|
Name |
Accession |
Description |
Interval |
E-value |
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
1-241 |
8.28e-174 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 477.56 E-value: 8.28e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 1 MISIKNVNKWYGDFQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGTSIADPKTNLPKLRSRVG 80
Cdd:COG1126 1 MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKKDINKLRRKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 81 MVFQHFELFPHLTITENLTIAQIKVLGRSKEEATKKGLQLLDRVGLSAHAHKHPGQLSGGQQQRVAIARALAMDPIVMLF 160
Cdd:COG1126 81 MVFQQFNLFPHLTVLENVTLAPIKVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKVMLF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 161 DEPTSALDPEMVNEVLDVMVQLAQEGMTMMCVTHEMGFARKVADRVIFMDAGKIIEDCPKEEFFGDisARSERAQHFLEK 240
Cdd:COG1126 161 DEPTSALDPELVGEVLDVMRDLAKEGMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFEN--PQHERTRAFLSK 238
|
.
gi 516455767 241 I 241
Cdd:COG1126 239 V 239
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
2-214 |
5.52e-146 |
|
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: 406.15 E-value: 5.52e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 2 ISIKNVNKWYGDFQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGTSIADPKTNLPKLRSRVGM 81
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNINELRQKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 82 VFQHFELFPHLTITENLTIAQIKVLGRSKEEATKKGLQLLDRVGLSAHAHKHPGQLSGGQQQRVAIARALAMDPIVMLFD 161
Cdd:cd03262 81 VFQQFNLFPHLTVLENITLAPIKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 516455767 162 EPTSALDPEMVNEVLDVMVQLAQEGMTMMCVTHEMGFARKVADRVIFMDAGKI 214
Cdd:cd03262 161 EPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1-244 |
1.30e-115 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 330.52 E-value: 1.30e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 1 MISIKNVNKWYGDFQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGTSIADPKTNLPKLRSRVG 80
Cdd:PRK09493 1 MIEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLIRQEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 81 MVFQHFELFPHLTITENLTIAQIKVLGRSKEEATKKGLQLLDRVGLSAHAHKHPGQLSGGQQQRVAIARALAMDPIVMLF 160
Cdd:PRK09493 81 MVFQQFYLFPHLTALENVMFGPLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 161 DEPTSALDPEMVNEVLDVMVQLAQEGMTMMCVTHEMGFARKVADRVIFMDAGKIIEDCPKEEFFGDISarSERAQHFlek 240
Cdd:PRK09493 161 DEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPP--SQRLQEF--- 235
|
....
gi 516455767 241 iLQH 244
Cdd:PRK09493 236 -LQH 238
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
1-243 |
1.43e-111 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 320.98 E-value: 1.43e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 1 MISIKNVNKWYGDFQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGTSI------------ADP 68
Cdd:COG4598 8 ALEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIrlkpdrdgelvpADR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 69 KTnLPKLRSRVGMVFQHFELFPHLTITENLTIAQIKVLGRSKEEATKKGLQLLDRVGLSAHAHKHPGQLSGGQQQRVAIA 148
Cdd:COG4598 88 RQ-LQRIRTRLGMVFQSFNLWSHMTVLENVIEAPVHVLGRPKAEAIERAEALLAKVGLADKRDAYPAHLSGGQQQRAAIA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 149 RALAMDPIVMLFDEPTSALDPEMVNEVLDVMVQLAQEGMTMMCVTHEMGFARKVADRVIFMDAGKIIEDCPKEEFFGdiS 228
Cdd:COG4598 167 RALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEEGRTMLVVTHEMGFARDVSSHVVFLHQGRIEEQGPPAEVFG--N 244
|
250
....*....|....*
gi 516455767 229 ARSERAQHFLEKILQ 243
Cdd:COG4598 245 PKSERLRQFLSSSLK 259
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
2-226 |
4.63e-92 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 270.73 E-value: 4.63e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 2 ISIKNVNKWYGDFQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIV-----DGTSIADPKTNLpKLR 76
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIagnhfDFSKTPSDKAIR-ELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 77 SRVGMVFQHFELFPHLTITENLTIAQIKVLGRSKEEATKKGLQLLDRVGLSAHAHKHPGQLSGGQQQRVAIARALAMDPI 156
Cdd:PRK11124 82 RNVGMVFQQYNLWPHLTVQQNLIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQ 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 516455767 157 VMLFDEPTSALDPEMVNEVLDVMVQLAQEGMTMMCVTHEMGFARKVADRVIFMDAGKIIE----DC---PKEEFFGD 226
Cdd:PRK11124 162 VLLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTHEVEVARKTASRVVYMENGHIVEqgdaSCftqPQTEAFKN 238
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-244 |
1.09e-91 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 270.08 E-value: 1.09e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 1 MISIKNVNKWYGDFQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEP-----FQKGDVIVDGT-SIADPKTNLPK 74
Cdd:PRK11264 3 AIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQpeagtIRVGDITIDTArSLSQQKGLIRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 75 LRSRVGMVFQHFELFPHLTITENLTIAQIKVLGRSKEEATKKGLQLLDRVGLSAHAHKHPGQLSGGQQQRVAIARALAMD 154
Cdd:PRK11264 83 LRQHVGFVFQNFNLFPHRTVLENIIEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 155 PIVMLFDEPTSALDPEMVNEVLDVMVQLAQEGMTMMCVTHEMGFARKVADRVIFMDAGKIIEDCPKEEFFGDisARSERA 234
Cdd:PRK11264 163 PEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFAD--PQQPRT 240
|
250
....*....|
gi 516455767 235 QHFLEKILQH 244
Cdd:PRK11264 241 RQFLEKFLLQ 250
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
2-238 |
1.13e-89 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 264.95 E-value: 1.13e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 2 ISIKNVNKWYGDFQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVivdgtSIADPKTNLPK------- 74
Cdd:COG4161 3 IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQL-----NIAGHQFDFSQkpsekai 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 75 --LRSRVGMVFQHFELFPHLTITENLTIAQIKVLGRSKEEATKKGLQLLDRVGLSAHAHKHPGQLSGGQQQRVAIARALA 152
Cdd:COG4161 78 rlLRQKVGMVFQQYNLWPHLTVMENLIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALM 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 153 MDPIVMLFDEPTSALDPEMVNEVLDVMVQLAQEGMTMMCVTHEMGFARKVADRVIFMDAGKIIEdcpkeefFGDISA--- 229
Cdd:COG4161 158 MEPQVLLFDEPTAALDPEITAQVVEIIRELSQTGITQVIVTHEVEFARKVASQVVYMEKGRIIE-------QGDASHftq 230
|
250
....*....|
gi 516455767 230 -RSERAQHFL 238
Cdd:COG4161 231 pQTEAFAHYL 240
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1-244 |
4.70e-88 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 263.86 E-value: 4.70e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 1 MISIKNVNKWY----GDFQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGTSIAD-PKTNLPKL 75
Cdd:COG1135 1 MIELENLSKTFptkgGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTAlSERELRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 76 RSRVGMVFQHFELFPHLTITENltIA-QIKVLGRSKEEATKKGLQLLDRVGLSAHAHKHPGQLSGGQQQRVAIARALAMD 154
Cdd:COG1135 81 RRKIGMIFQHFNLLSSRTVAEN--VAlPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 155 PIVMLFDEPTSALDPEMVNEVLDVMVQLAQE-GMTMMCVTHEMGFARKVADRVIFMDAGKIIEDCPKEEFFGDisARSER 233
Cdd:COG1135 159 PKVLLCDEATSALDPETTRSILDLLKDINRElGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVLDVFAN--PQSEL 236
|
250
....*....|.
gi 516455767 234 AQHFLEKILQH 244
Cdd:COG1135 237 TRRFLPTVLND 247
|
|
| ectoine_ehuA |
TIGR03005 |
ectoine/hydroxyectoine ABC transporter, ATP-binding protein; Members of this family are the ... |
2-243 |
8.47e-88 |
|
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: 260.53 E-value: 8.47e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 2 ISIKNVNKWYGDFQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGTSI------------ADPK 69
Cdd:TIGR03005 1 VRFSDVTKRFGILTVLDGLNFSVAAGEKVALIGPSGSGKSTILRILMTLEPIDEGQIQVEGEQLyhmpgrngplvpADEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 70 tNLPKLRSRVGMVFQHFELFPHLTITENLTIAQIKVLGRSKEEATKKGLQLLDRVGLSAHAHKHPGQLSGGQQQRVAIAR 149
Cdd:TIGR03005 81 -HLRQMRNKIGMVFQSFNLFPHKTVLDNVTEAPVLVLGMARAEAEKRAMELLDMVGLADKADHMPAQLSGGQQQRVAIAR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 150 ALAMDPIVMLFDEPTSALDPEMVNEVLDVMVQLAQE-GMTMMCVTHEMGFARKVADRVIFMDAGKIIEDCPKEEFFGdiS 228
Cdd:TIGR03005 160 ALAMRPKVMLFDEVTSALDPELVGEVLNVIRRLASEhDLTMLLVTHEMGFAREFADRVCFFDKGRIVEQGKPDEIFR--Q 237
|
250
....*....|....*
gi 516455767 229 ARSERAQHFLEKILQ 243
Cdd:TIGR03005 238 PKEERTREFLSKVIA 252
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-217 |
1.38e-84 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 251.12 E-value: 1.38e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 1 MISIKNVNKWYGD----FQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGTSIAD-PKTNLPKL 75
Cdd:COG1136 4 LLELRNLTKSYGTgegeVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSlSERELARL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 76 RSR-VGMVFQHFELFPHLTITENLTIAQIkVLGRSKEEATKKGLQLLDRVGLSAHAHKHPGQLSGGQQQRVAIARALAMD 154
Cdd:COG1136 84 RRRhIGFVFQFFNLLPELTALENVALPLL-LAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNR 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 516455767 155 PIVMLFDEPTSALDPEMVNEVLDVMVQLAQE-GMTMMCVTHEMGFARKvADRVIFMDAGKIIED 217
Cdd:COG1136 163 PKLILADEPTGNLDSKTGEEVLELLRELNRElGTTIVMVTHDPELAAR-ADRVIRLRDGRIVSD 225
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
2-243 |
1.66e-82 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 247.19 E-value: 1.66e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 2 ISIKNVNKWYGDFQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGTSI------------ADpK 69
Cdd:PRK10619 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTInlvrdkdgqlkvAD-K 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 70 TNLPKLRSRVGMVFQHFELFPHLTITENLTIAQIKVLGRSKEEATKKGLQLLDRVGLSAHAH-KHPGQLSGGQQQRVAIA 148
Cdd:PRK10619 85 NQLRLLRTRLTMVFQHFNLWSHMTVLENVMEAPIQVLGLSKQEARERAVKYLAKVGIDERAQgKYPVHLSGGQQQRVSIA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 149 RALAMDPIVMLFDEPTSALDPEMVNEVLDVMVQLAQEGMTMMCVTHEMGFARKVADRVIFMDAGKIIEDCPKEEFFGdiS 228
Cdd:PRK10619 165 RALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFG--N 242
|
250
....*....|....*
gi 516455767 229 ARSERAQHFLEKILQ 243
Cdd:PRK10619 243 PQSPRLQQFLKGSLK 257
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1-225 |
3.03e-82 |
|
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: 245.57 E-value: 3.03e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 1 MISIKNVNKWYGD----FQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGTSIAD-PKTNLPKL 75
Cdd:cd03258 1 MIELKNVSKVFGDtggkVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLlSGKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 76 RSRVGMVFQHFELFPHLTITENLTIAqIKVLGRSKEEATKKGLQLLDRVGLSAHAHKHPGQLSGGQQQRVAIARALAMDP 155
Cdd:cd03258 81 RRRIGMIFQHFNLLSSRTVFENVALP-LEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNP 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 516455767 156 IVMLFDEPTSALDPEMVNEVLDVMVQLAQE-GMTMMCVTHEMGFARKVADRVIFMDAGKIIEDCPKEEFFG 225
Cdd:cd03258 160 KVLLCDEATSALDPETTQSILALLRDINRElGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFA 230
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1-217 |
5.70e-79 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 236.87 E-value: 5.70e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 1 MISIKNVNKWY-GDFQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGTSIAD-PKTNLPKLRSR 78
Cdd:COG2884 1 MIRFENVSKRYpGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRlKRREIPYLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 79 VGMVFQHFELFPHLTITENLTIAQiKVLGRSKEEATKKGLQLLDRVGLSAHAHKHPGQLSGGQQQRVAIARALAMDPIVM 158
Cdd:COG2884 81 IGVVFQDFRLLPDRTVYENVALPL-RVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 516455767 159 LFDEPTSALDPEMVNEVLDVMVQLAQEGMTMMCVTHEMGFARKVADRVIFMDAGKIIED 217
Cdd:COG2884 160 LADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLELVDRMPKRVLELEDGRLVRD 218
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
1-223 |
1.63e-78 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 236.49 E-value: 1.63e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 1 MISIKNVNKWY-GDFQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGTSI-ADPKTNLPKLRSR 78
Cdd:COG3638 2 MLELRNLSKRYpGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVtALRGRALRRLRRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 79 VGMVFQHFELFPHLTITENltiaqikVL-GR--------------SKEEaTKKGLQLLDRVGLSAHAHKHPGQLSGGQQQ 143
Cdd:COG3638 82 IGMIFQQFNLVPRLSVLTN-------VLaGRlgrtstwrsllglfPPED-RERALEALERVGLADKAYQRADQLSGGQQQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 144 RVAIARALAMDPIVMLFDEPTSALDPEMVNEVLDVMVQLAQE-GMTMMCVTHEMGFARKVADRVIFMDAGKIIEDCPKEE 222
Cdd:COG3638 154 RVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREdGITVVVNLHQVDLARRYADRIIGLRDGRVVFDGPPAE 233
|
.
gi 516455767 223 F 223
Cdd:COG3638 234 L 234
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
2-226 |
4.23e-78 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 234.92 E-value: 4.23e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 2 ISIKNVNKWY-GDFQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGTSIAdpKTNLPKLRSRVG 80
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDIT--KKNLRELRRKVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 81 MVFQHFE--LFpHLTITENLTIAqIKVLGRSKEEATKKGLQLLDRVGLSAHAHKHPGQLSGGQQQRVAIARALAMDPIVM 158
Cdd:COG1122 79 LVFQNPDdqLF-APTVEEDVAFG-PENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 516455767 159 LFDEPTSALDPEMVNEVLDVMVQLAQEGMTMMCVTHEMGFARKVADRVIFMDAGKIIEDCPKEEFFGD 226
Cdd:COG1122 157 VLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSD 224
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-224 |
2.75e-77 |
|
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: 233.33 E-value: 2.75e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 1 MISIKNVNKWYGDFQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGTSIAD-PKTNLPKLRSRV 79
Cdd:COG1127 5 MIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGlSEKELYELRRRI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 80 GMVFQHFELFPHLTITENLTIAQIKVLGRSKEEATKKGLQLLDRVGLSAHAHKHPGQLSGGQQQRVAIARALAMDPIVML 159
Cdd:COG1127 85 GMLFQGGALFDSLTVFENVAFPLREHTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDPEILL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 516455767 160 FDEPTSALDPEMVNEVLDVMVQLAQE-GMTMMCVTHEMGFARKVADRVIFMDAGKIIEDCPKEEFF 224
Cdd:COG1127 165 YDEPTAGLDPITSAVIDELIRELRDElGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELL 230
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
2-223 |
5.84e-77 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 232.46 E-value: 5.84e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 2 ISIKNVNKWYGD-FQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGTSI-ADPKTNLPKLRSRV 79
Cdd:cd03256 1 IEVENLSKTYPNgKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDInKLKGKALRQLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 80 GMVFQHFELFPHLTITENL------TIAQIKVL-GRSKEEATKKGLQLLDRVGLSAHAHKHPGQLSGGQQQRVAIARALA 152
Cdd:cd03256 81 GMIFQQFNLIERLSVLENVlsgrlgRRSTWRSLfGLFPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIARALM 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 516455767 153 MDPIVMLFDEPTSALDPEMVNEVLDVMVQLAQE-GMTMMCVTHEMGFARKVADRVIFMDAGKIIEDCPKEEF 223
Cdd:cd03256 161 QQPKLILADEPVASLDPASSRQVMDLLKRINREeGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAEL 232
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
2-214 |
8.59e-77 |
|
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: 231.22 E-value: 8.59e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 2 ISIKNVNKWYGD----FQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGTSIADPK-TNLPKLR 76
Cdd:cd03255 1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSeKELAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 77 SR-VGMVFQHFELFPHLTITENLTIAQIkVLGRSKEEATKKGLQLLDRVGLSAHAHKHPGQLSGGQQQRVAIARALAMDP 155
Cdd:cd03255 81 RRhIGFVFQSFNLLPDLTALENVELPLL-LAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 156 IVMLFDEPTSALDPEMVNEVLDVMVQLAQE-GMTMMCVTHEMGFARKvADRVIFMDAGKI 214
Cdd:cd03255 160 KIILADEPTGNLDSETGKEVMELLRELNKEaGTTIVVVTHDPELAEY-ADRIIELRDGKI 218
|
|
| 3a0107s01c2 |
TIGR00972 |
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein ... |
2-224 |
3.36e-76 |
|
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: 230.64 E-value: 3.36e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 2 ISIKNVNKWYGDFQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALE---PFQK--GDVIVDGTSIADPKTNLPKLR 76
Cdd:TIGR00972 2 IEIENLNLFYGEKEALKNINLDIPKNQVTALIGPSGCGKSTLLRSLNRMNdlvPGVRieGKVLFDGQDIYDKKIDVVELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 77 SRVGMVFQHFELFPhLTITENLTIAqIKVLG-RSKEEATKKGLQLLDRVGL----SAHAHKHPGQLSGGQQQRVAIARAL 151
Cdd:TIGR00972 82 RRVGMVFQKPNPFP-MSIYDNIAYG-PRLHGiKDKKELDEIVEESLKKAALwdevKDRLHDSALGLSGGQQQRLCIARAL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 516455767 152 AMDPIVMLFDEPTSALDPEMVNEVLDVMVQLAqEGMTMMCVTHEMGFARKVADRVIFMDAGKIIEDCPKEEFF 224
Cdd:TIGR00972 160 AVEPEVLLLDEPTSALDPIATGKIEELIQELK-KKYTIVIVTHNMQQAARISDRTAFFYDGELVEYGPTEQIF 231
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
2-223 |
6.20e-76 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 229.57 E-value: 6.20e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 2 ISIKNVNKWYGDFQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGtsiADPKTNLPKLRSRVGM 81
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLG---EDVARDPAEVRRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 82 VFQHFELFPHLTITENLT-IAQIKvlGRSKEEATKKGLQLLDRVGLSAHAHKHPGQLSGGQQQRVAIARALAMDPIVMLF 160
Cdd:COG1131 78 VPQEPALYPDLTVRENLRfFARLY--GLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLIL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 516455767 161 DEPTSALDPEMVNEVLDVMVQLAQEGMTMMCVTHEMGFARKVADRVIFMDAGKIIEDCPKEEF 223
Cdd:COG1131 156 DEPTSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDEL 218
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-217 |
3.53e-75 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 228.44 E-value: 3.53e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 1 MISIKNVNKWY----GDFQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGTSIADPktnlpklR 76
Cdd:COG1116 7 ALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGP-------G 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 77 SRVGMVFQHFELFPHLTITENLTIAqIKVLGRSKEEATKKGLQLLDRVGLSAHAHKHPGQLSGGQQQRVAIARALAMDPI 156
Cdd:COG1116 80 PDRGVVFQEPALLPWLTVLDNVALG-LELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPE 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 516455767 157 VMLFDEPTSALDP----EMVNEVLDVmvqLAQEGMTMMCVTHEMGFARKVADRVIFMDA--GKIIED 217
Cdd:COG1116 159 VLLMDEPFGALDAltreRLQDELLRL---WQETGKTVLFVTHDVDEAVFLADRVVVLSArpGRIVEE 222
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-242 |
4.86e-75 |
|
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: 235.95 E-value: 4.86e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 1 MISIKNVNKWY-----GDFQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGTSIAD-PKTNLPK 74
Cdd:COG1123 260 LLEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKlSRRSLRE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 75 LRSRVGMVFQHFE--LFPHLTITEnlTIAQ-IKVLGR-SKEEATKKGLQLLDRVGLSA-HAHKHPGQLSGGQQQRVAIAR 149
Cdd:COG1123 340 LRRRVQMVFQDPYssLNPRMTVGD--IIAEpLRLHGLlSRAERRERVAELLERVGLPPdLADRYPHELSGGQRQRVAIAR 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 150 ALAMDPIVMLFDEPTSALDPEMVNEVLDVMVQLAQE-GMTMMCVTHEMGFARKVADRVIFMDAGKIIEDCPKEEFFGDis 228
Cdd:COG1123 418 ALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRElGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVFAN-- 495
|
250
....*....|....
gi 516455767 229 arserAQHFLEKIL 242
Cdd:COG1123 496 -----PQHPYTRAL 504
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-215 |
6.83e-75 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 230.76 E-value: 6.83e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 1 MISIKNVNKWYGDFQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGTSIadpkTNLPKLRSRVG 80
Cdd:COG3842 5 ALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDV----TGLPPEKRNVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 81 MVFQHFELFPHLTITENltIAQ-IKVLGRSKEEATKKGLQLLDRVGLSAHAHKHPGQLSGGQQQRVAIARALAMDPIVML 159
Cdd:COG3842 81 MVFQDYALFPHLTVAEN--VAFgLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 516455767 160 FDEPTSALDP----EMVNEVLDVmvqLAQEGMTMMCVTH--EMGFArkVADRVIFMDAGKII 215
Cdd:COG3842 159 LDEPLSALDAklreEMREELRRL---QRELGITFIYVTHdqEEALA--LADRIAVMNDGRIE 215
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
2-213 |
2.30e-74 |
|
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: 223.60 E-value: 2.30e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 2 ISIKNVNKWYGDFQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGTSIADPKTNLPKLRSRVGM 81
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPPLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 82 VFQHFELFPHLTITENLTIAqikvlgrskeeatkkglqlldrvglsahahkhpgqLSGGQQQRVAIARALAMDPIVMLFD 161
Cdd:cd03229 81 VFQDFALFPHLTVLENIALG-----------------------------------LSGGQQQRVALARALAMDPDVLLLD 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 516455767 162 EPTSALDPEMVNEVLDVMVQL-AQEGMTMMCVTHEMGFARKVADRVIFMDAGK 213
Cdd:cd03229 126 EPTSALDPITRREVRALLKSLqAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
2-216 |
5.19e-74 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 223.94 E-value: 5.19e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 2 ISIKNVNKWYGDFQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGTSIadpkTNLPKLRSRVGM 81
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDV----TGVPPERRNIGM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 82 VFQHFELFPHLTITENLTIAqIKVLGRSKEEATKKGLQLLDRVGLSAHAHKHPGQLSGGQQQRVAIARALAMDPIVMLFD 161
Cdd:cd03259 77 VFQDYALFPHLTVAENIAFG-LKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 516455767 162 EPTSALDP----EMVNEVLDVmvqLAQEGMTMMCVTHEMGFARKVADRVIFMDAGKIIE 216
Cdd:cd03259 156 EPLSALDAklreELREELKEL---QRELGITTIYVTHDQEEALALADRIAVMNEGRIVQ 211
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1-243 |
3.44e-73 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 226.22 E-value: 3.44e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 1 MISIKNVNKWY----GDFQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGTSI-ADPKTNLPKL 75
Cdd:PRK11153 1 MIELKNISKVFpqggRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLtALSEKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 76 RSRVGMVFQHFELFPHLTITEN----LTIAqikvlGRSKEEATKKGLQLLDRVGLSAHAHKHPGQLSGGQQQRVAIARAL 151
Cdd:PRK11153 81 RRQIGMIFQHFNLLSSRTVFDNvalpLELA-----GTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARAL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 152 AMDPIVMLFDEPTSALDPEMVNEVLDVMVQLAQE-GMTMMCVTHEMGFARKVADRVIFMDAGKIIEDCPKEEFFGDisAR 230
Cdd:PRK11153 156 ASNPKVLLCDEATSALDPATTRSILELLKDINRElGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSH--PK 233
|
250
....*....|...
gi 516455767 231 SERAQHFLEKILQ 243
Cdd:PRK11153 234 HPLTREFIQSTLH 246
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
1-223 |
6.32e-73 |
|
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: 222.17 E-value: 6.32e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 1 MISIKNVNKWYG-DFQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGTSIADPK-TNLPKLRSR 78
Cdd:TIGR02315 1 MLEVENLSKVYPnGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRgKKLRKLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 79 VGMVFQHFELFPHLTITENLTIAQI-------KVLGRSKEEATKKGLQLLDRVGLSAHAHKHPGQLSGGQQQRVAIARAL 151
Cdd:TIGR02315 81 IGMIFQHYNLIERLTVLENVLHGRLgykptwrSLLGRFSEEDKERALSALERVGLADKAYQRADQLSGGQQQRVAIARAL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 516455767 152 AMDPIVMLFDEPTSALDPEMVNEVLDVMVQLAQE-GMTMMCVTHEMGFARKVADRVIFMDAGKIIEDCPKEEF 223
Cdd:TIGR02315 161 AQQPDLILADEPIASLDPKTSKQVMDYLKRINKEdGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSEL 233
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
2-223 |
1.04e-72 |
|
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: 221.29 E-value: 1.04e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 2 ISIKNVNKWYGDFQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQK-----GDVIVDGTSIADPKTNLPKLR 76
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPgapdeGEVLLDGKDIYDLDVDVLELR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 77 SRVGMVFQHFELFPhLTITENLTIAQiKVLG-RSKEEATKKGLQLLDRVGL--SAHAHKHPGQLSGGQQQRVAIARALAM 153
Cdd:cd03260 81 RRVGMVFQKPNPFP-GSIYDNVAYGL-RLHGiKLKEELDERVEEALRKAALwdEVKDRLHALGLSGGQQQRLCLARALAN 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 154 DPIVMLFDEPTSALDPEMVNEVLDVMVQLAQEgMTMMCVTHEMGFARKVADRVIFMDAGKIIEDCPKEEF 223
Cdd:cd03260 159 EPEVLLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
2-224 |
1.23e-70 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 220.02 E-value: 1.23e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 2 ISIKNVNKWYGDFQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGTsiaDPKTNLPKLRSRVGM 81
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGR---DLFTNLPPRERRVGF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 82 VFQHFELFPHLTITENltIAQ-IKVLGRSKEEATKKGLQLLDRVGLSAHAHKHPGQLSGGQQQRVAIARALAMDPIVMLF 160
Cdd:COG1118 80 VFQHYALFPHMTVAEN--IAFgLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 516455767 161 DEPTSALD----PEMVNEVLDVmvqLAQEGMTMMCVTHEMGFARKVADRVIFMDAGKIIEDCPKEEFF 224
Cdd:COG1118 158 DEPFGALDakvrKELRRWLRRL---HDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVY 222
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
3-213 |
3.06e-70 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 214.25 E-value: 3.06e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 3 SIKNVNKWYGDF--QVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGTSIAdpKTNLPKLRSRVG 80
Cdd:cd03225 1 ELKNLSFSYPDGarPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLT--KLSLKELRRKVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 81 MVFQHFEL-FPHLTITENLTIAqIKVLGRSKEEATKKGLQLLDRVGLSAHAHKHPGQLSGGQQQRVAIARALAMDPIVML 159
Cdd:cd03225 79 LVFQNPDDqFFGPTVEEEVAFG-LENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 516455767 160 FDEPTSALDPEMVNEVLDVMVQLAQEGMTMMCVTHEMGFARKVADRVIFMDAGK 213
Cdd:cd03225 158 LDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
2-224 |
6.04e-70 |
|
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: 214.29 E-value: 6.04e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 2 ISIKNVNKWYGDFQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGTSIAD-PKTNLPKLRSRVG 80
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGlSEAELYRLRRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 81 MVFQHFELFPHLTITENLTIAQIKVLGRSKEEATKKGLQLLDRVGLSAHAHKHPGQLSGGQQQRVAIARALAMDPIVMLF 160
Cdd:cd03261 81 MLFQSGALFDSLTVFENVAFPLREHTRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLY 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 516455767 161 DEPTSALDPEMVNEVLDVMVQLAQE-GMTMMCVTHEMGFARKVADRVIFMDAGKIIEDCPKEEFF 224
Cdd:cd03261 161 DEPTAGLDPIASGVIDDLIRSLKKElGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELR 225
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1-217 |
3.07e-69 |
|
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: 212.37 E-value: 3.07e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 1 MISIKNVNKWY----GDFQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGTSIADPKTNLPKLR 76
Cdd:cd03257 1 LLEVKNLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 77 -SRVGMVFQH--FELFPHLTITENLT-IAQIKVLGRSKEEATKKGLQLLDRVGLSA-HAHKHPGQLSGGQQQRVAIARAL 151
Cdd:cd03257 81 rKEIQMVFQDpmSSLNPRMTIGEQIAePLRIHGKLSKKEARKEAVLLLLVGVGLPEeVLNRYPHELSGGQRQRVAIARAL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 516455767 152 AMDPIVMLFDEPTSALDPEMVNEVLDVMVQLAQE-GMTMMCVTHEMGFARKVADRVIFMDAGKIIED 217
Cdd:cd03257 161 ALNPKLLIADEPTSALDVSVQAQILDLLKKLQEElGLTLLFITHDLGVVAKIADRVAVMYAGKIVEE 227
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2-224 |
1.85e-68 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 211.43 E-value: 1.85e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 2 ISIKNVNKWYGDFQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVN---ALEPFQK--GDVIVDGTSIADPKTNLPKLR 76
Cdd:COG1117 12 IEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNrmnDLIPGARveGEILLDGEDIYDPDVDVVELR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 77 SRVGMVFQHFELFPHlTITENLTIAqIKVLG-RSKEEATKKGLQLLDRVGL----SAHAHKHPGQLSGGQQQRVAIARAL 151
Cdd:COG1117 92 RRVGMVFQKPNPFPK-SIYDNVAYG-LRLHGiKSKSELDEIVEESLRKAALwdevKDRLKKSALGLSGGQQQRLCIARAL 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 516455767 152 AMDPIVMLFDEPTSALDPEMVNEVLDVMVQLAQEgMTMMCVTHEMGFARKVADRVIFMDAGKIIEDCPKEEFF 224
Cdd:COG1117 170 AVEPEVLLMDEPTSALDPISTAKIEELILELKKD-YTIVIVTHNMQQAARVSDYTAFFYLGELVEFGPTEQIF 241
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
2-219 |
3.36e-68 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 209.25 E-value: 3.36e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 2 ISIKNVNKWYGD----FQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGTSIADPktnlpklRS 77
Cdd:cd03293 1 LEVRNVSKTYGGgggaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGP-------GP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 78 RVGMVFQHFELFPHLTITENLTIAqIKVLGRSKEEATKKGLQLLDRVGLSAHAHKHPGQLSGGQQQRVAIARALAMDPIV 157
Cdd:cd03293 74 DRGYVFQQDALLPWLTVLDNVALG-LELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDV 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 516455767 158 MLFDEPTSALDP----EMVNEVLDVmvqLAQEGMTMMCVTHEMGFARKVADRVIFMDA--GKIIEDCP 219
Cdd:cd03293 153 LLLDEPFSALDAltreQLQEELLDI---WRETGKTVLLVTHDIDEAVFLADRVVVLSArpGRIVAEVE 217
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-243 |
7.49e-68 |
|
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: 209.27 E-value: 7.49e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 1 MISIKNVNKWYG----DFQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGTSIadPKTNLPKLR 76
Cdd:COG1124 1 MLEVRNLSVSYGqggrRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPV--TRRRRKAFR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 77 SRVGMVFQHFE--LFPHLTITEnlTIAQ-IKVLGRSKEEAtkKGLQLLDRVGL-SAHAHKHPGQLSGGQQQRVAIARALA 152
Cdd:COG1124 79 RRVQMVFQDPYasLHPRHTVDR--ILAEpLRIHGLPDREE--RIAELLEQVGLpPSFLDRYPHQLSGGQRQRVAIARALI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 153 MDPIVMLFDEPTSALDPEMVNEVLDVMVQL-AQEGMTMMCVTHEMGFARKVADRVIFMDAGKIIEDCPKEEFFGDisARS 231
Cdd:COG1124 155 LEPELLLLDEPTSALDVSVQAEILNLLKDLrEERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAG--PKH 232
|
250
....*....|..
gi 516455767 232 ERAQHFLEKILQ 243
Cdd:COG1124 233 PYTRELLAASLA 244
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
1-215 |
4.30e-67 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 209.56 E-value: 4.30e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 1 MISIKNVNKWYGDFQV-LTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGTSIADpkTNLPKLRSRV 79
Cdd:COG1125 1 MIEFENVTKRYPDGTVaVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRD--LDPVELRRRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 80 GMVFQHFELFPHLTITENltIAQI-KVLGRSKEEATKKGLQLLDRVGL--SAHAHKHPGQLSGGQQQRVAIARALAMDPI 156
Cdd:COG1125 79 GYVIQQIGLFPHMTVAEN--IATVpRLLGWDKERIRARVDELLELVGLdpEEYRDRYPHELSGGQQQRVGVARALAADPP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 516455767 157 VMLFDEPTSALDPeMVNEVL-DVMVQLAQE-GMTMMCVTHEMGFARKVADRVIFMDAGKII 215
Cdd:COG1125 157 ILLMDEPFGALDP-ITREQLqDELLRLQRElGKTIVFVTHDIDEALKLGDRIAVMREGRIV 216
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
2-226 |
3.04e-64 |
|
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: 199.77 E-value: 3.04e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 2 ISIKNVNKWYGDFQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGTSIadpkTNLPKLRSRVGM 81
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDI----TNLPPHKRPVNT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 82 VFQHFELFPHLTITENLTIAqIKVLGRSKEEATKKGLQLLDRVGLSAHAHKHPGQLSGGQQQRVAIARALAMDPIVMLFD 161
Cdd:cd03300 77 VFQNYALFPHLTVFENIAFG-LRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLD 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 516455767 162 EPTSALDPEMVNEVLDVMVQLAQE-GMTMMCVTHEMGFARKVADRVIFMDAGKI--------IEDCPKEEFFGD 226
Cdd:cd03300 156 EPLGALDLKLRKDMQLELKRLQKElGITFVFVTHDQEEALTMSDRIAVMNKGKIqqigtpeeIYEEPANRFVAD 229
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
19-215 |
4.34e-64 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 204.18 E-value: 4.34e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 19 DCSTEVKKGEVIVVCGPSGSGKSTLIKCVNAL-EPFQkGDVIVDGTSIA--DPKTnLPKLR-SRVGMVFQHFELFPHLTI 94
Cdd:COG4175 45 DASFDVEEGEIFVIMGLSGSGKSTLVRCLNRLiEPTA-GEVLIDGEDITklSKKE-LRELRrKKMSMVFQHFALLPHRTV 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 95 TEN----LTIAqikvlGRSKEEATKKGLQLLDRVGLSAHAHKHPGQLSGGQQQRVAIARALAMDPIVMLFDEPTSALDP- 169
Cdd:COG4175 123 LENvafgLEIQ-----GVPKAERRERAREALELVGLAGWEDSYPDELSGGMQQRVGLARALATDPDILLMDEAFSALDPl 197
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 516455767 170 ---EMVNEVLDVmvqlaQEGM--TMMCVTHEMGFARKVADRVIFMDAGKII 215
Cdd:COG4175 198 irrEMQDELLEL-----QAKLkkTIVFITHDLDEALRLGDRIAIMKDGRIV 243
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
19-221 |
7.79e-63 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 197.48 E-value: 7.79e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 19 DCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGTSIAD-PKTNLPKLRS-RVGMVFQHFELFPHLTITE 96
Cdd:cd03294 42 DVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAmSRKELRELRRkKISMVFQSFALLPHRTVLE 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 97 NLTIAqIKVLGRSKEEATKKGLQLLDRVGLSAHAHKHPGQLSGGQQQRVAIARALAMDPIVMLFDEPTSALDPEMVNEVL 176
Cdd:cd03294 122 NVAFG-LEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQ 200
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 516455767 177 DVMVQL-AQEGMTMMCVTHEMGFARKVADRVIFMDAGKIIE-DCPKE 221
Cdd:cd03294 201 DELLRLqAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQvGTPEE 247
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-214 |
1.36e-62 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 199.53 E-value: 1.36e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 1 MISIKNVNKWYGDFQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGTSIadpkTNLPKLRSRVG 80
Cdd:COG3839 3 SLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDV----TDLPPKDRNIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 81 MVFQHFELFPHLTITENLTIAqIKVLGRSKEEATKKGLQLLDRVGLSAHAHKHPGQLSGGQQQRVAIARALAMDPIVMLF 160
Cdd:COG3839 79 MVFQSYALYPHMTVYENIAFP-LKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFLL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 516455767 161 DEPTSALDPEMVNEVLDVMVQLAQE-GMTMMCVTHE----MGFarkvADRVIFMDAGKI 214
Cdd:COG3839 158 DEPLSNLDAKLRVEMRAEIKRLHRRlGTTTIYVTHDqveaMTL----ADRIAVMNDGRI 212
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
2-228 |
6.11e-62 |
|
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: 194.96 E-value: 6.11e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 2 ISIKNVNKWY--GDFQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGTSIADPKtNLPKLRSRV 79
Cdd:TIGR04520 1 IEVENVSFSYpeSEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLDEE-NLWEIRKKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 80 GMVFQH---------------FELfphltitENLTIAQIKVLGRSKEeatkkglqLLDRVGLSAHAHKHPGQLSGGQQQR 144
Cdd:TIGR04520 80 GMVFQNpdnqfvgatveddvaFGL-------ENLGVPREEMRKRVDE--------ALKLVGMEDFRDREPHLLSGGQKQR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 145 VAIARALAMDPIVMLFDEPTSALDPEMVNEVLDVMVQL-AQEGMTMMCVTHEMGFARKvADRVIFMDAGKIIEDCPKEEF 223
Cdd:TIGR04520 145 VAIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLnKEEGITVISITHDMEEAVL-ADRVIVMNKGKIVAEGTPREI 223
|
....*
gi 516455767 224 FGDIS 228
Cdd:TIGR04520 224 FSQVE 228
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
2-224 |
1.86e-61 |
|
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: 192.90 E-value: 1.86e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 2 ISIKNVNKWYGD-FQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNAL-EPFQkGDVIVDGTSIADpkTNLPKLRSRV 79
Cdd:cd03295 1 IEFENVTKRYGGgKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLiEPTS-GEIFIDGEDIRE--QDPVELRRKI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 80 GMVFQHFELFPHLTITENLTIAQiKVLGRSKEEATKKGLQLLDRVGL--SAHAHKHPGQLSGGQQQRVAIARALAMDPIV 157
Cdd:cd03295 78 GYVIQQIGLFPHMTVEENIALVP-KLLKWPKEKIRERADELLALVGLdpAEFADRYPHELSGGQQQRVGVARALAADPPL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 516455767 158 MLFDEPTSALDPEMVNEVLDVMVQLAQE-GMTMMCVTHEMGFARKVADRVIFMDAGKIIEDCPKEEFF 224
Cdd:cd03295 157 LLMDEPFGALDPITRDQLQEEFKRLQQElGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEIL 224
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
1-213 |
2.30e-61 |
|
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: 191.69 E-value: 2.30e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 1 MISIKNVNKWY-GDFQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGTSIAD-PKTNLPKLRSR 78
Cdd:TIGR02673 1 MIEFHNVSKAYpGGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRlRGRQLPLLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 79 VGMVFQHFELFPHLTITENLTIAqIKVLGRSKEEATKKGLQLLDRVGLSAHAHKHPGQLSGGQQQRVAIARALAMDPIVM 158
Cdd:TIGR02673 81 IGVVFQDFRLLPDRTVYENVALP-LEVRGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPPLL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 516455767 159 LFDEPTSALDPEMVNEVLDVMVQLAQEGMTMMCVTHEMGFARKVADRVIFMDAGK 213
Cdd:TIGR02673 160 LADEPTGNLDPDLSERILDLLKRLNKRGTTVIVATHDLSLVDRVAHRVIILDDGR 214
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-226 |
2.33e-61 |
|
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: 200.51 E-value: 2.33e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 1 MISIKNVNKWY--GDFQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQ---KGDVIVDGTSIADpkTNLPKL 75
Cdd:COG1123 4 LLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLE--LSEALR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 76 RSRVGMVFQHFE--LFPhLTITENLTIAqIKVLGRSKEEATKKGLQLLDRVGLSAHAHKHPGQLSGGQQQRVAIARALAM 153
Cdd:COG1123 82 GRRIGMVFQDPMtqLNP-VTVGDQIAEA-LENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALAL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 516455767 154 DPIVMLFDEPTSALDPEMVNEVLDVMVQLAQE-GMTMMCVTHEMGFARKVADRVIFMDAGKIIEDCPKEEFFGD 226
Cdd:COG1123 160 DPDLLIADEPTTALDVTTQAEILDLLRELQRErGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAA 233
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
2-214 |
8.36e-61 |
|
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ATP-binding protein is found in a number of genomes in operon-like contexts strongly suggesting a substrate specificity for 2-aminoethylphosphonate (2-AEP). The characterized PhnSTUV system is absent in the genomes in which this system is found. These genomes encode systems for the catabolism of 2-AEP, making the need for a 2-AEP-specific transporter likely. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274496 [Multi-domain] Cd Length: 353 Bit Score: 194.87 E-value: 8.36e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 2 ISIKNVNKWYGDFQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGTSIadpkTNLPKLRSRVGM 81
Cdd:TIGR03265 5 LSIDNIRKRFGAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDI----TRLPPQKRDYGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 82 VFQHFELFPHLTITENltIAQ-IKVLGRSKEEATKKGLQLLDRVGLSAHAHKHPGQLSGGQQQRVAIARALAMDPIVMLF 160
Cdd:TIGR03265 81 VFQSYALFPNLTVADN--IAYgLKNRGMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALATSPGLLLL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 516455767 161 DEPTSALDPEmvnevldVMVQLAQE--------GMTMMCVTHEMGFARKVADRVIFMDAGKI 214
Cdd:TIGR03265 159 DEPLSALDAR-------VREHLRTEirqlqrrlGVTTIMVTHDQEEALSMADRIVVMNHGVI 213
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
2-222 |
2.63e-60 |
|
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: 189.96 E-value: 2.63e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 2 ISIKNVNKWYGDFQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGTSIADPKtnlPKLRSRVGM 81
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLP---PHEIARLGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 82 V--FQHFELFPHLTITENLTIAQIKVLG---------RSKEEATKKGLQLLDRVGLSAHAHKHPGQLSGGQQQRVAIARA 150
Cdd:cd03219 78 GrtFQIPRLFPELTVLENVMVAAQARTGsglllararREEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 516455767 151 LAMDPIVMLFDEPTSALDPEMVNEVLDVMVQLAQEGMTMMCVTHEMGFARKVADRVIFMDAGKIIEDCPKEE 222
Cdd:cd03219 158 LATDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDE 229
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-224 |
2.65e-60 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 189.91 E-value: 2.65e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 1 MISIKNVNKWYGDFQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGTSIADPktnlpklRSRVG 80
Cdd:COG1121 6 AIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRA-------RRRIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 81 MVFQHFELFPHLTIT-ENL----TIAQIKVLGRSKEEATKKGLQLLDRVGLSAHAHKHPGQLSGGQQQRVAIARALAMDP 155
Cdd:COG1121 79 YVPQRAEVDWDFPITvRDVvlmgRYGRRGLFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 516455767 156 IVMLFDEPTSALDPEMVNEVLDVMVQLAQEGMTMMCVTHEMGFARKVADRVIFMDaGKIIEDCPKEEFF 224
Cdd:COG1121 159 DLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLLN-RGLVAHGPPEEVL 226
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
2-241 |
5.20e-60 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275314 [Multi-domain] Cd Length: 277 Bit Score: 190.36 E-value: 5.20e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 2 ISIKNVNKWYG-----DFQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGTSI-ADPKTNLPKL 75
Cdd:TIGR04521 1 IKLKNVSYIYQpgtpfEKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDItAKKKKKLKDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 76 RSRVGMVFQhfelFPHLTITENLTIAQI----KVLGRSKEEATKKGLQLLDRVGLSAH-AHKHPGQLSGGQQQRVAIARA 150
Cdd:TIGR04521 81 RKKVGLVFQ----FPEHQLFEETVYKDIafgpKNLGLSEEEAEERVKEALELVGLDEEyLERSPFELSGGQMRRVAIAGV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 151 LAMDPIVMLFDEPTSALDPEMVNEVLDVMVQLAQE-GMTMMCVTHEMGFARKVADRVIFMDAGKIIEDCPKEEFFGDISa 229
Cdd:TIGR04521 157 LAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEkGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVFSDVD- 235
|
250
....*....|..
gi 516455767 230 rseraqhFLEKI 241
Cdd:TIGR04521 236 -------ELEKI 240
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1-224 |
1.21e-59 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 188.04 E-value: 1.21e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 1 MISIKNVNKWYGDFQVLTDCSteVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGTSIadpkTNLPKLRSRVG 80
Cdd:COG3840 1 MLRLDDLTYRYGDFPLRFDLT--IAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDL----TALPPAERPVS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 81 MVFQHFELFPHLTITENltIAqikvLGRSK-----EEATKKGLQLLDRVGLSAHAHKHPGQLSGGQQQRVAIARALAMDP 155
Cdd:COG3840 75 MLFQENNLFPHLTVAQN--IG----LGLRPglkltAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKR 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 156 IVMLFDEPTSALDPEMVNEVLDVMVQLAQE-GMTMMCVTHEMGFARKVADRVIFMDAGKIIEDCPKEEFF 224
Cdd:COG3840 149 PILLLDEPFSALDPALRQEMLDLVDELCRErGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALL 218
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
4-209 |
1.62e-59 |
|
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly wide distribution consists of a polypeptide related to the lactococcin 972 (see TIGR01653) and multiple-membrane-spanning putative immunity protein (see TIGR01654). This model represents a small clade within the ABC transporters that regularly are found adjacent to these bacteriocin system gene pairs and are likely serve as export proteins. [Cellular processes, Toxin production and resistance, Transport and binding proteins, Unknown substrate]
Pssm-ID: 188353 [Multi-domain] Cd Length: 206 Bit Score: 186.67 E-value: 1.62e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 4 IKNVNKWYGDFQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGTSIADPKTNLPK--LRSRVGM 81
Cdd:TIGR03608 1 LKNISKKFGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLNSKKASkfRREKLGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 82 VFQHFELFPHLTITENLTIAqIKVLGRSKEEATKKGLQLLDRVGLSAHAHKHPGQLSGGQQQRVAIARALAMDPIVMLFD 161
Cdd:TIGR03608 81 LFQNFALIENETVEENLDLG-LKYKKLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLILAD 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 516455767 162 EPTSALDPEMVNEVLDVMVQLAQEGMTMMCVTHEMGFArKVADRVIFM 209
Cdd:TIGR03608 160 EPTGSLDPKNRDEVLDLLLELNDEGKTIIIVTHDPEVA-KQADRVIEL 206
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
2-214 |
5.79e-59 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 185.40 E-value: 5.79e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 2 ISIKNVNKWYGDFQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGTSIADpkTNLPKLRSRVGM 81
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSA--MPPPEWRRQVAY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 82 VFQHFELFPHlTITENLT-IAQIKVLGRSKEEAtkkgLQLLDRVGLSAHA-HKHPGQLSGGQQQRVAIARALAMDPIVML 159
Cdd:COG4619 79 VPQEPALWGG-TVRDNLPfPFQLRERKFDRERA----LELLERLGLPPDIlDKPVERLSGGERQRLALIRALLLQPDVLL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 516455767 160 FDEPTSALDPEMVNEVLDVMVQL-AQEGMTMMCVTHEMGFARKVADRVIFMDAGKI 214
Cdd:COG4619 154 LDEPTSALDPENTRRVEELLREYlAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
2-214 |
1.32e-58 |
|
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: 183.37 E-value: 1.32e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 2 ISIKNVNKWYGDFQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGTsiaDPKTNLPKLRSRVGM 81
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGK---DIKKEPEEVKRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 82 VFQHFELFPHLTITENLtiaqikvlgrskeeatkkglqlldrvglsahahkhpgQLSGGQQQRVAIARALAMDPIVMLFD 161
Cdd:cd03230 78 LPEEPSLYENLTVRENL-------------------------------------KLSGGMKQRLALAQALLHDPELLILD 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 516455767 162 EPTSALDPEMVNEVLDVMVQLAQEGMTMMCVTHEMGFARKVADRVIFMDAGKI 214
Cdd:cd03230 121 EPTSGLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1-222 |
1.90e-58 |
|
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: 185.63 E-value: 1.90e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 1 MISIKNVNKWYGDFQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGTSIADPKTNlpKLRSRVG 80
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRR--ELARRIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 81 MVFQHFELFPHLTITEnlTIAQ-----IKVLGRSKEEATKKGLQLLDRVGLSAHAHKHPGQLSGGQQQRVAIARALAMDP 155
Cdd:COG1120 79 YVPQEPPAPFGLTVRE--LVALgryphLGLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 516455767 156 IVMLFDEPTSALDPEMVNEVLDVMVQLAQE-GMTMMCVTHEMGFARKVADRVIFMDAGKIIEDCPKEE 222
Cdd:COG1120 157 PLLLLDEPTSHLDLAHQLEVLELLRRLARErGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEE 224
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-226 |
5.69e-58 |
|
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: 186.41 E-value: 5.69e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 1 MISIKNVNKWY----GDFQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQ---KGDVIVDGTSIAD-PKTNL 72
Cdd:COG0444 1 LLEVRNLKVYFptrrGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPgitSGEILFDGEDLLKlSEKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 73 PKLR-SRVGMVFQhfE----LFPHLTITENLTIAQIKVLGRSKEEATKKGLQLLDRVGLS---AHAHKHPGQLSGGQQQR 144
Cdd:COG0444 81 RKIRgREIQMIFQ--DpmtsLNPVMTVGDQIAEPLRIHGGLSKAEARERAIELLERVGLPdpeRRLDRYPHELSGGMRQR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 145 VAIARALAMDPIVMLFDEPTSALDPEMVNEVLDVMVQLAQE-GMTMMCVTHEMGFARKVADRVIFMDAGKIIEDCPKEEF 223
Cdd:COG0444 159 VMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRElGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGPVEEL 238
|
...
gi 516455767 224 FGD 226
Cdd:COG0444 239 FEN 241
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
2-214 |
1.35e-57 |
|
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: 182.22 E-value: 1.35e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 2 ISIKNVNKWY-GDFQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGTSIAD-PKTNLPKLRSRV 79
Cdd:cd03292 1 IEFINVTKTYpNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDlRGRAIPYLRRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 80 GMVFQHFELFPHLTITENLTIAqIKVLGRSKEEATKKGLQLLDRVGLSAHAHKHPGQLSGGQQQRVAIARALAMDPIVML 159
Cdd:cd03292 81 GVVFQDFRLLPDRNVYENVAFA-LEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILI 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 516455767 160 FDEPTSALDPEMVNEVLDVMVQLAQEGMTMMCVTHEMGFARKVADRVIFMDAGKI 214
Cdd:cd03292 160 ADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1-244 |
2.04e-57 |
|
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: 182.75 E-value: 2.04e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 1 MISIKNVNKWYGDFQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGtsiADPKTNLPKLRSRVG 80
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDG---EDVRKEPREARRQIG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 81 MVFQHFELFPHLTITENLTIAqIKVLGRSKEEATKKGLQLLDRVGLSAHAHKHPGQLSGGQQQRVAIARALAMDPIVMLF 160
Cdd:COG4555 78 VLPDERGLYDRLTVRENIRYF-AELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 161 DEPTSALDPEMVNEVLDVMVQLAQEGMTMMCVTHEMGFARKVADRVIFMDAGKIIEDCPKEEfFGDISARSERAQHFLEK 240
Cdd:COG4555 157 DEPTNGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDE-LREEIGEENLEDAFVAL 235
|
....
gi 516455767 241 ILQH 244
Cdd:COG4555 236 IGSE 239
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
2-223 |
4.03e-57 |
|
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: 181.09 E-value: 4.03e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 2 ISIKNVNKWYGDFQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGTSIadpkTNLP---KLRSR 78
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDI----TGLPpheRARAG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 79 VGMVFQHFELFPHLTITENLTIAQIKVLGRSKEEATKKGLQLLDRvgLSAHAHKHPGQLSGGQQQRVAIARALAMDPIVM 158
Cdd:cd03224 77 IGYVPEGRRIFPELTVEENLLLGAYARRRAKRKARLERVYELFPR--LKERRKQLAGTLSGGEQQMLAIARALMSRPKLL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 516455767 159 LFDEPTSALDPEMVNEVLDVMVQLAQEGMTMMCVTHEMGFARKVADRVIFMDAGKIIEDCPKEEF 223
Cdd:cd03224 155 LLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAEL 219
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-222 |
4.46e-57 |
|
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: 182.16 E-value: 4.46e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 1 MISIKNVNKWYGDFQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGTSIADPKtnlPKLRSRVG 80
Cdd:COG0411 4 LLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLP---PHRIARLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 81 MV--FQHFELFPHLTITENLTIAQIKVLG--------------RSKEEATKKGLQLLDRVGLSAHAHKHPGQLSGGQQQR 144
Cdd:COG0411 81 IArtFQNPRLFPELTVLENVLVAAHARLGrgllaallrlprarREEREARERAEELLERVGLADRADEPAGNLSYGQQRR 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 516455767 145 VAIARALAMDPIVMLFDEPTSALDPEMVNEVLDVMVQLAQE-GMTMMCVTHEMGFARKVADRVIFMDAGKIIEDCPKEE 222
Cdd:COG0411 161 LEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDErGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGTPAE 239
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
2-216 |
1.24e-56 |
|
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: 180.61 E-value: 1.24e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 2 ISIKNVNKWYGDFQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGTSIadpkTNLPKLRSRVGM 81
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDA----TDVPVQERNVGF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 82 VFQHFELFPHLTITENLTIA-QIKVLGRSKEEATKKG--LQLLDRVGLSAHAHKHPGQLSGGQQQRVAIARALAMDPIVM 158
Cdd:cd03296 79 VFQHYALFRHMTVFDNVAFGlRVKPRSERPPEAEIRAkvHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 516455767 159 LFDEPTSALDPEMVNEVLDVMVQLAQE-GMTMMCVTHEMGFARKVADRVIFMDAGKIIE 216
Cdd:cd03296 159 LLDEPFGALDAKVRKELRRWLRRLHDElHVTTVFVTHDQEEALEVADRVVVMNKGRIEQ 217
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
2-227 |
1.28e-54 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 179.12 E-value: 1.28e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 2 ISIKNVNKWYGDFQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGTSIadpkTNLPKLRSRVGM 81
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDV----SRLHARDRKVGF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 82 VFQHFELFPHLTITENLTIAqIKVLGR----SKEEATKKGLQLLDRVGLSAHAHKHPGQLSGGQQQRVAIARALAMDPIV 157
Cdd:PRK10851 79 VFQHYALFRHMTVFDNIAFG-LTVLPRrerpNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 158 MLFDEPTSALDPEMVNEVLDVMVQLAQE-GMTMMCVTHEMGFARKVADRVIFMDAGKIIE-DCPKE-----------EFF 224
Cdd:PRK10851 158 LLLDEPFGALDAQVRKELRRWLRQLHEElKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQaGTPDQvwrepatrfvlEFM 237
|
...
gi 516455767 225 GDI 227
Cdd:PRK10851 238 GEV 240
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-217 |
1.42e-54 |
|
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: 174.93 E-value: 1.42e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 1 MISIKNVNKWYGD----FQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGTSIA----DPktnL 72
Cdd:COG4181 8 IIELRGLTKTVGTgageLTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFaldeDA---R 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 73 PKLRSR-VGMVFQHFELFPHLTITEN----LTIAqikvlGRSkeEATKKGLQLLDRVGLSAHAHKHPGQLSGGQQQRVAI 147
Cdd:COG4181 85 ARLRARhVGFVFQSFQLLPTLTALENvmlpLELA-----GRR--DARARARALLERVGLGHRLDHYPAQLSGGEQQRVAL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 516455767 148 ARALAMDPIVMLFDEPTSALDPEMVNEVLDVMVQLAQE-GMTMMCVTHEMGFARKvADRVIFMDAGKIIED 217
Cdd:COG4181 158 ARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRErGTTLVLVTHDPALAAR-CDRVLRLRAGRLVED 227
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
2-214 |
1.33e-53 |
|
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: 172.05 E-value: 1.33e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 2 ISIKNVNKWYGDFQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGTSIADPKtnlPKLRSrVGM 81
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLP---PKDRD-IAM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 82 VFQHFELFPHLTITENLTIAqIKVLGRSKEEATKKGLQLLDRVGLSAHAHKHPGQLSGGQQQRVAIARALAMDPIVMLFD 161
Cdd:cd03301 77 VFQNYALYPHMTVYDNIAFG-LKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 516455767 162 EPTSALDPEMVNEVLDVMVQLAQE-GMTMMCVTHEMGFARKVADRVIFMDAGKI 214
Cdd:cd03301 156 EPLSNLDAKLRVQMRAELKRLQQRlGTTTIYVTHDQVEAMTMADRIAVMNDGQI 209
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
3-214 |
1.72e-53 |
|
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: 171.56 E-value: 1.72e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 3 SIKNVNKWYGDFQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGTSIAdpktnlpKLRSRVGMV 82
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLE-------KERKRIGYV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 83 FQHFEL---FPhLTITENLTI---AQIKVLGRSKEEATKKGLQLLDRVGLSAHAHKHPGQLSGGQQQRVAIARALAMDPI 156
Cdd:cd03235 74 PQRRSIdrdFP-ISVRDVVLMglyGHKGLFRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPD 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 516455767 157 VMLFDEPTSALDPEMVNEVLDVMVQLAQEGMTMMCVTHEMGFARKVADRVIFMDAGKI 214
Cdd:cd03235 153 LLLLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRVLLLNRTVV 210
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-226 |
1.82e-53 |
|
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: 172.09 E-value: 1.82e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 1 MISIKNVNKWYGDFQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGTSIadpkTNLP---KLRS 77
Cdd:COG0410 3 MLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDI----TGLPphrIARL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 78 RVGMVFQHFELFPHLTITENLTIAQIKVLGRSKEEATkkglqlLDRVG-----LSAHAHKHPGQLSGGQQQRVAIARALA 152
Cdd:COG0410 79 GIGYVPEGRRIFPSLTVEENLLLGAYARRDRAEVRAD------LERVYelfprLKERRRQRAGTLSGGEQQMLAIGRALM 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 516455767 153 MDPIVMLFDEPTSALDPEMVNEVLDVMVQLAQEGMTMMCVTHEMGFARKVADRVIFMDAGKIIEDCPKEEFFGD 226
Cdd:COG0410 153 SRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNREGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLAD 226
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
3-213 |
7.16e-53 |
|
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: 168.19 E-value: 7.16e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 3 SIKNVNKWYGDFQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGTSIADPKtnLPKLRSRVGMV 82
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLP--LEELRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 83 FQhfelfphltitenltiaqikvlgrskeeatkkglqlldrvglsahahkhpgqLSGGQQQRVAIARALAMDPIVMLFDE 162
Cdd:cd00267 79 PQ----------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDE 106
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 516455767 163 PTSALDPEMVNEVLDVMVQLAQEGMTMMCVTHEMGFARKVADRVIFMDAGK 213
Cdd:cd00267 107 PTSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
1-226 |
8.76e-53 |
|
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: 174.13 E-value: 8.76e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 1 MISIkNVNKWYGDFQVltDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGTSIAD--PKTNLPKLRSR 78
Cdd:COG4148 2 MLEV-DFRLRRGGFTL--DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLQDsaRGIFLPPHRRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 79 VGMVFQHFELFPHLTITENLTIAQikvlGRSKEEATKKGL-QLLDRVGLSAHAHKHPGQLSGGQQQRVAIARALAMDPIV 157
Cdd:COG4148 79 IGYVFQEARLFPHLSVRGNLLYGR----KRAPRAERRISFdEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 158 MLFDEPTSALDPEMVNEVLDVMVQLAQE-GMTMMCVTHEMGFARKVADRVIFMDAGKIIEDCPKEEFFGD 226
Cdd:COG4148 155 LLMDEPLAALDLARKAEILPYLERLRDElDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSR 224
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
19-216 |
1.62e-52 |
|
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: 173.89 E-value: 1.62e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 19 DCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGTSIA--DPKTNLPKLRSRVGMVFQHFELFPHLTITE 96
Cdd:TIGR01186 11 DADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEPTAGQIFIDGENIMkqSPVELREVRRKKIGMVFQQFALFPHMTILQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 97 NLTIAqIKVLGRSKEEATKKGLQLLDRVGLSAHAHKHPGQLSGGQQQRVAIARALAMDPIVMLFDEPTSALDPEMVNEVL 176
Cdd:TIGR01186 91 NTSLG-PELLGWPEQERKEKALELLKLVGLEEYEHRYPDELSGGMQQRVGLARALAAEPDILLMDEAFSALDPLIRDSMQ 169
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 516455767 177 DVMVQL-AQEGMTMMCVTHEMGFARKVADRVIFMDAGKIIE 216
Cdd:TIGR01186 170 DELKKLqATLQKTIVFITHDLDEAIRIGDRIVIMKAGEIVQ 210
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
3-215 |
2.18e-52 |
|
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: 167.61 E-value: 2.18e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 3 SIKNVNKWYGDFQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGTSIADPKtnlPKLRSRvgmv 82
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLS---PKELAR---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 83 fqhfelfphltitenltiaQIKVLgrskeeatkkgLQLLDRVGLSAHAHKHPGQLSGGQQQRVAIARALAMDPIVMLFDE 162
Cdd:cd03214 74 -------------------KIAYV-----------PQALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDE 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 516455767 163 PTSALDPEMVNEVLDVMVQLAQE-GMTMMCVTHEMGFARKVADRVIFMDAGKII 215
Cdd:cd03214 124 PTSHLDIAHQIELLELLRRLARErGKTVVMVLHDLNLAARYADRVILLKDGRIV 177
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
2-238 |
7.92e-52 |
|
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: 168.28 E-value: 7.92e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 2 ISIKNVNKWYGDFQvLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGTSIadpkTNLPKLRSRVGM 81
Cdd:cd03299 1 LKVENLSKDWKEFK-LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDI----TNLPPEKRDISY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 82 VFQHFELFPHLTITENLTIAqIKVLGRSKEEATKKGLQLLDRVGLSAHAHKHPGQLSGGQQQRVAIARALAMDPIVMLFD 161
Cdd:cd03299 76 VPQNYALFPHMTVYKNIAYG-LKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLD 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 516455767 162 EPTSALDPEmVNEVLDVMVQLAQE--GMTMMCVTHEMGFARKVADRVIFMDAGKIIEDCPKEEFFGdiSARSERAQHFL 238
Cdd:cd03299 155 EPFSALDVR-TKEKLREELKKIRKefGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFK--KPKNEFVAEFL 230
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
2-222 |
1.57e-51 |
|
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: 177.72 E-value: 1.57e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 2 ISIKNVNKWYGDFQ--VLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGTSIADpkTNLPKLRSRV 79
Cdd:COG2274 474 IELENVSFRYPGDSppVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQ--IDPASLRRQI 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 80 GMVFQHFELFpHLTITENLTIAQIKVlgrSKEEAtkkgLQLLDRVGLSAHAHKHP-----------GQLSGGQQQRVAIA 148
Cdd:COG2274 552 GVVLQDVFLF-SGTIRENITLGDPDA---TDEEI----IEAARLAGLHDFIEALPmgydtvvgeggSNLSGGQRQRLAIA 623
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 516455767 149 RALAMDPIVMLFDEPTSALDPEMVNEVLDVMVQLAQeGMTMMCVTHEMGFARKvADRVIFMDAGKIIEDCPKEE 222
Cdd:COG2274 624 RALLRNPRILILDEATSALDAETEAIILENLRRLLK-GRTVIIIAHRLSTIRL-ADRIIVLDKGRIVEDGTHEE 695
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
2-215 |
1.63e-49 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 161.52 E-value: 1.63e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 2 ISIKNVNKWYGD--FQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGTSIAdpkTNLPKLRSRV 79
Cdd:cd03263 1 LQIRNLTKTYKKgtKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIR---TDRKAARQSL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 80 GMVFQHFELFPHLTITENLTI-AQIKvlGRSKEEATKKGLQLLDRVGLSAHAHKHPGQLSGGQQQRVAIARALAMDPIVM 158
Cdd:cd03263 78 GYCPQFDALFDELTVREHLRFyARLK--GLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 516455767 159 LFDEPTSALDPEMVNEVLDvMVQLAQEGMTMMCVTHEMGFARKVADRVIFMDAGKII 215
Cdd:cd03263 156 LLDEPTSGLDPASRRAIWD-LILEVRKGRSIILTTHSMDEAEALCDRIAIMSDGKLR 211
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
19-236 |
2.27e-49 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 164.52 E-value: 2.27e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 19 DCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGTSIAD-PKTNLPKLRSRVGMVFQ--HFELFPHLT-- 93
Cdd:COG4608 36 GVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGlSGRELRPLRRRMQMVFQdpYASLNPRMTvg 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 94 --ITENLTIAQIKvlgrSKEEATKKGLQLLDRVGLSA-HAHKHPGQLSGGQQQRVAIARALAMDPIVMLFDEPTSALDPE 170
Cdd:COG4608 116 diIAEPLRIHGLA----SKAERRERVAELLELVGLRPeHADRYPHEFSGGQRQRIGIARALALNPKLIVCDEPVSALDVS 191
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 516455767 171 MVNEVLDVMVQLAQE-GMTMMCVTHEMGFARKVADRVIFMDAGKIIEDCPKEEFFgdisarsERAQH 236
Cdd:COG4608 192 IQAQVLNLLEDLQDElGLTYLFISHDLSVVRHISDRVAVMYLGKIVEIAPRDELY-------ARPLH 251
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
2-213 |
6.14e-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: 158.70 E-value: 6.14e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 2 ISIKNVNKWYGDF--QVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGTSIADPktNLPKLRSRV 79
Cdd:cd03228 1 IEFKNVSFSYPGRpkPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDL--DLESLRKNI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 80 GMVFQHFELFpHLTITENLtiaqikvlgrskeeatkkglqlldrvglsahahkhpgqLSGGQQQRVAIARALAMDPIVML 159
Cdd:cd03228 79 AYVPQDPFLF-SGTIRENI--------------------------------------LSGGQRQRIAIARALLRDPPILI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 516455767 160 FDEPTSALDPEMVNEVLDVMVQLAQeGMTMMCVTHEMGFARKvADRVIFMDAGK 213
Cdd:cd03228 120 LDEATSALDPETEALILEALRALAK-GKTVIVIAHRLSTIRD-ADRIIVLDDGR 171
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
2-217 |
7.57e-49 |
|
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: 159.69 E-value: 7.57e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 2 ISIKNVNKWYGDFQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGTSIADPKTNLpklrSRVGM 81
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEAL----RRIGA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 82 VFQHFELFPHLTITENLTIAQiKVLGRSKEEATkkglQLLDRVGLSAHAHKHPGQLSGGQQQRVAIARALAMDPIVMLFD 161
Cdd:cd03268 77 LIEAPGFYPNLTARENLRLLA-RLLGIRKKRID----EVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILD 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 516455767 162 EPTSALDPEMVNEVLDVMVQLAQEGMTMMCVTHEMGFARKVADRVIFMDAGKIIED 217
Cdd:cd03268 152 EPTNGLDPDGIKELRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKLIEE 207
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
2-217 |
1.89e-48 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 158.81 E-value: 1.89e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 2 ISIKNVNKWYGDFQVLTDCSteVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGTSIadpkTNLPKLRSRVGM 81
Cdd:cd03298 1 VRLDKIRFSYGEQPMHFDLT--FAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDV----TAAPPADRPVSM 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 82 VFQHFELFPHLTITENLTIAQIKVLgRSKEEATKKGLQLLDRVGLSAHAHKHPGQLSGGQQQRVAIARALAMDPIVMLFD 161
Cdd:cd03298 75 LFQENNLFAHLTVEQNVGLGLSPGL-KLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLD 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 516455767 162 EPTSALDPEMVNEVLDVMVQL-AQEGMTMMCVTHEMGFARKVADRVIFMDAGKIIED 217
Cdd:cd03298 154 EPFAALDPALRAEMLDLVLDLhAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQ 210
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
2-221 |
2.67e-48 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 163.19 E-value: 2.67e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 2 ISIKNVNKWYGDFQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGTSIadpkTNLPKLRSRVGM 81
Cdd:PRK09452 15 VELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDI----THVPAENRHVNT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 82 VFQHFELFPHLTITENLTIAqIKVLGRSKEEATKKGLQLLDRVGLSAHAHKHPGQLSGGQQQRVAIARALAMDPIVMLFD 161
Cdd:PRK09452 91 VFQSYALFPHMTVFENVAFG-LRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLD 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 516455767 162 EPTSALD----PEMVNEVLDVMVQLaqeGMTMMCVTHEMGFARKVADRVIFMDAGKIIED-CPKE 221
Cdd:PRK09452 170 ESLSALDyklrKQMQNELKALQRKL---GITFVFVTHDQEEALTMSDRIVVMRDGRIEQDgTPRE 231
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-223 |
2.86e-48 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 165.58 E-value: 2.86e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 1 MISIKNVNKWYGDFQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDG--TSIADPKTNLpklRSR 78
Cdd:COG1129 4 LLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGepVRFRSPRDAQ---AAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 79 VGMVFQHFELFPHLTITENLtiaqikVLGRskeEATKKGL-----------QLLDRVGLSAHAHKHPGQLSGGQQQRVAI 147
Cdd:COG1129 81 IAIIHQELNLVPNLSVAENI------FLGR---EPRRGGLidwramrrrarELLARLGLDIDPDTPVGDLSVAQQQLVEI 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 516455767 148 ARALAMDPIVMLFDEPTSALDPEMVNEVLDVMVQLAQEGMTMMCVTHEMGFARKVADRV-IFMDaGKIIEDCPKEEF 223
Cdd:COG1129 152 ARALSRDARVLILDEPTASLTEREVERLFRIIRRLKAQGVAIIYISHRLDEVFEIADRVtVLRD-GRLVGTGPVAEL 227
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
7-215 |
3.00e-48 |
|
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: 158.23 E-value: 3.00e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 7 VNKWYGDFQVltDCSTEVKkGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGTSIADP--KTNLPKLRSRVGMVFQ 84
Cdd:cd03297 6 IEKRLPDFTL--KIDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSrkKINLPPQQRKIGLVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 85 HFELFPHLTITENLTIAQikvlgRSKEEATKKGL--QLLDRVGLSAHAHKHPGQLSGGQQQRVAIARALAMDPIVMLFDE 162
Cdd:cd03297 83 QYALFPHLNVRENLAFGL-----KRKRNREDRISvdELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDE 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 516455767 163 PTSALDPEMVNEVLDVMVQLAQE-GMTMMCVTHEMGFARKVADRVIFMDAGKII 215
Cdd:cd03297 158 PFSALDRALRLQLLPELKQIKKNlNIPVIFVTHDLSEAEYLADRIVVMEDGRLQ 211
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-224 |
6.16e-48 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 158.54 E-value: 6.16e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 2 ISIKNVNKWYGDFQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNAL-----EPFQKGDVIVDGTSIAdpKTNLPKLR 76
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQDIF--KMDVIELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 77 SRVGMVFQHFELFPHLTITENLTIA-QIKVLGRSKEE-------ATKKGlQLLDRVG--LSAHAhkhpGQLSGGQQQRVA 146
Cdd:PRK14247 82 RRVQMVFQIPNPIPNLSIFENVALGlKLNRLVKSKKElqervrwALEKA-QLWDEVKdrLDAPA----GKLSGGQQQRLC 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 516455767 147 IARALAMDPIVMLFDEPTSALDPEMVNEVLDVMVQLAQEgMTMMCVTHEMGFARKVADRVIFMDAGKIIEDCPKEEFF 224
Cdd:PRK14247 157 IARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKD-MTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVF 233
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-224 |
1.82e-47 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 157.70 E-value: 1.82e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 2 ISIKNVNKWYGDFQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNAL-----EPFQKGDVIVDGTSIADPKTNLPKLR 76
Cdd:PRK14267 5 IETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLlelneEARVEGEVRLFGRNIYSPDVDPIEVR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 77 SRVGMVFQHFELFPHLTITENLTIA-QIKVLGRSKEE-------ATKKGlQLLDRVglSAHAHKHPGQLSGGQQQRVAIA 148
Cdd:PRK14267 85 REVGMVFQYPNPFPHLTIYDNVAIGvKLNGLVKSKKEldervewALKKA-ALWDEV--KDRLNDYPSNLSGGQRQRLVIA 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 516455767 149 RALAMDPIVMLFDEPTSALDPEMVNEVLDVMVQLAQEgMTMMCVTHEMGFARKVADRVIFMDAGKIIEDCPKEEFF 224
Cdd:PRK14267 162 RALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKE-YTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVF 236
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
4-224 |
1.90e-47 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 160.27 E-value: 1.90e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 4 IKNVNKWYGDFQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGTSIADPKtnlpkLRSR-VGMV 82
Cdd:PRK11432 9 LKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRS-----IQQRdICMV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 83 FQHFELFPHLTITENLTIAqIKVLGRSKEEATKKGLQLLDRVGLSAHAHKHPGQLSGGQQQRVAIARALAMDPIVMLFDE 162
Cdd:PRK11432 84 FQSYALFPHMSLGENVGYG-LKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 516455767 163 PTSALDPEMVNEVLDVMVQLAQE-GMTMMCVTHEMGFARKVADRVIFMDAGKIIEDCPKEEFF 224
Cdd:PRK11432 163 PLSNLDANLRRSMREKIRELQQQfNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELY 225
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-213 |
1.23e-46 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 153.79 E-value: 1.23e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 1 MISIKNVNKWYGDFQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGTSIADPKtnlPKLRSRVG 80
Cdd:COG4133 2 MLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAR---EDYRRRLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 81 MVFQHFELFPHLTITENLTI-AQIKVLGRSKEEAtkkgLQLLDRVGLSAHAHKHPGQLSGGQQQRVAIARALAMDPIVML 159
Cdd:COG4133 79 YLGHADGLKPELTVRENLRFwAALYGLRADREAI----DEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 516455767 160 FDEPTSALDPEMVNEVLDVMVQLAQEGMTMMCVTH-EMGFArkvADRVIFMDAGK 213
Cdd:COG4133 155 LDEPFTALDAAGVALLAELIAAHLARGGAVLLTTHqPLELA---AARVLDLGDFK 206
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
17-241 |
1.56e-46 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 155.98 E-value: 1.56e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 17 LTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGTSIADPKTNLPKLRSRVGMVFQH--FELFPHlTI 94
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKLSDIRKKVGLVFQYpeYQLFEE-TI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 95 TENLTIAQIKvLGRSKEEATKKGLQLLDRVGLS--AHAHKHPGQLSGGQQQRVAIARALAMDPIVMLFDEPTSALDPEMV 172
Cdd:PRK13637 102 EKDIAFGPIN-LGLSEEEIENRVKRAMNIVGLDyeDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGR 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 173 NEVLDVMVQLAQE-GMTMMCVTHEMGFARKVADRVIFMDAGKIIEDCPKEEFFGDISArseraqhfLEKI 241
Cdd:PRK13637 181 DEILNKIKELHKEyNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVFKEVET--------LESI 242
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-216 |
4.22e-46 |
|
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: 161.09 E-value: 4.22e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 2 ISIKNVNKWY--GDFQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGTSIADPktNLPKLRSRV 79
Cdd:COG4987 334 LELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDL--DEDDLRRRI 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 80 GMVFQHFELFpHLTITENLTIAqikvlgrsKEEATKKGL-QLLDRVGLSAHAHKHPG-----------QLSGGQQQRVAI 147
Cdd:COG4987 412 AVVPQRPHLF-DTTLRENLRLA--------RPDATDEELwAALERVGLGDWLAALPDgldtwlgeggrRLSGGERRRLAL 482
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 148 ARALAMDPIVMLFDEPTSALDPEMVNEVLDVMVQLAQeGMTMMCVTHEM-GFARkvADRVIFMDAGKIIE 216
Cdd:COG4987 483 ARALLRDAPILLLDEPTEGLDAATEQALLADLLEALA-GRTVLLITHRLaGLER--MDRILVLEDGRIVE 549
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
9-221 |
4.83e-46 |
|
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: 155.24 E-value: 4.83e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 9 KWYGDFQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGTSI-ADPKtnlpKLRSRVGMVFQHFE 87
Cdd:TIGR01188 1 KVYGDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVvREPR----KVRRSIGIVPQYAS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 88 LFPHLTITENLTIAQiKVLGRSKEEATKKGLQLLDRVGLSAHAHKHPGQLSGGQQQRVAIARALAMDPIVMLFDEPTSAL 167
Cdd:TIGR01188 77 VDEDLTGRENLEMMG-RLYGLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 516455767 168 DPEMVNEVLDVMVQLAQEGMTMMCVTHEMGFARKVADRVIFMDAGKII-EDCPKE 221
Cdd:TIGR01188 156 DPRTRRAIWDYIRALKEEGVTILLTTHYMEEADKLCDRIAIIDHGRIIaEGTPEE 210
|
|
| ABC_ATP_DarD |
NF038007 |
darobactin export ABC transporter ATP-binding protein; |
1-214 |
7.62e-46 |
|
darobactin export ABC transporter ATP-binding protein;
Pssm-ID: 411600 [Multi-domain] Cd Length: 218 Bit Score: 152.18 E-value: 7.62e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 1 MISIKNVNKWYG----DFQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGTSIAD----PKTNL 72
Cdd:NF038007 1 MLNMQNAEKCYItktiKTKVLNHLNFSVEKGDFVSIMGPSGSGKSTLLNIIGMFDSLDSGSLTLAGKEVTNlsysQKIIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 73 PklRSRVGMVFQHFELFPHLTITENLTIAqIKVLGRSKEEATKKGLQLLDRVGLSAHAHKHPGQLSGGQQQRVAIARALA 152
Cdd:NF038007 81 R--RELIGYIFQSFNLIPHLSIFDNVALP-LKYRGVAKKERIERVNQVLNLFGIDNRRNHKPMQLSGGQQQRVAIARAMV 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 516455767 153 MDPIVMLFDEPTSALDPEMVNEVLDVMVQLAQEGMTMMCVTHEMGfARKVADRVIFMDAGKI 214
Cdd:NF038007 158 SNPALLLADEPTGNLDSKNARAVLQQLKYINQKGTTIIMVTHSDE-ASTYGNRIINMKDGKL 218
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
2-221 |
8.95e-46 |
|
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: 152.14 E-value: 8.95e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 2 ISIKNVNKWYGDFQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGTSIA-DPKtnlpKLRSRVG 80
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVrEPR----EVRRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 81 MVFQHFELFPHLTITENLTIaQIKVLGRSKEEATKKGLQLLDRVGLSAHAHKHPGQLSGGQQQRVAIARALAMDPIVMLF 160
Cdd:cd03265 77 IVFQDLSVDDELTGWENLYI-HARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 516455767 161 DEPTSALDPEMVNEVLDVMVQL-AQEGMTMMCVTHEMGFARKVADRVIFMDAGKII-EDCPKE 221
Cdd:cd03265 156 DEPTIGLDPQTRAHVWEYIEKLkEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIaEGTPEE 218
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
2-217 |
1.15e-45 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 154.47 E-value: 1.15e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 2 ISIKNVNKWYG-----DFQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNAL--------------EPFQK----GDV 58
Cdd:PRK13651 3 IKVKNIVKIFNkklptELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALllpdtgtiewifkdEKNKKktkeKEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 59 IVDGTSIADPKT----NLPKLRSRVGMVFQ--HFELFPHlTITENLTIAQIKvLGRSKEEATKKGLQLLDRVGLS-AHAH 131
Cdd:PRK13651 83 VLEKLVIQKTRFkkikKIKEIRRRVGVVFQfaEYQLFEQ-TIEKDIIFGPVS-MGVSKEEAKKRAAKYIELVGLDeSYLQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 132 KHPGQLSGGQQQRVAIARALAMDPIVMLFDEPTSALDPEMVNEVLDVMVQLAQEGMTMMCVTHEMGFARKVADRVIFMDA 211
Cdd:PRK13651 161 RSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTKRTIFFKD 240
|
....*.
gi 516455767 212 GKIIED 217
Cdd:PRK13651 241 GKIIKD 246
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1-223 |
1.28e-45 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 153.70 E-value: 1.28e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 1 MISIKNVNKWYGDFQ------VLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGTSIADPKtNLPK 74
Cdd:PRK13633 4 MIKCKNVSYKYESNEesteklALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEE-NLWD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 75 LRSRVGMVFQHFELFPHLTITENLTIAQIKVLGRSKEEATKKGLQLLDRVGLSAHAHKHPGQLSGGQQQRVAIARALAMD 154
Cdd:PRK13633 83 IRNKAGMVFQNPDNQIVATIVEEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMR 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 516455767 155 PIVMLFDEPTSALDPEMVNEVLDVMVQLAQE-GMTMMCVTHEMGFARKvADRVIFMDAGKII-EDCPKEEF 223
Cdd:PRK13633 163 PECIIFDEPTAMLDPSGRREVVNTIKELNKKyGITIILITHYMEEAVE-ADRIIVMDSGKVVmEGTPKEIF 232
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
3-222 |
2.91e-45 |
|
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: 151.14 E-value: 2.91e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 3 SIKNVNKWYGDFQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGTSIADPKtnlPKLRSRVGM- 81
Cdd:TIGR03410 2 EVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLP---PHERARAGIa 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 82 -VFQHFELFPHLTITENLTIAqIKVLGRSKEEATKKGLQL-------LDRVGlsahahkhpGQLSGGQQQRVAIARALAM 153
Cdd:TIGR03410 79 yVPQGREIFPRLTVEENLLTG-LAALPRRSRKIPDEIYELfpvlkemLGRRG---------GDLSGGQQQQLAIARALVT 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 154 DPIVMLFDEPTSALDPEMVNEVLDVMVQLAQE-GMTMMCVTHEMGFARKVADRVIFMDAGKIIEDCPKEE 222
Cdd:TIGR03410 149 RPKLLLLDEPTEGIQPSIIKDIGRVIRRLRAEgGMAILLVEQYLDFARELADRYYVMERGRVVASGAGDE 218
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1-241 |
3.35e-45 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 152.54 E-value: 3.35e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 1 MISIKNVNKWYGD-FQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNA-LEPfQKGDVIVDGTSIADPKTNLPKLRSR 78
Cdd:PRK13639 1 ILETRDLKYSYPDgTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGiLKP-TSGEVLIKGEPIKYDKKSLLEVRKT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 79 VGMVFQH--FELFPHlTITENLTIAQIKvLGRSKEEATKKGLQLLDRVGLSAHAHKHPGQLSGGQQQRVAIARALAMDPI 156
Cdd:PRK13639 80 VGIVFQNpdDQLFAP-TVEEDVAFGPLN-LGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 157 VMLFDEPTSALDPEMVNEVLDVMVQLAQEGMTMMCVTHEMGFARKVADRVIFMDAGKIIEDCPKEEFFGDISA------R 230
Cdd:PRK13639 158 IIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDIETirkanlR 237
|
250
....*....|.
gi 516455767 231 SERAQHFLEKI 241
Cdd:PRK13639 238 LPRVAHLIEIL 248
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
6-244 |
6.11e-45 |
|
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: 153.73 E-value: 6.11e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 6 NVNKWYGDFQVltDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGTSIADP--KTNLPKLRSRVGMVF 83
Cdd:TIGR02142 4 RFSKRLGDFSL--DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSrkGIFLPPEKRRIGYVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 84 QHFELFPHLTITENLTIAQIKVLGRSKEEATKKGLQLLdrvGLSAHAHKHPGQLSGGQQQRVAIARALAMDPIVMLFDEP 163
Cdd:TIGR02142 82 QEARLFPHLSVRGNLRYGMKRARPSERRISFERVIELL---GIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 164 TSALDPEMVNEVLDVMVQLAQE-GMTMMCVTHEMGFARKVADRVIFMDAGKIIEDCPKEEFFGDIS----ARSERAQHFL 238
Cdd:TIGR02142 159 LAALDDPRKYEILPYLERLHAEfGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPDlpwlAREDQGSLIE 238
|
....*.
gi 516455767 239 EKILQH 244
Cdd:TIGR02142 239 GVVAEH 244
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-224 |
1.52e-44 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 149.93 E-value: 1.52e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 1 MISIKNVNKWYGDFQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNAL-----EPFQKGDVIVDGTSIADPKTNLPKL 75
Cdd:PRK14239 5 ILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndlnpEVTITGSIVYNGHNIYSPRTDTVDL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 76 RSRVGMVFQHFELFPhLTITEN----LTIAQIK---VLGRSKEEATKkGLQLLDRVglSAHAHKHPGQLSGGQQQRVAIA 148
Cdd:PRK14239 85 RKEIGMVFQQPNPFP-MSIYENvvygLRLKGIKdkqVLDEAVEKSLK-GASIWDEV--KDRLHDSALGLSGGQQQRVCIA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 516455767 149 RALAMDPIVMLFDEPTSALDPEMVNEVLDVMVQLAQEgMTMMCVTHEMGFARKVADRVIFMDAGKIIEDCPKEEFF 224
Cdd:PRK14239 161 RVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDD-YTMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQMF 235
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
2-214 |
1.72e-44 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 152.88 E-value: 1.72e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 2 ISIKNVNKWYGDFQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGTSIADPKtnlPKLRSrVGM 81
Cdd:PRK11000 4 VTLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVP---PAERG-VGM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 82 VFQHFELFPHLTITENLTIAqIKVLGRSKEEATKKGLQLLDRVGLSAHAHKHPGQLSGGQQQRVAIARALAMDPIVMLFD 161
Cdd:PRK11000 80 VFQSYALYPHLSVAENMSFG-LKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLD 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 516455767 162 EPTSALDP----EMVNEVLDVMVQLaqeGMTMMCVTHEMGFARKVADRVIFMDAGKI 214
Cdd:PRK11000 159 EPLSNLDAalrvQMRIEISRLHKRL---GRTMIYVTHDQVEAMTLADKIVVLDAGRV 212
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
2-224 |
2.12e-44 |
|
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: 156.00 E-value: 2.12e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 2 ISIKNVNKWY-----------GDFQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQkGDVIVDGTSIA--DP 68
Cdd:COG4172 276 LEARDLKVWFpikrglfrrtvGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIPSE-GEIRFDGQDLDglSR 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 69 KTNLPkLRSRVGMVFQH-F-ELFPHLT----ITENLTIAQIkvlGRSKEEATKKGLQLLDRVGLS-AHAHKHPGQLSGGQ 141
Cdd:COG4172 355 RALRP-LRRRMQVVFQDpFgSLSPRMTvgqiIAEGLRVHGP---GLSAAERRARVAEALEEVGLDpAARHRYPHEFSGGQ 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 142 QQRVAIARALAMDPIVMLFDEPTSALDPEMVNEVLDVMVQLAQE-GMTMMCVTHEMGFARKVADRVIFMDAGKIIEDCPK 220
Cdd:COG4172 431 RQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREhGLAYLFISHDLAVVRALAHRVMVMKDGKVVEQGPT 510
|
....
gi 516455767 221 EEFF 224
Cdd:COG4172 511 EQVF 514
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
34-230 |
3.23e-44 |
|
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: 151.11 E-value: 3.23e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 34 GPSGSGKSTLIKCVNALEPFQKGDVIVDGTSIadpkTNLPKLRSRVGMVFQHFELFPHLTITENLTIAqIKVLGRSKEEA 113
Cdd:TIGR01187 3 GPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDV----TNVPPHLRHINMVFQSYALFPHMTVEENVAFG-LKMRKVPRAEI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 114 TKKGLQLLDRVGLSAHAHKHPGQLSGGQQQRVAIARALAMDPIVMLFDEPTSALD----PEMVNEVLDVMVQLaqeGMTM 189
Cdd:TIGR01187 78 KPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDkklrDQMQLELKTIQEQL---GITF 154
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 516455767 190 MCVTHEMGFARKVADRVIFMDAGKIIEDCPKEEFFGDISAR 230
Cdd:TIGR01187 155 VFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANL 195
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
2-224 |
3.90e-44 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 149.78 E-value: 3.90e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 2 ISIKNVNKWYGDF--QVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGTSIADpkTNLPKLRSRV 79
Cdd:PRK13635 6 IRVEHISFRYPDAatYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSE--ETVWDVRRQV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 80 GMVFQHFE-LFPHLTITENLTIAqIKVLGRSKEEATKKGLQLLDRVGLSAHAHKHPGQLSGGQQQRVAIARALAMDPIVM 158
Cdd:PRK13635 84 GMVFQNPDnQFVGATVQDDVAFG-LENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDII 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 516455767 159 LFDEPTSALDPEMVNEVLDVMVQL-AQEGMTMMCVTHEMGFARKvADRVIFMDAGKIIEDCPKEEFF 224
Cdd:PRK13635 163 ILDEATSMLDPRGRREVLETVRQLkEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEIF 228
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
17-165 |
4.43e-44 |
|
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: 145.48 E-value: 4.43e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 17 LTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGTSIadPKTNLPKLRSRVGMVFQHFELFPHLTITE 96
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDL--TDDERKSLRKEIGYVFQDPQLFPRLTVRE 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 516455767 97 NLTIAQIkVLGRSKEEATKKGLQLLDRVGLSAHAHKH----PGQLSGGQQQRVAIARALAMDPIVMLFDEPTS 165
Cdd:pfam00005 79 NLRLGLL-LKGLSKREKDARAEEALEKLGLGDLADRPvgerPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
2-216 |
5.43e-44 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 155.71 E-value: 5.43e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 2 ISIKNVNKWY-GDFQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGTSIADpkTNLPKLRSRVG 80
Cdd:COG1132 340 IEFENVSFSYpGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRD--LTLESLRRQIG 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 81 MVFQHFELFpHLTITENLTiaqikvLGRSK------EEATKKglqlldrvglsAHAH----KHPGQ-----------LSG 139
Cdd:COG1132 418 VVPQDTFLF-SGTIRENIR------YGRPDatdeevEEAAKA-----------AQAHefieALPDGydtvvgergvnLSG 479
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 516455767 140 GQQQRVAIARALAMDPIVMLFDEPTSALDPEMVNEVLDVMVQLAQeGMTMMCVTHEMGFARKvADRVIFMDAGKIIE 216
Cdd:COG1132 480 GQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMK-GRTTIVIAHRLSTIRN-ADRILVLDDGRIVE 554
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-216 |
8.43e-44 |
|
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: 154.92 E-value: 8.43e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 2 ISIKNVN-KWYGDFQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGTSIADpkTNLPKLRSRVG 80
Cdd:COG4988 337 IELEDVSfSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSD--LDPASWRRQIA 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 81 MVFQHFELFpHLTITENLTIAqikvlgrsKEEATKKGL-QLLDRVGLSAHAHKHPG-----------QLSGGQQQRVAIA 148
Cdd:COG4988 415 WVPQNPYLF-AGTIRENLRLG--------RPDASDEELeAALEAAGLDEFVAALPDgldtplgeggrGLSGGQAQRLALA 485
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 516455767 149 RALAMDPIVMLFDEPTSALDPEMVNEVLDVMVQLAQEGMTMMcVTHEMGFARKvADRVIFMDAGKIIE 216
Cdd:COG4988 486 RALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVIL-ITHRLALLAQ-ADRILVLDDGRIVE 551
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-222 |
2.12e-43 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 152.87 E-value: 2.12e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 1 MISIKNVNKWYGDFQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDG--TSIADPKTnlpKLRSR 78
Cdd:COG3845 5 ALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGkpVRIRSPRD---AIALG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 79 VGMVFQHFELFPHLTITENLTIAQ--IKVLGRSKEEATKKGLQLLDRVGLSAHAHKHPGQLSGGQQQRVAIARALAMDPI 156
Cdd:COG3845 82 IGMVHQHFMLVPNLTVAENIVLGLepTKGGRLDRKAARARIRELSERYGLDVDPDAKVEDLSVGEQQRVEILKALYRGAR 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 516455767 157 VMLFDEPTSALDPEMVNEVLDVMVQLAQEGMTMMCVTHEMGFARKVADRVIFMDAGKIIEDCPKEE 222
Cdd:COG3845 162 ILILDEPTAVLTPQEADELFEILRRLAAEGKSIIFITHKLREVMAIADRVTVLRRGKVVGTVDTAE 227
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
1-211 |
2.52e-43 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 145.32 E-value: 2.52e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 1 MISIKNVNKWYGDFQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVN-ALEP-FQ-KGDVIVDGTSIadpkTNLPKLRS 77
Cdd:COG4136 1 MLSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAgTLSPaFSaSGEVLLNGRRL----TALPAEQR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 78 RVGMVFQHFELFPHLTITENLTIAQIKVLGRSKEEATKkgLQLLDRVGLSAHAHKHPGQLSGGQQQRVAIARALAMDPIV 157
Cdd:COG4136 77 RIGILFQDDLLFPHLSVGENLAFALPPTIGRAQRRARV--EQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRA 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 516455767 158 MLFDEPTSALDPEMVNEVLD-VMVQLAQEGMTMMCVTHEMGfARKVADRVIFMDA 211
Cdd:COG4136 155 LLLDEPFSKLDAALRAQFREfVFEQIRQRGIPALLVTHDEE-DAPAAGRVLDLGN 208
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1-215 |
3.84e-43 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 147.06 E-value: 3.84e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 1 MISIKNVNKWYGDFQ--VLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGTSIAdpKTNLPKLRSR 78
Cdd:PRK13632 7 MIKVENVSFSYPNSEnnALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITIS--KENLKEIRKK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 79 VGMVFQH---------------FELfphltitENLTIaqikvlgrSKEEATKKGLQLLDRVGLSAHAHKHPGQLSGGQQQ 143
Cdd:PRK13632 85 IGIIFQNpdnqfigatveddiaFGL-------ENKKV--------PPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQ 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 516455767 144 RVAIARALAMDPIVMLFDEPTSALDPEMVNEVLDVMVQLAQEGM-TMMCVTHEMGFARKvADRVIFMDAGKII 215
Cdd:PRK13632 150 RVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKkTLISITHDMDEAIL-ADKVIVFSEGKLI 221
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
17-226 |
5.20e-43 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 147.09 E-value: 5.20e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 17 LTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGTSIADPKTN--LPKLRSRVGMVFQhfelFPHLTI 94
Cdd:PRK13634 23 LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKKNkkLKPLRKKVGIVFQ----FPEHQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 95 TENLTIAQI----KVLGRSKEEATKKGLQLLDRVGLSAHA-HKHPGQLSGGQQQRVAIARALAMDPIVMLFDEPTSALDP 169
Cdd:PRK13634 99 FEETVEKDIcfgpMNFGVSEEDAKQKAREMIELVGLPEELlARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDP 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 516455767 170 EMVNEVLDVMVQLAQE-GMTMMCVTHEMGFARKVADRVIFMDAGKIIEDCPKEEFFGD 226
Cdd:PRK13634 179 KGRKEMMEMFYKLHKEkGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFAD 236
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
2-223 |
1.24e-42 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 146.13 E-value: 1.24e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 2 ISIKNVNKWYG-----DFQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGTSIAdPKT---NLP 73
Cdd:PRK13641 3 IKFENVDYIYSpgtpmEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHIT-PETgnkNLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 74 KLRSRVGMVFQhfelFPHLTITENLTIAQI----KVLGRSKEEATKKGLQLLDRVGLSAH-AHKHPGQLSGGQQQRVAIA 148
Cdd:PRK13641 82 KLRKKVSLVFQ----FPEAQLFENTVLKDVefgpKNFGFSEDEAKEKALKWLKKVGLSEDlISKSPFELSGGQMRRVAIA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 516455767 149 RALAMDPIVMLFDEPTSALDPEMVNEVLDVMVQLAQEGMTMMCVTHEMGFARKVADRVIFMDAGKIIE-DCPKEEF 223
Cdd:PRK13641 158 GVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKhASPKEIF 233
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-222 |
1.37e-42 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 146.02 E-value: 1.37e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 1 MISIKNVNKWYGDFQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGTSIADPKTN----LPKLR 76
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDRRrigyLPEER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 77 SrvgmvfqhfeLFPHLTITENLT-IAQIKvlGRSKEEATKKGLQLLDRVGLSAHAHKHPGQLSGGQQQRVAIARALAMDP 155
Cdd:COG4152 81 G----------LYPKMKVGEQLVyLARLK--GLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDP 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 516455767 156 IVMLFDEPTSALDPEMVNEVLDVMVQLAQEGMTMMCVTHEMGFARKVADRVIFMDAGKIIEDCPKEE 222
Cdd:COG4152 149 ELLILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDE 215
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
12-199 |
7.07e-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: 141.02 E-value: 7.07e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 12 GDFQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGTSIADPKTNLPKLRSRVGMVFQHFE--LF 89
Cdd:TIGR01166 3 GGPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPLDYSRKGLLERRQRVGLVFQDPDdqLF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 90 pHLTITENLTIAQIKvLGRSKEEATKKGLQLLDRVGLSAHAHKHPGQLSGGQQQRVAIARALAMDPIVMLFDEPTSALDP 169
Cdd:TIGR01166 83 -AADVDQDVAFGPLN-LGLSEAEVERRVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAGLDP 160
|
170 180 190
....*....|....*....|....*....|
gi 516455767 170 EMVNEVLDVMVQLAQEGMTMMCVTHEMGFA 199
Cdd:TIGR01166 161 AGREQMLAILRRLRAEGMTVVISTHDVDLA 190
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1-230 |
7.92e-42 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 143.59 E-value: 7.92e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 1 MISIKNVNKWYGD-FQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGTSIADPkTNLPKLRSRV 79
Cdd:PRK13644 1 MIRLENVSYSYPDgTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDF-SKLQGIRKLV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 80 GMVFQHFEL-FPHLTITENLTIAQiKVLGRSKEEATKKGLQLLDRVGLSAHAHKHPGQLSGGQQQRVAIARALAMDPIVM 158
Cdd:PRK13644 80 GIVFQNPETqFVGRTVEEDLAFGP-ENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 516455767 159 LFDEPTSALDPEMVNEVLDVMVQLAQEGMTMMCVTHEMGfARKVADRVIFMDAGKIIEDCPKEEFFGDISAR 230
Cdd:PRK13644 159 IFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLE-ELHDADRIIVMDRGKIVLEGEPENVLSDVSLQ 229
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
3-215 |
1.26e-41 |
|
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: 140.86 E-value: 1.26e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 3 SIKNVNKWYGDFQ-VLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGtsiadPKTNLPKLRSRVGM 81
Cdd:cd03226 1 RIENISFSYKKGTeILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNG-----KPIKAKERRKSIGY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 82 VFQH--FELFPHlTITENLTIAqIKVLGRSKEEATkkglQLLDRVGLSAHAHKHPGQLSGGQQQRVAIARALAMDPIVML 159
Cdd:cd03226 76 VMQDvdYQLFTD-SVREELLLG-LKELDAGNEQAE----TVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLI 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 516455767 160 FDEPTSALDPEMVNEVLDVMVQLAQEGMTMMCVTHEMGFARKVADRVIFMDAGKII 215
Cdd:cd03226 150 FDEPTSGLDYKNMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-216 |
1.76e-41 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 142.31 E-value: 1.76e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 1 MISIKNVNKWYGDF----QVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGTSIADPKtnlpklr 76
Cdd:COG4525 3 MLTVRHVSVRYPGGgqpqPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPG------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 77 SRVGMVFQHFELFPHLTITENLTIAqIKVLGRSKEEATKKGLQLLDRVGLSAHAHKHPGQLSGGQQQRVAIARALAMDPI 156
Cdd:COG4525 76 ADRGVVFQKDALLPWLNVLDNVAFG-LRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPR 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 516455767 157 VMLFDEPTSALDP---EMVNE-VLDVMvqlAQEGMTMMCVTHEMGFARKVADRVIFMDA--GKIIE 216
Cdd:COG4525 155 FLLMDEPFGALDAltrEQMQElLLDVW---QRTGKGVFLITHSVEEALFLATRLVVMSPgpGRIVE 217
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1-222 |
2.07e-41 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 149.49 E-value: 2.07e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 1 MISIKNVNKWY----GDFQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGTSIADPKTN-LPKL 75
Cdd:PRK10535 4 LLELKDIRRSYpsgeEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADaLAQL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 76 R-SRVGMVFQHFELFPHLTITENLTIAQIKVlGRSKEEATKKGLQLLDRVGLSAHAHKHPGQLSGGQQQRVAIARALAMD 154
Cdd:PRK10535 84 RrEHFGFIFQRYHLLSHLTAAQNVEVPAVYA-GLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNG 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 516455767 155 PIVMLFDEPTSALDPEMVNEVLDVMVQLAQEGMTMMCVTHEMGFARKvADRVIFMDAGKIIEDCPKEE 222
Cdd:PRK10535 163 GQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHDPQVAAQ-AERVIEIRDGEIVRNPPAQE 229
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
17-212 |
2.10e-41 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 141.06 E-value: 2.10e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 17 LTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGTSIADPKTNlpklrsRVgMVFQHFELFPHLTITE 96
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPD------RM-VVFQNYSLLPWLTVRE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 97 NLTIAQIKVL-GRSKEEATKKGLQLLDRVGLSAHAHKHPGQLSGGQQQRVAIARALAMDPIVMLFDEPTSALDPEMVNEV 175
Cdd:TIGR01184 74 NIALAVDRVLpDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNL 153
|
170 180 190
....*....|....*....|....*....|....*...
gi 516455767 176 LDVMVQLAQE-GMTMMCVTHEMGFARKVADRVIFMDAG 212
Cdd:TIGR01184 154 QEELMQIWEEhRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
2-215 |
2.26e-41 |
|
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: 139.10 E-value: 2.26e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 2 ISIKNVNKWYGDFQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGT--SIADPKTnlpKLRSRV 79
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKevSFASPRD---ARRAGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 80 GMVFQhfelfphltitenltiaqikvlgrskeeatkkglqlldrvglsahahkhpgqLSGGQQQRVAIARALAMDPIVML 159
Cdd:cd03216 78 AMVYQ----------------------------------------------------LSVGERQMVEIARALARNARLLI 105
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 516455767 160 FDEPTSALDPEMVNEVLDVMVQLAQEGMTMMCVTHEMGFARKVADRVIFMDAGKII 215
Cdd:cd03216 106 LDEPTAALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
12-224 |
2.33e-41 |
|
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: 147.91 E-value: 2.33e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 12 GDFQVLTDCSTEVKKGEVIVVCGPSGSGKStlikcVNAL-------EPFQK--GDVIVDGTSI--ADPKTnLPKLR-SRV 79
Cdd:COG4172 21 GTVEAVKGVSFDIAAGETLALVGESGSGKS-----VTALsilrllpDPAAHpsGSILFDGQDLlgLSERE-LRRIRgNRI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 80 GMVFQhfE----LFPHLTI----TENLTIAQikvlGRSKEEATKKGLQLLDRVGLSAHAHK---HPGQLSGGQQQRVAIA 148
Cdd:COG4172 95 AMIFQ--EpmtsLNPLHTIgkqiAEVLRLHR----GLSGAAARARALELLERVGIPDPERRldaYPHQLSGGQRQRVMIA 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 516455767 149 RALAMDPIVMLFDEPTSALDPEMVNEVLDVMVQLAQE-GMTMMCVTHEMGFARKVADRVIFMDAGKIIEDCPKEEFF 224
Cdd:COG4172 169 MALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRElGMALLLITHDLGVVRRFADRVAVMRQGEIVEQGPTAELF 245
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
23-229 |
2.76e-41 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 140.87 E-value: 2.76e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 23 EVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGtsiaDPKTNLPKLRSRVGMVFQHFELFPHLTITENLTiaq 102
Cdd:PRK10771 21 TVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNG----QDHTTTPPSRRPVSMLFQENNLFSHLTVAQNIG--- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 103 ikvLG-----RSKEEATKKGLQLLDRVGLSAHAHKHPGQLSGGQQQRVAIARALAMDPIVMLFDEPTSALDPEMVNEVLD 177
Cdd:PRK10771 94 ---LGlnpglKLNAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLT 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 516455767 178 VMVQLAQE-GMTMMCVTHEMGFARKVADRVIFMDAGKIIEDCPKEEFF-GDISA 229
Cdd:PRK10771 171 LVSQVCQErQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELLsGKASA 224
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
2-215 |
2.76e-41 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 140.11 E-value: 2.76e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 2 ISIKNVNKWYGDFQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGTSIADPKtnlpklRSRVGM 81
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAA------RNRIGY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 82 VFQHFELFPHLTITENLT-IAQIKvlGRSKEEATKKGLQLLDRVGLSAHAHKHPGQLSGGQQQRVAIARALAMDPIVMLF 160
Cdd:cd03269 75 LPEERGLYPKMKVIDQLVyLAQLK--GLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLIL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 516455767 161 DEPTSALDPEMVNEVLDVMVQLAQEGMTMMCVTHEMGFARKVADRVIFMDAGKII 215
Cdd:cd03269 153 DEPFSGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRAV 207
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
17-216 |
5.06e-41 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 144.79 E-value: 5.06e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 17 LTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGTSIAdpKTNLPKLRS----RVGMVFQHFELFPHL 92
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIA--KISDAELREvrrkKIAMVFQSFALMPHM 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 93 TITENlTIAQIKVLGRSKEEATKKGLQLLDRVGLSAHAHKHPGQLSGGQQQRVAIARALAMDPIVMLFDEPTSALDPEMV 172
Cdd:PRK10070 122 TVLDN-TAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIR 200
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 516455767 173 NEVLDVMVQL-AQEGMTMMCVTHEMGFARKVADRVIFMDAGKIIE 216
Cdd:PRK10070 201 TEMQDELVKLqAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQ 245
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
13-240 |
6.98e-41 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 142.30 E-value: 6.98e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 13 DFQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDV----IVDGTSIADPKT----------NLPKLRSR 78
Cdd:PRK13631 38 ELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIqvgdIYIGDKKNNHELitnpyskkikNFKELRRR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 79 VGMVFQ--HFELFPHlTITENLTIAQIKvLGRSKEEATKKGLQLLDRVGL-SAHAHKHPGQLSGGQQQRVAIARALAMDP 155
Cdd:PRK13631 118 VSMVFQfpEYQLFKD-TIEKDIMFGPVA-LGVKKSEAKKLAKFYLNKMGLdDSYLERSPFGLSGGQKRRVAIAGILAIQP 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 156 IVMLFDEPTSALDPEMVNEVLDVMVQLAQEGMTMMCVTHEMGFARKVADRVIFMDAGKIIEDCPKEEFFGDisarseraQ 235
Cdd:PRK13631 196 EILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTGTPYEIFTD--------Q 267
|
....*
gi 516455767 236 HFLEK 240
Cdd:PRK13631 268 HIINS 272
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-222 |
1.60e-40 |
|
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: 139.45 E-value: 1.60e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 1 MISIKNVNKWYGDFQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALE-PFQKGDVIV-----DGTSIADpktnlpk 74
Cdd:COG1119 3 LLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLpPTYGNDVRLfgerrGGEDVWE------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 75 LRSRVGMVFQHFelfpHLTITENLTIAQI------KVLGRSKE---EATKKGLQLLDRVGLSAHAHKHPGQLSGGQQQRV 145
Cdd:COG1119 76 LRKRIGLVSPAL----QLRFPRDETVLDVvlsgffDSIGLYREptdEQRERARELLELLGLAHLADRPFGTLSQGEQRRV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 146 AIARALAMDPIVMLFDEPTSALDPEMVNEVLDVMVQLAQEG-MTMMCVTH---EM--GFarkvaDRVIFMDAGKIIEDCP 219
Cdd:COG1119 152 LIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGaPTLVLVTHhveEIppGI-----THVLLLKDGRVVAAGP 226
|
...
gi 516455767 220 KEE 222
Cdd:COG1119 227 KEE 229
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1-224 |
2.75e-40 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 142.28 E-value: 2.75e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 1 MISIKNVNKWYGDFQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGTSIADpktnLPKLRSRVG 80
Cdd:PRK11607 19 LLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSH----VPPYQRPIN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 81 MVFQHFELFPHLTITENLTIAqIKVLGRSKEEATKKGLQLLDRVGLSAHAHKHPGQLSGGQQQRVAIARALAMDPIVMLF 160
Cdd:PRK11607 95 MMFQSYALFPHMTVEQNIAFG-LKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLL 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 516455767 161 DEPTSALDPE----MVNEVLDVmvqLAQEGMTMMCVTHEMGFARKVADRVIFMDAGKIIEDCPKEEFF 224
Cdd:PRK11607 174 DEPMGALDKKlrdrMQLEVVDI---LERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIY 238
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
2-217 |
5.51e-40 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 136.94 E-value: 5.51e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 2 ISIKNVNKWYGDFQVLTDCSTEVKKGeVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGTsiaDPKTNLPKLRSRVGM 81
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQ---DVLKQPQKLRRRIGY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 82 VFQHFELFPHLTITENL-TIAQIKvlGRSKEEATKKGLQLLDRVGLSAHAHKHPGQLSGGQQQRVAIARALAMDPIVMLF 160
Cdd:cd03264 77 LPQEFGVYPNFTVREFLdYIAWLK--GIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIV 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 516455767 161 DEPTSALDPEMVNEVLDVMVQLAqEGMTMMCVTHEMGFARKVADRVIFMDAGKIIED 217
Cdd:cd03264 155 DEPTAGLDPEERIRFRNLLSELG-EDRIVILSTHIVEDVESLCNQVAVLNKGKLVFE 210
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
24-214 |
1.72e-39 |
|
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: 135.76 E-value: 1.72e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 24 VKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGTSIadpkTNLPKLRSRVGMVFQHFELFPHLTITENLTIAQI 103
Cdd:TIGR01277 21 VADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSH----TGLAPYQRPVSMLFQENNLFAHLTVRQNIGLGLH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 104 KVLGRSKEEaTKKGLQLLDRVGLSAHAHKHPGQLSGGQQQRVAIARALAMDPIVMLFDEPTSALDPEMVNEVLDVMVQLA 183
Cdd:TIGR01277 97 PGLKLNAEQ-QEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALVKQLC 175
|
170 180 190
....*....|....*....|....*....|..
gi 516455767 184 QE-GMTMMCVTHEMGFARKVADRVIFMDAGKI 214
Cdd:TIGR01277 176 SErQRTLLMVTHHLSDARAIASQIAVVSQGKI 207
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
2-241 |
2.14e-39 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 137.57 E-value: 2.14e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 2 ISIKNVNKWYG-----DFQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGTSIADPKTN--LPK 74
Cdd:PRK13649 3 INLQNVSYTYQagtpfEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNkdIKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 75 LRSRVGMVFQhfelFPHLTITENLTIAQIKV----LGRSKEEATKKGLQLLDRVGLSAHA-HKHPGQLSGGQQQRVAIAR 149
Cdd:PRK13649 83 IRKKVGLVFQ----FPESQLFEETVLKDVAFgpqnFGVSQEEAEALAREKLALVGISESLfEKNPFELSGGQMRRVAIAG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 150 ALAMDPIVMLFDEPTSALDPEMVNEVLDVMVQLAQEGMTMMCVTHEMGFARKVADRVIFMDAGKIIEDCPKEEFFGDIsa 229
Cdd:PRK13649 159 ILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIFQDV-- 236
|
250
....*....|..
gi 516455767 230 rseraqHFLEKI 241
Cdd:PRK13649 237 ------DFLEEK 242
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-215 |
2.90e-39 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 136.40 E-value: 2.90e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 1 MISIKNVNKWYGDFQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNA-LEPFQkGDVIVDGTSIAD-PKTNLPKLRsr 78
Cdd:COG4559 1 MLEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGeLTPSS-GEVRLNGRPLAAwSPWELARRR-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 79 vGMVFQHFEL-FPhltitenLTIAQIKVLGR-----SKEEATKKGLQLLDRVGLSAHAHKHPGQLSGGQQQRVAIARALA 152
Cdd:COG4559 78 -AVLPQHSSLaFP-------FTVEEVVALGRaphgsSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 153 -------MDPIVMLFDEPTSALDPEMVNEVLDVMVQLAQEGMTMMCVTHEMGFARKVADRVIFMDAGKII 215
Cdd:COG4559 150 qlwepvdGGPRWLFLDEPTSALDLAHQHAVLRLARQLARRGGGVVAVLHDLNLAAQYADRILLLHQGRLV 219
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
2-227 |
1.61e-38 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 135.52 E-value: 1.61e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 2 ISIKNVNKWYG-----DFQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGTSI-ADPKT--NLP 73
Cdd:PRK13645 7 IILDNVSYTYAkktpfEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIpANLKKikEVK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 74 KLRSRVGMVFQ--HFELFPHlTITENLTIAQIKvLGRSKEEATKKGLQLLDRVGL-SAHAHKHPGQLSGGQQQRVAIARA 150
Cdd:PRK13645 87 RLRKEIGLVFQfpEYQLFQE-TIEKDIAFGPVN-LGENKQEAYKKVPELLKLVQLpEDYVKRSPFELSGGQKRRVALAGI 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 516455767 151 LAMDPIVMLFDEPTSALDPEMVNEVLDVMVQLAQE-GMTMMCVTHEMGFARKVADRVIFMDAGKIIEDCPKEEFFGDI 227
Cdd:PRK13645 165 IAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEyKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFSNQ 242
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
5-224 |
2.41e-38 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 134.14 E-value: 2.41e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 5 KNVNKWYGDFQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNAL----EPFQ-KGDVIVDGTSIADPKTNLPKLRSRV 79
Cdd:PRK14243 14 ENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLndliPGFRvEGKVTFHGKNLYAPDVDPVEVRRRI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 80 GMVFQHFELFPHlTITENLTI-AQIKVLGRSKEEATKKGLQ---LLDRV-------GLSahahkhpgqLSGGQQQRVAIA 148
Cdd:PRK14243 94 GMVFQKPNPFPK-SIYDNIAYgARINGYKGDMDELVERSLRqaaLWDEVkdklkqsGLS---------LSGGQQQRLCIA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 149 RALAMDPIVMLFDEPTSALDPEMVNEVLDVMVQLAQEgMTMMCVTHEMGFARKVADRVIFMDA---------GKIIEDCP 219
Cdd:PRK14243 164 RAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQ-YTIIIVTHNMQQAARVSDMTAFFNVeltegggryGYLVEFDR 242
|
....*
gi 516455767 220 KEEFF 224
Cdd:PRK14243 243 TEKIF 247
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
15-226 |
3.52e-38 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 135.48 E-value: 3.52e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 15 QVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGTSIADP-KTNLPKLRSRVGMVFQHfelfPHLT 93
Cdd:PRK11308 29 KALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKAdPEAQKLLRQKIQIVFQN----PYGS 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 94 ITENLTIAQIkvLGR--------SKEEATKKGLQLLDRVGLSA-HAHKHPGQLSGGQQQRVAIARALAMDPIVMLFDEPT 164
Cdd:PRK11308 105 LNPRKKVGQI--LEEpllintslSAAERREKALAMMAKVGLRPeHYDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPV 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 516455767 165 SALDPEMVNEVLDVMVQLAQE-GMTMMCVTHEMGFARKVADRVIFMDAGKIIEDCPKEEFFGD 226
Cdd:PRK11308 183 SALDVSVQAQVLNLMMDLQQElGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFNN 245
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
10-215 |
3.93e-38 |
|
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: 131.52 E-value: 3.93e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 10 WYGDFQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQ--KGDVIVDGTSIaDPKTnlpkLRSRVGMVFQHFE 87
Cdd:cd03213 18 SKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLgvSGEVLINGRPL-DKRS----FRKIIGYVPQDDI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 88 LFPHLTITENLTI-AQIKvlgrskeeatkkglqlldrvglsahahkhpgQLSGGQQQRVAIARALAMDPIVMLFDEPTSA 166
Cdd:cd03213 93 LHPTLTVRETLMFaAKLR-------------------------------GLSGGERKRVSIALELVSNPSLLFLDEPTSG 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 516455767 167 LDPEMVNEVLDVMVQLAQEGMTMMCVTH----EMgFarKVADRVIFMDAGKII 215
Cdd:cd03213 142 LDSSSALQVMSLLRRLADTGRTIICSIHqpssEI-F--ELFDKLLLLSQGRVI 191
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-214 |
4.82e-38 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 135.74 E-value: 4.82e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 1 MISIKNVNKWY-GDFQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGTSIADPKtnlPKLRSrV 79
Cdd:PRK11650 3 GLKLQAVRKSYdGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELE---PADRD-I 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 80 GMVFQHFELFPHLTITENLTIAqIKVLGRSKEEATKKGL---------QLLDRvglsahahkHPGQLSGGQQQRVAIARA 150
Cdd:PRK11650 79 AMVFQNYALYPHMSVRENMAYG-LKIRGMPKAEIEERVAeaarilelePLLDR---------KPRELSGGQRQRVAMGRA 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 516455767 151 LAMDPIVMLFDEPTSALDP----EMVNEVLDVMVQLaqeGMTMMCVTHEMGFARKVADRVIFMDAGKI 214
Cdd:PRK11650 149 IVREPAVFLFDEPLSNLDAklrvQMRLEIQRLHRRL---KTTSLYVTHDQVEAMTLADRVVVMNGGVA 213
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
2-222 |
4.11e-37 |
|
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: 137.69 E-value: 4.11e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 2 ISIKNVN-KWYGDFQ-VLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGTSIA--DPKTnlpkLRS 77
Cdd:TIGR03375 464 IEFRNVSfAYPGQETpALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRqiDPAD----LRR 539
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 78 RVGMVFQHFELFpHLTITENLTiaqikvLGR---SKEEAtkkgLQLLDRVGLSAHAHKHP----------GQ-LSGGQQQ 143
Cdd:TIGR03375 540 NIGYVPQDPRLF-YGTLRDNIA------LGApyaDDEEI----LRAAELAGVTEFVRRHPdgldmqigerGRsLSGGQRQ 608
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 516455767 144 RVAIARALAMDPIVMLFDEPTSALDPEMVNEVLDVMVQLAqEGMTMMCVTHEMGFARKVaDRVIFMDAGKIIEDCPKEE 222
Cdd:TIGR03375 609 AVALARALLRDPPILLLDEPTSAMDNRSEERFKDRLKRWL-AGKTLVLVTHRTSLLDLV-DRIIVMDNGRIVADGPKDQ 685
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1-214 |
5.78e-37 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 129.61 E-value: 5.78e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 1 MISIKNVNKWY-GDFQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGTSIADPKTN-LPKLRSR 78
Cdd:PRK10908 1 MIRFEHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNReVPFLRRQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 79 VGMVFQHFELFPHLTITENLTIAQIkVLGRSKEEATKKGLQLLDRVGLSAHAHKHPGQLSGGQQQRVAIARALAMDPIVM 158
Cdd:PRK10908 81 IGMIFQDHHLLMDRTVYDNVAIPLI-IAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 516455767 159 LFDEPTSALDPEMVNEVLDVMVQLAQEGMTMMCVTHEMGFARKVADRVIFMDAGKI 214
Cdd:PRK10908 160 LADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
2-215 |
8.55e-37 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 130.63 E-value: 8.55e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 2 ISIKNVNKWYGD-FQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGTSIAdpKTNLPKLRSRVG 80
Cdd:PRK13647 5 IEVEDLHFRYKDgTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVN--AENEKWVRSKVG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 81 MVFQH--FELFPhLTITENLTIAQIKvLGRSKEEATKKGLQLLDRVGLSAHAHKHPGQLSGGQQQRVAIARALAMDPIVM 158
Cdd:PRK13647 83 LVFQDpdDQVFS-STVWDDVAFGPVN-MGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVI 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 516455767 159 LFDEPTSALDPEMVNEVLDVMVQLAQEGMTMMCVTHEMGFARKVADRVIFMDAGKII 215
Cdd:PRK13647 161 VLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVL 217
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
2-214 |
1.13e-36 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 129.80 E-value: 1.13e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 2 ISIKNVNKWYGDFQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGTSIADpktnlpkLRSRVGM 81
Cdd:PRK11247 13 LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAE-------AREDTRL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 82 VFQHFELFPHLTITENLTIAqikVLGRSKEEAtkkgLQLLDRVGLSAHAHKHPGQLSGGQQQRVAIARALAMDPIVMLFD 161
Cdd:PRK11247 86 MFQDARLLPWKKVIDNVGLG---LKGQWRDAA----LQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLD 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 516455767 162 EPTSALDPEMVNEVLDVMVQLAQE-GMTMMCVTHEMGFARKVADRVIFMDAGKI 214
Cdd:PRK11247 159 EPLGALDALTRIEMQDLIESLWQQhGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
2-216 |
2.52e-36 |
|
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: 128.43 E-value: 2.52e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 2 ISIKNVNKWY---GDFQVLTDCSTEVKKGEVIVVCGPSGSGKSTlikCVNALEPF---QKGDVIVDGTSIADpkTNLPKL 75
Cdd:cd03249 1 IEFKNVSFRYpsrPDVPILKGLSLTIPPGKTVALVGSSGCGKST---VVSLLERFydpTSGEILLDGVDIRD--LNLRWL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 76 RSRVGMVFQHFELFPhLTITENLTiaqikvLGRSK------EEATKKglqlldrvglsAHAHK---------------HP 134
Cdd:cd03249 76 RSQIGLVSQEPVLFD-GTIAENIR------YGKPDatdeevEEAAKK-----------ANIHDfimslpdgydtlvgeRG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 135 GQLSGGQQQRVAIARALAMDPIVMLFDEPTSALDPE---MVNEVLDvmvqLAQEGMTMMCVTHEMGFARKvADRVIFMDA 211
Cdd:cd03249 138 SQLSGGQKQRIAIARALLRNPKILLLDEATSALDAEsekLVQEALD----RAMKGRTTIVIAHRLSTIRN-ADLIAVLQN 212
|
....*
gi 516455767 212 GKIIE 216
Cdd:cd03249 213 GQVVE 217
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1-241 |
3.37e-36 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 128.59 E-value: 3.37e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 1 MISIKNVNKWYGDFQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALepfQKGDVIVD------GTSIADP---KTN 71
Cdd:PRK09984 4 IIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGL---ITGDKSAGshiellGRTVQREgrlARD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 72 LPKLRSRVGMVFQHFELFPHLTITENLTIAQI-------KVLGRSKEEATKKGLQLLDRVGLSAHAHKHPGQLSGGQQQR 144
Cdd:PRK09984 81 IRKSRANTGYIFQQFNLVNRLSVLENVLIGALgstpfwrTCFSWFTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 145 VAIARALAMDPIVMLFDEPTSALDPEMVNEVLDVMVQLAQ-EGMTMMCVTHEMGFARKVADRVIFMDAGKIIEDCPKEEF 223
Cdd:PRK09984 161 VAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQnDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQQF 240
|
250
....*....|....*...
gi 516455767 224 fgdisaRSERAQHFLEKI 241
Cdd:PRK09984 241 ------DNERFDHLYRSI 252
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1-222 |
3.78e-36 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 128.35 E-value: 3.78e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 1 MISIKNVNKWYGDFQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNA-LEPFQkGDVIVDGTSIADPKTnlPKLRSRV 79
Cdd:PRK13548 2 MLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGeLSPDS-GEVRLNGRPLADWSP--AELARRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 80 GMVFQHFEL-FPhltitenLTIAQIKVLGR-----SKEEATKKGLQLLDRVGLSAHAHKHPGQLSGGQQQRVAIARALA- 152
Cdd:PRK13548 79 AVLPQHSSLsFP-------FTVEEVVAMGRaphglSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAq 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 516455767 153 -----MDPIVMLFDEPTSALDPEMVNEVLDVMVQLAQE-GMTMMCVTHEMGFARKVADRVIFMDAGKIIEDCPKEE 222
Cdd:PRK13548 152 lwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHErGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAE 227
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
6-214 |
4.54e-36 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 127.62 E-value: 4.54e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 6 NVNKWYGDFQVLTDC----STEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGTSIAD-PKTNLPKLRSR-V 79
Cdd:PRK11629 10 NLCKRYQEGSVQTDVlhnvSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKlSSAAKAELRNQkL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 80 GMVFQHFELFPHLTITENltIAQIKVLGRSK-EEATKKGLQLLDRVGLSAHAHKHPGQLSGGQQQRVAIARALAMDPIVM 158
Cdd:PRK11629 90 GFIYQFHHLLPDFTALEN--VAMPLLIGKKKpAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLV 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 516455767 159 LFDEPTSALDPEMVNEVLDVMVQL-AQEGMTMMCVTHEMGFARKVaDRVIFMDAGKI 214
Cdd:PRK11629 168 LADEPTGNLDARNADSIFQLLGELnRLQGTAFLVVTHDLQLAKRM-SRQLEMRDGRL 223
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
2-217 |
9.64e-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: 126.58 E-value: 9.64e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 2 ISIKNVNKWYGD--FQVLTDCSTEVKKGEVIVVCGPSGSGKSTLikcVNALEPF---QKGDVIVDGTSIADPKtnLPKLR 76
Cdd:cd03251 1 VEFKNVTFRYPGdgPPVLRDISLDIPAGETVALVGPSGSGKSTL---VNLIPRFydvDSGRILIDGHDVRDYT--LASLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 77 SRVGMVFQHFELFpHLTITENLTIAqikvlgrsKEEATKKGLQlldRVGLSAHAH----KHPG-----------QLSGGQ 141
Cdd:cd03251 76 RQIGLVSQDVFLF-NDTVAENIAYG--------RPGATREEVE---EAARAANAHefimELPEgydtvigergvKLSGGQ 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 516455767 142 QQRVAIARALAMDPIVMLFDEPTSALDPEMVNEVLDVMVQLaQEGMTMMCVTHEMGFARKvADRVIFMDAGKIIED 217
Cdd:cd03251 144 RQRIAIARALLKDPPILILDEATSALDTESERLVQAALERL-MKNRTTFVIAHRLSTIEN-ADRIVVLEDGKIVER 217
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
2-217 |
1.34e-35 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 125.78 E-value: 1.34e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 2 ISIKNVNKWYGDFQ--VLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGTSIA--DPKTnlpkLRS 77
Cdd:cd03245 3 IEFRNVSFSYPNQEipALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRqlDPAD----LRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 78 RVGMVFQHFELFpHLTITENLTIAqikvLGRSKEEATkkgLQLLDRVGLSAHAHKHP----------GQ-LSGGQQQRVA 146
Cdd:cd03245 79 NIGYVPQDVTLF-YGTLRDNITLG----APLADDERI---LRAAELAGVTDFVNKHPngldlqigerGRgLSGGQRQAVA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 516455767 147 IARALAMDPIVMLFDEPTSALDPEMVNEVLDVMVQLAqEGMTMMCVTHEMGFArKVADRVIFMDAGKIIED 217
Cdd:cd03245 151 LARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLL-GDKTLIIITHRPSLL-DLVDRIIVMDSGRIVAD 219
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1-219 |
1.59e-35 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 127.11 E-value: 1.59e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 1 MISIKNVNKWY---------GDFQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGTSIADPKTN 71
Cdd:PRK10419 3 LLNVSGLSHHYahgglsgkhQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 72 LPK-LRSRVGMVFQHF--ELFPHLTITENLTIAQIKVLGRSKEEATKKGLQLLDRVGLSA-HAHKHPGQLSGGQQQRVAI 147
Cdd:PRK10419 83 QRKaFRRDIQMVFQDSisAVNPRKTVREIIREPLRHLLSLDKAERLARASEMLRAVDLDDsVLDKRPPQLSGGQLQRVCL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 516455767 148 ARALAMDPIVMLFDEPTSALDPEMVNEVLDVMVQLAQE-GMTMMCVTHEMGFARKVADRVIFMDAGKIIEDCP 219
Cdd:PRK10419 163 ARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQfGTACLFITHDLRLVERFCQRVMVMDNGQIVETQP 235
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
13-226 |
1.87e-35 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 127.20 E-value: 1.87e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 13 DFQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGTSIADpKTN---LPKLRSRVGMVFQhfelF 89
Cdd:PRK13646 19 EHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITH-KTKdkyIRPVRKRIGMVFQ----F 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 90 PHLTITENLTIAQI----KVLGRSKEEATKKGLQLLDRVGLSAHA-HKHPGQLSGGQQQRVAIARALAMDPIVMLFDEPT 164
Cdd:PRK13646 94 PESQLFEDTVEREIifgpKNFKMNLDEVKNYAHRLLMDLGFSRDVmSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPT 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 516455767 165 SALDPEMVNEVLDVMVQLA-QEGMTMMCVTHEMGFARKVADRVIFMDAGKIIEDCPKEEFFGD 226
Cdd:PRK13646 174 AGLDPQSKRQVMRLLKSLQtDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFKD 236
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1-243 |
1.88e-35 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 126.35 E-value: 1.88e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 1 MISIKNVNKWYGDFQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGTSIADPKtnlpklrSRVG 80
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPG-------AERG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 81 MVFQHFELFPHLTITENLTIAqIKVLGRSKEEATKKGLQLLDRVGLSAHAHKHPGQLSGGQQQRVAIARALAMDPIVMLF 160
Cdd:PRK11248 74 VVFQNEGLLPWRNVQDNVAFG-LQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 161 DEPTSALDPEMVNEVLDVMVQLAQE-GMTMMCVTHEMGFARKVADRVIFM--DAGKIIEDCP---KEEFFGDISARS--- 231
Cdd:PRK11248 153 DEPFGALDAFTREQMQTLLLKLWQEtGKQVLLITHDIEEAVFMATELVLLspGPGRVVERLPlnfARRFVAGESSRSiks 232
|
250
....*....|....*..
gi 516455767 232 -----ERAQHFLEKILQ 243
Cdd:PRK11248 233 dpqfiAMREYVLSRVFE 249
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
1-241 |
2.80e-35 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 127.16 E-value: 2.80e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 1 MISIKNVNKWYGD-----FQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNAL-EPFQK----GDVIVDGTSiadPKT 70
Cdd:PRK13643 1 MIKFEKVNYTYQPnspfaSRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLlQPTEGkvtvGDIVVSSTS---KQK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 71 NLPKLRSRVGMVFQhfelFPHLTITENLTIAQIKV----LGRSKEEATKKGLQLLDRVGLSAHA-HKHPGQLSGGQQQRV 145
Cdd:PRK13643 78 EIKPVRKKVGVVFQ----FPESQLFEETVLKDVAFgpqnFGIPKEKAEKIAAEKLEMVGLADEFwEKSPFELSGGQMRRV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 146 AIARALAMDPIVMLFDEPTSALDPEMVNEVLDVMVQLAQEGMTMMCVTHEMGFARKVADRVIFMDAGKIIEDCPKEEFFG 225
Cdd:PRK13643 154 AIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQ 233
|
250 260
....*....|....*....|..
gi 516455767 226 DISARSE------RAQHFLEKI 241
Cdd:PRK13643 234 EVDFLKAhelgvpKATHFADQL 255
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-225 |
2.93e-35 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 126.77 E-value: 2.93e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 1 MISIKNVNKWYGDFQ---VLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGTSIADpkTNLPKLRS 77
Cdd:PRK13650 4 IIEVKNLTFKYKEDQekyTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTE--ENVWDIRH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 78 RVGMVFQHFE-LFPHLTITENLTIAqIKVLGRSKEEATKKGLQLLDRVGLSAHAHKHPGQLSGGQQQRVAIARALAMDPI 156
Cdd:PRK13650 82 KIGMVFQNPDnQFVGATVEDDVAFG-LENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPK 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 516455767 157 VMLFDEPTSALDPEMVNEVLDVMVQLAQE-GMTMMCVTHEMGfarKVA--DRVIFMDAGKIIEDCPKEEFFG 225
Cdd:PRK13650 161 IIILDEATSMLDPEGRLELIKTIKGIRDDyQMTVISITHDLD---EVAlsDRVLVMKNGQVESTSTPRELFS 229
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
6-238 |
4.41e-35 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 125.54 E-value: 4.41e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 6 NVNKWY---GDFQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGTSIADPK----TNLPKLRSR 78
Cdd:PRK14246 12 NISRLYlyiNDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYFGKdifqIDAIKLRKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 79 VGMVFQHFELFPHLTITENLTIAqIKVLG-RSKEEATKKGLQLLDRVGLSAHAHKH----PGQLSGGQQQRVAIARALAM 153
Cdd:PRK14246 92 VGMVFQQPNPFPHLSIYDNIAYP-LKSHGiKEKREIKKIVEECLRKVGLWKEVYDRlnspASQLSGGQQQRLTIARALAL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 154 DPIVMLFDEPTSALDPEMVNEVLDVMVQLAQEgMTMMCVTHEMGFARKVADRVIFMDAGKIIEDCPKEEFFgdISARSER 233
Cdd:PRK14246 171 KPKVLLMDEPTSMIDIVNSQAIEKLITELKNE-IAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIF--TSPKNEL 247
|
....*
gi 516455767 234 AQHFL 238
Cdd:PRK14246 248 TEKYV 252
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1-222 |
6.50e-35 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 124.81 E-value: 6.50e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 1 MISIKNVNKWYGDFQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGTSIADPKTNlpKLRSRVG 80
Cdd:COG4604 1 MIEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSR--ELAKRLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 81 MVFQHfelfPHLTIteNLTIAQIKVLGR---SKEEATKKGLQL----LDRVGLSAHAHKHPGQLSGGQQQRVAIARALAM 153
Cdd:COG4604 79 ILRQE----NHINS--RLTVRELVAFGRfpySKGRLTAEDREIideaIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQ 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 154 DPIVMLFDEPTSALDPEMVNEVLDVMVQLAQE-GMTMMCVTHEMGFARKVADRVIFMDAGKIIEDCPKEE 222
Cdd:COG4604 153 DTDYVLLDEPLNNLDMKHSVQMMKLLRRLADElGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEE 222
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
23-221 |
7.22e-35 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 125.10 E-value: 7.22e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 23 EVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGTSIAdpktNLPKLR-SRVGMV--FQHFELFPHLTITENLT 99
Cdd:PRK11300 27 EVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIE----GLPGHQiARMGVVrtFQHVRLFREMTVIENLL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 100 IAQIKVLG--------------RSKEEATKKGLQLLDRVGLSAHAHKHPGQLSGGQQQRVAIARALAMDPIVMLFDEPTS 165
Cdd:PRK11300 103 VAQHQQLKtglfsgllktpafrRAESEALDRAATWLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILMLDEPAA 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 516455767 166 ALDPEMVNEVLDVMVQLAQE-GMTMMCVTHEMGFARKVADRVIFMDAGK-IIEDCPKE 221
Cdd:PRK11300 183 GLNPKETKELDELIAELRNEhNVTVLLIEHDMKLVMGISDRIYVVNQGTpLANGTPEE 240
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
11-207 |
7.97e-35 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 123.11 E-value: 7.97e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 11 YGDFQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGTSiadpktnlpklrsRVGMVFQHFEL-- 88
Cdd:NF040873 2 YGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGA-------------RVAYVPQRSEVpd 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 89 -FPhLTITENLTI---AQIKVLGRSKEEATKKGLQLLDRVGLSAHAHKHPGQLSGGQQQRVAIARALAMDPIVMLFDEPT 164
Cdd:NF040873 69 sLP-LTVRDLVAMgrwARRGLWRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPT 147
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 516455767 165 SALDPEMVNEVLDVMVQLAQEGMTMMCVTHEMGFARKvADRVI 207
Cdd:NF040873 148 TGLDAESRERIIALLAEEHARGATVVVVTHDLELVRR-ADPCV 189
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1-239 |
1.07e-34 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 125.35 E-value: 1.07e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 1 MISIKNVNKWYGD-FQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGTSIADPKTNLPKLRSRV 79
Cdd:PRK13636 5 ILKVEELNYNYSDgTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRKGLMKLRESV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 80 GMVFQH--FELFPhLTITENLTIAQIKvLGRSKEEATKKGLQLLDRVGLSAHAHKHPGQLSGGQQQRVAIARALAMDPIV 157
Cdd:PRK13636 85 GMVFQDpdNQLFS-ASVYQDVSFGAVN-LKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 158 MLFDEPTSALDPEMVNEVLDVMVQLAQE-GMTMMCVTHEMGFARKVADRVIFMDAGKIIEDCPKEEFFGD------ISAR 230
Cdd:PRK13636 163 LVLDEPTAGLDPMGVSEIMKLLVEMQKElGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFAEkemlrkVNLR 242
|
....*....
gi 516455767 231 SERAQHFLE 239
Cdd:PRK13636 243 LPRIGHLME 251
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
7-215 |
1.31e-34 |
|
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: 123.54 E-value: 1.31e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 7 VNKWYGDFQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQK---GDVIVDGTSIaDPKTnlpkLRSRVGMVF 83
Cdd:cd03234 13 AKNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGttsGQILFNGQPR-KPDQ----FQKCVAYVR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 84 QHFELFPHLTITENLTIAQIKVLGRSKEEATKKGL---QLLDRVGLSAHAHKHPGQLSGGQQQRVAIARALAMDPIVMLF 160
Cdd:cd03234 88 QDDILLPGLTVRETLTYTAILRLPRKSSDAIRKKRvedVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLIL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 516455767 161 DEPTSALDPEMVNEVLDVMVQLAQEGMTMMCVTHEMG---FarKVADRVIFMDAGKII 215
Cdd:cd03234 168 DEPTSGLDSFTALNLVSTLSQLARRNRIVILTIHQPRsdlF--RLFDRILLLSSGEIV 223
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-222 |
1.47e-34 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 124.43 E-value: 1.47e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 1 MISIKNVNKWYG-----DFQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGTSIadpkTNLP-- 73
Cdd:COG1101 1 MLELKNLSKTFNpgtvnEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDV----TKLPey 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 74 KlRSR-VGMVFQHFEL--FPHLTITENLTIAQIKV--------LGRSKEEATKKGLQLLDRvGLSAHAHKHPGQLSGGQQ 142
Cdd:COG1101 77 K-RAKyIGRVFQDPMMgtAPSMTIEENLALAYRRGkrrglrrgLTKKRRELFRELLATLGL-GLENRLDTKVGLLSGGQR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 143 QrvaiARALAM----DPIVMLFDEPTSALDPEMVNEVLDVMVQLAQE-GMTMMCVTHEMGFARKVADRVIFMDAGKIIED 217
Cdd:COG1101 155 Q----ALSLLMatltKPKLLLLDEHTAALDPKTAALVLELTEKIVEEnNLTTLMVTHNMEQALDYGNRLIMMHEGRIILD 230
|
....*
gi 516455767 218 CPKEE 222
Cdd:COG1101 231 VSGEE 235
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1-217 |
1.53e-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: 123.25 E-value: 1.53e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 1 MISIKNVNKWYGD----FQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCV-NALEPfQKGDVIVDGTsiaDPKTNLPKL 75
Cdd:cd03266 1 MITADALTKRFRDvkktVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLaGLLEP-DAGFATVDGF---DVVKEPAEA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 76 RSRVGMVFQHFELFPHLTITENLTIAQiKVLGRSKEEATKKGLQLLDRVGLSAHAHKHPGQLSGGQQQRVAIARALAMDP 155
Cdd:cd03266 77 RRRLGFVSDSTGLYDRLTARENLEYFA-GLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 516455767 156 IVMLFDEPTSALDPEMVNEVLDVMVQLAQEGMTMMCVTHEMGFARKVADRVIFMDAGKIIED 217
Cdd:cd03266 156 PVLLLDEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYE 217
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
2-222 |
1.76e-34 |
|
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: 129.45 E-value: 1.76e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 2 ISIKNVNKWYG--DFQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGTSIADPKtnLPKLRSRV 79
Cdd:TIGR02203 331 VEFRNVTFRYPgrDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYT--LASLRRQV 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 80 GMVFQHFELFPHlTITENLTIAQIKVLGRSKEEATKKGLQLLDRV-----GLSAHAHKHPGQLSGGQQQRVAIARALAMD 154
Cdd:TIGR02203 409 ALVSQDVVLFND-TIANNIAYGRTEQADRAEIERALAAAYAQDFVdklplGLDTPIGENGVLLSGGQRQRLAIARALLKD 487
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 516455767 155 PIVMLFDEPTSALDPEMVNEVLDVMVQLaQEGMTMMCVTHEMGFARKvADRVIFMDAGKIIEDCPKEE 222
Cdd:TIGR02203 488 APILILDEATSALDNESERLVQAALERL-MQGRTTLVIAHRLSTIEK-ADRIVVMDDGRIVERGTHNE 553
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-216 |
2.22e-34 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 129.17 E-value: 2.22e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 2 ISIKNVNKWYGD--FQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVN-ALEPfQKGDVIVDGTSIADpkTNLPKLRSR 78
Cdd:PRK11160 339 LTLNNVSFTYPDqpQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTrAWDP-QQGEILLNGQPIAD--YSEAALRQA 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 79 VGMVFQHFELFPHlTITENLTIAqikvlgrsKEEATKKGL-QLLDRVGLSAHAHKHPG----------QLSGGQQQRVAI 147
Cdd:PRK11160 416 ISVVSQRVHLFSA-TLRDNLLLA--------APNASDEALiEVLQQVGLEKLLEDDKGlnawlgeggrQLSGGEQRRLGI 486
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 516455767 148 ARALAMDPIVMLFDEPTSALDPEMVNEVLDVMVQLAQeGMTMMCVTHemgfaRKVA----DRVIFMDAGKIIE 216
Cdd:PRK11160 487 ARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQ-NKTVLMITH-----RLTGleqfDRICVMDNGQIIE 553
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
2-238 |
2.85e-34 |
|
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: 122.65 E-value: 2.85e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 2 ISIKNVNKWYGDFQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGTSIadpkTNLP-KLRSRVG 80
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDI----TKLPmHKRARLG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 81 MVF--QHFELFPHLTITENLtIAQIKVLGRSKEEATKKGLQLLDRVGLSAHAHKHPGQLSGGQQQRVAIARALAMDPIVM 158
Cdd:cd03218 77 IGYlpQEASIFRKLTVEENI-LAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 159 LFDEPTSALDPEMVNEVLDVMVQLAQEGMTMMCVTHEMGFARKVADRVIFMDAGKIIEDCPKEEFFGDISARseraQHFL 238
Cdd:cd03218 156 LLDEPFAGVDPIAVQDIQKIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANELVR----KVYL 231
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-208 |
2.95e-34 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 123.61 E-value: 2.95e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 2 ISIKNVNKWYGDFQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQkGDVIVDG------TSIADPKTNLPKL 75
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELE-SEVRVEGrveffnQNIYERRVNLNRL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 76 RSRVGMVFQHFELFPhLTITENLTIAqIKVLGRSKE-------EATKKGLQLLDRVglSAHAHKHPGQLSGGQQQRVAIA 148
Cdd:PRK14258 87 RRQVSMVHPKPNLFP-MSVYDNVAYG-VKIVGWRPKleiddivESALKDADLWDEI--KHKIHKSALDLSGGQQQRLCIA 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 516455767 149 RALAMDPIVMLFDEPTSALDP--EMVNEVLDVMVQLAQEgMTMMCVTHEMGFARKVADRVIF 208
Cdd:PRK14258 163 RALAVKPKVLLMDEPCFGLDPiaSMKVESLIQSLRLRSE-LTMVIVSHNLHQVSRLSDFTAF 223
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-212 |
4.55e-34 |
|
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: 122.16 E-value: 4.55e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 1 MISIKNVNKwygDF----------QVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIV--DGTSI--- 65
Cdd:COG4778 4 LLEVENLSK---TFtlhlqggkrlPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrhDGGWVdla 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 66 -ADPKTNLPKLRSRVGMVFQHFELFPHLTiTENLTIAQIKVLGRSKEEATKKGLQLLDRVGLSAH-AHKHPGQLSGGQQQ 143
Cdd:COG4778 81 qASPREILALRRRTIGYVSQFLRVIPRVS-ALDVVAEPLLERGVDREEARARARELLARLNLPERlWDLPPATFSGGEQQ 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 516455767 144 RVAIARALAMDPIVMLFDEPTSALDPEMVNEVLDVMVQLAQEGMTMMCVTHEMGFARKVADRVIFMDAG 212
Cdd:COG4778 160 RVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVREAVADRVVDVTPF 228
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
16-222 |
8.39e-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: 121.82 E-value: 8.39e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 16 VLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGTSIA--DPKTnlpkLRSRVGMVFQHFELFpHLT 93
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLAlaDPAW----LRRQVGVVLQENVLF-NRS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 94 ITENLTIAQIKVLGRSKEEATKKG------LQLldRVGLSAHAHKHPGQLSGGQQQRVAIARALAMDPIVMLFDEPTSAL 167
Cdd:cd03252 92 IRDNIALADPGMSMERVIEAAKLAgahdfiSEL--PEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATSAL 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 516455767 168 DPEMVNEVLDVMVQLAqEGMTMMCVTHEMGFARKvADRVIFMDAGKIIEDCPKEE 222
Cdd:cd03252 170 DYESEHAIMRNMHDIC-AGRTVIIIAHRLSTVKN-ADRIIVMEKGRIVEQGSHDE 222
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
2-209 |
1.81e-33 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 126.25 E-value: 1.81e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 2 ISIKNVNKWYGD-FQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGTSIADpkTNLPKLRSRVG 80
Cdd:TIGR02857 322 LEFSGVSVAYPGrRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLAD--ADADSWRDQIA 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 81 MVFQHFELFPHlTITENLTIAQIKVLGRSKEEATKK-GLQLLDRV---GLSAHAHKHPGQLSGGQQQRVAIARALAMDPI 156
Cdd:TIGR02857 400 WVPQHPFLFAG-TIAENIRLARPDASDAEIREALERaGLDEFVAAlpqGLDTPIGEGGAGLSGGQAQRLALARAFLRDAP 478
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 516455767 157 VMLFDEPTSALDPEMVNEVLDVMVQLAQeGMTMMCVTHEMGFARkVADRVIFM 209
Cdd:TIGR02857 479 LLLLDEPTAHLDAETEAEVLEALRALAQ-GRTVLLVTHRLALAA-LADRIVVL 529
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
2-222 |
1.83e-33 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 120.79 E-value: 1.83e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 2 ISIKNVNKWY-GDFQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGTSIADpkTNLPKLRSRVG 80
Cdd:cd03254 3 IEFENVNFSYdEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRD--ISRKSLRSMIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 81 MVFQHFELFPHlTITENLTiaqikvLGRS-----KEEATKKGLQLLDRV-----GLSAHAHKHPGQLSGGQQQRVAIARA 150
Cdd:cd03254 81 VVLQDTFLFSG-TIMENIR------LGRPnatdeEVIEAAKEAGAHDFImklpnGYDTVLGENGGNLSQGERQLLAIARA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 516455767 151 LAMDPIVMLFDEPTSALDPEMVNEVLDVMVQLaQEGMTMMCVTHEMGFARKvADRVIFMDAGKIIEDCPKEE 222
Cdd:cd03254 154 MLRDPKILILDEATSNIDTETEKLIQEALEKL-MKGRTSIIIAHRLSTIKN-ADKILVLDDGKIIEEGTHDE 223
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-187 |
2.09e-33 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 120.52 E-value: 2.09e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 1 MISIKNVNKWYGDFQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGTSIadpkTNLP-KLRSRV 79
Cdd:COG1137 3 TLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDI----THLPmHKRARL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 80 GMVF--QHFELFPHLTITENLtIAQIKVLGRSKEEATKKGLQLLDRVGLSAHAHKHPGQLSGGQQQRVAIARALAMDPIV 157
Cdd:COG1137 79 GIGYlpQEASIFRKLTVEDNI-LAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKF 157
|
170 180 190
....*....|....*....|....*....|
gi 516455767 158 MLFDEPTSALDPEMVNEVLDVMVQLAQEGM 187
Cdd:COG1137 158 ILLDEPFAGVDPIAVADIQKIIRHLKERGI 187
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
2-222 |
2.73e-33 |
|
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: 126.78 E-value: 2.73e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 2 ISIKNVNKWYGDFQ--VLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGT--SIADPKTnlpkLRS 77
Cdd:TIGR01846 456 ITFENIRFRYAPDSpeVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVdlAIADPAW----LRR 531
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 78 RVGMVFQHFELFPHlTITENLTIAQIkvlGRSKEE----ATKKGLQ---LLDRVGLSAHAHKHPGQLSGGQQQRVAIARA 150
Cdd:TIGR01846 532 QMGVVLQENVLFSR-SIRDNIALCNP---GAPFEHvihaAKLAGAHdfiSELPQGYNTEVGEKGANLSGGQRQRIAIARA 607
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 516455767 151 LAMDPIVMLFDEPTSALDPEMVNEVLDVMVQLAQeGMTMMCVTHEMGFARKvADRVIFMDAGKIIEDCPKEE 222
Cdd:TIGR01846 608 LVGNPRILIFDEATSALDYESEALIMRNMREICR-GRTVIIIAHRLSTVRA-CDRIIVLEKGQIAESGRHEE 677
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
2-222 |
6.04e-33 |
|
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: 119.64 E-value: 6.04e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 2 ISIKNVNKWYGD-FQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGTSIADpkTNLPKLRSRVG 80
Cdd:cd03253 1 IEFENVTFAYDPgRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIRE--VTLDSLRRAIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 81 MVFQHFELFpHLTITENLTIAQIKVLGRSKEEATKKGlQLLDRV--------------GLsahahkhpgQLSGGQQQRVA 146
Cdd:cd03253 79 VVPQDTVLF-NDTIGYNIRYGRPDATDEEVIEAAKAA-QIHDKImrfpdgydtivgerGL---------KLSGGEKQRVA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 516455767 147 IARALAMDPIVMLFDEPTSALDPEMVNEVLDVMVQLAQeGMTMMCVTHEMgfaRKV--ADRVIFMDAGKIIEDCPKEE 222
Cdd:cd03253 148 IARAILKNPPILLLDEATSALDTHTEREIQAALRDVSK-GRTTIVIAHRL---STIvnADKIIVLKDGRIVERGTHEE 221
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1-228 |
8.53e-33 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 124.53 E-value: 8.53e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 1 MISIKNVNKWY-----GDFQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVD-GTSIADPKTNLPK 74
Cdd:TIGR03269 279 IIKVRNVSKRYisvdrGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRvGDEWVDMTKPGPD 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 75 LRSRV----GMVFQHFELFPHLTITENLTIAqIKvLGRSKEEATKKGLQLLDRVGLSAHA-----HKHPGQLSGGQQQRV 145
Cdd:TIGR03269 359 GRGRAkryiGILHQEYDLYPHRTVLDNLTEA-IG-LELPDELARMKAVITLKMVGFDEEKaeeilDKYPDELSEGERHRV 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 146 AIARALAMDPIVMLFDEPTSALDPEMVNEVLDVMVQLAQE-GMTMMCVTHEMGFARKVADRVIFMDAGKIIEDCPKEEFF 224
Cdd:TIGR03269 437 ALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEmEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEEIV 516
|
....
gi 516455767 225 GDIS 228
Cdd:TIGR03269 517 EELT 520
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
2-226 |
1.08e-32 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 119.56 E-value: 1.08e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 2 ISIKNVNKWY---------GDFQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGTSIAdpkTNL 72
Cdd:COG4167 5 LEVRNLSKTFkyrtglfrrQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLE---YGD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 73 PKLRSR-VGMVFQHFE--LFPHLTITENLTIAQIKVLGRSKEEATKKGLQLLDRVGLSA-HAHKHPGQLSGGQQQRVAIA 148
Cdd:COG4167 82 YKYRCKhIRMIFQDPNtsLNPRLNIGQILEEPLRLNTDLTAEEREERIFATLRLVGLLPeHANFYPHMLSSGQKQRVALA 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 516455767 149 RALAMDPIVMLFDEPTSALDPEMVNEVLDVMVQLAQE-GMTMMCVTHEMGFARKVADRVIFMDAGKIIEDCPKEEFFGD 226
Cdd:COG4167 162 RALILQPKIIIADEALAALDMSVRSQIINLMLELQEKlGISYIYVSQHLGIVKHISDKVLVMHQGEVVEYGKTAEVFAN 240
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
2-214 |
1.13e-32 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 116.93 E-value: 1.13e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 2 ISIKNVNKWYGDFQ--VLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGTSIAdpKTNLPKLRSRV 79
Cdd:cd03246 1 LEVENVSFRYPGAEppVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADIS--QWDPNELGDHV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 80 GMVFQHFELFPHlTITENLtiaqikvlgrskeeatkkglqlldrvglsahahkhpgqLSGGQQQRVAIARALAMDPIVML 159
Cdd:cd03246 79 GYLPQDDELFSG-SIAENI--------------------------------------LSGGQRQRLGLARALYGNPRILV 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 516455767 160 FDEPTSALDPEmvNE--VLDVMVQLAQEGMTMMCVTHEMGFARKvADRVIFMDAGKI 214
Cdd:cd03246 120 LDEPNSHLDVE--GEraLNQAIAALKAAGATRIVIAHRPETLAS-ADRILVLEDGRV 173
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
15-216 |
2.03e-32 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 123.92 E-value: 2.03e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 15 QVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVN-ALEPfQKGDVIVDGTSIADpkTNLPKLRSRVGMVFQHFELFpHLT 93
Cdd:PRK13657 349 QGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQrVFDP-QSGRILIDGTDIRT--VTRASLRRNIAVVFQDAGLF-NRS 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 94 ITENLTIAqikvlgrsKEEATK-------KGLQLLDRV-----GLSAHAHKHPGQLSGGQQQRVAIARALAMDPIVMLFD 161
Cdd:PRK13657 425 IEDNIRVG--------RPDATDeemraaaERAQAHDFIerkpdGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILD 496
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 516455767 162 EPTSALDPEM---VNEVLD-VMvqlaqEGMTMMCVTHEMGFARKvADRVIFMDAGKIIE 216
Cdd:PRK13657 497 EATSALDVETeakVKAALDeLM-----KGRTTFIIAHRLSTVRN-ADRILVFDNGRVVE 549
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
13-214 |
3.90e-32 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 117.19 E-value: 3.90e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 13 DFQVLTDCSTEVKKGEVIVVCGPSGSGKSTlikCVNALEPF---QKGDVIVDGTSIADPKTNLpkLRSRVGMVFQHFELF 89
Cdd:cd03248 26 DTLVLQDVSFTLHPGEVTALVGPSGSGKST---VVALLENFyqpQGGQVLLDGKPISQYEHKY--LHSKVSLVGQEPVLF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 90 PHlTITENLTIA-QIKVLGRSKEEATKKG----LQLLDRvGLSAHAHKHPGQLSGGQQQRVAIARALAMDPIVMLFDEPT 164
Cdd:cd03248 101 AR-SLQDNIAYGlQSCSFECVKEAAQKAHahsfISELAS-GYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEAT 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 516455767 165 SALDPEMvNEVLDVMVQLAQEGMTMMCVTHEMGFARKvADRVIFMDAGKI 214
Cdd:cd03248 179 SALDAES-EQQVQQALYDWPERRTVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
5-217 |
4.70e-32 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 116.80 E-value: 4.70e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 5 KNVNKWYGDFQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGTSIAD-PKTNLPKLRSR-VGMV 82
Cdd:PRK10584 14 KSVGQGEHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQmDEEARAKLRAKhVGFV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 83 FQHFELFPHLTITENLtiaQIKVL--GRSKEEATKKGLQLLDRVGLSAHAHKHPGQLSGGQQQRVAIARALAMDPIVMLF 160
Cdd:PRK10584 94 FQSFMLIPTLNALENV---ELPALlrGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFA 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 516455767 161 DEPTSALDPEMVNEVLDVMVQLAQE-GMTMMCVTHEMGFARKVADRVIFMDaGKIIED 217
Cdd:PRK10584 171 DEPTGNLDRQTGDKIADLLFSLNREhGTTLILVTHDLQLAARCDRRLRLVN-GQLQEE 227
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
2-217 |
5.20e-32 |
|
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: 115.49 E-value: 5.20e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 2 ISIKNVNKWYG--DFQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIK-CVNALEPfQKGDVIVDGTSIADPKTNLpklRSR 78
Cdd:cd03247 1 LSINNVSFSYPeqEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQlLTGDLKP-QQGEITLDGVPVSDLEKAL---SSL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 79 VGMVFQHfelfPHL---TITENLtiaqikvlGRskeeatkkglqlldrvglsahahkhpgQLSGGQQQRVAIARALAMD- 154
Cdd:cd03247 77 ISVLNQR----PYLfdtTLRNNL--------GR---------------------------RFSGGERQRLALARILLQDa 117
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 516455767 155 PIVMLfDEPTSALDPEMVNEVLDVMVQLAqEGMTMMCVTHEM-GFARkvADRVIFMDAGKIIED 217
Cdd:cd03247 118 PIVLL-DEPTVGLDPITERQLLSLIFEVL-KDKTLIWITHHLtGIEH--MDKILFLENGKIIMQ 177
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-217 |
5.71e-32 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 116.90 E-value: 5.71e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 1 MISIKNVNKWYGDFQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGTSIADPKTNlPKLRSRVG 80
Cdd:PRK11614 5 MLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTA-KIMREAVA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 81 MVFQHFELFPHLTITENLTIAQIKVLGRSKEEATKKGLQLLDRvgLSAHAHKHPGQLSGGQQQRVAIARALAMDPIVMLF 160
Cdd:PRK11614 84 IVPEGRRVFSRMTVEENLAMGGFFAERDQFQERIKWVYELFPR--LHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 516455767 161 DEPTSALDPEMVNEVLDVMVQLAQEGMTMMCVTHEMGFARKVADRVIFMDAGKII-ED 217
Cdd:PRK11614 162 DEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHVVlED 219
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
15-215 |
8.73e-32 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 122.46 E-value: 8.73e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 15 QVLTDCSTEVKKGEVIVVCGPSGSGKSTLIkcvNALEPFQKGDVIVDGT-SIADPKTNLPKLRSRVGMVFQHFELFPHLT 93
Cdd:TIGR00955 39 HLLKNVSGVAKPGELLAVMGSSGAGKTTLM---NALAFRSPKGVKGSGSvLLNGMPIDAKEMRAISAYVQQDDLFIPTLT 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 94 ITENLTI-AQIKvLGRSKEEATKKGL--QLLDRVGLSAHAHKHPGQ------LSGGQQQRVAIARALAMDPIVMLFDEPT 164
Cdd:TIGR00955 116 VREHLMFqAHLR-MPRRVTKKEKRERvdEVLQALGLRKCANTRIGVpgrvkgLSGGERKRLAFASELLTDPPLLFCDEPT 194
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 516455767 165 SALDPEMVNEVLDVMVQLAQEGMTMMCVTH-------EMgFarkvaDRVIFMDAGKII 215
Cdd:TIGR00955 195 SGLDSFMAYSVVQVLKGLAQKGKTIICTIHqpsselfEL-F-----DKIILMAEGRVA 246
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
2-230 |
1.23e-31 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 121.99 E-value: 1.23e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 2 ISIKNVNKWYGD--FQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGTSIADpkTNLPKLRSRV 79
Cdd:TIGR03797 452 IEVDRVTFRYRPdgPLILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAG--LDVQAVRRQL 529
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 80 GMVFQHFELFPHlTITENLTIAQIKVLGRSKEEATKKGL-QLLDRVGLSAHA--HKHPGQLSGGQQQRVAIARALAMDPI 156
Cdd:TIGR03797 530 GVVLQNGRLMSG-SIFENIAGGAPLTLDEAWEAARMAGLaEDIRAMPMGMHTviSEGGGTLSGGQRQRLLIARALVRKPR 608
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 157 VMLFDEPTSALDPEMvNEVldVMVQLAQEGMTMMCVTHEMGFARKvADRVIFMDAGKIIEDCPKEE------FFGDISAR 230
Cdd:TIGR03797 609 ILLFDEATSALDNRT-QAI--VSESLERLKVTRIVIAHRLSTIRN-ADRIYVLDAGRVVQQGTYDElmaregLFAQLARR 684
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1-222 |
1.86e-31 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 116.27 E-value: 1.86e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 1 MISIKNVNKWYGDFQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGTSIADpktnlpkLRSRVg 80
Cdd:PRK11231 2 TLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISM-------LSSRQ- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 81 mVFQHFELFP-HLTITENLTIAQIKVLGRS---------KEEATKKGLQLLDRVGLSAHAHKHPGQLSGGQQQRVAIARA 150
Cdd:PRK11231 74 -LARRLALLPqHHLTPEGITVRELVAYGRSpwlslwgrlSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMV 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 516455767 151 LAMD-PIVMLfDEPTSALDPEMVNEVLDVMVQLAQEGMTMMCVTHEMGFARKVADRVIFMDAGKIIEDCPKEE 222
Cdd:PRK11231 153 LAQDtPVVLL-DEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEE 224
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
15-216 |
3.52e-31 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 120.20 E-value: 3.52e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 15 QVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEP-----FQKGDVIVDGTSI--ADPKTnLPKLR-SRVGMVFQH- 85
Cdd:PRK15134 23 TVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPsppvvYPSGDIRFHGESLlhASEQT-LRGVRgNKIAMIFQEp 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 86 -FELFPHLTITENLtiaqIKVL----GRSKEEATKKGLQLLDRVGLSAHAHK---HPGQLSGGQQQRVAIARALAMDPIV 157
Cdd:PRK15134 102 mVSLNPLHTLEKQL----YEVLslhrGMRREAARGEILNCLDRVGIRQAAKRltdYPHQLSGGERQRVMIAMALLTRPEL 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 158 MLFDEPTSALDPEMVNEVLDVMVQLAQE-GMTMMCVTHEMGFARKVADRVIFMDAGKIIE 216
Cdd:PRK15134 178 LIADEPTTALDVSVQAQILQLLRELQQElNMGLLFITHNLSIVRKLADRVAVMQNGRCVE 237
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-221 |
4.34e-31 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 116.44 E-value: 4.34e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 2 ISIKNVNKWYGDFQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGTSIAdpkTNLPKLRSRVGM 81
Cdd:PRK13537 8 IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVP---SRARHARQRVGV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 82 VFQHFELFPHLTITENLTIAQiKVLGRSKEEATKKGLQLLDRVGLSAHAHKHPGQLSGGQQQRVAIARALAMDPIVMLFD 161
Cdd:PRK13537 85 VPQFDNLDPDFTVRENLLVFG-RYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLD 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 516455767 162 EPTSALDPEMVNEVLDVMVQLAQEGMTMMCVTHEMGFARKVADRVIFMDAG-KIIEDCPKE 221
Cdd:PRK13537 164 EPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGrKIAEGAPHA 224
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
10-194 |
6.05e-31 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 119.39 E-value: 6.05e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 10 WYGDFQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGTSIADPKTNLpkLRSRVGMVFQHFELF 89
Cdd:TIGR02868 344 YPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDE--VRRRVSVCAQDAHLF 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 90 pHLTITENLTIAQIKVlgrSKEEATKkglqLLDRVGLSAHAHKHPG-----------QLSGGQQQRVAIARALAMDPIVM 158
Cdd:TIGR02868 422 -DTTVRENLRLARPDA---TDEELWA----ALERVGLADWLRALPDgldtvlgeggaRLSGGERQRLALARALLADAPIL 493
|
170 180 190
....*....|....*....|....*....|....*.
gi 516455767 159 LFDEPTSALDPEMVNEVLDVMVQlAQEGMTMMCVTH 194
Cdd:TIGR02868 494 LLDEPTEHLDAETADELLEDLLA-ALSGRTVVLITH 528
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
12-224 |
7.63e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 114.90 E-value: 7.63e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 12 GDFQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGTSIAdpKTNLPKLRSRVGMVFQHF--ELF 89
Cdd:PRK13652 15 GSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPIT--KENIREVRKFVGLVFQNPddQIF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 90 PHlTITENLTIAQIKvLGRSKEEATKKGLQLLDRVGLSAHAHKHPGQLSGGQQQRVAIARALAMDPIVMLFDEPTSALDP 169
Cdd:PRK13652 93 SP-TVEQDIAFGPIN-LGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDP 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 516455767 170 EMVNEVLDVMVQLAQE-GMTMMCVTHEMGFARKVADRVIFMDAGKIIEDCPKEEFF 224
Cdd:PRK13652 171 QGVKELIDFLNDLPETyGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIF 226
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
2-228 |
9.54e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 114.90 E-value: 9.54e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 2 ISIKNVNKWYGDFQ--VLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNAL---EPFQKGDVIVDGTSIAdpKTNLPKLR 76
Cdd:PRK13640 6 VEFKHVSFTYPDSKkpALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLllpDDNPNSKITVDGITLT--AKTVWDIR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 77 SRVGMVFQHFE-LFPHLTITENLTIAqIKVLGRSKEEATKKGLQLLDRVGLSAHAHKHPGQLSGGQQQRVAIARALAMDP 155
Cdd:PRK13640 84 EKVGIVFQNPDnQFVGATVGDDVAFG-LENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEP 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 516455767 156 IVMLFDEPTSALDPEMVNEVLDVMVQLAQE-GMTMMCVTHEMGFArKVADRVIFMDAGKIIEDCPKEEFFGDIS 228
Cdd:PRK13640 163 KIIILDESTSMLDPAGKEQILKLIRKLKKKnNLTVISITHDIDEA-NMADQVLVLDDGKLLAQGSPVEIFSKVE 235
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
2-222 |
1.80e-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: 117.98 E-value: 1.80e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 2 ISIKNVNKWYGDFQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQ--KGDVI-------------------- 59
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQYEptSGRIIyhvalcekcgyverpskvge 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 60 -------------VDGTSIADPKTNlpKLRSRVGMVFQH-FELFPHLTITENLtIAQIKVLGRSKEEATKKGLQLLDRVG 125
Cdd:TIGR03269 81 pcpvcggtlepeeVDFWNLSDKLRR--RIRKRIAIMLQRtFALYGDDTVLDNV-LEALEEIGYEGKEAVGRAVDLIEMVQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 126 LSaHAHKHPGQ-LSGGQQQRVAIARALAMDPIVMLFDEPTSALDPEMVNEVLDVMVQLAQE-GMTMMCVTHEMGFARKVA 203
Cdd:TIGR03269 158 LS-HRITHIARdLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKAsGISMVLTSHWPEVIEDLS 236
|
250
....*....|....*....
gi 516455767 204 DRVIFMDAGKIIEDCPKEE 222
Cdd:TIGR03269 237 DKAIWLENGEIKEEGTPDE 255
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
34-215 |
1.28e-29 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 113.43 E-value: 1.28e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 34 GPSGSGKSTLIKCVNALEPFQKGDVIVDGTSIADP--KTNLPKLRSRVGMVFQHFELFPHLTITENLTIAqikvLGRSKE 111
Cdd:PRK11144 31 GRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAekGICLPPEKRRIGYVFQDARLFPHYKVRGNLRYG----MAKSMV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 112 EATKKGLQLLdrvGLSAHAHKHPGQLSGGQQQRVAIARALAMDPIVMLFDEPTSALDPEMVNEVLDVMVQLAQE-GMTMM 190
Cdd:PRK11144 107 AQFDKIVALL---GIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLERLAREiNIPIL 183
|
170 180
....*....|....*....|....*
gi 516455767 191 CVTHEMGFARKVADRVIFMDAGKII 215
Cdd:PRK11144 184 YVSHSLDEILRLADRVVVLEQGKVK 208
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
16-214 |
2.41e-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: 108.67 E-value: 2.41e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 16 VLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGTSIADPKtnlPKLRSRVGMVF-----QHFELFP 90
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRS---PRDAIRAGIAYvpedrKREGLVL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 91 HLTITENLTIAQikvlgrskeeatkkglqlldrvglsahahkhpgQLSGGQQQRVAIARALAMDPIVMLFDEPTSALDPE 170
Cdd:cd03215 92 DLSVAENIALSS---------------------------------LLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVG 138
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 516455767 171 MVNEVLDVMVQLAQEGMTMMCVTHEMGFARKVADRVIFMDAGKI 214
Cdd:cd03215 139 AKAEIYRLIRELADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
16-224 |
3.32e-29 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 110.96 E-value: 3.32e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 16 VLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEP-----FQKGDVIVDGTSIADPKTNLpKLRSRVGMVFQHFELFP 90
Cdd:PRK14271 36 VLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDkvsgyRYSGDVLLGGRSIFNYRDVL-EFRRRVGMLFQRPNPFP 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 91 hLTITENLT--------IAQIKVLGRSKEEATKKGL--QLLDRVGLSahahkhPGQLSGGQQQRVAIARALAMDPIVMLF 160
Cdd:PRK14271 115 -MSIMDNVLagvrahklVPRKEFRGVAQARLTEVGLwdAVKDRLSDS------PFRLSGGQQQLLCLARTLAVNPEVLLL 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 516455767 161 DEPTSALDPEMVNEVLDVMVQLAQEgMTMMCVTHEMGFARKVADRVIFMDAGKIIEDCPKEEFF 224
Cdd:PRK14271 188 DEPTSALDPTTTEKIEEFIRSLADR-LTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLF 250
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1-228 |
7.59e-29 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 113.24 E-value: 7.59e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 1 MISIKNVNKWYGDFQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVdGTSIadpktnlpklrsRVG 80
Cdd:COG0488 315 VLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETV------------KIG 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 81 MVFQHFELF-PHLTITENLTiaqikvlgRSKEEATKKGL-QLLDRVGLS-AHAHKHPGQLSGGQQQRVAIARALAMDPIV 157
Cdd:COG0488 382 YFDQHQEELdPDKTVLDELR--------DGAPGGTEQEVrGYLGRFLFSgDDAFKPVGVLSGGEKARLALAKLLLSPPNV 453
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 516455767 158 MLFDEPTSALDPEMVNEVLDVmvqLAQ-EGmTMMCVTHEMGFARKVADRVIFMDAGKIiedcpkEEFFGDIS 228
Cdd:COG0488 454 LLLDEPTNHLDIETLEALEEA---LDDfPG-TVLLVSHDRYFLDRVATRILEFEDGGV------REYPGGYD 515
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
16-223 |
1.01e-28 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 112.80 E-value: 1.01e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 16 VLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGTSIaDPKTnlPKLRSRVGMVF-----QHFELFP 90
Cdd:COG1129 267 VVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPV-RIRS--PRDAIRAGIAYvpedrKGEGLVL 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 91 HLTITENLTIAQIKVLGR----SKEEATKKGLQLLDRVGLSAHAHKHP-GQLSGGQQQRVAIARALAMDPIVMLFDEPTS 165
Cdd:COG1129 344 DLSIRENITLASLDRLSRggllDRRRERALAEEYIKRLRIKTPSPEQPvGNLSGGNQQKVVLAKWLATDPKVLILDEPTR 423
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 516455767 166 ALDpemV---NEVLDVMVQLAQEGMTMMCVTHEMGFARKVADRVIFMDAGKIIEDCPKEEF 223
Cdd:COG1129 424 GID---VgakAEIYRLIRELAAEGKAVIVISSELPELLGLSDRILVMREGRIVGELDREEA 481
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-221 |
1.85e-28 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 110.31 E-value: 1.85e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 2 ISIKNVNKWYGDFQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGTSIADpKTNLPklRSRVGM 81
Cdd:PRK13536 42 IDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPA-RARLA--RARIGV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 82 VFQHFELFPHLTITENLTIAQiKVLGRSKEEATKKGLQLLDRVGLSAHAHKHPGQLSGGQQQRVAIARALAMDPIVMLFD 161
Cdd:PRK13536 119 VPQFDNLDLEFTVRENLLVFG-RYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILD 197
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 516455767 162 EPTSALDPEMVNEVLDVMVQLAQEGMTMMCVTHEMGFARKVADRVIFMDAG-KIIEDCPKE 221
Cdd:PRK13536 198 EPTTGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGrKIAEGRPHA 258
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-216 |
2.08e-28 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 108.09 E-value: 2.08e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 1 MISIKNVNKWYGDFQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVI--------VDGTSIADPKTNL 72
Cdd:PRK11701 6 LLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHyrmrdgqlRDLYALSEAERRR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 73 pKLRSRVGMVFQHFE--LFPHLT----ITENLTIAQIKVLGRSKEEATkkglQLLDRVGL-SAHAHKHPGQLSGGQQQRV 145
Cdd:PRK11701 86 -LLRTEWGFVHQHPRdgLRMQVSaggnIGERLMAVGARHYGDIRATAG----DWLERVEIdAARIDDLPTTFSGGMQQRL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 516455767 146 AIARALAMDPIVMLFDEPTSALDPEMVNEVLDVMVQLAQE-GMTMMCVTHEMGFARKVADRVIFMDAGKIIE 216
Cdd:PRK11701 161 QIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRElGLAVVIVTHDLAVARLLAHRLLVMKQGRVVE 232
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-212 |
2.63e-28 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 111.80 E-value: 2.63e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 1 MISIKNVNKWYGDFQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGTSIadPKTNlPKLRSR-- 78
Cdd:PRK09700 5 YISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINY--NKLD-HKLAAQlg 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 79 VGMVFQHFELFPHLTITENLTIAQI---KVLGRSK---EEATKKGLQLLDRVGLSAHAHKHPGQLSGGQQQRVAIARALA 152
Cdd:PRK09700 82 IGIIYQELSVIDELTVLENLYIGRHltkKVCGVNIidwREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLM 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 153 MDPIVMLFDEPTSALDPEMVNEVLDVMVQLAQEGMTMMCVTHEMGFARKVADRVIFMDAG 212
Cdd:PRK09700 162 LDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDG 221
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1-215 |
5.10e-28 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 107.54 E-value: 5.10e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 1 MISIKNVNKWYGDFQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGTSI-ADPKTNLPKLRSRV 79
Cdd:PRK11831 7 LVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIpAMSRSRLYTVRKRM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 80 GMVFQHFELFPHLTITENLTIAqIKVLGRSKEEATKKGLQL-LDRVGLSAHAHKHPGQLSGGQQQRVAIARALAMDPIVM 158
Cdd:PRK11831 87 SMLFQSGALFTDMNVFDNVAYP-LREHTQLPAPLLHSTVMMkLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLI 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 516455767 159 LFDEPTSALDPemvnEVLDVMVQLAQE-----GMTMMCVTHEMGFARKVADRVIFMDAGKII 215
Cdd:PRK11831 166 MFDEPFVGQDP----ITMGVLVKLISElnsalGVTCVVVSHDVPEVLSIADHAYIVADKKIV 223
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
13-225 |
9.24e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 107.10 E-value: 9.24e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 13 DFQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGTSIAdpKTNLPKLRSRVGMVFQHFE-LFPH 91
Cdd:PRK13642 19 DVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLT--AENVWNLRRKIGMVFQNPDnQFVG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 92 LTITENLTIAqIKVLGRSKEEATKKGLQLLDRVGLSAHAHKHPGQLSGGQQQRVAIARALAMDPIVMLFDEPTSALDPEM 171
Cdd:PRK13642 97 ATVEDDVAFG-MENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTG 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 516455767 172 VNEVLDVMVQLAQE-GMTMMCVTHEMGFARKvADRVIFMDAGKIIEDCPKEEFFG 225
Cdd:PRK13642 176 RQEIMRVIHEIKEKyQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELFA 229
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-222 |
1.44e-27 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 108.78 E-value: 1.44e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 1 MISIKNVNKWYGDFQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGTSIADpkTNLPKLRSRVG 80
Cdd:PRK09536 3 MIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEA--LSARAASRRVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 81 MVFQHfelfphLTITENLTIAQIKVLGRS--------KEEATKKGL-QLLDRVGLSAHAHKHPGQLSGGQQQRVAIARAL 151
Cdd:PRK09536 81 SVPQD------TSLSFEFDVRQVVEMGRTphrsrfdtWTETDRAAVeRAMERTGVAQFADRPVTSLSGGERQRVLLARAL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 516455767 152 AMDPIVMLFDEPTSALDPEMVNEVLDVMVQLAQEGMTMMCVTHEMGFARKVADRVIFMDAGKIIEDCPKEE 222
Cdd:PRK09536 155 AQATPVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPAD 225
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
27-236 |
1.99e-27 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 109.94 E-value: 1.99e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 27 GEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGTSIAD-PKTNLPKLRSRVGMVFQ--HFELFPHLTITENLtIAQI 103
Cdd:PRK10261 350 GETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTlSPGKLQALRRDIQFIFQdpYASLDPRQTVGDSI-MEPL 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 104 KVLGR-SKEEATKKGLQLLDRVGLSA-HAHKHPGQLSGGQQQRVAIARALAMDPIVMLFDEPTSALDPEMVNEVLDVMVQ 181
Cdd:PRK10261 429 RVHGLlPGKAAAARVAWLLERVGLLPeHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLD 508
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 516455767 182 LAQE-GMTMMCVTHEMGFARKVADRVIFMDAGKIIEDCPKEEFFgdisarsERAQH 236
Cdd:PRK10261 509 LQRDfGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVF-------ENPQH 557
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1-232 |
2.97e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 105.60 E-value: 2.97e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 1 MISIKNVN-KWYGDFQ-VLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGTSIADpkTNLPKLRSR 78
Cdd:PRK13648 7 IIVFKNVSfQYQSDASfTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITD--DNFEKLRKH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 79 VGMVFQHFE-LFPHLTIT-------ENLTIaqikvlgrSKEEATKKGLQLLDRVGLSAHAHKHPGQLSGGQQQRVAIARA 150
Cdd:PRK13648 85 IGIVFQNPDnQFVGSIVKydvafglENHAV--------PYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 151 LAMDPIVMLFDEPTSALDPEMVNEVLDVMVQLAQE-GMTMMCVTHEMGFARKvADRVIFMDAGKIIEDCPKEEFFGDISA 229
Cdd:PRK13648 157 LALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEhNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIFDHAEE 235
|
...
gi 516455767 230 RSE 232
Cdd:PRK13648 236 LTR 238
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
16-231 |
3.99e-27 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 108.68 E-value: 3.99e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 16 VLTDCSTEVKKGEVIVVCGPSGSGKSTLIKC-VNALEPFQkGDVIVDGTSIA--DPKTnlpkLRSRVGMVFQHFELFPHl 92
Cdd:COG4618 347 ILRGVSFSLEPGEVLGVIGPSGSGKSTLARLlVGVWPPTA-GSVRLDGADLSqwDREE----LGRHIGYLPQDVELFDG- 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 93 TITENltIAqikvlgRSKE-------EATKKG------LQLLD----RVGLSAHAhkhpgqLSGGQQQRVAIARALAMDP 155
Cdd:COG4618 421 TIAEN--IA------RFGDadpekvvAAAKLAgvhemiLRLPDgydtRIGEGGAR------LSGGQRQRIGLARALYGDP 486
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 516455767 156 IVMLFDEPTSALDPEMVNEVLDVMVQLAQEGMTMMCVTHEMGFARkVADRVIFMDAGKIIEDCPKEEFFGDISARS 231
Cdd:COG4618 487 RLVVLDEPNSNLDDEGEAALAAAIRALKARGATVVVITHRPSLLA-AVDKLLVLRDGRVQAFGPRDEVLARLARPA 561
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
1-216 |
5.30e-27 |
|
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: 104.53 E-value: 5.30e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 1 MISIKNVNKWYGDFQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDV--------IVDGTSIADPKTNL 72
Cdd:TIGR02323 3 LLQVSGLSKSYGGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTAtyimrsgaELELYQLSEAERRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 73 pKLRSRVGMVFQH------FELFPHLTITENLTIAQIKVLGRSKEEATKkglqLLDRVGLS-AHAHKHPGQLSGGQQQRV 145
Cdd:TIGR02323 83 -LMRTEWGFVHQNprdglrMRVSAGANIGERLMAIGARHYGNIRATAQD----WLEEVEIDpTRIDDLPRAFSGGMQQRL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 516455767 146 AIARALAMDPIVMLFDEPTSALDPEMVNEVLDVMVQLAQE-GMTMMCVTHEMGFARKVADRVIFMDAGKIIE 216
Cdd:TIGR02323 158 QIARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDlGLAVIIVTHDLGVARLLAQRLLVMQQGRVVE 229
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
2-219 |
5.83e-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: 103.34 E-value: 5.83e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 2 ISIKNVNKWYGD--FQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGTSIAdpKTNLPKLRSRV 79
Cdd:cd03244 3 IEFKNVSLRYRPnlPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDIS--KIGLHDLRSRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 80 GMVFQHFELFPHlTITENLTIaqikvLGRSKEEATkkgLQLLDRVGLSAHAHKHPGQL-----------SGGQQQRVAIA 148
Cdd:cd03244 81 SIIPQDPVLFSG-TIRSNLDP-----FGEYSDEEL---WQALERVGLKEFVESLPGGLdtvveeggenlSVGQRQLLCLA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 149 RALAMDPIVMLFDEPTSALDPEmvnevLDVMVQ-LAQEGM---TMMCVTHE----MGFarkvaDRVIFMDAGKIIE-DCP 219
Cdd:cd03244 152 RALLRKSKILVLDEATASVDPE-----TDALIQkTIREAFkdcTVLTIAHRldtiIDS-----DRILVLDKGRVVEfDSP 221
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1-224 |
1.13e-26 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 105.21 E-value: 1.13e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 1 MISIKNVNKWYGD----FQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFqKGDVIVDGTSI--ADPKTNLPK 74
Cdd:PRK11022 3 LLNVDKLSVHFGDesapFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDY-PGRVMAEKLEFngQDLQRISEK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 75 LR-----SRVGMVFQH--FELFPHLT----ITENLTIAQikvlGRSKEEATKKGLQLLDRVGLSAHAHK---HPGQLSGG 140
Cdd:PRK11022 82 ERrnlvgAEVAMIFQDpmTSLNPCYTvgfqIMEAIKVHQ----GGNKKTRRQRAIDLLNQVGIPDPASRldvYPHQLSGG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 141 QQQRVAIARALAMDPIVMLFDEPTSALDPEMVNEVLDVMVQLAQ-EGMTMMCVTHEMGFARKVADRVIFMDAGKIIEDCP 219
Cdd:PRK11022 158 MSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQkENMALVLITHDLALVAEAAHKIIVMYAGQVVETGK 237
|
....*
gi 516455767 220 KEEFF 224
Cdd:PRK11022 238 AHDIF 242
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
19-224 |
1.36e-26 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 103.24 E-value: 1.36e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 19 DCSTEVKKGEVIVVCGPSGSGKStlIKCVNALEPFQKGDVIVDGTSIADPKTNLP-KLRSR-VGMVFQH----FElfPHL 92
Cdd:PRK10418 21 GVSLTLQRGRVLALVGGSGSGKS--LTCAAALGILPAGVRQTAGRVLLDGKPVAPcALRGRkIATIMQNprsaFN--PLH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 93 TITENlTIAQIKVLGRSKEEATKkgLQLLDRVGLsAHAHK----HPGQLSGGQQQRVAIARALAMDPIVMLFDEPTSALD 168
Cdd:PRK10418 97 TMHTH-ARETCLALGKPADDATL--TAALEAVGL-ENAARvlklYPFEMSGGMLQRMMIALALLCEAPFIIADEPTTDLD 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 516455767 169 PEMVNEVLDVMVQLAQE-GMTMMCVTHEMGFARKVADRVIFMDAGKIIEDCPKEEFF 224
Cdd:PRK10418 173 VVAQARILDLLESIVQKrALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLF 229
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
26-214 |
1.65e-26 |
|
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: 107.79 E-value: 1.65e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 26 KGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGTSIadpKTNLPKLRSRVGMVFQHFELFPHLTITEN-LTIAQIK 104
Cdd:TIGR01257 955 ENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI---ETNLDAVRQSLGMCPQHNILFHHLTVAEHiLFYAQLK 1031
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 105 vlGRSKEEATKKGLQLLDRVGLSAHAHKHPGQLSGGQQQRVAIARALAMDPIVMLFDEPTSALDPEMVNEVLDVMVQLaQ 184
Cdd:TIGR01257 1032 --GRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKY-R 1108
|
170 180 190
....*....|....*....|....*....|
gi 516455767 185 EGMTMMCVTHEMGFARKVADRVIFMDAGKI 214
Cdd:TIGR01257 1109 SGRTIIMSTHHMDEADLLGDRIAIISQGRL 1138
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
17-223 |
4.97e-26 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 105.26 E-value: 4.97e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 17 LTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPF--QKGDVIVDGT-----SIADPKtnlpklrsRVGMVFQHFEL- 88
Cdd:NF040905 17 LDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHgsYEGEILFDGEvcrfkDIRDSE--------ALGIVIIHQELa 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 89 -FPHLTITENLtiaqikVLG--RSK------EEATKKGLQLLDRVGLSAHAHKHPGQLSGGQQQRVAIARALAMDPIVML 159
Cdd:NF040905 89 lIPYLSIAENI------FLGneRAKrgvidwNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLI 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 516455767 160 FDEPTSALDPEMVNEVLDVMVQLAQEGMTMMCVTHEMGFARKVADRVIFMDAGKIIE--DCPKEEF 223
Cdd:NF040905 163 LDEPTAALNEEDSAALLDLLLELKAQGITSIIISHKLNEIRRVADSITVLRDGRTIEtlDCRADEV 228
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
15-224 |
5.81e-26 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 105.56 E-value: 5.81e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 15 QVLTDCSTEVKKGEVIVVCGPSGSGKST----LIKCVNAlepfqKGDVIVDGTSIA--DPKTNLPkLRSRVGMVFQ--HF 86
Cdd:PRK15134 300 VVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLINS-----QGEIWFDGQPLHnlNRRQLLP-VRHRIQVVFQdpNS 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 87 ELFPHLT----ITENLTIAQIKVLGRSKEEATKKGLQlldRVGLSAHA-HKHPGQLSGGQQQRVAIARALAMDPIVMLFD 161
Cdd:PRK15134 374 SLNPRLNvlqiIEEGLRVHQPTLSAAQREQQVIAVME---EVGLDPETrHRYPAEFSGGQRQRIAIARALILKPSLIILD 450
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 516455767 162 EPTSALDPEMVNEVLDVMVQLAQE-GMTMMCVTHEMGFARKVADRVIFMDAGKIIEDCPKEEFF 224
Cdd:PRK15134 451 EPTSSLDKTVQAQILALLKSLQQKhQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERVF 514
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-217 |
2.47e-25 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 99.77 E-value: 2.47e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 1 MISIKNVNKWY----------------------GDFQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDV 58
Cdd:COG1134 4 MIEVENVSKSYrlyhepsrslkelllrrrrtrrEEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 59 IVDG--TSIADpktnlpklrsrVGMVFQhfelfPHLTITENLT-IAQIkvLGRSKEEATKKglqlLDRV----GLSAHAH 131
Cdd:COG1134 84 EVNGrvSALLE-----------LGAGFH-----PELTGRENIYlNGRL--LGLSRKEIDEK----FDEIvefaELGDFID 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 132 ---KHpgqLSGGQQQRVAIARALAMDPIVMLFDEPTSALDPEMVNEVLDVMVQLAQEGMTMMCVTHEMGFARKVADRVIF 208
Cdd:COG1134 142 qpvKT---YSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRESGRTVIFVSHSMGAVRRLCDRAIW 218
|
....*....
gi 516455767 209 MDAGKIIED 217
Cdd:COG1134 219 LEKGRLVMD 227
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-215 |
3.95e-25 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 102.84 E-value: 3.95e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 4 IKNVNKWYGDFQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGtsiadpktnlpklRSRVGMVF 83
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK-------------GLRIGYLP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 84 QHFELFPHLTITENL---------TIAQIKVLGRSKEEATKKGL----------------------QLLDRVGLSAHAHK 132
Cdd:COG0488 68 QEPPLDDDLTVLDTVldgdaelraLEAELEELEAKLAEPDEDLErlaelqeefealggweaearaeEILSGLGFPEEDLD 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 133 HP-GQLSGGQQQRVAIARALAMDPIVMLFDEPTSALDPEMVN--EVLdvmvqLAQEGMTMMCVTHEMGFARKVADRVIFM 209
Cdd:COG0488 148 RPvSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIEwlEEF-----LKNYPGTVLVVSHDRYFLDRVATRILEL 222
|
....*.
gi 516455767 210 DAGKII 215
Cdd:COG0488 223 DRGKLT 228
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
4-215 |
8.17e-25 |
|
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: 97.85 E-value: 8.17e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 4 IKNVNKWYGDFQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGTsiadpKTNLPKLRSrVGMVF 83
Cdd:TIGR03740 3 TKNLSKRFGKQTAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGH-----PWTRKDLHK-IGSLI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 84 QHFELFPHLTITENLTIaQIKVLGRSKEEAtkkgLQLLDRVGLSAHAHKHPGQLSGGQQQRVAIARALAMDPIVMLFDEP 163
Cdd:TIGR03740 77 ESPPLYENLTARENLKV-HTTLLGLPDSRI----DEVLNIVDLTNTGKKKAKQFSLGMKQRLGIAIALLNHPKLLILDEP 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 516455767 164 TSALDPEMVNEVLDVMVQLAQEGMTMMCVTHEMGFARKVADRVIFMDAGKII 215
Cdd:TIGR03740 152 TNGLDPIGIQELRELIRSFPEQGITVILSSHILSEVQQLADHIGIISEGVLG 203
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
13-216 |
8.31e-25 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 102.49 E-value: 8.31e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 13 DFQVLTDCSTEVKKGEVIVVCGPSGSGKSTlikCVNALEPFQK---GDVIVDGTSIadPKTNLPKLRSRVGMVFQHFELF 89
Cdd:TIGR00958 493 DVPVLKGLTFTLHPGEVVALVGPSGSGKST---VAALLQNLYQptgGQVLLDGVPL--VQYDHHYLHRQVALVGQEPVLF 567
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 90 PHlTITENLTIAqikvLGRSKEEATKKGLQLldrvglsAHAH---------------KHPGQLSGGQQQRVAIARALAMD 154
Cdd:TIGR00958 568 SG-SVRENIAYG----LTDTPDEEIMAAAKA-------ANAHdfimefpngydtevgEKGSQLSGGQKQRIAIARALVRK 635
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 516455767 155 PIVMLFDEPTSALDPEMVNEVLDVMvqlAQEGMTMMCVTHEMGFARKvADRVIFMDAGKIIE 216
Cdd:TIGR00958 636 PRVLILDEATSALDAECEQLLQESR---SRASRTVLLIAHRLSTVER-ADQILVLKKGSVVE 693
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
11-217 |
1.52e-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: 101.74 E-value: 1.52e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 11 YGDfQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKC-VNALEPfQKGDVIVDGTSIADpkTNLPKLRSRVGMVFQHFELF 89
Cdd:TIGR01193 485 YGS-NILSDISLTIKMNSKTTIVGMSGSGKSTLAKLlVGFFQA-RSGEILLNGFSLKD--IDRHTLRQFINYLPQEPYIF 560
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 90 PHlTITENLTIAqikvlgrSKEEATKkglQLLDRV---------------GLSAHAHKHPGQLSGGQQQRVAIARALAMD 154
Cdd:TIGR01193 561 SG-SILENLLLG-------AKENVSQ---DEIWAAceiaeikddienmplGYQTELSEEGSSISGGQKQRIALARALLTD 629
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 516455767 155 PIVMLFDEPTSALDPEMVNEVLDVMVQLAQEgmTMMCVTHEMGFARKVaDRVIFMDAGKIIED 217
Cdd:TIGR01193 630 SKVLILDESTSNLDTITEKKIVNNLLNLQDK--TIIFVAHRLSVAKQS-DKIIVLDHGKIIEQ 689
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
5-226 |
2.76e-24 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 96.89 E-value: 2.76e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 5 KNVNKWYGDFQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGTSIadpkTNLP---KLRSRVGM 81
Cdd:PRK10895 7 KNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDI----SLLPlhaRARRGIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 82 VFQHFELFPHLTITENL-TIAQIKVlGRSKEEATKKGLQLLDRVGLSaHAHKHPGQ-LSGGQQQRVAIARALAMDPIVML 159
Cdd:PRK10895 83 LPQEASIFRRLSVYDNLmAVLQIRD-DLSAEQREDRANELMEEFHIE-HLRDSMGQsLSGGERRRVEIARALAANPKFIL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 516455767 160 FDEPTSALDPEMVNEVLDVMVQLAQEGMTMMCVTHEMGFARKVADRVIFMDAGKIIEDCPKEEFFGD 226
Cdd:PRK10895 161 LDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQD 227
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1-194 |
3.88e-24 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 95.71 E-value: 3.88e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 1 MISIKNVNKWYGDFQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGTSIADPKtnlpkLRSRVG 80
Cdd:PRK13539 2 MLEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPD-----VAEACH 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 81 MVFQHFELFPHLTITENLTI-AQIKVLGRSKEEATkkglqlLDRVGLSAHAHKHPGQLSGGQQQRVAIARALAMDPIVML 159
Cdd:PRK13539 77 YLGHRNAMKPALTVAENLEFwAAFLGGEELDIAAA------LEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWI 150
|
170 180 190
....*....|....*....|....*....|....*.
gi 516455767 160 FDEPTSALDPEMVNEVLDVM-VQLAQEGMTMMcVTH 194
Cdd:PRK13539 151 LDEPTAALDAAAVALFAELIrAHLAQGGIVIA-ATH 185
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
5-223 |
6.39e-24 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 99.62 E-value: 6.39e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 5 KNVNKWYGDFQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPF--QKGDVIVDG-----TSIADPKtnlpklrs 77
Cdd:PRK13549 9 KNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHgtYEGEIIFEGeelqaSNIRDTE-------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 78 RVGMVFQHFEL--FPHLTITENLtiaqikVLGRskeEATKKGL-----------QLLDRVGLSAHAHKHPGQLSGGQQQR 144
Cdd:PRK13549 81 RAGIAIIHQELalVKELSVLENI------FLGN---EITPGGImdydamylraqKLLAQLKLDINPATPVGNLGLGQQQL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 516455767 145 VAIARALAMDPIVMLFDEPTSALDPEMVNEVLDVMVQLAQEGMTMMCVTHEMGFARKVADRVIFMDAGKIIEDCPKEEF 223
Cdd:PRK13549 152 VEIAKALNKQARLLILDEPTASLTESETAVLLDIIRDLKAHGIACIYISHKLNEVKAISDTICVIRDGRHIGTRPAAGM 230
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
21-216 |
7.72e-24 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 99.53 E-value: 7.72e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 21 STEVKKGEVIVVCGPSGSGKSTLIkcvNALEPF--QKGDVIVDGTSIADpkTNLPKLRSRVGMVFQHFELFpHLTITENL 98
Cdd:PRK11174 370 NFTLPAGQRIALVGPSGAGKTSLL---NALLGFlpYQGSLKINGIELRE--LDPESWRKHLSWVGQNPQLP-HGTLRDNV 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 99 TIAQIKVlgrSKEEATkkglQLLDRVGLSAHAHKHP-----------GQLSGGQQQRVAIARALAMDPIVMLFDEPTSAL 167
Cdd:PRK11174 444 LLGNPDA---SDEQLQ----QALENAWVSEFLPLLPqgldtpigdqaAGLSVGQAQRLALARALLQPCQLLLLDEPTASL 516
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 516455767 168 DPEMVNEVLDVMVQLAQEGMTMMcVTHEMGFARKVaDRVIFMDAGKIIE 216
Cdd:PRK11174 517 DAHSEQLVMQALNAASRRQTTLM-VTHQLEDLAQW-DQIWVMQDGQIVQ 563
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
11-221 |
8.47e-24 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 96.21 E-value: 8.47e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 11 YGDFQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGTSIADPKTNlpKLRSRVGMVFQHfelfp 90
Cdd:PRK10253 17 YGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASK--EVARRIGLLAQN----- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 91 hLTITENLTIAQIKVLGR------------SKEEATKKGLQlldRVGLSAHAHKHPGQLSGGQQQRVAIARALAMDPIVM 158
Cdd:PRK10253 90 -ATTPGDITVQELVARGRyphqplftrwrkEDEEAVTKAMQ---ATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIM 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 516455767 159 LFDEPTSALDPEMVNEVLDVMVQLAQE-GMTMMCVTHEMGFARKVADRVIFMDAGKII-EDCPKE 221
Cdd:PRK10253 166 LLDEPTTWLDISHQIDLLELLSELNREkGYTLAAVLHDLNQACRYASHLIALREGKIVaQGAPKE 230
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
21-216 |
8.98e-24 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 96.01 E-value: 8.98e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 21 STEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGTSIADPKTnlpKLRS-RVGMVFQ--HFELFPHLTITEN 97
Cdd:PRK15112 33 SFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDY---SYRSqRIRMIFQdpSTSLNPRQRISQI 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 98 LTIAQIKVLGRSKEEATKKGLQLLDRVGLSA-HAHKHPGQLSGGQQQRVAIARALAMDPIVMLFDEPTSALDPEMVNEVL 176
Cdd:PRK15112 110 LDFPLRLNTDLEPEQREKQIIETLRQVGLLPdHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLI 189
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 516455767 177 DVMVQLAQE-GMTMMCVTHEMGFARKVADRVIFMDAGKIIE 216
Cdd:PRK15112 190 NLMLELQEKqGISYIYVTQHLGMMKHISDQVLVMHQGEVVE 230
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
2-216 |
1.74e-23 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 98.55 E-value: 1.74e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 2 ISIKNVNKWY--GDFQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGTSIADPKtnLPKLRSRV 79
Cdd:PRK11176 342 IEFRNVTFTYpgKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYT--LASLRNQV 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 80 GMVFQHFELFpHLTITENLTIAQIKVLGRSKEEATKKGLQLLDRV-----GLSAHAHKHPGQLSGGQQQRVAIARALAMD 154
Cdd:PRK11176 420 ALVSQNVHLF-NDTIANNIAYARTEQYSREQIEEAARMAYAMDFInkmdnGLDTVIGENGVLLSGGQRQRIAIARALLRD 498
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 516455767 155 PIVMLFDEPTSALDPE---MVNEVLDVMvqlaQEGMTMMCVTHEMGFARKvADRVIFMDAGKIIE 216
Cdd:PRK11176 499 SPILILDEATSALDTEserAIQAALDEL----QKNRTSLVIAHRLSTIEK-ADEILVVEDGEIVE 558
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
27-226 |
1.98e-23 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 96.31 E-value: 1.98e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 27 GEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGTSIADPKTN-LPKLRSRVGMVFQH--FELFPHLT----ITENLT 99
Cdd:PRK15079 47 GETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDeWRAVRSDIQMIFQDplASLNPRMTigeiIAEPLR 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 100 IAQIKVlgrSKEEATKKGLQLLDRVGLSAHA-HKHPGQLSGGQQQRVAIARALAMDPIVMLFDEPTSALDPEMVNEVLDV 178
Cdd:PRK15079 127 TYHPKL---SRQEVKDRVKAMMLKVGLLPNLiNRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNL 203
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 516455767 179 MVQLAQE-GMTMMCVTHEMGFARKVADRVIFMDAGKIIEDCPKEEFFGD 226
Cdd:PRK15079 204 LQQLQREmGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHN 252
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
2-213 |
3.23e-23 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 91.36 E-value: 3.23e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 2 ISIKNVNKWYGDFQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGTsiadpktnlpklrsrvgM 81
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGST-----------------V 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 82 VFQHFElfphltitenltiaqikvlgrskeeatkkglqlldrvglsahahkhpgQLSGGQQQRVAIARALAMDPIVMLFD 161
Cdd:cd03221 64 KIGYFE------------------------------------------------QLSGGEKMRLALAKLLLENPNLLLLD 95
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 516455767 162 EPTSALDPEMVNEVLDVMVQLAQegmTMMCVTHEMGFARKVADRVIFMDAGK 213
Cdd:cd03221 96 EPTNHLDLESIEALEEALKEYPG---TVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1-207 |
3.36e-23 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 93.63 E-value: 3.36e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 1 MISIKNVNKWYGDFQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGTSIA--DPKTnlpkLRSR 78
Cdd:PRK10247 7 LLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDIStlKPEI----YRQQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 79 VGMVFQHFELFPHlTITENLTIA-QIkvlgRSKEEATKKGLQLLDRVGLSAHA-HKHPGQLSGGQQQRVAIARALAMDPI 156
Cdd:PRK10247 83 VSYCAQTPTLFGD-TVYDNLIFPwQI----RNQQPDPAIFLDDLERFALPDTIlTKNIAELSGGEKQRISLIRNLQFMPK 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 516455767 157 VMLFDEPTSALDP---EMVNEVLDVMVQlaQEGMTMMCVTHEMGfARKVADRVI 207
Cdd:PRK10247 158 VLLLDEITSALDEsnkHNVNEIIHRYVR--EQNIAVLWVTHDKD-EINHADKVI 208
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
27-197 |
3.41e-23 |
|
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: 92.81 E-value: 3.41e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 27 GEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGTSIAD----PKTNLPKLRSRVGMVfqhfelfPHLTITENLTIaq 102
Cdd:TIGR01189 26 GEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEqrdePHENILYLGHLPGLK-------PELSALENLHF-- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 103 ikvLGRSKEEATKKGLQLLDRVGLSAHAHKHPGQLSGGQQQRVAIARALAMDPIVMLFDEPTSALDPEMVNEVLDVMVQ- 181
Cdd:TIGR01189 97 ---WAAIHGGAQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVALLAGLLRAh 173
|
170
....*....|....*.
gi 516455767 182 LAQEGMTMMCVTHEMG 197
Cdd:TIGR01189 174 LARGGIVLLTTHQDLG 189
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
15-216 |
3.91e-23 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 97.58 E-value: 3.91e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 15 QVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKcvnaL-----EPfQKGDVIVDGTSIADpkTNLPKLRSRVGMVFQHFELF 89
Cdd:COG5265 372 PILKGVSFEVPAGKTVAIVGPSGAGKSTLAR----LlfrfyDV-TSGRILIDGQDIRD--VTQASLRAAIGIVPQDTVLF 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 90 pHLTITENltIAqikvLGR---SKEE--ATKKGLQLLD-----------RVG---LsahahkhpgQLSGGQQQRVAIARA 150
Cdd:COG5265 445 -NDTIAYN--IA----YGRpdaSEEEveAAARAAQIHDfieslpdgydtRVGergL---------KLSGGEKQRVAIART 508
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 151 LAMDPIVMLFDEPTSALDPEMVNEVLDVMVQLAQeGMTMMCVTHemgfaR--KV--ADRVIFMDAGKIIE 216
Cdd:COG5265 509 LLKNPPILIFDEATSALDSRTERAIQAALREVAR-GRTTLVIAH-----RlsTIvdADEILVLEAGRIVE 572
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
4-216 |
3.95e-23 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 97.16 E-value: 3.95e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 4 IKNVNKWygDFQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGTSIAdPKTNLPKLRSRVGMVF 83
Cdd:PRK09700 268 VRNVTSR--DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDIS-PRSPLDAVKKGMAYIT 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 84 QHFE---LFPHLTITENLTIAQIKVLGRSK------EEATKKGLQLLDRVGLSAHAH---KHPGQLSGGQQQRVAIARAL 151
Cdd:PRK09700 345 ESRRdngFFPNFSIAQNMAISRSLKDGGYKgamglfHEVDEQRTAENQRELLALKCHsvnQNITELSGGNQQKVLISKWL 424
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 516455767 152 AMDPIVMLFDEPTSALDPEMVNEVLDVMVQLAQEGMTMMCVTHEMGFARKVADRVIFMDAGKIIE 216
Cdd:PRK09700 425 CCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRLTQ 489
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1-224 |
4.50e-23 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 97.23 E-value: 4.50e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 1 MISIKNVNKWY----GDFQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGTSIADPKTNLPKLR 76
Cdd:PRK10261 12 VLAVENLNIAFmqeqQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRRRSRQVIELS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 77 SR------------VGMVFQH--FELFPHLTITENltIAQIKVL--GRSKEEATKKGLQLLDRVGL-SAHA--HKHPGQL 137
Cdd:PRK10261 92 EQsaaqmrhvrgadMAMIFQEpmTSLNPVFTVGEQ--IAESIRLhqGASREEAMVEAKRMLDQVRIpEAQTilSRYPHQL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 138 SGGQQQRVAIARALAMDPIVMLFDEPTSALDPEMVNEVLDVMVQLAQE-GMTMMCVTHEMGFARKVADRVIFMDAGKIIE 216
Cdd:PRK10261 170 SGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEmSMGVIFITHDMGVVAEIADRVLVMYQGEAVE 249
|
....*...
gi 516455767 217 DCPKEEFF 224
Cdd:PRK10261 250 TGSVEQIF 257
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
7-218 |
8.12e-23 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 92.78 E-value: 8.12e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 7 VNKWYGDFQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGTsiaDPKTNLPKLRSRVGMVF-QH 85
Cdd:cd03267 27 FKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGL---VPWKRRKKFLRRIGVVFgQK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 86 FELFPHLTITENLTIAQiKVLGRSKEEATKKGLQLLDRVGLSAHAHKHPGQLSGGQQQRVAIARALAMDPIVMLFDEPTS 165
Cdd:cd03267 104 TQLWWDLPVIDSFYLLA-AIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTI 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 516455767 166 ALDPEMVNEVLDVMVQLAQE-GMTMMCVTHEMGFARKVADRVIFMDAGKIIEDC 218
Cdd:cd03267 183 GLDVVAQENIRNFLKEYNRErGTTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
27-222 |
8.56e-23 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 93.31 E-value: 8.56e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 27 GEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGTSIADPKTnlpKLRSR-VGMVFQHFELFPHLTITENLTIAQIK- 104
Cdd:PRK10575 37 GKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSS---KAFARkVAYLPQQLPAAEGMTVRELVAIGRYPw 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 105 --VLGRSKEEATKKGLQLLDRVGLSAHAHKHPGQLSGGQQQRVAIARALAMDPIVMLFDEPTSALDPEMVNEVLDVMVQL 182
Cdd:PRK10575 114 hgALGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRL 193
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 516455767 183 AQE-GMTMMCVTHEMGFARKVADRVIFMDAGKIIEDCPKEE 222
Cdd:PRK10575 194 SQErGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAE 234
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
16-214 |
1.09e-22 |
|
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: 96.26 E-value: 1.09e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 16 VLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGTSIA--DPKTnlpkLRSRVGMVFQHFELFPHlT 93
Cdd:TIGR01842 333 TLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKqwDRET----FGKHIGYLPQDVELFPG-T 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 94 ITENltIAQIKVLGRSKE--EATKkglqlldrvglSAHAH----KHP-----------GQLSGGQQQRVAIARALAMDPI 156
Cdd:TIGR01842 408 VAEN--IARFGENADPEKiiEAAK-----------LAGVHelilRLPdgydtvigpggATLSGGQRQRIALARALYGDPK 474
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 516455767 157 VMLFDEPTSALDPEMVNEVLDVMVQLAQEGMTMMCVTHEMGfARKVADRVIFMDAGKI 214
Cdd:TIGR01842 475 LVVLDEPNSNLDEEGEQALANAIKALKARGITVVVITHRPS-LLGCVDKILVLQDGRI 531
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
12-224 |
1.12e-22 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 94.41 E-value: 1.12e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 12 GDFQVLTDCSTEVKKGEVIVVCGPSGSGKStliKCVNALEPFQKGDVIVDGTSIAD-------PKTNLPKLRS-RVGMVF 83
Cdd:PRK09473 27 GDVTAVNDLNFSLRAGETLGIVGESGSGKS---QTAFALMGLLAANGRIGGSATFNgreilnlPEKELNKLRAeQISMIF 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 84 QH--FELFPHLTITENLTiaqiKVL----GRSKEEATKKGLQLLDRVGLSaHAHK----HPGQLSGGQQQRVAIARALAM 153
Cdd:PRK09473 104 QDpmTSLNPYMRVGEQLM----EVLmlhkGMSKAEAFEESVRMLDAVKMP-EARKrmkmYPHEFSGGMRQRVMIAMALLC 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 516455767 154 DPIVMLFDEPTSALDPEMVNEVLDVMVQLAQE-GMTMMCVTHEMGFARKVADRVIFMDAGKIIEDCPKEEFF 224
Cdd:PRK09473 179 RPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARDVF 250
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
11-232 |
1.40e-22 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 93.15 E-value: 1.40e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 11 YGDFQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGTSIADPKTNLPKLRSRVGMVFQHFELFP 90
Cdd:PRK13638 11 YQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKRGLLALRQQVATVFQDPEQQI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 91 HLTITENLTIAQIKVLGRSKEEATKK---GLQLLDrvglSAHAHKHPGQ-LSGGQQQRVAIARALAMDPIVMLFDEPTSA 166
Cdd:PRK13638 91 FYTDIDSDIAFSLRNLGVPEAEITRRvdeALTLVD----AQHFRHQPIQcLSHGQKKRVAIAGALVLQARYLLLDEPTAG 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 516455767 167 LDPEMVNEVLDVMVQLAQEGMTMMCVTHEMGFARKVADRVIFMDAGKIIEDCPKEEFFgdisARSE 232
Cdd:PRK13638 167 LDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVF----ACTE 228
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
2-217 |
1.97e-22 |
|
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: 91.44 E-value: 1.97e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 2 ISIKNVNKWY----------------------GDFQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVI 59
Cdd:cd03220 1 IELENVSKSYptykggssslkklgilgrkgevGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 60 VDGTSIADPktnlpklrsRVGMVFQhfelfPHLTITENLTIAQIkVLGRSKEEATKKglqlLDRV----GLSAHAHKHPG 135
Cdd:cd03220 81 VRGRVSSLL---------GLGGGFN-----PELTGRENIYLNGR-LLGLSRKEIDEK----IDEIiefsELGDFIDLPVK 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 136 QLSGGQQQRVAIARALAMDPIVMLFDEPTSALDPEMVNEVLDVMVQLAQEGMTMMCVTHEMGFARKVADRVIFMDAGKII 215
Cdd:cd03220 142 TYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIR 221
|
..
gi 516455767 216 ED 217
Cdd:cd03220 222 FD 223
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
2-221 |
2.74e-22 |
|
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: 90.66 E-value: 2.74e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 2 ISIKNVNKWYGDFQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQ--KGDVIVDGTSIadpkTNL-PKLRSR 78
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKYEvtEGEILFKGEDI----TDLpPEERAR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 79 VG--MVFQHFELFPHLTITENLtiaqikvlgRSKEEAtkkglqlldrvglsahahkhpgqLSGGQQQRVAIARALAMDPI 156
Cdd:cd03217 77 LGifLAFQYPPEIPGVKNADFL---------RYVNEG-----------------------FSGGEKKRNEILQLLLLEPD 124
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 516455767 157 VMLFDEPTSALDPEMVNEVLDVMVQLAQEGMTMMCVTH-EMGFARKVADRVIFMDAGKIIEDCPKE 221
Cdd:cd03217 125 LAILDEPDSGLDIDALRLVAEVINKLREEGKSVLIITHyQRLLDYIKPDRVHVLYDGRIVKSGDKE 190
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
16-194 |
4.02e-22 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 94.49 E-value: 4.02e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 16 VLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIV-DGTSIA----DPKTNLPKLRSRVgmvfqhfeLFP 90
Cdd:COG4178 378 LLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARpAGARVLflpqRPYLPLGTLREAL--------LYP 449
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 91 HLTitENLTIAQIKvlgrskeeatkkglQLLDRVGLSAHAHKH------PGQLSGGQQQRVAIARALAMDPIVMLFDEPT 164
Cdd:COG4178 450 ATA--EAFSDAELR--------------EALEAVGLGHLAERLdeeadwDQVLSLGEQQRLAFARLLLHKPDWLFLDEAT 513
|
170 180 190
....*....|....*....|....*....|
gi 516455767 165 SALDPEMVNEVLDvMVQLAQEGMTMMCVTH 194
Cdd:COG4178 514 SALDEENEAALYQ-LLREELPGTTVISVGH 542
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
10-234 |
9.91e-22 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 90.71 E-value: 9.91e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 10 WYGDFQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGTSiadpkTNLPKLRSRVGMVFQHFEL- 88
Cdd:PRK15056 16 WRNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQP-----TRQALQKNLVAYVPQSEEVd 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 89 --FPHLTitENLTI----AQIKVLGRSKEEATKKGLQLLDRVGLSAHAHKHPGQLSGGQQQRVAIARALAMDPIVMLFDE 162
Cdd:PRK15056 91 wsFPVLV--EDVVMmgryGHMGWLRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDE 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 516455767 163 PTSALDPEMVNEVLDVMVQLAQEGMTMMCVTHEMGFARKVADRVIfMDAGKIIEDCPKEEFFgdISARSERA 234
Cdd:PRK15056 169 PFTGVDVKTEARIISLLRELRDEGKTMLVSTHNLGSVTEFCDYTV-MVKGTVLASGPTETTF--TAENLELA 237
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
21-215 |
1.41e-21 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 89.90 E-value: 1.41e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 21 STEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQkGDVIVDGTSIAD-PKTNLPKLRS--------RVGM-VFQHFELF- 89
Cdd:COG4138 16 SAQVNAGELIHLIGPNGAGKSTLLARMAGLLPGQ-GEILLNGRPLSDwSAAELARHRAylsqqqspPFAMpVFQYLALHq 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 90 PHLTITEnltiAQIKVLGrskeeatkkglQLLDRVGLSAHAHKHPGQLSGGQQQRVAIARA-LAMDPIV------MLFDE 162
Cdd:COG4138 95 PAGASSE----AVEQLLA-----------QLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVlLQVWPTInpegqlLLLDE 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 516455767 163 PTSALDPEMVNEVLDVMVQLAQEGMTMMCVTHEMGFARKVADRVIFMDAGKII 215
Cdd:COG4138 160 PMNSLDVAQQAALDRLLRELCQQGITVVMSSHDLNHTLRHADRVWLLKQGKLV 212
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1-235 |
1.97e-21 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 92.42 E-value: 1.97e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 1 MISIKNVNKWYGDFQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGTsiadPKTNL-PKLRSRV 79
Cdd:PRK15439 11 LLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGN----PCARLtPAKAHQL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 80 G--MVFQHFELFPHLTITENLtiaqikVLGRSKEEATKKGL-QLLDRVGLSAHAHKHPGQLSGGQQQRVAIARALAMDPI 156
Cdd:PRK15439 87 GiyLVPQEPLLFPNLSVKENI------LFGLPKRQASMQKMkQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 157 VMLFDEPTSALDPEMVNEVLDVMVQLAQEGMTMMCVTHEMGFARKVADRVIFMDAGKIIEDCPKEEFFGD--ISARSERA 234
Cdd:PRK15439 161 ILILDEPTASLTPAETERLFSRIRELLAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTADLSTDdiIQAITPAA 240
|
.
gi 516455767 235 Q 235
Cdd:PRK15439 241 R 241
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1-215 |
3.41e-21 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 91.81 E-value: 3.41e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 1 MISIKNVNKWYGDFQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPF--QKGDVIVDGTSIadpKTNLPKLRSR 78
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHgtWDGEIYWSGSPL---KASNIRDTER 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 79 VGMVFQHFEL--FPHLTITENLTIA-QIKVLGR--SKEEATKKGLQLLDRVGLSAHAHKHP-GQLSGGQQQRVAIARALA 152
Cdd:TIGR02633 78 AGIVIIHQELtlVPELSVAENIFLGnEITLPGGrmAYNAMYLRAKNLLRELQLDADNVTRPvGDYGGGQQQLVEIAKALN 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 516455767 153 MDPIVMLFDEPTSALDPEMVNEVLDVMVQLAQEGMTMMCVTHEMGFARKVADRVIFMDAGKII 215
Cdd:TIGR02633 158 KQARLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQHV 220
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
27-195 |
4.80e-21 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 91.48 E-value: 4.80e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 27 GEVIVVCGPSGSGKSTLIkcvNALEPFQKGDVIVDGTSIADPKTNLPKLRsRVGMVFQHFELFPHLTITENLTIAQIKVL 106
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLL---NALAGRIQGNNFTGTILANNRKPTKQILK-RTGFVTQDDILYPHLTVRETLVFCSLLRL 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 107 GRS--KEEATKKGLQLLDRVGLSAHAHKHPGQ-----LSGGQQQRVAIARALAMDPIVMLFDEPTSALDPEMVNEVLDVM 179
Cdd:PLN03211 170 PKSltKQEKILVAESVISELGLTKCENTIIGNsfirgISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLTL 249
|
170
....*....|....*.
gi 516455767 180 VQLAQEGMTMMCVTHE 195
Cdd:PLN03211 250 GSLAQKGKTIVTSMHQ 265
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
19-217 |
8.59e-21 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 90.65 E-value: 8.59e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 19 DCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQ-KGDVIVDGTSIaDPKTNLPKLRSRVGMVFQHFE---LFPHLTI 94
Cdd:TIGR02633 278 DVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKPV-DIRNPAQAIRAGIAMVPEDRKrhgIVPILGV 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 95 TENLTIAQIK---VLGRSKEEATKKGL-QLLDRVGLSAHAHKHP-GQLSGGQQQRVAIARALAMDPIVMLFDEPTSALDP 169
Cdd:TIGR02633 357 GKNITLSVLKsfcFKMRIDAAAELQIIgSAIQRLKVKTASPFLPiGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDV 436
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 516455767 170 EMVNEVLDVMVQLAQEGMTMMCVTHEMGFARKVADRVIFMDAGKIIED 217
Cdd:TIGR02633 437 GAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGKLKGD 484
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
2-213 |
1.69e-20 |
|
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: 85.98 E-value: 1.69e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 2 ISIKNVN-KWYGDFQ----VLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGtsiadpktnlpklr 76
Cdd:cd03250 1 ISVEDASfTWDSGEQetsfTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG-------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 77 sRVGMVFQhfelFPHL---TITENLtiaqikVLGRSKEE----------ATKKGLQLL---DRV-----GLSahahkhpg 135
Cdd:cd03250 67 -SIAYVSQ----EPWIqngTIRENI------LFGKPFDEeryekvikacALEPDLEILpdgDLTeigekGIN-------- 127
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 516455767 136 qLSGGQQQRVAIARALAMDPIVMLFDEPTSALDPEMVNEVLD-VMVQLAQEGMTMMCVTHEMGFARKvADRVIFMDAGK 213
Cdd:cd03250 128 -LSGGQKQRISLARAVYSDADIYLLDDPLSAVDAHVGRHIFEnCILGLLLNNKTRILVTHQLQLLPH-ADQIVVLDNGR 204
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
16-206 |
2.80e-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: 85.24 E-value: 2.80e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 16 VLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGTSIADPKtnlPKLRSRVGMVFQHFELFPHLTIT 95
Cdd:cd03231 15 LFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQR---DSIARGLLYLGHAPGIKTTLSVL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 96 ENLTIAQikvlgrsKEEATKKGLQLLDRVGLSAHAHKHPGQLSGGQQQRVAIARALAMDPIVMLFDEPTSALDPEMVNEV 175
Cdd:cd03231 92 ENLRFWH-------ADHSDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARF 164
|
170 180 190
....*....|....*....|....*....|..
gi 516455767 176 LDVMVQ-LAQEGMTMMCVTHEMGFARKVADRV 206
Cdd:cd03231 165 AEAMAGhCARGGMVVLTTHQDLGLSEAGAREL 196
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
3-214 |
5.48e-20 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 88.04 E-value: 5.48e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 3 SIKNVNKWYGDFQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGTSIADPKTNlPKLRSRVGMV 82
Cdd:PRK11288 6 SFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTT-AALAAGVAII 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 83 FQHFELFPHLTITENLTIAQIK----VLGRSkeEATKKGLQLLDRVGLSAHAHKHPGQLSGGQQQRVAIARALAMDPIVM 158
Cdd:PRK11288 85 YQELHLVPEMTVAENLYLGQLPhkggIVNRR--LLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARVI 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 516455767 159 LFDEPTSALDPEMVNEVLDVMVQLAQEGMTMMCVTHEMGFARKVADRV-IFMDAGKI 214
Cdd:PRK11288 163 AFDEPTSSLSAREIEQLFRVIRELRAEGRVILYVSHRMEEIFALCDAItVFKDGRYV 219
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-207 |
2.16e-19 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 84.01 E-value: 2.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 1 MISIKNVNKWYGDFQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDgtsiadpktnlPKLrsRVG 80
Cdd:PRK09544 4 LVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRN-----------GKL--RIG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 81 MVFQHFelfpHLTITENLTIAQIKVLgrskEEATKKG--LQLLDRVGlSAHAHKHPGQ-LSGGQQQRVAIARALAMDPIV 157
Cdd:PRK09544 71 YVPQKL----YLDTTLPLTVNRFLRL----RPGTKKEdiLPALKRVQ-AGHLIDAPMQkLSGGETQRVLLARALLNRPQL 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 516455767 158 MLFDEPTSALDPEMVNEVLDVMVQLAQE-GMTMMCVTHEMGFARKVADRVI 207
Cdd:PRK09544 142 LVLDEPTQGVDVNGQVALYDLIDQLRRElDCAVLMVSHDLHLVMAKTDEVL 192
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
3-216 |
2.23e-19 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 83.96 E-value: 2.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 3 SIKNVNKWYGDFQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQ--KGDVIVDGTSIadpkTNL-PKLRSRV 79
Cdd:COG0396 2 EIKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPKYEvtSGSILLDGEDI----LELsPDERARA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 80 G--MVFQHFELFPHLTITENLTIAQIKVLGR--SKEEATKKGLQLLDRVGLSAHAHKHP---GqLSGGQQQRVAIARALA 152
Cdd:COG0396 78 GifLAFQYPVEIPGVSVSNFLRTALNARRGEelSAREFLKLLKEKMKELGLDEDFLDRYvneG-FSGGEKKRNEILQMLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 516455767 153 MDPIVMLFDEPTSALDPEMVNEVLDVMVQLAQEGMTMMCVTHemgFAR----KVADRVIFMDAGKIIE 216
Cdd:COG0396 157 LEPKLAILDETDSGLDIDALRIVAEGVNKLRSPDRGILIITH---YQRildyIKPDFVHVLVDGRIVK 221
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
9-210 |
4.28e-19 |
|
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: 83.23 E-value: 4.28e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 9 KWYGDFQvLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGTSIA-DPKTNLPKLRSRVgmvfqhfE 87
Cdd:cd03237 8 KTLGEFT-LEVEGGSISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSyKPQYIKADYEGTV-------R 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 88 LFPHLTITENLTIAQIKVlgrskEEATKKGL-QLLDRVGLsahahkhpgQLSGGQQQRVAIARALAMDPIVMLFDEPTSA 166
Cdd:cd03237 80 DLLSSITKDFYTHPYFKT-----EIAKPLQIeQILDREVP---------ELSGGELQRVAIAACLSKDADIYLLDEPSAY 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 516455767 167 LDPE---MVNEVLDVMVQLAQEgmTMMCVTHEMGFARKVADRVIFMD 210
Cdd:cd03237 146 LDVEqrlMASKVIRRFAENNEK--TAFVVEHDIIMIDYLADRLIVFE 190
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
16-222 |
1.11e-18 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 84.31 E-value: 1.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 16 VLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGTSIadpkTNL-PKLRSRVGMVF-----QHFELF 89
Cdd:COG3845 273 ALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDI----TGLsPRERRRLGVAYipedrLGRGLV 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 90 PHLTITENLtiaqikVLGRSKEEATKKGLqLLDRVGLSAHAHK--------------HPGQLSGGQQQRVAIARALAMDP 155
Cdd:COG3845 349 PDMSVAENL------ILGRYRRPPFSRGG-FLDRKAIRAFAEElieefdvrtpgpdtPARSLSGGNQQKVILARELSRDP 421
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 516455767 156 IVMLFDEPTSALDPEMVNEVLDVMVQLAQEGMTMMCVTHEMGFARKVADRVIFMDAGKIIEDCPKEE 222
Cdd:COG3845 422 KLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVLLISEDLDEILALSDRIAVMYEGRIVGEVPAAE 488
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1-219 |
2.00e-18 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 83.51 E-value: 2.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 1 MISIKNVNKWYGDFQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDG--TSIADPKTNLpklRSR 78
Cdd:PRK10762 4 LLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGkeVTFNGPKSSQ---EAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 79 VGMVFQHFELFPHLTITENLtiaqikVLGRSK-------------EEATKkglqLLDRVGLSAHAHKHPGQLSGGQQQRV 145
Cdd:PRK10762 81 IGIIHQELNLIPQLTIAENI------FLGREFvnrfgridwkkmyAEADK----LLARLNLRFSSDKLVGELSIGEQQMV 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 516455767 146 AIARALAMDPIVMLFDEPTSALDPEMVNEVLDVMVQLAQEGMTMMCVTHEMGFARKVADRVIFMDAGKIIEDCP 219
Cdd:PRK10762 151 EIAKVLSFESKVIIMDEPTDALTDTETESLFRVIRELKSQGRGIVYISHRLKEIFEICDDVTVFRDGQFIAERE 224
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
2-216 |
2.86e-18 |
|
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: 80.15 E-value: 2.86e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 2 ISIKNVNKWYGDF--QVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCV-NALEPfQKGDVIVDGTSIAdpKTNLPKLRSR 78
Cdd:cd03369 7 IEVENLSVRYAPDlpPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALfRFLEA-EEGKIEIDGIDIS--TIPLEDLRSS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 79 VGMVFQHFELFPHlTITENLTIaqikvLGRSKEEATKKGLQLLDRvGLSahahkhpgqLSGGQQQRVAIARALAMDPIVM 158
Cdd:cd03369 84 LTIIPQDPTLFSG-TIRSNLDP-----FDEYSDEEIYGALRVSEG-GLN---------LSQGQRQLLCLARALLKRPRVL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 159 LFDEPTSALDPEMVNEVLDVMVQLAQeGMTMMCVTHEMgfaRKVA--DRVIFMDAGKIIE 216
Cdd:cd03369 148 VLDEATASIDYATDALIQKTIREEFT-NSTILTIAHRL---RTIIdyDKILVMDAGEVKE 203
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
23-217 |
4.20e-18 |
|
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: 82.92 E-value: 4.20e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 23 EVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGTSIADpkTNLPKLRSRVGMVFQHFELFPHLtitenltiaq 102
Cdd:COG4615 354 TIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTA--DNREAYRQLFSAVFSDFHLFDRL---------- 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 103 ikvLGRSKEEATKKGLQLLDRVGLsahAHK--------HPGQLSGGQQQRVAIARALAMD-PIvMLFDEPTSALDPE--- 170
Cdd:COG4615 422 ---LGLDGEADPARARELLERLEL---DHKvsvedgrfSTTDLSQGQRKRLALLVALLEDrPI-LVFDEWAADQDPEfrr 494
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 516455767 171 -MVNEVLdvmVQLAQEGMTMMCVTH-EMGFArkVADRVIFMDAGKIIED 217
Cdd:COG4615 495 vFYTELL---PELKARGKTVIAISHdDRYFD--LADRVLKMDYGKLVEL 538
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
19-222 |
6.43e-18 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 82.28 E-value: 6.43e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 19 DCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQK-GDVIVDGT---------SIADPKTNLPKLRSRVGMVfqhfel 88
Cdd:PRK13549 280 DVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPGRWeGEIFIDGKpvkirnpqqAIAQGIAMVPEDRKRDGIV------ 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 89 fPHLTITENLTIAQIK------VLGRSKEEATKkgLQLLDRVGL-SAHAHKHPGQLSGGQQQRVAIARALAMDPIVMLFD 161
Cdd:PRK13549 354 -PVMGVGKNITLAALDrftggsRIDDAAELKTI--LESIQRLKVkTASPELAIARLSGGNQQKAVLAKCLLLNPKILILD 430
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 516455767 162 EPTSALDPEMVNEVLDVMVQLAQEGMTMMCVTHEMGFARKVADRVIFMDAGKIIEDCPKEE 222
Cdd:PRK13549 431 EPTRGIDVGAKYEIYKLINQLVQQGVAIIVISSELPEVLGLSDRVLVMHEGKLKGDLINHN 491
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
14-216 |
8.45e-18 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 79.23 E-value: 8.45e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 14 FQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDgtsiadpktnlpklrsrvgmvfqhfelFPHLT 93
Cdd:COG2401 43 RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVD---------------------------VPDNQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 94 ITENLTIaqIKVLGRSKEeaTKKGLQLLDRVGLSAHA--HKHPGQLSGGQQQRVAIARALAMDPIVMLFDEPTSALDPEM 171
Cdd:COG2401 96 FGREASL--IDAIGRKGD--FKDAVELLNAVGLSDAVlwLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQT 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 516455767 172 VNEVLDVMVQLAQE-GMTMMCVTHEMGFARKVA-DRVIFMDAGKIIE 216
Cdd:COG2401 172 AKRVARNLQKLARRaGITLVVATHHYDVIDDLQpDLLIFVGYGGVPE 218
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
21-223 |
9.54e-18 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 81.50 E-value: 9.54e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 21 STEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGTSIadpKTNLPKLRSRVGMVF----QHFE-LFPHLTIT 95
Cdd:PRK11288 273 SFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPI---DIRSPRDAIRAGIMLcpedRKAEgIIPVHSVA 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 96 ENLTIAQIK-------VLGRSKEEAT-KKGLQLLdRVGlSAHAHKHPGQLSGGQQQRVAIARALAMDPIVMLFDEPTSAL 167
Cdd:PRK11288 350 DNINISARRhhlragcLINNRWEAENaDRFIRSL-NIK-TPSREQLIMNLSGGNQQKAILGRWLSEDMKVILLDEPTRGI 427
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 168 DPEMVNEVLDVMVQLAQEGMTMMCVTHE----MGfarkVADRVIFMDAGKIIEDCPKEEF 223
Cdd:PRK11288 428 DVGAKHEIYNVIYELAAQGVAVLFVSSDlpevLG----VADRIVVMREGRIAGELAREQA 483
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
18-199 |
1.71e-17 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 77.92 E-value: 1.71e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 18 TDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGTSIAdpktnlpklrsRVGMVFQHFELF-------- 89
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIR-----------RQRDEYHQDLLYlghqpgik 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 90 PHLTITENLTIAQiKVLGRSKEEATkkgLQLLDRVGLSAHAHKHPGQLSGGQQQRVAIARALAMDPIVMLFDEPTSALDP 169
Cdd:PRK13538 87 TELTALENLRFYQ-RLHGPGDDEAL---WEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDK 162
|
170 180 190
....*....|....*....|....*....|.
gi 516455767 170 EMVNEVLDVMVQ-LAQEGMTMMCVTHEMGFA 199
Cdd:PRK13538 163 QGVARLEALLAQhAEQGGMVILTTHQDLPVA 193
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
2-233 |
3.39e-17 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 80.02 E-value: 3.39e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 2 ISIKNVNKWYGD--FQV----LTdcsteVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGTSIADpkTNLPKL 75
Cdd:PRK10522 323 LELRNVTFAYQDngFSVgpinLT-----IKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTA--EQPEDY 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 76 RSRVGMVFQHFELFPHLtitenltiaqikvLGRSKEEATKKGLQL-LDRVGLsAHAHKHPG------QLSGGQQQRVAIA 148
Cdd:PRK10522 396 RKLFSAVFTDFHLFDQL-------------LGPEGKPANPALVEKwLERLKM-AHKLELEDgrisnlKLSKGQKKRLALL 461
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 149 RALAMDPIVMLFDEPTSALDPEMVNEVLDVMVQLAQE-GMTMMCVTHEMGFARKvADRVIFMDAGKIIedcpkeEFFGDI 227
Cdd:PRK10522 462 LALAEERDILLLDEWAADQDPHFRREFYQVLLPLLQEmGKTIFAISHDDHYFIH-ADRLLEMRNGQLS------ELTGEE 534
|
....*.
gi 516455767 228 SARSER 233
Cdd:PRK10522 535 RDAASR 540
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
19-222 |
7.96e-17 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 78.89 E-value: 7.96e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 19 DCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGTSIadpKTNLPKLRSRVGMVFqhfelfphltITEN- 97
Cdd:PRK10762 270 DVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEV---VTRSPQDGLANGIVY----------ISEDr 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 98 ----LtiaqikVLGRS-KEEATKKGLQLLDRVGLSAHAH---------------KHP------GQLSGGQQQRVAIARAL 151
Cdd:PRK10762 337 krdgL------VLGMSvKENMSLTALRYFSRAGGSLKHAdeqqavsdfirlfniKTPsmeqaiGLLSGGNQQKVAIARGL 410
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 516455767 152 AMDPIVMLFDEPTSALDPEMVNEVLDVMVQLAQEGMTMMCVTHEMGFARKVADRVIFMDAGKIIEDCPKEE 222
Cdd:PRK10762 411 MTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAEGLSIILVSSEMPEVLGMSDRILVMHEGRISGEFTREQ 481
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
21-215 |
8.99e-17 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 76.90 E-value: 8.99e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 21 STEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFqKGDVIVDGTSIAD-PKTNLPKLRSRV--------GM-VFQHFELF- 89
Cdd:PRK03695 16 SAEVRAGEILHLVGPNGAGKSTLLARMAGLLPG-SGSIQFAGQPLEAwSAAELARHRAYLsqqqtppfAMpVFQYLTLHq 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 90 PHLTITEnltiAQIKVLGRskeeatkkglqLLDRVGLSAHAHKHPGQLSGGQQQRVAIARA-LAMDPIV------MLFDE 162
Cdd:PRK03695 95 PDKTRTE----AVASALNE-----------VAEALGLDDKLGRSVNQLSGGEWQRVRLAAVvLQVWPDInpagqlLLLDE 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 516455767 163 PTSALDPEMVNeVLD-VMVQLAQEGMTMMCVTHEMGFARKVADRVIFMDAGKII 215
Cdd:PRK03695 160 PMNSLDVAQQA-ALDrLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLL 212
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
2-239 |
9.03e-17 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 79.25 E-value: 9.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 2 ISIKNVN-KWYGDFQ--VLTDCSTEVKKGEVIVVCGPSGSGKSTLIKC-VNALEPFQKGDVIVDGTSIADPKtnlpklrs 77
Cdd:PLN03232 615 ISIKNGYfSWDSKTSkpTLSDINLEIPVGSLVAIVGGTGEGKTSLISAmLGELSHAETSSVVIRGSVAYVPQ-------- 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 78 rVGMVFqhfelfpHLTITENltiaqikVLGRSKEEATKKGlQLLDRVGLSAHAHKHPGQ-----------LSGGQQQRVA 146
Cdd:PLN03232 687 -VSWIF-------NATVREN-------ILFGSDFESERYW-RAIDVTALQHDLDLLPGRdlteigergvnISGGQKQRVS 750
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 147 IARALAMDPIVMLFDEPTSALDPEMVNEVLDVMVQLAQEGMTMMCVTHEMGFARKVaDRVIFMDAGKIIEdcpkEEFFGD 226
Cdd:PLN03232 751 MARAVYSNSDIYIFDDPLSALDAHVAHQVFDSCMKDELKGKTRVLVTNQLHFLPLM-DRIILVSEGMIKE----EGTFAE 825
|
250
....*....|...
gi 516455767 227 ISARSERAQHFLE 239
Cdd:PLN03232 826 LSKSGSLFKKLME 838
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
11-221 |
1.30e-16 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 78.63 E-value: 1.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 11 YGDFQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDV-----IVDGTSIAdpktnlpkLRSRVGMVFQH 85
Cdd:NF033858 276 FGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAwlfgqPVDAGDIA--------TRRRVGYMSQA 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 86 FELFPHLTITENLTI-AQIKVLgrSKEEATKKGLQLLDRVGLSAHAHKHPGQLSGGQQQRVAIARALAMDPIVMLFDEPT 164
Cdd:NF033858 348 FSLYGELTVRQNLELhARLFHL--PAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPT 425
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 516455767 165 SALDPEMVNEVLDVMVQLA-QEGMTMMCVTHEMGFARKvADRVIFMDAGKIIE-DCPKE 221
Cdd:NF033858 426 SGVDPVARDMFWRLLIELSrEDGVTIFISTHFMNEAER-CDRISLMHAGRVLAsDTPAA 483
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-232 |
2.10e-16 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 76.66 E-value: 2.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 1 MISIKNVNKwygDFQV------------------------LTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNA-LEPfQK 55
Cdd:COG4586 1 IIEVENLSK---TYRVyekepglkgalkglfrreyreveaVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGiLVP-TS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 56 GDVIVDGTsiaDPKTNLPKLRSRVGMVF-QHFELFPHLTITENLTIAQiKVLGRSKEEATKKGLQLLDRVGLSAHAHKHP 134
Cdd:COG4586 77 GEVRVLGY---VPFKRRKEFARRIGVVFgQRSQLWWDLPAIDSFRLLK-AIYRIPDAEYKKRLDELVELLDLGELLDTPV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 135 GQLSGGQQQRVAIARALAMDPIVMLFDEPTSALDPEMVNEVLDVMVQLAQE-GMTMMCVTHEMGFARKVADRVIFMDAGK 213
Cdd:COG4586 153 RQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRErGTTILLTSHDMDDIEALCDRVIVIDHGR 232
|
250
....*....|....*....
gi 516455767 214 IIEDCPKEEFFGDISARSE 232
Cdd:COG4586 233 IIYDGSLEELKERFGPYKT 251
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
104-231 |
3.46e-16 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 76.70 E-value: 3.46e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 104 KVLGRSKEEATKKGLQLLDRVGLSAHAHKHPGQLSGGQQQRVAIARALAMDPIVMLFDEPTSALDPEMVNEVLDVMVQLA 183
Cdd:NF000106 112 R*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMV 191
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 516455767 184 QEGMTMMCVTHEMGFARKVADRVIFMDAGKIIEDCPKEEFFGDISARS 231
Cdd:NF000106 192 RDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDELKTKVGGRT 239
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
24-212 |
1.18e-15 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 76.21 E-value: 1.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 24 VKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGTSIAdpkTNLPKLRSRVGMVFQHFELFPHLTITENLTIAQi 103
Cdd:TIGR01257 1962 VRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSIL---TNISDVHQNMGYCPQFDAIDDLLTGREHLYLYA- 2037
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 104 KVLGRSKEEATKKGLQLLDRVGLSAHAHKHPGQLSGGQQQRVAIARALAMDPIVMLFDEPTSALDPEMVNEVLDVMVQLA 183
Cdd:TIGR01257 2038 RLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSII 2117
|
170 180
....*....|....*....|....*....
gi 516455767 184 QEGMTMMCVTHEMGFARKVADRVIFMDAG 212
Cdd:TIGR01257 2118 REGRAVVLTSHSMEECEALCTRLAIMVKG 2146
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
21-222 |
1.19e-15 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 74.84 E-value: 1.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 21 STEVKKGEVIVVCGPSGSGKSTLIKCVNALepfQKGDVIVDGTSIADPKTNLPKLRSR---------VGMVFQHFE--LF 89
Cdd:PRK15093 27 SMTLTEGEIRGLVGESGSGKSLIAKAICGV---TKDNWRVTADRMRFDDIDLLRLSPRerrklvghnVSMIFQEPQscLD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 90 PHLTITENL--TIAQIKVLGRSKEE---ATKKGLQLLDRVGLSAHA---HKHPGQLSGGQQQRVAIARALAMDPIVMLFD 161
Cdd:PRK15093 104 PSERVGRQLmqNIPGWTYKGRWWQRfgwRKRRAIELLHRVGIKDHKdamRSFPYELTEGECQKVMIAIALANQPRLLIAD 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 516455767 162 EPTSALDPEMVNEVLDVMVQLAQ-EGMTMMCVTHEMGFARKVADRVIFMDAGKIIEDCPKEE 222
Cdd:PRK15093 184 EPTNAMEPTTQAQIFRLLTRLNQnNNTTILLISHDLQMLSQWADKINVLYCGQTVETAPSKE 245
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
16-219 |
1.83e-15 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 73.71 E-value: 1.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 16 VLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQ--------KGDVIVDGTSIAD-PKTNLPKLR------SRVG 80
Cdd:PRK13547 16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGgaprgarvTGDVTLNGEPLAAiDAPRLARLRavlpqaAQPA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 81 MVFQHFEL-----FPHLTITENLTIAQIKVLGRSkeeatkkglqlLDRVGLSAHAHKHPGQLSGGQQQRVAIARALAM-- 153
Cdd:PRK13547 96 FAFSAREIvllgrYPHARRAGALTHRDGEIAWQA-----------LALAGATALVGRDVTTLSGGELARVQFARVLAQlw 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 516455767 154 -------DPIVMLFDEPTSALDPEMVNEVLDVMVQLAQE-GMTMMCVTHEMGFARKVADRVIFMDAGKIIEDCP 219
Cdd:PRK13547 165 pphdaaqPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDwNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGA 238
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
14-225 |
2.33e-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: 71.91 E-value: 2.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 14 FQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCV-NALEPFQK--GDVIVDGTsiaDPKTNLPKLRSRVGMVFQHFELFP 90
Cdd:cd03233 20 IPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALaNRTEGNVSveGDIHYNGI---PYKEFAEKYPGEIIYVSEEDVHFP 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 91 HLTITENLTIAqikvlgrskeeatkkglqlldrvgLSAHAHKHPGQLSGGQQQRVAIARALAMDPIVMLFDEPTSALDPE 170
Cdd:cd03233 97 TLTVRETLDFA------------------------LRCKGNEFVRGISGGERKRVSIAEALVSRASVLCWDNSTRGLDSS 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 516455767 171 MVNEVLDVMVQLAQE-GMT-MMCVTHEMGFARKVADRVIFMDAGKIIedcpkeeFFG 225
Cdd:cd03233 153 TALEILKCIRTMADVlKTTtFVSLYQASDEIYDLFDKVLVLYEGRQI-------YYG 202
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
4-241 |
2.81e-15 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 74.38 E-value: 2.81e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 4 IKNVNKWYGDFQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGTSIaDPKTNLPKLRSRVGMVF 83
Cdd:PRK10982 1 MSNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEI-DFKSSKEALENGISMVH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 84 QHFELFPHLTITENLTIAQIKVLGRSKEEA-----TKKglqLLDRVGLSAHAHKHPGQLSGGQQQRVAIARALAMDPIVM 158
Cdd:PRK10982 80 QELNLVLQRSVMDNMWLGRYPTKGMFVDQDkmyrdTKA---IFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 159 LFDEPTSALDPEMVNEVLDVMVQLAQEGMTMMCVTHEMGFARKVADRVIFMDAGKIIEDCPKEEFFGD--ISARSERA-- 234
Cdd:PRK10982 157 IMDEPTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQWIATQPLAGLTMDkiIAMMVGRSlt 236
|
....*..
gi 516455767 235 QHFLEKI 241
Cdd:PRK10982 237 QRFPDKE 243
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
2-240 |
4.54e-15 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 74.39 E-value: 4.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 2 ISIKNVN-KW--YGDFQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCV-NALEPFQKGDVIVDGTsiadpktnlpklrs 77
Cdd:PLN03130 615 ISIKNGYfSWdsKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMlGELPPRSDASVVIRGT-------------- 680
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 78 rVGMVFQHFELFpHLTITENltiaqikVLGRSKEEATK-------KGLQLlDRVGLSAHAHKHPGQ----LSGGQQQRVA 146
Cdd:PLN03130 681 -VAYVPQVSWIF-NATVRDN-------ILFGSPFDPERyeraidvTALQH-DLDLLPGGDLTEIGErgvnISGGQKQRVS 750
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 147 IARALAMDPIVMLFDEPTSALDPEMVNEVLDVMVQLAQEGMTMMCVTHEMGFARKVaDRVIFMDAGKIIEdcpkEEFFGD 226
Cdd:PLN03130 751 MARAVYSNSDVYIFDDPLSALDAHVGRQVFDKCIKDELRGKTRVLVTNQLHFLSQV-DRIILVHEGMIKE----EGTYEE 825
|
250
....*....|....
gi 516455767 227 ISARSERAQHFLEK 240
Cdd:PLN03130 826 LSNNGPLFQKLMEN 839
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
16-210 |
5.91e-15 |
|
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: 70.26 E-value: 5.91e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 16 VLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIvdgtsiadpktnLPkLRSRVGMVFQHfelfPHLTit 95
Cdd:cd03223 16 LLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIG------------MP-EGEDLLFLPQR----PYLP-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 96 enltiaqikvLGRSKEeatkkglQLL---DRVglsahahkhpgqLSGGQQQRVAIARALAMDPIVMLFDEPTSALDPEMV 172
Cdd:cd03223 77 ----------LGTLRE-------QLIypwDDV------------LSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESE 127
|
170 180 190
....*....|....*....|....*....|....*...
gi 516455767 173 NEVLDVmvqLAQEGMTMMCVTHEMGFaRKVADRVIFMD 210
Cdd:cd03223 128 DRLYQL---LKELGITVISVGHRPSL-WKFHDRVLDLD 161
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
16-216 |
6.38e-15 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 73.59 E-value: 6.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 16 VLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGTSIadPKTNLPKLRSRVGMVFQHFELFPHltit 95
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPL--TKLQLDSWRSRLAVVSQTPFLFSD---- 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 96 enlTIAQIKVLGRSkeEATKkglQLLDRVGLSAHAH----KHP-------GQ----LSGGQQQRVAIARALAMDPIVMLF 160
Cdd:PRK10789 404 ---TVANNIALGRP--DATQ---QEIEHVARLASVHddilRLPqgydtevGErgvmLSGGQKQRISIARALLLNAEILIL 475
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 516455767 161 DEPTSALDPEMVNEVLDVMVQLAQeGMTMMCVTHEMGfARKVADRVIFMDAGKIIE 216
Cdd:PRK10789 476 DDALSAVDGRTEHQILHNLRQWGE-GRTVIISAHRLS-ALTEASEILVMQHGHIAQ 529
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
2-198 |
1.32e-14 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 72.35 E-value: 1.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 2 ISIKNVNKWYGDFQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCV---------NALEPF--QKGDvivdGTSIADPKT 70
Cdd:PRK10938 261 IVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLItgdhpqgysNDLTLFgrRRGS----GETIWDIKK 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 71 NLPKLRSRVgmvfqhfelfpHL-----TITENLTIA----QIKVLGRSKEEATKKGLQLLDRVGLSAHAHKHPGQ-LSGG 140
Cdd:PRK10938 337 HIGYVSSSL-----------HLdyrvsTSVRNVILSgffdSIGIYQAVSDRQQKLAQQWLDILGIDKRTADAPFHsLSWG 405
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 516455767 141 QQQRVAIARALAMDPIVMLFDEPTSALDP---EMVNEVLDVMVqlaQEGMTMM------------CVTHEMGF 198
Cdd:PRK10938 406 QQRLALIVRALVKHPTLLILDEPLQGLDPlnrQLVRRFVDVLI---SEGETQLlfvshhaedapaCITHRLEF 475
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
14-240 |
1.40e-14 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 72.83 E-value: 1.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 14 FQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNA-LEPFQKGD---VIVDGTSIADPKtnlPKLRSRVGMVFQHFELF 89
Cdd:TIGR00956 74 FDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASnTDGFHIGVegvITYDGITPEEIK---KHYRGDVVYNAETDVHF 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 90 PHLTITENLTIA------QIKVLGRSKEEATKKGLQLLDRV-GLSAHAHKHPGQ-----LSGGQQQRVAIARALAMDPIV 157
Cdd:TIGR00956 151 PHLTVGETLDFAarcktpQNRPDGVSREEYAKHIADVYMATyGLSHTRNTKVGNdfvrgVSGGERKRVSIAEASLGGAKI 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 158 MLFDEPTSALDP-----------EMVNE----VLDVMVQLAQEgmtmmcvthemgfARKVADRVIFMDAGKIIedcpkee 222
Cdd:TIGR00956 231 QCWDNATRGLDSatalefiralkTSANIldttPLVAIYQCSQD-------------AYELFDKVIVLYEGYQI------- 290
|
250
....*....|....*...
gi 516455767 223 FFGDISarseRAQHFLEK 240
Cdd:TIGR00956 291 YFGPAD----KAKQYFEK 304
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
19-214 |
3.51e-14 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 71.24 E-value: 3.51e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 19 DCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGTSIADPKTnlpKLRSRVGMVF-----QHFELFPHLT 93
Cdd:PRK15439 281 NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALST---AQRLARGLVYlpedrQSSGLYLDAP 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 94 ITEN---LTIAQIKVLGRSKEEATkkglqLLDR----VGLS-AHAHKHPGQLSGGQQQRVAIARALAMDPIVMLFDEPTS 165
Cdd:PRK15439 358 LAWNvcaLTHNRRGFWIKPARENA-----VLERyrraLNIKfNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTR 432
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 516455767 166 ALDPEMVNEVLDVMVQLAQEGMTMMCVTHEMGFARKVADRVIFMDAGKI 214
Cdd:PRK15439 433 GVDVSARNDIYQLIRSIAAQNVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
2-212 |
3.66e-14 |
|
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: 68.42 E-value: 3.66e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 2 ISIKNVNkwY------GDFQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNAlepfQKGDVIVDGTSIADPKTNLPKL 75
Cdd:cd03232 4 LTWKNLN--YtvpvkgGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAG----RKTAGVITGEILINGRPLDKNF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 76 RSRVGMVFQHFELFPHLTITENLTIAqikvlgrskeeATKKGLQLLDRvglsahahkhpgqlsggqqQRVAIARALAMDP 155
Cdd:cd03232 78 QRSTGYVEQQDVHSPNLTVREALRFS-----------ALLRGLSVEQR-------------------KRLTIGVELAAKP 127
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 156 IVMLFDEPTSALDPEMVNEVLDVMVQLAQEGMTMMCVTHEMG---FARkvADRVIFMDAG 212
Cdd:cd03232 128 SILFLDEPTSGLDSQAAYNIVRFLKKLADSGQAILCTIHQPSasiFEK--FDRLLLLKRG 185
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1-215 |
7.80e-14 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 70.36 E-value: 7.80e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 1 MISIKNVNKWYGDFQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGTSIA-----DPktnlPkl 75
Cdd:PRK11147 3 LISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLIVarlqqDP----P-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 76 RSRVGMVF-----------QHFELFPHLT--ITENLTIAQIKVLGRSKEEATKKGL-QLLDRVG-----LSAHAHKHPGQ 136
Cdd:PRK11147 77 RNVEGTVYdfvaegieeqaEYLKRYHDIShlVETDPSEKNLNELAKLQEQLDHHNLwQLENRINevlaqLGLDPDAALSS 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 516455767 137 LSGGQQQRVAIARALAMDPIVMLFDEPTSALDPEMVnEVLDVMVqLAQEGmTMMCVTHEMGFARKVADRVIFMDAGKII 215
Cdd:PRK11147 157 LSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETI-EWLEGFL-KTFQG-SIIFISHDRSFIRNMATRIVDLDRGKLV 232
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
24-224 |
1.03e-13 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 69.16 E-value: 1.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 24 VKKGEVIVVCGPSGSGKSTLIKC-VNALEPfqKGDVIVDGTSIADpkTNLPKLRSR---------VGMVFQHFE--LFPH 91
Cdd:COG4170 30 LNEGEIRGLVGESGSGKSLIAKAiCGITKD--NWHVTADRFRWNG--IDLLKLSPRerrkiigreIAMIFQEPSscLDPS 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 92 LTITENL--TIAQIKVLG---RSKEEATKKGLQLLDRVGLSAHAH---KHPGQLSGGQQQRVAIARALAMDPIVMLFDEP 163
Cdd:COG4170 106 AKIGDQLieAIPSWTFKGkwwQRFKWRKKRAIELLHRVGIKDHKDimnSYPHELTEGECQKVMIAMAIANQPRLLIADEP 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 516455767 164 TSALDPEMVNEVLDVMVQLAQ-EGMTMMCVTHEMGFARKVADRVIFMDAGKIIEDCPKEEFF 224
Cdd:COG4170 186 TNAMESTTQAQIFRLLARLNQlQGTSILLISHDLESISQWADTITVLYCGQTVESGPTEQIL 247
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1-216 |
1.24e-13 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 68.13 E-value: 1.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 1 MISIKNVNKWYGDFQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQ--KGDVIVDGTSIADPKtnlPKLRSR 78
Cdd:CHL00131 7 ILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPAYKilEGDILFKGESILDLE---PEERAH 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 79 VG--MVFQHFELFPHLTITENLTIA---QIKVLGRSKEEA-------TKKglqlLDRVGLSAH-AHKHPGQ-LSGGQQQR 144
Cdd:CHL00131 84 LGifLAFQYPIEIPGVSNADFLRLAynsKRKFQGLPELDPlefleiiNEK----LKLVGMDPSfLSRNVNEgFSGGEKKR 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 516455767 145 VAIARALAMDPIVMLFDEPTSALDPEMVNEVLDVMVQLAQEGMTMMCVTHemgFARK----VADRVIFMDAGKIIE 216
Cdd:CHL00131 160 NEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIILITH---YQRLldyiKPDYVHVMQNGKIIK 232
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
2-215 |
1.56e-13 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 69.38 E-value: 1.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 2 ISIKNVNKWYGDFQVLTDCSTEVKKGEVIVVCGPSGSGKSTL---IKCVNALepfQKGDVIVDGTSIADPKtnlpkLRSR 78
Cdd:NF033858 2 ARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLlslIAGARKI---QQGRVEVLGGDMADAR-----HRRA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 79 VG-----MVfQHF--ELFPHLTITENLtiaQI--KVLGRSKEEATKKGLQLLDRVGLSAHAHKHPGQLSGGQQQRVAIAR 149
Cdd:NF033858 74 VCpriayMP-QGLgkNLYPTLSVFENL---DFfgRLFGQDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCC 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 516455767 150 ALAMDPIVMLFDEPTSALDP-------EMVNEvldvmVQLAQEGMTMMCVTHEMGFARKVaDRVIFMDAGKII 215
Cdd:NF033858 150 ALIHDPDLLILDEPTTGVDPlsrrqfwELIDR-----IRAERPGMSVLVATAYMEEAERF-DWLVAMDAGRVL 216
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
16-221 |
2.43e-13 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 69.20 E-value: 2.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 16 VLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGTSIAdpKTNLPKLRSRVGMVFQHFELFPHlTIT 95
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIA--KIGLHDLRFKITIIPQDPVLFSG-SLR 1377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 96 ENLtiaqiKVLGRSKEEATKKGLQLLDRVGLSA-------HAHKHPGQ-LSGGQQQRVAIARALAMDPIVMLFDEPTSAL 167
Cdd:TIGR00957 1378 MNL-----DPFSQYSDEEVWWALELAHLKTFVSalpdkldHECAEGGEnLSVGQRQLVCLARALLRKTKILVLDEATAAV 1452
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 516455767 168 DPEMVNeVLDVMVQLAQEGMTMMCVTHEMgfaRKVAD--RVIFMDAGKIIE-DCPKE 221
Cdd:TIGR00957 1453 DLETDN-LIQSTIRTQFEDCTVLTIAHRL---NTIMDytRVIVLDKGEVAEfGAPSN 1505
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
17-214 |
2.56e-13 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 68.60 E-value: 2.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 17 LTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGTSIADpKTNLPKLRSRVGMVFQHFE---LFPHLT 93
Cdd:PRK10982 264 IRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINN-HNANEAINHGFALVTEERRstgIYAYLD 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 94 ITENLTIAQIKV----LGRSKEEATKKGLQ-LLDRVGLSAHAHK-HPGQLSGGQQQRVAIARALAMDPIVMLFDEPTSAL 167
Cdd:PRK10982 343 IGFNSLISNIRNyknkVGLLDNSRMKSDTQwVIDSMRVKTPGHRtQIGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGI 422
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 516455767 168 DPEMVNEVLDVMVQLAQEGMTMMCVTHEMGFARKVADRVIFMDAGKI 214
Cdd:PRK10982 423 DVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNGLV 469
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
2-224 |
2.67e-13 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 69.20 E-value: 2.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 2 ISIKNVN-KW-YGDFQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGTSIADPKTNLPK---LR 76
Cdd:TIGR00957 637 ITVHNATfTWaRDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSVAYVPQQAWIQndsLR 716
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 77 SRVGMVFQHFELFPHLTITENLTIAQIKVL-GRSKEEATKKGLQLldrvglsahahkhpgqlSGGQQQRVAIARALAMDP 155
Cdd:TIGR00957 717 ENILFGKALNEKYYQQVLEACALLPDLEILpSGDRTEIGEKGVNL-----------------SGGQKQRVSLARAVYSNA 779
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 516455767 156 IVMLFDEPTSALDPEMVNEVLDVMVqlAQEGM----TMMCVTHEMGFARKVaDRVIFMDAGKIIEDCPKEEFF 224
Cdd:TIGR00957 780 DIYLFDDPLSAVDAHVGKHIFEHVI--GPEGVlknkTRILVTHGISYLPQV-DVIIVMSGGKISEMGSYQELL 849
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
17-212 |
3.74e-13 |
|
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: 66.51 E-value: 3.74e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 17 LTDCSTEVKKGEVIVVCGPSGSGKSTLI----------KCVNALEPF--------QKGDV-IVDGTSIA---DPKTNLPK 74
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSSLAfdtiyaegqrRYVESLSAYarqflgqmDKPDVdSIEGLSPAiaiDQKTTSRN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 75 LRSRVGmvfqhfelfphlTITE-----NLTIAQIKVLGRskeeatkkgLQLLDRVGL-------SAhahkhpGQLSGGQQ 142
Cdd:cd03270 91 PRSTVG------------TVTEiydylRLLFARVGIRER---------LGFLVDVGLgyltlsrSA------PTLSGGEA 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 516455767 143 QRVAIARALAM--DPIVMLFDEPTSALDPEMVNEVLDVMVQLAQEGMTMMCVTHEMGFARkVADRVIFMDAG 212
Cdd:cd03270 144 QRIRLATQIGSglTGVLYVLDEPSIGLHPRDNDRLIETLKRLRDLGNTVLVVEHDEDTIR-AADHVIDIGPG 214
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
1-207 |
1.05e-12 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 67.14 E-value: 1.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 1 MISIKNVNKWYGDFQvLTDCSTEVKKGEVIVVCGPSGSGKSTLIKC-VNALEPfQKGDVIVDGTSIADPktnlpklrsrv 79
Cdd:PRK13409 340 LVEYPDLTKKLGDFS-LEVEGGEIYEGEVIGIVGPNGIGKTTFAKLlAGVLKP-DEGEVDPELKISYKP----------- 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 80 gmvfQHFELFPHLTITENLtiAQIKV-LGRS--KEEATKKgLQL---LDR-VGlsahahkhpgQLSGGQQQRVAIARALA 152
Cdd:PRK13409 407 ----QYIKPDYDGTVEDLL--RSITDdLGSSyyKSEIIKP-LQLerlLDKnVK----------DLSGGELQRVAIAACLS 469
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 516455767 153 MDPIVMLFDEPTSALDPEMVNEVLDVMVQLAQE-GMTMMCVTHEMGFARKVADRVI 207
Cdd:PRK13409 470 RDADLYLLDEPSAHLDVEQRLAVAKAIRRIAEErEATALVVDHDIYMIDYISDRLM 525
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
2-168 |
2.72e-12 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 65.89 E-value: 2.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 2 ISIKNVNKWYGDFQ-VLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGTSIADPKTNLpkLRSRVG 80
Cdd:PRK10790 341 IDIDNVSFAYRDDNlVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSV--LRQGVA 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 81 MVFQHfelfPHL---TITENLTiaqikvLGRS-KEEATKKGL---QLLDRV-GLSAHAHKHPGQ----LSGGQQQRVAIA 148
Cdd:PRK10790 419 MVQQD----PVVladTFLANVT------LGRDiSEEQVWQALetvQLAELArSLPDGLYTPLGEqgnnLSVGQKQLLALA 488
|
170 180
....*....|....*....|
gi 516455767 149 RALAMDPIVMLFDEPTSALD 168
Cdd:PRK10790 489 RVLVQTPQILILDEATANID 508
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
2-168 |
3.63e-12 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 65.82 E-value: 3.63e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 2 ISIKNVNKWYG---DFQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIV-DGTSIADpkTNLPKLRS 77
Cdd:PTZ00265 383 IQFKNVRFHYDtrkDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKD--INLKWWRS 460
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 78 RVGMVFQHFELFPHlTITENL-----TIAQIKVLGRSKEEAT------------------------------------KK 116
Cdd:PTZ00265 461 KIGVVSQDPLLFSN-SIKNNIkyslySLKDLEALSNYYNEDGndsqenknkrnscrakcagdlndmsnttdsneliemRK 539
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 516455767 117 GLQLLDR---VGLSAHAHKH-----------------PGQLSGGQQQRVAIARALAMDPIVMLFDEPTSALD 168
Cdd:PTZ00265 540 NYQTIKDsevVDVSKKVLIHdfvsalpdkyetlvgsnASKLSGGQKQRISIARAIIRNPKILILDEATSSLD 611
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
24-196 |
4.54e-12 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 65.21 E-value: 4.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 24 VKKGEVIVVCGPSGSGKSTLIKcvnalepfqkgdvIVDGTSIadPktNLPKLRSRVGM--VFQHF---ELFPHLtitENL 98
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVK-------------ILSGELI--P--NLGDYEEEPSWdeVLKRFrgtELQNYF---KKL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 99 TIAQIKVL--------------GRSKEEATK-----KGLQLLDRVGLSAHAHKHPGQLSGGQQQRVAIARALAMDPIVML 159
Cdd:PRK13409 156 YNGEIKVVhkpqyvdlipkvfkGKVRELLKKvdergKLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYF 235
|
170 180 190
....*....|....*....|....*....|....*....
gi 516455767 160 FDEPTSALDpemVNEVLDV--MVQLAQEGMTMMCVTHEM 196
Cdd:PRK13409 236 FDEPTSYLD---IRQRLNVarLIRELAEGKYVLVVEHDL 271
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
16-216 |
5.24e-12 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 63.77 E-value: 5.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 16 VLTDCSTEVKKGEVIVVCGPSGSGKSTL-IKCVNALEPFQkGDVIVDGTSIAdpKTNLPKLRSRVGMVFQ---------H 85
Cdd:cd03288 36 VLKHVKAYIKPGQKVGICGRTGSGKSSLsLAFFRMVDIFD-GKIVIDGIDIS--KLPLHTLRSRLSIILQdpilfsgsiR 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 86 FELFPHLTIT-----ENLTIAQIKVLGRSKEEatkkglqlldrvGLSAHAHKHPGQLSGGQQQRVAIARALAMDPIVMLF 160
Cdd:cd03288 113 FNLDPECKCTddrlwEALEIAQLKNMVKSLPG------------GLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIM 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 516455767 161 DEPTSALDpeMVNE-VLDVMVQLAQEGMTMMCVTHEMGFARKvADRVIFMDAGKIIE 216
Cdd:cd03288 181 DEATASID--MATEnILQKVVMTAFADRTVVTIAHRVSTILD-ADLVLVLSRGILVE 234
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
2-207 |
5.95e-12 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 64.81 E-value: 5.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 2 ISIKNVNKWYGDFQVLTDcSTEVKKGEVIVVCGPSGSGKSTLIKC-VNALEPfQKGDVIVDgTSIA-DPktnlpklrsrv 79
Cdd:COG1245 342 VEYPDLTKSYGGFSLEVE-GGEIREGEVLGIVGPNGIGKTTFAKIlAGVLKP-DEGEVDED-LKISyKP----------- 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 80 gmvfQHFELFPHLTITENLTIAQIKVLGRSKEEAtkkglQLLDRVGLSAHAHKHPGQLSGGQQQRVAIARALAMDPIVML 159
Cdd:COG1245 408 ----QYISPDYDGTVEEFLRSANTDDFGSSYYKT-----EIIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYL 478
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 516455767 160 FDEPTSALDPEMVNEVLDVMVQLAQE-GMTMMCVTHEMGFARKVADRVI 207
Cdd:COG1245 479 LDEPSAHLDVEQRLAVAKAIRRFAENrGKTAMVVDHDIYLIDYISDRLM 527
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
25-206 |
8.02e-12 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 64.42 E-value: 8.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 25 KKGEVIVVCGPSGSGKSTLIKcvnalepfqkgdvIVDGTSIadPktNLPKLRSRVG--MVFQHF---ELFPHLT--ITEN 97
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALK-------------ILSGELK--P--NLGDYDEEPSwdEVLKRFrgtELQDYFKklANGE 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 98 LTIA-------QI-KVL-GRSKE---EATKKGL--QLLDRVGLSAHAHKHPGQLSGGQQQRVAIARALAMDPIVMLFDEP 163
Cdd:COG1245 160 IKVAhkpqyvdLIpKVFkGTVRElleKVDERGKldELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEP 239
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 516455767 164 TSALDpemVNE---VLDVMVQLAQEGMTMMCVTHEMGFARKVADRV 206
Cdd:COG1245 240 SSYLD---IYQrlnVARLIRELAEEGKYVLVVEHDLAILDYLADYV 282
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
24-176 |
1.01e-11 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 62.17 E-value: 1.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 24 VKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGtsiadpKTNLPKLRSRVGMVFQHFE-LFPHLTITENLTIAQ 102
Cdd:PRK13543 34 VDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDG------KTATRGDRSRFMAYLGHLPgLKADLSTLENLHFLC 107
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 516455767 103 iKVLGRSKEEATKKGLQLldrVGLSAHAHKHPGQLSGGQQQRVAIARALAMDPIVMLFDEPTSALDPE---MVNEVL 176
Cdd:PRK13543 108 -GLHGRRAKQMPGSALAI---VGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEgitLVNRMI 180
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
56-208 |
1.07e-11 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 64.28 E-value: 1.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 56 GDVIVDGTSIADpkTNLPKLRSRVGMVFQHFELFpHLTITENLTIAqikvlgrsKEEATKKGLQLLDR-VGLSAHAHKHP 134
Cdd:PTZ00265 1277 GKILLDGVDICD--YNLKDLRNLFSIVSQEPMLF-NMSIYENIKFG--------KEDATREDVKRACKfAAIDEFIESLP 1345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 135 GQ-----------LSGGQQQRVAIARALAMDPIVMLFDEPTSALDPEMVNEVLDVMVQLAQEG-MTMMCVTHEMGFARKV 202
Cdd:PTZ00265 1346 NKydtnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKAdKTIITIAHRIASIKRS 1425
|
....*.
gi 516455767 203 ADRVIF 208
Cdd:PTZ00265 1426 DKIVVF 1431
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
9-207 |
1.19e-11 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 61.43 E-value: 1.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 9 KWYGDFQVLTDcSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGTSIA-DPktnlpklrsrvgmvfqhfe 87
Cdd:cd03222 8 KRYGVFFLLVE-LGVVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITPVyKP------------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 88 lfphltitenltiaqikvlgrskeeatkkglQLLDrvglsahahkhpgqLSGGQQQRVAIARALAMDPIVMLFDEPTSAL 167
Cdd:cd03222 68 -------------------------------QYID--------------LSGGELQRVAIAAALLRNATFYLFDEPSAYL 102
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 516455767 168 DPEMVNEVLDVMVQLAQEGM-TMMCVTHEMGFARKVADRVI 207
Cdd:cd03222 103 DIEQRLNAARAIRRLSEEGKkTALVVEHDLAVLDYLSDRIH 143
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
17-216 |
1.19e-11 |
|
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: 61.18 E-value: 1.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 17 LTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNAlepfqkgdvivdgtsiADPKTNLPKLRSRvgmvfqhfeLFPHLTITe 96
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVNEGLY----------------ASGKARLISFLPK---------FSRNKLIF- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 97 nltIAQikvlgrskeeatkkgLQLLDRVGLSahaHKHPGQ----LSGGQQQRVAIARALA--MDPIVMLFDEPTSALDPE 170
Cdd:cd03238 65 ---IDQ---------------LQFLIDVGLG---YLTLGQklstLSGGELQRVKLASELFsePPGTLFILDEPSTGLHQQ 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 516455767 171 MVNEVLDVMVQLAQEGMTMMCVTHEMGFARKvADRVIFM------DAGKIIE 216
Cdd:cd03238 124 DINQLLEVIKGLIDLGNTVILIEHNLDVLSS-ADWIIDFgpgsgkSGGKVVF 174
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
10-212 |
2.13e-11 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 61.58 E-value: 2.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 10 WYGDFQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVnaLEPFQK--GDVIVDGTSIADPKTNLPKLRSR--VGMVFQH 85
Cdd:cd03290 10 WGSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAI--LGEMQTleGKVHWSNKNESEPSFEATRSRNRysVAYAAQK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 86 FELFpHLTITENLTIAQikVLGRSKEEATKKGLQLLDRVGLSAHAHK-HPGQ----LSGGQQQRVAIARALAMDPIVMLF 160
Cdd:cd03290 88 PWLL-NATVEENITFGS--PFNKQRYKAVTDACSLQPDIDLLPFGDQtEIGErginLSGGQRQRICVARALYQNTNIVFL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 516455767 161 DEPTSALDPEMVNEVLD--VMVQLAQEGMTMMCVTHEMGFARKvADRVIFMDAG 212
Cdd:cd03290 165 DDPFSALDIHLSDHLMQegILKFLQDDKRTLVLVTHKLQYLPH-ADWIIAMKDG 217
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
16-194 |
3.99e-11 |
|
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: 62.46 E-value: 3.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 16 VLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPfqkgdvIVDGTSIADPKTNLPKLRSRvgmvfqhfelfPHLTit 95
Cdd:TIGR00954 467 LIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWP------VYGGRLTKPAKGKLFYVPQR-----------PYMT-- 527
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 96 eNLTIAQIKVLGRSKEEATKKGL------QLLDRVGLSaHAHKHPG----------QLSGGQQQRVAIARALAMDPIVML 159
Cdd:TIGR00954 528 -LGTLRDQIIYPDSSEDMKRRGLsdkdleQILDNVQLT-HILEREGgwsavqdwmdVLSGGEKQRIAMARLFYHKPQFAI 605
|
170 180 190
....*....|....*....|....*....|....*.
gi 516455767 160 FDEPTSALDPEMVnevlDVMVQLAQE-GMTMMCVTH 194
Cdd:TIGR00954 606 LDECTSAVSVDVE----GYMYRLCREfGITLFSVSH 637
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
1-195 |
4.15e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 60.35 E-value: 4.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 1 MISIKNVNKWYGDFQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGTSIadpKTNLPKLRSRVG 80
Cdd:PRK13540 1 MLDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSI---KKDLCTYQKQLC 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 81 MVFQHFELFPHLTITENltiaqikVLGRSKEEATKKGLQLLDRVGLSAHAHKHP-GQLSGGQQQRVAIARALAMDPIVML 159
Cdd:PRK13540 78 FVGHRSGINPYLTLREN-------CLYDIHFSPGAVGITELCRLFSLEHLIDYPcGLLSSGQKRQVALLRLWMSKAKLWL 150
|
170 180 190
....*....|....*....|....*....|....*.
gi 516455767 160 FDEPTSALDPEMVNEVLDVMVQLAQEGMTMMCVTHE 195
Cdd:PRK13540 151 LDEPLVALDELSLLTIITKIQEHRAKGGAVLLTSHQ 186
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
12-240 |
7.44e-11 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 61.66 E-value: 7.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 12 GDFQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIkcvNALEPFQKGDVIVDGTSIadpkTNLPKLRS----RVGMVFQHFE 87
Cdd:TIGR00956 774 EKRVILNNVDGWVKPGTLTALMGASGAGKTTLL---NVLAERVTTGVITGGDRL----VNGRPLDSsfqrSIGYVQQQDL 846
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 88 LFPHLTITENLTIA----QIKVLGRS-KEEATKKGLQLLDR-------VGLsahahkhPGQ-LSGGQQQRVAIARALAMD 154
Cdd:TIGR00956 847 HLPTSTVRESLRFSaylrQPKSVSKSeKMEYVEEVIKLLEMesyadavVGV-------PGEgLNVEQRKRLTIGVELVAK 919
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 155 PIVMLF-DEPTSALDPEMVNEVLDVMVQLAQEGMTMMCVTHE---MGFARkvADRVIFMDAGKiiedcpKEEFFGDISAR 230
Cdd:TIGR00956 920 PKLLLFlDEPTSGLDSQTAWSICKLMRKLADHGQAILCTIHQpsaILFEE--FDRLLLLQKGG------QTVYFGDLGEN 991
|
250
....*....|
gi 516455767 231 SERAQHFLEK 240
Cdd:TIGR00956 992 SHTIINYFEK 1001
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
26-208 |
1.41e-10 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 57.77 E-value: 1.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 26 KGEVIVVCGPSGSGKSTLIKCV-NALEPFQKGDVIVDGTSIADPKTNLPKLRSRVGmvfqhfelfphltitenltiaqik 104
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALaRELGPPGGGVIYIDGEDILEEVLDQLLLIIVGG------------------------ 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 105 vlgrskeeatkkglqlldrvglsahahkHPGQLSGGQQQRVAIARALAMDPIVMLFDEPTSALDPEMVNEVLD------V 178
Cdd:smart00382 57 ----------------------------KKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLleelrlL 108
|
170 180 190
....*....|....*....|....*....|
gi 516455767 179 MVQLAQEGMTMMCVTHEMGFARKVADRVIF 208
Cdd:smart00382 109 LLLKSEKNLTVILTTNDEKDLGPALLRRRF 138
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
4-215 |
1.56e-10 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 60.29 E-value: 1.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 4 IKNVNKWYGDFQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKC-VNALEPfQKGDVivdgtsiadpktnlpKL--RSRVG 80
Cdd:PRK15064 322 VENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTlVGELEP-DSGTV---------------KWseNANIG 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 81 MVFQ-HFELFPH-LTITEnlTIAQIK-----------VLGR---SKEEATKKGlqlldRVglsahahkhpgqLSGGQQQR 144
Cdd:PRK15064 386 YYAQdHAYDFENdLTLFD--WMSQWRqegddeqavrgTLGRllfSQDDIKKSV-----KV------------LSGGEKGR 446
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 516455767 145 VAIARALAMDPIVMLFDEPTSALDPEMV---NEVLDVMvqlaqEGmTMMCVTHEMGFARKVADRVIFMDAGKII 215
Cdd:PRK15064 447 MLFGKLMMQKPNVLVMDEPTNHMDMESIeslNMALEKY-----EG-TLIFVSHDREFVSSLATRIIEITPDGVV 514
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
16-235 |
2.13e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 60.37 E-value: 2.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 16 VLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGTSIAdpKTNLPKLRSRVGMVFQHFELFPHlTIT 95
Cdd:PLN03232 1251 VLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVA--KFGLTDLRRVLSIIPQSPVLFSG-TVR 1327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 96 ENL---TIAQIKVLGRSKEEATKKGLQLLDRVGLSAHAHKHPGQLSGGQQQRVAIARALAMDPIVMLFDEPTSALDPEmV 172
Cdd:PLN03232 1328 FNIdpfSEHNDADLWEALERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVR-T 1406
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 516455767 173 NEVLDVMVQLAQEGMTMMCVTHEMGFARKvADRVIFMDAGKIIE-DCPKEEFFGDISARSERAQ 235
Cdd:PLN03232 1407 DSLIQRTIREEFKSCTMLVIAHRLNTIID-CDKILVLSSGQVLEyDSPQELLSRDTSAFFRMVH 1469
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
3-215 |
2.39e-10 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 59.95 E-value: 2.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 3 SIKNVNKWY-GDFQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALepfqkgDVIVDGTSIADPKTNlpklrsrVGM 81
Cdd:TIGR03719 6 TMNRVSKVVpPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGV------DKDFNGEARPQPGIK-------VGY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 82 VFQHFELFPHLTITEN--LTIAQIK-VLGR------------------SKEEA-------TKKGLQLLDRVGLSAHAHKH 133
Cdd:TIGR03719 73 LPQEPQLDPTKTVRENveEGVAEIKdALDRfneisakyaepdadfdklAAEQAelqeiidAADAWDLDSQLEIAMDALRC 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 134 P------GQLSGGQQQRVAIARALAMDPIVMLFDEPTSALDPEMVnevlDVMVQ-LAQEGMTMMCVTHEMGFARKVADRV 206
Cdd:TIGR03719 153 PpwdadvTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESV----AWLERhLQEYPGTVVAVTHDRYFLDNVAGWI 228
|
....*....
gi 516455767 207 IFMDAGKII 215
Cdd:TIGR03719 229 LELDRGRGI 237
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
24-196 |
3.15e-10 |
|
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: 58.53 E-value: 3.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 24 VKKGEVIVVCGPSGSGKSTLIKCVNA-----LEPFQKG---DVIVD---GTSIADPKTNLPKLRSRVGMVFQHFELFPHL 92
Cdd:cd03236 23 PREGQVLGLVGPNGIGKSTALKILAGklkpnLGKFDDPpdwDEILDefrGSELQNYFTKLLEGDVKVIVKPQYVDLIPKA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 93 ---TITENLTiaqikvlgrsKEEATKKGLQLLDRVGLSAHAHKHPGQLSGGQQQRVAIARALAMDPIVMLFDEPTSALDP 169
Cdd:cd03236 103 vkgKVGELLK----------KKDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDI 172
|
170 180
....*....|....*....|....*..
gi 516455767 170 EMVNEVLDVMVQLAQEGMTMMCVTHEM 196
Cdd:cd03236 173 KQRLNAARLIRELAEDDNYVLVVEHDL 199
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
16-235 |
7.14e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 58.98 E-value: 7.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 16 VLTDCSTEVKKGEVIVVCGPSGSGKSTLIkcvNAL----EPfQKGDVIVDGTSIAdpKTNLPKLRSRVGMVFQHFELFPH 91
Cdd:PLN03130 1254 VLHGLSFEISPSEKVGIVGRTGAGKSSML---NALfrivEL-ERGRILIDGCDIS--KFGLMDLRKVLGIIPQAPVLFSG 1327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 92 lTITENL------TIAQikvLGRSKEEATKKGLQLLDRVGLSAHAHKHPGQLSGGQQQRVAIARALAMDPIVMLFDEPTS 165
Cdd:PLN03130 1328 -TVRFNLdpfnehNDAD---LWESLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATA 1403
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 516455767 166 ALDPEMvnevlDVMVQ--LAQE--GMTMMCVTHEMGFARKvADRVIFMDAGKIIE-DCPKEEFFGDISARSERAQ 235
Cdd:PLN03130 1404 AVDVRT-----DALIQktIREEfkSCTMLIIAHRLNTIID-CDRILVLDAGRVVEfDTPENLLSNEGSAFSKMVQ 1472
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
2-170 |
1.84e-09 |
|
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: 57.25 E-value: 1.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 2 ISIKNVNKWYGDFQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGT-SIA---------DPKTN 71
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETvKLAyvdqsrdalDPNKT 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 72 lpklrsrvgmVFQhfelfphlTITENLTIAQI---KVLGRskeeatkkglQLLDRVGLS-AHAHKHPGQLSGGQQQRVAI 147
Cdd:TIGR03719 403 ----------VWE--------EISGGLDIIKLgkrEIPSR----------AYVGRFNFKgSDQQKKVGQLSGGERNRVHL 454
|
170 180
....*....|....*....|...
gi 516455767 148 ARALAMDPIVMLFDEPTSALDPE 170
Cdd:TIGR03719 455 AKTLKSGGNVLLLDEPTNDLDVE 477
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
16-226 |
2.60e-09 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 57.10 E-value: 2.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 16 VLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDgTSIAdpktNLPK--------LRSRVgmvfqhfe 87
Cdd:PTZ00243 675 LLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAE-RSIA----YVPQqawimnatVRGNI-------- 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 88 LFPHLTITENLTIAqIKVlgrSKEEATkkgLQLLDRvGLSAHAHKHPGQLSGGQQQRVAIARALAMDPIVMLFDEPTSAL 167
Cdd:PTZ00243 742 LFFDEEDAARLADA-VRV---SQLEAD---LAQLGG-GLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSAL 813
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 516455767 168 DPEMVNEVLDVMVQLAQEGMTMMCVTHEMGFARKvADRVIFMDAGKIiedcpkeEFFGD 226
Cdd:PTZ00243 814 DAHVGERVVEECFLGALAGKTRVLATHQVHVVPR-ADYVVALGDGRV-------EFSGS 864
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
5-242 |
3.49e-09 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 55.59 E-value: 3.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 5 KNVNKwygDFQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGtsiadpktnlpklrsRVGMVFQ 84
Cdd:PRK13546 31 KHKNK---TFFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG---------------EVSVIAI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 85 HFELFPHLTITENLTIAQIkVLGRSKEEATKKGLQLLDRVGLSAHAHKHPGQLSGGQQQRVAIARALAMDPIVMLFDEPT 164
Cdd:PRK13546 93 SAGLSGQLTGIENIEFKML-CMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEAL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 165 SALDPEMVNEVLDVMVQLAQEGMTMMCVTHEMGFARKVADRVIFMDAGKI-----IEDC-PK-EEFFGDISARSERAQHF 237
Cdd:PRK13546 172 SVGDQTFAQKCLDKIYEFKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLkdygeLDDVlPKyEAFLNDFKKKSKAEQKE 251
|
....*
gi 516455767 238 LEKIL 242
Cdd:PRK13546 252 FRNKL 256
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
4-240 |
3.61e-09 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 56.50 E-value: 3.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 4 IKNVNKWYGDFQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKC-VNALEPfQKGDVIVdGTsiadpktnlpKLrsRVGMV 82
Cdd:PRK11147 322 MENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLmLGQLQA-DSGRIHC-GT----------KL--EVAYF 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 83 FQH-FELFPHLTITENltiaqikvLGRSKEEATKKGlqlLDRvglsaHAHK-------HPGQ-------LSGGQQQRVAI 147
Cdd:PRK11147 388 DQHrAELDPEKTVMDN--------LAEGKQEVMVNG---RPR-----HVLGylqdflfHPKRamtpvkaLSGGERNRLLL 451
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 148 ARALAMDPIVMLFDEPTSALDPEMVnEVLDVMvqLAQEGMTMMCVTHEMGFA-RKVADRVIFMDAGKIiedcpkEEFFGD 226
Cdd:PRK11147 452 ARLFLKPSNLLILDEPTNDLDVETL-ELLEEL--LDSYQGTVLLVSHDRQFVdNTVTECWIFEGNGKI------GRYVGG 522
|
250
....*....|....*
gi 516455767 227 IS-ARSERAQHFLEK 240
Cdd:PRK11147 523 YHdARQQQAQYLALK 537
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
27-207 |
4.14e-09 |
|
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: 55.31 E-value: 4.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 27 GEVIVVCGPSGSGKSTLI-------------------KCVNALEPFQKGD--VIVDGTSIA-DPKTNlPKLRSRVgmvFQ 84
Cdd:cd03271 21 GVLTCVTGVSGSGKSSLIndtlypalarrlhlkkeqpGNHDRIEGLEHIDkvIVIDQSPIGrTPRSN-PATYTGV---FD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 85 HF-ELF-----------PHLTIT-ENLTIAQikVLGRSKEEATK---------KGLQLLDRVGLSahaHKHPGQ----LS 138
Cdd:cd03271 97 EIrELFcevckgkrynrETLEVRyKGKSIAD--VLDMTVEEALEffenipkiaRKLQTLCDVGLG---YIKLGQpattLS 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 516455767 139 GGQQQRVAIARALAM---DPIVMLFDEPTSALDPEMVNEVLDVMVQLAQEGMTMMCVTHEMGFArKVADRVI 207
Cdd:cd03271 172 GGEAQRIKLAKELSKrstGKTLYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIEHNLDVI-KCADWII 242
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
16-212 |
4.83e-09 |
|
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: 55.25 E-value: 4.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 16 VLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCV-NALEPfQKGDVivdgtsiadpktnlpKLRSRVGMVFQHFELFPHlTI 94
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLIlGELEP-SEGKI---------------KHSGRISFSSQFSWIMPG-TI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 95 TENLtiaqikVLGRSKEE----ATKKGLQLLDRVGLSAHAHKHP-GQ----LSGGQQQRVAIARALAMDPIVMLFDEPTS 165
Cdd:cd03291 115 KENI------IFGVSYDEyrykSVVKACQLEEDITKFPEKDNTVlGEggitLSGGQRARISLARAVYKDADLYLLDSPFG 188
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 516455767 166 ALDPEMVNEVLDVMVQLAQEGMTMMCVTHEMGFARKvADRVIFMDAG 212
Cdd:cd03291 189 YLDVFTEKEIFESCVCKLMANKTRILVTSKMEHLKK-ADKILILHEG 234
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
16-212 |
4.98e-09 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 56.46 E-value: 4.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 16 VLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCV-NALEPfQKGDVivdgtsiadpktnlpKLRSRVGMVFQHFELFPHlTI 94
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMImGELEP-SEGKI---------------KHSGRISFSPQTSWIMPG-TI 503
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 95 TENLtiaqikVLGRSKEE----ATKKGLQLLDRVGLSAHAHKHP-GQ----LSGGQQQRVAIARALAMDPIVMLFDEPTS 165
Cdd:TIGR01271 504 KDNI------IFGLSYDEyrytSVIKACQLEEDIALFPEKDKTVlGEggitLSGGQRARISLARAVYKDADLYLLDSPFT 577
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 516455767 166 ALDPEMVNEVLDVMVQLAQEGMTMMCVTHEMGFARKvADRVIFMDAG 212
Cdd:TIGR01271 578 HLDVVTEKEIFESCLCKLMSNKTRILVTSKLEHLKK-ADKILLLHEG 623
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
26-209 |
7.46e-09 |
|
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: 53.13 E-value: 7.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 26 KGEVIVVCGPSGSGKSTLIKCVNalepfqkgdVIVDGTSIADPKTNLPKLRSRVGMVfqhfELFPHLTITenltiaqikv 105
Cdd:cd03227 20 EGSLTIITGPNGSGKSTILDAIG---------LALGGAQSATRRRSGVKAGCIVAAV----SAELIFTRL---------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 106 lgrskeeatkkglqlldrvglsahahkhpgQLSGGQQQRVAIARALAM-----DPIVmLFDEPTSALDPEMVNEVLDVMV 180
Cdd:cd03227 77 ------------------------------QLSGGEKELSALALILALaslkpRPLY-ILDEIDRGLDPRDGQALAEAIL 125
|
170 180
....*....|....*....|....*....
gi 516455767 181 QLAQEGMTMMCVTHEMGFARKvADRVIFM 209
Cdd:cd03227 126 EHLVKGAQVIVITHLPELAEL-ADKLIHI 153
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
99-222 |
1.21e-08 |
|
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: 55.02 E-value: 1.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 99 TIAQikVLGRSKEEATK---------KGLQLLDRVGLSahaHKHPGQ----LSGGQQQRVAIARAL---AMDPIVMLFDE 162
Cdd:TIGR00630 784 NIAD--VLDMTVEEAYEffeavpsisRKLQTLCDVGLG---YIRLGQpattLSGGEAQRIKLAKELskrSTGRTLYILDE 858
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 516455767 163 PTSALDPEMVNEVLDVMVQLAQEGMTMMCVTHEMGFArKVADRVIFM------DAGKIIEDCPKEE 222
Cdd:TIGR00630 859 PTTGLHFDDIKKLLEVLQRLVDKGNTVVVIEHNLDVI-KTADYIIDLgpeggdGGGTVVASGTPEE 923
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
2-169 |
3.93e-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: 52.55 E-value: 3.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 2 ISIKNVNKWY--GDFQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALePFQKGDVIVDGTSIAdpKTNLPKLRSRV 79
Cdd:cd03289 3 MTVKDLTAKYteGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRL-LNTEGDIQIDGVSWN--SVPLQKWRKAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 80 GMVFQHFELFPHlTITENLtiaqiKVLGRSKEEATKKglqLLDRVGLSAHAHKHPGQL-----------SGGQQQRVAIA 148
Cdd:cd03289 80 GVIPQKVFIFSG-TFRKNL-----DPYGKWSDEEIWK---VAEEVGLKSVIEQFPGQLdfvlvdggcvlSHGHKQLMCLA 150
|
170 180
....*....|....*....|.
gi 516455767 149 RALAMDPIVMLFDEPTSALDP 169
Cdd:cd03289 151 RSVLSKAKILLLDEPSAHLDP 171
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
16-169 |
5.20e-08 |
|
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: 53.38 E-value: 5.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 16 VLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPfQKGDVIVDGTSIAdpKTNLPKLRSRVGMVFQHFELFPHlTIT 95
Cdd:TIGR01271 1234 VLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVSWN--SVTLQTWRKAFGVIPQKVFIFSG-TFR 1309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 96 ENLT-IAQIkvlgrSKEEATKkglqLLDRVGLSAHAHKHPGQL-----------SGGQQQRVAIARALAMDPIVMLFDEP 163
Cdd:TIGR01271 1310 KNLDpYEQW-----SDEEIWK----VAEEVGLKSVIEQFPDKLdfvlvdggyvlSNGHKQLMCLARSILSKAKILLLDEP 1380
|
....*.
gi 516455767 164 TSALDP 169
Cdd:TIGR01271 1381 SAHLDP 1386
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
1-194 |
1.54e-07 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 50.56 E-value: 1.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 1 MISIKNVNKWYGDFQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQ--KGDVIVDGTSIADPKtnlPKLRSR 78
Cdd:PRK09580 1 MLSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDYEvtGGTVEFKGKDLLELS---PEDRAG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 79 VG--MVFQHFELFPHLTITENLTIAQIKVLGRSKEEATKKgLQLLDRVGLSAHAHKHPGQL---------SGGQQQRVAI 147
Cdd:PRK09580 78 EGifMAFQYPVEIPGVSNQFFLQTALNAVRSYRGQEPLDR-FDFQDLMEEKIALLKMPEDLltrsvnvgfSGGEKKRNDI 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 516455767 148 ARALAMDPIVMLFDEPTSALDPEMVNEVLDVMVQLAQEGMTMMCVTH 194
Cdd:PRK09580 157 LQMAVLEPELCILDESDSGLDIDALKIVADGVNSLRDGKRSFIIVTH 203
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
135-222 |
1.74e-07 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 51.33 E-value: 1.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 135 GQLSGGQQQRVAIARALAMDPIVMLFDEPTSALDPEMVNEVLDVMVQLAQEGMTMMCVTHEMGFARKVADRVIFMDAGKI 214
Cdd:NF040905 403 GNLSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAEGKGVIVISSELPELLGMCDRIYVMNEGRI 482
|
....*...
gi 516455767 215 IEDCPKEE 222
Cdd:NF040905 483 TGELPREE 490
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
2-183 |
2.79e-07 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 49.62 E-value: 2.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 2 ISIKNVNKwYGDFQVLtdcstEVKKGeVIVVCGPSGSGKSTLIKCVN-ALEpfqkGDVIVDGTSIADpKTNLPKLRSRVG 80
Cdd:COG0419 5 LRLENFRS-YRDTETI-----DFDDG-LNLIVGPNGAGKSTILEAIRyALY----GKARSRSKLRSD-LINVGSEEASVE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 81 MVFQH-------------FELFPHLT---ITENL-TIAQIKVLGRSKEEATKKGLQLLDRVGLSAHAHK----------- 132
Cdd:COG0419 73 LEFEHggkryrierrqgeFAEFLEAKpseRKEALkRLLGLEIYEELKERLKELEEALESALEELAELQKlkqeilaqlsg 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 516455767 133 --HPGQLSGGQQQRVAIARALAmdpivMLFDepTSALDPEMVNEVLDVMVQLA 183
Cdd:COG0419 153 ldPIETLSGGERLRLALADLLS-----LILD--FGSLDEERLERLLDALEELA 198
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
2-170 |
4.18e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 50.12 E-value: 4.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 2 ISIKNVNKWYGDFQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGT-----------SIADPKT 70
Cdd:PRK11819 325 IEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGETvklayvdqsrdALDPNKT 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 71 nlpklrsrvgmVFQhfelfphlTITENLTIaqIKVLGRskeeatkkglQLLDRVGLSAHAHKHP------GQLSGGQQQR 144
Cdd:PRK11819 405 -----------VWE--------EISGGLDI--IKVGNR----------EIPSRAYVGRFNFKGGdqqkkvGVLSGGERNR 453
|
170 180
....*....|....*....|....*.
gi 516455767 145 VAIARALAMDPIVMLFDEPTSALDPE 170
Cdd:PRK11819 454 LHLAKTLKQGGNVLLLDEPTNDLDVE 479
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
3-216 |
4.93e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 50.12 E-value: 4.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 3 SIKNVNKWYG-DFQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALE-PFQkgdvivdGTSIADPKTnlpklrsRVG 80
Cdd:PRK11819 8 TMNRVSKVVPpKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDkEFE-------GEARPAPGI-------KVG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 81 MVFQHFELFPHLTITENLT--IAQIKVL-------------------------GRSKEEATKKGLQLLD-RVGLSAHAHK 132
Cdd:PRK11819 74 YLPQEPQLDPEKTVRENVEegVAEVKAAldrfneiyaayaepdadfdalaaeqGELQEIIDAADAWDLDsQLEIAMDALR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 133 HP------GQLSGGQQQRVAIARALAMDPIVMLFDEPTSALDPEMVN--EvldvmvQ-LAQEGMTMMCVTHemgfarkva 203
Cdd:PRK11819 154 CPpwdakvTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAwlE------QfLHDYPGTVVAVTH--------- 218
|
250
....*....|....*
gi 516455767 204 DRViFMD--AGKIIE 216
Cdd:PRK11819 219 DRY-FLDnvAGWILE 232
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
13-192 |
8.68e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 49.24 E-value: 8.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 13 DFQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGTSIAdpKTNLPKLRSRVGMVFQHFE---LF 89
Cdd:PRK10938 15 DTKTLQLPSLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHIT--RLSFEQLQKLVSDEWQRNNtdmLS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 90 PHLTITeNLTIAQIKVLGRSKEEATkkgLQLLDRVGLSAHAHKHPGQLSGGQQQRVAIARALAMDPIVMLFDEPTSALDP 169
Cdd:PRK10938 93 PGEDDT-GRTTAEIIQDEVKDPARC---EQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDV 168
|
170 180
....*....|....*....|...
gi 516455767 170 EMVNEVLDVMVQLAQEGMTMMCV 192
Cdd:PRK10938 169 ASRQQLAELLASLHQSGITLVLV 191
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
30-195 |
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 516455767 30 IVVCGPSGSGKSTLIKCVNA-LEPfqkgdviVDGTSIADPKTnlpklrsRVGMVFQHFelFPHLTITENLTIAQIKVLGR 108
Cdd:PLN03073 538 IAMVGPNGIGKSTILKLISGeLQP-------SSGTVFRSAKV-------RMAVFSQHH--VDGLDLSSNPLLYMMRCFPG 601
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 109 SKEEATKKGLQLLdrvGLSAHAHKHPG-QLSGGQQQRVAIARALAMDPIVMLFDEPTSALDPEMVNEVLDVMVqLAQEGM 187
Cdd:PLN03073 602 VPEQKLRAHLGSF---GVTGNLALQPMyTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEALIQGLV-LFQGGV 677
|
....*...
gi 516455767 188 TMmcVTHE 195
Cdd:PLN03073 678 LM--VSHD 683
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
137-207 |
1.98e-06 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 48.29 E-value: 1.98e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 516455767 137 LSGGQQQRVAIARALA--MDPIVMLFDEPTSALDPEMVNEVLDVMVQLAQEGMTMMCVTHEMGFArKVADRVI 207
Cdd:PRK00635 477 LSGGEQERTALAKHLGaeLIGITYILDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEHDEQMI-SLADRII 548
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
131-215 |
2.68e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 47.93 E-value: 2.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 131 HKHPGQLSGGQQQRVAIARALAMDPIVMLFDEPTSALDpemVNEVLDVMVQLAQEGMTMMCVTHEMGFARKVADRVIFMD 210
Cdd:PLN03073 339 VKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLD---LHAVLWLETYLLKWPKTFIVVSHAREFLNTVVTDILHLH 415
|
....*
gi 516455767 211 AGKII 215
Cdd:PLN03073 416 GQKLV 420
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
29-207 |
5.52e-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: 45.68 E-value: 5.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 29 VIVvcGPSGSGKSTLIKCVN-----ALEPFQKG-----DVIVDGTSIADpktnlpklrsrVGMVFQHFELFPHlTITENL 98
Cdd:cd03240 26 LIV--GQNGAGKTTIIEALKyaltgELPPNSKGgahdpKLIREGEVRAQ-----------VKLAFENANGKKY-TITRSL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 99 TIAQiKVLGRSKEEATKkglqLLDRvglsahahkHPGQLSGGQQQ------RVAIARALAMD-PIVMLfDEPTSALDPEM 171
Cdd:cd03240 92 AILE-NVIFCHQGESNW----PLLD---------MRGRCSGGEKVlasliiRLALAETFGSNcGILAL-DEPTTNLDEEN 156
|
170 180 190
....*....|....*....|....*....|....*...
gi 516455767 172 VNEVL-DVM-VQLAQEGMTMMCVTHEMGFARKvADRVI 207
Cdd:cd03240 157 IEESLaEIIeERKSQKNFQLIVITHDEELVDA-ADHIY 193
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
15-195 |
8.24e-06 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 46.38 E-value: 8.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 15 QVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEP--FQKGDVIVDGtsiadpktnLPKLR---SRV-GMVFQHFEL 88
Cdd:PLN03140 894 QLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTggYIEGDIRISG---------FPKKQetfARIsGYCEQNDIH 964
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 89 FPHLTITENLTIAQIKVLGR--SKEEA---TKKGLQLLDRVGLSAHAHKHPG--QLSGGQQQRVAIARALAMDPIVMLFD 161
Cdd:PLN03140 965 SPQVTVRESLIYSAFLRLPKevSKEEKmmfVDEVMELVELDNLKDAIVGLPGvtGLSTEQRKRLTIAVELVANPSIIFMD 1044
|
170 180 190
....*....|....*....|....*....|....
gi 516455767 162 EPTSALDPEMVNEVLDVMVQLAQEGMTMMCVTHE 195
Cdd:PLN03140 1045 EPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQ 1078
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
137-240 |
8.65e-06 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 46.36 E-value: 8.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 137 LSGGQQQRVAIARAL---AMDPIVMLFDEPTSALDPEMVNEVLDVMVQLAQEGMTMMCVTHEMGFArKVADRVIFMD--- 210
Cdd:PRK00635 810 LSGGEIQRLKLAYELlapSKKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVVIIEHNMHVV-KVADYVLELGpeg 888
|
90 100 110
....*....|....*....|....*....|...
gi 516455767 211 ---AGKIIEDCPKEEFFGDISARSERAQHFLEK 240
Cdd:PRK00635 889 gnlGGYLLASCSPEELIHLHTPTAKALRPYLSS 921
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1-227 |
1.29e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 45.93 E-value: 1.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 1 MISIKNVNKWYGDFQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCV-NALEPfQKGDVivdgtsiadpktNLPKlRSRV 79
Cdd:PRK10636 312 LLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLaGELAP-VSGEI------------GLAK-GIKL 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 80 GMVFQHFELFphLTITEnltiAQIKVLGRSKEEATKKglQLLDRVG-LSAHAHK---HPGQLSGGQQQRVAIARALAMDP 155
Cdd:PRK10636 378 GYFAQHQLEF--LRADE----SPLQHLARLAPQELEQ--KLRDYLGgFGFQGDKvteETRRFSGGEKARLVLALIVWQRP 449
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 516455767 156 IVMLFDEPTSALDPEMVNEVLDVMVQLaqEGmTMMCVTHEMGFARKVADRVIFMDAGKIiedcpkEEFFGDI 227
Cdd:PRK10636 450 NLLLLDEPTNHLDLDMRQALTEALIDF--EG-ALVVVSHDRHLLRSTTDDLYLVHDGKV------EPFDGDL 512
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
16-216 |
2.65e-05 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 45.15 E-value: 2.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 16 VLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGTSIAdpKTNLPKLRSRVGMVFQHFELF------ 89
Cdd:PTZ00243 1325 VLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIG--AYGLRELRRQFSMIPQDPVLFdgtvrq 1402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 90 ---PHLTITENLTIAQIKVLGRSKEEATKKGlqlldrvGLSAHAHKHPGQLSGGQQQRVAIARA-LAMDPIVMLFDEPTS 165
Cdd:PTZ00243 1403 nvdPFLEASSAEVWAALELVGLRERVASESE-------GIDSRVLEGGSNYSVGQRQLMCMARAlLKKGSGFILMDEATA 1475
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 516455767 166 ALDPEMVNEVlDVMVQLAQEGMTMMCVTHEMgfaRKVA--DRVIFMDAGKIIE 216
Cdd:PTZ00243 1476 NIDPALDRQI-QATVMSAFSAYTVITIAHRL---HTVAqyDKIIVMDHGAVAE 1524
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
26-52 |
1.20e-04 |
|
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: 42.00 E-value: 1.20e-04
10 20
....*....|....*....|....*..
gi 516455767 26 KGEVIVVCGPSGSGKSTLIkcvNALEP 52
Cdd:cd01854 84 KGKTSVLVGQSGVGKSTLL---NALLP 107
|
|
| PRK00098 |
PRK00098 |
GTPase RsgA; Reviewed |
26-52 |
1.28e-04 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234631 [Multi-domain] Cd Length: 298 Bit Score: 42.11 E-value: 1.28e-04
10 20
....*....|....*....|....*..
gi 516455767 26 KGEVIVVCGPSGSGKSTLIkcvNALEP 52
Cdd:PRK00098 163 AGKVTVLAGQSGVGKSTLL---NALAP 186
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
99-207 |
1.99e-04 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 42.32 E-value: 1.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 99 TIAQikVLGRSKEEAT---------KKGLQLLDRVGLSahaHKHPGQ----LSGGQQQRVAIARALAM---DPIVMLFDE 162
Cdd:COG0178 781 NIAD--VLDMTVEEALeffenipkiARKLQTLQDVGLG---YIKLGQpattLSGGEAQRVKLASELSKrstGKTLYILDE 855
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 516455767 163 PTSALDPEMVNEVLDVMVQLAQEGMTMMCVTHEMGFArKVADRVI 207
Cdd:COG0178 856 PTTGLHFHDIRKLLEVLHRLVDKGNTVVVIEHNLDVI-KTADWII 899
|
|
| Gmk |
COG0194 |
Guanylate kinase [Nucleotide transport and metabolism]; |
26-47 |
3.59e-04 |
|
Guanylate kinase [Nucleotide transport and metabolism];
Pssm-ID: 439964 Cd Length: 190 Bit Score: 40.05 E-value: 3.59e-04
|
| GMPK |
cd00071 |
Guanosine monophosphate kinase (GMPK, EC 2.7.4.8), also known as guanylate kinase (GKase), ... |
29-47 |
6.03e-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: 39.05 E-value: 6.03e-04
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
134-194 |
7.14e-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: 40.07 E-value: 7.14e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 516455767 134 PGQLSGGQQQ---RVAIARALAMDPIVMLFDEPTSALDPEMVNEVLDVMVQLAQEGMTMMCVTH 194
Cdd:pfam13304 234 AFELSDGTKRllaLLAALLSALPKGGLLLIDEPESGLHPKLLRRLLELLKELSRNGAQLILTTH 297
|
|
| COG4639 |
COG4639 |
Predicted kinase [General function prediction only]; |
26-45 |
7.38e-04 |
|
Predicted kinase [General function prediction only];
Pssm-ID: 443677 [Multi-domain] Cd Length: 145 Bit Score: 38.66 E-value: 7.38e-04
|
| RsgA_GTPase |
pfam03193 |
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ... |
26-52 |
7.85e-04 |
|
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are broadly conserved in bacteria and are indispensable for growth. The GTPase domain of RsgA is very similar to several P-loop GTPases, but differs in having a circular permutation of the GTPase structure described by a G4-G1-G3 pattern.
Pssm-ID: 427191 [Multi-domain] Cd Length: 174 Bit Score: 39.06 E-value: 7.85e-04
10 20
....*....|....*....|....*..
gi 516455767 26 KGEVIVVCGPSGSGKSTLIkcvNALEP 52
Cdd:pfam03193 105 KGKTTVLAGQSGVGKSTLL---NALLP 128
|
|
| gmk |
PRK00300 |
guanylate kinase; Provisional |
25-47 |
9.98e-04 |
|
guanylate kinase; Provisional
Pssm-ID: 234719 Cd Length: 205 Bit Score: 38.92 E-value: 9.98e-04
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
118-212 |
1.21e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 39.81 E-value: 1.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 118 LQLLDRVGLSahaHKHPGQ----LSGGQQQRVAIARALA--MDPIVMLFDEPTSALDPEMVNEVLDVMVQLAQEGMTMMc 191
Cdd:PRK00635 1368 LTFIDKVGLS---YITLGQeqdtLSDGEHYRLHLAKKISsnLTDIIYLLEDPLSGLHPQDAPTLLQLIKELVTNNNTVI- 1443
|
90 100
....*....|....*....|.
gi 516455767 192 VTHEMGFARKVADRVIFMDAG 212
Cdd:PRK00635 1444 ATDRSGSLAEHADHLIHLGPG 1464
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
34-214 |
1.31e-03 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 39.49 E-value: 1.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 34 GPSGSGKSTLIKCV-NALEPfQKGDVIVDgtsiadPKTNLPKLR---------SRVGMVFQ-HFELF------------P 90
Cdd:PRK15064 34 GANGCGKSTFMKILgGDLEP-SAGNVSLD------PNERLGKLRqdqfafeefTVLDTVIMgHTELWevkqerdriyalP 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 91 HLTITENLTIAQIKVL-----GRSKEeaTKKGlQLLDRVGLSAHAHKHP-GQLSGGQQQRVAIARALAMDPIVMLFDEPT 164
Cdd:PRK15064 107 EMSEEDGMKVADLEVKfaemdGYTAE--ARAG-ELLLGVGIPEEQHYGLmSEVAPGWKLRVLLAQALFSNPDILLLDEPT 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 516455767 165 SALDPEMVNEVLDVmvqLAQEGMTMMCVTHEMGFARKV----ADrvifMDAGKI 214
Cdd:PRK15064 184 NNLDINTIRWLEDV---LNERNSTMIIISHDRHFLNSVcthmAD----LDYGEL 230
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
99-207 |
1.43e-03 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 39.67 E-value: 1.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 99 TIAQikVLGRSKEEAT---------KKGLQLLDRVGLSahaHKHPGQ----LSGGQQQRVAIARALAMDP---IVMLFDE 162
Cdd:PRK00349 785 NIAD--VLDMTVEEALeffeaipkiARKLQTLVDVGLG---YIKLGQpattLSGGEAQRVKLAKELSKRStgkTLYILDE 859
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 516455767 163 PTSALDPEMVNEVLDVMVQLAQEGMTMMCVTHEMGFArKVADRVI 207
Cdd:PRK00349 860 PTTGLHFEDIRKLLEVLHRLVDKGNTVVVIEHNLDVI-KTADWII 903
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
58-212 |
1.63e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 39.23 E-value: 1.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 58 VIVDGTSIADpKTNLPklrsrvgmVFQHFELFPHLTITENLTIAQIKVLgrsKEeaTKKGLQLLDRVGLS-AHAHKHPGQ 136
Cdd:TIGR00630 423 VTVGGKSIAD-VSELS--------IREAHEFFNQLTLTPEEKKIAEEVL---KE--IRERLGFLIDVGLDyLSLSRAAGT 488
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 516455767 137 LSGGQQQRVAIARALAMDPIVMLF--DEPTSALDPEMVNEVLDVMVQLAQEGMTMMCVTHEMGfARKVADRVIFMDAG 212
Cdd:TIGR00630 489 LSGGEAQRIRLATQIGSGLTGVLYvlDEPSIGLHQRDNRRLINTLKRLRDLGNTLIVVEHDED-TIRAADYVIDIGPG 565
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
120-216 |
2.37e-03 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 39.00 E-value: 2.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 120 LLDRVGLSAHAHKHP-GQLSGGQQQRVAIARALAMDPIVMLFDEPTSALDpemvnevLDVMVQLAQ-----EGmTMMCVT 193
Cdd:PRK10636 132 LLHGLGFSNEQLERPvSDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLD-------LDAVIWLEKwlksyQG-TLILIS 203
|
90 100
....*....|....*....|...
gi 516455767 194 HEMGFARKVADRVIFMDAGKIIE 216
Cdd:PRK10636 204 HDRDFLDPIVDKIIHIEQQSLFE 226
|
|
| type_II_IV_secretion_ATPases |
cd19477 |
type II/type IV hexameric secretion ATPases; RecA-like NTPases. This family includes the NTP ... |
24-102 |
2.40e-03 |
|
type II/type IV hexameric secretion ATPases; RecA-like NTPases. This family includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. This group also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410885 [Multi-domain] Cd Length: 168 Bit Score: 37.76 E-value: 2.40e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 516455767 24 VKKGEVIVVCGPSGSGKSTLIKCVnaLEPFQKGDVIVdgtSIADPktnlpklrsrVGMVFQHFELFPHLTITENLTIAQ 102
Cdd:cd19477 7 IAIGKNVIVCGGTGSGKTTYIKSI--LEFIPKEERII---SIEDT----------EEIVFKHHKNYTQLFFGGNITSAD 70
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
2-47 |
3.94e-03 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 37.09 E-value: 3.94e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 516455767 2 ISIKNVNKwYGDFQVltdcstEVKKGeVIVVCGPSGSGKSTLIKCV 47
Cdd:pfam13476 1 LTIENFRS-FRDQTI------DFSKG-LTLITGPNGSGKTTILDAI 38
|
|
| ABC_SMC3_euk |
cd03272 |
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ... |
136-170 |
4.19e-03 |
|
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213239 [Multi-domain] Cd Length: 243 Bit Score: 37.62 E-value: 4.19e-03
10 20 30
....*....|....*....|....*....|....*....
gi 516455767 136 QLSGGQQQRVAIARALAM---DPIVM-LFDEPTSALDPE 170
Cdd:cd03272 158 QLSGGQKSLVALALIFAIqkcDPAPFyLFDEIDAALDAQ 196
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
26-43 |
4.66e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 38.08 E-value: 4.66e-03
|
| guanyl_kin |
TIGR03263 |
guanylate kinase; Members of this family are the enzyme guanylate kinase, also called GMP ... |
29-45 |
5.67e-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: 36.70 E-value: 5.67e-03
|
| SbcC_Walker_B |
pfam13558 |
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from ... |
131-181 |
5.70e-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: 35.29 E-value: 5.70e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 516455767 131 HKHPGQLSGGQQQR---VAIARALAM----------DPIVMLFDEPTSALDPEMVNEVLDVMVQ 181
Cdd:pfam13558 27 YRRSGGLSGGEKQLlayLPLAAALAAqygsaegrppAPRLVFLDEAFAKLDEENIRTALELLRA 90
|
|
| AAA_33 |
pfam13671 |
AAA domain; This family of domains contain only a P-loop motif, that is characteriztic of the ... |
29-45 |
5.88e-03 |
|
AAA domain; This family of domains contain only a P-loop motif, that is characteriztic of the AAA superfamily. Many of the proteins in this family are just short fragments so there is no Walker B motif.
Pssm-ID: 463952 [Multi-domain] Cd Length: 143 Bit Score: 36.13 E-value: 5.88e-03
|
| BMS1 |
cd01882 |
Bms1, an essential GTPase, promotes assembly of preribosomal RNA processing complexes; Bms1 is ... |
29-46 |
7.07e-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: 36.55 E-value: 7.07e-03
|
| COG0645 |
COG0645 |
Predicted kinase, contains AAA domain [General function prediction only]; |
29-43 |
8.27e-03 |
|
Predicted kinase, contains AAA domain [General function prediction only];
Pssm-ID: 440410 [Multi-domain] Cd Length: 164 Bit Score: 36.04 E-value: 8.27e-03
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
69-207 |
8.79e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 37.05 E-value: 8.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516455767 69 KTNLPKLRSRVGmvfqhfELFPHLTitenltiaqikvLGRSKEEATKKGLQLldRVGLSAHAHKHPGQLSGG-QQQ---- 143
Cdd:COG4717 511 EERLPPVLERAS------EYFSRLT------------DGRYRLIRIDEDLSL--KVDTEDGRTRPVEELSRGtREQlyla 570
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 516455767 144 -RVAIARALAMDPIVMLFDEPTSALDPEMVNEVLDVMVQLAQEG----MTmmCVTHEMGFARKVADRVI 207
Cdd:COG4717 571 lRLALAELLAGEPLPLILDDAFVNFDDERLRAALELLAELAKGRqviyFT--CHEELVELFQEEGAHVI 637
|
|
| TrwB_TraG_TraD_VirD4 |
cd01127 |
TrwB/TraG/TraD/VirD4 family of bacterial conjugation proteins; The TraG/TraD/VirD4 family are ... |
30-69 |
8.84e-03 |
|
TrwB/TraG/TraD/VirD4 family of bacterial conjugation proteins; The TraG/TraD/VirD4 family are bacterial conjugation proteins involved in type IV secretion (T4S) systems, versatile bacterial secretion systems mediating transport of protein and/or DNA. They are present in gram-negative and gram-positive bacteria, as well as archaea. They form hexameric rings and belong to the RecA-like NTPases superfamily, which also includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases.
Pssm-ID: 410871 [Multi-domain] Cd Length: 144 Bit Score: 35.66 E-value: 8.84e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 516455767 30 IVVCGPSGSGKSTLIKCVNALEPFQKGDVIvdgtsIADPK 69
Cdd:cd01127 2 TLVLGTTGSGKTTSIVIPLLDQAARGGSVI-----ITDPK 36
|
|
| AAA_22 |
pfam13401 |
AAA domain; |
29-80 |
9.85e-03 |
|
AAA domain;
Pssm-ID: 379165 [Multi-domain] Cd Length: 129 Bit Score: 35.40 E-value: 9.85e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 516455767 29 VIVVCGPSGSGKSTLIKCVNALEPFQKGDVI-VDGTSIADPKTNLPKLRSRVG 80
Cdd:pfam13401 7 ILVLTGESGTGKTTLLRRLLEQLPEVRDSVVfVDLPSGTSPKDLLRALLRALG 59
|
|
| |
