299 76 VPQNYALFPHMT-VYKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLD 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 500071467 173 EPTSALDPEMVGEVLDTMRGLAAE-GMTMMIVTHEMGFARQVADRVVFMDRGQIVEQAPPAAFFGAPVHERTRRFLS 248
Cdd:cd03299 155 EPFSALDVRTKEKLREELKKIRKEfGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPKNEFVAEFLG 231
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
20-226 |
9.31e-44 |
|
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: 149.85 E-value: 9.31e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 20 KWYGAFQVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIELgqSENAAQaVRREVGMVFQHFNL 99
Cdd:TIGR01188 1 KVYGDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDV--VREPRK-VRRSIGIVPQYASV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 100 FPHLDLVQNCILAPmSVRGMSRRAAEALAVGLLERVRLGEHAHKYPSQLSGGQQQRAAIARALCMEPRVMLFDEPTSALD 179
Cdd:TIGR01188 78 DEDLTGRENLEMMG-RLYGLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLD 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 500071467 180 PEMVGEVLDTMRGLAAEGMTMMIVTHEMGFARQVADRVVFMDRGQIV 226
Cdd:TIGR01188 157 PRTRRAIWDYIRALKEEGVTILLTTHYMEEADKLCDRIAIIDHGRII 203
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
26-231 |
1.55e-43 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 155.65 E-value: 1.55e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 26 QVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIELGQSENAAQA-VRRE-VGMVFQHFNLFPHL 103
Cdd:PRK10535 22 EVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAqLRREhFGFIFQRYHLLSHL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 104 DLVQNcILAPMSVRGMSRRAAEALAVGLLERVRLGEHAHKYPSQLSGGQQQRAAIARALCMEPRVMLFDEPTSALDPEMV 183
Cdd:PRK10535 102 TAAQN-VEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDSHSG 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 500071467 184 GEVLDTMRGLAAEGMTMMIVTHEMGFARQvADRVVFMDRGQIVEQAPP 231
Cdd:PRK10535 181 EEVMAILHQLRDRGHTVIIVTHDPQVAAQ-AERVIEIRDGEIVRNPPA 227
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
4-233 |
1.89e-43 |
|
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: 154.15 E-value: 1.89e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 4 PDASPAAPIISVAGVN-KWYGAFQVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIELgqSENA 82
Cdd:COG4988 328 PLPAAGPPSIELEDVSfSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDL--SDLD 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 83 AQAVRREVGMVFQHfnlfPHldlvqnciLAPMSVR---GMSRRAA------EAL-AVGLLERV---------RLGEHAhk 143
Cdd:COG4988 406 PASWRRQIAWVPQN----PY--------LFAGTIRenlRLGRPDAsdeeleAALeAAGLDEFVaalpdgldtPLGEGG-- 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 144 ypSQLSGGQQQRAAIARALCMEPRVMLFDEPTSALDPEMVGEVLDTMRGLAAeGMTMMIVTHEMGFARQvADRVVFMDRG 223
Cdd:COG4988 472 --RGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAK-GRTVILITHRLALLAQ-ADRILVLDDG 547
|
250
....*....|
gi 500071467 224 QIVEQAPPAA 233
Cdd:COG4988 548 RIVEQGTHEE 557
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
13-228 |
4.68e-43 |
|
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: 145.12 E-value: 4.68e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 13 ISVAGVNKWYGAFQVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGielgqsENAAQAVRREVGM 92
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDG------KPLDIAARNRIGY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 93 VFQHFNLFPHLDLVQNCI-LApmSVRGMSRRAAEALAVGLLERVRLGEHAHKYPSQLSGGQQQRAAIARALCMEPRVMLF 171
Cdd:cd03269 75 LPEERGLYPKMKVIDQLVyLA--QLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLIL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 500071467 172 DEPTSALDPEMVGEVLDTMRGLAAEGMTMMIVTHEMGFARQVADRVVFMDRGQIVEQ 228
Cdd:cd03269 153 DEPFSGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLY 209
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
38-229 |
5.09e-43 |
|
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: 145.13 E-value: 5.09e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 38 GEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIELGQSENAAQ--AVRREVGMVFQHFNLFPHLDLVQNCILAPMS 115
Cdd:cd03297 23 EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRKKINlpPQQRKIGLVFQQYALFPHLNVRENLAFGLKR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 116 VRGMSRRAAEAlavGLLERVRLGEHAHKYPSQLSGGQQQRAAIARALCMEPRVMLFDEPTSALDPEMVGEVLDTMRGLAA 195
Cdd:cd03297 103 KRNREDRISVD---ELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELKQIKK 179
|
170 180 190
....*....|....*....|....*....|....*
gi 500071467 196 E-GMTMMIVTHEMGFARQVADRVVFMDRGQIVEQA 229
Cdd:cd03297 180 NlNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
13-226 |
9.81e-43 |
|
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: 144.57 E-value: 9.81e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 13 ISVAGVNKWYG--AFQVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIELGQSENAAqavRREV 90
Cdd:cd03263 1 LQIRNLTKTYKkgTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAA---RQSL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 91 GMVFQHFNLFPHLDLVQN----CILapmsvRGMSRRAAEALAVGLLERVRLGEHAHKYPSQLSGGQQQRAAIARALCMEP 166
Cdd:cd03263 78 GYCPQFDALFDELTVREHlrfyARL-----KGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGP 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 167 RVMLFDEPTSALDPEMVGEVLDTMRGLaAEGMTMMIVTHEMGFARQVADRVVFMDRGQIV 226
Cdd:cd03263 153 SVLLLDEPTSGLDPASRRAIWDLILEV-RKGRSIILTTHSMDEAEALCDRIAIMSDGKLR 211
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
26-210 |
1.81e-42 |
|
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: 142.95 E-value: 1.81e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 26 QVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIELGQSENAAQAVRREVGMVFQHFN--LFpHL 103
Cdd:TIGR01166 6 EVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPLDYSRKGLLERRQRVGLVFQDPDdqLF-AA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 104 DLVQNCILAPMSVrGMSRRAAEALAVGLLERVRLGEHAHKYPSQLSGGQQQRAAIARALCMEPRVMLFDEPTSALDPEMV 183
Cdd:TIGR01166 85 DVDQDVAFGPLNL-GLSEAEVERRVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAGLDPAGR 163
|
170 180
....*....|....*....|....*..
gi 500071467 184 GEVLDTMRGLAAEGMTMMIVTHEMGFA 210
Cdd:TIGR01166 164 EQMLAILRRLRAEGMTVVISTHDVDLA 190
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
22-239 |
2.64e-42 |
|
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: 147.18 E-value: 2.64e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 22 YGAFQVltDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIELGQSENAAQ--AVRREVGMVFQHFNL 99
Cdd:TIGR02142 9 LGDFSL--DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKGIFlpPEKRRIGYVFQEARL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 100 FPHLDLVQNCILAPMSVRGMSRRAAEALAVGLLErvrLGEHAHKYPSQLSGGQQQRAAIARALCMEPRVMLFDEPTSALD 179
Cdd:TIGR02142 87 FPHLSVRGNLRYGMKRARPSERRISFERVIELLG---IGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALD 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 500071467 180 PEMVGEVLDTMRGLAAE-GMTMMIVTHEMGFARQVADRVVFMDRGQIVEQAPPAAFFGAPV 239
Cdd:TIGR02142 164 DPRKYEILPYLERLHAEfGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPD 224
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
11-206 |
4.52e-42 |
|
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: 142.23 E-value: 4.52e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 11 PIISVAGVNKWYGAFQVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIELGQsenAAQAVRREV 90
Cdd:COG4133 1 MMLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRD---AREDYRRRL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 91 GMVFQHFNLFPHLDLVQNCILApMSVRGMSRRAAEALAvgLLERVRLGEHAHKYPSQLSGGQQQRAAIARALCMEPRVML 170
Cdd:COG4133 78 AYLGHADGLKPELTVRENLRFW-AALYGLRADREAIDE--ALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWL 154
|
170 180 190
....*....|....*....|....*....|....*.
gi 500071467 171 FDEPTSALDPEMVGEVLDTMRGLAAEGMTMMIVTHE 206
Cdd:COG4133 155 LDEPFTALDAAGVALLAELIAAHLARGGAVLLTTHQ 190
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
26-248 |
7.97e-42 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 145.49 E-value: 7.97e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 26 QVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIE-LGQSENAAQAVRREVGMVFQhfNLFPHLD 104
Cdd:PRK11308 29 KALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDlLKADPEAQKLLRQKIQIVFQ--NPYGSLN 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 105 LVQNC--ILA-PMSVR---GMSRRAAEALAvgLLERVRL-GEHAHKYPSQLSGGQQQRAAIARALCMEPRVMLFDEPTSA 177
Cdd:PRK11308 107 PRKKVgqILEePLLINtslSAAERREKALA--MMAKVGLrPEHYDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSA 184
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 500071467 178 LDPEMVGEVLDTMRGLAAE-GMTMMIVTHEMGFARQVADRVVFMDRGQIVEQAPPAAFFGAPVHERTRRFLS 248
Cdd:PRK11308 185 LDVSVQAQVLNLMMDLQQElGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFNNPRHPYTQALLS 256
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
28-238 |
9.64e-42 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 144.01 E-value: 9.64e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 28 LTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVV--DGIELGQSENAAQAVRREVGMVFQhfnlFPHLDL 105
Cdd:PRK13634 23 LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIgeRVITAGKKNKKLKPLRKKVGIVFQ----FPEHQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 106 VQNCIL-----APMSVrGMSRRAAEALAVGLLERVRLGEHA-HKYPSQLSGGQQQRAAIARALCMEPRVMLFDEPTSALD 179
Cdd:PRK13634 99 FEETVEkdicfGPMNF-GVSEEDAKQKAREMIELVGLPEELlARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLD 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 180 PEMVGEVLDTMRGLAAE-GMTMMIVTHEMGFARQVADRVVFMDRGQIVEQAPPAAFFGAP 238
Cdd:PRK13634 178 PKGRKEMMEMFYKLHKEkGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADP 237
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
11-224 |
1.11e-41 |
|
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: 142.19 E-value: 1.11e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 11 PIISVAGVNKwygAF----------QVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVD----GIEL 76
Cdd:COG4778 3 TLLEVENLSK---TFtlhlqggkrlPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRhdggWVDL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 77 GQ-SENAAQAVRR-EVGMVFQHFNLFPH---LDLVqnciLAPMSVRGMSRRAAEALAVGLLERVRLGEH-AHKYPSQLSG 150
Cdd:COG4778 80 AQaSPREILALRRrTIGYVSQFLRVIPRvsaLDVV----AEPLLERGVDREEARARARELLARLNLPERlWDLPPATFSG 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 500071467 151 GQQQRAAIARALCMEPRVMLFDEPTSALDPEMVGEVLDTMRGLAAEGMTMMIVTHEMGFARQVADRVVFMDRGQ 224
Cdd:COG4778 156 GEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVREAVADRVVDVTPFS 229
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
26-251 |
1.87e-41 |
|
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: 142.64 E-value: 1.87e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 26 QVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIELGQSENA-AQAVRREVGMVFQH-FNLFPHL 103
Cdd:TIGR02769 25 PVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKqRRAFRRDVQLVFQDsPSAVNPR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 104 DLVQNCILAPM-SVRGMSRRAAEALAVGLLERVRL-GEHAHKYPSQLSGGQQQRAAIARALCMEPRVMLFDEPTSALDPE 181
Cdd:TIGR02769 105 MTVRQIIGEPLrHLTSLDESEQKARIAELLDMVGLrSEDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSNLDMV 184
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 500071467 182 MVGEVLDTMRGLAAE-GMTMMIVTHEMGFARQVADRVVFMDRGQIVEQAPPAAFFGAPvHERTRRFLSQIL 251
Cdd:TIGR02769 185 LQAVILELLRKLQQAfGTAYLFITHDLRLVQSFCQRVAVMDKGQIVEECDVAQLLSFK-HPAGRNLQSAVL 254
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
14-248 |
2.33e-41 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 141.51 E-value: 2.33e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 14 SVAGVNKWYGAFQVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIELGQSEnAAQAVRREVGMV 93
Cdd:TIGR03410 2 EVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLP-PHERARAGIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 94 FQHFNLFPHLDLVQNcILAPMSVRGMSRRAAEALAVGL---LERVRlgehaHKYPSQLSGGQQQRAAIARALCMEPRVML 170
Cdd:TIGR03410 81 PQGREIFPRLTVEEN-LLTGLAALPRRSRKIPDEIYELfpvLKEML-----GRRGGDLSGGQQQQLAIARALVTRPKLLL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 500071467 171 FDEPTSALDPEMVGEVLDTMRGLAAE-GMTMMIVTHEMGFARQVADRVVFMDRGQIVEQAPPAAFfgapVHERTRRFLS 248
Cdd:TIGR03410 155 LDEPTEGIQPSIIKDIGRVIRRLRAEgGMAILLVEQYLDFARELADRYYVMERGRVVASGAGDEL----DEDKVRRYLA 229
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1-250 |
3.08e-41 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 144.98 E-value: 3.08e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 1 MPNPDASP---AAPIISVAGVNKWYGAFQVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIELG 77
Cdd:PRK11607 5 IPRPQAKTrkaLTPLLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 78 QsenaAQAVRREVGMVFQHFNLFPHLDLVQNcILAPMSVRGMSRRAAEALAVGLLERVRLGEHAHKYPSQLSGGQQQRAA 157
Cdd:PRK11607 85 H----VPPYQRPINMMFQSYALFPHMTVEQN-IAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 158 IARALCMEPRVMLFDEPTSALDPE----MVGEVLDTMRGLaaeGMTMMIVTHEMGFARQVADRVVFMDRGQIVEQAPPAA 233
Cdd:PRK11607 160 LARSLAKRPKLLLLDEPMGALDKKlrdrMQLEVVDILERV---GVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEE 236
|
250
....*....|....*..
gi 500071467 234 FFGAPVHERTRRFLSQI 250
Cdd:PRK11607 237 IYEHPTTRYSAEFIGSV 253
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
11-230 |
4.89e-41 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 141.75 E-value: 4.89e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 11 PIISVAGVNKWY---------GAFQVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIELGQSEN 81
Cdd:PRK10419 2 TLLNVSGLSHHYahgglsgkhQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 82 AAQ-AVRREVGMVFQH----FNlfPHLDlVQNCILAPMS-VRGMSRRAAEALAVGLLERVRLG-EHAHKYPSQLSGGQQQ 154
Cdd:PRK10419 82 AQRkAFRRDIQMVFQDsisaVN--PRKT-VREIIREPLRhLLSLDKAERLARASEMLRAVDLDdSVLDKRPPQLSGGQLQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 500071467 155 RAAIARALCMEPRVMLFDEPTSALDPEMVGEVLDTMRGLAAE-GMTMMIVTHEMGFARQVADRVVFMDRGQIVEQAP 230
Cdd:PRK10419 159 RVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQfGTACLFITHDLRLVERFCQRVMVMDNGQIVETQP 235
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
13-229 |
5.46e-41 |
|
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: 139.66 E-value: 5.46e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 13 ISVAGVNKWYGAFQVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIELGQSENAaqavRREVGM 92
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEA----LRRIGA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 93 VFQHFNLFPHLDLVQNCILAPMSVRGMSRRAAEalavgLLERVRLGEHAHKYPSQLSGGQQQRAAIARALCMEPRVMLFD 172
Cdd:cd03268 77 LIEAPGFYPNLTARENLRLLARLLGIRKKRIDE-----VLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILD 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 500071467 173 EPTSALDPEMVGEVLDTMRGLAAEGMTMMIVTHEMGFARQVADRVVFMDRGQIVEQA 229
Cdd:cd03268 152 EPTNGLDPDGIKELRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
32-233 |
6.28e-41 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 140.49 E-value: 6.28e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 32 SLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGielgQSENAAQAVRREVGMVFQHFNLFPHLDLVQNcI- 110
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNG----QDHTTTPPSRRPVSMLFQENNLFSHLTVAQN-Ig 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 111 --LAP-MSVRGMSRRAAEALAvgllERVRLGEHAHKYPSQLSGGQQQRAAIARALCMEPRVMLFDEPTSALDPEMVGEVL 187
Cdd:PRK10771 94 lgLNPgLKLNAAQREKLHAIA----RQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEML 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 500071467 188 DTMRGLAAE-GMTMMIVTHEMGFARQVADRVVFMDRGQIVEQAPPAA 233
Cdd:PRK10771 170 TLVSQVCQErQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDE 216
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
26-228 |
9.62e-41 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 147.23 E-value: 9.62e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 26 QVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIELgqSENAAQAVRREVGMVFQHFNLFPhldl 105
Cdd:COG1132 354 PVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDI--RDLTLESLRRQIGVVPQDTFLFS---- 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 106 vqncilapMSVR---GMSRRAA------EAL-AVGLLERVR---------LGEHAHKypsqLSGGQQQRAAIARALCMEP 166
Cdd:COG1132 428 --------GTIReniRYGRPDAtdeeveEAAkAAQAHEFIEalpdgydtvVGERGVN----LSGGQRQRIAIARALLKDP 495
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 500071467 167 RVMLFDEPTSALDPEMVGEVLDTMRGLAAeGMTMMIVTHEMGFARQvADRVVFMDRGQIVEQ 228
Cdd:COG1132 496 PILILDEATSALDTETEALIQEALERLMK-GRTTIVIAHRLSTIRN-ADRILVLDDGRIVEQ 555
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
28-247 |
1.06e-40 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 144.02 E-value: 1.06e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 28 LTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIELGQSENAA--QAVRREVGMVFQHFNLFPHLDL 105
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAElrEVRRKKIAMVFQSFALMPHMTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 106 VQNCILApMSVRGMSRRAAEALAVGLLERVRLGEHAHKYPSQLSGGQQQRAAIARALCMEPRVMLFDEPTSALDPEMVGE 185
Cdd:PRK10070 124 LDNTAFG-MELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTE 202
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 500071467 186 VLDTMRGLAAEGM-TMMIVTHEMGFARQVADRVVFMDRGQIVEQAPPAAFFGAPVHERTRRFL 247
Cdd:PRK10070 203 MQDELVKLQAKHQrTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFF 265
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
27-235 |
1.17e-40 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 140.99 E-value: 1.17e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 27 VLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIELGQSENAAQaVRREVGMVFQHfnlfPHLDLV 106
Cdd:PRK13633 25 ALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLWD-IRNKAGMVFQN----PDNQIV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 107 ------------QNCILAPMSVRgmsRRAAEAL-AVGLLERVRlgeHAhkyPSQLSGGQQQRAAIARALCMEPRVMLFDE 173
Cdd:PRK13633 100 ativeedvafgpENLGIPPEEIR---ERVDESLkKVGMYEYRR---HA---PHLLSGGQKQRVAIAGILAMRPECIIFDE 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 500071467 174 PTSALDPEMVGEVLDTMRGLAAE-GMTMMIVTHEMGFARQvADRVVFMDRGQIVEQAPPAAFF 235
Cdd:PRK13633 171 PTAMLDPSGRREVVNTIKELNKKyGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIF 232
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
12-226 |
1.36e-40 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 141.40 E-value: 1.36e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 12 IISVAGVNKWYGAFQVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIELGQSenaaqAVRR--- 88
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPE-----DRRRigy 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 89 ---EVGmvfqhfnLFPHLDlVQNCILAPMSVRGMSRRAAEALAVGLLERVRLGEHAHKYPSQLSGGQQQRAAIARALCME 165
Cdd:COG4152 76 lpeERG-------LYPKMK-VGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHD 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 500071467 166 PRVMLFDEPTSALDPEMVGEVLDTMRGLAAEGMTMMIVTHEMGFARQVADRVVFMDRGQIV 226
Cdd:COG4152 148 PELLILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQMELVEELCDRIVIINKGRKV 208
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
24-226 |
3.34e-40 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 140.61 E-value: 3.34e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 24 AFQVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSI------------------VVDGIELGQSE----N 81
Cdd:PRK13651 19 ELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewifkdeknkkktkekekVLEKLVIQKTRfkkiK 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 82 AAQAVRREVGMVFQ--HFNLFPHlDLVQNCILAPMSVrGMSRRAAEALAVGLLERVRLGE-HAHKYPSQLSGGQQQRAAI 158
Cdd:PRK13651 99 KIKEIRRRVGVVFQfaEYQLFEQ-TIEKDIIFGPVSM-GVSKEEAKKRAAKYIELVGLDEsYLQRSPFELSGGQKRRVAL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 500071467 159 ARALCMEPRVMLFDEPTSALDPEMVGEVLDTMRGLAAEGMTMMIVTHEMGFARQVADRVVFMDRGQIV 226
Cdd:PRK13651 177 AGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTKRTIFFKDGKII 244
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
28-235 |
3.34e-40 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 140.18 E-value: 3.34e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 28 LTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIELGQSENAAQAVRREVGMVFQhfnlFPHLDLVQ 107
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKLSDIRKKVGLVFQ----YPEYQLFE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 108 NCI-----LAP----MSVRGMSRRAAEAL-AVGLlervRLGEHAHKYPSQLSGGQQQRAAIARALCMEPRVMLFDEPTSA 177
Cdd:PRK13637 99 ETIekdiaFGPinlgLSEEEIENRVKRAMnIVGL----DYEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAG 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 500071467 178 LDPEMVGEVLDTMRGLAAE-GMTMMIVTHEMGFARQVADRVVFMDRGQIVEQAPPAAFF 235
Cdd:PRK13637 175 LDPKGRDEILNKIKELHKEyNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVF 233
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
13-240 |
3.47e-40 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 139.10 E-value: 3.47e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 13 ISVAGVNKWYGAFQVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIELGQSENAAQAVRREVgm 92
Cdd:COG4559 2 LEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRRAV-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 93 vfqhfnlfphldLVQNCILA-PMSVR----------GMSRRAAEALAVGLLERVRLGEHAHKYPSQLSGGQQQRAAIARA 161
Cdd:COG4559 80 ------------LPQHSSLAfPFTVEevvalgraphGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 162 LC-------MEPRVMLFDEPTSALDPEMVGEVLDTMRGLAAEGMTMMIVTHEMGFARQVADRVVFMDRGQIVEQAPPA-- 232
Cdd:COG4559 148 LAqlwepvdGGPRWLFLDEPTSALDLAHQHAVLRLARQLARRGGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPEev 227
|
250
....*....|....*
gi 500071467 233 -------AFFGAPVH 240
Cdd:COG4559 228 ltdelleRVYGADLR 242
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
27-226 |
3.57e-40 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 137.39 E-value: 3.57e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 27 VLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGielgqsENAAQAVRRE-VGMVFQH--FNLFphL 103
Cdd:cd03226 15 ILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNG------KPIKAKERRKsIGYVMQDvdYQLF--T 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 104 DLVQNCILapMSVRGMSRRAAEALAVglLERVRLGEHAHKYPSQLSGGQQQRAAIARALCMEPRVMLFDEPTSALDPEMV 183
Cdd:cd03226 87 DSVREELL--LGLKELDAGNEQAETV--LKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNM 162
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 500071467 184 GEVLDTMRGLAAEGMTMMIVTHEMGFARQVADRVVFMDRGQIV 226
Cdd:cd03226 163 ERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
13-231 |
5.64e-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: 5.64e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 13 ISVAGVNKWYGAFQVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIELGQSenaAQAVRREVGM 92
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVRE---PREVRRRIGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 93 VFQHFNLFPHLDLVQNcILAPMSVRGMSRRAAEALAVGLLERVRLGEHAHKYPSQLSGGQQQRAAIARALCMEPRVMLFD 172
Cdd:cd03265 78 VFQDLSVDDELTGWEN-LYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLD 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 500071467 173 EPTSALDP---EMVGEVLDTMrgLAAEGMTMMIVTHEMGFARQVADRVVFMDRGQIVEQAPP 231
Cdd:cd03265 157 EPTIGLDPqtrAHVWEYIEKL--KEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTP 216
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
18-248 |
8.53e-40 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 138.38 E-value: 8.53e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 18 VNKWYGAFQVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQ-----HQEGSIVVDGIELGQSENAAQAVRREVGM 92
Cdd:PRK14243 16 LNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDlipgfRVEGKVTFHGKNLYAPDVDPVEVRRRIGM 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 93 VFQHFNLFPHlDLVQNCILAPmSVRGMSRRAAEALAVGLLERVRLGEHAHKYP---SQLSGGQQQRAAIARALCMEPRVM 169
Cdd:PRK14243 96 VFQKPNPFPK-SIYDNIAYGA-RINGYKGDMDELVERSLRQAALWDEVKDKLKqsgLSLSGGQQQRLCIARAIAVQPEVI 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 170 LFDEPTSALDPEMVGEVLDTMRGLaAEGMTMMIVTHEMGFARQVADRVVFMD---------RGQIVEQAPPAAFFGAPVH 240
Cdd:PRK14243 174 LMDEPCSALDPISTLRIEELMHEL-KEQYTIIIVTHNMQQAARVSDMTAFFNveltegggrYGYLVEFDRTEKIFNSPQQ 252
|
....*...
gi 500071467 241 ERTRRFLS 248
Cdd:PRK14243 253 QATRDYVS 260
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
11-232 |
1.19e-39 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 137.60 E-value: 1.19e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 11 PIISVAGVNKWYGAFQVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIELGQSENAAQAVRRev 90
Cdd:PRK13548 1 AMLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRR-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 91 GMVFQHFNL-FPHldLVQNCILAPMSVRGMSRRAAEALAVGLLERVRLGEHAHKYPSQLSGGQQQRAAIARALC------ 163
Cdd:PRK13548 79 AVLPQHSSLsFPF--TVEEVVAMGRAPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAqlwepd 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 164 MEPRVMLFDEPTSALDPEMVGEVLDTMRGLAAE-GMTMMIVTHEMGFARQVADRVVFMDRGQIVEQAPPA 232
Cdd:PRK13548 157 GPPRWLLLDEPTSALDLAHQHHVLRLARQLAHErGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPA 226
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
25-247 |
1.25e-39 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 138.05 E-value: 1.25e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 25 FQVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIELgQSENAAQAVRReVGMVFQHFN--LFPH 102
Cdd:COG4167 26 FEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKL-EYGDYKYRCKH-IRMIFQDPNtsLNPR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 103 LDLVQncIL-APMSVR-GMSRRAAEALAVGLLERVRL-GEHAHKYPSQLSGGQQQRAAIARALCMEPRVMLFDEPTSALD 179
Cdd:COG4167 104 LNIGQ--ILeEPLRLNtDLTAEEREERIFATLRLVGLlPEHANFYPHMLSSGQKQRVALARALILQPKIIIADEALAALD 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 500071467 180 PEMVGEVLDTMRGLAAE-GMTMMIVTHEMGFARQVADRVVFMDRGQIVEQAPPAAFFGAPVHERTRRFL 247
Cdd:COG4167 182 MSVRSQIINLMLELQEKlGISYIYVSQHLGIVKHISDKVLVMHQGEVVEYGKTAEVFANPQHEVTKRLI 250
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
26-235 |
2.15e-39 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 137.52 E-value: 2.15e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 26 QVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIELGQSENAAQAVRREVGMVFQHFN--LF-PH 102
Cdd:PRK13639 16 EALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSLLEVRKTVGIVFQNPDdqLFaPT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 103 LDlvQNCILAPMSVrGMSRRAAEALAVGLLERVRLGEHAHKYPSQLSGGQQQRAAIARALCMEPRVMLFDEPTSALDPEM 182
Cdd:PRK13639 96 VE--EDVAFGPLNL-GLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMG 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 500071467 183 VGEVLDTMRGLAAEGMTMMIVTHEMGFARQVADRVVFMDRGQIVEQAPPAAFF 235
Cdd:PRK13639 173 ASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVF 225
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
4-238 |
3.11e-39 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 137.04 E-value: 3.11e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 4 PDASPAapiisvagvnkwygafqvLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIELGQSeNAA 83
Cdd:PRK13644 12 PDGTPA------------------LENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDF-SKL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 84 QAVRREVGMVFQHfnlfPHLDLV------------QNCILAPMSVRGMSRRAaealavglLERVRLGEHAHKYPSQLSGG 151
Cdd:PRK13644 73 QGIRKLVGIVFQN----PETQFVgrtveedlafgpENLCLPPIEIRKRVDRA--------LAEIGLEKYRHRSPKTLSGG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 152 QQQRAAIARALCMEPRVMLFDEPTSALDPEMVGEVLDTMRGLAAEGMTMMIVTHEMGfARQVADRVVFMDRGQIVEQAPP 231
Cdd:PRK13644 141 QGQCVALAGILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLE-ELHDADRIIVMDRGKIVLEGEP 219
|
....*..
gi 500071467 232 AAFFGAP 238
Cdd:PRK13644 220 ENVLSDV 226
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
13-228 |
3.44e-39 |
|
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: 135.01 E-value: 3.44e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 13 ISVAGVNKWYGAFQVLTDVSLSVARGEKVVIcGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIELGQSEnaaQAVRREVGM 92
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPGMYGLL-GPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQP---QKLRRRIGY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 93 VFQHFNLFPHLDLVQncILAPMSV-RGMSRRAAEALAVGLLERVRLGEHAHKYPSQLSGGQQQRAAIARALCMEPRVMLF 171
Cdd:cd03264 77 LPQEFGVYPNFTVRE--FLDYIAWlKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIV 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 500071467 172 DEPTSALDPE-------MVGEVldtmrglaAEGMTMMIVTHEMGFARQVADRVVFMDRGQIVEQ 228
Cdd:cd03264 155 DEPTAGLDPEerirfrnLLSEL--------GEDRIVILSTHIVEDVESLCNQVAVLNKGKLVFE 210
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
13-238 |
4.97e-39 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 139.01 E-value: 4.97e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 13 ISVAGVNKWYGAFQVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGielgQSENAAQAVRREVGM 92
Cdd:PRK11000 4 VTLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGE----KRMNDVPPAERGVGM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 93 VFQHFNLFPHLDLVQNCI----LAPMSVRGMSRR---AAEALAVG-LLERvrlgehahkYPSQLSGGQQQRAAIARALCM 164
Cdd:PRK11000 80 VFQSYALYPHLSVAENMSfglkLAGAKKEEINQRvnqVAEVLQLAhLLDR---------KPKALSGGQRQRVAIGRTLVA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 165 EPRVMLFDEPTSALDP----EMVGEVLDTMRGLaaeGMTMMIVTHEMGFARQVADRVVFMDRGQIVEQAPP--------- 231
Cdd:PRK11000 151 EPSVFLLDEPLSNLDAalrvQMRIEISRLHKRL---GRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPlelyhypan 227
|
250
....*....|
gi 500071467 232 ---AAFFGAP 238
Cdd:PRK11000 228 rfvAGFIGSP 237
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
27-247 |
5.79e-39 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 135.95 E-value: 5.79e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 27 VLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIELGQSENAAQ----AVRREVGMVFQHFNLFPH 102
Cdd:PRK14246 25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYFGKDIFQidaiKLRKEVGMVFQQPNPFPH 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 103 LDLVQNcILAPMSVRGMS-RRAAEALAVGLLERVRLGEHAHKY----PSQLSGGQQQRAAIARALCMEPRVMLFDEPTSA 177
Cdd:PRK14246 105 LSIYDN-IAYPLKSHGIKeKREIKKIVEECLRKVGLWKEVYDRlnspASQLSGGQQQRLTIARALALKPKVLLMDEPTSM 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 178 LDPEMVGEVLDTMRGLAAEgMTMMIVTHEMGFARQVADRVVFMDRGQIVEQAPPAAFFGAPVHERTRRFL 247
Cdd:PRK14246 184 IDIVNSQAIEKLITELKNE-IAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNELTEKYV 252
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
11-240 |
9.75e-39 |
|
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: 135.21 E-value: 9.75e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 11 PIISVAGVNKWYGAFQVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQlEQHQ--EGSIVVDGIELGQsENAAQaVRR 88
Cdd:COG1119 2 PLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITG-DLPPtyGNDVRLFGERRGG-EDVWE-LRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 89 EVGMV---FQHFnlFPHLDLVQNCIL-APMSVRGMSRR---AAEALAVGLLERVRLGEHAHKYPSQLSGGQQQRAAIARA 161
Cdd:COG1119 79 RIGLVspaLQLR--FPRDETVLDVVLsGFFDSIGLYREptdEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIARA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 162 LCMEPRVMLFDEPTSALDPEMVGEVLDTMRGLAAEGMTMMI-VTH---EM--GFarqvaDRVVFMDRGQIVEQAPPA--- 232
Cdd:COG1119 157 LVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVlVTHhveEIppGI-----THVLLLKDGRVVAAGPKEevl 231
|
250
....*....|....
gi 500071467 233 ------AFFGAPVH 240
Cdd:COG1119 232 tsenlsEAFGLPVE 245
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
28-235 |
2.39e-38 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 134.87 E-value: 2.39e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 28 LTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIEL-GQSENA-AQAVRREVGMVFQhfnlFPHLDL 105
Cdd:PRK13649 23 LFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLItSTSKNKdIKQIRKKVGLVFQ----FPESQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 106 VQNCILAPMSVR----GMSRRAAEALAVGLLERVRLGEHA-HKYPSQLSGGQQQRAAIARALCMEPRVMLFDEPTSALDP 180
Cdd:PRK13649 99 FEETVLKDVAFGpqnfGVSQEEAEALAREKLALVGISESLfEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDP 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 500071467 181 EMVGEVLDTMRGLAAEGMTMMIVTHEMGFARQVADRVVFMDRGQIVEQAPPAAFF 235
Cdd:PRK13649 179 KGRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIF 233
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
11-231 |
4.17e-38 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 133.83 E-value: 4.17e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 11 PIISVAGVNKWYGAF----QVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIELgQSENAAQAV 86
Cdd:COG4525 2 SMLTVRHVSVRYPGGgqpqPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPV-TGPGADRGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 87 rrevgmVFQHFNLFPHLDLVQNCILaPMSVRGMSRRAAEALAVGLLERVRLGEHAHKYPSQLSGGQQQRAAIARALCMEP 166
Cdd:COG4525 81 ------VFQKDALLPWLNVLDNVAF-GLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADP 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 167 RVMLFDEPTSALDP---EMVGEVLdtMRGLAAEGMTMMIVTHEMGFARQVADRVVFMDR--GQIVEQAPP 231
Cdd:COG4525 154 RFLLMDEPFGALDAltrEQMQELL--LDVWQRTGKGVFLITHSVEEALFLATRLVVMSPgpGRIVERLEL 221
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
26-231 |
4.39e-38 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 134.09 E-value: 4.39e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 26 QVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIELgqSENAAQAVRREVGMVFQH-----FNLF 100
Cdd:PRK13647 19 KALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREV--NAENEKWVRSKVGLVFQDpddqvFSST 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 101 PHLDLV---QNCILAPMSVRgmsRRAAEALAVgllerVRLGEHAHKYPSQLSGGQQQRAAIARALCMEPRVMLFDEPTSA 177
Cdd:PRK13647 97 VWDDVAfgpVNMGLDKDEVE---RRVEEALKA-----VRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAY 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 500071467 178 LDPEMVGEVLDTMRGLAAEGMTMMIVTHEMGFARQVADRVVFMDRGQIVEQAPP 231
Cdd:PRK13647 169 LDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDK 222
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
32-228 |
5.78e-38 |
|
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: 132.29 E-value: 5.78e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 32 SLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGielgQSENAAQAVRREVGMVFQHFNLFPHLDLVQNCIL 111
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVND----QSHTGLAPYQRPVSMLFQENNLFAHLTVRQNIGL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 112 A---PMSVRGMSRRAAEALAvgllERVRLGEHAHKYPSQLSGGQQQRAAIARALCMEPRVMLFDEPTSALDPEMVGEVLD 188
Cdd:TIGR01277 94 GlhpGLKLNAEQQEKVVDAA----QQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLA 169
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 500071467 189 TMRGLAAE-GMTMMIVTHEMGFARQVADRVVFMDRGQIVEQ 228
Cdd:TIGR01277 170 LVKQLCSErQRTLLMVTHHLSDARAIASQIAVVSQGKIKVV 210
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
8-229 |
1.17e-37 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 131.82 E-value: 1.17e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 8 PAAPIISVAGVNKWYG----AFQVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIELGQ--SEN 81
Cdd:PRK10584 2 PAENIVEVHHLKKSVGqgehELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQmdEEA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 82 AAQAVRREVGMVFQHFNLFPHLDLVQNCILaPMSVRGMSRRAAEALAVGLLERVRLGEHAHKYPSQLSGGQQQRAAIARA 161
Cdd:PRK10584 82 RAKLRAKHVGFVFQSFMLIPTLNALENVEL-PALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 500071467 162 LCMEPRVMLFDEPTSALDPEMVGEVLDTMRGLAAE-GMTMMIVTHEMGFARQVADRVVFMDrGQIVEQA 229
Cdd:PRK10584 161 FNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREhGTTLILVTHDLQLAARCDRRLRLVN-GQLQEEA 228
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
13-239 |
1.23e-37 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 134.97 E-value: 1.23e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 13 ISVAGVNKWY-GAFQVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIELGQSENAAqavrREVG 91
Cdd:PRK11650 4 LKLQAVRKSYdGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPAD----RDIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 92 MVFQHFNLFPHLDLVQNcilapMS----VRGMS-----RRAAEAlaVGLLErvrLGEHAHKYPSQLSGGQQQRAAIARAL 162
Cdd:PRK11650 80 MVFQNYALYPHMSVREN-----MAyglkIRGMPkaeieERVAEA--ARILE---LEPLLDRKPRELSGGQRQRVAMGRAI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 163 CMEPRVMLFDEPTSALDP----EMVGEVLDTMRGLAAegmTMMIVTHEMGFARQVADRVVFMDRGQIvEQappaafFGAP 238
Cdd:PRK11650 150 VREPAVFLFDEPLSNLDAklrvQMRLEIQRLHRRLKT---TSLYVTHDQVEAMTLADRVVVMNGGVA-EQ------IGTP 219
|
.
gi 500071467 239 V 239
Cdd:PRK11650 220 V 220
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
26-235 |
1.79e-37 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 133.03 E-value: 1.79e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 26 QVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDG--IELGQSENAAQAVRREVGMVFQhfnlFPHL 103
Cdd:PRK13641 21 KGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGyhITPETGNKNLKKLRKKVSLVFQ----FPEA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 104 DLVQNCIL-----APMSVrGMSRRAAEALAVGLLERVRLGEH-AHKYPSQLSGGQQQRAAIARALCMEPRVMLFDEPTSA 177
Cdd:PRK13641 97 QLFENTVLkdvefGPKNF-GFSEDEAKEKALKWLKKVGLSEDlISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAG 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 500071467 178 LDPEMVGEVLDTMRGLAAEGMTMMIVTHEMGFARQVADRVVFMDRGQIVEQAPPAAFF 235
Cdd:PRK13641 176 LDPEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIF 233
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
25-235 |
2.30e-37 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 133.44 E-value: 2.30e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 25 FQVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIELGQSENAAQAV--------------RREV 90
Cdd:PRK13631 39 LVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIGDKKNNHELItnpyskkiknfkelRRRV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 91 GMVFQhfnlFPHLDLVQNCI-----LAPMSVrGMSRRAAEALAVGLLERVRLGE-HAHKYPSQLSGGQQQRAAIARALCM 164
Cdd:PRK13631 119 SMVFQ----FPEYQLFKDTIekdimFGPVAL-GVKKSEAKKLAKFYLNKMGLDDsYLERSPFGLSGGQKRRVAIAGILAI 193
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 500071467 165 EPRVMLFDEPTSALDPEMVGEVLDTMRGLAAEGMTMMIVTHEMGFARQVADRVVFMDRGQIVEQAPPAAFF 235
Cdd:PRK13631 194 QPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTGTPYEIF 264
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
5-248 |
5.03e-37 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 131.37 E-value: 5.03e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 5 DASPAAPIISVAGVNKWYGAFQVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQ-----HQEGSIVVDGIELGQS 79
Cdd:PRK14271 14 DVDAAAPAMAAVNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDkvsgyRYSGDVLLGGRSIFNY 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 80 ENAAQaVRREVGMVFQHFNLFPhLDLVQNCILAPMSVRGMSRRAAEALA------VGLLERVRlgEHAHKYPSQLSGGQQ 153
Cdd:PRK14271 94 RDVLE-FRRRVGMLFQRPNPFP-MSIMDNVLAGVRAHKLVPRKEFRGVAqarlteVGLWDAVK--DRLSDSPFRLSGGQQ 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 154 QRAAIARALCMEPRVMLFDEPTSALDPEMVGEVLDTMRGLaAEGMTMMIVTHEMGFARQVADRVVFMDRGQIVEQAPPAA 233
Cdd:PRK14271 170 QLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSL-ADRLTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQ 248
|
250
....*....|....*
gi 500071467 234 FFGAPVHERTRRFLS 248
Cdd:PRK14271 249 LFSSPKHAETARYVA 263
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
12-225 |
5.11e-37 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 131.29 E-value: 5.11e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 12 IISVAGVNKWYGAFQVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQL---EQHQEGSIVVDGIELGQSENAAQAVRR 88
Cdd:PRK09984 4 IIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgDKSAGSHIELLGRTVQREGRLARDIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 89 ---EVGMVFQHFNLFPHLDLVQNCILAPMSVRGMSR-------RAAEALAVGLLERVRLGEHAHKYPSQLSGGQQQRAAI 158
Cdd:PRK09984 84 sraNTGYIFQQFNLVNRLSVLENVLIGALGSTPFWRtcfswftREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAI 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 500071467 159 ARALCMEPRVMLFDEPTSALDPEMVGEVLDTMRGL-AAEGMTMMIVTHEMGFARQVADRVVFMDRGQI 225
Cdd:PRK09984 164 ARALMQQAKVILADEPIASLDPESARIVMDTLRDInQNDGITVVVTLHQVDYALRYCERIVALRQGHV 231
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
27-226 |
7.50e-37 |
|
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: 129.25 E-value: 7.50e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 27 VLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIELGQSEnaAQAVRREVGMVFQHFNLFpHLDLV 106
Cdd:cd03245 19 ALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLD--PADLRRNIGYVPQDVTLF-YGTLR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 107 QNCIL-APMSVRGMSRRAAEALAVGLLER-------VRLGEHAhkypSQLSGGQQQRAAIARALCMEPRVMLFDEPTSAL 178
Cdd:cd03245 96 DNITLgAPLADDERILRAAELAGVTDFVNkhpngldLQIGERG----RGLSGGQRQAVALARALLNDPPILLLDEPTSAM 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 500071467 179 DPEMVGEVLDTMRGLAAeGMTMMIVTHEMGFArQVADRVVFMDRGQIV 226
Cdd:cd03245 172 DMNSEERLKERLRQLLG-DKTLIIITHRPSLL-DLVDRIIVMDSGRIV 217
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
1-225 |
1.43e-36 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 129.80 E-value: 1.43e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 1 MPNPDASPAAPIISVAGVNKWYGAFQVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIELGQse 80
Cdd:PRK11247 1 MMNTARLNQGTPLLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAE-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 81 naaqaVRREVGMVFQHFNLFPHLDLVQNCILApmsVRGMSRRAA-EAL-AVGLLERvrlgehAHKYPSQLSGGQQQRAAI 158
Cdd:PRK11247 79 -----AREDTRLMFQDARLLPWKKVIDNVGLG---LKGQWRDAAlQALaAVGLADR------ANEWPAALSGGQKQRVAL 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 500071467 159 ARALCMEPRVMLFDEPTSALDPEMVGEVLDTMRGLAAE-GMTMMIVTHEMGFARQVADRVVFMDRGQI 225
Cdd:PRK11247 145 ARALIHRPGLLLLDEPLGALDALTRIEMQDLIESLWQQhGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
24-235 |
2.69e-36 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 129.85 E-value: 2.69e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 24 AFQVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIELGQS--ENAAQAVRREVGMVFQhfnlFP 101
Cdd:PRK13643 18 ASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTskQKEIKPVRKKVGVVFQ----FP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 102 HLDLVQNCILAPMSVR----GMSRRAAEALAVGLLERVRLG-EHAHKYPSQLSGGQQQRAAIARALCMEPRVMLFDEPTS 176
Cdd:PRK13643 94 ESQLFEETVLKDVAFGpqnfGIPKEKAEKIAAEKLEMVGLAdEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTA 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 500071467 177 ALDPEMVGEVLDTMRGLAAEGMTMMIVTHEMGFARQVADRVVFMDRGQIVEQAPPAAFF 235
Cdd:PRK13643 174 GLDPKARIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVF 232
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
13-231 |
3.50e-36 |
|
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: 135.47 E-value: 3.50e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 13 ISVAGVNKWYG--AFQVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIELGQSEnaAQAVRREV 90
Cdd:TIGR03797 452 IEVDRVTFRYRpdGPLILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAGLD--VQAVRRQL 529
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 91 GMVFQHFNLFPHlDLVQN-CILAPMSVRgmsrRAAEALA-VGLLERVR---LGehAHKYPSQ----LSGGQQQRAAIARA 161
Cdd:TIGR03797 530 GVVLQNGRLMSG-SIFENiAGGAPLTLD----EAWEAARmAGLAEDIRampMG--MHTVISEgggtLSGGQRQRLLIARA 602
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 500071467 162 LCMEPRVMLFDEPTSALD---PEMVGEVLDTMRGlaaegmTMMIVTHEMGFARQvADRVVFMDRGQIVEQAPP 231
Cdd:TIGR03797 603 LVRKPRILLFDEATSALDnrtQAIVSESLERLKV------TRIVIAHRLSTIRN-ADRIYVLDAGRVVQQGTY 668
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
27-228 |
3.88e-36 |
|
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: 128.12 E-value: 3.88e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 27 VLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIELgqSENAAQAVRREVGMVFQHFNLFPhlDLV 106
Cdd:cd03251 17 VLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDV--RDYTLASLRRQIGLVSQDVFLFN--DTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 107 QNCIL--APMSVRGMSRRAAE-ALAVGLLERV------RLGEHAhkypSQLSGGQQQRAAIARALCMEPRVMLFDEPTSA 177
Cdd:cd03251 93 AENIAygRPGATREEVEEAARaANAHEFIMELpegydtVIGERG----VKLSGGQRQRIAIARALLKDPPILILDEATSA 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 500071467 178 LDPEMVGEVLDTMRGLaAEGMTMMIVTHEMGFARQvADRVVFMDRGQIVEQ 228
Cdd:cd03251 169 LDTESERLVQAALERL-MKNRTTFVIAHRLSTIEN-ADRIVVLEDGKIVER 217
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-232 |
4.78e-36 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 130.72 E-value: 4.78e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 2 PNPDASPAAPI----ISVAGVNKWYGAFQVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIelg 77
Cdd:PRK13536 27 SEAKASIPGSMstvaIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGV--- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 78 QSENAAQAVRREVGMVFQHFNLFPHLDLVQNcILAPMSVRGMSRRAAEALAVGLLERVRLGEHAHKYPSQLSGGQQQRAA 157
Cdd:PRK13536 104 PVPARARLARARIGVVPQFDNLDLEFTVREN-LLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLT 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 500071467 158 IARALCMEPRVMLFDEPTSALDPEMVGEVLDTMRGLAAEGMTMMIVTHEMGFARQVADRVVFMDRG-QIVEQAPPA 232
Cdd:PRK13536 183 LARALINDPQLLILDEPTTGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGrKIAEGRPHA 258
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
28-236 |
5.18e-36 |
|
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: 127.58 E-value: 5.18e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 28 LTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIELgqsenAAQAVRREVgmVFQHFNLFPHLDLVQ 107
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQI-----TEPGPDRMV--VFQNYSLLPWLTVRE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 108 NCILAPMSV-RGMSRRAAEALAVGLLERVRLGEHAHKYPSQLSGGQQQRAAIARALCMEPRVMLFDEPTSALDPEMVGEV 186
Cdd:TIGR01184 74 NIALAVDRVlPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 500071467 187 LDTMRGLAAE-GMTMMIVTHEMGFARQVADRVVFMDRGqiveqapPAAFFG 236
Cdd:TIGR01184 154 QEELMQIWEEhRVTVLMVTHDVDEALLLSDRVVMLTNG-------PAANIG 197
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
27-233 |
6.06e-36 |
|
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: 134.61 E-value: 6.06e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 27 VLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIELGQSENAAqaVRREVGMVFQHFNLFpHLDLV 106
Cdd:TIGR03375 480 ALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQIDPAD--LRRNIGYVPQDPRLF-YGTLR 556
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 107 QNCIL-APMSVRGMSRRAAEAlaVGLLERVRLgeHAHKYPSQ-------LSGGQQQRAAIARALCMEPRVMLFDEPTSAL 178
Cdd:TIGR03375 557 DNIALgAPYADDEEILRAAEL--AGVTEFVRR--HPDGLDMQigergrsLSGGQRQAVALARALLRDPPILLLDEPTSAM 632
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 500071467 179 DPEMVGEVLDTMRGLAAeGMTMMIVTHEMGFARQVaDRVVFMDRGQIVEQAPPAA 233
Cdd:TIGR03375 633 DNRSEERFKDRLKRWLA-GKTLVLVTHRTSLLDLV-DRIIVMDNGRIVADGPKDQ 685
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
30-250 |
9.36e-36 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 133.83 E-value: 9.36e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 30 DVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIELGQ-SENAAQAVRREVGMVFQ--HFNLFPHLDlV 106
Cdd:PRK10261 342 KVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTlSPGKLQALRRDIQFIFQdpYASLDPRQT-V 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 107 QNCILAPMSVRGMSR-RAAEALAVGLLERVRL-GEHAHKYPSQLSGGQQQRAAIARALCMEPRVMLFDEPTSALDPEMVG 184
Cdd:PRK10261 421 GDSIMEPLRVHGLLPgKAAAARVAWLLERVGLlPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRG 500
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 500071467 185 EVLDTMRGLAAE-GMTMMIVTHEMGFARQVADRVVFMDRGQIVEQAPPAAFFGAPVHERTRRFLSQI 250
Cdd:PRK10261 501 QIINLLLDLQRDfGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENPQHPYTRKLMAAV 567
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
6-226 |
1.14e-35 |
|
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: 125.36 E-value: 1.14e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 6 ASPAAPIISVAGVNKWYGA-FQVLTDVSLSVARGEKVVICGPSGSGKSTLIRCL-NQLEQHQ-EGSIVVDGIELGqsena 82
Cdd:cd03213 2 VTLSFRNLTVTVKSSPSKSgKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALaGRRTGLGvSGEVLINGRPLD----- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 83 AQAVRREVGMVFQHFNLFPHLdlvqncilapmSVRgmsrraaEALAVGLLERvrlgehahkypsQLSGGQQQRAAIARAL 162
Cdd:cd03213 77 KRSFRKIIGYVPQDDILHPTL-----------TVR-------ETLMFAAKLR------------GLSGGERKRVSIALEL 126
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 500071467 163 CMEPRVMLFDEPTSALDPEMVGEVLDTMRGLAAEGMTMMIVTH----EMgFarQVADRVVFMDRGQIV 226
Cdd:cd03213 127 VSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADTGRTIICSIHqpssEI-F--ELFDKLLLLSQGRVI 191
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
28-205 |
1.21e-35 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 126.06 E-value: 1.21e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 28 LTDVSLSVARGEKVVICGPSGSGKSTLIRCLN-QLEQH--QEGSIVVDGIELgqseNAAQAVRREVGMVFQHFNLFPHLD 104
Cdd:COG4136 17 LAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAgTLSPAfsASGEVLLNGRRL----TALPAEQRRIGILFQDDLLFPHLS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 105 LVQNCILA-PMSVRGMSRRAAEALAvglLERVRLGEHAHKYPSQLSGGQQQRAAIARALCMEPRVMLFDEPTSALDPEMV 183
Cdd:COG4136 93 VGENLAFAlPPTIGRAQRRARVEQA---LEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKLDAALR 169
|
170 180
....*....|....*....|...
gi 500071467 184 GEVLDTMRG-LAAEGMTMMIVTH 205
Cdd:COG4136 170 AQFREFVFEqIRQRGIPALLVTH 192
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
26-235 |
2.88e-35 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 126.64 E-value: 2.88e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 26 QVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIELgQSENAAQAvRREVGMVFQH-FNLFPHLD 104
Cdd:PRK13632 23 NALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITI-SKENLKEI-RKKIGIIFQNpDNQFIGAT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 105 lVQNCILAPMSVRGMSRRAAEALAVGLLERVRLGEHAHKYPSQLSGGQQQRAAIARALCMEPRVMLFDEPTSALDPEMVG 184
Cdd:PRK13632 101 -VEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFDESTSMLDPKGKR 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 500071467 185 EVLDTMRGLAAEGMTMMI-VTHEMGFARQvADRVVFMDRGQIVEQAPPAAFF 235
Cdd:PRK13632 180 EIKKIMVDLRKTRKKTLIsITHDMDEAIL-ADKVIVFSEGKLIAQGKPKEIL 230
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
26-247 |
5.17e-35 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 130.98 E-value: 5.17e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 26 QVLTDVSLSVARGEKVVICGPSGSGKS-TLIRCLNQLEQ----HQEGSIVVDGIE-LGQSENAAQAVR-REVGMVFQH-- 96
Cdd:PRK15134 23 TVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSppvvYPSGDIRFHGESlLHASEQTLRGVRgNKIAMIFQEpm 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 97 FNLFPhLDLVQNCILAPMSV-RGMSRRAAEALAVGLLERVRLGEHAHK---YPSQLSGGQQQRAAIARALCMEPRVMLFD 172
Cdd:PRK15134 103 VSLNP-LHTLEKQLYEVLSLhRGMRREAARGEILNCLDRVGIRQAAKRltdYPHQLSGGERQRVMIAMALLTRPELLIAD 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 500071467 173 EPTSALDPEMVGEVLDTMRGLAAE-GMTMMIVTHEMGFARQVADRVVFMDRGQIVEQAPPAAFFGAPVHERTRRFL 247
Cdd:PRK15134 182 EPTTALDVSVQAQILQLLRELQQElNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAATLFSAPTHPYTQKLL 257
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
27-228 |
7.58e-35 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 124.54 E-value: 7.58e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 27 VLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIELGQSENAAQA-VR-REVGMVFQHFNLFPHLD 104
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAeLRnQKLGFIYQFHHLLPDFT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 105 LVQNcILAPMSVRGMSRRAAEALAVGLLERVRLGEHAHKYPSQLSGGQQQRAAIARALCMEPRVMLFDEPTSALDPEMVG 184
Cdd:PRK11629 104 ALEN-VAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNAD 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 500071467 185 EVLDTMRGL-AAEGMTMMIVTHEMGFARQVaDRVVFMDRGQIVEQ 228
Cdd:PRK11629 183 SIFQLLGELnRLQGTAFLVVTHDLQLAKRM-SRQLEMRDGRLTAE 226
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
28-236 |
1.01e-34 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 125.61 E-value: 1.01e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 28 LTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIELgqSENAAQAVRREVGMVFQH-FNLFPHLDlV 106
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLL--TEENVWDIRHKIGMVFQNpDNQFVGAT-V 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 107 QNCILAPMSVRGMSRRAAEALAVGLLERVRLGEHAHKYPSQLSGGQQQRAAIARALCMEPRVMLFDEPTSALDPEMVGEV 186
Cdd:PRK13650 100 EDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLEL 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 500071467 187 LDTMRGLAAE-GMTMMIVTHEMGfarQVA--DRVVFMDRGQIVEQAPPAAFFG 236
Cdd:PRK13650 180 IKTIKGIRDDyQMTVISITHDLD---EVAlsDRVLVMKNGQVESTSTPRELFS 229
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
8-228 |
1.35e-34 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 124.65 E-value: 1.35e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 8 PAAPIISVAGVNKWYGAFQVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIELGQSENAA--QA 85
Cdd:PRK11701 2 MDQPLLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYAlsEA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 86 VRR-----EVGMVFQHF--NLFPHLDLVQNCILAPMSVRGMSRRAAEALAVGLLERV-----RLGEHahkyPSQLSGGQQ 153
Cdd:PRK11701 82 ERRrllrtEWGFVHQHPrdGLRMQVSAGGNIGERLMAVGARHYGDIRATAGDWLERVeidaaRIDDL----PTTFSGGMQ 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 500071467 154 QRAAIARALCMEPRVMLFDEPTSALDPEMVGEVLDTMRGLAAE-GMTMMIVTHEMGFARQVADRVVFMDRGQIVEQ 228
Cdd:PRK11701 158 QRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRElGLAVVIVTHDLAVARLLAHRLLVMKQGRVVES 233
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
25-236 |
1.38e-34 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 125.28 E-value: 1.38e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 25 FQVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIELGQS--ENAAQAVRREVGMVFQhfnlFPH 102
Cdd:PRK13646 20 HQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKtkDKYIRPVRKRIGMVFQ----FPE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 103 LDLVQN-----CILAPMSVrGMSRRAAEALAVGLLerVRLG---EHAHKYPSQLSGGQQQRAAIARALCMEPRVMLFDEP 174
Cdd:PRK13646 96 SQLFEDtvereIIFGPKNF-KMNLDEVKNYAHRLL--MDLGfsrDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEP 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 500071467 175 TSALDPEMVGEVLDTMRGLAAE-GMTMMIVTHEMGFARQVADRVVFMDRGQIVEQAPPAAFFG 236
Cdd:PRK13646 173 TAGLDPQSKRQVMRLLKSLQTDeNKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFK 235
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
4-220 |
1.40e-34 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 129.71 E-value: 1.40e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 4 PDASPAAPIISVAGVNKWY-GAFQVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIELGQSEna 82
Cdd:TIGR02857 313 PVTAAPASSLEFSGVSVAYpGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADAD-- 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 83 AQAVRREVGMVFQHFNLFPHlDLVQNCILA-PMSVRGMSRRAAEAlaVGLLERV---------RLGEHahkyPSQLSGGQ 152
Cdd:TIGR02857 391 ADSWRDQIAWVPQHPFLFAG-TIAENIRLArPDASDAEIREALER--AGLDEFVaalpqgldtPIGEG----GAGLSGGQ 463
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 500071467 153 QQRAAIARALCMEPRVMLFDEPTSALDPEMVGEVLDTMRGLaAEGMTMMIVTHEMGFARqVADRVVFM 220
Cdd:TIGR02857 464 AQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRAL-AQGRTVLLVTHRLALAA-LADRIVVL 529
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
27-228 |
1.85e-34 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 123.75 E-value: 1.85e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 27 VLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIELGQSENAAqaVRREVGMVFQHFNLFpHLDLV 106
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAW--LRRQVGVVLQENVLF-NRSIR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 107 QNCILAPmsvRGMSRRAAEALA--VGLLERVR---------LGEHAhkypSQLSGGQQQRAAIARALCMEPRVMLFDEPT 175
Cdd:cd03252 94 DNIALAD---PGMSMERVIEAAklAGAHDFISelpegydtiVGEQG----AGLSGGQRQRIAIARALIHNPRILIFDEAT 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 500071467 176 SALDPEMVGEVLDTMRGLAAeGMTMMIVTHEMGFARQvADRVVFMDRGQIVEQ 228
Cdd:cd03252 167 SALDYESEHAIMRNMHDICA-GRTVIIIAHRLSTVKN-ADRIIVMEKGRIVEQ 217
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
12-226 |
2.20e-34 |
|
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: 122.86 E-value: 2.20e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 12 IISVAGVNKWYGA----FQVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIELGQSEnaaQAVR 87
Cdd:cd03266 1 MITADALTKRFRDvkktVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEP---AEAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 88 REVGMVFQHFNLFPHLDLVQNcILAPMSVRGMSRRAAEALAVGLLERVRLGEHAHKYPSQLSGGQQQRAAIARALCMEPR 167
Cdd:cd03266 78 RRLGFVSDSTGLYDRLTAREN-LEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPP 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 500071467 168 VMLFDEPTSALDPEMVGEVLDTMRGLAAEGMTMMIVTHEMGFARQVADRVVFMDRGQIV 226
Cdd:cd03266 157 VLLLDEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVV 215
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
10-232 |
3.41e-34 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 124.92 E-value: 3.41e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 10 APIISVAGVNKWYGAFQVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIELGQsenAAQAVRRE 89
Cdd:PRK13537 5 VAPIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPS---RARHARQR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 90 VGMVFQHFNLFPHLDLVQNcILAPMSVRGMSRRAAEALAVGLLERVRLGEHAHKYPSQLSGGQQQRAAIARALCMEPRVM 169
Cdd:PRK13537 82 VGVVPQFDNLDPDFTVREN-LLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 500071467 170 LFDEPTSALDPEMVGEVLDTMRGLAAEGMTMMIVTHEMGFARQVADRVVFMDRG-QIVEQAPPA 232
Cdd:PRK13537 161 VLDEPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGrKIAEGAPHA 224
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
11-247 |
3.47e-34 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 123.61 E-value: 3.47e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 11 PIISVAGVNKWYGAFQVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQhQEGSIVVDG-IEL-GQSENAAQA--- 85
Cdd:PRK14258 6 PAIKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNE-LESEVRVEGrVEFfNQNIYERRVnln 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 86 -VRREVGMVFQHFNLFPhLDLVQNCILAPMSVRGMSRRAAEALAVGLLERVRLGEHA----HKYPSQLSGGQQQRAAIAR 160
Cdd:PRK14258 85 rLRRQVSMVHPKPNLFP-MSVYDNVAYGVKIVGWRPKLEIDDIVESALKDADLWDEIkhkiHKSALDLSGGQQQRLCIAR 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 161 ALCMEPRVMLFDEPTSALDP--EMVGEVLDTMRGLAAEgMTMMIVTHEMGFARQVADRVVFMDR-----GQIVEQAPPAA 233
Cdd:PRK14258 164 ALAVKPKVLLMDEPCFGLDPiaSMKVESLIQSLRLRSE-LTMVIVSHNLHQVSRLSDFTAFFKGnenriGQLVEFGLTKK 242
|
250
....*....|....
gi 500071467 234 FFGAPVHERTRRFL 247
Cdd:PRK14258 243 IFNSPHDSRTREYV 256
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
25-232 |
3.80e-34 |
|
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: 122.72 E-value: 3.80e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 25 FQVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIELgqSENAAQAVRREVGMVFQHFNLFpHLD 104
Cdd:cd03253 14 RPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDI--REVTLDSLRRAIGVVPQDTVLF-NDT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 105 LVQNCILAPMSVRGMSRRAAeALAVGLLERV---------RLGEHAHKypsqLSGGQQQRAAIARALCMEPRVMLFDEPT 175
Cdd:cd03253 91 IGYNIRYGRPDATDEEVIEA-AKAAQIHDKImrfpdgydtIVGERGLK----LSGGEKQRVAIARAILKNPPILLLDEAT 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 500071467 176 SALDPEMVGEVLDTMRGLAAeGMTMMIVTHEMgfaRQV--ADRVVFMDRGQIVEQAPPA 232
Cdd:cd03253 166 SALDTHTEREIQAALRDVSK-GRTTIVIAHRL---STIvnADKIIVLKDGRIVERGTHE 220
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
26-228 |
4.07e-34 |
|
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: 129.48 E-value: 4.07e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 26 QVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIELGQSENAAqaVRREVGMVFQHFNLFPHLDL 105
Cdd:TIGR01846 471 EVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPAW--LRRQMGVVLQENVLFSRSIR 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 106 VQNCILAP-MSVRGMSRRAAEALAVGLLERVR------LGEHAhkypSQLSGGQQQRAAIARALCMEPRVMLFDEPTSAL 178
Cdd:TIGR01846 549 DNIALCNPgAPFEHVIHAAKLAGAHDFISELPqgynteVGEKG----ANLSGGQRQRIAIARALVGNPRILIFDEATSAL 624
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 500071467 179 DPEMVGEVLDTMRGLAAeGMTMMIVTHEMGFARQvADRVVFMDRGQIVEQ 228
Cdd:TIGR01846 625 DYESEALIMRNMREICR-GRTVIIIAHRLSTVRA-CDRIIVLEKGQIAES 672
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
13-232 |
6.30e-34 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 122.50 E-value: 6.30e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 13 ISVAGVNKWYGAFQVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIELGQSENAAQAvrREVGM 92
Cdd:COG4604 2 IEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELA--KRLAI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 93 VFQ--HFNL------------FPHldlvqncilapmsvrgmSR-------RAAEALAVGLLErvrLGEHAHKYPSQLSGG 151
Cdd:COG4604 80 LRQenHINSrltvrelvafgrFPY-----------------SKgrltaedREIIDEAIAYLD---LEDLADRYLDELSGG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 152 QQQRAAIARALCMEPRVMLFDEPTSALDPEMVGEVLDTMRGLAAE-GMTMMIVTHEMGFARQVADRVVFMDRGQIVEQAP 230
Cdd:COG4604 140 QRQRAFIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADElGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGT 219
|
..
gi 500071467 231 PA 232
Cdd:COG4604 220 PE 221
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
27-239 |
1.20e-33 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 122.99 E-value: 1.20e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 27 VLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQL---EQHQEGSIVVDGIELGqsENAAQAVRREVGMVFQH-FNLFPH 102
Cdd:PRK13640 22 ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLllpDDNPNSKITVDGITLT--AKTVWDIREKVGIVFQNpDNQFVG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 103 LDlVQNCILAPMSVRGMSRRAAEALAVGLLERVRLGEHAHKYPSQLSGGQQQRAAIARALCMEPRVMLFDEPTSALDPEM 182
Cdd:PRK13640 100 AT-VGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAG 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 500071467 183 VGEVLDTMRGLAAE-GMTMMIVTHEMGFARQvADRVVFMDRGQIVEQAPPAAFFGAPV 239
Cdd:PRK13640 179 KEQILKLIRKLKKKnNLTVISITHDIDEANM-ADQVLVLDDGKLLAQGSPVEIFSKVE 235
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
10-251 |
2.26e-33 |
|
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: 121.48 E-value: 2.26e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 10 APIISVAGVNKWYGAFQVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIELGQSE--NAAQAVR 87
Cdd:TIGR02323 1 KPLLQVSGLSKSYGGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMRSGAELElyQLSEAER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 88 R-----EVGMVFQHfnlfPHLDLvqncilaPMSVRGMSRRAAEALAVGLLERVRLGEHAHKY--------------PSQL 148
Cdd:TIGR02323 81 RrlmrtEWGFVHQN----PRDGL-------RMRVSAGANIGERLMAIGARHYGNIRATAQDWleeveidptriddlPRAF 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 149 SGGQQQRAAIARALCMEPRVMLFDEPTSALDPEMVGEVLDTMRGLAAE-GMTMMIVTHEMGFARQVADRVVFMDRGQIVE 227
Cdd:TIGR02323 150 SGGMQQRLQIARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDlGLAVIIVTHDLGVARLLAQRLLVMQQGRVVE 229
|
250 260
....*....|....*....|....
gi 500071467 228 QAPPAAFFGAPVHERTRRFLSQIL 251
Cdd:TIGR02323 230 SGLTDQVLDDPQHPYTQLLVSSIL 253
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
26-231 |
3.26e-33 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 120.02 E-value: 3.26e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 26 QVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIELGQSENAaqAVRREVGMVFQHFNLFPHlDL 105
Cdd:cd03254 17 PVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRK--SLRSMIGVVLQDTFLFSG-TI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 106 VQNCILAPMSVRgMSRRAAEALAVGLLERVR---------LGEHAHkypsQLSGGQQQRAAIARALCMEPRVMLFDEPTS 176
Cdd:cd03254 94 MENIRLGRPNAT-DEEVIEAAKEAGAHDFIMklpngydtvLGENGG----NLSQGERQLLAIARAMLRDPKILILDEATS 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 500071467 177 ALDPEMVGEVLDTMRGLaAEGMTMMIVTHEMGFARQvADRVVFMDRGQIVEQAPP 231
Cdd:cd03254 169 NIDTETEKLIQEALEKL-MKGRTSIIIAHRLSTIKN-ADKILVLDDGKIIEEGTH 221
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
2-226 |
4.09e-33 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 125.13 E-value: 4.09e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 2 PNPDASPAAPIISVAGVNKWygafQVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIELGQSeN 81
Cdd:COG1129 246 PKRAAAPGEVVLEVEGLSVG----GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIR-S 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 82 AAQAVRRevGMVF-----QHFNLFPHLDLVQNCILAPMSVRG----MSRRAAEALAVGLLERVRLgehahKYPS------ 146
Cdd:COG1129 321 PRDAIRA--GIAYvpedrKGEGLVLDLSIRENITLASLDRLSrgglLDRRRERALAEEYIKRLRI-----KTPSpeqpvg 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 147 QLSGGQQQRAAIARALCMEPRVMLFDEPTSALDpemVG---EVLDTMRGLAAEGMTMMIVTHEMGFARQVADRVVFMDRG 223
Cdd:COG1129 394 NLSGGNQQKVVLAKWLATDPKVLILDEPTRGID---VGakaEIYRLIRELAAEGKAVIVISSELPELLGLSDRILVMREG 470
|
...
gi 500071467 224 QIV 226
Cdd:COG1129 471 RIV 473
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
26-228 |
1.00e-32 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 119.18 E-value: 1.00e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 26 QVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIELgqSENAAQAVRREVGMVFQHFNLFphldl 105
Cdd:cd03249 17 PILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDI--RDLNLRWLRSQIGLVSQEPVLF----- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 106 vqNCILA--------PMSVRGMSRRAAEALA----VGLLER--VRLGEHAhkypSQLSGGQQQRAAIARALCMEPRVMLF 171
Cdd:cd03249 90 --DGTIAenirygkpDATDEEVEEAAKKANIhdfiMSLPDGydTLVGERG----SQLSGGQKQRIAIARALLRNPKILLL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 172 DEPTSALDPE---MVGEVLDTmrglAAEGMTMMIVTHEMGfARQVADRVVFMDRGQIVEQ 228
Cdd:cd03249 164 DEATSALDAEsekLVQEALDR----AMKGRTTIVIAHRLS-TIRNADLIAVLQNGQVVEQ 218
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
2-248 |
1.62e-32 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 124.05 E-value: 1.62e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 2 PNPDASPAAPIISVAGVNKWY-----------GAFQVLTDVSLSVARGEKVVICGPSGSGKST----LIRCLNQleqhqE 66
Cdd:PRK15134 265 PVPLPEPASPLLDVEQLQVAFpirkgilkrtvDHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLINS-----Q 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 67 GSIVVDGIELGQ-SENAAQAVRREVGMVFQHFN--LFPHLDlVQNCILAPMSV--RGMSRRAAEALAVGLLERVRLG-EH 140
Cdd:PRK15134 340 GEIWFDGQPLHNlNRRQLLPVRHRIQVVFQDPNssLNPRLN-VLQIIEEGLRVhqPTLSAAQREQQVIAVMEEVGLDpET 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 141 AHKYPSQLSGGQQQRAAIARALCMEPRVMLFDEPTSALDPEMVGEVLDTMRGLAAE-GMTMMIVTHEMGFARQVADRVVF 219
Cdd:PRK15134 419 RHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKhQLAYLFISHDLHVVRALCHQVIV 498
|
250 260
....*....|....*....|....*....
gi 500071467 220 MDRGQIVEQAPPAAFFGAPVHERTRRFLS 248
Cdd:PRK15134 499 LRQGEVVEQGDCERVFAAPQQEYTRQLLA 527
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
22-231 |
3.35e-32 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 118.26 E-value: 3.35e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 22 YGAFQVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIelgqsenAAQAVRREVGMVFQHFNLFP 101
Cdd:PRK11248 11 YGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGK-------PVEGPGAERGVVFQNEGLLP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 102 HLDLVQNCILApMSVRGMSRRAAEALAVGLLERVRLGEHAHKYPSQLSGGQQQRAAIARALCMEPRVMLFDEPTSALDP- 180
Cdd:PRK11248 84 WRNVQDNVAFG-LQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAf 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 500071467 181 --EMVGEVLdtMRGLAAEGMTMMIVTHEMGFARQVADRVVFM--DRGQIVEQAPP 231
Cdd:PRK11248 163 trEQMQTLL--LKLWQETGKQVLLITHDIEEAVFMATELVLLspGPGRVVERLPL 215
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
30-250 |
7.91e-32 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 119.04 E-value: 7.91e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 30 DVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIEL-GQSENAAQAVRREVGMVFQH--FNLFPHLDlV 106
Cdd:PRK15079 39 GVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLlGMKDDEWRAVRSDIQMIFQDplASLNPRMT-I 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 107 QNCILAPMSVR--GMSRRA------AEALAVGLLERVrlgehAHKYPSQLSGGQQQRAAIARALCMEPRVMLFDEPTSAL 178
Cdd:PRK15079 118 GEIIAEPLRTYhpKLSRQEvkdrvkAMMLKVGLLPNL-----INRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSAL 192
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 500071467 179 DPEMVGEVLDTMRGLAAE-GMTMMIVTHEMGFARQVADRVVFMDRGQIVEQAPPAAFFGAPVHERTRRFLSQI 250
Cdd:PRK15079 193 DVSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNPLHPYTKALMSAV 265
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
23-238 |
3.41e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 116.44 E-value: 3.41e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 23 GAFQVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGiELGQSENAAQaVRREVGMVFQH-----F 97
Cdd:PRK13652 15 GSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRG-EPITKENIRE-VRKFVGLVFQNpddqiF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 98 NLFPHLDLVQNCILAPMSVRGMSRRAAEALAVGLLERVRlgehaHKYPSQLSGGQQQRAAIARALCMEPRVMLFDEPTSA 177
Cdd:PRK13652 93 SPTVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELR-----DRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAG 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 500071467 178 LDPEMVGEVLDTMRGLAAE-GMTMMIVTHEMGFARQVADRVVFMDRGQIVEQAPPAAFFGAP 238
Cdd:PRK13652 168 LDPQGVKELIDFLNDLPETyGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
13-232 |
8.48e-31 |
|
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: 113.79 E-value: 8.48e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 13 ISVAGVNKWYGAFQVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIELGQSENAAQAvRREVGM 92
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRA-RLGIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 93 VFQHFNLFPHLDLVQNcILAPMSVRGMSRRAAEALAVGLLERVRLGEHAHKYPSQLSGGQQQRAAIARALCMEPRVMLFD 172
Cdd:cd03218 80 LPQEASIFRKLTVEEN-ILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLD 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 173 EPTSALDPEMVGEVLDTMRGLAAEGMTMMIVTHEMGFARQVADRVVFMDRGQIVEQAPPA 232
Cdd:cd03218 159 EPFAGVDPIAVQDIQKIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPE 218
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1-250 |
2.95e-30 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 118.42 E-value: 2.95e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 1 MPNPDASPAAPIISVAGVNKWY----GAFQVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDG--- 73
Cdd:PRK10261 1 MPHSDELDARDVLAVENLNIAFmqeqQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKmll 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 74 -------IELG-QSENAAQAVR-REVGMVFQH--FNLFPHLDLVQNCILAPMSVRGMSRRAAEALAVGLLERVRLGEHA- 141
Cdd:PRK10261 81 rrrsrqvIELSeQSAAQMRHVRgADMAMIFQEpmTSLNPVFTVGEQIAESIRLHQGASREEAMVEAKRMLDQVRIPEAQt 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 142 --HKYPSQLSGGQQQRAAIARALCMEPRVMLFDEPTSALDPEMVGEVLDTMRGLAAE-GMTMMIVTHEMGFARQVADRVV 218
Cdd:PRK10261 161 ilSRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEmSMGVIFITHDMGVVAEIADRVL 240
|
250 260 270
....*....|....*....|....*....|..
gi 500071467 219 FMDRGQIVEQAPPAAFFGAPVHERTRRFLSQI 250
Cdd:PRK10261 241 VMYQGEAVETGSVEQIFHAPQHPYTRALLAAV 272
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
11-227 |
3.99e-30 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 117.09 E-value: 3.99e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 11 PIISVAGVNKWYGAFQVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSivvdgIELGQSenaaqaVRreV 90
Cdd:COG0488 314 KVLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGT-----VKLGET------VK--I 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 91 GMVFQHF-NLFPHLDLVQNcilapmsVRGMSRRAAEALAVGLLERVRL-GEHAHKYPSQLSGGQQQRAAIARALCMEPRV 168
Cdd:COG0488 381 GYFDQHQeELDPDKTVLDE-------LRDGAPGGTEQEVRGYLGRFLFsGDDAFKPVGVLSGGEKARLALAKLLLSPPNV 453
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 169 MLFDEPTSALDPEMVgEVLdtMRGLAA-EGmTMMIVTHEMGFARQVADRVVFMDRGQIVE 227
Cdd:COG0488 454 LLLDEPTNHLDIETL-EAL--EEALDDfPG-TVLLVSHDRYFLDRVATRILEFEDGGVRE 509
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
11-232 |
4.00e-30 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 112.43 E-value: 4.00e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 11 PIISVAGVNKWYGAFQVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIELGQ---SENAaqavR 87
Cdd:COG1137 2 MTLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHlpmHKRA----R 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 88 REVGMVFQHFNLFPHLDLVQNcILAPMSVRGMSRRAAEALAVGLLERVRLGEHAHKYPSQLSGGQQQRAAIARALCMEPR 167
Cdd:COG1137 78 LGIGYLPQEASIFRKLTVEDN-ILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPK 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 500071467 168 VMLFDEPTSALDPEMVGEVLDTMRGLAAEGMTMMIVTHEmgfAR---QVADRVVFMDRGQIVEQAPPA 232
Cdd:COG1137 157 FILLDEPFAGVDPIAVADIQKIIRHLKERGIGVLITDHN---VRetlGICDRAYIISEGKVLAEGTPE 221
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
11-232 |
5.09e-30 |
|
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: 117.21 E-value: 5.09e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 11 PIISVAGVNKWY-----GAFQVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIV-------VDGIELGQ 78
Cdd:TIGR03269 278 PIIKVRNVSKRYisvdrGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNvrvgdewVDMTKPGP 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 79 SENAAqaVRREVGMVFQHFNLFPHLDLVQN---CILAPMSVRGMSRRAAEALAVGLLERVRLGEHAHKYPSQLSGGQQQR 155
Cdd:TIGR03269 358 DGRGR--AKRYIGILHQEYDLYPHRTVLDNlteAIGLELPDELARMKAVITLKMVGFDEEKAEEILDKYPDELSEGERHR 435
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 500071467 156 AAIARALCMEPRVMLFDEPTSALDPEMVGEVLDTMRGLAAE-GMTMMIVTHEMGFARQVADRVVFMDRGQIVEQAPPA 232
Cdd:TIGR03269 436 VALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEmEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPE 513
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
22-218 |
5.29e-30 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 110.79 E-value: 5.29e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 22 YGAFQVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGielgqsenaaqavRREVGMVFQHFNLFP 101
Cdd:NF040873 2 YGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG-------------GARVAYVPQRSEVPD 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 102 HL-----DLVQNCILAPMSVRGMSRRAAEALAVGLLERVRLGEHAHKYPSQLSGGQQQRAAIARALCMEPRVMLFDEPTS 176
Cdd:NF040873 69 SLpltvrDLVAMGRWARRGLWRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTT 148
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 500071467 177 ALDPEMVGEVLDTMRGLAAEGMTMMIVTHEMGFARQvADRVV 218
Cdd:NF040873 149 GLDAESRERIIALLAEEHARGATVVVVTHDLELVRR-ADPCV 189
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
26-235 |
5.97e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 113.02 E-value: 5.97e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 26 QVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIELGQSENAAQAVRREVGMVFQH--FNLFPhL 103
Cdd:PRK13636 20 HALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRKGLMKLRESVGMVFQDpdNQLFS-A 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 104 DLVQNCILAPMSVrGMSRRAAEALAVGLLERVRLGEHAHKYPSQLSGGQQQRAAIARALCMEPRVMLFDEPTSALDPEMV 183
Cdd:PRK13636 99 SVYQDVSFGAVNL-KLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGV 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 500071467 184 GEVLDTMRGLAAE-GMTMMIVTHEMGFARQVADRVVFMDRGQIVEQAPPAAFF 235
Cdd:PRK13636 178 SEIMKLLVEMQKElGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVF 230
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
27-230 |
7.45e-30 |
|
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: 116.74 E-value: 7.45e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 27 VLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIELgqSENAAQAVRREVGMVFQHFNLFPhlDLV 106
Cdd:TIGR02203 347 ALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDL--ADYTLASLRRQVALVSQDVVLFN--DTI 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 107 QNCI----LAPMSVRGMSRRAAEALAVGLLERVRLGEHAH--KYPSQLSGGQQQRAAIARALCMEPRVMLFDEPTSALDP 180
Cdd:TIGR02203 423 ANNIaygrTEQADRAEIERALAAAYAQDFVDKLPLGLDTPigENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDN 502
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 500071467 181 EMVGEVLDTMRGLaAEGMTMMIVTHEMGfARQVADRVVFMDRGQIVEQAP 230
Cdd:TIGR02203 503 ESERLVQAALERL-MQGRTTLVIAHRLS-TIEKADRIVVMDDGRIVERGT 550
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
9-225 |
1.67e-29 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 109.06 E-value: 1.67e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 9 AAPIISVAGVNKWYgafqVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIELGQSeNAAQAVRR 88
Cdd:cd03215 1 GEPVLEVRGLSVKG----AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRR-SPRDAIRA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 89 EVGMV---FQHFNLFPHLDLVQNCILapmsvrgmsrraaealavgllervrlgehahkyPSQLSGGQQQRAAIARALCME 165
Cdd:cd03215 76 GIAYVpedRKREGLVLDLSVAENIAL---------------------------------SSLLSGGNQQKVVLARWLARD 122
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 166 PRVMLFDEPTSALDPEMVGEVLDTMRGLAAEGMTMMIVTHEMGFARQVADRVVFMDRGQI 225
Cdd:cd03215 123 PRVLILDEPTRGVDVGAKAEIYRLIRELADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
27-225 |
2.83e-29 |
|
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: 108.46 E-value: 2.83e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 27 VLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIELGQSenAAQAVRREVGMVFQHFNLFPHldlv 106
Cdd:cd03246 17 VLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQW--DPNELGDHVGYLPQDDELFSG---- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 107 qncilapmSVrgmsrraAEALavgllervrlgehahkypsqLSGGQQQRAAIARALCMEPRVMLFDEPTSALDPEMVGEV 186
Cdd:cd03246 91 --------SI-------AENI--------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERAL 135
|
170 180 190
....*....|....*....|....*....|....*....
gi 500071467 187 LDTMRGLAAEGMTMMIVTHEMGFARQvADRVVFMDRGQI 225
Cdd:cd03246 136 NQAIAALKAAGATRIVIAHRPETLAS-ADRILVLEDGRV 173
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
12-226 |
3.79e-29 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 109.58 E-value: 3.79e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 12 IISVAGVNKWY-GAFQVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIELGQSENA-AQAVRRE 89
Cdd:PRK10908 1 MIRFEHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNReVPFLRRQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 90 VGMVFQHFNLFPHLDLVQNC----ILAPMSVRGMSRRAAEAL-AVGLLERvrlgehAHKYPSQLSGGQQQRAAIARALCM 164
Cdd:PRK10908 81 IGMIFQDHHLLMDRTVYDNVaiplIIAGASGDDIRRRVSAALdKVGLLDK------AKNFPIQLSGGEQQRVGIARAVVN 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 500071467 165 EPRVMLFDEPTSALDPEMVGEVLDTMRGLAAEGMTMMIVTHEMGFARQVADRVVFMDRGQIV 226
Cdd:PRK10908 155 KPAVLLADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHLH 216
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
26-228 |
5.39e-29 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 114.82 E-value: 5.39e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 26 QVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIELGQSENaaQAVRREVGMVFQHFNLFPHldL 105
Cdd:TIGR00958 495 PVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDH--HYLHRQVALVGQEPVLFSG--S 570
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 106 VQNCIL-----APMS-VRGMSRRAAEALAVGLLER---VRLGEHAhkypSQLSGGQQQRAAIARALCMEPRVMLFDEPTS 176
Cdd:TIGR00958 571 VRENIAygltdTPDEeIMAAAKAANAHDFIMEFPNgydTEVGEKG----SQLSGGQKQRIAIARALVRKPRVLILDEATS 646
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 500071467 177 ALDPEMVGEVLDTMRglaAEGMTMMIVTHEMGFARQvADRVVFMDRGQIVEQ 228
Cdd:TIGR00958 647 ALDAECEQLLQESRS---RASRTVLLIAHRLSTVER-ADQILVLKKGSVVEM 694
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
30-248 |
5.91e-29 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 109.79 E-value: 5.91e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 30 DVSLSVARGEKVVICGPSGSGKStlIRCLNQLE------QHQEGSIVVDGIELgqsenAAQAVR-REVGMVFQH----FN 98
Cdd:PRK10418 21 GVSLTLQRGRVLALVGGSGSGKS--LTCAAALGilpagvRQTAGRVLLDGKPV-----APCALRgRKIATIMQNprsaFN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 99 lfPHLDLVQNCI--LAPMSVRGMSRRAAEAL-AVGLLERVRLgehAHKYPSQLSGGQQQRAAIARALCMEPRVMLFDEPT 175
Cdd:PRK10418 94 --PLHTMHTHARetCLALGKPADDATLTAALeAVGLENAARV---LKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPT 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 500071467 176 SALDPEMVGEVLDTMRGLAAE-GMTMMIVTHEMGFARQVADRVVFMDRGQIVEQAPPAAFFGAPVHERTRRFLS 248
Cdd:PRK10418 169 TDLDVVAQARILDLLESIVQKrALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPKHAVTRSLVS 242
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
26-228 |
7.48e-29 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 107.40 E-value: 7.48e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 26 QVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIELGQSENAaqaVRREVGMVFQHFNLFpHLDL 105
Cdd:cd03247 16 QVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKA---LSSLISVLNQRPYLF-DTTL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 106 VQNcilapmsvrgmsrraaealavgllervrLGEhahkypsQLSGGQQQRAAIARALCMEPRVMLFDEPTSALDPEMVGE 185
Cdd:cd03247 92 RNN----------------------------LGR-------RFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQ 136
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 500071467 186 VLDTMRGlAAEGMTMMIVTHEM-GFARqvADRVVFMDRGQIVEQ 228
Cdd:cd03247 137 LLSLIFE-VLKDKTLIWITHHLtGIEH--MDKILFLENGKIIMQ 177
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
25-235 |
1.12e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 110.10 E-value: 1.12e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 25 FQVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIELGQSENAAQAV---RREVGMVFQhfnlFP 101
Cdd:PRK13645 24 FKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPANLKKIKEVkrlRKEIGLVFQ----FP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 102 HLDLVQNCI-----LAPMSVrGMSRRAAEALAVGLLERVRLG-EHAHKYPSQLSGGQQQRAAIARALCMEPRVMLFDEPT 175
Cdd:PRK13645 100 EYQLFQETIekdiaFGPVNL-GENKQEAYKKVPELLKLVQLPeDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPT 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 500071467 176 SALDPEMVGEVLDTMRGLAAE-GMTMMIVTHEMGFARQVADRVVFMDRGQIVEQAPPAAFF 235
Cdd:PRK13645 179 GGLDPKGEEDFINLFERLNKEyKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIF 239
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
16-226 |
1.40e-28 |
|
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: 108.13 E-value: 1.40e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 16 AGVNKWYGAFQVLTDVSLSVARGEKVVICGPSGSGKSTL---IRCLNQLEQHQEGSIVVDGielgqSENAAQAVRREVGM 92
Cdd:cd03234 11 LKAKNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLldaISGRVEGGGTTSGQILFNG-----QPRKPDQFQKCVAY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 93 VFQHFNLFPHLDLVQN---CILAPMSVRGMSRRAAEALAVGLLERVRLGEHAHKYPSQLSGGQQQRAAIARALCMEPRVM 169
Cdd:cd03234 86 VRQDDILLPGLTVRETltyTAILRLPRKSSDAIRKKRVEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 170 LFDEPTSALDPEMVGEVLDTMRGLAAEGMTMMIVTHEMG---FarQVADRVVFMDRGQIV 226
Cdd:cd03234 166 ILDEPTSGLDSFTALNLVSTLSQLARRNRIVILTIHQPRsdlF--RLFDRILLLSSGEIV 223
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
22-250 |
2.65e-28 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 108.18 E-value: 2.65e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 22 YGAFQVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIELGQSenAAQAVRREVGMVFQHfNLFP 101
Cdd:PRK11231 12 YGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISML--SSRQLARRLALLPQH-HLTP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 102 HLDLVQNCIL---AP-MSVRGMSRRAAEALAVGLLERVRLGEHAHKYPSQLSGGQQQRAAIARALCMEPRVMLFDEPTSA 177
Cdd:PRK11231 89 EGITVRELVAygrSPwLSLWGRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTY 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 500071467 178 LDPEMVGEVLDTMRGLAAEGMTMMIVTHEMGFARQVADRVVFMDRGQIVEQappaaffGAPVHERTRRFLSQI 250
Cdd:PRK11231 169 LDINHQVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQ-------GTPEEVMTPGLLRTV 234
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
15-225 |
2.77e-28 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 112.08 E-value: 2.77e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 15 VAGVNKWYGAFQVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVD-GIELG-----QSENAAQAVRR 88
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPkGLRIGylpqePPLDDDLTVLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 89 EVGMVFQH-FNLFPHLDLVQNciLAPMSVRGMSRRA-------------AEALAVGLLERVRLGEHAHKYP-SQLSGGQQ 153
Cdd:COG0488 81 TVLDGDAElRALEAELEELEA--KLAEPDEDLERLAelqeefealggweAEARAEEILSGLGFPEEDLDRPvSELSGGWR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 500071467 154 QRAAIARALCMEPRVMLFDEPTSALDPEMVG---EVLDTMRGlaaegmTMMIVTHEMGFARQVADRVVFMDRGQI 225
Cdd:COG0488 159 RRVALARALLSEPDLLLLDEPTNHLDLESIEwleEFLKNYPG------TVLVVSHDRYFLDRVATRILELDRGKL 227
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
10-232 |
2.89e-28 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 107.47 E-value: 2.89e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 10 APIISVAGVNKWY----------------------GAFQVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEG 67
Cdd:COG1134 2 SSMIEVENVSKSYrlyhepsrslkelllrrrrtrrEEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 68 SIVVDG-----IELGqsenaaqavrreVGMVfqhfnlfPHLDLVQNCILApMSVRGMSRRAAEAlavgLLERVR----LG 138
Cdd:COG1134 82 RVEVNGrvsalLELG------------AGFH-------PELTGRENIYLN-GRLLGLSRKEIDE----KFDEIVefaeLG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 139 EHAHK----YPSqlsgGQQQRAAIARALCMEPRVMLFDEPTSALDPEMVGEVLDTMRGLAAEGMTMMIVTHEMGFARQVA 214
Cdd:COG1134 138 DFIDQpvktYSS----GMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRESGRTVIFVSHSMGAVRRLC 213
|
250
....*....|....*...
gi 500071467 215 DRVVFMDRGQIVEQAPPA 232
Cdd:COG1134 214 DRAIWLEKGRLVMDGDPE 231
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
9-233 |
3.03e-28 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 107.77 E-value: 3.03e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 9 AAPIISVAGVNKWYGAFQVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIEL-GQSenaAQAVR 87
Cdd:PRK11300 2 SQPLLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIeGLP---GHQIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 88 REvGMV--FQHFNLFPHLDLVQNCILAP------------MSVRGMSRRAAEAL--AVGLLERVRLGEHAHKYPSQLSGG 151
Cdd:PRK11300 79 RM-GVVrtFQHVRLFREMTVIENLLVAQhqqlktglfsglLKTPAFRRAESEALdrAATWLERVGLLEHANRQAGNLAYG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 152 QQQRAAIARALCMEPRVMLFDEPTSALDPEMVGEVLDTMRGLAAE-GMTMMIVTHEMGFARQVADRVVFMDRGQIVEQAP 230
Cdd:PRK11300 158 QQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEhNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGT 237
|
...
gi 500071467 231 PAA 233
Cdd:PRK11300 238 PEE 240
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
3-229 |
3.16e-28 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 112.23 E-value: 3.16e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 3 NPDASPAAPIISVAGVNKWY--GAFQVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIELGQ-S 79
Cdd:PRK11160 329 TSTAAADQVSLTLNNVSFTYpdQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADyS 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 80 EnaaQAVRREVGMVFQHFNLFPHlDLVQNCILApmsvrgmSRRAAEALAVGLLERVRLGEHAHKYPS----------QLS 149
Cdd:PRK11160 409 E---AALRQAISVVSQRVHLFSA-TLRDNLLLA-------APNASDEALIEVLQQVGLEKLLEDDKGlnawlgeggrQLS 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 150 GGQQQRAAIARALCMEPRVMLFDEPTSALDPEMVGEVLDTMRGLAAeGMTMMIVTHEMGFARQVaDRVVFMDRGQIVEQA 229
Cdd:PRK11160 478 GGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQ-NKTVLMITHRLTGLEQF-DRICVMDNGQIIEQG 555
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
26-228 |
3.32e-28 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 112.36 E-value: 3.32e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 26 QVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIELgqSENAAQAVRREVGMVFQHFNLFPHlDL 105
Cdd:PRK13657 349 QGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDI--RTVTRASLRRNIAVVFQDAGLFNR-SI 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 106 VQNCILA-PMSVRGMSRRAAE-ALAVGLLER--VRLGEHAHKYPSQLSGGQQQRAAIARALCMEPRVMLFDEPTSALDPE 181
Cdd:PRK13657 426 EDNIRVGrPDATDEEMRAAAErAQAHDFIERkpDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVE 505
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 500071467 182 M---VGEVLDTMRglaaEGMTMMIVTHEMGFARQvADRVVFMDRGQIVEQ 228
Cdd:PRK13657 506 TeakVKAALDELM----KGRTTFIIAHRLSTVRN-ADRILVFDNGRVVES 550
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
11-226 |
3.48e-28 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 107.27 E-value: 3.48e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 11 PIISVAGVNKWYGAFQVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIELGQSENAaQAVRREV 90
Cdd:PRK11614 4 VMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTA-KIMREAV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 91 GMVFQHFNLFPHLDLVQNCILAPMSVRGMSRRAAEALAVGLLERvrLGEHAHKYPSQLSGGQQQRAAIARALCMEPRVML 170
Cdd:PRK11614 83 AIVPEGRRVFSRMTVEENLAMGGFFAERDQFQERIKWVYELFPR--LHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 500071467 171 FDEPTSALDPEMVGEVLDTMRGLAAEGMTMMIVTHEMGFARQVADRVVFMDRGQIV 226
Cdd:PRK11614 161 LDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHVV 216
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
28-236 |
5.36e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 107.87 E-value: 5.36e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 28 LTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIELgQSENAAQaVRREVGMVFQHFNLFPHLDLVQ 107
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELL-TAENVWN-LRRKIGMVFQNPDNQFVGATVE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 108 NCILAPMSVRGMSR-----RAAEAL-AVGLLErvrlgeHAHKYPSQLSGGQQQRAAIARALCMEPRVMLFDEPTSALDPE 181
Cdd:PRK13642 101 DDVAFGMENQGIPReemikRVDEALlAVNMLD------FKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPT 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 500071467 182 MVGEVLDTMRGLAAE-GMTMMIVTHEMGFARQvADRVVFMDRGQIVEQAPPAAFFG 236
Cdd:PRK13642 175 GRQEIMRVIHEIKEKyQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELFA 229
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
26-228 |
8.78e-28 |
|
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: 111.07 E-value: 8.78e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 26 QVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIELgqSENAAQAVRREVGMVFQH---FNlfph 102
Cdd:COG5265 372 PILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDI--RDVTQASLRAAIGIVPQDtvlFN---- 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 103 lDLVQNCIL-----APMS-VRGMSRRAA-----EALAVGLLERVrlGEHAHKypsqLSGGQQQRAAIARALCMEPRVMLF 171
Cdd:COG5265 446 -DTIAYNIAygrpdASEEeVEAAARAAQihdfiESLPDGYDTRV--GERGLK----LSGGEKQRVAIARTLLKNPPILIF 518
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 500071467 172 DEPTSALDPEMVGEVLDTMRgLAAEGMTMMIVTHemgfaR----QVADRVVFMDRGQIVEQ 228
Cdd:COG5265 519 DEATSALDSRTERAIQAALR-EVARGRTTLVIAH-----RlstiVDADEILVLEAGRIVER 573
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
30-248 |
1.43e-27 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 106.41 E-value: 1.43e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 30 DVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDG--IELGQSENAAQAVRrevgMVFQ--HFNLFPH--- 102
Cdd:PRK15112 31 PLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDhpLHFGDYSYRSQRIR----MIFQdpSTSLNPRqri 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 103 ---LD--LVQNCILAPMSVRgmsRRAAEAL-AVGLLErvrlgEHAHKYPSQLSGGQQQRAAIARALCMEPRVMLFDEPTS 176
Cdd:PRK15112 107 sqiLDfpLRLNTDLEPEQRE---KQIIETLrQVGLLP-----DHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALA 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 500071467 177 ALDPEMVGEVLDTMRGL-AAEGMTMMIVTHEMGFARQVADRVVFMDRGQIVEQAPPAAFFGAPVHERTRRFLS 248
Cdd:PRK15112 179 SLDMSMRSQLINLMLELqEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVLASPLHELTKRLIA 251
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
9-250 |
2.45e-27 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 106.00 E-value: 2.45e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 9 AAPIISVAGVNKWYGAFQVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIELGQ-SENAAQAVR 87
Cdd:PRK11831 4 VANLVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAmSRSRLYTVR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 88 REVGMVFQHFNLFPHLDLVQNcILAPMsvRGMSRRAAEALAVGL---LERVRLGEHAHKYPSQLSGGQQQRAAIARALCM 164
Cdd:PRK11831 84 KRMSMLFQSGALFTDMNVFDN-VAYPL--REHTQLPAPLLHSTVmmkLEAVGLRGAAKLMPSELSGGMARRAALARAIAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 165 EPRVMLFDEPTSALDPEMVGEVLDTMRGL-AAEGMTMMIVTHEMGFARQVADRVVFMDRGQIVEQAPPAAFFGAPVHeRT 243
Cdd:PRK11831 161 EPDLIMFDEPFVGQDPITMGVLVKLISELnSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQANPDP-RV 239
|
....*..
gi 500071467 244 RRFLSQI 250
Cdd:PRK11831 240 RQFLDGI 246
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
27-231 |
2.91e-27 |
|
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: 104.50 E-value: 2.91e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 27 VLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIELgqSENAAQAVRREVGMVFQ---------HF 97
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDI--SKIGLHDLRSRISIIPQdpvlfsgtiRS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 98 NLFPH-----------LDLVQNcilapmsvrgmsRRAAEALAVGLLERVRLGEhahkypSQLSGGQQQRAAIARALCMEP 166
Cdd:cd03244 97 NLDPFgeysdeelwqaLERVGL------------KEFVESLPGGLDTVVEEGG------ENLSVGQRQLLCLARALLRKS 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 500071467 167 RVMLFDEPTSALDPE---MVGEVLDTMRglaaEGMTMMIVTHE----MGFarqvaDRVVFMDRGQIVEQAPP 231
Cdd:cd03244 159 KILVLDEATASVDPEtdaLIQKTIREAF----KDCTVLTIAHRldtiIDS-----DRILVLDKGRVVEFDSP 221
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
28-235 |
2.92e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 105.60 E-value: 2.92e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 28 LTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIELgqSENAAQAVRREVGMVFQHfnlfPHLDLVQ 107
Cdd:PRK13648 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAI--TDDNFEKLRKHIGIVFQN----PDNQFVG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 108 NCI-------LAPMSV--RGMSRRAAEALavgllERVRLGEHAHKYPSQLSGGQQQRAAIARALCMEPRVMLFDEPTSAL 178
Cdd:PRK13648 99 SIVkydvafgLENHAVpyDEMHRRVSEAL-----KQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSML 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 500071467 179 DPEMVGEVLDTMRGLAAE-GMTMMIVTHEMGFARQvADRVVFMDRGQIVEQAPPAAFF 235
Cdd:PRK13648 174 DPDARQNLLDLVRKVKSEhNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIF 230
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
5-205 |
3.59e-27 |
|
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: 108.99 E-value: 3.59e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 5 DASPAAPIISVAGVN-KWYGAFQVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIELgqSENAA 83
Cdd:TIGR02868 327 AVGLGKPTLELRDLSaGYPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPV--SSLDQ 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 84 QAVRREVGMVFQHFNLFpHLDLVQNCILAPMSVRGmsrraAEALAVglLERVRLGEHAHKYP-----------SQLSGGQ 152
Cdd:TIGR02868 405 DEVRRRVSVCAQDAHLF-DTTVRENLRLARPDATD-----EELWAA--LERVGLADWLRALPdgldtvlgeggARLSGGE 476
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 500071467 153 QQRAAIARALCMEPRVMLFDEPTSALDPEMVGEVLDTMRGlAAEGMTMMIVTH 205
Cdd:TIGR02868 477 RQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLA-ALSGRTVVLITH 528
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
26-225 |
5.43e-27 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 104.09 E-value: 5.43e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 26 QVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIELGQSENaaQAVRREVGMVFQHFNLFPHLdl 105
Cdd:cd03248 28 LVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEH--KYLHSKVSLVGQEPVLFARS-- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 106 VQNCI---LAPMSVRGMSRRAAEALAVGLLERVRLG--EHAHKYPSQLSGGQQQRAAIARALCMEPRVMLFDEPTSALDP 180
Cdd:cd03248 104 LQDNIaygLQSCSFECVKEAAQKAHAHSFISELASGydTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDA 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 500071467 181 EMVGEVLDTMRGlAAEGMTMMIVTHEMGFARQvADRVVFMDRGQI 225
Cdd:cd03248 184 ESEQQVQQALYD-WPERRTVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
43-230 |
5.60e-27 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 106.50 E-value: 5.60e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 43 ICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIELGQSENAAQ--AVRREVGMVFQHFNLFPHldlvqncilapMSVR--- 117
Cdd:PRK11144 29 IFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEKGIClpPEKRRIGYVFQDARLFPH-----------YKVRgnl 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 118 --GMSRRAAEALA--VGLLErvrLGEHAHKYPSQLSGGQQQRAAIARALCMEPRVMLFDEPTSALDPEMVGEVLDTMRGL 193
Cdd:PRK11144 98 ryGMAKSMVAQFDkiVALLG---IEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLERL 174
|
170 180 190
....*....|....*....|....*....|....*...
gi 500071467 194 AAEGMTMMI-VTHEMGFARQVADRVVFMDRGQIVEQAP 230
Cdd:PRK11144 175 AREINIPILyVSHSLDEILRLADRVVVLEQGKVKAFGP 212
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
13-231 |
7.75e-27 |
|
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: 107.97 E-value: 7.75e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 13 ISVAGVNKWYGAFQVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQ--EGSIV-------------------- 70
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQYEptSGRIIyhvalcekcgyverpskvge 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 71 -------------VDGIELgqSENAAQAVRREVGMVFQH-FNLFPHLDLVQNcILAPMSVRGMSRRAAEALAVGLLERVR 136
Cdd:TIGR03269 81 pcpvcggtlepeeVDFWNL--SDKLRRRIRKRIAIMLQRtFALYGDDTVLDN-VLEALEEIGYEGKEAVGRAVDLIEMVQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 137 LGEHAHKYPSQLSGGQQQRAAIARALCMEPRVMLFDEPTSALDPEMVGEVLDTMR-GLAAEGMTMMIVTHEMGFARQVAD 215
Cdd:TIGR03269 158 LSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEeAVKASGISMVLTSHWPEVIEDLSD 237
|
250
....*....|....*.
gi 500071467 216 RVVFMDRGQIVEQAPP 231
Cdd:TIGR03269 238 KAIWLENGEIKEEGTP 253
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
10-238 |
8.81e-27 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 106.85 E-value: 8.81e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 10 APIISVAGVNKWYGAFQVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIELgqSENAAQAVRRE 89
Cdd:PRK09536 1 MPMIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDV--EALSARAASRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 90 VGMVFQHFNLFPHLDLVQNCILAPMSVRGMSRRAAEA--LAV-GLLERVRLGEHAHKYPSQLSGGQQQRAAIARALCMEP 166
Cdd:PRK09536 79 VASVPQDTSLSFEFDVRQVVEMGRTPHRSRFDTWTETdrAAVeRAMERTGVAQFADRPVTSLSGGERQRVLLARALAQAT 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 500071467 167 RVMLFDEPTSALDPEMVGEVLDTMRGLAAEGMTMMIVTHEMGFARQVADRVVFMDRGQIVEQAPPAAFFGAP 238
Cdd:PRK09536 159 PVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVLTAD 230
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
17-227 |
2.01e-26 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 106.80 E-value: 2.01e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 17 GVNKWYGAFQVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQH--QEGSIVVDGIE-----LGQSEnaaqavrrE 89
Cdd:NF040905 6 GITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHgsYEGEILFDGEVcrfkdIRDSE--------A 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 90 VGMVF--QHFNLFPHLDLVQNCILA-PMSVRG-MSRRAAEALAVGLLERVRLGEHAHKYPSQLSGGQQQRAAIARALCME 165
Cdd:NF040905 78 LGIVIihQELALIPYLSIAENIFLGnERAKRGvIDWNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKD 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 500071467 166 PRVMLFDEPTSALDPEMVGEVLDTMRGLAAEGMTMMIVTHEMGFARQVADRVVFMDRGQIVE 227
Cdd:NF040905 158 VKLLILDEPTAALNEEDSAALLDLLLELKAQGITSIIISHKLNEIRRVADSITVLRDGRTIE 219
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
27-226 |
2.89e-26 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 102.86 E-value: 2.89e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 27 VLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIELGQSENAAQAvrREVGMVFQHFNL--FPHLD 104
Cdd:COG1101 21 ALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRA--KYIGRVFQDPMMgtAPSMT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 105 LVQNCILAPMsvRGMSR-------RAAEALAVGLLERVRLG-EHAHKYP-SQLSGGQQQraaiARALCM----EPRVMLF 171
Cdd:COG1101 99 IEENLALAYR--RGKRRglrrgltKKRRELFRELLATLGLGlENRLDTKvGLLSGGQRQ----ALSLLMatltKPKLLLL 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 500071467 172 DEPTSALDPEMVGEVLD-TMRGLAAEGMTMMIVTHEMGFARQVADRVVFMDRGQIV 226
Cdd:COG1101 173 DEHTAALDPKTAALVLElTEKIVEENNLTTLMVTHNMEQALDYGNRLIMMHEGRII 228
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
22-227 |
1.00e-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: 100.30 E-value: 1.00e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 22 YGAFQVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDG-----IELGQSENAAQAVRREVGMVfqh 96
Cdd:cd03220 32 VGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGrvsslLGLGGGFNPELTGRENIYLN--- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 97 fnlfphldlvqncilapMSVRGMSRRAAEALAVGLLERVRLGEHAHKYPSQLSGGQQQRAAIARALCMEPRVMLFDEPTS 176
Cdd:cd03220 109 -----------------GRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLA 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 500071467 177 ALDPEMVGEVLDTMRGLAAEGMTMMIVTHEMGFARQVADRVVFMDRGQIVE 227
Cdd:cd03220 172 VGDAAFQEKCQRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRF 222
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
22-242 |
6.48e-25 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 99.29 E-value: 6.48e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 22 YGAFQVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIELGQSenAAQAVRREVGMVFQHFNLfP 101
Cdd:PRK10253 17 YGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHY--ASKEVARRIGLLAQNATT-P 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 102 HLDLVQNCIL------APMSVRGmsRRAAEALAVGLLERVRLGEHAHKYPSQLSGGQQQRAAIARALCMEPRVMLFDEPT 175
Cdd:PRK10253 94 GDITVQELVArgryphQPLFTRW--RKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPT 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 500071467 176 SALDPEMVGEVLDTMRGLAAE-GMTMMIVTHEMGFARQVADRVVFMDRGQIVEQAPPAAFFGAPVHER 242
Cdd:PRK10253 172 TWLDISHQIDLLELLSELNREkGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVTAELIER 239
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
26-235 |
7.15e-25 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 99.31 E-value: 7.15e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 26 QVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIELGQSENAAQAVRREVGMVFQHfnlfPHLDL 105
Cdd:PRK13638 15 PVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKRGLLALRQQVATVFQD----PEQQI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 106 VQNCILAPM--SVRGM-------SRRAAEALAvgLLErvrlGEHAHKYPSQ-LSGGQQQRAAIARALCMEPRVMLFDEPT 175
Cdd:PRK13638 91 FYTDIDSDIafSLRNLgvpeaeiTRRVDEALT--LVD----AQHFRHQPIQcLSHGQKKRVAIAGALVLQARYLLLDEPT 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 176 SALDPEMVGEVLDTMRGLAAEGMTMMIVTHEMGFARQVADRVVFMDRGQIVEQAPPAAFF 235
Cdd:PRK13638 165 AGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVF 224
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
27-233 |
7.35e-25 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 102.58 E-value: 7.35e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 27 VLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVV-DGIELgqsenaaqavrrevgmvfqhfnLF----- 100
Cdd:COG4178 378 LLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARpAGARV----------------------LFlpqrp 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 101 --PHLDLVQnCILAPMSVRGMSRraAEALAVglLERVRLGEHAHKY------PSQLSGGQQQRAAIARALCMEPRVMLFD 172
Cdd:COG4178 436 ylPLGTLRE-ALLYPATAEAFSD--AELREA--LEAVGLGHLAERLdeeadwDQVLSLGEQQRLAFARLLLHKPDWLFLD 510
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 500071467 173 EPTSALDPEMVGEVLDTMRGlAAEGMTMMIVTHEMGFArQVADRVVFMDRGQIVEQAPPAA 233
Cdd:COG4178 511 EATSALDEENEAALYQLLRE-ELPGTTVISVGHRSTLA-AFHDRVLELTGDGSWQLLPAEA 569
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
4-232 |
7.64e-25 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 102.41 E-value: 7.64e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 4 PDASPAAPIISVAGVN-KWYGAFQVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIELGqseNA 82
Cdd:COG3845 249 APAEPGEVVLEVENLSvRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDIT---GL 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 83 AQAVRREVGMVF-----QHFNLFPHLDLVQNCIL-----APMSVRG-MSRRAAEALAVGLLER--VRL-GEHAHkyPSQL 148
Cdd:COG3845 326 SPRERRRLGVAYipedrLGRGLVPDMSVAENLILgryrrPPFSRGGfLDRKAIRAFAEELIEEfdVRTpGPDTP--ARSL 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 149 SGGQQQRAAIARALCMEPRVMLFDEPTSALDpemVG---EVLDTMRGLAAEGMTMMIVTHEMGFARQVADRVVFMDRGQI 225
Cdd:COG3845 404 SGGNQQKVILARELSRDPKLLIAAQPTRGLD---VGaieFIHQRLLELRDAGAAVLLISEDLDEILALSDRIAVMYEGRI 480
|
....*..
gi 500071467 226 VEQAPPA 232
Cdd:COG3845 481 VGEVPAA 487
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
9-226 |
7.74e-25 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 102.56 E-value: 7.74e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 9 AAPIISVAGVNKWYGAFQVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIELGQSENAAqAVRR 88
Cdd:PRK09700 2 ATPYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKL-AAQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 89 EVGMVFQHFNLFPHLDLVQNCILAPMSVRG-----------MSRRAAEalavgLLERVRLGEHAHKYPSQLSGGQQQRAA 157
Cdd:PRK09700 81 GIGIIYQELSVIDELTVLENLYIGRHLTKKvcgvniidwreMRVRAAM-----MLLRVGLKVDLDEKVANLSISHKQMLE 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 500071467 158 IARALCMEPRVMLFDEPTSALDPEMVGEVLDTMRGLAAEGMTMMIVTHEMGFARQVADRVVFMDRGQIV 226
Cdd:PRK09700 156 IAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSV 224
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
13-224 |
1.25e-24 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 95.21 E-value: 1.25e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 13 ISVAGVNKWYGAFQVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDgielgqsenaaqavrrevgm 92
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWG-------------------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 93 vfqhfnlfphldlvqncilapmsvrgmsrraaealavgllERVRLGehahkYPSQLSGGQQQRAAIARALCMEPRVMLFD 172
Cdd:cd03221 61 ----------------------------------------STVKIG-----YFEQLSGGEKMRLALAKLLLENPNLLLLD 95
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 500071467 173 EPTSALDPEMV---GEVLDTMRGlaaegmTMMIVTHEMGFARQVADRVVFMDRGQ 224
Cdd:cd03221 96 EPTNHLDLESIealEEALKEYPG------TVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
25-247 |
1.33e-24 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 99.82 E-value: 1.33e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 25 FQVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHqEGSIVVDGIELGQ------SENAA-QAVRREVGMVFQH- 96
Cdd:PRK11022 20 FRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDY-PGRVMAEKLEFNGqdlqriSEKERrNLVGAEVAMIFQDp 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 97 -FNLFPHLDLVQNCILAPMSVRGMSRRAAEALAVGLLERVRLGEHAHK---YPSQLSGGQQQRAAIARALCMEPRVMLFD 172
Cdd:PRK11022 99 mTSLNPCYTVGFQIMEAIKVHQGGNKKTRRQRAIDLLNQVGIPDPASRldvYPHQLSGGMSQRVMIAMAIACRPKLLIAD 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 500071467 173 EPTSALDPEMVGEVLDTMRGLA-AEGMTMMIVTHEMGFARQVADRVVFMDRGQIVEQAPPAAFFGAPVHERTRRFL 247
Cdd:PRK11022 179 EPTTALDVTIQAQIIELLLELQqKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDIFRAPRHPYTQALL 254
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
26-231 |
4.98e-24 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 95.56 E-value: 4.98e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 26 QVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIELgqSENAAQAVRREVGMVFQHFNLFPHldl 105
Cdd:cd03369 22 PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDI--STIPLEDLRSSLTIIPQDPTLFSG--- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 106 vqncilapmSVRGMSRRAAEALAVGLLERVRLGEHAhkypSQLSGGQQQRAAIARALCMEPRVMLFDEPTSALDPEMVGE 185
Cdd:cd03369 97 ---------TIRSNLDPFDEYSDEEIYGALRVSEGG----LNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDAL 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 500071467 186 VLDTMRGLAAeGMTMMIVTHEMgfaRQVA--DRVVFMDRGQIVEQAPP 231
Cdd:cd03369 164 IQKTIREEFT-NSTILTIAHRL---RTIIdyDKILVMDAGEVKEYDHP 207
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
22-228 |
6.36e-24 |
|
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: 100.20 E-value: 6.36e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 22 YGAfQVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIELGQSENaaQAVRREVGMVFQHFNLFP 101
Cdd:TIGR01193 485 YGS-NILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDR--HTLRQFINYLPQEPYIFS 561
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 102 HlDLVQNCILApmSVRGMS-------------RRAAEALAVGLleRVRLGEHAhkypSQLSGGQQQRAAIARALCMEPRV 168
Cdd:TIGR01193 562 G-SILENLLLG--AKENVSqdeiwaaceiaeiKDDIENMPLGY--QTELSEEG----SSISGGQKQRIALARALLTDSKV 632
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 169 MLFDEPTSALDPEMVGEVLDTMRGLAAEgmTMMIVTHEMGFARQVaDRVVFMDRGQIVEQ 228
Cdd:TIGR01193 633 LILDESTSNLDTITEKKIVNNLLNLQDK--TIIFVAHRLSVAKQS-DKIIVLDHGKIIEQ 689
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
9-234 |
7.09e-24 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 99.62 E-value: 7.09e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 9 AAPIISVAGVNKWYGAFQVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQH--QEGSIVVDGIELgQSENAAQAV 86
Cdd:PRK13549 2 MEYLLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHgtYEGEIIFEGEEL-QASNIRDTE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 87 RREVGMVFQHFNLFPHLDLVQNCILAPMSVRG-------MSRRAAEalavgLLERVRLGEHAHKYPSQLSGGQQQRAAIA 159
Cdd:PRK13549 81 RAGIAIIHQELALVKELSVLENIFLGNEITPGgimdydaMYLRAQK-----LLAQLKLDINPATPVGNLGLGQQQLVEIA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 500071467 160 RALCMEPRVMLFDEPTSALDPEMVGEVLDTMRGLAAEGMTMMIVTHEMGFARQVADRVVFMDRGQIVEQAPPAAF 234
Cdd:PRK13549 156 KALNKQARLLILDEPTASLTESETAVLLDIIRDLKAHGIACIYISHKLNEVKAISDTICVIRDGRHIGTRPAAGM 230
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
27-224 |
7.36e-24 |
|
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: 94.84 E-value: 7.36e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 27 VLTDVSLSVARGEKVVICGPSGSGKSTLIRC-LNQLEQHqEGSIVVDG-IELgqsenAAQ------AVRREV---GMVFQ 95
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSAlLGELEKL-SGSVSVPGsIAY-----VSQepwiqnGTIRENilfGKPFD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 96 H---------------FNLFPHLDLVQncilapMSVRGMSrraaealavgllervrlgehahkypsqLSGGQQQRAAIAR 160
Cdd:cd03250 94 EeryekvikacalepdLEILPDGDLTE------IGEKGIN---------------------------LSGGQKQRISLAR 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 500071467 161 ALCMEPRVMLFDEPTSALDPEmVGEVL--DTMRGLAAEGMTMMIVTHEMGFARQvADRVVFMDRGQ 224
Cdd:cd03250 141 AVYSDADIYLLDDPLSAVDAH-VGRHIfeNCILGLLLNNKTRILVTHQLQLLPH-ADQIVVLDNGR 204
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
26-228 |
1.20e-23 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 99.15 E-value: 1.20e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 26 QVLTD-VSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQeGSIVVDGIELgqSENAAQAVRREVGMVFQHFNLFpHLD 104
Cdd:PRK11174 363 KTLAGpLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPYQ-GSLKINGIEL--RELDPESWRKHLSWVGQNPQLP-HGT 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 105 LVQNCILApmsvrgmSRRAAEALAVGLLERVRLGEHAHKYP-----------SQLSGGQQQRAAIARALCMEPRVMLFDE 173
Cdd:PRK11174 439 LRDNVLLG-------NPDASDEQLQQALENAWVSEFLPLLPqgldtpigdqaAGLSVGQAQRLALARALLQPCQLLLLDE 511
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 500071467 174 PTSALDPEMVGEVLDTMRGLAAEGMTMMiVTHEMGFARQVaDRVVFMDRGQIVEQ 228
Cdd:PRK11174 512 PTASLDAHSEQLVMQALNAASRRQTTLM-VTHQLEDLAQW-DQIWVMQDGQIVQQ 564
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
26-231 |
2.07e-23 |
|
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: 93.75 E-value: 2.07e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 26 QVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQ--EGSIVVDG---IELGQSENAaqavRREVGMVFQHfnlf 100
Cdd:cd03217 14 EILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKYEvtEGEILFKGediTDLPPEERA----RLGIFLAFQY---- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 101 phldlvqncilaPMSVRGmsrraaealaVGLLERVR-LGEhahkypsQLSGGQQQRAAIARALCMEPRVMLFDEPTSALD 179
Cdd:cd03217 86 ------------PPEIPG----------VKNADFLRyVNE-------GFSGGEKKRNEILQLLLLEPDLAILDEPDSGLD 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 500071467 180 P---EMVGEVLDTMRGlaaEGMTMMIVTH-EMGFARQVADRVVFMDRGQIVEQAPP 231
Cdd:cd03217 137 IdalRLVAEVINKLRE---EGKSVLIITHyQRLLDYIKPDRVHVLYDGRIVKSGDK 189
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
12-233 |
2.24e-23 |
|
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: 98.36 E-value: 2.24e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 12 IISVAGVNKWYGAFQVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQH--QEGSIVVDGIELgQSENAAQAVRRE 89
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHgtWDGEIYWSGSPL-KASNIRDTERAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 90 VGMVFQHFNLFPHLDLVQNCILAP--------MSVRGMSRRAAEalavgLLERVRLGEHAHKYP-SQLSGGQQQRAAIAR 160
Cdd:TIGR02633 80 IVIIHQELTLVPELSVAENIFLGNeitlpggrMAYNAMYLRAKN-----LLRELQLDADNVTRPvGDYGGGQQQLVEIAK 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 500071467 161 ALCMEPRVMLFDEPTSALDPEMVGEVLDTMRGLAAEGMTMMIVTHEMGFARQVADRVVFMDRGQIVEQAPPAA 233
Cdd:TIGR02633 155 ALNKQARLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQHVATKDMST 227
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
27-230 |
2.34e-23 |
|
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: 98.28 E-value: 2.34e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 27 VLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIELGQSEnaaqavRREVGmvfQHFNLFPhldlv 106
Cdd:COG4618 347 ILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWD------REELG---RHIGYLP----- 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 107 QNCILAPMSVR-GMSR----------RAAEAlaVGLLERV---------RLGEHAHkypsQLSGGQQQRAAIARALCMEP 166
Cdd:COG4618 413 QDVELFDGTIAeNIARfgdadpekvvAAAKL--AGVHEMIlrlpdgydtRIGEGGA----RLSGGQRQRIGLARALYGDP 486
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 500071467 167 RVMLFDEPTSALDPEmvGE--VLDTMRGLAAEGMTMMIVTHEMGfARQVADRVVFMDRGQIVEQAP 230
Cdd:COG4618 487 RLVVLDEPNSNLDDE--GEaaLAAAIRALKARGATVVVITHRPS-LLAAVDKLLVLRDGRVQAFGP 549
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
17-229 |
3.30e-23 |
|
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: 94.00 E-value: 3.30e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 17 GVNKWYGAFQVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIELGQSEnaaqavRREVGMVFQH 96
Cdd:TIGR03740 5 NLSKRFGKQTAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGHPWTRKD------LHKIGSLIES 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 97 FNLFPHLDLVQNcilapMSVRGMSRRAAEALAVGLLERVRLGEHAHKYPSQLSGGQQQRAAIARALCMEPRVMLFDEPTS 176
Cdd:TIGR03740 79 PPLYENLTAREN-----LKVHTTLLGLPDSRIDEVLNIVDLTNTGKKKAKQFSLGMKQRLGIAIALLNHPKLLILDEPTN 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 500071467 177 ALDPEMVGEVLDTMRGLAAEGMTMMIVTHEMGFARQVADRVVFMDRGQIVEQA 229
Cdd:TIGR03740 154 GLDPIGIQELRELIRSFPEQGITVILSSHILSEVQQLADHIGIISEGVLGYQG 206
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
28-227 |
4.44e-23 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 97.40 E-value: 4.44e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 28 LTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIELgqSENAAQAVRREVGMVFQHFNLFPhlDLVQ 107
Cdd:PRK11176 359 LRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDL--RDYTLASLRNQVALVSQNVHLFN--DTIA 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 108 NCIlAPMSVRGMSR----RAAE-ALAVGLLERVR------LGEHAhkypSQLSGGQQQRAAIARALCMEPRVMLFDEPTS 176
Cdd:PRK11176 435 NNI-AYARTEQYSReqieEAARmAYAMDFINKMDngldtvIGENG----VLLSGGQRQRIAIARALLRDSPILILDEATS 509
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 500071467 177 ALDPE---MVGEVLDTMRglaaEGMTMMIVTHEMGFARQvADRVVFMDRGQIVE 227
Cdd:PRK11176 510 ALDTEserAIQAALDELQ----KNRTSLVIAHRLSTIEK-ADEILVVEDGEIVE 558
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
30-240 |
1.13e-22 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 94.41 E-value: 1.13e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 30 DVSLSVARGEKVVICGPSGSGKSTLIRCLNQL---EQHQEGSIVVDGIE-LGQSENAAQAVRRE-VGMVFQH--FNLFPH 102
Cdd:PRK09473 34 DLNFSLRAGETLGIVGESGSGKSQTAFALMGLlaaNGRIGGSATFNGREiLNLPEKELNKLRAEqISMIFQDpmTSLNPY 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 103 LDLVQNCILAPMSVRGMSRRAAEALAVGLLERVRLGEhAHK----YPSQLSGGQQQRAAIARALCMEPRVMLFDEPTSAL 178
Cdd:PRK09473 114 MRVGEQLMEVLMLHKGMSKAEAFEESVRMLDAVKMPE-ARKrmkmYPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTAL 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 500071467 179 DPEMVGEVLDTMRGLAAEGMTMMI-VTHEMGFARQVADRVVFMDRGQIVEQAPPAAFFGAPVH 240
Cdd:PRK09473 193 DVTVQAQIMTLLNELKREFNTAIImITHDLGVVAGICDKVLVMYAGRTMEYGNARDVFYQPSH 255
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
9-242 |
2.88e-22 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 92.25 E-value: 2.88e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 9 AAPIISVAGVN-KWYGAFQVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVdgieLGQSENaaQAVR 87
Cdd:PRK15056 3 QQAGIVVNDVTvTWRNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISI----LGQPTR--QALQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 88 RE-VGMVFQHFNL---FPHL--DLVQNCILAPMsvrGMSRRAAE---ALAVGLLERVRLGEHAHKYPSQLSGGQQQRAAI 158
Cdd:PRK15056 77 KNlVAYVPQSEEVdwsFPVLveDVVMMGRYGHM---GWLRRAKKrdrQIVTAALARVDMVEFRHRQIGELSGGQKKRVFL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 159 ARALCMEPRVMLFDEPTSALDPEMVGEVLDTMRGLAAEGMTMMIVTHEMGFARQVADRVVfMDRGQIVEQAPPAAFFGAP 238
Cdd:PRK15056 154 ARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRDEGKTMLVSTHNLGSVTEFCDYTV-MVKGTVLASGPTETTFTAE 232
|
....
gi 500071467 239 VHER 242
Cdd:PRK15056 233 NLEL 236
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
20-233 |
2.95e-22 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 91.88 E-value: 2.95e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 20 KWYGAFQVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIELGQSENAAQAvRREVGMVFQHFNL 99
Cdd:PRK10895 11 KAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARA-RRGIGYLPQEASI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 100 FPHLDLVQNcILAPMSVR-GMSRRAAEALAVGLLERVRLGEHAHKYPSQLSGGQQQRAAIARALCMEPRVMLFDEPTSAL 178
Cdd:PRK10895 90 FRRLSVYDN-LMAVLQIRdDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGV 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 500071467 179 DPEMVGEVLDTMRGLAAEGMTMMIVTHEMGFARQVADRVVFMDRGQIVEQAPPAA 233
Cdd:PRK10895 169 DPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTE 223
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
30-225 |
4.48e-22 |
|
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: 94.51 E-value: 4.48e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 30 DVSLSVARGEKVVICGPSGSGKSTLIRCL-NQLEQHQEGSIVVDGIELgQSENAAQAVRREVGMV---FQHFNLFPHLDL 105
Cdd:TIGR02633 278 DVSFSLRRGEILGVAGLVGAGRTELVQALfGAYPGKFEGNVFINGKPV-DIRNPAQAIRAGIAMVpedRKRHGIVPILGV 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 106 VQNCILAPM---SVRGMSRRAAEALAVGL-LERVRLGEHAHKYP-SQLSGGQQQRAAIARALCMEPRVMLFDEPTSALDP 180
Cdd:TIGR02633 357 GKNITLSVLksfCFKMRIDAAAELQIIGSaIQRLKVKTASPFLPiGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDV 436
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 500071467 181 EMVGEVLDTMRGLAAEGMTMMIVTHEMGFARQVADRVVFMDRGQI 225
Cdd:TIGR02633 437 GAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGKL 481
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
9-206 |
5.94e-22 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 90.54 E-value: 5.94e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 9 AAPIISVAGVNKWYGAFQVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIELgqSENAAQAVRR 88
Cdd:PRK10247 4 NSPLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDI--STLKPEIYRQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 89 EVGMVFQHFNLFPhlDLVQNCILAPMSVRGmsRRAAEALAVGLLERVRLGEHAHKYP-SQLSGGQQQRAAIARALCMEPR 167
Cdd:PRK10247 82 QVSYCAQTPTLFG--DTVYDNLIFPWQIRN--QQPDPAIFLDDLERFALPDTILTKNiAELSGGEKQRISLIRNLQFMPK 157
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 500071467 168 VMLFDEPTSALDPEMVGEVLDTMRGLAAE-GMTMMIVTHE 206
Cdd:PRK10247 158 VLLLDEITSALDESNKHNVNEIIHRYVREqNIAVLWVTHD 197
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
26-239 |
2.74e-21 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 92.42 E-value: 2.74e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 26 QVLTDVSlSVAR-GEKVVICGPSGSGKSTLircLNQLEQHQE------GSIVVDGIELGQSEnaaqaVRREVGMVFQHFN 98
Cdd:TIGR00955 39 HLLKNVS-GVAKpGELLAVMGSSGAGKTTL---MNALAFRSPkgvkgsGSVLLNGMPIDAKE-----MRAISAYVQQDDL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 99 LFPHLDLVQNCILAPMsVRgMSRRAAEA---LAVG-LLERVRLGEHAHK---YPSQ---LSGGQQQRAAIARALCMEPRV 168
Cdd:TIGR00955 110 FIPTLTVREHLMFQAH-LR-MPRRVTKKekrERVDeVLQALGLRKCANTrigVPGRvkgLSGGERKRLAFASELLTDPPL 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 169 MLFDEPTSALDPEMVGEVLDTMRGLAAEGMTMMIVTH-------EMgFarqvaDRVVFMDRGQIVEQAPP---AAFF--- 235
Cdd:TIGR00955 188 LFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIHqpsselfEL-F-----DKIILMAEGRVAYLGSPdqaVPFFsdl 261
|
....
gi 500071467 236 GAPV 239
Cdd:TIGR00955 262 GHPC 265
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
30-227 |
3.07e-21 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 92.15 E-value: 3.07e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 30 DVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIELGQSeNAAQAVRREVGMVFQH---FNLFPHLDLV 106
Cdd:PRK09700 281 DISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPR-SPLDAVKKGMAYITESrrdNGFFPNFSIA 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 107 QNcilapMSVRGMSRRAAEALAVGLL---ERVRLGEHAHKYPS-----------QLSGGQQQRAAIARALCMEPRVMLFD 172
Cdd:PRK09700 360 QN-----MAISRSLKDGGYKGAMGLFhevDEQRTAENQRELLAlkchsvnqnitELSGGNQQKVLISKWLCCCPEVIIFD 434
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 500071467 173 EPTSALDPEMVGEVLDTMRGLAAEGMTMMIVTHEMGFARQVADRVVFMDRGQIVE 227
Cdd:PRK09700 435 EPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRLTQ 489
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
9-227 |
3.62e-21 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 91.90 E-value: 3.62e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 9 AAPIISVAGVNKWYGAFQVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIELgQSENAAQAVRR 88
Cdd:PRK11288 1 SSPYLSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEM-RFASTTAALAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 89 EVGMVFQHFNLFPHLDLVQNCILAPMSVRG--MSRRAAEALAVGLLErvRLGEHAHkyPSQ----LSGGQQQRAAIARAL 162
Cdd:PRK11288 80 GVAIIYQELHLVPEMTVAENLYLGQLPHKGgiVNRRLLNYEAREQLE--HLGVDID--PDTplkyLSIGQRQMVEIAKAL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 500071467 163 CMEPRVMLFDEPTSALDPEMVGEVLDTMRGLAAEGMTMMIVTHEMGFARQVADRV-VFMDrGQIVE 227
Cdd:PRK11288 156 ARNARVIAFDEPTSSLSAREIEQLFRVIRELRAEGRVILYVSHRMEEIFALCDAItVFKD-GRYVA 220
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
28-232 |
2.50e-20 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 86.82 E-value: 2.50e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 28 LTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQeGSIVVDGIELGQSENAAQAVRRevGMVFQH----FNL--FP 101
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLLPGQ-GEILLNGRPLSDWSAAELARHR--AYLSQQqsppFAMpvFQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 102 HLDLvqncilapmSVRGMSRRAAEALAVG-LLERVRLGEHAHKYPSQLSGGQQQRAAIARALCM-------EPRVMLFDE 173
Cdd:COG4138 89 YLAL---------HQPAGASSEAVEQLLAqLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLQvwptinpEGQLLLLDE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 500071467 174 PTSALDpemVGE--VLDTM-RGLAAEGMTMMIVTHEMGFARQVADRVVFMDRGQIVEQAPPA 232
Cdd:COG4138 160 PMNSLD---VAQqaALDRLlRELCQQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETA 218
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
27-225 |
3.71e-20 |
|
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: 88.94 E-value: 3.71e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 27 VLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIELGQSENaaQAVRREVGMVFQHFNLFPHlDLV 106
Cdd:TIGR01842 333 TLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDR--ETFGKHIGYLPQDVELFPG-TVA 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 107 QNciLAPMsvrgmsRRAAEALAVglLERVRLGEhAH----KYP-----------SQLSGGQQQRAAIARALCMEPRVMLF 171
Cdd:TIGR01842 410 EN--IARF------GENADPEKI--IEAAKLAG-VHelilRLPdgydtvigpggATLSGGQRQRIALARALYGDPKLVVL 478
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 500071467 172 DEPTSALDPEMVGEVLDTMRGLAAEGMTMMIVTHEMGfARQVADRVVFMDRGQI 225
Cdd:TIGR01842 479 DEPNSNLDEEGEQALANAIKALKARGITVVVITHRPS-LLGCVDKILVLQDGRI 531
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
27-226 |
5.17e-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: 85.46 E-value: 5.17e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 27 VLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIElgQSENAAQAVRReVGMVF-QHFNLFPHLDL 105
Cdd:cd03267 36 ALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLV--PWKRRKKFLRR-IGVVFgQKTQLWWDLPV 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 106 VQNCILAPMSVRGMSRRAAEALAvGLLERVRLGEHAHKYPSQLSGGQQQRAAIARALCMEPRVMLFDEPTSALDPEMVGE 185
Cdd:cd03267 113 IDSFYLLAAIYDLPPARFKKRLD-ELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQEN 191
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 500071467 186 VLDTMRGLAAE-GMTMMIVTHEMGFARQVADRVVFMDRGQIV 226
Cdd:cd03267 192 IRNFLKEYNRErGTTVLLTSHYMKDIEALARRVLVIDKGRLL 233
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
30-225 |
5.80e-20 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 88.45 E-value: 5.80e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 30 DVSLSVARGEKVVICGPSGSGKSTLIRCL-NQLEQHQEGSIVVDGIELgQSENAAQAVRREVGMVFQ---HFNLFPHLDL 105
Cdd:PRK13549 280 DVSFSLRRGEILGIAGLVGAGRTELVQCLfGAYPGRWEGEIFIDGKPV-KIRNPQQAIAQGIAMVPEdrkRDGIVPVMGV 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 106 VQNCILAPM---SVRGMSRRAAEALAVG-LLERVRLgehahKYPS------QLSGGQQQRAAIARALCMEPRVMLFDEPT 175
Cdd:PRK13549 359 GKNITLAALdrfTGGSRIDDAAELKTILeSIQRLKV-----KTASpelaiaRLSGGNQQKAVLAKCLLLNPKILILDEPT 433
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 500071467 176 SALDpemVG---EVLDTMRGLAAEGMTMMIVTHEMGFARQVADRVVFMDRGQI 225
Cdd:PRK13549 434 RGID---VGakyEIYKLINQLVQQGVAIIVISSELPEVLGLSDRVLVMHEGKL 483
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
27-205 |
8.37e-20 |
|
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: 84.08 E-value: 8.37e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 27 VLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIELGQSENAAQAVRREVGmvfqhfnlfpHLDLV 106
Cdd:cd03231 15 LFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLG----------HAPGI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 107 QNCILAPMSVRGMSRRAAEALAVGLLERVRLGEHAHKYPSQLSGGQQQRAAIARALCMEPRVMLFDEPTSALDPEMVGEV 186
Cdd:cd03231 85 KTTLSVLENLRFWHADHSDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARF 164
|
170
....*....|....*....
gi 500071467 187 LDTMRGLAAEGMTMMIVTH 205
Cdd:cd03231 165 AEAMAGHCARGGMVVLTTH 183
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
26-227 |
1.68e-19 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 84.35 E-value: 1.68e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 26 QVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQ--EGSIVVDG---IELGQSENAaqavRREVGMVFQHfnlf 100
Cdd:COG0396 14 EILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPKYEvtSGSILLDGediLELSPDERA----RAGIFLAFQY---- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 101 phldlvqncilaPMSVRGMS-----RRAAEA-------------LAVGLLERVRLGE-HAHKYPSQ-LSGGQQQRAAIAR 160
Cdd:COG0396 86 ------------PVEIPGVSvsnflRTALNArrgeelsareflkLLKEKMKELGLDEdFLDRYVNEgFSGGEKKRNEILQ 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 500071467 161 ALCMEPRVMLFDEPTSALDPE---MVGEVLDTMRGlaaEGMTMMIVTHemgFAR----QVADRVVFMDRGQIVE 227
Cdd:COG0396 154 MLLLEPKLAILDETDSGLDIDalrIVAEGVNKLRS---PDRGILIITH---YQRildyIKPDFVHVLVDGRIVK 221
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
27-205 |
4.28e-19 |
|
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: 81.43 E-value: 4.28e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 27 VLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVdgielgqsenaaqAVRREVGMVFQHfnlfPHLdlv 106
Cdd:cd03223 16 LLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGM-------------PEGEDLLFLPQR----PYL--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 107 qncilapmsVRGMSRraaEALAvgllervrlgehahkYPSQ--LSGGQQQRAAIARALCMEPRVMLFDEPTSALDPEMVG 184
Cdd:cd03223 76 ---------PLGTLR---EQLI---------------YPWDdvLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESED 128
|
170 180
....*....|....*....|.
gi 500071467 185 EVLDTMRGlaaEGMTMMIVTH 205
Cdd:cd03223 129 RLYQLLKE---LGITVISVGH 146
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
11-229 |
5.72e-19 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 85.44 E-value: 5.72e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 11 PIISVAGVNKWYGAFQVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIELG-----QSENAAqa 85
Cdd:PRK10762 3 ALLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTfngpkSSQEAG-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 86 vrreVGMVFQHFNLFPHLDLVQNCILAPMSVRGMSR---RAAEALAVGLLERVRLGEHAHKYPSQLSGGQQQRAAIARAL 162
Cdd:PRK10762 81 ----IGIIHQELNLIPQLTIAENIFLGREFVNRFGRidwKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 500071467 163 CMEPRVMLFDEPTSALDPEMVGEVLDTMRGLAAEGMTMMIVTHEMGFARQVADRV-VFMDRGQIVEQA 229
Cdd:PRK10762 157 SFESKVIIMDEPTDALTDTETESLFRVIRELKSQGRGIVYISHRLKEIFEICDDVtVFRDGQFIAERE 224
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
45-231 |
7.34e-19 |
|
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: 85.84 E-value: 7.34e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 45 GPSGSGKSTLIRCLNQLEQHQEGSIVVDGIELgqsENAAQAVRREVGMVFQHFNLFPHLDLVQNcILAPMSVRGMSRRAA 124
Cdd:TIGR01257 963 GHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI---ETNLDAVRQSLGMCPQHNILFHHLTVAEH-ILFYAQLKGRSWEEA 1038
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 125 EALAVGLLERVRLGEHAHKYPSQLSGGQQQRAAIARALCMEPRVMLFDEPTSALDPEMVGEVLDTMRGLAAeGMTMMIVT 204
Cdd:TIGR01257 1039 QLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRS-GRTIIMST 1117
|
170 180
....*....|....*....|....*..
gi 500071467 205 HEMGFARQVADRVVFMDRGQIVEQAPP 231
Cdd:TIGR01257 1118 HHMDEADLLGDRIAIISQGRLYCSGTP 1144
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
23-205 |
8.25e-19 |
|
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: 81.64 E-value: 8.25e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 23 GAFQVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIELGQSENAAQavrrevgmvfQHFNLFPH 102
Cdd:TIGR01189 11 GERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPH----------ENILYLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 103 LDLVQNCILAPMSVRGMSR--RAAEALAVGLLERVRLGEHAHKYPSQLSGGQQQRAAIARALCMEPRVMLFDEPTSALDP 180
Cdd:TIGR01189 81 LPGLKPELSALENLHFWAAihGGAQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDK 160
|
170 180
....*....|....*....|....*
gi 500071467 181 EMVGEVLDTMRGLAAEGMTMMIVTH 205
Cdd:TIGR01189 161 AGVALLAGLLRAHLARGGIVLLTTH 185
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
25-227 |
1.51e-18 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 81.16 E-value: 1.51e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 25 FQVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDgielgqsenaaqavrrevgmvfqhfnlFPHLD 104
Cdd:COG2401 43 RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVD---------------------------VPDNQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 105 LVQNCILapmsVRGMSRRAAEALAVGLLERVRLGEhAHKY---PSQLSGGQQQRAAIARALCMEPRVMLFDEPTSALDPE 181
Cdd:COG2401 96 FGREASL----IDAIGRKGDFKDAVELLNAVGLSD-AVLWlrrFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQ 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 500071467 182 MVGEVLDTMRGLAAE-GMTMMIVTHEMGFARQVA-DRVVFMDRGQIVE 227
Cdd:COG2401 171 TAKRVARNLQKLARRaGITLVVATHHYDVIDDLQpDLLIFVGYGGVPE 218
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
27-241 |
1.65e-18 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 82.14 E-value: 1.65e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 27 VLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIELGQSENAAQAvrREVGMVFQHFnlfPHLDlv 106
Cdd:PRK10575 26 LLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFA--RKVAYLPQQL---PAAE-- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 107 qncilaPMSVRGM-------------------SRRAAEALAVgllerVRLGEHAHKYPSQLSGGQQQRAAIARALCMEPR 167
Cdd:PRK10575 99 ------GMTVRELvaigrypwhgalgrfgaadREKVEEAISL-----VGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSR 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 500071467 168 VMLFDEPTSALDPEMVGEVLDTMRGLAAE-GMTMMIVTHEMGFARQVADRVVFMDRGQIVEQAPPAAFFGAPVHE 241
Cdd:PRK10575 168 CLLLDEPTSALDIAHQVDVLALVHRLSQErGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRGETLE 242
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
12-226 |
1.69e-18 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 84.23 E-value: 1.69e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 12 IISVAGVNKWYGAFQVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLN-------------------QLEQ----HQEGS 68
Cdd:PRK11147 3 LISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNgevllddgriiyeqdlivaRLQQdpprNVEGT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 69 I---VVDGI-ELGQSENAAQAVRREVGMVFQHFNL---------FPHLDLVQncilapmsvrgMSRRAAEALAvgllerv 135
Cdd:PRK11147 83 VydfVAEGIeEQAEYLKRYHDISHLVETDPSEKNLnelaklqeqLDHHNLWQ-----------LENRINEVLA------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 136 RLGEHAHKYPSQLSGGQQQRAAIARALCMEPRVMLFDEPTSALDPEMVG---EVLDTMRGlaaegmTMMIVTHEMGFARQ 212
Cdd:PRK11147 145 QLGLDPDAALSSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEwleGFLKTFQG------SIIFISHDRSFIRN 218
|
250
....*....|....
gi 500071467 213 VADRVVFMDRGQIV 226
Cdd:PRK11147 219 MATRIVDLDRGKLV 232
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1-226 |
4.70e-18 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 82.79 E-value: 4.70e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 1 MPNPDASPAaPIISVAGVNKWYGAFQVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIELGQSe 80
Cdd:PRK15439 1 MQTSDTTAP-PLLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARL- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 81 NAAQAVRREVGMVFQHFNLFPHLDLVQNcILAPMSVRGMSRRAAEALAVGLLERVRLGEHAhkypSQLSGGQQQRAAIAR 160
Cdd:PRK15439 79 TPAKAHQLGIYLVPQEPLLFPNLSVKEN-ILFGLPKRQASMQKMKQLLAALGCQLDLDSSA----GSLEVADRQIVEILR 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 500071467 161 ALCMEPRVMLFDEPTSALDPEMVGEVLDTMRGLAAEGMTMMIVTHEMGFARQVADRVVFMDRGQIV 226
Cdd:PRK15439 154 GLMRDSRILILDEPTASLTPAETERLFSRIRELLAQGVGIVFISHKLPEIRQLADRISVMRDGTIA 219
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
119-226 |
7.06e-18 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 81.71 E-value: 7.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 119 MSRRAAEALAVGLLERVRLGEHAHKYPSQLSGGQQQRAAIARALCMEPRVMLFDEPTSALDPEMVGEVLDTMRGLAAEGM 198
Cdd:NF000106 116 LSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGA 195
|
90 100
....*....|....*....|....*...
gi 500071467 199 TMMIVTHEMGFARQVADRVVFMDRGQIV 226
Cdd:NF000106 196 TVLLTTQYMEEAEQLAHELTVIDRGRVI 223
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
27-205 |
1.53e-17 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 78.38 E-value: 1.53e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 27 VLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIELGQSENAAQAVRreVGmvfqHFN-LFPHLDL 105
Cdd:PRK13539 17 LFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACHY--LG----HRNaMKPALTV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 106 VQNCIL-ApmSVRGMSRRAAEALavglLERVRLGEHAHKYPSQLSGGQQQRAAIARALCMEPRVMLFDEPTSALDPEMVG 184
Cdd:PRK13539 91 AENLEFwA--AFLGGEELDIAAA----LEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVA 164
|
170 180
....*....|....*....|.
gi 500071467 185 EVLDTMRGLAAEGMTMMIVTH 205
Cdd:PRK13539 165 LFAELIRAHLAQGGIVIAATH 185
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
23-250 |
2.68e-17 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 79.85 E-value: 2.68e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 23 GAFQVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQ----EGSIVVDGIELGQSENAA--QAVRREVGMVFQH 96
Cdd:PRK15093 18 GWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDNwrvtADRMRFDDIDLLRLSPRErrKLVGHNVSMIFQE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 97 FN--LFPHLDLVQNCILA-P---------MSVRGMSRRAAEalavgLLERVRLGEHA---HKYPSQLSGGQQQRAAIARA 161
Cdd:PRK15093 98 PQscLDPSERVGRQLMQNiPgwtykgrwwQRFGWRKRRAIE-----LLHRVGIKDHKdamRSFPYELTEGECQKVMIAIA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 162 LCMEPRVMLFDEPTSALDPEMVGEVLDTMRGL-AAEGMTMMIVTHEMGFARQVADRVVFMDRGQIVEQAPPAAFFGAPVH 240
Cdd:PRK15093 173 LANQPRLLIADEPTNAMEPTTQAQIFRLLTRLnQNNNTTILLISHDLQMLSQWADKINVLYCGQTVETAPSKELVTTPHH 252
|
250
....*....|
gi 500071467 241 ERTRRFLSQI 250
Cdd:PRK15093 253 PYTQALIRAI 262
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
2-228 |
2.84e-17 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 80.79 E-value: 2.84e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 2 PNPDASPAAPIISVA-GVNKWYGAFQ--VLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQleqhqegsivvdgiELGQ 78
Cdd:PLN03232 604 QNPPLQPGAPAISIKnGYFSWDSKTSkpTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLG--------------ELSH 669
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 79 SENAAQAVRREVGMVfqhfnlfPHLDLVQNCILAPMSVRGM---SRRAAEALAVGLLE----------RVRLGEHAhkyp 145
Cdd:PLN03232 670 AETSSVVIRGSVAYV-------PQVSWIFNATVRENILFGSdfeSERYWRAIDVTALQhdldllpgrdLTEIGERG---- 738
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 146 SQLSGGQQQRAAIARALCMEPRVMLFDEPTSALDPEMVGEVLDTMRGLAAEGMTMMIVTHEMGFARQVaDRVVFMDRGQI 225
Cdd:PLN03232 739 VNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDSCMKDELKGKTRVLVTNQLHFLPLM-DRIILVSEGMI 817
|
...
gi 500071467 226 VEQ 228
Cdd:PLN03232 818 KEE 820
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
28-226 |
1.53e-16 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 77.43 E-value: 1.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 28 LTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIELGQSENAaqaVRREVGMVF-QHFNLFPHLDLV 106
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPFKRRKE---FARRIGVVFgQRSQLWWDLPAI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 107 QN-CILApmSVRGMSRRA--------AEALAVG-LLER-VRlgehahkypsQLSGGQQQRAAIARALCMEPRVMLFDEPT 175
Cdd:COG4586 115 DSfRLLK--AIYRIPDAEykkrldelVELLDLGeLLDTpVR----------QLSLGQRMRCELAAALLHRPKILFLDEPT 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 500071467 176 SALDPEMVGEVLDTMRGLAAE-GMTMMIVTHEMGFARQVADRVVFMDRGQIV 226
Cdd:COG4586 183 IGLDVVSKEAIREFLKEYNRErGTTILLTSHDMDDIEALCDRVIVIDHGRII 234
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
31-233 |
2.91e-16 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 77.53 E-value: 2.91e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 31 VSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIELgqSENAAQAVRREVGMVFQHFNLFPHLDlvqnci 110
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPV--TADNREAYRQLFSAVFSDFHLFDRLL------ 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 111 lapmsvrGMSRRAAEALAVGLLERVRLgehAHKYPSQ--------LSGGQQQRAAIARALcMEPR-VMLFDEPTSALDP- 180
Cdd:COG4615 423 -------GLDGEADPARARELLERLEL---DHKVSVEdgrfsttdLSQGQRKRLALLVAL-LEDRpILVFDEWAADQDPe 491
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 181 -------EMVGEvldtmrgLAAEGMTMMIVTHEMGFArQVADRVVFMDRGQIVEQAPPAA 233
Cdd:COG4615 492 frrvfytELLPE-------LKARGKTVIAISHDDRYF-DLADRVLKMDYGKLVELTGPAA 543
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
28-232 |
3.89e-16 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 75.35 E-value: 3.89e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 28 LTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHqEGSIVVDGIELGQSENAAQAVRRevGMVFQH----FNL--FP 101
Cdd:PRK03695 12 LGPLSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPG-SGSIQFAGQPLEAWSAAELARHR--AYLSQQqtppFAMpvFQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 102 HLDLVQncilaPMSVRgmsRRAAEALAVGLLERVRLGEHAHKYPSQLSGGQQQR---AA----IARALCMEPRVMLFDEP 174
Cdd:PRK03695 89 YLTLHQ-----PDKTR---TEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRvrlAAvvlqVWPDINPAGQLLLLDEP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 500071467 175 TSALDPEMVGeVLDTM-RGLAAEGMTMMIVTHEMGFARQVADRVVFMDRGQIVEQAPPA 232
Cdd:PRK03695 161 MNSLDVAQQA-ALDRLlSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRD 218
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
29-233 |
4.86e-16 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 76.87 E-value: 4.86e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 29 TDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIELgQSENAAQAVRRevGMVfqhfnLFPHlDLVQN 108
Cdd:PRK11288 270 EPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPI-DIRSPRDAIRA--GIM-----LCPE-DRKAE 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 109 CILAPMSVR---GMSRRAAEALAVGLLERVRLGEHAHKY--------PS------QLSGGQQQRAAIARALCMEPRVMLF 171
Cdd:PRK11288 341 GIIPVHSVAdniNISARRHHLRAGCLINNRWEAENADRFirslniktPSreqlimNLSGGNQQKAILGRWLSEDMKVILL 420
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 172 DEPTSALDpemVG---EVLDTMRGLAAEGMTMMIVTHEMGFARQVADRVVFMDRGQIV-----EQAPPAA 233
Cdd:PRK11288 421 DEPTRGID---VGakhEIYNVIYELAAQGVAVLFVSSDLPEVLGVADRIVVMREGRIAgelarEQATERQ 487
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
31-227 |
5.65e-16 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 76.93 E-value: 5.65e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 31 VSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIELgqSENAAQAVRREVGMVFQHFNLFPHLdlvqnci 110
Cdd:PRK10522 342 INLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPV--TAEQPEDYRKLFSAVFTDFHLFDQL------- 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 111 LAPmsvRGMSrrAAEALAVGLLERVRLgehAHKYP--------SQLSGGQQQRAAIARALCMEPRVMLFDEPTSALDP-- 180
Cdd:PRK10522 413 LGP---EGKP--ANPALVEKWLERLKM---AHKLEledgrisnLKLSKGQKKRLALLLALAEERDILLLDEWAADQDPhf 484
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 500071467 181 --EMVGEVLDTMRglaAEGMTMMIVTHEMGFARQvADRVVFMDRGQIVE 227
Cdd:PRK10522 485 rrEFYQVLLPLLQ---EMGKTIFAISHDDHYFIH-ADRLLEMRNGQLSE 529
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
17-230 |
1.28e-15 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 75.54 E-value: 1.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 17 GVNKWYGAFQVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIELgQSENAAQAVRREVGMVFQH 96
Cdd:PRK10982 3 NISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEI-DFKSSKEALENGISMVHQE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 97 FNLFPHLDLVQNCILAPMSVRGM----------SRRAAEALAVGLLERVRLGEhahkypsqLSGGQQQRAAIARALCMEP 166
Cdd:PRK10982 82 LNLVLQRSVMDNMWLGRYPTKGMfvdqdkmyrdTKAIFDELDIDIDPRAKVAT--------LSVSQMQMIEIAKAFSYNA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 500071467 167 RVMLFDEPTSALDPEMVGEVLDTMRGLAAEGMTMMIVTHEMGFARQVADRVVFMDRGQIVEQAP 230
Cdd:PRK10982 154 KIVIMDEPTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQWIATQP 217
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
11-179 |
1.54e-15 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 73.61 E-value: 1.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 11 PIISVAGVNKWYGAFQVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGielgqsenaaqavRREV 90
Cdd:PRK09544 3 SLVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNG-------------KLRI 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 91 GMVFQHFNLFPHLDLVqncILAPMSVRGMSRRAAEALAvglLERVRLGeHAHKYPSQ-LSGGQQQRAAIARALCMEPRVM 169
Cdd:PRK09544 70 GYVPQKLYLDTTLPLT---VNRFLRLRPGTKKEDILPA---LKRVQAG-HLIDAPMQkLSGGETQRVLLARALLNRPQLL 142
|
170
....*....|
gi 500071467 170 LFDEPTSALD 179
Cdd:PRK09544 143 VLDEPTQGVD 152
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
25-236 |
1.66e-15 |
|
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: 72.68 E-value: 1.66e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 25 FQVLTDVSLSVARGEKVVICGPSGSGKSTLIRCL-NQLEQHQ--EGSIVVDGIELGQsenAAQAVRREVGMVFQHFNLFP 101
Cdd:cd03233 20 IPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALaNRTEGNVsvEGDIHYNGIPYKE---FAEKYPGEIIYVSEEDVHFP 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 102 HLdLVQNCILAPMSVRGmsrraaealavgllervrlgehaHKYPSQLSGGQQQRAAIARALCMEPRVMLFDEPTSALDPE 181
Cdd:cd03233 97 TL-TVRETLDFALRCKG-----------------------NEFVRGISGGERKRVSIAEALVSRASVLCWDNSTRGLDSS 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 500071467 182 MVGEVLDTMRGLA-AEGMTMMIVTHEMG------FarqvaDRVVFMDRGQIVeqappaaFFG 236
Cdd:cd03233 153 TALEILKCIRTMAdVLKTTTFVSLYQASdeiydlF-----DKVLVLYEGRQI-------YYG 202
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
2-233 |
3.10e-15 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 74.78 E-value: 3.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 2 PNPDASPAAPIISVAGVNKWYGAFQVLTDVSLSVARGEkvvICGPSGS---GKSTLIRCLNQLEQHQEGSIVVdgieLGQ 78
Cdd:NF033858 256 PRPADDDDEPAIEARGLTMRFGDFTAVDHVSFRIRRGE---IFGFLGSngcGKSTTMKMLTGLLPASEGEAWL----FGQ 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 79 SENAAQ-AVRREVGMVFQHFNLFPHLDLVQNCIL-ApmsvR--GMSRRAAEALAVGLLERVRLGEHAHKYPSQLSGGQQQ 154
Cdd:NF033858 329 PVDAGDiATRRRVGYMSQAFSLYGELTVRQNLELhA----RlfHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQ 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 155 RAAIARALCMEPRVMLFDEPTSALDPEMVGEVLDTMRGLAAE-GMTMMIVTHEMGFArQVADRVVFMDRGQIVEQAPPAA 233
Cdd:NF033858 405 RLSLAVAVIHKPELLILDEPTSGVDPVARDMFWRLLIELSREdGVTIFISTHFMNEA-ERCDRISLMHAGRVLASDTPAA 483
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
27-228 |
3.61e-15 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 74.37 E-value: 3.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 27 VLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIELgqSENAAQAVRREVGMVFQhfnlfphlDLV 106
Cdd:PRK10790 356 VLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPL--SSLSHSVLRQGVAMVQQ--------DPV 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 107 qncILAPmSVRG---MSRRAAEALAVGLLERVRLGEHAHKYP-----------SQLSGGQQQRAAIARALCMEPRVMLFD 172
Cdd:PRK10790 426 ---VLAD-TFLAnvtLGRDISEEQVWQALETVQLAELARSLPdglytplgeqgNNLSVGQKQLLALARVLVQTPQILILD 501
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 500071467 173 EPTSALDP---EMVGEVLDTMRglaaEGMTMMIVTHEMGFARQvADRVVFMDRGQIVEQ 228
Cdd:PRK10790 502 EATANIDSgteQAIQQALAAVR----EHTTLVVIAHRLSTIVE-ADTILVLHRGQAVEQ 555
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
27-232 |
9.89e-15 |
|
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: 73.44 E-value: 9.89e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 27 VLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIELgqSENAAQAVRREVGMVFQHFNLFPHlDLV 106
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNI--AKIGLHDLRFKITIIPQDPVLFSG-SLR 1377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 107 QNciLAPMSvrgmsrRAAEALAVGLLERVRLGEHAHKYPSQ-----------LSGGQQQRAAIARALCMEPRVMLFDEPT 175
Cdd:TIGR00957 1378 MN--LDPFS------QYSDEEVWWALELAHLKTFVSALPDKldhecaeggenLSVGQRQLVCLARALLRKTKILVLDEAT 1449
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 500071467 176 SALDPEMVGEVLDTMRgLAAEGMTMMIVTHEMgfaRQVAD--RVVFMDRGQIVEQAPPA 232
Cdd:TIGR00957 1450 AAVDLETDNLIQSTIR-TQFEDCTVLTIAHRL---NTIMDytRVIVLDKGEVAEFGAPS 1504
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
30-225 |
1.08e-14 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 73.11 E-value: 1.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 30 DVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIELgQSENAAQAVRRevGMVF-----QHFNLFPHLD 104
Cdd:PRK10762 270 DVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEV-VTRSPQDGLAN--GIVYisedrKRDGLVLGMS 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 105 LVQN---CILAPMSVRGMS-RRAAEALAVGllERVRLgeHAHKYPSQ------LSGGQQQRAAIARALCMEPRVMLFDEP 174
Cdd:PRK10762 347 VKENmslTALRYFSRAGGSlKHADEQQAVS--DFIRL--FNIKTPSMeqaiglLSGGNQQKVAIARGLMTRPKVLILDEP 422
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 500071467 175 TSALDpemVG---EVLDTMRGLAAEGMTMMIVTHEMGFARQVADRVVFMDRGQI 225
Cdd:PRK10762 423 TRGVD---VGakkEIYQLINQFKAEGLSIILVSSEMPEVLGMSDRILVMHEGRI 473
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
1-228 |
1.30e-14 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 73.23 E-value: 1.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 1 MPNPDASPAAPIISVA-GVNKWYGAFQ--VLTDVSLSVARGEKVVICGPSGSGKSTLIRC-LNQLEQHQEGSIVVDGiel 76
Cdd:PLN03130 603 LPNPPLEPGLPAISIKnGYFSWDSKAErpTLSNINLDVPVGSLVAIVGSTGEGKTSLISAmLGELPPRSDASVVIRG--- 679
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 77 gqsenaAQAVRREVGMVFQHfnlfphldLVQNCIL--APMSvrgmSRRAAEALAVGLLER----------VRLGEHAhky 144
Cdd:PLN03130 680 ------TVAYVPQVSWIFNA--------TVRDNILfgSPFD----PERYERAIDVTALQHdldllpggdlTEIGERG--- 738
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 145 pSQLSGGQQQRAAIARALCMEPRVMLFDEPTSALDPEMVGEVLDTMRGLAAEGMTMMIVTHEMGFARQVaDRVVFMDRGQ 224
Cdd:PLN03130 739 -VNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFDKCIKDELRGKTRVLVTNQLHFLSQV-DRIILVHEGM 816
|
....
gi 500071467 225 IVEQ 228
Cdd:PLN03130 817 IKEE 820
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
27-206 |
1.37e-14 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 72.99 E-value: 1.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 27 VLTDVSLSVARGEKVVICGPSGSGKSTLircLNQLEQHQEGSIVVDGIELGQSENAAQAVRReVGMVFQHFNLFPHLDLV 106
Cdd:PLN03211 83 ILNGVTGMASPGEILAVLGPSGSGKSTL---LNALAGRIQGNNFTGTILANNRKPTKQILKR-TGFVTQDDILYPHLTVR 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 107 QNCILA-----PMSV-RGMSRRAAEA----LAVGLLERVRLGehaHKYPSQLSGGQQQRAAIARALCMEPRVMLFDEPTS 176
Cdd:PLN03211 159 ETLVFCsllrlPKSLtKQEKILVAESviseLGLTKCENTIIG---NSFIRGISGGERKRVSIAHEMLINPSLLILDEPTS 235
|
170 180 190
....*....|....*....|....*....|
gi 500071467 177 ALDPEMVGEVLDTMRGLAAEGMTMMIVTHE 206
Cdd:PLN03211 236 GLDATAAYRLVLTLGSLAQKGKTIVTSMHQ 265
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
28-230 |
2.62e-14 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 72.29 E-value: 2.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 28 LTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGielgqsenaaqavrrEVGMVfqhfnlfPHLDLVQ 107
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKG---------------SVAYV-------PQQAWIQ 711
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 108 NCILAPMSVRGMS------RRAAEALAvgLL---------ERVRLGEHAhkypSQLSGGQQQRAAIARALCMEPRVMLFD 172
Cdd:TIGR00957 712 NDSLRENILFGKAlnekyyQQVLEACA--LLpdleilpsgDRTEIGEKG----VNLSGGQKQRVSLARAVYSNADIYLFD 785
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 500071467 173 EPTSALDPEMVGEVLDTMRGlaAEGM----TMMIVTHEMGFARQVaDRVVFMDRGQIVEQAP 230
Cdd:TIGR00957 786 DPLSAVDAHVGKHIFEHVIG--PEGVlknkTRILVTHGISYLPQV-DVIIVMSGGKISEMGS 844
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
30-225 |
5.42e-14 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 70.85 E-value: 5.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 30 DVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIELGQSENAAqavRREVGMVF-----QHFNLFPHLD 104
Cdd:PRK15439 281 NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQ---RLARGLVYlpedrQSSGLYLDAP 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 105 LVQN-CILAPMSVRGMSRRAAEAlAVglLERVR--LG---EHAHKYPSQLSGGQQQRAAIARALCMEPRVMLFDEPTSAL 178
Cdd:PRK15439 358 LAWNvCALTHNRRGFWIKPAREN-AV--LERYRraLNikfNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGV 434
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 500071467 179 DPEMVGEVLDTMRGLAAEGMTMMIVTHEMGFARQVADRVVFMDRGQI 225
Cdd:PRK15439 435 DVSARNDIYQLIRSIAAQNVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
26-223 |
1.84e-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: 66.88 E-value: 1.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 26 QVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQ--HQEGSIVVDGIELGQSenaaqaVRREVGMVfqhfnlfPHL 103
Cdd:cd03232 21 QLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTagVITGEILINGRPLDKN------FQRSTGYV-------EQQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 104 DlvqncILAPMS-VRgmsrraaEALAVGLLERvrlgehahkypsQLSGGQQQRAAIARALCMEPRVMLFDEPTSALDPEM 182
Cdd:cd03232 88 D-----VHSPNLtVR-------EALRFSALLR------------GLSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQA 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 500071467 183 VGEVLDTMRGLAAEGMTMMIVTHEMG---FARqvADRVVFMDRG 223
Cdd:cd03232 144 AYNIVRFLKKLADSGQAILCTIHQPSasiFEK--FDRLLLLKRG 185
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
27-230 |
2.42e-13 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 68.97 E-value: 2.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 27 VLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIELGQSEnaAQAVRREVGMVFQHFNLFPhlDLV 106
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQ--LDSWRSRLAVVSQTPFLFS--DTV 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 107 QNCIL--APMSVRGMSRRAAEaLAVGLLERVRLGEhahKYPSQ-------LSGGQQQRAAIARALCMEPRVMLFDEPTSA 177
Cdd:PRK10789 406 ANNIAlgRPDATQQEIEHVAR-LASVHDDILRLPQ---GYDTEvgergvmLSGGQKQRISIARALLLNAEILILDDALSA 481
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 500071467 178 LDPEMVGEVLDTMRgLAAEGMTMMIVTHEMGfARQVADRVVFMDRGQIVEQAP 230
Cdd:PRK10789 482 VDGRTEHQILHNLR-QWGEGRTVIISAHRLS-ALTEASEILVMQHGHIAQRGN 532
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
29-205 |
4.04e-13 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 65.98 E-value: 4.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 29 TDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIELgqsenaaQAVRREVgmvfqHFNLF-------- 100
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPI-------RRQRDEY-----HQDLLylghqpgi 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 101 -PHLDLVQN-CILAPMSVRGMSRRAAEALA-VGLLERvrlgEHAhkyP-SQLSGGQQQRAAIARALCMEPRVMLFDEPTS 176
Cdd:PRK13538 86 kTELTALENlRFYQRLHGPGDDEALWEALAqVGLAGF----EDV---PvRQLSAGQQRRVALARLWLTRAPLWILDEPFT 158
|
170 180
....*....|....*....|....*....
gi 500071467 177 ALDPEMVGEVLDTMRGLAAEGMTMMIVTH 205
Cdd:PRK13538 159 AIDKQGVARLEALLAQHAEQGGMVILTTH 187
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
12-224 |
4.78e-13 |
|
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: 68.04 E-value: 4.78e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 12 IISVAGVNKWYGA-FQVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVV-DGIElgqsenaaqavrre 89
Cdd:TIGR03719 4 IYTMNRVSKVVPPkKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPqPGIK-------------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 90 VGMVFQHFNLFPHLDLVQNCILAPMSVRGMSRRAAE-------------ALAV--GLLE-------------RVRLGEHA 141
Cdd:TIGR03719 70 VGYLPQEPQLDPTKTVRENVEEGVAEIKDALDRFNEisakyaepdadfdKLAAeqAELQeiidaadawdldsQLEIAMDA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 142 HKYP------SQLSGGQQQRAAIARALCMEPRVMLFDEPTSALDPEMVG--EvldtmRGLAAEGMTMMIVTHEMGFARQV 213
Cdd:TIGR03719 150 LRCPpwdadvTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAwlE-----RHLQEYPGTVVAVTHDRYFLDNV 224
|
250
....*....|.
gi 500071467 214 ADRVVFMDRGQ 224
Cdd:TIGR03719 225 AGWILELDRGR 235
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
28-224 |
8.90e-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: 8.90e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 28 LTDVSLSVARGEKVVICGPSGSGKSTLirclnqleqhqegsiVVDGIelgqsenAAQAVRREVGMV---FQHFNLFphLD 104
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTL---------------VNEGL-------YASGKARLISFLpkfSRNKLIF--ID 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 105 LVQNCIlapmsvrgmsrraaealAVGLlERVRLGEHAhkypSQLSGGQQQRAAIARALCMEPR--VMLFDEPTSALDPEM 182
Cdd:cd03238 67 QLQFLI-----------------DVGL-GYLTLGQKL----STLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQD 124
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 500071467 183 VGEVLDTMRGLAAEGMTMMIVTHEMGFARQvADRVVFMDRGQ 224
Cdd:cd03238 125 INQLLEVIKGLIDLGNTVILIEHNLDVLSS-ADWIIDFGPGS 165
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
15-226 |
2.85e-12 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 65.68 E-value: 2.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 15 VAGVNKWYGAFQVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIvvdgielGQSENAaqavrrEVGMVF 94
Cdd:PRK15064 322 VENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV-------KWSENA------NIGYYA 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 95 Q-HFNLFP----------------HLDLVqncilapmsVRGMSRRaaealavgLLERvrlGEHAHKYPSQLSGGQQQRAA 157
Cdd:PRK15064 389 QdHAYDFEndltlfdwmsqwrqegDDEQA---------VRGTLGR--------LLFS---QDDIKKSVKVLSGGEKGRML 448
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 500071467 158 IARALCMEPRVMLFDEPTSALDPEMVgEVLDtmrgLAAE---GmTMMIVTHEMGFARQVADRVVFMDRGQIV 226
Cdd:PRK15064 449 FGKLMMQKPNVLVMDEPTNHMDMESI-ESLN----MALEkyeG-TLIFVSHDREFVSSLATRIIEITPDGVV 514
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
27-232 |
5.11e-12 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 64.08 E-value: 5.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 27 VLTDVSLSVARGEKVVICGPSGSGKSTLIRCL-NQLEQHQE-------GSIVVDGIELGQSENAAQAVRREVgmvfqhfn 98
Cdd:PRK13547 16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALaGDLTGGGAprgarvtGDVTLNGEPLAAIDAPRLARLRAV-------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 99 lfphldLVQNCILA-PMSVRGM--------SRRAAEA------LAVGLLERVRLGEHAHKYPSQLSGGQQQRAAIARALC 163
Cdd:PRK13547 88 ------LPQAAQPAfAFSAREIvllgryphARRAGALthrdgeIAWQALALAGATALVGRDVTTLSGGELARVQFARVLA 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 500071467 164 M---------EPRVMLFDEPTSALDPEMVGEVLDTMRGLAAE-GMTMMIVTHEMGFARQVADRVVFMDRGQIVEQAPPA 232
Cdd:PRK13547 162 QlwpphdaaqPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDwNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPA 240
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
2-219 |
6.60e-12 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 64.83 E-value: 6.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 2 PNPDASPAAPIISVAGVNKWYGAFQvLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDgIELGQSen 81
Cdd:PRK13409 330 PPRDESERETLVEYPDLTKKLGDFS-LEVEGGEIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE-LKISYK-- 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 82 aAQAVRREVgmvfqhfnlfphldlvqncilaPMSVRGMSRRAAEALA-----VGLLERVRLGEHAHKYPSQLSGGQQQRA 156
Cdd:PRK13409 406 -PQYIKPDY----------------------DGTVEDLLRSITDDLGssyykSEIIKPLQLERLLDKNVKDLSGGELQRV 462
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 500071467 157 AIARALCMEPRVMLFDEPTSALDPEMVGEVLDTMRGLAAE-GMTMMIVTHEMGFARQVADRV-VF 219
Cdd:PRK13409 463 AIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAEErEATALVVDHDIYMIDYISDRLmVF 527
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
34-221 |
9.70e-12 |
|
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: 62.81 E-value: 9.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 34 SVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIELG---QSENAAQAVRREvGMVFQHFNLFPHLDLVQNCI 110
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSykpQYIKADYEGTVR-DLLSSITKDFYTHPYFKTEI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 111 LAPMSVRGmsrraaealavgLLERvRLGEhahkypsqLSGGQQQRAAIARALCMEPRVMLFDEPTSALDPE---MVGEVL 187
Cdd:cd03237 100 AKPLQIEQ------------ILDR-EVPE--------LSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEqrlMASKVI 158
|
170 180 190
....*....|....*....|....*....|....
gi 500071467 188 DtmRGLAAEGMTMMIVTHEMGFARQVADRVVFMD 221
Cdd:cd03237 159 R--RFAENNEKTAFVVEHDIIMIDYLADRLIVFE 190
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
6-231 |
1.34e-11 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 64.03 E-value: 1.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 6 ASP--AAPIISVAG------VNKWY--GAFQVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIE 75
Cdd:PTZ00243 1294 ASPtsAAPHPVQAGslvfegVQMRYreGLPLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGRE 1373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 76 LGQSenAAQAVRREVGMVFQHFNLF---------PHLDLVQNCILAPMSVRGMSRRAAeALAVGLLERVRLGEhahkypS 146
Cdd:PTZ00243 1374 IGAY--GLRELRRQFSMIPQDPVLFdgtvrqnvdPFLEASSAEVWAALELVGLRERVA-SESEGIDSRVLEGG------S 1444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 147 QLSGGQQQRAAIARALCMEPR-VMLFDEPTSALDPEMVGEVLDTMRGlAAEGMTMMIVTHEMGFARQVaDRVVFMDRGQI 225
Cdd:PTZ00243 1445 NYSVGQRQLMCMARALLKKGSgFILMDEATANIDPALDRQIQATVMS-AFSAYTVITIAHRLHTVAQY-DKIIVMDHGAV 1522
|
....*.
gi 500071467 226 VEQAPP 231
Cdd:PTZ00243 1523 AEMGSP 1528
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
30-229 |
1.45e-11 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 63.60 E-value: 1.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 30 DVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIELgQSENAAQAVRREVGMVFQH---FNLFPHLDLV 106
Cdd:PRK10982 266 DVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKI-NNHNANEAINHGFALVTEErrsTGIYAYLDIG 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 107 QNCILAPM-SVRGmsrraaealAVGLLERVRLGEHAH--------KYPSQ------LSGGQQQRAAIARALCMEPRVMLF 171
Cdd:PRK10982 345 FNSLISNIrNYKN---------KVGLLDNSRMKSDTQwvidsmrvKTPGHrtqigsLSGGNQQKVIIGRWLLTQPEILML 415
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 500071467 172 DEPTSALDPEMVGEVLDTMRGLAAEGMTMMIVTHEMGFARQVADRVVFMDRGQ---IVEQA 229
Cdd:PRK10982 416 DEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNGLvagIVDTK 476
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
27-231 |
4.39e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 62.69 E-value: 4.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 27 VLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIELgqSENAAQAVRREVGMVFQ---------HF 97
Cdd:PLN03232 1251 VLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDV--AKFGLTDLRRVLSIIPQspvlfsgtvRF 1328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 98 NLFP---HLDLVQNCILAPMSVRGMSRRAAEALAVGLLERvrlGEHahkypsqLSGGQQQRAAIARALCMEPRVMLFDEP 174
Cdd:PLN03232 1329 NIDPfseHNDADLWEALERAHIKDVIDRNPFGLDAEVSEG---GEN-------FSVGQRQLLSLARALLRRSKILVLDEA 1398
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 500071467 175 TSALDPEMVGEVLDTMRGlAAEGMTMMIVTHEMGFARQvADRVVFMDRGQIVEQAPP 231
Cdd:PLN03232 1399 TASVDVRTDSLIQRTIRE-EFKSCTMLVIAHRLNTIID-CDKILVLSSGQVLEYDSP 1453
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
27-244 |
7.34e-11 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 62.10 E-value: 7.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 27 VLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSI-------------------VVDGIELGQSENAAQAVr 87
Cdd:PTZ00243 675 LLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVwaersiayvpqqawimnatVRGNILFFDEEDAARLA- 753
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 88 revgmvfqhfnlfphlDLVQNCILapmsvrgmsrRAAEALAVGLLErVRLGEHAhkypSQLSGGQQQRAAIARALCMEPR 167
Cdd:PTZ00243 754 ----------------DAVRVSQL----------EADLAQLGGGLE-TEIGEKG----VNLSGGQKARVSLARAVYANRD 802
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 500071467 168 VMLFDEPTSALDPEmVGE--VLDTMRGlAAEGMTMMIVTHEMGFARQvADRVVFMDRGQIVEQAPPAAFFGAPVHERTR 244
Cdd:PTZ00243 803 VYLLDDPLSALDAH-VGErvVEECFLG-ALAGKTRVLATHQVHVVPR-ADYVVALGDGRVEFSGSSADFMRTSLYATLA 878
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
27-235 |
7.56e-11 |
|
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: 60.69 E-value: 7.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 27 VLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIELgqSENAAQAVRREVGMVFQ---------HF 97
Cdd:cd03288 36 VLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDI--SKLPLHTLRSRLSIILQdpilfsgsiRF 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 98 NLFPHLDLVQNCILAPMSVRGMsRRAAEALAVGLLERVRLGEHahkypsQLSGGQQQRAAIARALCMEPRVMLFDEPTSA 177
Cdd:cd03288 114 NLDPECKCTDDRLWEALEIAQL-KNMVKSLPGGLDAVVTEGGE------NFSVGQRQLFCLARAFVRKSSILIMDEATAS 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 500071467 178 LDpeMVGE-VLDTMRGLAAEGMTMMIVTHEMGFARQvADRVVFMDRGQIVEQAPPAAFF 235
Cdd:cd03288 187 ID--MATEnILQKVVMTAFADRTVVTIAHRVSTILD-ADLVLVLSRGILVECDTPENLL 242
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
40-220 |
8.36e-11 |
|
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: 61.34 E-value: 8.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 40 KVV-ICGPSGSGKSTLIRCLNqleqhqeGSIVVDgieLGQSENAAqavrrEVGMVFQHFN---LFPHL-DLVQNCI---- 110
Cdd:COG1245 100 KVTgILGPNGIGKSTALKILS-------GELKPN---LGDYDEEP-----SWDEVLKRFRgteLQDYFkKLANGEIkvah 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 111 ------LAPMSVRGMSR----RAAE-ALAVGLLERVRLGEHAHKYPSQLSGGQQQRAAIARALCMEPRVMLFDEPTSALD 179
Cdd:COG1245 165 kpqyvdLIPKVFKGTVRelleKVDErGKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLD 244
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 500071467 180 pemVGE---VLDTMRGLAAEGMTMMIVTHEMGFARQVADRVVFM 220
Cdd:COG1245 245 ---IYQrlnVARLIRELAEEGKYVLVVEHDLAILDYLADYVHIL 285
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
28-218 |
1.29e-10 |
|
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: 59.58 E-value: 1.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 28 LTDVSLSVARGEKVVICGPSGSGKSTLI----------RCLNQLEQ------HQEGSIVVDGIElGQS-------ENAAQ 84
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSSLAfdtiyaegqrRYVESLSAyarqflGQMDKPDVDSIE-GLSpaiaidqKTTSR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 85 AVRREVGMVFQHFNLFphldlvqnCILapMSVRGMSRRAAEALAVGLlERVRLGEHAhkypSQLSGGQQQRAAIARALCM 164
Cdd:cd03270 90 NPRSTVGTVTEIYDYL--------RLL--FARVGIRERLGFLVDVGL-GYLTLSRSA----PTLSGGEAQRIRLATQIGS 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 500071467 165 EPRVML--FDEPTSALDPEMVGEVLDTMRGLAAEGMTMMIVTHEMGFARQvADRVV 218
Cdd:cd03270 155 GLTGVLyvLDEPSIGLHPRDNDRLIETLKRLRDLGNTVLVVEHDEDTIRA-ADHVI 209
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
12-222 |
1.55e-10 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 60.72 E-value: 1.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 12 IISVAGVNKWYGAFQVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVV-DGIELG---QSENA---AQ 84
Cdd:TIGR03719 322 VIEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIgETVKLAyvdQSRDAldpNK 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 85 AVRREV--GmvfqhfnlfphLDLVQncilapMSVRGMSRRAaealAVGllervRL---GEHAHKYPSQLSGGQQQRAAIA 159
Cdd:TIGR03719 402 TVWEEIsgG-----------LDIIK------LGKREIPSRA----YVG-----RFnfkGSDQQKKVGQLSGGERNRVHLA 455
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 500071467 160 RALCMEPRVMLFDEPTSALDPEmvgevldTMRGL--AAEGM--TMMIVTHemgfarqvaDRvVFMDR 222
Cdd:TIGR03719 456 KTLKSGGNVLLLDEPTNDLDVE-------TLRALeeALLNFagCAVVISH---------DR-WFLDR 505
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
7-181 |
1.63e-10 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 59.09 E-value: 1.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 7 SPAAPIISVAGVNKWYGAFQVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIELGQSENAaqav 86
Cdd:PRK13543 6 HTAPPLLAAHALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRS---- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 87 rREVGMVFQHFNLFPHLDLVQNC-ILAPMSVRGMSRRAAEALAVgllerVRLGEHAHKYPSQLSGGQQQRAAIARALCME 165
Cdd:PRK13543 82 -RFMAYLGHLPGLKADLSTLENLhFLCGLHGRRAKQMPGSALAI-----VGLAGYEDTLVRQLSAGQKKRLALARLWLSP 155
|
170
....*....|....*.
gi 500071467 166 PRVMLFDEPTSALDPE 181
Cdd:PRK13543 156 APLWLLDEPYANLDLE 171
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
27-232 |
1.71e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 60.91 E-value: 1.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 27 VLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIELGQSenAAQAVRREVGMVFQ---------HF 97
Cdd:PLN03130 1254 VLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKF--GLMDLRKVLGIIPQapvlfsgtvRF 1331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 98 NLFP---HLDLVQNCILAPMSVRGMSRRAAEALAVGLLERvrlGEHahkypsqLSGGQQQRAAIARALCMEPRVMLFDEP 174
Cdd:PLN03130 1332 NLDPfneHNDADLWESLERAHLKDVIRRNSLGLDAEVSEA---GEN-------FSVGQRQLLSLARALLRRSKILVLDEA 1401
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 500071467 175 TSALDPEMVGEVLDTMRGlAAEGMTMMIVTHEMGFARQvADRVVFMDRGQIVEQAPPA 232
Cdd:PLN03130 1402 TAAVDVRTDALIQKTIRE-EFKSCTMLIIAHRLNTIID-CDRILVLDAGRVVEFDTPE 1457
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
27-205 |
3.61e-10 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 59.76 E-value: 3.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 27 VLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDgielgqSENaaqavrrevgmvfqhfNLF-----P 101
Cdd:TIGR00954 467 LIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKP------AKG----------------KLFyvpqrP 524
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 102 HLDL--VQNCILAPMSVRGMSRRA-AEALAVGLLERVRLG---------EHAHKYPSQLSGGQQQRAAIARALCMEPRVM 169
Cdd:TIGR00954 525 YMTLgtLRDQIIYPDSSEDMKRRGlSDKDLEQILDNVQLThilereggwSAVQDWMDVLSGGEKQRIAMARLFYHKPQFA 604
|
170 180 190
....*....|....*....|....*....|....*.
gi 500071467 170 LFDEPTSALDPEMVGEVLDTMRGLaaeGMTMMIVTH 205
Cdd:TIGR00954 605 ILDECTSAVSVDVEGYMYRLCREF---GITLFSVSH 637
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
27-180 |
4.48e-10 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 59.54 E-value: 4.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 27 VLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLeQHQEGSIVVDGIelgqSENAA--QAVRREVGMVFQHF------- 97
Cdd:TIGR01271 1234 VLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRL-LSTEGEIQIDGV----SWNSVtlQTWRKAFGVIPQKVfifsgtf 1308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 98 --NLFPHldlvqncilAPMSVRGMSRRAAEalaVGLLERVrlgehaHKYPSQ-----------LSGGQQQRAAIARALCM 164
Cdd:TIGR01271 1309 rkNLDPY---------EQWSDEEIWKVAEE---VGLKSVI------EQFPDKldfvlvdggyvLSNGHKQLMCLARSILS 1370
|
170
....*....|....*.
gi 500071467 165 EPRVMLFDEPTSALDP 180
Cdd:TIGR01271 1371 KAKILLLDEPSAHLDP 1386
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
1-205 |
4.83e-10 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 59.26 E-value: 4.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 1 MPNPDASPA-------APIISVAGVNKWYGAFQVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQleQHQEG---SIV 70
Cdd:PRK10938 242 LPEPDEPSArhalpanEPRIVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITG--DHPQGysnDLT 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 71 VDGIELGQSENAAQaVRREVGMVFQHFnlfpHLDL-----VQNCILAPM--SVrGMSRRAAEA---LAVGLLERVRLGEH 140
Cdd:PRK10938 320 LFGRRRGSGETIWD-IKKHIGYVSSSL----HLDYrvstsVRNVILSGFfdSI-GIYQAVSDRqqkLAQQWLDILGIDKR 393
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 141 AHKYPSQ-LSGGQQQRAAIARALCMEPRVMLFDEPTSALDP---EMVGEVLDTMRGlaaEGMTMMI-VTH 205
Cdd:PRK10938 394 TADAPFHsLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPlnrQLVRRFVDVLIS---EGETQLLfVSH 460
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
33-223 |
5.52e-10 |
|
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: 59.26 E-value: 5.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 33 LSVARGEKVVICGPSGSGKSTLIRCLNqleqhqeGSIVVDGielGQSENAAQAVRREVGMVFQHFNLFPHLDLVQNCILA 112
Cdd:TIGR01257 1960 VGVRPGECFGLLGVNGAGKTTTFKMLT-------GDTTVTS---GDATVAGKSILTNISDVHQNMGYCPQFDAIDDLLTG 2029
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 113 P------MSVRGMSRRAAEALAVGLLERVRLGEHAHKYPSQLSGGQQQRAAIARALCMEPRVMLFDEPTSALDPEMVGEV 186
Cdd:TIGR01257 2030 RehlylyARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRML 2109
|
170 180 190
....*....|....*....|....*....|....*..
gi 500071467 187 LDTMRGLAAEGMTMMIVTHEMGFARQVADRVVFMDRG 223
Cdd:TIGR01257 2110 WNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKG 2146
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
12-224 |
5.87e-10 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 58.98 E-value: 5.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 12 IISVAGVNKWYGA-FQVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVV-DGIELG--QSE---NAAQ 84
Cdd:PRK11819 6 IYTMNRVSKVVPPkKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPaPGIKVGylPQEpqlDPEK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 85 AVRREVGMVFQH-FNLFPHLDLVQNCILAPMS-----VRGMSR------------------RAAEALavgllervRLgeh 140
Cdd:PRK11819 86 TVRENVEEGVAEvKAALDRFNEIYAAYAEPDAdfdalAAEQGElqeiidaadawdldsqleIAMDAL--------RC--- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 141 ahkyP------SQLSGGQQQRAAIARALCMEPRVMLFDEPTSALDPEMVG--EvldtmRGLAAEGMTMMIVTHEMGFARQ 212
Cdd:PRK11819 155 ----PpwdakvTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAwlE-----QFLHDYPGTVVAVTHDRYFLDN 225
|
250
....*....|..
gi 500071467 213 VADRVVFMDRGQ 224
Cdd:PRK11819 226 VAGWILELDRGR 237
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
25-227 |
8.55e-10 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 57.52 E-value: 8.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 25 FQVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGielgqsenaaqavrrEVGMVFQHFNLFPHLD 104
Cdd:PRK13546 37 FFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG---------------EVSVIAISAGLSGQLT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 105 LVQNcILAPMSVRGMSRRAAEALAVGLLERVRLGEHAHKYPSQLSGGQQQRAAIARALCMEPRVMLFDEPTSALDPEMVG 184
Cdd:PRK13546 102 GIEN-IEFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQ 180
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 500071467 185 EVLDTMRGLAAEGMTMMIVTHEMGFARQVADRVVFMDRGQIVE 227
Cdd:PRK13546 181 KCLDKIYEFKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKD 223
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
27-206 |
9.54e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 56.50 E-value: 9.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 27 VLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIELGQSENAAQavrREVGMVFQHFNLFPHLDLV 106
Cdd:PRK13540 16 LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQ---KQLCFVGHRSGINPYLTLR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 107 QNCILAPMSVRGmsrraaealAVGLLERVRLG--EHAHKYP-SQLSGGQQQRAAIARALCMEPRVMLFDEPTSALDPEMV 183
Cdd:PRK13540 93 ENCLYDIHFSPG---------AVGITELCRLFslEHLIDYPcGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSL 163
|
170 180
....*....|....*....|...
gi 500071467 184 GEVLDTMRGLAAEGMTMMIVTHE 206
Cdd:PRK13540 164 LTIITKIQEHRAKGGAVLLTSHQ 186
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
37-223 |
9.77e-10 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 55.84 E-value: 9.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 37 RGEKVVICGPSGSGKSTLIRCL-NQLEQHQEGSIVVDGIELGQSenaaqavrrevgmvfqhfnlfphldlvqncilapms 115
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALaRELGPPGGGVIYIDGEDILEE------------------------------------ 44
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 116 vrgmsrraaealavglLERVRLGEHAHKYPSQLSGGQQQRAAIARALCMEPRVMLFDEPTSALDPEMVGEVLDTMRG--- 192
Cdd:smart00382 45 ----------------VLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELrll 108
|
170 180 190
....*....|....*....|....*....|....*....
gi 500071467 193 ---LAAEGMTMMIVTHEMGF-----ARQVADRVVFMDRG 223
Cdd:smart00382 109 lllKSEKNLTVILTTNDEKDlgpalLRRRFDRRIVLLLI 147
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
17-223 |
1.01e-09 |
|
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: 56.96 E-value: 1.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 17 GVNKWYGAFQVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSI-------VVDGIELGQSEN---AAQAV 86
Cdd:cd03290 6 GYFSWGSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhwsnkneSEPSFEATRSRNrysVAYAA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 87 RR--------EVGMVFQH-FNLFPHLDLVQNCILAPmsvrgmsrrAAEALAVGllERVRLGEHAhkypSQLSGGQQQRAA 157
Cdd:cd03290 86 QKpwllnatvEENITFGSpFNKQRYKAVTDACSLQP---------DIDLLPFG--DQTEIGERG----INLSGGQRQRIC 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 500071467 158 IARALCMEPRVMLFDEPTSALDPEMVGEVLDT--MRGLAAEGMTMMIVTHEMGFARQvADRVVFMDRG 223
Cdd:cd03290 151 VARALYQNTNIVFLDDPFSALDIHLSDHLMQEgiLKFLQDDKRTLVLVTHKLQYLPH-ADWIIAMKDG 217
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
2-219 |
1.03e-09 |
|
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: 58.26 E-value: 1.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 2 PNPDASPAAPIISVAGVNKWYGAFqvltdvSLSVA-----RGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDgIEL 76
Cdd:COG1245 331 APRREKEEETLVEYPDLTKSYGGF------SLEVEggeirEGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDED-LKI 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 77 GQSenaAQAVRREvgmvfqhfnlfphldlvqncilAPMSVRGMSRRAAEA------LAVGLLERVRLGEHAHKYPSQLSG 150
Cdd:COG1245 404 SYK---PQYISPD----------------------YDGTVEEFLRSANTDdfgssyYKTEIIKPLGLEKLLDKNVKDLSG 458
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 500071467 151 GQQQRAAIARALCMEPRVMLFDEPTSALDPEMVGEVLDTMRGLAAE-GMTMMIVTHEMGFARQVADRV-VF 219
Cdd:COG1245 459 GELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAENrGKTAMVVDHDIYLIDYISDRLmVF 529
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
12-243 |
1.18e-09 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 58.21 E-value: 1.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 12 IISVAGVNKWYGAFQVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIELGQSenaaqAVRREVG 91
Cdd:NF033858 1 VARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMADA-----RHRRAVC 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 92 -----MVfQHF--NLFPHLdlvqncilapmSVR----------GMSRRAAEALAVGLLERVRLGEHAHKYPSQLSGGQQQ 154
Cdd:NF033858 76 priayMP-QGLgkNLYPTL-----------SVFenldffgrlfGQDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 155 RAAIARALCMEPRVMLFDEPTSALDP-------EMVgevlDTMRGlAAEGMTMMIVTHEMGFARQVaDRVVFMDRGQIVE 227
Cdd:NF033858 144 KLGLCCALIHDPDLLILDEPTTGVDPlsrrqfwELI----DRIRA-ERPGMSVLVATAYMEEAERF-DWLVAMDAGRVLA 217
|
250
....*....|....*.
gi 500071467 228 QAPPAAffgapVHERT 243
Cdd:NF033858 218 TGTPAE-----LLART 228
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
40-207 |
1.27e-09 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 57.90 E-value: 1.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 40 KVV-ICGPSGSGKSTLIRCLNqleqhqeGSIVVDgieLGQSENAAQAVRrevgmVFQHFN---LFPHL-DLVQNCI---- 110
Cdd:PRK13409 100 KVTgILGPNGIGKTTAVKILS-------GELIPN---LGDYEEEPSWDE-----VLKRFRgteLQNYFkKLYNGEIkvvh 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 111 ------LAPMSVRGMSR----RAAEALAVG-LLERVRLGEHAHKYPSQLSGGQQQRAAIARALCMEPRVMLFDEPTSALD 179
Cdd:PRK13409 165 kpqyvdLIPKVFKGKVRellkKVDERGKLDeVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLD 244
|
170 180 190
....*....|....*....|....*....|.
gi 500071467 180 pemVGE---VLDTMRGLaAEGMTMMIVTHEM 207
Cdd:PRK13409 245 ---IRQrlnVARLIREL-AEGKYVLVVEHDL 271
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
26-226 |
1.72e-09 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 57.49 E-value: 1.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 26 QVLTDVSLSVARGEKVVICGPSGSGKSTLIRCL--NQLEQHQEGSIVVDGIELGQSeNAAQAV----------RREVGMV 93
Cdd:NF040905 274 KVVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVfgRSYGRNISGTVFKDGKEVDVS-TVSDAIdaglayvtedRKGYGLN 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 94 FQHfnlfphlDLVQNCILApmSVRGMSRRaaealavGLLERVRLGEHAHKY--------PS------QLSGGQQQRAAIA 159
Cdd:NF040905 353 LID-------DIKRNITLA--NLGKVSRR-------GVIDENEEIKVAEEYrkkmniktPSvfqkvgNLSGGNQQKVVLS 416
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 160 RALCMEPRVMLFDEPTSALDpemVG---EVLDTMRGLAAEGMTMMIVTHEMGFARQVADRVVFMDRGQIV 226
Cdd:NF040905 417 KWLFTDPDVLILDEPTRGID---VGakyEIYTIINELAAEGKGVIVISSELPELLGMCDRIYVMNEGRIT 483
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
144-179 |
8.84e-09 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 55.81 E-value: 8.84e-09
10 20 30
....*....|....*....|....*....|....*.
gi 500071467 144 YPSQLSGGQQQRAAIARALCMEPRVMLFDEPTSALD 179
Cdd:PTZ00265 1355 YGKSLSGGQKQRIAIARALLREPKILLLDEATSSLD 1390
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
29-205 |
1.21e-08 |
|
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: 52.75 E-value: 1.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 29 TDVSLSvaRGEKVVICGPSGSGKSTLIRClnqleqhqegsivvdgIELGqsenaaqavrreVGMvfQHFNLFPHLDLVQN 108
Cdd:cd03227 14 NDVTFG--EGSLTIITGPNGSGKSTILDA----------------IGLA------------LGG--AQSATRRRSGVKAG 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 109 CILAPMSVRGMSRRaaealavgllervrlgehahkypSQLSGGQQQRAAIARAL----CMEPRVMLFDEPTSALDPEMVG 184
Cdd:cd03227 62 CIVAAVSAELIFTR-----------------------LQLSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQ 118
|
170 180
....*....|....*....|.
gi 500071467 185 EVLDTMRGLAAEGMTMMIVTH 205
Cdd:cd03227 119 ALAEAILEHLVKGAQVIVITH 139
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
20-218 |
2.03e-08 |
|
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: 52.57 E-value: 2.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 20 KWYGAFQVLTDVSlSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVVDGIELgqsenaaqavrrevgmvfqhfnl 99
Cdd:cd03222 8 KRYGVFFLLVELG-VVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITP----------------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 100 fphldlvqncILAPMSVrgmsrraaealavgllervrlgehahkypsQLSGGQQQRAAIARALCMEPRVMLFDEPTSALD 179
Cdd:cd03222 64 ----------VYKPQYI------------------------------DLSGGELQRVAIAAALLRNATFYLFDEPSAYLD 103
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 500071467 180 PEMVGEVLDTMRGLAAEGM-TMMIVTHEMGFARQVADRVV 218
Cdd:cd03222 104 IEQRLNAARAIRRLSEEGKkTALVVEHDLAVLDYLSDRIH 143
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
26-218 |
2.67e-08 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 54.19 E-value: 2.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 26 QVLTDVSLSVARGEKVVICGPSGSGKSTL--------------IRCLNQLE-----QHQEG----SIVVDGIELGQSENA 82
Cdd:PRK11147 333 QLVKDFSAQVQRGDKIALIGPNGCGKTTLlklmlgqlqadsgrIHCGTKLEvayfdQHRAEldpeKTVMDNLAEGKQEVM 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 83 AQAVRREVGMVFQHFnLFPhldlvqncilaPMsvRGMSRRAAealavgllervrlgehahkypsqLSGGQQQRAAIARAL 162
Cdd:PRK11147 413 VNGRPRHVLGYLQDF-LFH-----------PK--RAMTPVKA-----------------------LSGGERNRLLLARLF 455
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 500071467 163 CMEPRVMLFDEPTSALDPEMVgEVLDTMrgLAAEGMTMMIVTHEmgfaRQVADRVV 218
Cdd:PRK11147 456 LKPSNLLILDEPTNDLDVETL-ELLEEL--LDSYQGTVLLVSHD----RQFVDNTV 504
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
146-222 |
3.43e-08 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 53.88 E-value: 3.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 146 SQLSGGQQQRAAIARALCMEPRVMLFDEPTSALDPE---MVGEVLDTMRGlaAEGMTMMIVTHEMGFARQVADRVVFMDR 222
Cdd:PTZ00265 578 SKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKseyLVQKTINNLKG--NENRITIIIAHRLSTIRYANTIFVLSNR 655
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
23-180 |
7.01e-08 |
|
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: 52.16 E-value: 7.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 23 GAFQVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLeQHQEGSIVVDGIELGQSenAAQAVRREVGMVFQHFNLFPH 102
Cdd:cd03289 15 GGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRL-LNTEGDIQIDGVSWNSV--PLQKWRKAFGVIPQKVFIFSG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 103 lDLVQNciLAPMSvrgmSRRAAEALAVGllERVRLGEHAHKYPSQ-----------LSGGQQQRAAIARALCMEPRVMLF 171
Cdd:cd03289 92 -TFRKN--LDPYG----KWSDEEIWKVA--EEVGLKSVIEQFPGQldfvlvdggcvLSHGHKQLMCLARSVLSKAKILLL 162
|
....*....
gi 500071467 172 DEPTSALDP 180
Cdd:cd03289 163 DEPSAHLDP 171
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
26-205 |
7.67e-08 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 51.72 E-value: 7.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 26 QVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQ--EGSIVVDG---IELGQSENAAQAVRrevgMVFQHFNLF 100
Cdd:PRK09580 15 AILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDYEvtGGTVEFKGkdlLELSPEDRAGEGIF----MAFQYPVEI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 101 PHldlVQNCILAPMSVRGMSR-RAAEAL-----AVGLLERVRLgehaHKYPSQL---------SGGQQQRAAIARALCME 165
Cdd:PRK09580 91 PG---VSNQFFLQTALNAVRSyRGQEPLdrfdfQDLMEEKIAL----LKMPEDLltrsvnvgfSGGEKKRNDILQMAVLE 163
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 500071467 166 PRVMLFDEPTSALDPEMVGEVLDTMRGLAAEGMTMMIVTH 205
Cdd:PRK09580 164 PELCILDESDSGLDIDALKIVADGVNSLRDGKRSFIIVTH 203
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
28-231 |
1.68e-07 |
|
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: 50.69 E-value: 1.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 28 LTDVSLSVARGEKVVICGPSGSGKSTLI-----RCLNQLEQHQEGS----------------IVVDGIELGQS--ENAA- 83
Cdd:cd03271 11 LKNIDVDIPLGVLTCVTGVSGSGKSSLIndtlyPALARRLHLKKEQpgnhdrieglehidkvIVIDQSPIGRTprSNPAt 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 84 ----------------QAVR--REVGMV-FQHFNLFPHLDlvqncilapMSVR----------GMSRRAAEALAVGLlER 134
Cdd:cd03271 91 ytgvfdeirelfcevcKGKRynRETLEVrYKGKSIADVLD---------MTVEealeffenipKIARKLQTLCDVGL-GY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 135 VRLGEHAhkypSQLSGGQQQRAAIARALCMEPR---VMLFDEPTSALDPEMVGEVLDTMRGLAAEGMTMMIVTHEMGFAR 211
Cdd:cd03271 161 IKLGQPA----TTLSGGEAQRIKLAKELSKRSTgktLYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIEHNLDVIK 236
|
250 260
....*....|....*....|....*.
gi 500071467 212 qVADRVVFM-----DR-GQIVEQAPP 231
Cdd:cd03271 237 -CADWIIDLgpeggDGgGQVVASGTP 261
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
146-207 |
1.73e-07 |
|
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: 50.83 E-value: 1.73e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 500071467 146 SQLSGGQQQRAAIARALCMEPRVMLFDEPTSALDPEMVGEVLDTMRGLAAEGMTMMIVTHEM 207
Cdd:cd03236 138 DQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRLNAARLIRELAEDDNYVLVVEHDL 199
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
26-223 |
3.71e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 50.88 E-value: 3.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 26 QVLTDVSLSVARGEKVVICGPSGSGKSTLircLNQLEQHQEGSIVVDGIELGQSENAAQAVRREVGMVFQhfnlfphldl 105
Cdd:TIGR00956 777 VILNNVDGWVKPGTLTALMGASGAGKTTL---LNVLAERVTTGVITGGDRLVNGRPLDSSFQRSIGYVQQ---------- 843
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 106 vQNCILAPMSVRGMSRRAA---EALAVGLLERVRLGEHAHK------YPSQLSG--------GQQQRAAIARALCMEPRV 168
Cdd:TIGR00956 844 -QDLHLPTSTVRESLRFSAylrQPKSVSKSEKMEYVEEVIKllemesYADAVVGvpgeglnvEQRKRLTIGVELVAKPKL 922
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 500071467 169 MLF-DEPTSALDPEMVGEVLDTMRGLAAEGMTMMIVTHE---MGFARqvADRVVFMDRG 223
Cdd:TIGR00956 923 LLFlDEPTSGLDSQTAWSICKLMRKLADHGQAILCTIHQpsaILFEE--FDRLLLLQKG 979
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
2-206 |
6.58e-07 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 49.86 E-value: 6.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 2 PNPDASPAAPIISVAGVNKWY-GAFQVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVvdgielgqse 80
Cdd:PLN03073 498 PTPDDRPGPPIISFSDASFGYpGGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVF---------- 567
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 81 naaQAVRREVGMVFQHFnlFPHLDLVQNCILAPMsvRGMSRRAAEALAVGLLERVRLGEHAHKYPSQLSGGQQQRAAIAR 160
Cdd:PLN03073 568 ---RSAKVRMAVFSQHH--VDGLDLSSNPLLYMM--RCFPGVPEQKLRAHLGSFGVTGNLALQPMYTLSGGQKSRVAFAK 640
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 500071467 161 ALCMEPRVMLFDEPTSALDPEMVgEVLdtMRGLAAEGMTMMIVTHE 206
Cdd:PLN03073 641 ITFKKPHILLLDEPSNHLDLDAV-EAL--IQGLVLFQGGVLMVSHD 683
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
16-227 |
8.32e-07 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 48.87 E-value: 8.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 16 AGVNKwygaFQVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQ--EGSIVVDGIELGQSENAAQAvRREVGMV 93
Cdd:CHL00131 15 ASVNE----NEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPAYKilEGDILFKGESILDLEPEERA-HLGIFLA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 94 FQHfnlfphldlvqncilaPMSVRGMS-----------RRAAEALA-----------VGLLERVRLGEH-AHKYPSQ-LS 149
Cdd:CHL00131 90 FQY----------------PIEIPGVSnadflrlaynsKRKFQGLPeldplefleiiNEKLKLVGMDPSfLSRNVNEgFS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 150 GGQQQRAAIARALCMEPRVMLFDEPTSALDPEMVGEVLDTMRGLAAEGMTMMIVTHemgFARQ----VADRVVFMDRGQI 225
Cdd:CHL00131 154 GGEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIILITH---YQRLldyiKPDYVHVMQNGKI 230
|
..
gi 500071467 226 VE 227
Cdd:CHL00131 231 IK 232
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
5-218 |
1.15e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 49.09 E-value: 1.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 5 DASPAAPIISVAGVNKWYGAFQVLTDVSLSVARGEKVVICGPSGSGKSTLIRCL----------NQLEQHQEGSIVVDGI 74
Cdd:PLN03073 170 GGGPAIKDIHMENFSISVGGRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRYMamhaidgipkNCQILHVEQEVVGDDT 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 75 E-----LGQSENAAQAVRREVGMVFQHFNLFPHLDLVQNCILAPMSVRG--MSRR--------------AAEALAVGLLE 133
Cdd:PLN03073 250 TalqcvLNTDIERTQLLEEEAQLVAQQRELEFETETGKGKGANKDGVDKdaVSQRleeiykrlelidayTAEARAASILA 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 134 RVRLG-EHAHKYPSQLSGGQQQRAAIARALCMEPRVMLFDEPTSALDpemVGEVLDTMRGLAAEGMTMMIVTHemgfARQ 212
Cdd:PLN03073 330 GLSFTpEMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLD---LHAVLWLETYLLKWPKTFIVVSH----ARE 402
|
....*.
gi 500071467 213 VADRVV 218
Cdd:PLN03073 403 FLNTVV 408
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
8-193 |
1.25e-06 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 48.96 E-value: 1.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 8 PAAP-----IISVAGVNKWYGAFQVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSIVV-DGIELG---Q 78
Cdd:PRK11819 315 PPGPrlgdkVIEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIgETVKLAyvdQ 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 79 SE---NAAQAVRREV--GmvfqhfnlfphLDLVQncilapMSVRGMSRRAaealAVGllervRL---GEHAHKYPSQLSG 150
Cdd:PRK11819 395 SRdalDPNKTVWEEIsgG-----------LDIIK------VGNREIPSRA----YVG-----RFnfkGGDQQKKVGVLSG 448
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 500071467 151 GQQQRAAIARALCMEPRVMLFDEPTSALDPEmvgevldTMRGL 193
Cdd:PRK11819 449 GERNRLHLAKTLKQGGNVLLLDEPTNDLDVE-------TLRAL 484
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
124-225 |
2.77e-06 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 47.96 E-value: 2.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 124 AEALAVGLLERVRLGEHAHKYP-SQLSGGQQQRAAIARALCMEPRVMLFDEPTSALDpemvgevLDTMRGLaaEGM---- 198
Cdd:PRK15064 131 AEARAGELLLGVGIPEEQHYGLmSEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLD-------INTIRWL--EDVlner 201
|
90 100
....*....|....*....|....*....
gi 500071467 199 --TMMIVTHEMGFARQVADRVVFMDRGQI 225
Cdd:PRK15064 202 nsTMIIISHDRHFLNSVCTHMADLDYGEL 230
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
42-222 |
3.89e-06 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 46.45 E-value: 3.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 42 VICGPSGSGKSTLIRCLN-----QLEQHQEGSIVVDGIelgqseNAAQAVRREVGMVFQHFN-----LFPHLDLVQNCIL 111
Cdd:cd03240 26 LIVGQNGAGKTTIIEALKyaltgELPPNSKGGAHDPKL------IREGEVRAQVKLAFENANgkkytITRSLAILENVIF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 112 ApmsvrgmsrRAAEALAVGLLERVRLgehahkypsqlSGGQQQ------RAAIARALCMEPRVMLFDEPTSALDPEMVGE 185
Cdd:cd03240 100 C---------HQGESNWPLLDMRGRC-----------SGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENIEE 159
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 500071467 186 VL----DTMRGLaaEGMTMMIVTHEMGFaRQVADRVVFMDR 222
Cdd:cd03240 160 SLaeiiEERKSQ--KNFQLIVITHDEEL-VDAADHIYRVEK 197
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
25-230 |
4.19e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 47.41 E-value: 4.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 25 FQVLTDVSLSVARGEKVVICGPSGSGKSTLIRCL-NQLEQHQ---EGSIVVDGIELgqsENAAQAVRREVGMVFQHFNLF 100
Cdd:TIGR00956 74 FDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIaSNTDGFHigvEGVITYDGITP---EEIKKHYRGDVVYNAETDVHF 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 101 PH------LDLVQNCILAPMSVRGMSR------RAAEALAVGLLERVRLGEHAHKYPSQLSGGQQQRAAIARALCMEPRV 168
Cdd:TIGR00956 151 PHltvgetLDFAARCKTPQNRPDGVSReeyakhIADVYMATYGLSHTRNTKVGNDFVRGVSGGERKRVSIAEASLGGAKI 230
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 500071467 169 MLFDEPTSALDPEMVGEVLDTMRGLAAEGMTMMIVThemgfARQVA-------DRVVFMDRGQIVEQAP 230
Cdd:TIGR00956 231 QCWDNATRGLDSATALEFIRALKTSANILDTTPLVA-----IYQCSqdayelfDKVIVLYEGYQIYFGP 294
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
4-225 |
4.34e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 47.47 E-value: 4.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 4 PDASPAaPIISVAGVNKWYGAFQVLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSI-VVDGIELGQSENA 82
Cdd:PRK10636 305 PESLPN-PLLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIgLAKGIKLGYFAQH 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 83 AQAVRREVGMVFQHfnlfphldlvqncilapmsvrgMSRRAAEALAVGLleRVRL------GEHAHKYPSQLSGGQQQRA 156
Cdd:PRK10636 384 QLEFLRADESPLQH----------------------LARLAPQELEQKL--RDYLggfgfqGDKVTEETRRFSGGEKARL 439
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 500071467 157 AIARALCMEPRVMLFDEPTSALDPEM---VGEVLDTMRGlaaegmTMMIVTHEMGFARQVADRVVFMDRGQI 225
Cdd:PRK10636 440 VLALIVWQRPNLLLLDEPTNHLDLDMrqaLTEALIDFEG------ALVVVSHDRHLLRSTTDDLYLVHDGKV 505
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
148-239 |
6.06e-06 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 47.13 E-value: 6.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 148 LSGGQQQRAAIARALCMEPR--VMLFDEPTSALDPEMVGEVLDTMRGLAAEGMTMMIVTHEmgfarqvaDRVV-FMDRgq 224
Cdd:PRK00635 477 LSGGEQERTALAKHLGAELIgiTYILDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEHD--------EQMIsLADR-- 546
|
90
....*....|....*
gi 500071467 225 IVEQAPPAAFFGAPV 239
Cdd:PRK00635 547 IIDIGPGAGIFGGEV 561
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
129-231 |
6.90e-06 |
|
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: 46.93 E-value: 6.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 129 VGLlERVRLGEHAhkypSQLSGGQQQRAAIARALCME---PRVMLFDEPTSALDPEMVGEVLDTMRGLAAEGMTMMIVTH 205
Cdd:TIGR00630 816 VGL-GYIRLGQPA----TTLSGGEAQRIKLAKELSKRstgRTLYILDEPTTGLHFDDIKKLLEVLQRLVDKGNTVVVIEH 890
|
90 100 110
....*....|....*....|....*....|..
gi 500071467 206 EMGFARQvADRVVFM-----DR-GQIVEQAPP 231
Cdd:TIGR00630 891 NLDVIKT-ADYIIDLgpeggDGgGTVVASGTP 921
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
41-205 |
2.11e-05 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 44.23 E-value: 2.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 41 VVICGPSGSGKSTLIRCLNQL---EQHQEGSIVVDGIELGQSENaaqavrrEVGMVFQH-------------FNLFPHLD 104
Cdd:COG0419 26 NLIVGPNGAGKSTILEAIRYAlygKARSRSKLRSDLINVGSEEA-------SVELEFEHggkryrierrqgeFAEFLEAK 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 105 ------LVQNcILAPMSVRGMSRRAAE---ALAVGLLERVRLGEHAHKY---------PSQLSGGQQQRAAIARALcmep 166
Cdd:COG0419 99 pserkeALKR-LLGLEIYEELKERLKEleeALESALEELAELQKLKQEIlaqlsgldpIETLSGGERLRLALADLL---- 173
|
170 180 190
....*....|....*....|....*....|....*....
gi 500071467 167 rVMLFDepTSALDPEMVGEVLDTMRGLAaegmtmmIVTH 205
Cdd:COG0419 174 -SLILD--FGSLDEERLERLLDALEELA-------IITH 202
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
27-224 |
3.05e-05 |
|
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: 44.08 E-value: 3.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 27 VLTDVSLSVARGEKVVICGPSGSGKSTLIRCLnqleqhqegsivvdgieLGQSENAAQAVRREVGMVFQHfnlfphldlv 106
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLI-----------------LGELEPSEGKIKHSGRISFSS---------- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 107 QNCILAPMSVR-----GMSRRAAEALAVglLERVRLGEHAHKYPSQ-----------LSGGQQQRAAIARALCMEPRVML 170
Cdd:cd03291 105 QFSWIMPGTIKeniifGVSYDEYRYKSV--VKACQLEEDITKFPEKdntvlgeggitLSGGQRARISLARAVYKDADLYL 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 500071467 171 FDEPTSALDPEMVGEVLDTMRGLAAEGMTMMIVTHEMGFARQvADRVVFMDRGQ 224
Cdd:cd03291 183 LDSPFGYLDVFTEKEIFESCVCKLMANKTRILVTSKMEHLKK-ADKILILHEGS 235
|
|
| Kti12 |
COG4088 |
tRNA uridine 5-carbamoylmethylation protein Kti12 (Killer toxin insensitivity protein) ... |
36-90 |
3.65e-05 |
|
tRNA uridine 5-carbamoylmethylation protein Kti12 (Killer toxin insensitivity protein) [Translation, ribosomal structure and biogenesis, Defense mechanisms];
Pssm-ID: 443264 [Multi-domain] Cd Length: 179 Bit Score: 43.18 E-value: 3.65e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 36 ARGEKVVICGPSGSGKSTLIRCLNQlEQHQEGSIVV----DGI-ELGQSENAAQAVRREV 90
Cdd:COG4088 2 DSPMLLILTGPPGSGKTTFAKALAQ-RLYAEGIAVAllhsDDFrRFLVNESFPKETYEEV 60
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
147-203 |
8.60e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 43.08 E-value: 8.60e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 500071467 147 QLSGGQQQRAAIARALCMEPRVMLFDEPTSALDPEMVGEVLDTMRGLAAEGMTMMIV 203
Cdd:PRK10938 135 YLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQSGITLVLV 191
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
28-54 |
1.20e-04 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 43.09 E-value: 1.20e-04
10 20
....*....|....*....|....*..
gi 500071467 28 LTDVSLSVARGEKVVICGPSGSGKSTL 54
Cdd:COG0178 16 LKNIDVDIPRNKLVVITGLSGSGKSSL 42
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
148-230 |
1.28e-04 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 42.91 E-value: 1.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 148 LSGGQQQRAAIARALCMEPRVMLFDEPTSALDPEMVGEVLDTMRGLAAEGMTMMIVTHEMGF-ARQVADRVVFMDR-GQI 225
Cdd:PLN03140 1020 LSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQPSIdIFEAFDELLLMKRgGQV 1099
|
....*
gi 500071467 226 VEQAP 230
Cdd:PLN03140 1100 IYSGP 1104
|
|
| GMPK |
cd00071 |
Guanosine monophosphate kinase (GMPK, EC 2.7.4.8), also known as guanylate kinase (GKase), ... |
41-60 |
1.63e-04 |
|
Guanosine monophosphate kinase (GMPK, EC 2.7.4.8), also known as guanylate kinase (GKase), catalyzes the reversible phosphoryl transfer from adenosine triphosphate (ATP) to guanosine monophosphate (GMP) to yield adenosine diphosphate (ADP) and guanosine diphosphate (GDP). It plays an essential role in the biosynthesis of guanosine triphosphate (GTP). This enzyme is also important for the activation of some antiviral and anticancer agents, such as acyclovir, ganciclovir, carbovir, and thiopurines.
Pssm-ID: 238026 Cd Length: 137 Bit Score: 40.59 E-value: 1.63e-04
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
145-205 |
4.89e-04 |
|
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: 40.84 E-value: 4.89e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 500071467 145 PSQLSGGQQQ---RAAIARALCMEPRVMLFDEPTSALDPEMVGEVLDTMRGLAAEGMTMMIVTH 205
Cdd:pfam13304 234 AFELSDGTKRllaLLAALLSALPKGGLLLIDEPESGLHPKLLRRLLELLKELSRNGAQLILTTH 297
|
|
| Gmk |
COG0194 |
Guanylate kinase [Nucleotide transport and metabolism]; |
41-66 |
6.09e-04 |
|
Guanylate kinase [Nucleotide transport and metabolism];
Pssm-ID: 439964 Cd Length: 190 Bit Score: 39.67 E-value: 6.09e-04
10 20
....*....|....*....|....*.
gi 500071467 41 VVICGPSGSGKSTLIRCLnqLEQHQE 66
Cdd:COG0194 5 IVLSGPSGAGKTTLVKAL--LERDPD 28
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
146-218 |
8.49e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 40.58 E-value: 8.49e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 500071467 146 SQLSGGQQQRAAIARALCM---EPRVMLFDEPTSALDPEMVGEVLDTMRGLAAEGMTMMIVTHEMGFARqVADRVV 218
Cdd:PRK00635 808 SSLSGGEIQRLKLAYELLApskKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVVIIEHNMHVVK-VADYVL 882
|
|
| AAA_22 |
pfam13401 |
AAA domain; |
41-91 |
8.68e-04 |
|
AAA domain;
Pssm-ID: 379165 [Multi-domain] Cd Length: 129 Bit Score: 38.48 E-value: 8.68e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 500071467 41 VVICGPSGSGKSTLIRCL-NQLEQHQEGSIVVDGIELGQSENAAQAVRREVG 91
Cdd:pfam13401 8 LVLTGESGTGKTTLLRRLlEQLPEVRDSVVFVDLPSGTSPKDLLRALLRALG 59
|
|
| SbcC_Walker_B |
pfam13558 |
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from ... |
146-191 |
1.39e-03 |
|
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from eukaryotes and the prokaryotic homolog SbcCD complex subunit C. RAD50-ATPase forms a complex with Mre11-nuclease that detects and processes diverse and obstructed DNA ends. This domain is separated of the Walker A domain by a long coiled-coil domain and forms the nucleotide-binding domain (NBD) when the coiled coils fold back on themselves and bring together Walker A and B domains. Two RAD50-NBDs forms heterotetramers with a Mre11 nuclease dimer that assemble as catalytic head module that binds and cleaves DNA in an ATP-dependent reaction. Through secondary structural analysis, it has been suggested that there is a wide structural conservation in the Rad50/SMC protein family as seen in structural similarities between RAD50's hook and ABC-ATPase MukB's elbow region.
Pssm-ID: 463921 [Multi-domain] Cd Length: 90 Bit Score: 36.83 E-value: 1.39e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 500071467 146 SQLSGGQQQR-------AAIARALCME------PRVMLFDEPTSALDPEMVGEVLDTMR 191
Cdd:pfam13558 31 GGLSGGEKQLlaylplaAALAAQYGSAegrppaPRLVFLDEAFAKLDEENIRTALELLR 89
|
|
| ExeA |
COG3267 |
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, ... |
26-64 |
2.65e-03 |
|
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];
Pssm-ID: 442498 [Multi-domain] Cd Length: 261 Bit Score: 38.23 E-value: 2.65e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 500071467 26 QVLTDVSLSVARGEK-VVICGPSGSGKSTLIRCL-NQLEQH 64
Cdd:COG3267 30 EALARLEYALAQGGGfVVLTGEVGTGKTTLLRRLlERLPDD 70
|
|
| COG4185 |
COG4185 |
Predicted ABC-type ATPase or kinase [General function prediction only]; |
41-96 |
4.06e-03 |
|
Predicted ABC-type ATPase or kinase [General function prediction only];
Pssm-ID: 443339 Cd Length: 197 Bit Score: 37.18 E-value: 4.06e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 500071467 41 VVICGPSGSGKSTLIRCLnqLEQHQEGSIVV--DGIELGQSENAAQAVRREVGMVFQH 96
Cdd:COG4185 7 YIIAGPNGAGKSTFARTI--LPEELGGLEFVnaDLIARGLSPFNPETAAYEAGRLALE 62
|
|
| gmk |
PRK00300 |
guanylate kinase; Provisional |
37-66 |
4.06e-03 |
|
guanylate kinase; Provisional
Pssm-ID: 234719 Cd Length: 205 Bit Score: 37.38 E-value: 4.06e-03
10 20 30
....*....|....*....|....*....|
gi 500071467 37 RGEKVVICGPSGSGKSTLIRCLnqLEQHQE 66
Cdd:PRK00300 4 RGLLIVLSGPSGAGKSTLVKAL--LERDPN 31
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
28-54 |
4.41e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 38.07 E-value: 4.41e-03
10 20
....*....|....*....|....*..
gi 500071467 28 LTDVSLSVARGEKVVICGPSGSGKSTL 54
Cdd:TIGR00630 12 LKNIDVEIPRDKLVVITGLSGSGKSSL 38
|
|
| COG4639 |
COG4639 |
Predicted kinase [General function prediction only]; |
41-72 |
4.81e-03 |
|
Predicted kinase [General function prediction only];
Pssm-ID: 443677 [Multi-domain] Cd Length: 145 Bit Score: 36.35 E-value: 4.81e-03
10 20 30
....*....|....*....|....*....|..
gi 500071467 41 VVICGPSGSGKSTLIRclnqleQHQEGSIVVD 72
Cdd:COG4639 5 VVLIGLPGSGKSTFAR------RLFAPTEVVS 30
|
|
| BMS1 |
cd01882 |
Bms1, an essential GTPase, promotes assembly of preribosomal RNA processing complexes; Bms1 is ... |
41-58 |
5.79e-03 |
|
Bms1, an essential GTPase, promotes assembly of preribosomal RNA processing complexes; Bms1 is an essential, evolutionarily conserved, nucleolar protein. Its depletion interferes with processing of the 35S pre-rRNA at sites A0, A1, and A2, and the formation of 40S subunits. Bms1, the putative endonuclease Rc11, and the essential U3 small nucleolar RNA form a stable subcomplex that is believed to control an early step in the formation of the 40S subumit. The C-terminal domain of Bms1 contains a GTPase-activating protein (GAP) that functions intramolecularly. It is believed that Rc11 activates Bms1 by acting as a guanine-nucleotide exchange factor (GEF) to promote GDP/GTP exchange, and that activated (GTP-bound) Bms1 delivers Rc11 to the preribosomes.
Pssm-ID: 206669 [Multi-domain] Cd Length: 231 Bit Score: 36.93 E-value: 5.79e-03
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
146-223 |
5.86e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 37.89 E-value: 5.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 146 SQLSGGQQQRAAIARALCM---EPRVMLFDEPTSALDPEMVGEVLDTMRGLAAEGMTMMIVTHEMGFARQvADRVVFMDR 222
Cdd:PRK00635 1698 SSLSLSEKIAIKIAKFLYLppkHPTLFLLDEIATSLDNQQKSALLVQLRTLVSLGHSVIYIDHDPALLKQ-ADYLIEMGP 1776
|
.
gi 500071467 223 G 223
Cdd:PRK00635 1777 G 1777
|
|
| CLP1_P |
pfam16575 |
mRNA cleavage and polyadenylation factor CLP1 P-loop; CLP1_P is the P-loop carrying domain of ... |
45-80 |
5.90e-03 |
|
mRNA cleavage and polyadenylation factor CLP1 P-loop; CLP1_P is the P-loop carrying domain of Clp1 mRNA cleavage and polyadenylation factor, Clp1, proteins in eukaryotes. Clp1 is essential for 3'-end processing of mRNAs. This region carries the P-loop suggesting it is the region that binds adenine or guanine nucleotide.
Pssm-ID: 406878 Cd Length: 187 Bit Score: 36.85 E-value: 5.90e-03
10 20 30
....*....|....*....|....*....|....*..
gi 500071467 45 GPSGSGKSTLIRCL-NQLEQHQEGSIVVDgIELGQSE 80
Cdd:pfam16575 1 GPKDSGKSTLCRILlNYAVRKGRKPVYVD-LDVGQSE 36
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
27-227 |
6.16e-03 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 37.46 E-value: 6.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 27 VLTDVSLSVARGEKVVICGPSGSGKSTLIRCLNQLEQHQEGSI-------------------------VVDG-IELGQSE 80
Cdd:PRK10636 16 LLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYtfpgnwqlawvnqetpalpqpaleyVIDGdREYRQLE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 81 NA-AQAVRREVGMVFQHfnLFPHLDLVQncilaPMSVRGmsrRAAEalavgLLERVRLGEHAHKYP-SQLSGGQQQRAAI 158
Cdd:PRK10636 96 AQlHDANERNDGHAIAT--IHGKLDAID-----AWTIRS---RAAS-----LLHGLGFSNEQLERPvSDFSGGWRMRLNL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 500071467 159 ARALCMEPRVMLFDEPTSALDpemVGEVLDTMRGLAAEGMTMMIVTHEMGFARQVADRVVFMDRGQIVE 227
Cdd:PRK10636 161 AQALICRSDLLLLDEPTNHLD---LDAVIWLEKWLKSYQGTLILISHDRDFLDPIVDKIIHIEQQSLFE 226
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
41-58 |
6.25e-03 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 36.71 E-value: 6.25e-03
|
| guanyl_kin |
TIGR03263 |
guanylate kinase; Members of this family are the enzyme guanylate kinase, also called GMP ... |
41-66 |
7.01e-03 |
|
guanylate kinase; Members of this family are the enzyme guanylate kinase, also called GMP kinase. This enzyme transfers a phosphate from ATP to GMP, yielding ADP and GDP. [Purines, pyrimidines, nucleosides, and nucleotides, Nucleotide and nucleoside interconversions]
Pssm-ID: 213788 Cd Length: 179 Bit Score: 36.32 E-value: 7.01e-03
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
145-206 |
7.67e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 37.33 E-value: 7.67e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 500071467 145 PSQLSGGQQQ------RAAIARALC--------MEPrvMLFDEPTSALDPEMVGEVLD---TMRGLAAEgmTMMIVTHE 206
Cdd:PRK02224 779 PEQLSGGERAlfnlslRCAIYRLLAegiegdapLPP--LILDEPTVFLDSGHVSQLVDlveSMRRLGVE--QIVVVSHD 853
|
|
| ABC_ATPase |
pfam09818 |
ATPase of the ABC class; This is the C-terminal ATPase domain from bacterial ABC class ATPases. ... |
149-221 |
9.85e-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: 36.42 E-value: 9.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071467 149 SGGQQQRAAIARALCMEPRVMLFDEPTSA-----LDPEMVGEV----------LDTMRGLAAE-GMTMMIVTHEMGFARQ 212
Cdd:pfam09818 159 SGSTSQAANIMEALEAGASLLLIDEDTSAtnfmiRDERMQALVskdkepitpfVDRVRSLYDDlGVSTILVVGGSGDYLD 238
|
....*....
gi 500071467 213 VADRVVFMD 221
Cdd:pfam09818 239 VADTVILMD 247
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
37-78 |
9.92e-03 |
|
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; YjeQ (YloQ in Bacillus subtilis) is a ribosomal small subunit-dependent GTPase; hence also known as RsgA. YjeQ is a late-stage ribosomal biogenesis factor involved in the 30S subunit maturation, and it represents a protein family whose members are broadly conserved in bacteria and have been shown to be essential to the growth of E. coli and B. subtilis. Proteins of the YjeQ family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. All YjeQ family proteins display a unique domain architecture, which includes an N-terminal OB-fold RNA-binding domain, the central permuted GTPase domain, and a zinc knuckle-like C-terminal cysteine domain.
Pssm-ID: 206747 [Multi-domain] Cd Length: 211 Bit Score: 36.22 E-value: 9.92e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 500071467 37 RGEKVVICGPSGSGKSTLIrclNQL--EQHQEGSIVVDGIELGQ 78
Cdd:cd01854 84 KGKTSVLVGQSGVGKSTLL---NALlpELVLATGEISEKLGRGR 124
|
|
| |
