|
Name |
Accession |
Description |
Interval |
E-value |
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
3-240 |
1.09e-122 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 348.14 E-value: 1.09e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 3 LEITQLEKAYNKQKVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVPLIFEEKQLRQHRLKLGI 82
Cdd:COG1126 2 IEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKKDINKLRRKVGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 83 LFQSWNLFPHLTALENISLPLYRVHGYSKEDADSQAMTLLNRFELAKHAHKKPAELSGGQCQRVAIIRAIAIQPSMLLFD 162
Cdd:COG1126 82 VFQQFNLFPHLTVLENVTLAPIKVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKVMLFD 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 503691651 163 EPTSALDPLMTSEVLDLIVELKKEGKQFIIVTHHISFARKICDWILFLSEGKVLDSKPTSQFFDHPASPEIQYYLEQV 240
Cdd:COG1126 162 EPTSALDPELVGEVLDVMRDLAKEGMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFENPQHERTRAFLSKV 239
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
3-215 |
3.13e-95 |
|
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: 277.87 E-value: 3.13e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 3 LEITQLEKAYNKQKVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVPLIFEEKQLRQHRLKLGI 82
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNINELRQKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 83 LFQSWNLFPHLTALENISLPLYRVHGYSKEDADSQAMTLLNRFELAKHAHKKPAELSGGQCQRVAIIRAIAIQPSMLLFD 162
Cdd:cd03262 81 VFQQFNLFPHLTVLENITLAPIKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 503691651 163 EPTSALDPLMTSEVLDLIVELKKEGKQFIIVTHHISFARKICDWILFLSEGKV 215
Cdd:cd03262 161 EPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
3-237 |
1.84e-84 |
|
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: 251.44 E-value: 1.84e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 3 LEITQLEKAYNKQKVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVPLI-FEEKQLRQHRLKLG 81
Cdd:COG1127 6 IEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITgLSEKELYELRRRIG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 82 ILFQSWNLFPHLTALENISLPLYRVHGYSKEDADSQAMTLLNRFELAKHAHKKPAELSGGQCQRVAIIRAIAIQPSMLLF 161
Cdd:COG1127 86 MLFQGGALFDSLTVFENVAFPLREHTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDPEILLY 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 503691651 162 DEPTSALDPLMTSEVLDLIVELKKE-GKQFIIVTHHISFARKICDWILFLSEGKVLDSKPTSQFFDHPaSPEIQYYL 237
Cdd:COG1127 166 DEPTAGLDPITSAVIDELIRELRDElGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLASD-DPWVRQFL 241
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
3-240 |
2.42e-81 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 243.46 E-value: 2.42e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 3 LEITQLEKAYNKQKVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVPLIFEEKQLRQHRLKLGI 82
Cdd:PRK09493 2 IEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLIRQEAGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 83 LFQSWNLFPHLTALENISLPLYRVHGYSKEDADSQAMTLLNRFELAKHAHKKPAELSGGQCQRVAIIRAIAIQPSMLLFD 162
Cdd:PRK09493 82 VFQQFYLFPHLTALENVMFGPLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFD 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 503691651 163 EPTSALDPLMTSEVLDLIVELKKEGKQFIIVTHHISFARKICDWILFLSEGKVLDSKPTSQFFDHPASPEIQYYLEQV 240
Cdd:PRK09493 162 EPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPPSQRLQEFLQHV 239
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
3-215 |
5.41e-81 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 242.26 E-value: 5.41e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 3 LEITQLEKAY----NKQKVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVPLI-FEEKQLRQHR 77
Cdd:COG1136 5 LELRNLTKSYgtgeGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISsLSERELARLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 78 L-KLGILFQSWNLFPHLTALENISLPLyRVHGYSKEDADSQAMTLLNRFELAKHAHKKPAELSGGQCQRVAIIRAIAIQP 156
Cdd:COG1136 85 RrHIGFVFQFFNLLPELTALENVALPL-LLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNRP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 157 SMLLFDEPTSALDPLMTSEVLDLIVELKKE-GKQFIIVTHHISFARkICDWILFLSEGKV 215
Cdd:COG1136 164 KLILADEPTGNLDSKTGEEVLELLRELNRElGTTIVMVTHDPELAA-RADRVIRLRDGRI 222
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
3-215 |
2.26e-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: 232.77 E-value: 2.26e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 3 LEITQLEKAY----NKQKVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVPLI-FEEKQLRQHR 77
Cdd:cd03255 1 IELKNLSKTYggggEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISkLSEKELAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 78 LK-LGILFQSWNLFPHLTALENISLPLyRVHGYSKEDADSQAMTLLNRFELAKHAHKKPAELSGGQCQRVAIIRAIAIQP 156
Cdd:cd03255 81 RRhIGFVFQSFNLLPDLTALENVELPL-LLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 157 SMLLFDEPTSALDPLMTSEVLDLIVELKKE-GKQFIIVTHHISFARkICDWILFLSEGKV 215
Cdd:cd03255 160 KIILADEPTGNLDSETGKEVMELLRELNKEaGTTIVVVTHDPELAE-YADRIIELRDGKI 218
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
2-242 |
2.32e-77 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 233.92 E-value: 2.32e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 2 KLEITQLEKAYNKQKVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVPLIF-----------EE 70
Cdd:COG4598 8 ALEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIRLkpdrdgelvpaDR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 71 KQLRQHRLKLGILFQSWNLFPHLTALENISLPLYRVHGYSKEDADSQAMTLLNRFELAKHAHKKPAELSGGQCQRVAIIR 150
Cdd:COG4598 88 RQLQRIRTRLGMVFQSFNLWSHMTVLENVIEAPVHVLGRPKAEAIERAEALLAKVGLADKRDAYPAHLSGGQQQRAAIAR 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 151 AIAIQPSMLLFDEPTSALDPLMTSEVLDLIVELKKEGKQFIIVTHHISFARKICDWILFLSEGKVLDSKPTSQFFDHPAS 230
Cdd:COG4598 168 ALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEEGRTMLVVTHEMGFARDVSSHVVFLHQGRIEEQGPPAEVFGNPKS 247
|
250
....*....|..
gi 503691651 231 PEIQYYLEQVLK 242
Cdd:COG4598 248 ERLRQFLSSSLK 259
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
3-228 |
1.25e-76 |
|
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: 231.24 E-value: 1.25e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 3 LEITQLEKAYNKQKVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVPLI-FEEKQLRQHRLKLG 81
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISgLSEAELYRLRRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 82 ILFQSWNLFPHLTALENISLPLYRVHGYSKEDADSQAMTLLNRFELAKHAHKKPAELSGGQCQRVAIIRAIAIQPSMLLF 161
Cdd:cd03261 81 MLFQSGALFDSLTVFENVAFPLREHTRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLY 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 162 DEPTSALDPLMTSEVLDLIVELKKE-GKQFIIVTHHISFARKICDWILFLSEGKVLDSKPTSQFF--DHP 228
Cdd:cd03261 161 DEPTAGLDPIASGVIDDLIRSLKKElGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRasDDP 230
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
1-237 |
1.81e-75 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 228.74 E-value: 1.81e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 1 MKLEITQLEKAYNKQKVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVPLIFE----EKQLRQH 76
Cdd:COG4161 1 MSIQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFDFSqkpsEKAIRLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 77 RLKLGILFQSWNLFPHLTALEN-ISLPLyRVHGYSKEDADSQAMTLLNRFELAKHAHKKPAELSGGQCQRVAIIRAIAIQ 155
Cdd:COG4161 81 RQKVGMVFQQYNLWPHLTVMENlIEAPC-KVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMME 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 156 PSMLLFDEPTSALDPLMTSEVLDLIVELKKEGKQFIIVTHHISFARKICDWILFLSEGKVLDsKPTSQFFDHPASPEIQY 235
Cdd:COG4161 160 PQVLLFDEPTAALDPEITAQVVEIIRELSQTGITQVIVTHEVEFARKVASQVVYMEKGRIIE-QGDASHFTQPQTEAFAH 238
|
..
gi 503691651 236 YL 237
Cdd:COG4161 239 YL 240
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
3-216 |
6.04e-75 |
|
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: 226.25 E-value: 6.04e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 3 LEITQLEKAYNKQKVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVPLIFEEKQLRqhrlKLGI 82
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPERR----NIGM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 83 LFQSWNLFPHLTALENISLPLyRVHGYSKEDADSQAMTLLNRFELAKHAHKKPAELSGGQCQRVAIIRAIAIQPSMLLFD 162
Cdd:cd03259 77 VFQDYALFPHLTVAENIAFGL-KLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 503691651 163 EPTSALDPLMTSEVLDLIVELKKE-GKQFIIVTHHISFARKICDWILFLSEGKVL 216
Cdd:cd03259 156 EPLSALDAKLREELREELKELQRElGITTIYVTHDQEEALALADRIAVMNEGRIV 210
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
3-240 |
6.65e-75 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 226.87 E-value: 6.65e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 3 LEITQLEKAYNKQKVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVPLIFEEKQLRQHrlkLGI 82
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRR---IGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 83 LFQSWNLFPHLTALENISLpLYRVHGYSKEDADSQAMTLLNRFELAKHAHKKPAELSGGQCQRVAIIRAIAIQPSMLLFD 162
Cdd:COG1131 78 VPQEPALYPDLTVRENLRF-FARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILD 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 503691651 163 EPTSALDPLMTSEVLDLIVELKKEGKQFIIVTHHISFARKICDWILFLSEGKVLDSKPTSQFfdhpaspeIQYYLEQV 240
Cdd:COG1131 157 EPTSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDEL--------KARLLEDV 226
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
1-237 |
6.89e-75 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 227.20 E-value: 6.89e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 1 MKLEITQLEKAYNKQKVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVPLIFE----EKQLRQH 76
Cdd:PRK11124 1 MSIQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFDFSktpsDKAIREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 77 RLKLGILFQSWNLFPHLTALEN-ISLPLyRVHGYSKEDADSQAMTLLNRFELAKHAHKKPAELSGGQCQRVAIIRAIAIQ 155
Cdd:PRK11124 81 RRNVGMVFQQYNLWPHLTVQQNlIEAPC-RVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMME 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 156 PSMLLFDEPTSALDPLMTSEVLDLIVELKKEGKQFIIVTHHISFARKICDWILFLSEGKVLDsKPTSQFFDHPASPEIQY 235
Cdd:PRK11124 160 PQVLLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTHEVEVARKTASRVVYMENGHIVE-QGDASCFTQPQTEAFKN 238
|
..
gi 503691651 236 YL 237
Cdd:PRK11124 239 YL 240
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
3-231 |
1.54e-74 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 229.58 E-value: 1.54e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 3 LEITQLEKAY--NKQKV--LKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVPLI-FEEKQLRQHR 77
Cdd:COG1135 2 IELENLSKTFptKGGPVtaLDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTaLSERELRAAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 78 LKLGILFQSWNLFPHLTALENISLPLyRVHGYSKEDADSQAMTLLNRFELAKHAHKKPAELSGGQCQRVAIIRAIAIQPS 157
Cdd:COG1135 82 RKIGMIFQHFNLLSSRTVAENVALPL-EIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPK 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 503691651 158 MLLFDEPTSALDPLMTSEVLDLIVELKKE-GKQFIIVTHHISFARKICDWILFLSEGKVLDSKPTSQFFDHPASP 231
Cdd:COG1135 161 VLLCDEATSALDPETTRSILDLLKDINRElGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVLDVFANPQSE 235
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
3-231 |
3.77e-74 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 228.83 E-value: 3.77e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 3 LEITQLEKAYNKQKVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVPLIfeekQLRQHRLKLGI 82
Cdd:COG3842 6 LELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVT----GLPPEKRNVGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 83 LFQSWNLFPHLTALENISLPLyRVHGYSKEDADSQAMTLLNRFELAKHAHKKPAELSGGQCQRVAIIRAIAIQPSMLLFD 162
Cdd:COG3842 82 VFQDYALFPHLTVAENVAFGL-RMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLLD 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503691651 163 EPTSALDPLMTSEVLDLIVELKKE-GKQFIIVTHHIS--FArkICDWILFLSEGKVLDSKPTSQFFDHPASP 231
Cdd:COG3842 161 EPLSALDAKLREEMREELRRLQRElGITFIYVTHDQEeaLA--LADRIAVMNDGRIEQVGTPEEIYERPATR 230
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
3-231 |
1.02e-72 |
|
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: 230.18 E-value: 1.02e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 3 LEITQLEKAY-----NKQKVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVPL-IFEEKQLRQH 76
Cdd:COG1123 261 LEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLtKLSRRSLREL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 77 RLKLGILFQ----SwnLFPHLTALENISLPLyRVHG-YSKEDADSQAMTLLNRFEL-AKHAHKKPAELSGGQCQRVAIIR 150
Cdd:COG1123 341 RRRVQMVFQdpysS--LNPRMTVGDIIAEPL-RLHGlLSRAERRERVAELLERVGLpPDLADRYPHELSGGQRQRVAIAR 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 151 AIAIQPSMLLFDEPTSALDPLMTSEVLDLIVELKKE-GKQFIIVTHHISFARKICDWILFLSEGKVLDSKPTSQFFDHPA 229
Cdd:COG1123 418 ALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRElGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVFANPQ 497
|
..
gi 503691651 230 SP 231
Cdd:COG1123 498 HP 499
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
3-214 |
1.18e-72 |
|
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: 218.98 E-value: 1.18e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 3 LEITQLEKAYNKQKVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVPLIFEEKQLRQHRLKLGI 82
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPPLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 83 LFQSWNLFPHLTALENISLPlyrvhgyskedadsqamtllnrfelakhahkkpaeLSGGQCQRVAIIRAIAIQPSMLLFD 162
Cdd:cd03229 81 VFQDFALFPHLTVLENIALG-----------------------------------LSGGQQQRVALARALAMDPDVLLLD 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 503691651 163 EPTSALDPLMTSEVLDLIVELKKE-GKQFIIVTHHISFARKICDWILFLSEGK 214
Cdd:cd03229 126 EPTSALDPITRREVRALLKSLQAQlGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-213 |
1.47e-71 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 219.19 E-value: 1.47e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 1 MKLEITQLEKAYNKQK----VLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGvplifeeKQLRQH 76
Cdd:COG1116 6 PALELRGVSKRFPTGGggvtALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDG-------KPVTGP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 77 RLKLGILFQSWNLFPHLTALENISLPLyRVHGYSKEDADSQAMTLLNRFELAKHAHKKPAELSGGQCQRVAIIRAIAIQP 156
Cdd:COG1116 79 GPDRGVVFQEPALLPWLTVLDNVALGL-ELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 503691651 157 SMLLFDEPTSALDPLMTSEVLDLIVEL-KKEGKQFIIVTHHISFARKICDWILFLSEG 213
Cdd:COG1116 158 EVLLMDEPFGALDALTRERLQDELLRLwQETGKTVLFVTHDVDEAVFLADRVVVLSAR 215
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
3-228 |
2.48e-71 |
|
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: 217.59 E-value: 2.48e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 3 LEITQLEKAYNKQK-VLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVPLifEEKQLRQHRLKLG 81
Cdd:COG1122 1 IELENLSFSYPGGTpALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDI--TKKNLRELRRKVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 82 ILFQswN----LFpHLTALENISLPLyRVHGYSKEDADSQAMTLLNRFELAKHAHKKPAELSGGQCQRVAIIRAIAIQPS 157
Cdd:COG1122 79 LVFQ--NpddqLF-APTVEEDVAFGP-ENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPE 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 503691651 158 MLLFDEPTSALDPLMTSEVLDLIVELKKEGKQFIIVTHHISFARKICDWILFLSEGKVLDSKPTSQFFDHP 228
Cdd:COG1122 155 VLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDY 225
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1-231 |
4.54e-70 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 218.48 E-value: 4.54e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 1 MKLEITQLEKAYNKQKVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVPLIFeekQLRQHRLKL 80
Cdd:COG1118 1 MSIEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFT---NLPPRERRV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 81 GILFQSWNLFPHLTALENISLPLyRVHGYSKEDADSQAMTLLNRFELAKHAHKKPAELSGGQCQRVAIIRAIAIQPSMLL 160
Cdd:COG1118 78 GFVFQHYALFPHMTVAENIAFGL-RVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503691651 161 FDEPTSALDPLMTSEVLDLIVELKKEGKQF-IIVTHHISFARKICDWILFLSEGKVLDSKPTSQFFDHPASP 231
Cdd:COG1118 157 LDEPFGALDAKVRKELRRWLRRLHDELGGTtVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDRPATP 228
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
3-228 |
1.64e-69 |
|
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: 213.21 E-value: 1.64e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 3 LEITQLEKAY----NKQKVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVPLI-FEEKQLRQHR 77
Cdd:cd03258 2 IELKNVSKVFgdtgGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTlLSGKELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 78 LKLGILFQSWNLFPHLTALENISLPLyRVHGYSKEDADSQAMTLLNRFELAKHAHKKPAELSGGQCQRVAIIRAIAIQPS 157
Cdd:cd03258 82 RRIGMIFQHFNLLSSRTVFENVALPL-EIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPK 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503691651 158 MLLFDEPTSALDPLMTSEVLDLIVELKKE-GKQFIIVTHHISFARKICDWILFLSEGKVLDSKPTSQFFDHP 228
Cdd:cd03258 161 VLLCDEATSALDPETTQSILALLRDINRElGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFANP 232
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
3-230 |
1.81e-69 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 213.38 E-value: 1.81e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 3 LEITQLEKAY-NKQKVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVPLI-FEEKQLRQHRLKL 80
Cdd:COG3638 3 LELRNLSKRYpGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTaLRGRALRRLRRRI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 81 GILFQSWNLFPHLTALENI------SLPLYR--VHGYSKEDADsQAMTLLNRFELAKHAHKKPAELSGGQCQRVAIIRAI 152
Cdd:COG3638 83 GMIFQQFNLVPRLSVLTNVlagrlgRTSTWRslLGLFPPEDRE-RALEALERVGLADKAYQRADQLSGGQQQRVAIARAL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 503691651 153 AIQPSMLLFDEPTSALDPLMTSEVLDLIVEL-KKEGKQFIIVTHHISFARKICDWILFLSEGKVldskptsqFFDHPAS 230
Cdd:COG3638 162 VQEPKLILADEPVASLDPKTARQVMDLLRRIaREDGITVVVNLHQVDLARRYADRIIGLRDGRV--------VFDGPPA 232
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
3-241 |
7.25e-69 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 212.30 E-value: 7.25e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 3 LEITQLEKAYNKQKVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGV------PLIFEEKQLRQH 76
Cdd:PRK11264 4 IEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDItidtarSLSQQKGLIRQL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 77 RLKLGILFQSWNLFPHLTALENISLPLYRVHGYSKEDADSQAMTLLNRFELAKHAHKKPAELSGGQCQRVAIIRAIAIQP 156
Cdd:PRK11264 84 RQHVGFVFQNFNLFPHRTVLENIIEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 157 SMLLFDEPTSALDPLMTSEVLDLIVELKKEGKQFIIVTHHISFARKICDWILFLSEGKVLDSKPTSQFFDHPASPEIQYY 236
Cdd:PRK11264 164 EVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADPQQPRTRQF 243
|
....*
gi 503691651 237 LEQVL 241
Cdd:PRK11264 244 LEKFL 248
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
3-217 |
1.26e-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: 210.41 E-value: 1.26e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 3 LEITQLEKAY----NKQKVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVPLifeekqlRQHRL 78
Cdd:cd03293 1 LEVRNVSKTYggggGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPV-------TGPGP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 79 KLGILFQSWNLFPHLTALENISLPLyRVHGYSKEDADSQAMTLLNRFELAKHAHKKPAELSGGQCQRVAIIRAIAIQPSM 158
Cdd:cd03293 74 DRGYVFQQDALLPWLTVLDNVALGL-ELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDV 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503691651 159 LLFDEPTSALDPLMTSEVLDLIVEL-KKEGKQFIIVTHHISFARKICDWILFLSE--GKVLD 217
Cdd:cd03293 153 LLLDEPFSALDALTREQLQEELLDIwRETGKTVLLVTHDIDEAVFLADRVVVLSArpGRIVA 214
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
3-217 |
3.15e-67 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 206.83 E-value: 3.15e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 3 LEITQLEKAY-NKQKVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVPLI-FEEKQLRQHRLKL 80
Cdd:COG2884 2 IRFENVSKRYpGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSrLKRREIPYLRRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 81 GILFQSWNLFPHLTALENISLPLyRVHGYSKEDADSQAMTLLNRFELAKHAHKKPAELSGGQCQRVAIIRAIAIQPSMLL 160
Cdd:COG2884 82 GVVFQDFRLLPDRTVYENVALPL-RVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 503691651 161 FDEPTSALDPLMTSEVLDLIVELKKEGKQFIIVTHHISFARKICDWILFLSEGKVLD 217
Cdd:COG2884 161 ADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLELVDRMPKRVLELEDGRLVR 217
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
3-231 |
6.64e-67 |
|
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: 206.96 E-value: 6.64e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 3 LEITQLEKAY----NKQKVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVPLifEEKQLRQHRL 78
Cdd:COG1124 2 LEVRNLSVSYgqggRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPV--TRRRRKAFRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 79 KLGILFQ----SWNlfPHLTALENISLPLyRVHGysKEDADSQAMTLLNRFEL-AKHAHKKPAELSGGQCQRVAIIRAIA 153
Cdd:COG1124 80 RVQMVFQdpyaSLH--PRHTVDRILAEPL-RIHG--LPDREERIAELLEQVGLpPSFLDRYPHQLSGGQRQRVAIARALI 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 503691651 154 IQPSMLLFDEPTSALDPLMTSEVLDLIVELKKE-GKQFIIVTHHISFARKICDWILFLSEGKVLDSKPTSQFFDHPASP 231
Cdd:COG1124 155 LEPELLLLDEPTSALDVSVQAEILNLLKDLREErGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAGPKHP 233
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
2-242 |
4.33e-65 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 202.89 E-value: 4.33e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 2 KLEITQLEKAYNKQKVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNF-----------DGVPLIFEE 70
Cdd:PRK10619 5 KLNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVngqtinlvrdkDGQLKVADK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 71 KQLRQHRLKLGILFQSWNLFPHLTALENISLPLYRVHGYSKEDADSQAMTLLNRFELAKHAHKK-PAELSGGQCQRVAII 149
Cdd:PRK10619 85 NQLRLLRTRLTMVFQHFNLWSHMTVLENVMEAPIQVLGLSKQEARERAVKYLAKVGIDERAQGKyPVHLSGGQQQRVSIA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 150 RAIAIQPSMLLFDEPTSALDPLMTSEVLDLIVELKKEGKQFIIVTHHISFARKICDWILFLSEGKVLDSKPTSQFFDHPA 229
Cdd:PRK10619 165 RALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGNPQ 244
|
250
....*....|...
gi 503691651 230 SPEIQYYLEQVLK 242
Cdd:PRK10619 245 SPRLQQFLKGSLK 257
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
3-230 |
8.07e-65 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 201.64 E-value: 8.07e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 3 LEITQLEKAY-NKQKVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVPLIF-EEKQLRQHRLKL 80
Cdd:cd03256 1 IEVENLSKTYpNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKlKGKALRQLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 81 GILFQSWNLFPHLTALENI------SLPLYRV--HGYSKEDAdSQAMTLLNRFELAKHAHKKPAELSGGQCQRVAIIRAI 152
Cdd:cd03256 81 GMIFQQFNLIERLSVLENVlsgrlgRRSTWRSlfGLFPKEEK-QRALAALERVGLLDKAYQRADQLSGGQQQRVAIARAL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 503691651 153 AIQPSMLLFDEPTSALDPLMTSEVLDLIVEL-KKEGKQFIIVTHHISFARKICDWILFLSEGKVldskptsqFFDHPAS 230
Cdd:cd03256 160 MQQPKLILADEPVASLDPASSRQVMDLLKRInREEGITVIVSLHQVDLAREYADRIVGLKDGRI--------VFDGPPA 230
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
3-224 |
3.95e-64 |
|
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: 199.33 E-value: 3.95e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 3 LEITQLEKAYNKQKVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGL-----ESPTCGRVNFDGVPLIFEEKQLRQHR 77
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLndlipGAPDEGEVLLDGKDIYDLDVDVLELR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 78 LKLGILFQSWNLFPhLTALENISLPLyRVHGY-SKEDADSQAMTLLNRFELAKHAHKK--PAELSGGQCQRVAIIRAIAI 154
Cdd:cd03260 81 RRVGMVFQKPNPFP-GSIYDNVAYGL-RLHGIkLKEELDERVEEALRKAALWDEVKDRlhALGLSGGQQQRLCLARALAN 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 155 QPSMLLFDEPTSALDPLMTSEVLDLIVELKKEgKQFIIVTHHISFARKICDWILFLSEGKVLDSKPTSQF 224
Cdd:cd03260 159 EPEVLLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
3-230 |
4.89e-64 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 203.00 E-value: 4.89e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 3 LEITQLEKAYNKQKVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGV------PlifeekqlrQH 76
Cdd:COG3839 4 LELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRdvtdlpP---------KD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 77 RlKLGILFQSWNLFPHLTALENISLPLyRVHGYSKEDADSQAMTLLNRFELAKHAHKKPAELSGGQCQRVAIIRAIAIQP 156
Cdd:COG3839 75 R-NIAMVFQSYALYPHMTVYENIAFPL-KLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREP 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 503691651 157 SMLLFDEPTSALDPLMTSEVLDLIVELKKE-GKQFIIVTHHISFARKICDWILFLSEGKVLDSKPTSQFFDHPAS 230
Cdd:COG3839 153 KVFLLDEPLSNLDAKLRVEMRAEIKRLHRRlGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGTPEELYDRPAN 227
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
3-242 |
8.51e-64 |
|
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: 198.93 E-value: 8.51e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 3 LEITQLEKAYNKQKVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVPLIFEEKQLRQHrlkLGI 82
Cdd:COG4555 2 IEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQ---IGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 83 LFQSWNLFPHLTALENISLpLYRVHGYSKEDADSQAMTLLNRFELAKHAHKKPAELSGGQCQRVAIIRAIAIQPSMLLFD 162
Cdd:COG4555 79 LPDERGLYDRLTVRENIRY-FAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 163 EPTSALDPLMTSEVLDLIVELKKEGKQFIIVTHHISFARKICDWILFLSEGKVLDSKPTSQFFDHPASPEIQYYLEQVLK 242
Cdd:COG4555 158 EPTNGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREEIGEENLEDAFVALIG 237
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
3-215 |
6.87e-63 |
|
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: 196.19 E-value: 6.87e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 3 LEITQLEKAY----NKQKVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVPLI-FEEKQLRQHR 77
Cdd:cd03257 2 LEVKNLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLkLSRRLRKIRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 78 LKLGILFQ----SWNlfPHLTALENISLPLYRVHGYSKEDADSQAMTL-LNRFELAK-HAHKKPAELSGGQCQRVAIIRA 151
Cdd:cd03257 82 KEIQMVFQdpmsSLN--PRMTIGEQIAEPLRIHGKLSKKEARKEAVLLlLVGVGLPEeVLNRYPHELSGGQRQRVAIARA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 503691651 152 IAIQPSMLLFDEPTSALDPLMTSEVLDLIVELKKE-GKQFIIVTHHISFARKICDWILFLSEGKV 215
Cdd:cd03257 160 LALNPKLLIADEPTSALDVSVQAQILDLLKKLQEElGLTLLFITHDLGVVAKIADRVAVMYAGKI 224
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
3-230 |
3.43e-62 |
|
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: 194.38 E-value: 3.43e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 3 LEITQLEKAYNKQKVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVPLIfeekQLRQHRLKLGI 82
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDIT----NLPPHKRPVNT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 83 LFQSWNLFPHLTALENISLPLyRVHGYSKEDADSQAMTLLNRFELAKHAHKKPAELSGGQCQRVAIIRAIAIQPSMLLFD 162
Cdd:cd03300 77 VFQNYALFPHLTVFENIAFGL-RLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLD 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 503691651 163 EPTSALDPLMTSEVLDLIVELKKE-GKQFIIVTHHISFARKICDWILFLSEGKVLDSKPTSQFFDHPAS 230
Cdd:cd03300 156 EPLGALDLKLRKDMQLELKRLQKElGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPAN 224
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
4-214 |
7.09e-62 |
|
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: 193.07 E-value: 7.09e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 4 EITQLEKAYNKQ--KVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVPLifEEKQLRQHRLKLG 81
Cdd:cd03225 1 ELKNLSFSYPDGarPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDL--TKLSLKELRRKVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 82 ILFQ--SWNLFpHLTALENISLPLyRVHGYSKEDADSQAMTLLNRFELAKHAHKKPAELSGGQCQRVAIIRAIAIQPSML 159
Cdd:cd03225 79 LVFQnpDDQFF-GPTVEEEVAFGL-ENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDIL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 503691651 160 LFDEPTSALDPLMTSEVLDLIVELKKEGKQFIIVTHHISFARKICDWILFLSEGK 214
Cdd:cd03225 157 LLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
3-227 |
3.12e-61 |
|
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: 192.51 E-value: 3.12e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 3 LEITQLEKAYNKQK-VLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVPLIFE-EKQLRQHRLKL 80
Cdd:TIGR02315 2 LEVENLSKVYPNGKqALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLrGKKLRKLRRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 81 GILFQSWNLFPHLTALENISLPLYRVHG--------YSKEDADsQAMTLLNRFELAKHAHKKPAELSGGQCQRVAIIRAI 152
Cdd:TIGR02315 82 GMIFQHYNLIERLTVLENVLHGRLGYKPtwrsllgrFSEEDKE-RALSALERVGLADKAYQRADQLSGGQQQRVAIARAL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 503691651 153 AIQPSMLLFDEPTSALDPLMTSEVLDLIVEL-KKEGKQFIIVTHHISFARKICDWILFLSEGKVLDSKPTSQFFDH 227
Cdd:TIGR02315 161 AQQPDLILADEPIASLDPKTSKQVMDYLKRInKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSELDDE 236
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
3-237 |
2.80e-60 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 189.58 E-value: 2.80e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 3 LEITQLEKAYNKQkvLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVPLIfeekQLRQHRLKLGI 82
Cdd:COG3840 2 LRLDDLTYRYGDF--PLRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLT----ALPPAERPVSM 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 83 LFQSWNLFPHLTALENISL---PLYRvhgYSKEDAdSQAMTLLNRFELAKHAHKKPAELSGGQCQRVAIIRAIAIQPSML 159
Cdd:COG3840 76 LFQENNLFPHLTVAQNIGLglrPGLK---LTAEQR-AQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPIL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 503691651 160 LFDEPTSALDPLMTSEVLDLIVELKKE-GKQFIIVTHHISFARKICDWILFLSEGKVLDSKPTSQFFDHPASPEIQYYL 237
Cdd:COG3840 152 LLDEPFSALDPALRQEMLDLVDELCRErGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPPALAAYL 230
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
3-215 |
1.04e-59 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 186.06 E-value: 1.04e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 3 LEITQLEKAYNKQKVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVPLIFEEKQLRQHrlkLGI 82
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKRR---IGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 83 LFQSWNLFPHLTALENIslplyrvhgyskedadsqamtllnrfelakhahkkpaELSGGQCQRVAIIRAIAIQPSMLLFD 162
Cdd:cd03230 78 LPEEPSLYENLTVRENL-------------------------------------KLSGGMKQRLALAQALLHDPELLILD 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 503691651 163 EPTSALDPLMTSEVLDLIVELKKEGKQFIIVTHHISFARKICDWILFLSEGKV 215
Cdd:cd03230 121 EPTSGLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2-237 |
8.57e-58 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 184.08 E-value: 8.57e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 2 KLEITQLEKAYNKQKVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGL--ESPTC---GRVNFDGVPlIFEEK----Q 72
Cdd:COG1117 11 KIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMndLIPGArveGEILLDGED-IYDPDvdvvE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 73 LRQhrlKLGILFQSWNLFPHlTALENISLPLyRVHGY-SKEDADSQAMTLLnrfelaKHAH---------KKPA-ELSGG 141
Cdd:COG1117 90 LRR---RVGMVFQKPNPFPK-SIYDNVAYGL-RLHGIkSKSELDEIVEESL------RKAAlwdevkdrlKKSAlGLSGG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 142 QCQRVAIIRAIAIQPSMLLFDEPTSALDPLMTSEVLDLIVELKkegKQF--IIVTHHISFARKICDWILFLSEGKVLDSK 219
Cdd:COG1117 159 QQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELK---KDYtiVIVTHNMQQAARVSDYTAFFYLGELVEFG 235
|
250
....*....|....*...
gi 503691651 220 PTSQFFDHPASPEIQYYL 237
Cdd:COG1117 236 PTEQIFTNPKDKRTEDYI 253
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
4-231 |
1.01e-57 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 186.55 E-value: 1.01e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 4 EITQLEKAY--NKQKV--LKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVPLI-FEEKQLRQHRL 78
Cdd:PRK11153 3 ELKNISKVFpqGGRTIhaLNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTaLSEKELRKARR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 79 KLGILFQSWNLFPHLTALENISLPLyRVHGYSKEDADSQAMTLLNRFELAKHAHKKPAELSGGQCQRVAIIRAIAIQPSM 158
Cdd:PRK11153 83 QIGMIFQHFNLLSSRTVFDNVALPL-ELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPKV 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 503691651 159 LLFDEPTSALDPLMTSEVLDLIVELKKE-GKQFIIVTHHISFARKICDWILFLSEGKVLDSKPTSQFFDHPASP 231
Cdd:PRK11153 162 LLCDEATSALDPATTRSILELLKDINRElGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHPKHP 235
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
17-222 |
1.69e-57 |
|
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: 182.63 E-value: 1.69e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 17 VLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVPL--IFEEKQLRQHRLKLGILFQSWNLFPHLT 94
Cdd:COG4181 27 ILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLfaLDEDARARLRARHVGFVFQSFQLLPTLT 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 95 ALENISLPLYRVhgySKEDADSQAMTLLNRFELAKHAHKKPAELSGGQCQRVAIIRAIAIQPSMLLFDEPTSALDPlMTS 174
Cdd:COG4181 107 ALENVMLPLELA---GRRDARARARALLERVGLGHRLDHYPAQLSGGEQQRVALARAFATEPAILFADEPTGNLDA-ATG 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 503691651 175 E-VLDLIVELKKE-GKQFIIVTHHISFARKiCDWILFLSEGKVLDSKPTS 222
Cdd:COG4181 183 EqIIDLLFELNRErGTTLVLVTHDPALAAR-CDRVLRLRAGRLVEDTAAT 231
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
3-216 |
2.89e-56 |
|
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: 179.85 E-value: 2.89e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 3 LEITQLEKAYNKQKVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVPLifeeKQLRQHRL--KL 80
Cdd:COG1120 2 LEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDL----ASLSRRELarRI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 81 GILFQSWNLFPHLTALENISLPLY----RVHGYSKEDADsQAMTLLNRFELAKHAHKKPAELSGGQCQRVAIIRAIAIQP 156
Cdd:COG1120 78 AYVPQEPPAPFGLTVRELVALGRYphlgLFGRPSAEDRE-AVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 503691651 157 SMLLFDEPTSALDPLMTSEVLDLIVELKKE-GKQFIIVTHHISFARKICDWILFLSEGKVL 216
Cdd:COG1120 157 PLLLLDEPTSHLDLAHQLEVLELLRRLARErGRTVVMVLHDLNLAARYADRLVLLKDGRIV 217
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
3-216 |
6.46e-56 |
|
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: 178.40 E-value: 6.46e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 3 LEITQLEKAYNKQKVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVPLifeeKQLRQHRL-KLG 81
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDI----TGLPPHEIaRLG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 82 IL--FQSWNLFPHLTALENISLPLYRVHGYS---------KEDADSQAMTLLNRFELAKHAHKKPAELSGGQCQRVAIIR 150
Cdd:cd03219 77 IGrtFQIPRLFPELTVLENVMVAAQARTGSGlllararreEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIAR 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 503691651 151 AIAIQPSMLLFDEPTSALDPLMTSEVLDLIVELKKEGKQFIIVTHHISFARKICDWILFLSEGKVL 216
Cdd:cd03219 157 ALATDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRVI 222
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
3-229 |
7.62e-56 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 178.74 E-value: 7.62e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 3 LEITQLEKAYNKQKVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVPLifeekqlRQHRLKLGI 82
Cdd:COG1121 7 IELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPP-------RRARRRIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 83 LFQS----WNlFPhLTALENISLPLYRVHG----YSKEDADsQAMTLLNRFELAKHAHKKPAELSGGQCQRVAIIRAIAI 154
Cdd:COG1121 80 VPQRaevdWD-FP-ITVRDVVLMGRYGRRGlfrrPSRADRE-AVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQ 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 503691651 155 QPSMLLFDEPTSALDPLMTSEVLDLIVELKKEGKQFIIVTHHISFARKICDWILFLSEGkVLDSKPTSQFFDHPA 229
Cdd:COG1121 157 DPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLLNRG-LVAHGPPEEVLTPEN 230
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
8-242 |
4.11e-55 |
|
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: 177.45 E-value: 4.11e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 8 LEKAYNKQKVLK---------NINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVPLI-FEEKQLRQ-H 76
Cdd:cd03294 21 LAKGKSKEEILKktgqtvgvnDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAaMSRKELRElR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 77 RLKLGILFQSWNLFPHLTALENISLPLyRVHGYSKEDADSQAMTLLNRFELAKHAHKKPAELSGGQCQRVAIIRAIAIQP 156
Cdd:cd03294 101 RKKISMVFQSFALLPHRTVLENVAFGL-EVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDP 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 157 SMLLFDEPTSALDPLMTSEVLDLIVELKKE-GKQFIIVTHHISFARKICDWILFLSEGKVLDSKPTSQFFDHPASPEIQY 235
Cdd:cd03294 180 DILLMDEAFSALDPLIRREMQDELLRLQAElQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDYVRE 259
|
....*..
gi 503691651 236 YLEQVLK 242
Cdd:cd03294 260 FFRGVDR 266
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
3-231 |
8.41e-54 |
|
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: 173.26 E-value: 8.41e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 3 LEITQLEKAYNK-QKVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVPLI-FEEKQLRQhrlKL 80
Cdd:cd03295 1 IEFENVTKRYGGgKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIReQDPVELRR---KI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 81 GILFQSWNLFPHLTALENISLpLYRVHGYSKEDADSQAMTLLN--RFELAKHAHKKPAELSGGQCQRVAIIRAIAIQPSM 158
Cdd:cd03295 78 GYVIQQIGLFPHMTVEENIAL-VPKLLKWPKEKIRERADELLAlvGLDPAEFADRYPHELSGGQQQRVGVARALAADPPL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 503691651 159 LLFDEPTSALDPLMTSEVLDLIVELKKE-GKQFIIVTHHISFARKICDWILFLSEGKVLDSKPTSQFFDHPASP 231
Cdd:cd03295 157 LLMDEPFGALDPITRDQLQEEFKRLQQElGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPAND 230
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1-231 |
2.34e-53 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 172.14 E-value: 2.34e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 1 MKLEITQLEKAYNKQKVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVPLIFEEKQLRQhrlkL 80
Cdd:cd03296 1 MSIEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQERN----V 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 81 GILFQSWNLFPHLTALENISLPL---YRVHGYSKEDADSQAMTLLNRFELAKHAHKKPAELSGGQCQRVAIIRAIAIQPS 157
Cdd:cd03296 77 GFVFQHYALFRHMTVFDNVAFGLrvkPRSERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPK 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 503691651 158 MLLFDEPTSALDPLMTSEVLDLIVELKKE-GKQFIIVTHHISFARKICDWILFLSEGKVLDSKPTSQFFDHPASP 231
Cdd:cd03296 157 VLLLDEPFGALDAKVRKELRRWLRRLHDElHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPASP 231
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
3-215 |
5.43e-52 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 167.69 E-value: 5.43e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 3 LEITQLEKAYNKQKVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVPLifEEKQLRQHRLKLGI 82
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPL--SAMPPPEWRRQVAY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 83 LFQSWNLFPHlTALENISLPL-YRVHGYSKEDADSqamtLLNRFELAKHAHKKPA-ELSGGQCQRVAIIRAIAIQPSMLL 160
Cdd:COG4619 79 VPQEPALWGG-TVRDNLPFPFqLRERKFDRERALE----LLERLGLPPDILDKPVeRLSGGERQRLALIRALLLQPDVLL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 503691651 161 FDEPTSALDPLMTSEVLDLIVEL-KKEGKQFIIVTHHISFARKICDWILFLSEGKV 215
Cdd:COG4619 154 LDEPTSALDPENTRRVEELLREYlAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-203 |
5.65e-52 |
|
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: 167.66 E-value: 5.65e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 1 MKLEITQLEKAYNKQKVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVPLifeEKQLRQHRLKL 80
Cdd:COG4133 1 MMLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPI---RDAREDYRRRL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 81 GILFQSWNLFPHLTALENISLpLYRVHGYSkeDADSQAMTLLNRFELAKHAHKKPAELSGGQCQRVAIIRAIAIQPSMLL 160
Cdd:COG4133 78 AYLGHADGLKPELTVRENLRF-WAALYGLR--ADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWL 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 503691651 161 FDEPTSALDPLMTSEVLDLIVELKKEGKQFIIVTHH---ISFARKI 203
Cdd:COG4133 155 LDEPFTALDAAGVALLAELIAAHLARGGAVLLTTHQpleLAAARVL 200
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
3-215 |
1.33e-51 |
|
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: 166.66 E-value: 1.33e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 3 LEITQLEKAYNKQKVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVPLIFEEKQLRQhrlkLGI 82
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDRD----IAM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 83 LFQSWNLFPHLTALENISLPLyRVHGYSKEDADSQAMTLLNRFELAKHAHKKPAELSGGQCQRVAIIRAIAIQPSMLLFD 162
Cdd:cd03301 77 VFQNYALYPHMTVYDNIAFGL-KLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 503691651 163 EPTSALDPLMTSEVLDLIVELKKE-GKQFIIVTHHISFARKICDWILFLSEGKV 215
Cdd:cd03301 156 EPLSNLDAKLRVQMRAELKRLQQRlGTTTIYVTHDQVEAMTMADRIAVMNDGQI 209
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
4-214 |
1.52e-51 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 164.73 E-value: 1.52e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 4 EITQLEKAYNKQKVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVPLifEEKQLRQHRLKLGIL 83
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDI--AKLPLEELRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 84 FQswnlfphltalenislplyrvhgyskedadsqamtllnrfelakhahkkpaeLSGGQCQRVAIIRAIAIQPSMLLFDE 163
Cdd:cd00267 79 PQ----------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDE 106
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 503691651 164 PTSALDPLMTSEVLDLIVELKKEGKQFIIVTHHISFARKICDWILFLSEGK 214
Cdd:cd00267 107 PTSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
3-231 |
2.97e-51 |
|
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: 169.08 E-value: 2.97e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 3 LEITQLEKAYNKQ----KVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTC---GRVNFDGVPLI-FEEKQLR 74
Cdd:COG0444 2 LEVRNLKVYFPTRrgvvKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPGitsGEILFDGEDLLkLSEKELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 75 QHRLK-LGILFQ----SWNlfPHLTALENISLPLyRVH-GYSKEDADSQAMTLLNRFEL---AKHAHKKPAELSGGQCQR 145
Cdd:COG0444 82 KIRGReIQMIFQdpmtSLN--PVMTVGDQIAEPL-RIHgGLSKAEARERAIELLERVGLpdpERRLDRYPHELSGGMRQR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 146 VAIIRAIAIQPSMLLFDEPTSALDPLMTSEVLDLIVELKKE-GKQFIIVTHHISFARKICDWILFLSEGKVLDSKPTSQF 224
Cdd:COG0444 159 VMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRElGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGPVEEL 238
|
....*..
gi 503691651 225 FDHPASP 231
Cdd:COG0444 239 FENPRHP 245
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
3-230 |
3.18e-51 |
|
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: 173.94 E-value: 3.18e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 3 LEITQLEKAYNKQ--KVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTC---GRVNFDGVPLIFEEKQLRQHR 77
Cdd:COG1123 5 LEVRDLSVRYPGGdvPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGrisGEVLLDGRDLLELSEALRGRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 78 LklGILFQSW--NLFPhLTALENISLPLyRVHGYSKEDADSQAMTLLNRFELAKHAHKKPAELSGGQCQRVAIIRAIAIQ 155
Cdd:COG1123 85 I--GMVFQDPmtQLNP-VTVGDQIAEAL-ENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALD 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 503691651 156 PSMLLFDEPTSALDPLMTSEVLDLIVELKKE-GKQFIIVTHHISFARKICDWILFLSEGKVLDSKPTSQFFDHPAS 230
Cdd:COG1123 161 PDLLIADEPTTALDVTTQAEILDLLRELQRErGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAPQA 236
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1-230 |
1.06e-50 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 168.72 E-value: 1.06e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 1 MKLEITQLEKAYNKQKVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVPLifeeKQLRQHRLKL 80
Cdd:PRK10851 1 MSIEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDV----SRLHARDRKV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 81 GILFQSWNLFPHLTALENIS-----LPlyRVHGYSKEDADSQAMTLLNRFELAKHAHKKPAELSGGQCQRVAIIRAIAIQ 155
Cdd:PRK10851 77 GFVFQHYALFRHMTVFDNIAfgltvLP--RRERPNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVE 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 503691651 156 PSMLLFDEPTSALDPLMTSEVLDLIVELKKEGKqF--IIVTHHISFARKICDWILFLSEGKVLDSKPTSQFFDHPAS 230
Cdd:PRK10851 155 PQILLLDEPFGALDAQVRKELRRWLRQLHEELK-FtsVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREPAT 230
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
3-216 |
1.52e-50 |
|
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: 164.22 E-value: 1.52e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 3 LEITQLEKAYNK--QKVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVPLIFEEKQLRQHrlkL 80
Cdd:cd03263 1 LQIRNLTKTYKKgtKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAARQS---L 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 81 GILFQSWNLFPHLTALENisLPLY-RVHGYSKEDADSQAMTLLNRFELAKHAHKKPAELSGGQCQRVAIIRAIAIQPSML 159
Cdd:cd03263 78 GYCPQFDALFDELTVREH--LRFYaRLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 503691651 160 LFDEPTSALDPLMTSEVLDLIVELKKeGKQFIIVTHHISFARKICDWILFLSEGKVL 216
Cdd:cd03263 156 LLDEPTSGLDPASRRAIWDLILEVRK-GRSIILTTHSMDEAEALCDRIAIMSDGKLR 211
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
4-210 |
2.13e-50 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 163.86 E-value: 2.13e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 4 EITQLEKAYNKQKVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVPLifeekqlRQHRLKLGIL 83
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPL-------EKERKRIGYV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 84 FQSWNL---FPhLTALENISLPLYR----VHGYSKEDADsQAMTLLNRFELAKHAHKKPAELSGGQCQRVAIIRAIAIQP 156
Cdd:cd03235 74 PQRRSIdrdFP-ISVRDVVLMGLYGhkglFRRLSKADKA-KVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDP 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 503691651 157 SMLLFDEPTSALDPLMTSEVLDLIVELKKEGKQFIIVTHHISFARKICDWILFL 210
Cdd:cd03235 152 DLLLLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRVLLL 205
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
3-214 |
1.16e-49 |
|
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: 162.03 E-value: 1.16e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 3 LEITQLEKAYNKQ-KVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVPLI-FEEKQLRQHRLKL 80
Cdd:TIGR02673 2 IEFHNVSKAYPGGvAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNrLRGRQLPLLRRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 81 GILFQSWNLFPHLTALENISLPLyRVHGYSKEDADSQAMTLLNRFELAKHAHKKPAELSGGQCQRVAIIRAIAIQPSMLL 160
Cdd:TIGR02673 82 GVVFQDFRLLPDRTVYENVALPL-EVRGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPPLLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 503691651 161 FDEPTSALDPLMTSEVLDLIVELKKEGKQFIIVTHHISFARKICDWILFLSEGK 214
Cdd:TIGR02673 161 ADEPTGNLDPDLSERILDLLKRLNKRGTTVIVATHDLSLVDRVAHRVIILDDGR 214
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
18-166 |
6.79e-49 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 157.81 E-value: 6.79e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 18 LKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVPLIFEEkqLRQHRLKLGILFQSWNLFPHLTALE 97
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDE--RKSLRKEIGYVFQDPQLFPRLTVRE 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503691651 98 NISLPLyRVHGYSKEDADSQAMTLLNRFEL----AKHAHKKPAELSGGQCQRVAIIRAIAIQPSMLLFDEPTS 166
Cdd:pfam00005 79 NLRLGL-LLKGLSKREKDARAEEALEKLGLgdlaDRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
3-229 |
8.86e-49 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 160.15 E-value: 8.86e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 3 LEITQLEKAYNKQKVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVPLIfeekQLRQHRL-KLG 81
Cdd:COG0410 4 LEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDIT----GLPPHRIaRLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 82 ILF--QSWNLFPHLTALENISLPLYRVHGYSKEDADSQAMtlLNRF-ELAKHAHKKPAELSGGQCQRVAIIRAIAIQPSM 158
Cdd:COG0410 80 IGYvpEGRRIFPSLTVEENLLLGAYARRDRAEVRADLERV--YELFpRLKERRRQRAGTLSGGEQQMLAIGRALMSRPKL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 503691651 159 LLFDEPTSALDPLMTSEVLDLIVELKKEGKQFIIVTHHISFARKICDWILFLSEGKVLDSKPTSQFFDHPA 229
Cdd:COG0410 158 LLLDEPSLGLAPLIVEEIFEIIRRLNREGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLADPE 228
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
15-216 |
1.20e-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: 159.38 E-value: 1.20e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 15 QKVLKNINLSIP---EAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVPLIFEEKQ--LRQHRLKLGILFQSWNL 89
Cdd:cd03297 7 EKRLPDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRKKinLPPQQRKIGLVFQQYAL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 90 FPHLTALENISLPLYRVHgySKEDADsQAMTLLNRFELAKHAHKKPAELSGGQCQRVAIIRAIAIQPSMLLFDEPTSALD 169
Cdd:cd03297 87 FPHLNVRENLAFGLKRKR--NREDRI-SVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALD 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 503691651 170 PLMTSEvldLIVELKKEGKQF----IIVTHHISFARKICDWILFLSEGKVL 216
Cdd:cd03297 164 RALRLQ---LLPELKQIKKNLnipvIFVTHDLSEAEYLADRIVVMEDGRLQ 211
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
3-218 |
1.23e-48 |
|
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: 158.92 E-value: 1.23e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 3 LEITQLEKAYNKQKVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVPLIFEEKQLRQhrlkLGI 82
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALRR----IGA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 83 LFQSWNLFPHLTALENISLpLYRVHGYSKEDADSqamtLLNRFELAKHAHKKPAELSGGQCQRVAIIRAIAIQPSMLLFD 162
Cdd:cd03268 77 LIEAPGFYPNLTARENLRL-LARLLGIRKKRIDE----VLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILD 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 503691651 163 EPTSALDPLMTSEVLDLIVELKKEGKQFIIVTHHISFARKICDWILFLSEGKVLDS 218
Cdd:cd03268 152 EPTNGLDPDGIKELRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKLIEE 207
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
33-230 |
1.84e-48 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 162.28 E-value: 1.84e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 33 LLGPSGSGKSTLLRILAGLESPTCGRVNFDGVPLIfeekQLRQHRLKLGILFQSWNLFPHLTALENISLPLyRVHGYSKE 112
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVT----NVPPHLRHINMVFQSYALFPHMTVEENVAFGL-KMRKVPRA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 113 DADSQAMTLLNRFELAKHAHKKPAELSGGQCQRVAIIRAIAIQPSMLLFDEPTSALD----PLMTSEVLDLIVELkkeGK 188
Cdd:TIGR01187 76 EIKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDkklrDQMQLELKTIQEQL---GI 152
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 503691651 189 QFIIVTHHISFARKICDWILFLSEGKVLDSKPTSQFFDHPAS 230
Cdd:TIGR01187 153 TFVFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPAN 194
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
5-210 |
2.95e-48 |
|
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: 158.16 E-value: 2.95e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 5 ITQLEKAYNKQKVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGV--PLIFEEKQLRQHRLKLGI 82
Cdd:TIGR03608 1 LKNISKKFGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQetPPLNSKKASKFRREKLGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 83 LFQSWNLFPHLTALENISLPLYRVHGySKEDADSQAMTLLNRFELAKHAHKKPAELSGGQCQRVAIIRAIAIQPSMLLFD 162
Cdd:TIGR03608 81 LFQNFALIENETVEENLDLGLKYKKL-SKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLILAD 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 503691651 163 EPTSALDPLMTSEVLDLIVELKKEGKQFIIVTHHISFArKICDWILFL 210
Cdd:TIGR03608 160 EPTGSLDPKNRDEVLDLLLELNDEGKTIIIVTHDPEVA-KQADRVIEL 206
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
3-224 |
3.39e-47 |
|
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: 155.67 E-value: 3.39e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 3 LEITQLEKAYNKQKVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVPLIfeekQLRQH-RLKLG 81
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDIT----GLPPHeRARAG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 82 ILF--QSWNLFPHLTALENISLPLYRVHGySKEDADSQAMtlLNRF-ELAKHAHKKPAELSGGQCQRVAIIRAIAIQPSM 158
Cdd:cd03224 77 IGYvpEGRRIFPELTVEENLLLGAYARRR-AKRKARLERV--YELFpRLKERRKQLAGTLSGGEQQMLAIARALMSRPKL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 503691651 159 LLFDEPTSALDPLMTSEVLDLIVELKKEGKQFIIVTHHISFARKICDWILFLSEGKVLDSKPTSQF 224
Cdd:cd03224 154 LLLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAEL 219
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
3-195 |
4.38e-47 |
|
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: 155.26 E-value: 4.38e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 3 LEITQLEKAY-NKQKVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVPLI-FEEKQLRQHRLKL 80
Cdd:cd03292 1 IEFINVTKTYpNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSdLRGRAIPYLRRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 81 GILFQSWNLFPHLTALENISLPLyRVHGYSKEDADSQAMTLLNRFELAKHAHKKPAELSGGQCQRVAIIRAIAIQPSMLL 160
Cdd:cd03292 81 GVVFQDFRLLPDRNVYENVAFAL-EVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILI 159
|
170 180 190
....*....|....*....|....*....|....*
gi 503691651 161 FDEPTSALDPLMTSEVLDLIVELKKEGKQFIIVTH 195
Cdd:cd03292 160 ADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATH 194
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
4-216 |
5.71e-47 |
|
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: 153.75 E-value: 5.71e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 4 EITQLEKAYNKQKVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVPLifEEKQLRQHRLKLGIL 83
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDL--ASLSPKELARKIAYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 84 fqswnlfphltalenislplyrvhgyskedadSQAMTLLNrfeLAKHAHKKPAELSGGQCQRVAIIRAIAIQPSMLLFDE 163
Cdd:cd03214 79 --------------------------------PQALELLG---LAHLADRPFNELSGGERQRVLLARALAQEPPILLLDE 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 503691651 164 PTSALDPLMTSEVLDLIVELKKE-GKQFIIVTHHISFARKICDWILFLSEGKVL 216
Cdd:cd03214 124 PTSHLDIAHQIELLELLRRLARErGKTVVMVLHDLNLAARYADRVILLKDGRIV 177
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
8-215 |
1.12e-46 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 159.11 E-value: 1.12e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 8 LEKAYNKQKVLK---------NINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVPLI-FEEKQLRQHR 77
Cdd:COG4175 24 LDQGKSKDEILEktgqtvgvnDASFDVEEGEIFVIMGLSGSGKSTLVRCLNRLIEPTAGEVLIDGEDITkLSKKELRELR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 78 L-KLGILFQSWNLFPHLTALENISLPLyRVHGYSKEDADSQAMTLLNRFELAKHAHKKPAELSGGQCQRVAIIRAIAIQP 156
Cdd:COG4175 104 RkKMSMVFQHFALLPHRTVLENVAFGL-EIQGVPKAERRERAREALELVGLAGWEDSYPDELSGGMQQRVGLARALATDP 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 503691651 157 SMLLFDEPTSALDPL----MTSEVLDLIVELKKEgkqfII-VTHHISFARKICDWILFLSEGKV 215
Cdd:COG4175 183 DILLMDEAFSALDPLirreMQDELLELQAKLKKT----IVfITHDLDEALRLGDRIAIMKDGRI 242
|
|
| ABC_ATP_DarD |
NF038007 |
darobactin export ABC transporter ATP-binding protein; |
3-195 |
2.48e-46 |
|
darobactin export ABC transporter ATP-binding protein;
Pssm-ID: 411600 [Multi-domain] Cd Length: 218 Bit Score: 153.34 E-value: 2.48e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 3 LEITQLEKAYN----KQKVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDG---VPLIFEEK-QLR 74
Cdd:NF038007 2 LNMQNAEKCYItktiKTKVLNHLNFSVEKGDFVSIMGPSGSGKSTLLNIIGMFDSLDSGSLTLAGkevTNLSYSQKiILR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 75 qhRLKLGILFQSWNLFPHLTALENISLPL-YRvhGYSKEDADSQAMTLLNRFELAKHAHKKPAELSGGQCQRVAIIRAIA 153
Cdd:NF038007 82 --RELIGYIFQSFNLIPHLSIFDNVALPLkYR--GVAKKERIERVNQVLNLFGIDNRRNHKPMQLSGGQQQRVAIARAMV 157
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 503691651 154 IQPSMLLFDEPTSALDPLMTSEVLDLIVELKKEGKQFIIVTH 195
Cdd:NF038007 158 SNPALLLADEPTGNLDSKNARAVLQQLKYINQKGTTIIMVTH 199
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
3-215 |
2.88e-46 |
|
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: 153.21 E-value: 2.88e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 3 LEITQLEKAYNKQKVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVPLIFEekqlrqHRLKLGI 82
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIA------ARNRIGY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 83 LFQSWNLFPHLTALENIsLPLYRVHGYSKEDADSQAMTLLNRFELAKHAHKKPAELSGGQCQRVAIIRAIAIQPSMLLFD 162
Cdd:cd03269 75 LPEERGLYPKMKVIDQL-VYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILD 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 503691651 163 EPTSALDPLMTSEVLDLIVELKKEGKQFIIVTHHISFARKICDWILFLSEGKV 215
Cdd:cd03269 154 EPFSGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRA 206
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
3-203 |
2.90e-46 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 153.82 E-value: 2.90e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 3 LEITQLEKAYNKQK----VLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVPL----IFEEKQLR 74
Cdd:PRK11629 6 LQCDNLCKRYQEGSvqtdVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMsklsSAAKAELR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 75 QHrlKLGILFQSWNLFPHLTALENISLPLYrVHGYSKEDADSQAMTLLNRFELAKHAHKKPAELSGGQCQRVAIIRAIAI 154
Cdd:PRK11629 86 NQ--KLGFIYQFHHLLPDFTALENVAMPLL-IGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVN 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 503691651 155 QPSMLLFDEPTSALDPLMTSEVLDLIVEL-KKEGKQFIIVTHHISFARKI 203
Cdd:PRK11629 163 NPRLVLADEPTGNLDARNADSIFQLLGELnRLQGTAFLVVTHDLQLAKRM 212
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
10-216 |
5.27e-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: 5.27e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 10 KAYNKQKVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVPLIFEEKQLRQhrlKLGILFQSWNL 89
Cdd:TIGR01188 1 KVYGDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVVREPRKVRR---SIGIVPQYASV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 90 FPHLTALENISLpLYRVHGYSKEDADSQAMTLLNRFELaKHAHKKPAE-LSGGQCQRVAIIRAIAIQPSMLLFDEPTSAL 168
Cdd:TIGR01188 78 DEDLTGRENLEM-MGRLYGLPKDEAEERAEELLELFEL-GEAADRPVGtYSGGMRRRLDIAASLIHQPDVLFLDEPTTGL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 503691651 169 DPLMTSEVLDLIVELKKEGKQFIIVTHHISFARKICDWILFLSEGKVL 216
Cdd:TIGR01188 156 DPRTRRAIWDYIRALKEEGVTILLTTHYMEEADKLCDRIAIIDHGRII 203
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
15-234 |
9.44e-46 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 153.69 E-value: 9.44e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 15 QKVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVPLI-FEEKQLRQHRLKLGILFQ----SWNl 89
Cdd:PRK10419 25 QTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAkLNRAQRKAFRRDIQMVFQdsisAVN- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 90 fPHLTALENISLPLYRVHGYSKEDADSQAMTLLNRFELA-KHAHKKPAELSGGQCQRVAIIRAIAIQPSMLLFDEPTSAL 168
Cdd:PRK10419 104 -PRKTVREIIREPLRHLLSLDKAERLARASEMLRAVDLDdSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNL 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 503691651 169 DPLMTSEVLDLIVELKKE-GKQFIIVTHHISFARKICDWILFLSEGKVLDSKPT--SQFFDHPASPEIQ 234
Cdd:PRK10419 183 DLVLQAGVIRLLKKLQQQfGTACLFITHDLRLVERFCQRVMVMDNGQIVETQPVgdKLTFSSPAGRVLQ 251
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
3-214 |
1.38e-45 |
|
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: 149.84 E-value: 1.38e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 3 LEITQLEKAY--NKQKVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVPL-IFEEKQLRQHrlk 79
Cdd:cd03228 1 IEFKNVSFSYpgRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLrDLDLESLRKN--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 80 LGILFQSWNLFpHLTALENIslplyrvhgyskedadsqamtllnrfelakhahkkpaeLSGGQCQRVAIIRAIAIQPSML 159
Cdd:cd03228 78 IAYVPQDPFLF-SGTIRENI--------------------------------------LSGGQRQRIAIARALLRDPPIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 503691651 160 LFDEPTSALDPLMTSEVLDLIVELKKeGKQFIIVTHHISFARKiCDWILFLSEGK 214
Cdd:cd03228 119 ILDEATSALDPETEALILEALRALAK-GKTVIVIAHRLSTIRD-ADRIIVLDDGR 171
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
23-215 |
1.44e-45 |
|
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: 151.49 E-value: 1.44e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 23 LSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVPLIFEEKQLRqhrlKLGILFQSWNLFPHLTALENISLP 102
Cdd:cd03298 19 LTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADR----PVSMLFQENNLFAHLTVEQNVGLG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 103 lyRVHGYSKEDADSQAM-TLLNRFELAKHAHKKPAELSGGQCQRVAIIRAIAIQPSMLLFDEPTSALDPLMTSEVLDLIV 181
Cdd:cd03298 95 --LSPGLKLTAEDRQAIeVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVL 172
|
170 180 190
....*....|....*....|....*....|....*
gi 503691651 182 ELKKE-GKQFIIVTHHISFARKICDWILFLSEGKV 215
Cdd:cd03298 173 DLHAEtKMTVLMVTHQPEDAKRLAQRVVFLDNGRI 207
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
16-231 |
1.62e-45 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 159.08 E-value: 1.62e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 16 KVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLEsPTCGRVNFDGVPLI-FEEKQLRQHRLKLGILFQ----SWNlf 90
Cdd:COG4172 300 KAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLI-PSEGEIRFDGQDLDgLSRRALRPLRRRMQVVFQdpfgSLS-- 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 91 PHLTALENISLPLyRVH--GYSKEDADSQAMTLLNRFEL-AKHAHKKPAELSGGQCQRVAIIRAIAIQPSMLLFDEPTSA 167
Cdd:COG4172 377 PRMTVGQIIAEGL-RVHgpGLSAAERRARVAEALEEVGLdPAARHRYPHEFSGGQRQRIAIARALILEPKLLVLDEPTSA 455
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 503691651 168 LDplMT--SEVLDLIVEL-KKEGKQFIIVTHHISFARKICDWILFLSEGKVLDSKPTSQFFDHPASP 231
Cdd:COG4172 456 LD--VSvqAQILDLLRDLqREHGLAYLFISHDLAVVRALAHRVMVMKDGKVVEQGPTEQVFDAPQHP 520
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
3-215 |
1.78e-45 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 153.73 E-value: 1.78e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 3 LEITQLEKAYNKQKVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVPLIFEekqlrqHRLKLGI 82
Cdd:COG4152 2 LELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPE------DRRRIGY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 83 LFQSWNLFPHLTALENIslpLY--RVHGYSKEDADSQAMTLLNRFELAKHAHKKPAELSGGQCQRVAIIRAIAIQPSMLL 160
Cdd:COG4152 76 LPEERGLYPKMKVGEQL---VYlaRLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLI 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 503691651 161 FDEPTSALDPLMTSEVLDLIVELKKEGKQFIIVTHHISFARKICDWILFLSEGKV 215
Cdd:COG4152 153 LDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQMELVEELCDRIVIINKGRK 207
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
3-215 |
2.31e-45 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 155.49 E-value: 2.31e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 3 LEITQLEKAYNKQKVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVPLIFEEKQLRQhrlkLGI 82
Cdd:PRK09452 15 VELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAENRH----VNT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 83 LFQSWNLFPHLTALENISLPLyRVHGYSKEDADSQAMTLLNRFELAKHAHKKPAELSGGQCQRVAIIRAIAIQPSMLLFD 162
Cdd:PRK09452 91 VFQSYALFPHMTVFENVAFGL-RMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLD 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 503691651 163 EPTSALD----PLMTSEVLDLIVELkkeGKQFIIVTHHISFARKICDWILFLSEGKV 215
Cdd:PRK09452 170 ESLSALDyklrKQMQNELKALQRKL---GITFVFVTHDQEEALTMSDRIVVMRDGRI 223
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
3-230 |
3.98e-45 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 154.99 E-value: 3.98e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 3 LEITQLEKAYNKQKVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVPLifeeKQLRQHRLKLGI 82
Cdd:PRK11607 20 LEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDL----SHVPPYQRPINM 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 83 LFQSWNLFPHLTALENISLPLyRVHGYSKEDADSQAMTLLNRFELAKHAHKKPAELSGGQCQRVAIIRAIAIQPSMLLFD 162
Cdd:PRK11607 96 MFQSYALFPHMTVEQNIAFGL-KQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLD 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503691651 163 EPTSALDP----LMTSEVLDLiveLKKEGKQFIIVTHHISFARKICDWILFLSEGKVLDSKPTSQFFDHPAS 230
Cdd:PRK11607 175 EPMGALDKklrdRMQLEVVDI---LERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTT 243
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
3-230 |
4.84e-45 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 154.11 E-value: 4.84e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 3 LEITQLEKAYNKQKVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVPLIFEEKQLRQhrlkLGI 82
Cdd:PRK11432 7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQRD----ICM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 83 LFQSWNLFPHLTALENISLPLyRVHGYSKEDADSQAMTLLNRFELAKHAHKKPAELSGGQCQRVAIIRAIAIQPSMLLFD 162
Cdd:PRK11432 83 VFQSYALFPHMSLGENVGYGL-KMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFD 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503691651 163 EPTSALDPLMTSEVLDLIVELKkegKQFII----VTHHISFARKICDWILFLSEGKVLDSKPTSQFFDHPAS 230
Cdd:PRK11432 162 EPLSNLDANLRRSMREKIRELQ---QQFNItslyVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPAS 230
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
3-216 |
1.05e-44 |
|
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: 148.88 E-value: 1.05e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 3 LEITQLEKAYNKQKVLKNINLSIPEAQsLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVPLIFEEKQLRQHrlkLGI 82
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPGM-YGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRR---IGY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 83 LFQSWNLFPHLTALENISLpLYRVHGYSKEDADSQAMTLLNRFELAKHAHKKPAELSGGQCQRVAIIRAIAIQPSMLLFD 162
Cdd:cd03264 77 LPQEFGVYPNFTVREFLDY-IAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 503691651 163 EPTSALDPLMTSEVLDLIVELkKEGKQFIIVTHHISFARKICDWILFLSEGKVL 216
Cdd:cd03264 156 EPTAGLDPEERIRFRNLLSEL-GEDRIVILSTHIVEDVESLCNQVAVLNKGKLV 208
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
3-241 |
1.73e-44 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 149.99 E-value: 1.73e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 3 LEITQLEKAYNKQKVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGL-----ESPTCGRVNFDGVPLIFEEKQLRQHR 77
Cdd:PRK14267 5 IETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLlelneEARVEGEVRLFGRNIYSPDVDPIEVR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 78 LKLGILFQSWNLFPHLTALENISLPLyRVHGY--SKEDADSQAMTLLNRF----ELAKHAHKKPAELSGGQCQRVAIIRA 151
Cdd:PRK14267 85 REVGMVFQYPNPFPHLTIYDNVAIGV-KLNGLvkSKKELDERVEWALKKAalwdEVKDRLNDYPSNLSGGQRQRLVIARA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 152 IAIQPSMLLFDEPTSALDPLMTSEVLDLIVELKKEgKQFIIVTHHISFARKICDWILFLSEGKVLDSKPTSQFFDHPASP 231
Cdd:PRK14267 164 LAMKPKILLMDEPTANIDPVGTAKIEELLFELKKE-YTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENPEHE 242
|
250
....*....|
gi 503691651 232 EIQYYLEQVL 241
Cdd:PRK14267 243 LTEKYVTGAL 252
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
20-229 |
1.74e-44 |
|
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: 152.56 E-value: 1.74e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 20 NINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVPLiFEEKQ---LRQHRLKLGILFQSWNLFPHLTAL 96
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVL-QDSARgifLPPHRRRIGYVFQEARLFPHLSVR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 97 ENIslpLYrvhGYSKEDADS------QAMTLLnrfELAKHAHKKPAELSGGQCQRVAIIRAIAIQPSMLLFDEPTSALDP 170
Cdd:COG4148 96 GNL---LY---GRKRAPRAErrisfdEVVELL---GIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 171 LMTSEVLDLIVELKKEGKQFII-VTHHISFARKICDWILFLSEGKVLDSKPTSQFFDHPA 229
Cdd:COG4148 167 ARKAEILPYLERLRDELDIPILyVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRPD 226
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
12-239 |
1.80e-44 |
|
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: 150.29 E-value: 1.80e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 12 YNK-----QKVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVPLIFEEK-QLRQHRLKLGILFQ 85
Cdd:TIGR04521 10 YQPgtpfeKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKkKLKDLRKKVGLVFQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 86 swnlFPH-----LTALENISL-PlyRVHGYSKEDADSQAMTLLNRFELAKH-AHKKPAELSGGQCQRVAIIRAIAIQPSM 158
Cdd:TIGR04521 90 ----FPEhqlfeETVYKDIAFgP--KNLGLSEEEAEERVKEALELVGLDEEyLERSPFELSGGQMRRVAIAGVLAMEPEV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 159 LLFDEPTSALDPLMTSEVLDLIVELKKE-GKQFIIVTHHISFARKICDWILFLSEGKVLDSKPTSQFFDH---------- 227
Cdd:TIGR04521 164 LILDEPTAGLDPKGRKEILDLFKRLHKEkGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVFSDvdelekigld 243
|
250
....*....|...
gi 503691651 228 -PASPEIQYYLEQ 239
Cdd:TIGR04521 244 vPEITELARKLKE 256
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
3-237 |
2.05e-44 |
|
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: 148.85 E-value: 2.05e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 3 LEITQLEKAYNKQKVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVPLifeeKQLRQH---RLK 79
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDI----TKLPMHkraRLG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 80 LGILFQSWNLFPHLTALENISLPLyRVHGYSKEDADSQAMTLLNRFELAKHAHKKPAELSGGQCQRVAIIRAIAIQPSML 159
Cdd:cd03218 77 IGYLPQEASIFRKLTVEENILAVL-EIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 503691651 160 LFDEPTSALDPLMTSEVLDLIVELKKEGKQFIIVTHHISFARKICDWILFLSEGKVLDSKPTSQFFdhpASPEI-QYYL 237
Cdd:cd03218 156 LLDEPFAGVDPIAVQDIQKIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIA---ANELVrKVYL 231
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
20-231 |
5.53e-44 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 150.65 E-value: 5.53e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 20 NINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVPLI-FEEKQLRQHRLKLGILFQ----SWNlfPHLT 94
Cdd:COG4608 36 GVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITgLSGRELRPLRRRMQMVFQdpyaSLN--PRMT 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 95 ALENISLPLyRVHG-YSKEDADSQAMTLLNRFEL-AKHAHKKPAELSGGQCQRVAIIRAIAIQPSMLLFDEPTSALDPLM 172
Cdd:COG4608 114 VGDIIAEPL-RIHGlASKAERRERVAELLELVGLrPEHADRYPHEFSGGQRQRIGIARALALNPKLIVCDEPVSALDVSI 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 173 TSEVLDLIVELKKE-GKQFIIVTHHISFARKICDWILFLSEGKVLDSKPTSQFFDHPASP 231
Cdd:COG4608 193 QAQVLNLLEDLQDElGLTYLFISHDLSVVRHISDRVAVMYLGKIVEIAPRDELYARPLHP 252
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
3-239 |
7.69e-44 |
|
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: 148.35 E-value: 7.69e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 3 LEITQLEKAY--NKQKVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVPLIfEEKQLRQHRLKL 80
Cdd:TIGR04520 1 IEVENVSFSYpeSEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTL-DEENLWEIRKKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 81 GILFQSW-NLFPHLT-------ALENISLPL----YRVhgyskEDAdsqamtlLNRFELAKHAHKKPAELSGGQCQRVAI 148
Cdd:TIGR04520 80 GMVFQNPdNQFVGATveddvafGLENLGVPReemrKRV-----DEA-------LKLVGMEDFRDREPHLLSGGQKQRVAI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 149 IRAIAIQPSMLLFDEPTSALDPLMTSEVLDLIVELKKE-GKQFIIVTHHISFARKiCDWILFLSEGKVLDSKPTSQFF-- 225
Cdd:TIGR04520 148 AGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEeGITVISITHDMEEAVL-ADRVIVMNKGKIVAEGTPREIFsq 226
|
250 260
....*....|....*....|...
gi 503691651 226 ---------DHPASPEIQYYLEQ 239
Cdd:TIGR04520 227 vellkeiglDVPFITELAKALKK 249
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
3-217 |
2.06e-43 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 147.13 E-value: 2.06e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 3 LEITQLEKAYNKQKVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVPLIFEEKQLRqhrlklgI 82
Cdd:PRK11247 13 LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEAREDTR-------L 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 83 LFQSWNLFPHLTALENISLPLyrvhgysKEDADSQAMTLLNRFELAKHAHKKPAELSGGQCQRVAIIRAIAIQPSMLLFD 162
Cdd:PRK11247 86 MFQDARLLPWKKVIDNVGLGL-------KGQWRDAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLD 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 503691651 163 EPTSALDPLMTSEVLDLIVEL-KKEGKQFIIVTHHISFARKICDWILFLSEGKV-LD 217
Cdd:PRK11247 159 EPLGALDALTRIEMQDLIESLwQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKIgLD 215
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-211 |
2.23e-43 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 147.32 E-value: 2.23e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 1 MKLEITQLEKAYNK----QKVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVPLifeekqlrQH 76
Cdd:COG4525 2 SMLTVRHVSVRYPGggqpQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPV--------TG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 77 ----RlklGILFQSWNLFPHLTALENISLPLyRVHGYSKEDADSQAMTLLNRFELAKHAHKKPAELSGGQCQRVAIIRAI 152
Cdd:COG4525 74 pgadR---GVVFQKDALLPWLNVLDNVAFGL-RLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARAL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 153 AIQPSMLLFDEPTSALDPLMTSEVLDLIVEL-KKEGKQFIIVTHHISFArkicdwiLFLS 211
Cdd:COG4525 150 AADPRFLLMDEPFGALDALTREQMQELLLDVwQRTGKGVFLITHSVEEA-------LFLA 202
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
3-215 |
2.95e-43 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 146.08 E-value: 2.95e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 3 LEITQLEKAY----NKQKVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVPLI-FEEKQLRQHR 77
Cdd:PRK10584 7 VEVHHLKKSVgqgeHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHqMDEEARAKLR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 78 LK-LGILFQSWNLFPHLTALENISLP-LYRvhGYSKEDADSQAMTLLNRFELAKHAHKKPAELSGGQCQRVAIIRAIAIQ 155
Cdd:PRK10584 87 AKhVGFVFQSFMLIPTLNALENVELPaLLR--GESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGR 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 503691651 156 PSMLLFDEPTSALDPLMTSEVLDLIVELKKE-GKQFIIVTHHISFARKiCDWILFLSEGKV 215
Cdd:PRK10584 165 PDVLFADEPTGNLDRQTGDKIADLLFSLNREhGTTLILVTHDLQLAAR-CDRRLRLVNGQL 224
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-228 |
3.29e-43 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 146.60 E-value: 3.29e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 2 KLEITQLEKAYNKQKVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGL-----ESPTCGRVNFDGVPlIFEeKQLRQH 76
Cdd:PRK14247 3 KIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQD-IFK-MDVIEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 77 RLKLGILFQSWNLFPHLTALENISL--PLYRVHGYSKE--DADSQAMTLLNRFELAKHAHKKPA-ELSGGQCQRVAIIRA 151
Cdd:PRK14247 81 RRRVQMVFQIPNPIPNLSIFENVALglKLNRLVKSKKElqERVRWALEKAQLWDEVKDRLDAPAgKLSGGQQQRLCIARA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 503691651 152 IAIQPSMLLFDEPTSALDPLMTSEVLDLIVELKKEgKQFIIVTHHISFARKICDWILFLSEGKVLDSKPTSQFFDHP 228
Cdd:PRK14247 161 LAFQPEVLLADEPTANLDPENTAKIESLFLELKKD-MTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTNP 236
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
13-220 |
6.48e-43 |
|
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: 154.22 E-value: 6.48e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 13 NKQKVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVPL-IFEEKQLRQHrlkLGILFQSWNLFp 91
Cdd:COG2274 486 DSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLrQIDPASLRRQ---IGVVLQDVFLF- 561
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 92 HLTALENISLplyrvhgySKEDA-DSQAMTLLNRFELAKHAHKKP-----------AELSGGQCQRVAIIRAIAIQPSML 159
Cdd:COG2274 562 SGTIRENITL--------GDPDAtDEEIIEAARLAGLHDFIEALPmgydtvvgeggSNLSGGQRQRLAIARALLRNPRIL 633
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 503691651 160 LFDEPTSALDPLMTSEVLDLIVELKKeGKQFIIVTHHISFARKiCDWILFLSEGKVLDSKP 220
Cdd:COG2274 634 ILDEATSALDAETEAIILENLRRLLK-GRTVIIIAHRLSTIRL-ADRIIVLDKGRIVEDGT 692
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
3-237 |
1.23e-42 |
|
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: 144.40 E-value: 1.23e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 3 LEITQLEKAYNKQKvLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVPLIFEEKQLRQhrlkLGI 82
Cdd:cd03299 1 LKVENLSKDWKEFK-LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEKRD----ISY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 83 LFQSWNLFPHLTALENISLPLyRVHGYSKEDADSQAMTLLNRFELAKHAHKKPAELSGGQCQRVAIIRAIAIQPSMLLFD 162
Cdd:cd03299 76 VPQNYALFPHMTVYKNIAYGL-KKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLD 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 503691651 163 EPTSALDPLmTSEVldLIVELKKEGKQF----IIVTHHISFARKICDWILFLSEGKVLDSKPTSQFFDHPASPEIQYYL 237
Cdd:cd03299 155 EPFSALDVR-TKEK--LREELKKIRKEFgvtvLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPKNEFVAEFL 230
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
3-224 |
2.65e-42 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 149.78 E-value: 2.65e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 3 LEITQLEKAYNKQKVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVPLIFEEkqlRQHRLKLGI 82
Cdd:COG1129 5 LEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRS---PRDAQAAGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 83 --LFQSWNLFPHLTALENISLPLYRVHG----YSKEDADSQAmtLLNRFELAKHAHKKPAELSGGQCQRVAIIRAIAIQP 156
Cdd:COG1129 82 aiIHQELNLVPNLSVAENIFLGREPRRGglidWRAMRRRARE--LLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRDA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 503691651 157 SMLLFDEPTSALDPlmtSEV---LDLIVELKKEGKQFIIVTHHISFARKICDWILFLSEGKVLDSKPTSQF 224
Cdd:COG1129 160 RVLILDEPTASLTE---REVerlFRIIRRLKAQGVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVAEL 227
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
3-218 |
5.75e-42 |
|
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: 142.12 E-value: 5.75e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 3 LEITQLEKAYNKQK----VLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVPLIfeeKQLRQHRL 78
Cdd:cd03266 2 ITADALTKRFRDVKktvqAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVV---KEPAEARR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 79 KLGILFQSWNLFPHLTALENIslpLY--RVHGYSKEDADSQAMTLLNRFELAKHAHKKPAELSGGQCQRVAIIRAIAIQP 156
Cdd:cd03266 79 RLGFVSDSTGLYDRLTARENL---EYfaGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503691651 157 SMLLFDEPTSALDPLMTSEVLDLIVELKKEGKQFIIVTHHISFARKICDWILFLSEGKVLDS 218
Cdd:cd03266 156 PVLLLDEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYE 217
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
14-215 |
6.83e-42 |
|
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: 141.63 E-value: 6.83e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 14 KQKVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVPLifeekQLRQHRLKLGILFQS--WNLFP 91
Cdd:cd03226 12 GTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPI-----KAKERRKSIGYVMQDvdYQLFT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 92 HLTALE-NISLPLYrvhgyskEDADSQAMTLLNRFELAKHAHKKPAELSGGQCQRVAIIRAIAIQPSMLLFDEPTSALDP 170
Cdd:cd03226 87 DSVREElLLGLKEL-------DAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDY 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 503691651 171 LMTSEVLDLIVELKKEGKQFIIVTHHISFARKICDWILFLSEGKV 215
Cdd:cd03226 160 KNMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAI 204
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
13-200 |
5.10e-41 |
|
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: 139.10 E-value: 5.10e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 13 NKQKVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVPLIFEEKQLRQHRLKLGILFQSWN--LF 90
Cdd:TIGR01166 3 GGPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPLDYSRKGLLERRQRVGLVFQDPDdqLF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 91 pHLTALENISLPLyRVHGYSKEDADSQAMTLLNRFELAKHAHKKPAELSGGQCQRVAIIRAIAIQPSMLLFDEPTSALDP 170
Cdd:TIGR01166 83 -AADVDQDVAFGP-LNLGLSEAEVERRVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAGLDP 160
|
170 180 190
....*....|....*....|....*....|
gi 503691651 171 LMTSEVLDLIVELKKEGKQFIIVTHHISFA 200
Cdd:TIGR01166 161 AGREQMLAILRRLRAEGMTVVISTHDVDLA 190
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
3-227 |
1.80e-40 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 139.76 E-value: 1.80e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 3 LEITQLEKAYNKQKVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGL----ESPTCgRVNFDGVPLIFEEK---QLRQ 75
Cdd:PRK09984 5 IRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgdKSAGS-HIELLGRTVQREGRlarDIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 76 HRLKLGILFQSWNLFPHLTALENI------SLPLYRV-HGYSKEDADSQAMTLLNRFELAKHAHKKPAELSGGQCQRVAI 148
Cdd:PRK09984 84 SRANTGYIFQQFNLVNRLSVLENVligalgSTPFWRTcFSWFTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 149 IRAIAIQPSMLLFDEPTSALDPLMTSEVLDLIVELKK-EGKQFIIVTHHISFARKICDWILFLSEGKVLDSKPTSQF--- 224
Cdd:PRK09984 164 ARALMQQAKVILADEPIASLDPESARIVMDTLRDINQnDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQQFdne 243
|
....
gi 503691651 225 -FDH 227
Cdd:PRK09984 244 rFDH 247
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
11-215 |
5.20e-40 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 144.92 E-value: 5.20e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 11 AYNKQK-VLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVPLifeeKQLRQHRL--KLGILFQSW 87
Cdd:COG1132 348 SYPGDRpVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDI----RDLTLESLrrQIGVVPQDT 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 88 NLFpHLTALENIslplyrvhGYSKEDADSQAMtllnrFELAKHAH------KKP-----------AELSGGQCQRVAIIR 150
Cdd:COG1132 424 FLF-SGTIRENI--------RYGRPDATDEEV-----EEAAKAAQahefieALPdgydtvvgergVNLSGGQRQRIAIAR 489
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 503691651 151 AIAIQPSMLLFDEPTSALDPLMTSEVLDLIVELKKeGKQFIIVTHHISFARKiCDWILFLSEGKV 215
Cdd:COG1132 490 ALLKDPPILILDEATSALDTETEALIQEALERLMK-GRTTIVIAHRLSTIRN-ADRILVLDDGRI 552
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
3-215 |
5.38e-40 |
|
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: 135.25 E-value: 5.38e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 3 LEITQLEKAYNKQKVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVPLIFEEkqlRQHRLKLGI 82
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFAS---PRDARRAGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 83 lfqswnlfphltalenislplYRVHgyskedadsqamtllnrfelakhahkkpaELSGGQCQRVAIIRAIAIQPSMLLFD 162
Cdd:cd03216 78 ---------------------AMVY-----------------------------QLSVGERQMVEIARALARNARLLILD 107
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 503691651 163 EPTSALDPLMTSEVLDLIVELKKEGKQFIIVTHHISFARKICDWILFLSEGKV 215
Cdd:cd03216 108 EPTAALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRV 160
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
8-240 |
1.47e-39 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 140.94 E-value: 1.47e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 8 LEKAYNKQKVL---------KNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVPLI-FEEKQLRQ-H 76
Cdd:PRK10070 25 IEQGLSKEQILektglslgvKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAkISDAELREvR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 77 RLKLGILFQSWNLFPHLTALENISLPLyRVHGYSKEDADSQAMTLLNRFELAKHAHKKPAELSGGQCQRVAIIRAIAIQP 156
Cdd:PRK10070 105 RKKIAMVFQSFALMPHMTVLDNTAFGM-ELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINP 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 157 SMLLFDEPTSALDPLMTSEVLDLIVELK-KEGKQFIIVTHHISFARKICDWILFLSEGKVLDSKPTSQFFDHPASPEIQY 235
Cdd:PRK10070 184 DILLMDEAFSALDPLIRTEMQDELVKLQaKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRT 263
|
....*
gi 503691651 236 YLEQV 240
Cdd:PRK10070 264 FFRGV 268
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
3-195 |
3.56e-39 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 134.92 E-value: 3.56e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 3 LEITQLEKAYNKQKVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESP---TCGRVNFDGVPLifeeKQLRQHRLK 79
Cdd:COG4136 2 LSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRL----TALPAEQRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 80 LGILFQSWNLFPHLTALENIS--LPlyrvHGYSKEDADSQAMTLLNRFELAKHAHKKPAELSGGQCQRVAIIRAIAIQPS 157
Cdd:COG4136 78 IGILFQDDLLFPHLSVGENLAfaLP----PTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPR 153
|
170 180 190
....*....|....*....|....*....|....*....
gi 503691651 158 MLLFDEPTSALDPLMTSEVLDLIVE-LKKEGKQFIIVTH 195
Cdd:COG4136 154 ALLLDEPFSKLDAALRAQFREFVFEqIRQRGIPALLVTH 192
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-237 |
6.57e-39 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 134.77 E-value: 6.57e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 1 MKLEITQLEKAYNKQKVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVPL----IFEekqlrqh 76
Cdd:COG1137 2 MTLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDIthlpMHK------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 77 RLKLGI--LFQSWNLFPHLTALENISLPLyRVHGYSKEDADSQAMTLLNRFELAKHAHKKPAELSGGQCQRVAIIRAIAI 154
Cdd:COG1137 75 RARLGIgyLPQEASIFRKLTVEDNILAVL-ELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALAT 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 155 QPSMLLFDEPTSALDPLMTSEVLDLIVELKKEGKQFIIVTHHISFARKICDWILFLSEGKVLDSKPTSQFFDHPASpeIQ 234
Cdd:COG1137 154 NPKFILLDEPFAGVDPIAVADIQKIIRHLKERGIGVLITDHNVRETLGICDRAYIISEGKVLAEGTPEEILNNPLV--RK 231
|
...
gi 503691651 235 YYL 237
Cdd:COG1137 232 VYL 234
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
3-237 |
9.62e-39 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 134.90 E-value: 9.62e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 3 LEITQLEKAYNKQKVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGL-----ESPTCGRVNFDGVPLIFEEKQLRQHR 77
Cdd:PRK14239 6 LQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndlnpEVTITGSIVYNGHNIYSPRTDTVDLR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 78 LKLGILFQSWNLFPhLTALENISLPLyRVHG-YSKEDADSQAMTLLNRF----ELAKHAHKKPAELSGGQCQRVAIIRAI 152
Cdd:PRK14239 86 KEIGMVFQQPNPFP-MSIYENVVYGL-RLKGiKDKQVLDEAVEKSLKGAsiwdEVKDRLHDSALGLSGGQQQRVCIARVL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 153 AIQPSMLLFDEPTSALDPLMTSEVLDLIVELKKEgKQFIIVTHHISFARKICDWILFLSEGKVLDSKPTSQFFDHPASPE 232
Cdd:PRK14239 164 ATSPKIILLDEPTSALDPISAGKIEETLLGLKDD-YTMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQMFMNPKHKE 242
|
....*
gi 503691651 233 IQYYL 237
Cdd:PRK14239 243 TEDYI 247
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
18-213 |
2.60e-38 |
|
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: 133.36 E-value: 2.60e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 18 LKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGvplifeeKQLRQHRLKLGILFQSWNLFPHLTALE 97
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEG-------KQITEPGPDRMVVFQNYSLLPWLTVRE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 98 NISLPLYRV-HGYSKEDADSQAMTLLNRFELAKHAHKKPAELSGGQCQRVAIIRAIAIQPSMLLFDEPTSALDPLMTSEV 176
Cdd:TIGR01184 74 NIALAVDRVlPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNL 153
|
170 180 190
....*....|....*....|....*....|....*...
gi 503691651 177 LDLIVELKKE-GKQFIIVTHHISFARKICDWILFLSEG 213
Cdd:TIGR01184 154 QEELMQIWEEhRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
3-215 |
2.65e-38 |
|
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: 132.91 E-value: 2.65e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 3 LEITQLEKAYNKQKVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVPliFEEKQLRqhrlKLGI 82
Cdd:TIGR03740 1 LETKNLSKRFGKQTAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGHP--WTRKDLH----KIGS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 83 LFQSWNLFPHLTALENIslplyRVHGYSKEDADSQAMTLLNRFELAKHAHKKPAELSGGQCQRVAIIRAIAIQPSMLLFD 162
Cdd:TIGR03740 75 LIESPPLYENLTARENL-----KVHTTLLGLPDSRIDEVLNIVDLTNTGKKKAKQFSLGMKQRLGIAIALLNHPKLLILD 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 503691651 163 EPTSALDPLMTSEVLDLIVELKKEGKQFIIVTHHISFARKICDWILFLSEGKV 215
Cdd:TIGR03740 150 EPTNGLDPIGIQELRELIRSFPEQGITVILSSHILSEVQQLADHIGIISEGVL 202
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
3-237 |
2.67e-38 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 134.02 E-value: 2.67e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 3 LEITQLEKAYNKQKVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVPLIFEEKQLRQHRLKL-- 80
Cdd:PRK14246 11 FNISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYFGKDIFQIDAIKLrk 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 81 --GILFQSWNLFPHLTALENISLPLyRVHGYSKEDADSQAMT-LLNRFELAKHAHKK---PA-ELSGGQCQRVAIIRAIA 153
Cdd:PRK14246 91 evGMVFQQPNPFPHLSIYDNIAYPL-KSHGIKEKREIKKIVEeCLRKVGLWKEVYDRlnsPAsQLSGGQQQRLTIARALA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 154 IQPSMLLFDEPTSALDPLMTSEVLDLIVELKKEgKQFIIVTHHISFARKICDWILFLSEGKVLDSKPTSQFFDHPASPEI 233
Cdd:PRK14246 170 LKPKVLLMDEPTSMIDIVNSQAIEKLITELKNE-IAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNELT 248
|
....
gi 503691651 234 QYYL 237
Cdd:PRK14246 249 EKYV 252
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
13-215 |
3.66e-38 |
|
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: 131.18 E-value: 3.66e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 13 NKQKVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVPL-IFEEKQLRQHrlkLGILFQSWNLFP 91
Cdd:cd03246 13 AEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADIsQWDPNELGDH---VGYLPQDDELFS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 92 HlTALENIslplyrvhgyskedadsqamtllnrfelakhahkkpaeLSGGQCQRVAIIRAIAIQPSMLLFDEPTSALDPL 171
Cdd:cd03246 90 G-SIAENI--------------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVE 130
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 503691651 172 MTSEVLDLIVELKKEGKQFIIVTHHISFARkICDWILFLSEGKV 215
Cdd:cd03246 131 GERALNQAIAALKAAGATRIVIAHRPETLA-SADRILVLEDGRV 173
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
4-215 |
4.18e-38 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 133.96 E-value: 4.18e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 4 EITQLEKAYNKQK--VLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVPLIFEekQLRQHRLKLG 81
Cdd:PRK13632 9 KVENVSFSYPNSEnnALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKE--NLKEIRKKIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 82 ILFQSW-NLFPHLTA-------LENISLPLYRVHGYSKEDADSQAMTllnrfelaKHAHKKPAELSGGQCQRVAIIRAIA 153
Cdd:PRK13632 87 IIFQNPdNQFIGATVeddiafgLENKKVPPKKMKDIIDDLAKKVGME--------DYLDKEPQNLSGGQKQRVAIASVLA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503691651 154 IQPSMLLFDEPTSALDPLMTSEVLDLIVELKKEGKQFII-VTHHISFARKiCDWILFLSEGKV 215
Cdd:PRK13632 159 LNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLIsITHDMDEAIL-ADKVIVFSEGKL 220
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
3-228 |
1.34e-37 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 132.51 E-value: 1.34e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 3 LEITQLEKAYNK-QKVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVPLIFEEKQLRQHRLKLG 81
Cdd:PRK13639 2 LETRDLKYSYPDgTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSLLEVRKTVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 82 ILFQSWN--LFPHlTALENISL-PLYRvhGYSKEDADSQAMTLLNRFELAKHAHKKPAELSGGQCQRVAIIRAIAIQPSM 158
Cdd:PRK13639 82 IVFQNPDdqLFAP-TVEEDVAFgPLNL--GLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEI 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 159 LLFDEPTSALDPLMTSEVLDLIVELKKEGKQFIIVTHHISFARKICDWILFLSEGKVLDSKPTSQFFDHP 228
Cdd:PRK13639 159 IVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDI 228
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
3-215 |
1.48e-37 |
|
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: 137.98 E-value: 1.48e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 3 LEITQLEKAY--NKQKVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVPL-IFEEKQLRQHrlk 79
Cdd:COG4987 334 LELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLrDLDEDDLRRR--- 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 80 LGILFQSwnlfPHL---TALENISLplyrvhgySKEDA-DSQAMTLLNRFELAKHAHKKP-----------AELSGGQCQ 144
Cdd:COG4987 411 IAVVPQR----PHLfdtTLRENLRL--------ARPDAtDEELWAALERVGLGDWLAALPdgldtwlgeggRRLSGGERR 478
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 503691651 145 RVAIIRAIAIQPSMLLFDEPTSALDPLMTSEVLDLIVELKKeGKQFIIVTHHISFARKiCDWILFLSEGKV 215
Cdd:COG4987 479 RLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALA-GRTVLLITHRLAGLER-MDRILVLEDGRI 547
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
22-215 |
2.99e-37 |
|
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: 129.98 E-value: 2.99e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 22 NLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVplifEEKQLRQHRLKLGILFQSWNLFPHLTALENISL 101
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQ----SHTGLAPYQRPVSMLFQENNLFAHLTVRQNIGL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 102 ---PLYRVHGYSKEDADSQAMTLlnrfELAKHAHKKPAELSGGQCQRVAIIRAIAIQPSMLLFDEPTSALDPLMTSEVLD 178
Cdd:TIGR01277 94 glhPGLKLNAEQQEKVVDAAQQV----GIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLA 169
|
170 180 190
....*....|....*....|....*....|....*...
gi 503691651 179 LIVELKKEGKQ-FIIVTHHISFARKICDWILFLSEGKV 215
Cdd:TIGR01277 170 LVKQLCSERQRtLLMVTHHLSDARAIASQIAVVSQGKI 207
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
1-243 |
3.22e-37 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 132.07 E-value: 3.22e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 1 MKLEITQLEKAYNK-----QKVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFdGVPLIF---EEKQ 72
Cdd:PRK13634 1 MDITFQKVEHRYQYktpfeRRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTI-GERVITagkKNKK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 73 LRQHRLKLGILFQswnlFPHL-----TALENISL-PLYrvHGYSKEDADSQAMTLLNRFEL-AKHAHKKPAELSGGQCQR 145
Cdd:PRK13634 80 LKPLRKKVGIVFQ----FPEHqlfeeTVEKDICFgPMN--FGVSEEDAKQKAREMIELVGLpEELLARSPFELSGGQMRR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 146 VAIIRAIAIQPSMLLFDEPTSALDPLMTSEVLDLIVELKKEGKQFII-VTHHISFARKICDWILFLSEGKVLDSKPTSQF 224
Cdd:PRK13634 154 VAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVlVTHSMEDAARYADQIVVMHKGTVFLQGTPREI 233
|
250 260
....*....|....*....|
gi 503691651 225 FDHPAS-PEIQYYLEQVLKY 243
Cdd:PRK13634 234 FADPDElEAIGLDLPETVKF 253
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
15-238 |
4.19e-37 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 131.04 E-value: 4.19e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 15 QKVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDG--VPLIfEEKQLRQHRLKLGILFQSWNLFPH 92
Cdd:PRK11831 20 RCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGenIPAM-SRSRLYTVRKRMSMLFQSGALFTD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 93 LTALENISLPLYRVHGYSKEDADSQAMTLLNRFELAKHAHKKPAELSGGQCQRVAIIRAIAIQPSMLLFDEPTSALDPLM 172
Cdd:PRK11831 99 MNVFDNVAYPLREHTQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDPIT 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 503691651 173 TSEVLDLIVELKKE-GKQFIIVTHHISFARKICDWILFLSEGKVLdSKPTSQFFDHPASPEIQYYLE 238
Cdd:PRK11831 179 MGVLVKLISELNSAlGVTCVVVSHDVPEVLSIADHAYIVADKKIV-AHGSAQALQANPDPRVRQFLD 244
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
12-228 |
4.88e-37 |
|
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: 130.59 E-value: 4.88e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 12 YNKQKVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPT-----------CGRVNfdgvplIFEekqLRQHrlkL 80
Cdd:COG1119 13 RGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTygndvrlfgerRGGED------VWE---LRKR---I 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 81 GIL--FQSWNLFPHLTALENI------SLPLYRvhGYSKEDADsQAMTLLNRFELAKHAHKKPAELSGGQCQRVAIIRAI 152
Cdd:COG1119 81 GLVspALQLRFPRDETVLDVVlsgffdSIGLYR--EPTDEQRE-RARELLELLGLAHLADRPFGTLSQGEQRRVLIARAL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 153 AIQPSMLLFDEPTSALDPLMTSEVLDLIVELKKEG-KQFIIVTHHISfarKICDWI---LFLSEGK---------VLDSK 219
Cdd:COG1119 158 VKDPELLILDEPTAGLDLGARELLLALLDKLAAEGaPTLVLVTHHVE---EIPPGIthvLLLKDGRvvaagpkeeVLTSE 234
|
....*....
gi 503691651 220 PTSQFFDHP 228
Cdd:COG1119 235 NLSEAFGLP 243
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
3-195 |
9.72e-37 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 136.39 E-value: 9.72e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 3 LEITQLEKAY----NKQKVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCG--RVNFDGVPLIFEEKQLRQH 76
Cdd:PRK10535 5 LELKDIRRSYpsgeEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGtyRVAGQDVATLDADALAQLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 77 RLKLGILFQSWNLFPHLTALENISLP-LYRvhGYSKEDADSQAMTLLNRFELAKHAHKKPAELSGGQCQRVAIIRAIAIQ 155
Cdd:PRK10535 85 REHFGFIFQRYHLLSHLTAAQNVEVPaVYA--GLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNG 162
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 503691651 156 PSMLLFDEPTSALDPLMTSEVLDLIVELKKEGKQFIIVTH 195
Cdd:PRK10535 163 GQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTH 202
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
15-231 |
1.00e-36 |
|
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: 135.20 E-value: 1.00e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 15 QKVLKNINLSIPEAQSLALLGPSGSGKS----TLLRILAGLESPTCGRVNFDGVPLI-FEEKQLRQHR-LKLGILFQ--- 85
Cdd:COG4172 23 VEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLgLSERELRRIRgNRIAMIFQepm 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 86 -SWNlfPHLTALENISLPLyRVH-GYSKEDADSQAMTLLNRFEL---AKHAHKKPAELSGGQCQRVAIIRAIAIQPSMLL 160
Cdd:COG4172 103 tSLN--PLHTIGKQIAEVL-RLHrGLSGAAARARALELLERVGIpdpERRLDAYPHQLSGGQRQRVMIAMALANEPDLLI 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503691651 161 FDEPTSALDPLMTSEVLDLIVELKKE-GKQFIIVTHHISFARKICDWILFLSEGKVLDSKPTSQFFDHPASP 231
Cdd:COG4172 180 ADEPTTALDVTVQAQILDLLKDLQRElGMALLLITHDLGVVRRFADRVAVMRQGEIVEQGPTAELFAAPQHP 251
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
3-215 |
1.24e-36 |
|
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: 128.64 E-value: 1.24e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 3 LEITQLEKAYNKQKVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVPLIFEEKQLRQhrlKLGI 82
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREVRR---RIGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 83 LFQSWNLFPHLTALENISLpLYRVHGYSKEDADSQAMTLLNRFELAKHAHKKPAELSGGQCQRVAIIRAIAIQPSMLLFD 162
Cdd:cd03265 78 VFQDLSVDDELTGWENLYI-HARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLD 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 503691651 163 EPTSALDPLMTSEVLDLIVELKKE-GKQFIIVTHHISFARKICDWILFLSEGKV 215
Cdd:cd03265 157 EPTIGLDPQTRAHVWEYIEKLKEEfGMTILLTTHYMEEAEQLCDRVAIIDHGRI 210
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
13-227 |
1.31e-36 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 130.14 E-value: 1.31e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 13 NKQKVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVPLifEEKQLRQHRLKLGILFQSW-NLFP 91
Cdd:PRK13635 18 AATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVL--SEETVWDVRRQVGMVFQNPdNQFV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 92 HLT-------ALENISLP----LYRVHgyskedadsQAMTLLNRFELAKHahkKPAELSGGQCQRVAIIRAIAIQPSMLL 160
Cdd:PRK13635 96 GATvqddvafGLENIGVPreemVERVD---------QALRQVGMEDFLNR---EPHRLSGGQKQRVAIAGVLALQPDIII 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 503691651 161 FDEPTSALDPLMTSEVLDLIVELKKEGKQFII-VTHHISFARKiCDWILFLSEGKVLDSKPTSQFFDH 227
Cdd:PRK13635 164 LDEATSMLDPRGRREVLETVRQLKEQKGITVLsITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEIFKS 230
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
3-213 |
1.87e-36 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 129.05 E-value: 1.87e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 3 LEITQLEKAYNKQKVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVPLifeeKQLRQHRlklGI 82
Cdd:PRK11248 2 LQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPV----EGPGAER---GV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 83 LFQSWNLFPHLTALENISLPLyRVHGYSKEDADSQAMTLLNRFELAKHAHKKPAELSGGQCQRVAIIRAIAIQPSMLLFD 162
Cdd:PRK11248 75 VFQNEGLLPWRNVQDNVAFGL-QLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLD 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 503691651 163 EPTSALDPLMTSEVLDLIVELKKE-GKQFIIVTHHISFARKICDWILFLSEG 213
Cdd:PRK11248 154 EPFGALDAFTREQMQTLLLKLWQEtGKQVLLITHDIEEAVFMATELVLLSPG 205
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
2-238 |
2.27e-36 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 129.13 E-value: 2.27e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 2 KLEITQLEKAYNKQKVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLES--PTC---GRVNFDGVPLIFEEKQLRQH 76
Cdd:PRK14243 10 VLRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDliPGFrveGKVTFHGKNLYAPDVDPVEV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 77 RLKLGILFQSWNLFPHlTALENISLPLyRVHGYsKEDADSQAMTLLNRFELAKHAHKKPAE----LSGGQCQRVAIIRAI 152
Cdd:PRK14243 90 RRRIGMVFQKPNPFPK-SIYDNIAYGA-RINGY-KGDMDELVERSLRQAALWDEVKDKLKQsglsLSGGQQQRLCIARAI 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 153 AIQPSMLLFDEPTSALDPLMTSEVLDLIVELkKEGKQFIIVTHHISFARKICDWILFLS---------EGKVLDSKPTSQ 223
Cdd:PRK14243 167 AVQPEVILMDEPCSALDPISTLRIEELMHEL-KEQYTIIIVTHNMQQAARVSDMTAFFNveltegggrYGYLVEFDRTEK 245
|
250
....*....|....*
gi 503691651 224 FFDHPASPEIQYYLE 238
Cdd:PRK14243 246 IFNSPQQQATRDYVS 260
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1-216 |
2.70e-36 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 128.59 E-value: 2.70e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 1 MKLEITQLEKAYNKQKVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVPL-IFEEKQLRQHrlk 79
Cdd:PRK11231 1 MTLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPIsMLSSRQLARR--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 80 LGILFQswnlfpHLTALENIS------------LPLY-RVHGYSKEDADsQAMtllNRFELAKHAHKKPAELSGGQCQRV 146
Cdd:PRK11231 78 LALLPQ------HHLTPEGITvrelvaygrspwLSLWgRLSAEDNARVN-QAM---EQTRINHLADRRLTDLSGGQRQRA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 147 AIIRAIAIQPSMLLFDEPTSALDPLMTSEVLDLIVELKKEGKQFIIVTHHISFARKICDWILFLSEGKVL 216
Cdd:PRK11231 148 FLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVM 217
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
10-215 |
3.96e-36 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 130.92 E-value: 3.96e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 10 KAYNKQKVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVPLIFEEKQLRQhrlkLGILFQSWNL 89
Cdd:PRK11000 11 KAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAERG----VGMVFQSYAL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 90 FPHLTALENISLPLyRVHGYSKEDADS---QAMTLLnrfELAKHAHKKPAELSGGQCQRVAIIRAIAIQPSMLLFDEPTS 166
Cdd:PRK11000 87 YPHLSVAENMSFGL-KLAGAKKEEINQrvnQVAEVL---QLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLS 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 503691651 167 ALDPLMTSEVLDLIVEL-KKEGKQFIIVTHHISFARKICDWILFLSEGKV 215
Cdd:PRK11000 163 NLDAALRVQMRIEISRLhKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRV 212
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
3-223 |
1.03e-35 |
|
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: 126.49 E-value: 1.03e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 3 LEITQLEKAYNKQKVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVPLifeEKQLRQHRLKLGI 82
Cdd:TIGR03410 1 LEVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDI---TKLPPHERARAGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 83 LF--QSWNLFPHLTALENISLPLYRVHGYSKEDADSqamtLLNRFE-LAKHAHKKPAELSGGQCQRVAIIRAIAIQPSML 159
Cdd:TIGR03410 78 AYvpQGREIFPRLTVEENLLTGLAALPRRSRKIPDE----IYELFPvLKEMLGRRGGDLSGGQQQQLAIARALVTRPKLL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 503691651 160 LFDEPTSALDPLMTSEVLDLIVELKKEGKQFII-VTHHISFARKICDWILFLSEGKVLDSKPTSQ 223
Cdd:TIGR03410 154 LLDEPTEGIQPSIIKDIGRVIRRLRAEGGMAILlVEQYLDFARELADRYYVMERGRVVASGAGDE 218
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1-224 |
1.28e-35 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 127.86 E-value: 1.28e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 1 MKLEITQLEKAYNK-----QKVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVPLIFEEKQLRQ 75
Cdd:PRK13637 1 MSIKIENLTHIYMEgtpfeKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKLSD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 76 HRLKLGILFQ--SWNLFPHlTALENISLPLYRVhGYSKEDADS---QAMTLLNrFELAKHAHKKPAELSGGQCQRVAIIR 150
Cdd:PRK13637 81 IRKKVGLVFQypEYQLFEE-TIEKDIAFGPINL-GLSEEEIENrvkRAMNIVG-LDYEDYKDKSPFELSGGQKRRVAIAG 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 503691651 151 AIAIQPSMLLFDEPTSALDPLMTSEVLDLIVELKKEGKQFII-VTHHISFARKICDWILFLSEGKV-LDSKPTSQF 224
Cdd:PRK13637 158 VVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIIlVSHSMEDVAKLADRIIVMNKGKCeLQGTPREVF 233
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
3-218 |
1.51e-35 |
|
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: 132.57 E-value: 1.51e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 3 LEITQLEKAY-NKQKVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVPLI-FEEKQLRQHrlkL 80
Cdd:COG4988 337 IELEDVSFSYpGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSdLDPASWRRQ---I 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 81 GILFQSWNLFpHLTALENISLplyrvhgySKEDADSQAM-TLLNRFELAKHAHKKP-----------AELSGGQCQRVAI 148
Cdd:COG4988 414 AWVPQNPYLF-AGTIRENLRL--------GRPDASDEELeAALEAAGLDEFVAALPdgldtplgeggRGLSGGQAQRLAL 484
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 149 IRAIAIQPSMLLFDEPTSALDPLMTSEVLDLIVELKKeGKQFIIVTHHISFARkICDWILFLSEGKVLDS 218
Cdd:COG4988 485 ARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAK-GRTVILITHRLALLA-QADRILVLDDGRIVEQ 552
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
18-216 |
2.13e-35 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 127.27 E-value: 2.13e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 18 LKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVPLIFEEKQLRQHRLKLGILFQSWN--LFPhLTA 95
Cdd:PRK13636 22 LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRKGLMKLRESVGMVFQDPDnqLFS-ASV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 96 LENISLPLYRVhGYSKEDADSQAMTLLNRFELAKHAHKKPAELSGGQCQRVAIIRAIAIQPSMLLFDEPTSALDPLMTSE 175
Cdd:PRK13636 101 YQDVSFGAVNL-KLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSE 179
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 503691651 176 VLDLIVELKKE-GKQFIIVTHHISFARKICDWILFLSEGKVL 216
Cdd:PRK13636 180 IMKLLVEMQKElGLTIIIATHDIDIVPLYCDNVFVMKEGRVI 221
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
21-233 |
2.78e-35 |
|
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: 128.69 E-value: 2.78e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 21 INLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVPLIFEEK--QLRQHRLKLGILFQSWNLFPHLTALEN 98
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKgiFLPPEKRRIGYVFQEARLFPHLSVRGN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 99 ISLPLYRVHGYSKEDADSQAMTLLNRFELAKhahKKPAELSGGQCQRVAIIRAIAIQPSMLLFDEPTSALDPLMTSEVLD 178
Cdd:TIGR02142 96 LRYGMKRARPSERRISFERVIELLGIGHLLG---RLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILP 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 503691651 179 LIVELKKEGKQFII-VTHHISFARKICDWILFLSEGKVLDSKPTSQFFDHPASPEI 233
Cdd:TIGR02142 173 YLERLHAEFGIPILyVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPDLPWL 228
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
2-169 |
3.51e-35 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 128.04 E-value: 3.51e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 2 KLEITQLEKAY-NKQKVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVPLIFEEKQLRqhrlkl 80
Cdd:PRK11650 3 GLKLQAVRKSYdGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPADR------ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 81 GI--LFQSWNLFPHLTALENISLPLyRVHGYSKEDADS---QAMTLLnrfELAKHAHKKPAELSGGQCQRVAIIRAIAIQ 155
Cdd:PRK11650 77 DIamVFQNYALYPHMSVRENMAYGL-KIRGMPKAEIEErvaEAARIL---ELEPLLDRKPRELSGGQRQRVAMGRAIVRE 152
|
170
....*....|....
gi 503691651 156 PSMLLFDEPTSALD 169
Cdd:PRK11650 153 PAVFLFDEPLSNLD 166
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-223 |
6.32e-35 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 130.15 E-value: 6.32e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 1 MKLEITQLEKAYNKQKVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVPLIFEEKQlrqHRLKL 80
Cdd:COG3845 4 PALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPR---DAIAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 81 GI--LFQSWNLFPHLTALENISLPLYRVHG--YSKEDADSQAMTLLNRFELAKHAHKKPAELSGGQCQRVAIIRAIAIQP 156
Cdd:COG3845 81 GIgmVHQHFMLVPNLTVAENIVLGLEPTKGgrLDRKAARARIRELSERYGLDVDPDAKVEDLSVGEQQRVEILKALYRGA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 503691651 157 SMLLFDEPTSALDPLMTSEVLDLIVELKKEGKQFIIVTHHISFARKICDWILFLSEGKVLDSKPTSQ 223
Cdd:COG3845 161 RILILDEPTAVLTPQEADELFEILRRLAAEGKSIIFITHKLREVMAIADRVTVLRRGKVVGTVDTAE 227
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
2-215 |
1.17e-34 |
|
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: 123.47 E-value: 1.17e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 2 KLEITQLEKAYN--KQKVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVPLifeeKQ-----LR 74
Cdd:cd03245 2 RIEFRNVSFSYPnqEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDI----RQldpadLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 75 QHrlkLGILFQSWNLFpHLTALENISLPlyrvHGYSKEDADSQAMTL--LNRFeLAKHAH-------KKPAELSGGQCQR 145
Cdd:cd03245 78 RN---IGYVPQDVTLF-YGTLRDNITLG----APLADDERILRAAELagVTDF-VNKHPNgldlqigERGRGLSGGQRQA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503691651 146 VAIIRAIAIQPSMLLFDEPTSALDplMTSEVLdLIVELKK--EGKQFIIVTHHISFArKICDWILFLSEGKV 215
Cdd:cd03245 149 VALARALLNDPPILLLDEPTSAMD--MNSEER-LKERLRQllGDKTLIIITHRPSLL-DLVDRIIVMDSGRI 216
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
15-218 |
2.13e-34 |
|
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: 123.42 E-value: 2.13e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 15 QKVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVPLifEEKQLRQHRLKLGILFQSWNLFPhLT 94
Cdd:cd03249 16 VPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDI--RDLNLRWLRSQIGLVSQEPVLFD-GT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 95 ALENISLPLYRVHGYSKEDADSQA------MTLLNRFElaKHAHKKPAELSGGQCQRVAIIRAIAIQPSMLLFDEPTSAL 168
Cdd:cd03249 93 IAENIRYGKPDATDEEVEEAAKKAnihdfiMSLPDGYD--TLVGERGSQLSGGQKQRIAIARALLRNPKILLLDEATSAL 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 503691651 169 DPLMTSEVLDLIVELKKeGKQFIIVTHHISFARKiCDWILFLSEGKVLDS 218
Cdd:cd03249 171 DAESEKLVQEALDRAMK-GRTTIVIAHRLSTIRN-ADLIAVLQNGQVVEQ 218
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1-229 |
3.42e-34 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 123.34 E-value: 3.42e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 1 MKLEITQLEKAYNKQKVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVPLI-FEEKQLRQHRlk 79
Cdd:PRK13548 1 AMLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLAdWSPAELARRR-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 80 lGILFQSWNL-FPhLTALENISLPLYrVHGYSKEDADSQAMTLLNRFELAKHAHKKPAELSGGQCQRVAIIRAIA----- 153
Cdd:PRK13548 79 -AVLPQHSSLsFP-FTVEEVVAMGRA-PHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAqlwep 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 154 -IQPSMLLFDEPTSALDPLMTSEVLDLIVEL-KKEGKQFIIVTHHISFARKICDWILFLSEGK---------VLDSKPTS 222
Cdd:PRK13548 156 dGPPRWLLLDEPTSALDLAHQHHVLRLARQLaHERGLAVIVVLHDLNLAARYADRIVLLHQGRlvadgtpaeVLTPETLR 235
|
....*..
gi 503691651 223 QFFDHPA 229
Cdd:PRK13548 236 RVYGADV 242
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
3-216 |
7.03e-34 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 122.53 E-value: 7.03e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 3 LEITQLEKAYNKQKVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVPLifeeKQLRQHRL--KL 80
Cdd:COG4559 2 LEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPL----AAWSPWELarRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 81 GILFQSWNL-FPhLTALENISLPLYRVHGYSKEDAD--SQAMTllnRFELAKHAHKKPAELSGGQCQRVAIIRAIA---- 153
Cdd:COG4559 78 AVLPQHSSLaFP-FTVEEVVALGRAPHGSSAAQDRQivREALA---LVGLAHLAGRSYQTLSGGEQQRVQLARVLAqlwe 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 503691651 154 ---IQPSMLLFDEPTSALDPLMTSEVLDLIVELKKEGKQFIIVTHHISFARKICDWILFLSEGKVL 216
Cdd:COG4559 154 pvdGGPRWLFLDEPTSALDLAHQHAVLRLARQLARRGGGVVAVLHDLNLAAQYADRILLLHQGRLV 219
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
11-216 |
2.35e-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: 120.41 E-value: 2.35e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 11 AYN-KQKVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVPLifeeKQLRQH--RLKLGILFQSW 87
Cdd:cd03253 9 AYDpGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDI----REVTLDslRRAIGVVPQDT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 88 NLFpHLTALENIslplyrvhGYSKEDADSQAMtllnrFELAKHAHKKPA-----------------ELSGGQCQRVAIIR 150
Cdd:cd03253 85 VLF-NDTIGYNI--------RYGRPDATDEEV-----IEAAKAAQIHDKimrfpdgydtivgerglKLSGGEKQRVAIAR 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 503691651 151 AIAIQPSMLLFDEPTSALDPLMTSEVLDLIVELKKeGKQFIIVTHHISfarKI--CDWILFLSEGKVL 216
Cdd:cd03253 151 AILKNPPILLLDEATSALDTHTEREIQAALRDVSK-GRTTIVIAHRLS---TIvnADKIIVLKDGRIV 214
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
1-216 |
3.28e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 122.12 E-value: 3.28e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 1 MKLEITQLEKAYNKQ-----KVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNF-------DGVPLIF 68
Cdd:PRK13651 1 MQIKVKNIVKIFNKKlptelKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWifkdeknKKKTKEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 69 EE---------------KQLRQHRLKLGILFQ--SWNLFPHlTALENISL-PlyRVHGYSKEDADSQAMTLLNRFEL-AK 129
Cdd:PRK13651 81 EKvleklviqktrfkkiKKIKEIRRRVGVVFQfaEYQLFEQ-TIEKDIIFgP--VSMGVSKEEAKKRAAKYIELVGLdES 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 130 HAHKKPAELSGGQCQRVAIIRAIAIQPSMLLFDEPTSALDPLMTSEVLDLIVELKKEGKQFIIVTHHISFARKICDWILF 209
Cdd:PRK13651 158 YLQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTKRTIF 237
|
....*..
gi 503691651 210 LSEGKVL 216
Cdd:PRK13651 238 FKDGKII 244
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
18-243 |
5.41e-33 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 120.62 E-value: 5.41e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 18 LKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVPLIF--EEKQLRQHRLKLGILFQswnlFPHL-- 93
Cdd:PRK13649 23 LFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITStsKNKDIKQIRKKVGLVFQ----FPESql 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 94 ---TALENISL-PlyRVHGYSKEDADSQAMTLLNRFELAKHA-HKKPAELSGGQCQRVAIIRAIAIQPSMLLFDEPTSAL 168
Cdd:PRK13649 99 feeTVLKDVAFgP--QNFGVSQEEAEALAREKLALVGISESLfEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGL 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 503691651 169 DPLMTSEVLDLIVELKKEGKQFIIVTHHISFARKICDWILFLSEGK-VLDSKPTSQFFDHPASPEIQYYLEQVLKY 243
Cdd:PRK13649 177 DPKGRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKlVLSGKPKDIFQDVDFLEEKQLGVPKITKF 252
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
3-241 |
5.61e-33 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 125.20 E-value: 5.61e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 3 LEITQLEKAYNKQK-----------VLKNINLSIPEAQSLALLGPSGSGKST----LLRILAglespTCGRVNFDGVPL- 66
Cdd:PRK15134 276 LDVEQLQVAFPIRKgilkrtvdhnvVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLIN-----SQGEIWFDGQPLh 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 67 IFEEKQLRQHRLKLGILFQSWN--LFPHLTALENISLPLyRVH--GYSKEDADSQAMTLLNRFEL-AKHAHKKPAELSGG 141
Cdd:PRK15134 351 NLNRRQLLPVRHRIQVVFQDPNssLNPRLNVLQIIEEGL-RVHqpTLSAAQREQQVIAVMEEVGLdPETRHRYPAEFSGG 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 142 QCQRVAIIRAIAIQPSMLLFDEPTSALDPLMTSEVLDLIVELKKEGK-QFIIVTHHISFARKICDWILFLSEGKVLDSKP 220
Cdd:PRK15134 430 QRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQlAYLFISHDLHVVRALCHQVIVLRQGEVVEQGD 509
|
250 260
....*....|....*....|.
gi 503691651 221 TSQFFDHPAspeiQYYLEQVL 241
Cdd:PRK15134 510 CERVFAAPQ----QEYTRQLL 526
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
17-213 |
6.86e-33 |
|
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: 119.08 E-value: 6.86e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 17 VLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFD----GVPLI-FEEKQ---LRQHRLklGILFQSWN 88
Cdd:COG4778 26 VLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRhdggWVDLAqASPREilaLRRRTI--GYVSQFLR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 89 LFPHLTALENISLPLyRVHGYSKEDADSQAMTLLNRFELAKH-AHKKPAELSGGQCQRVAIIRAIAIQPSMLLFDEPTSA 167
Cdd:COG4778 104 VIPRVSALDVVAEPL-LERGVDREEARARARELLARLNLPERlWDLPPATFSGGEQQRVNIARGFIADPPLLLLDEPTAS 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 503691651 168 LDPLMTSEVLDLIVELKKEGKQFIIVTHHISFARKICDWILFLSEG 213
Cdd:COG4778 183 LDAANRAVVVELIEEAKARGTAIIGIFHDEEVREAVADRVVDVTPF 228
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
22-223 |
1.51e-32 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 118.15 E-value: 1.51e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 22 NLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVPlifeekqlrqHRLK------LGILFQSWNLFPHLTA 95
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQD----------HTTTppsrrpVSMLFQENNLFSHLTV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 96 LENISL---PLYRVHGYSKEDADSQA-----MTLLNRFelakhahkkPAELSGGQCQRVAIIRAIAIQPSMLLFDEPTSA 167
Cdd:PRK10771 89 AQNIGLglnPGLKLNAAQREKLHAIArqmgiEDLLARL---------PGQLSGGQRQRVALARCLVREQPILLLDEPFSA 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 503691651 168 LDPLMTSEVLDLIVELKKEgKQF--IIVTHHISFARKICDWILFLSEGKVLDSKPTSQ 223
Cdd:PRK10771 160 LDPALRQEMLTLVSQVCQE-RQLtlLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDE 216
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
3-220 |
4.80e-32 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 118.75 E-value: 4.80e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 3 LEITQLEKAYNKQKVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVPLifeEKQLRQHRLKLGI 82
Cdd:PRK13537 8 IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPV---PSRARHARQRVGV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 83 LFQSWNLFPHLTALENIsLPLYRVHGYSKEDADSQAMTLLNRFELAKHAHKKPAELSGGQCQRVAIIRAIAIQPSMLLFD 162
Cdd:PRK13537 85 VPQFDNLDPDFTVRENL-LVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLD 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 503691651 163 EPTSALDPLMTSEVLDLIVELKKEGKQFIIVTHHISFARKICDWILFLSEG-KVLDSKP 220
Cdd:PRK13537 164 EPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGrKIAEGAP 222
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-236 |
6.18e-32 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 119.55 E-value: 6.18e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 1 MKLEITQLEKAYNKQKVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVPlifEEKQLRQHRLKL 80
Cdd:PRK13536 40 VAIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVP---VPARARLARARI 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 81 GILFQSWNLFPHLTALENIsLPLYRVHGYSKEDADSQAMTLLNRFELAKHAHKKPAELSGGQCQRVAIIRAIAIQPSMLL 160
Cdd:PRK13536 117 GVVPQFDNLDLEFTVRENL-LVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLI 195
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 503691651 161 FDEPTSALDPLMTSEVLDLIVELKKEGKQFIIVTHHISFARKICDWILFLSEG-KVLDSKPTSQFFDHPASPEIQYY 236
Cdd:PRK13536 196 LDEPTTGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGrKIAEGRPHALIDEHIGCQVIEIY 272
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
14-226 |
8.77e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 117.62 E-value: 8.77e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 14 KQKVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVPLIFE--EKQLRQHRLKLGILFQswnlFP 91
Cdd:PRK13641 19 EKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPEtgNKNLKKLRKKVSLVFQ----FP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 92 HLTALENISL------PlyRVHGYSKEDADSQAMTLLNRFELAKH-AHKKPAELSGGQCQRVAIIRAIAIQPSMLLFDEP 164
Cdd:PRK13641 95 EAQLFENTVLkdvefgP--KNFGFSEDEAKEKALKWLKKVGLSEDlISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEP 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503691651 165 TSALDPLMTSEVLDLIVELKKEGKQFIIVTHHISFARKICDWILFLSEGKVLD-SKPTSQFFD 226
Cdd:PRK13641 173 AAGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKhASPKEIFSD 235
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
14-215 |
1.17e-31 |
|
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: 121.39 E-value: 1.17e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 14 KQKVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVPL-IFEEKQLRQHrlkLGILFQSWNLFPH 92
Cdd:COG4618 344 KRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLsQWDREELGRH---IGYLPQDVELFDG 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 93 lTALENIS-LPlyrvhgyskeDADSQAMtllnrFELAKHA--H----KKP-----------AELSGGQCQRVAIIRAIAI 154
Cdd:COG4618 421 -TIAENIArFG----------DADPEKV-----VAAAKLAgvHemilRLPdgydtrigeggARLSGGQRQRIGLARALYG 484
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 503691651 155 QPSMLLFDEPTSALDPLMTSEVLDLIVELKKEGKQFIIVTHHISFARkICDWILFLSEGKV 215
Cdd:COG4618 485 DPRLVVLDEPNSNLDDEGEAALAAAIRALKARGATVVVITHRPSLLA-AVDKLLVLRDGRV 544
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
16-223 |
1.50e-31 |
|
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: 121.06 E-value: 1.50e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 16 KVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNF----DGVPLIfEEKQLRQHRLK--LGILFQSWNL 89
Cdd:TIGR03269 298 KAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdEWVDMT-KPGPDGRGRAKryIGILHQEYDL 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 90 FPHLTALEN----ISLPL------------YRVHGYSKEDADSqamtLLNRFelakhahkkPAELSGGQCQRVAIIRAIA 153
Cdd:TIGR03269 377 YPHRTVLDNlteaIGLELpdelarmkavitLKMVGFDEEKAEE----ILDKY---------PDELSEGERHRVALAQVLI 443
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 503691651 154 IQPSMLLFDEPTSALDPLMTSEVLDLIVELKKE-GKQFIIVTHHISFARKICDWILFLSEGKVLDSKPTSQ 223
Cdd:TIGR03269 444 KEPRIVILDEPTGTMDPITKVDVTHSILKAREEmEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEE 514
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
3-210 |
2.80e-31 |
|
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: 120.47 E-value: 2.80e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 3 LEITQLEKAY-NKQKVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVPLI-FEEKQLRQHrlkL 80
Cdd:TIGR02857 322 LEFSGVSVAYpGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLAdADADSWRDQ---I 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 81 GILFQSWNLFPHlTALENISlpLYRvhGYSKEDADSQAMTL--LNRFE------LAKHAHKKPAELSGGQCQRVAIIRAI 152
Cdd:TIGR02857 399 AWVPQHPFLFAG-TIAENIR--LAR--PDASDAEIREALERagLDEFVaalpqgLDTPIGEGGAGLSGGQAQRLALARAF 473
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 503691651 153 AIQPSMLLFDEPTSALDPLMTSEVLDLIVELkKEGKQFIIVTHHISFARKiCDWILFL 210
Cdd:TIGR02857 474 LRDAPLLLLDEPTAHLDAETEAEVLEALRAL-AQGRTVLLVTHRLALAAL-ADRIVVL 529
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
3-228 |
4.12e-31 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 115.66 E-value: 4.12e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 3 LEITQLEKAY-------NKQKV--LKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVPLIFEEKQL 73
Cdd:PRK15112 5 LEVRNLSKTFryrtgwfRRQTVeaVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 74 RQHRLKLgiLFQ--SWNLFPHLTALENISLPLYRVHGYSKEDADSQAMTLLNRFEL-AKHAHKKPAELSGGQCQRVAIIR 150
Cdd:PRK15112 85 RSQRIRM--IFQdpSTSLNPRQRISQILDFPLRLNTDLEPEQREKQIIETLRQVGLlPDHASYYPHMLAPGQKQRLGLAR 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 503691651 151 AIAIQPSMLLFDEPTSALDPLMTSEVLDLIVELK-KEGKQFIIVTHHISFARKICDWILFLSEGKVLDSKPTSQFFDHP 228
Cdd:PRK15112 163 ALILRPKVIIADEALASLDMSMRSQLINLMLELQeKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVLASP 241
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
9-226 |
5.58e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 116.49 E-value: 5.58e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 9 EKAYNKQKVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVN----FDGVPLIFEE----------KQLR 74
Cdd:PRK13631 33 EKQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQvgdiYIGDKKNNHElitnpyskkiKNFK 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 75 QHRLKLGILFQ--SWNLFPHlTALENISL-PLyrVHGYSKEDADSQAMTLLNRFEL-AKHAHKKPAELSGGQCQRVAIIR 150
Cdd:PRK13631 113 ELRRRVSMVFQfpEYQLFKD-TIEKDIMFgPV--ALGVKKSEAKKLAKFYLNKMGLdDSYLERSPFGLSGGQKRRVAIAG 189
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 503691651 151 AIAIQPSMLLFDEPTSALDPLMTSEVLDLIVELKKEGKQFIIVTHHISFARKICDWILFLSEGKVLDS-KPTSQFFD 226
Cdd:PRK13631 190 ILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTgTPYEIFTD 266
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
7-215 |
6.19e-31 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 113.82 E-value: 6.19e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 7 QLEKAY-NKQKVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVPLI-FEEKQLRQHRLKLGILF 84
Cdd:PRK10908 6 HVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITrLKNREVPFLRRQIGMIF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 85 QSWNLFPHLTALENISLPLYrVHGYSKEDADSQAMTLLNRFELAKHAHKKPAELSGGQCQRVAIIRAIAIQPSMLLFDEP 164
Cdd:PRK10908 86 QDHHLLMDRTVYDNVAIPLI-IAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEP 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 503691651 165 TSALDPLMTSEVLDLIVELKKEGKQFIIVTHHISFARKICDWILFLSEGKV 215
Cdd:PRK10908 165 TGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
3-237 |
7.96e-31 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 114.75 E-value: 7.96e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 3 LEITQLEKAYNKQKVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGL-----ESPTCGRVNFDGVPLIFEEKQLRQHR 77
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMnelesEVRVEGRVEFFNQNIYERRVNLNRLR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 78 LKLGILFQSWNLFPhLTALENISLPLYRVHGYSKEDADSQAMTLLNRFEL---AKHA-HKKPAELSGGQCQRVAIIRAIA 153
Cdd:PRK14258 88 RQVSMVHPKPNLFP-MSVYDNVAYGVKIVGWRPKLEIDDIVESALKDADLwdeIKHKiHKSALDLSGGQQQRLCIARALA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 154 IQPSMLLFDEPTSALDPLMTSEVLDLIVELKKEGK-QFIIVTHHISFARKICDWILFLSE-----GKVLDSKPTSQFFDH 227
Cdd:PRK14258 167 VKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSElTMVIVSHNLHQVSRLSDFTAFFKGnenriGQLVEFGLTKKIFNS 246
|
250
....*....|
gi 503691651 228 PASPEIQYYL 237
Cdd:PRK14258 247 PHDSRTREYV 256
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
16-231 |
8.92e-31 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 115.96 E-value: 8.92e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 16 KVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVPLI-FEEKQLRQHRLKLGILFQ----SWNlf 90
Cdd:PRK15079 35 KAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLgMKDDEWRAVRSDIQMIFQdplaSLN-- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 91 PHLTALENISLPLYRVH-GYSKEDADS--QAM--------TLLNRFelakhahkkPAELSGGQCQRVAIIRAIAIQPSML 159
Cdd:PRK15079 113 PRMTIGEIIAEPLRTYHpKLSRQEVKDrvKAMmlkvgllpNLINRY---------PHEFSGGQCQRIGIARALILEPKLI 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503691651 160 LFDEPTSALDPLMTSEVLDLIVELKKE-GKQFIIVTHHISFARKICDWILFLSEGKVLDSKPTSQFFDHPASP 231
Cdd:PRK15079 184 ICDEPVSALDVSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNPLHP 256
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
16-216 |
9.00e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 114.83 E-value: 9.00e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 16 KVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVPLifEEKQLRQHRLKLGILFQSWN--LFPhL 93
Cdd:PRK13647 19 KALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREV--NAENEKWVRSKVGLVFQDPDdqVFS-S 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 94 TALENISL-PLYRvhGYSKEDADSQAMTLLNRFELAKHAHKKPAELSGGQCQRVAIIRAIAIQPSMLLFDEPTSALDPLM 172
Cdd:PRK13647 96 TVWDDVAFgPVNM--GLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRG 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 503691651 173 TSEVLDLIVELKKEGKQFIIVTHHISFARKICDWILFLSEGKVL 216
Cdd:PRK13647 174 QETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVL 217
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
1-215 |
1.12e-30 |
|
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: 113.01 E-value: 1.12e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 1 MKLEITQLEKAYNKQKVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDG--VPLIFeekqlrqhrl 78
Cdd:cd03220 21 KKLGILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGrvSSLLG---------- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 79 kLGILFQswnlfPHLTALENISLPLyRVHGYSKEDADSqamtLLNRF----ELAKHAHKKPAELSGGQCQRVAIIRAIAI 154
Cdd:cd03220 91 -LGGGFN-----PELTGRENIYLNG-RLLGLSRKEIDE----KIDEIiefsELGDFIDLPVKTYSSGMKARLAFAIATAL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 503691651 155 QPSMLLFDEPTSALDPLMTSEVLDLIVELKKEGKQFIIVTHHISFARKICDWILFLSEGKV 215
Cdd:cd03220 160 EPDILLIDEVLAVGDAAFQEKCQRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKI 220
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
14-224 |
1.41e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 114.51 E-value: 1.41e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 14 KQKVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESP---TCGRVNFDGVPLifEEKQLRQHRLKLGILFQSW-NL 89
Cdd:PRK13640 19 KKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPddnPNSKITVDGITL--TAKTVWDIREKVGIVFQNPdNQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 90 FPHLTALENISLPLYRvHGYSKEDADSQAMTLLNRFELAKHAHKKPAELSGGQCQRVAIIRAIAIQPSMLLFDEPTSALD 169
Cdd:PRK13640 97 FVGATVGDDVAFGLEN-RAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLD 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 503691651 170 PLMTSEVLDLIVELKKEGKQFII-VTHHISFArKICDWILFLSEGKVLDS-KPTSQF 224
Cdd:PRK13640 176 PAGKEQILKLIRKLKKKNNLTVIsITHDIDEA-NMADQVLVLDDGKLLAQgSPVEIF 231
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
12-218 |
1.58e-30 |
|
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: 113.09 E-value: 1.58e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 12 YNKQK-VLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVPLI-FEEKQLRQhrlKLGILFQSWNL 89
Cdd:cd03254 12 YDEKKpVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRdISRKSLRS---MIGVVLQDTFL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 90 FPHlTALENISLPlyrvHGYSKEDADSQAMTLLNRFELAKHAHK--------KPAELSGGQCQRVAIIRAIAIQPSMLLF 161
Cdd:cd03254 89 FSG-TIMENIRLG----RPNATDEEVIEAAKEAGAHDFIMKLPNgydtvlgeNGGNLSQGERQLLAIARAMLRDPKILIL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 503691651 162 DEPTSALDPLMTSEVLDLIVELKKeGKQFIIVTHHISFARKiCDWILFLSEGKVLDS 218
Cdd:cd03254 164 DEATSNIDTETEKLIQEALEKLMK-GRTSIIIAHRLSTIKN-ADKILVLDDGKIIEE 218
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
5-215 |
2.19e-30 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 117.86 E-value: 2.19e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 5 ITQLEKAYNKQKVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGvplifeekqlrqhRLKLGILF 84
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK-------------GLRIGYLP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 85 QSWNLFPHLTALENIS---LPLYRV-------------------------------HGYskeDADSQAMTLLNRFELAKH 130
Cdd:COG0488 68 QEPPLDDDLTVLDTVLdgdAELRALeaeleeleaklaepdedlerlaelqeefealGGW---EAEARAEEILSGLGFPEE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 131 AHKKP-AELSGGQCQRVAIIRAIAIQPSMLLFDEPTSALDplmtsevLDLIV----ELKKEGKQFIIVTHHISFARKICD 205
Cdd:COG0488 145 DLDRPvSELSGGWRRRVALARALLSEPDLLLLDEPTNHLD-------LESIEwleeFLKNYPGTVLVVSHDRYFLDRVAT 217
|
250
....*....|
gi 503691651 206 WILFLSEGKV 215
Cdd:COG0488 218 RILELDRGKL 227
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
16-216 |
2.41e-30 |
|
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: 111.49 E-value: 2.41e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 16 KVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESP--TCGRVNFDGVPLIfeekqLRQHRLKLGILFQSWNLFPHL 93
Cdd:cd03213 23 QLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGlgVSGEVLINGRPLD-----KRSFRKIIGYVPQDDILHPTL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 94 TALENISLplyrvhgyskedadsqamtllnrfelakHAHKKpaELSGGQCQRVAIIRAIAIQPSMLLFDEPTSALDPLMT 173
Cdd:cd03213 98 TVRETLMF----------------------------AAKLR--GLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSA 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 503691651 174 SEVLDLIVELKKEGKQFIIVTHHIS-FARKICDWILFLSEGKVL 216
Cdd:cd03213 148 LQVMSLLRRLADTGRTIICSIHQPSsEIFELFDKLLLLSQGRVI 191
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
4-223 |
4.24e-30 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 112.48 E-value: 4.24e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 4 EITQLEKAYNKQKVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVPLifeeKQLRQHRL--KLG 81
Cdd:COG4604 3 EIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDV----ATTPSRELakRLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 82 ILFQSWNLFPHLTALENISL---PlyrvhgYSK-----EDAD--SQAmtlLNRFELAKHAHKKPAELSGGQCQRVAIIRA 151
Cdd:COG4604 79 ILRQENHINSRLTVRELVAFgrfP------YSKgrltaEDREiiDEA---IAYLDLEDLADRYLDELSGGQRQRAFIAMV 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503691651 152 IAIQPSMLLFDEPTSALDPLMTSEVLDLIVELKKE-GKQFIIVTHHISFARKICDWILFLSEGKVLDSKPTSQ 223
Cdd:COG4604 150 LAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADElGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEE 222
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
3-215 |
7.47e-30 |
|
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: 109.71 E-value: 7.47e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 3 LEITQLEKAY--NKQKVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVPLIFEEKQLRQhrlKL 80
Cdd:cd03247 1 LSINNVSFSYpeQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSS---LI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 81 GILFQSwnlfPHL---TALENISLPlyrvhgyskedadsqamtllnrfelakhahkkpaeLSGGQCQRVAIIRAIAIQPS 157
Cdd:cd03247 78 SVLNQR----PYLfdtTLRNNLGRR-----------------------------------FSGGERQRLALARILLQDAP 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 503691651 158 MLLFDEPTSALDPLMTSEVLDLIVELKKEgKQFIIVTHHISFARKIcDWILFLSEGKV 215
Cdd:cd03247 119 IVLLDEPTVGLDPITERQLLSLIFEVLKD-KTLIWITHHLTGIEHM-DKILFLENGKI 174
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
11-201 |
1.33e-29 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 109.63 E-value: 1.33e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 11 AYNKQKVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVnfdgvplifeekqLRQHRLKLGILFQSWNL- 89
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTV-------------RRAGGARVAYVPQRSEVp 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 90 --FPhLTALENISLPLYRVHG----YSKED--ADSQAMTllnRFELAKHAHKKPAELSGGQCQRVAIIRAIAIQPSMLLF 161
Cdd:NF040873 68 dsLP-LTVRDLVAMGRWARRGlwrrLTRDDraAVDDALE---RVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLL 143
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 503691651 162 DEPTSALDPLMTSEVLDLIVELKKEGKQFIIVTHHISFAR 201
Cdd:NF040873 144 DEPTTGLDAESRERIIALLAEEHARGATVVVVTHDLELVR 183
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
3-241 |
1.65e-29 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 115.19 E-value: 1.65e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 3 LEITQLEKAYNKQK----VLKNINLSIPEAQSLALLGPSGSGKS-TLLRILAGLESP----TCGRVNFDGVPLIF-EEKQ 72
Cdd:PRK15134 6 LAIENLSVAFRQQQtvrtVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPpvvyPSGDIRFHGESLLHaSEQT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 73 LRQHR-LKLGILFQSwnlfP--HLTALENISLPLYRV----HGYSKEDADSQAMTLLNRF---ELAKHAHKKPAELSGGQ 142
Cdd:PRK15134 86 LRGVRgNKIAMIFQE----PmvSLNPLHTLEKQLYEVlslhRGMRREAARGEILNCLDRVgirQAAKRLTDYPHQLSGGE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 143 CQRVAIIRAIAIQPSMLLFDEPTSALDPLMTSEVLDLIVELKKE-GKQFIIVTHHISFARKICDWILFLSEGKVLDSKPT 221
Cdd:PRK15134 162 RQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQElNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRA 241
|
250 260
....*....|....*....|
gi 503691651 222 SQFFDHPASPeiqyYLEQVL 241
Cdd:PRK15134 242 ATLFSAPTHP----YTQKLL 257
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
16-216 |
1.89e-29 |
|
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: 110.40 E-value: 1.89e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 16 KVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVPLifEEKQLRQHRLKLGILFQSWNLFpHLTA 95
Cdd:cd03251 16 PVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDV--RDYTLASLRRQIGLVSQDVFLF-NDTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 96 LENISlplYRVHGYSKEDADSQAmtllnrfELAkHAH----KKP-----------AELSGGQCQRVAIIRAIAIQPSMLL 160
Cdd:cd03251 93 AENIA---YGRPGATREEVEEAA-------RAA-NAHefimELPegydtvigergVKLSGGQRQRIAIARALLKDPPILI 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 503691651 161 FDEPTSALDPLMTSEVLDLIVELKKeGKQFIIVTHHISFARKIcDWILFLSEGKVL 216
Cdd:cd03251 162 LDEATSALDTESERLVQAALERLMK-NRTTFVIAHRLSTIENA-DRIVVLEDGKIV 215
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
16-225 |
1.99e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 111.75 E-value: 1.99e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 16 KVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVPLIF--EEKQLRQHRLKLGILFQswnlFPHL 93
Cdd:PRK13643 20 RALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSStsKQKEIKPVRKKVGVVFQ----FPES 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 94 TALENISLPLY----RVHGYSKEDADSQAMTLLNRFELAKHA-HKKPAELSGGQCQRVAIIRAIAIQPSMLLFDEPTSAL 168
Cdd:PRK13643 96 QLFEETVLKDVafgpQNFGIPKEKAEKIAAEKLEMVGLADEFwEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGL 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 503691651 169 DPLMTSEVLDLIVELKKEGKQFIIVTHHISFARKICDWILFLSEGKVLDSKPTSQFF 225
Cdd:PRK13643 176 DPKARIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVF 232
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
8-237 |
2.51e-29 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 110.96 E-value: 2.51e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 8 LEKAYNKQKVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCG-RVNFD---GVPLIFEEKQLRQHRLKLGIL 83
Cdd:PRK14271 27 LTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyRYSGDvllGGRSIFNYRDVLEFRRRVGML 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 84 FQSWNLFPhLTALENIsLPLYRVHGY-SKEDADSQAMTLLNRFELAKHAHKK----PAELSGGQCQRVAIIRAIAIQPSM 158
Cdd:PRK14271 107 FQRPNPFP-MSIMDNV-LAGVRAHKLvPRKEFRGVAQARLTEVGLWDAVKDRlsdsPFRLSGGQQQLLCLARTLAVNPEV 184
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 503691651 159 LLFDEPTSALDPLMTSEVLDLIVELkKEGKQFIIVTHHISFARKICDWILFLSEGKVLDSKPTSQFFDHPASPEIQYYL 237
Cdd:PRK14271 185 LLLDEPTSALDPTTTEKIEEFIRSL-ADRLTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKHAETARYV 262
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
13-216 |
3.94e-29 |
|
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: 114.96 E-value: 3.94e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 13 NKQKVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVPLifeeKQ-----LRQHrlkLGILFQSW 87
Cdd:TIGR03375 476 QETPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDI----RQidpadLRRN---IGYVPQDP 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 88 NLFpHLTALENISL--PLYrvhgyskEDAD-SQAMTL--LNRFeLAKHA-------HKKPAELSGGQCQRVAIIRAIAIQ 155
Cdd:TIGR03375 549 RLF-YGTLRDNIALgaPYA-------DDEEiLRAAELagVTEF-VRRHPdgldmqiGERGRSLSGGQRQAVALARALLRD 619
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503691651 156 PSMLLFDEPTSALDplMTSEVLdLIVELKK--EGKQFIIVTHHISFArKICDWILFLSEGKVL 216
Cdd:TIGR03375 620 PPILLLDEPTSAMD--NRSEER-FKDRLKRwlAGKTLVLVTHRTSLL-DLVDRIIVMDNGRIV 678
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-220 |
5.12e-29 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 112.63 E-value: 5.12e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 1 MKLEITQLEKAYNKQKVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVPLifEEKQLRQHRLKL 80
Cdd:PRK09536 2 PMIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDV--EALSARAASRRV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 81 GILFQSWNL---F-----------PHLTALENislplyrvHGYSKEDADSQAMtllNRFELAKHAHKKPAELSGGQCQRV 146
Cdd:PRK09536 80 ASVPQDTSLsfeFdvrqvvemgrtPHRSRFDT--------WTETDRAAVERAM---ERTGVAQFADRPVTSLSGGERQRV 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 503691651 147 AIIRAIAIQPSMLLFDEPTSALDPLMTSEVLDLIVELKKEGKQFIIVTHHISFARKICDWILFLSEGKVLDSKP 220
Cdd:PRK09536 149 LLARALAQATPVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGP 222
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
3-215 |
7.27e-29 |
|
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: 113.36 E-value: 7.27e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 3 LEITQLEKAYNKQKVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLES---------------PTCGRV---NFDGV 64
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQyeptsgriiyhvalcEKCGYVerpSKVGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 65 P---------------LIFEEKQLRQHRLKLGILFQ-SWNLFPHLTALENISLPLYRVhGYSKEDADSQAMTLLNRFELA 128
Cdd:TIGR03269 81 PcpvcggtlepeevdfWNLSDKLRRRIRKRIAIMLQrTFALYGDDTVLDNVLEALEEI-GYEGKEAVGRAVDLIEMVQLS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 129 KHAHKKPAELSGGQCQRVAIIRAIAIQPSMLLFDEPTSALDPLMTSEVLDLIVEL-KKEGKQFIIVTHHISFARKICDWI 207
Cdd:TIGR03269 160 HRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAvKASGISMVLTSHWPEVIEDLSDKA 239
|
....*...
gi 503691651 208 LFLSEGKV 215
Cdd:TIGR03269 240 IWLENGEI 247
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
17-239 |
7.47e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 109.79 E-value: 7.47e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 17 VLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVPlIFEEKQLRQHRLKLGILFQswNLFPHLTAL 96
Cdd:PRK13633 25 ALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLD-TSDEENLWDIRNKAGMVFQ--NPDNQIVAT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 97 ----------ENISLPLYRVhgysKEDADsQAMTLLNRFELAKHAhkkPAELSGGQCQRVAIIRAIAIQPSMLLFDEPTS 166
Cdd:PRK13633 102 iveedvafgpENLGIPPEEI----RERVD-ESLKKVGMYEYRRHA---PHLLSGGQKQRVAIAGILAMRPECIIFDEPTA 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 167 ALDPLMTSEVLDLIVEL-KKEGKQFIIVTHHISFARKiCDWILFLSEGKV-LDSKPTSQF----------FDHPASPEIQ 234
Cdd:PRK13633 174 MLDPSGRREVVNTIKELnKKYGITIILITHYMEEAVE-ADRIIVMDSGKVvMEGTPKEIFkevemmkkigLDVPQVTELA 252
|
....*
gi 503691651 235 YYLEQ 239
Cdd:PRK13633 253 YELKK 257
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
17-243 |
7.70e-29 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 109.02 E-value: 7.70e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 17 VLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDG--VPLifeekqlrqhrLKLGILFQswnlfPHLT 94
Cdd:COG1134 41 ALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGrvSAL-----------LELGAGFH-----PELT 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 95 ALENISLPLyRVHGYSKEDADSqamtllnRF-------ELAKHAHKKPAELSGGQCQRVAIIRAIAIQPSMLLFDEPTSA 167
Cdd:COG1134 105 GRENIYLNG-RLLGLSRKEIDE-------KFdeivefaELGDFIDQPVKTYSSGMRARLAFAVATAVDPDILLVDEVLAV 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 503691651 168 LDPLMTSEVLDLIVELKKEGKQFIIVTHHISFARKICDWILFLSEGKVLdskptsqfFDHPASPEIQYYLEQVLKY 243
Cdd:COG1134 177 GDAAFQKKCLARIRELRESGRTVIFVSHSMGAVRRLCDRAIWLEKGRLV--------MDGDPEEVIAAYEALLAGR 244
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
3-226 |
1.32e-28 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 112.84 E-value: 1.32e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 3 LEITQLEKAYNKQKVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVPLiFEEKQLRQHRLKLGI 82
Cdd:PRK15439 12 LCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPC-ARLTPAKAHQLGIYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 83 LFQSWNLFPHLTALENISLplyrvhGYSKEDADSQAMTLLNRfELAKH--AHKKPAELSGGQCQRVAIIRAIAIQPSMLL 160
Cdd:PRK15439 91 VPQEPLLFPNLSVKENILF------GLPKRQASMQKMKQLLA-ALGCQldLDSSAGSLEVADRQIVEILRGLMRDSRILI 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 503691651 161 FDEPTSALDPLMTSEVLDLIVELKKEGKQFIIVTHHISFARKICDWILFLSEGKVLDSKPTSQFFD 226
Cdd:PRK15439 164 LDEPTASLTPAETERLFSRIRELLAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTADLST 229
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
18-227 |
2.97e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 107.91 E-value: 2.97e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 18 LKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVPLIFEEKQ-LRQHrlkLGILFQS-WNLFPHLT- 94
Cdd:PRK13648 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEkLRKH---IGIVFQNpDNQFVGSIv 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 95 ------ALENISLPLYRVHGYSKEdadsqamtLLNRFELAKHAHKKPAELSGGQCQRVAIIRAIAIQPSMLLFDEPTSAL 168
Cdd:PRK13648 102 kydvafGLENHAVPYDEMHRRVSE--------ALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSML 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 169 DPLMTSEVLDLIVELKKEGKQFII-VTHHISFARKiCDWILFLSEGKVLDSKPTSQFFDH 227
Cdd:PRK13648 174 DPDARQNLLDLVRKVKSEHNITIIsITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIFDH 232
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
16-234 |
4.04e-28 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 108.90 E-value: 4.04e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 16 KVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVPLIF----EEKQLRQhrlKLGILFQ----SW 87
Cdd:PRK11308 29 KALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKadpeAQKLLRQ---KIQIVFQnpygSL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 88 NlfPHLTALENISLPLYRVHGYSKEDADSQAMTLLNRFEL-AKHAHKKPAELSGGQCQRVAIIRAIAIQPSMLLFDEPTS 166
Cdd:PRK11308 106 N--PRKKVGQILEEPLLINTSLSAAERREKALAMMAKVGLrPEHYDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVS 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 503691651 167 ALDPLMTSEVLDLIVELKKE-GKQFIIVTHHISFARKICDWILFLSEGKVLDSKPTSQFFDHPASPEIQ 234
Cdd:PRK11308 184 ALDVSVQAQVLNLMMDLQQElGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFNNPRHPYTQ 252
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
15-196 |
4.11e-28 |
|
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: 111.30 E-value: 4.11e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 15 QKVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVPLifeeKQLRQHRLKLGILF--QSWNLFpH 92
Cdd:TIGR02868 348 PPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPV----SSLDQDEVRRRVSVcaQDAHLF-D 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 93 LTALENISLplyrvhgySKEDA-DSQAMTLLNRFELAKHAHKKP-----------AELSGGQCQRVAIIRAIAIQPSMLL 160
Cdd:TIGR02868 423 TTVRENLRL--------ARPDAtDEELWAALERVGLADWLRALPdgldtvlgeggARLSGGERQRLALARALLADAPILL 494
|
170 180 190
....*....|....*....|....*....|....*.
gi 503691651 161 FDEPTSALDPLMTSEVLDLIVElKKEGKQFIIVTHH 196
Cdd:TIGR02868 495 LDEPTEHLDAETADELLEDLLA-ALSGRTVVLITHH 529
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
14-217 |
5.79e-28 |
|
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: 111.29 E-value: 5.79e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 14 KQKVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVPLI-FEEKQLRQHrlkLGILFQSWNLFPH 92
Cdd:TIGR01842 330 KKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKqWDRETFGKH---IGYLPQDVELFPG 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 93 lTALENISlplyRVhgysKEDADSQAMtllnrFELAKHA--H----KKP-----------AELSGGQCQRVAIIRAIAIQ 155
Cdd:TIGR01842 407 -TVAENIA----RF----GENADPEKI-----IEAAKLAgvHelilRLPdgydtvigpggATLSGGQRQRIALARALYGD 472
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503691651 156 PSMLLFDEPTSALDPLMTSEVLDLIVELKKEGKQFIIVTHHISfARKICDWILFLSEGKVLD 217
Cdd:TIGR01842 473 PKLVVLDEPNSNLDEEGEQALANAIKALKARGITVVVITHRPS-LLGCVDKILVLQDGRIAR 533
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
3-223 |
7.16e-28 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 110.48 E-value: 7.16e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 3 LEITQLEKAYNKQKVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVPLIFEEKQLRQHRlKLGI 82
Cdd:PRK10762 5 LQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQEA-GIGI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 83 LFQSWNLFPHLTALENISLPLYRVHGYSKEDAD---SQAMTLLNRFELAKHAHKKPAELSGGQCQRVAIIRAIAIQPSML 159
Cdd:PRK10762 84 IHQELNLIPQLTIAENIFLGREFVNRFGRIDWKkmyAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVI 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 503691651 160 LFDEPTSALDPLMTSEVLDLIVELKKEGKQFIIVTHHISFARKICDWILFLSEGKVLDSKPTSQ 223
Cdd:PRK10762 164 IMDEPTDALTDTETESLFRVIRELKSQGRGIVYISHRLKEIFEICDDVTVFRDGQFIAEREVAD 227
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
17-215 |
8.35e-28 |
|
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: 111.20 E-value: 8.35e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 17 VLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVPLifEEKQLRQHRLKLGILFQSWNLFPHlTAL 96
Cdd:TIGR03797 468 ILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDL--AGLDVQAVRRQLGVVLQNGRLMSG-SIF 544
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 97 ENIslplyrvhgyskedADSQAMTLLNRFELAKHA-------------HKKPAE----LSGGQCQRVAIIRAIAIQPSML 159
Cdd:TIGR03797 545 ENI--------------AGGAPLTLDEAWEAARMAglaedirampmgmHTVISEgggtLSGGQRQRLLIARALVRKPRIL 610
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 503691651 160 LFDEPTSALDPLMTSEVLDlivELKKEGKQFIIVTHHISFARKiCDWILFLSEGKV 215
Cdd:TIGR03797 611 LFDEATSALDNRTQAIVSE---SLERLKVTRIVIAHRLSTIRN-ADRIYVLDAGRV 662
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
1-239 |
8.60e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 107.17 E-value: 8.60e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 1 MKLEITQLEKAYNK-----QKVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVPLIFE--EKQL 73
Cdd:PRK13646 1 MTIRFDNVSYTYQKgtpyeHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKtkDKYI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 74 RQHRLKLGILFQswnlFPHLTALE------------NISLPLyrvhgyskEDADSQAMTLLNRFELAKHA-HKKPAELSG 140
Cdd:PRK13646 81 RPVRKRIGMVFQ----FPESQLFEdtvereiifgpkNFKMNL--------DEVKNYAHRLLMDLGFSRDVmSQSPFQMSG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 141 GQCQRVAIIRAIAIQPSMLLFDEPTSALDPLMTSEVLDLIVELK-KEGKQFIIVTHHISFARKICDWILFLSEGKVLD-S 218
Cdd:PRK13646 149 GQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQtDENKTIILVSHDMNEVARYADEVIVMKEGSIVSqT 228
|
250 260 270
....*....|....*....|....*....|.
gi 503691651 219 KPTSQFFD-------HPASPEI---QYYLEQ 239
Cdd:PRK13646 229 SPKELFKDkkkladwHIGLPEIvqlQYDFEQ 259
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
10-216 |
1.52e-27 |
|
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: 105.05 E-value: 1.52e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 10 KAYNKQKVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGL---ESPTCGRVNFDGVPLifEEKQLRQHrlkLGILFQS 86
Cdd:cd03234 15 NWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRvegGGTTSGQILFNGQPR--KPDQFQKC---VAYVRQD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 87 WNLFPHLTALENIslpLYRVH---GYSKEDADSQAM---TLLNRFELAKHAHKKPAELSGGQCQRVAIIRAIAIQPSMLL 160
Cdd:cd03234 90 DILLPGLTVRETL---TYTAIlrlPRKSSDAIRKKRvedVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLI 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 503691651 161 FDEPTSALDPLMTSEVLDLIVELKKEGKqFIIVTHHI--SFARKICDWILFLSEGKVL 216
Cdd:cd03234 167 LDEPTSGLDSFTALNLVSTLSQLARRNR-IVILTIHQprSDLFRLFDRILLLSSGEIV 223
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
3-215 |
3.62e-27 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 108.61 E-value: 3.62e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 3 LEITQLEKAYNKQKVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNfdgvplifeekqlRQHRLKLGI 82
Cdd:COG0488 316 LELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVK-------------LGETVKIGY 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 83 LFQSW-NLFPHLTALENISlplyrvhGYSKEDADSQAMTLLNRFeL--AKHAHKKPAELSGGQCQRVAIIRAIAIQPSML 159
Cdd:COG0488 383 FDQHQeELDPDKTVLDELR-------DGAPGGTEQEVRGYLGRF-LfsGDDAFKPVGVLSGGEKARLALAKLLLSPPNVL 454
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 160 LFDEPTSALDPLMTSEVLDLIvelkkegKQF----IIVTHHISFARKICDWILFLSEGKV 215
Cdd:COG0488 455 LLDEPTNHLDIETLEALEEAL-------DDFpgtvLLVSHDRYFLDRVATRILEFEDGGV 507
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
14-228 |
5.08e-27 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 109.04 E-value: 5.08e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 14 KQKVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVPLI-FEEKQLRQHrlkLGILFQSWNLFPH 92
Cdd:TIGR00958 493 DVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVqYDHHYLHRQ---VALVGQEPVLFSG 569
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 93 lTALENIslpLYRVHGYSKEDADSQAMtllnrfelAKHAH---------------KKPAELSGGQCQRVAIIRAIAIQPS 157
Cdd:TIGR00958 570 -SVRENI---AYGLTDTPDEEIMAAAK--------AANAHdfimefpngydtevgEKGSQLSGGQKQRIAIARALVRKPR 637
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503691651 158 MLLFDEPTSALDplmtSEVLDLIVELKK-EGKQFIIVTHHISFARKiCDWILFLSEGKVLDSKPTSQFFDHP 228
Cdd:TIGR00958 638 VLILDEATSALD----AECEQLLQESRSrASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQLMEDQ 704
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
16-227 |
7.48e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 104.70 E-value: 7.48e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 16 KVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGR--VNFDGVPLIFEE-KQLRQHRLKLGILFQ--SWNLF 90
Cdd:PRK13645 25 KALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQtiVGDYAIPANLKKiKEVKRLRKEIGLVFQfpEYQLF 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 91 PHlTALENISL-PLYRvhGYSKEDADSQAMTLLNRFELAK-HAHKKPAELSGGQCQRVAIIRAIAIQPSMLLFDEPTSAL 168
Cdd:PRK13645 105 QE-TIEKDIAFgPVNL--GENKQEAYKKVPELLKLVQLPEdYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGL 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 169 DPLMTSEVLDLIVELKKE-GKQFIIVTHHISFARKICDWILFLSEGKVLDSKPTSQFFDH 227
Cdd:PRK13645 182 DPKGEEDFINLFERLNKEyKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFSN 241
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
3-195 |
2.13e-26 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 102.10 E-value: 2.13e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 3 LEITQLEKAYNKQKVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVPLifEEKQLRQHRLKLGI 82
Cdd:PRK10247 8 LQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDI--STLKPEIYRQQVSY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 83 LFQSWNLFPHlTALENISLPlYRVHgysKEDADSQAMTL-LNRFELAKHAHKKP-AELSGGQCQRVAIIRAIAIQPSMLL 160
Cdd:PRK10247 86 CAQTPTLFGD-TVYDNLIFP-WQIR---NQQPDPAIFLDdLERFALPDTILTKNiAELSGGEKQRISLIRNLQFMPKVLL 160
|
170 180 190
....*....|....*....|....*....|....*.
gi 503691651 161 FDEPTSALDPLMTSEVLDLIVELKKEGKQFII-VTH 195
Cdd:PRK10247 161 LDEITSALDESNKHNVNEIIHRYVREQNIAVLwVTH 196
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
16-228 |
3.05e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 102.96 E-value: 3.05e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 16 KVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVPLIfeEKQLRQHRLKLGILFQSWN--LFPHl 93
Cdd:PRK13652 18 EALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPIT--KENIREVRKFVGLVFQNPDdqIFSP- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 94 TALENISLPLYRVhGYSKEDADSQAMTLLNRFELAKHAHKKPAELSGGQCQRVAIIRAIAIQPSMLLFDEPTSALDPLMT 173
Cdd:PRK13652 95 TVEQDIAFGPINL-GLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGV 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 503691651 174 SEVLDLIVELKKE-GKQFIIVTHHISFARKICDWILFLSEGKVLDSKPTSQFFDHP 228
Cdd:PRK13652 174 KELIDFLNDLPETyGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
17-217 |
4.26e-26 |
|
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: 101.41 E-value: 4.26e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 17 VLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVPLIFEEKQlrQHRLKLGILFQSwNLFPHLTAL 96
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPA--WLRRQVGVVLQE-NVLFNRSIR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 97 ENISL-----PLYRVHgYSKEDADSQAMTLLNRFELAKHAHKKPAELSGGQCQRVAIIRAIAIQPSMLLFDEPTSALDpl 171
Cdd:cd03252 94 DNIALadpgmSMERVI-EAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATSALD-- 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 503691651 172 MTSEVLdLIVELKK--EGKQFIIVTHHISFARKiCDWILFLSEGKVLD 217
Cdd:cd03252 171 YESEHA-IMRNMHDicAGRTVIIIAHRLSTVKN-ADRIIVMEKGRIVE 216
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
3-225 |
8.70e-26 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 101.62 E-value: 8.70e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 3 LEITQLEKAYNKQKVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVPLIFEEKQLRQHRLKLGI 82
Cdd:PRK13638 2 LATSDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKRGLLALRQQVAT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 83 LFQSWNLFPHLTALE-NISLPLyRVHGYSKEDAD---SQAMTLLNrfelAKHAHKKPAE-LSGGQCQRVAIIRAIAIQPS 157
Cdd:PRK13638 82 VFQDPEQQIFYTDIDsDIAFSL-RNLGVPEAEITrrvDEALTLVD----AQHFRHQPIQcLSHGQKKRVAIAGALVLQAR 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 503691651 158 MLLFDEPTSALDPLMTSEVLDLIVELKKEGKQFIIVTHHISFARKICDWILFLSEGKVLDSKPTSQFF 225
Cdd:PRK13638 157 YLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVF 224
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
18-226 |
1.02e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 101.60 E-value: 1.02e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 18 LKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVPlIFEEKQLRQHRLKLGILFQSwnlfPHLTAL- 96
Cdd:PRK13644 18 LENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGID-TGDFSKLQGIRKLVGIVFQN----PETQFVg 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 97 -----------ENISLPLYRVhgysKEDADSQamtlLNRFELAKHAHKKPAELSGGQCQRVAIIRAIAIQPSMLLFDEPT 165
Cdd:PRK13644 93 rtveedlafgpENLCLPPIEI----RKRVDRA----LAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVT 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503691651 166 SALDPLMTSEVLDLIVELKKEGKQFIIVTHHISfARKICDWILFLSEGK-VLDSKPTSQFFD 226
Cdd:PRK13644 165 SMLDPDSGIAVLERIKKLHEKGKTIVYITHNLE-ELHDADRIIVMDRGKiVLEGEPENVLSD 225
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
2-216 |
1.04e-25 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 101.22 E-value: 1.04e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 2 KLEITQLEKAYNKQKVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVPLI-FEEKQLRQhrlKL 80
Cdd:PRK10253 7 RLRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQhYASKEVAR---RI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 81 GILFQSWNLFPHLTALENIS------LPLYRVHGYSKEDADSQAMTLLNRFELAKHAHKKpaeLSGGQCQRVAIIRAIAI 154
Cdd:PRK10253 84 GLLAQNATTPGDITVQELVArgryphQPLFTRWRKEDEEAVTKAMQATGITHLADQSVDT---LSGGQRQRAWIAMVLAQ 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503691651 155 QPSMLLFDEPTSALDPLMTSEVLDLIVELKKE-GKQFIIVTHHISFARKICDWILFLSEGKVL 216
Cdd:PRK10253 161 ETAIMLLDEPTTWLDISHQIDLLELLSELNREkGYTLAAVLHDLNQACRYASHLIALREGKIV 223
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
3-217 |
1.16e-25 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 100.93 E-value: 1.16e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 3 LEITQLEKAYNK-----QKVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVPLIF--EEKQLRQ 75
Cdd:COG1101 2 LELKNLSKTFNPgtvneKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKlpEYKRAKY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 76 hrlkLGILFQ--SWNLFPHLTALENISLPLYRVH------GYSKEDADsQAMTLLNRFE--LAKHAHKKPAELSGGQCQR 145
Cdd:COG1101 82 ----IGRVFQdpMMGTAPSMTIEENLALAYRRGKrrglrrGLTKKRRE-LFRELLATLGlgLENRLDTKVGLLSGGQRQA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 503691651 146 VAIIRAIAIQPSMLLFDEPTSALDPLMTSEVLDLIVELKKEGK-QFIIVTHHISFARKICDWILFLSEGK-VLD 217
Cdd:COG1101 157 LSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNlTTLMVTHNMEQALDYGNRLIMMHEGRiILD 230
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
17-218 |
1.36e-25 |
|
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: 104.82 E-value: 1.36e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 17 VLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVPL-IFEEKQLRQhrlKLGILFQSWNLFPHlTA 95
Cdd:TIGR01846 472 VLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLaIADPAWLRR---QMGVVLQENVLFSR-SI 547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 96 LENISL-----PLYRVHgYSKEDADSQAMTLLNRFELAKHAHKKPAELSGGQCQRVAIIRAIAIQPSMLLFDEPTSALDp 170
Cdd:TIGR01846 548 RDNIALcnpgaPFEHVI-HAAKLAGAHDFISELPQGYNTEVGEKGANLSGGQRQRIAIARALVGNPRILIFDEATSALD- 625
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 503691651 171 lmtSEVLDLIVELKKE---GKQFIIVTHHISFARKiCDWILFLSEGKVLDS 218
Cdd:TIGR01846 626 ---YESEALIMRNMREicrGRTVIIIAHRLSTVRA-CDRIIVLEKGQIAES 672
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
20-229 |
1.83e-25 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 102.26 E-value: 1.83e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 20 NINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVPLIFEEKQ--LRQHRLKLGILFQSWNLFPHLTALE 97
Cdd:PRK11144 16 TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEKGicLPPEKRRIGYVFQDARLFPHYKVRG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 98 NIslpLYRVHGYSKEDADSQAM-----TLLNRFelakhahkkPAELSGGQCQRVAIIRAIAIQPSMLLFDEPTSALDPLM 172
Cdd:PRK11144 96 NL---RYGMAKSMVAQFDKIVAllgiePLLDRY---------PGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPR 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 503691651 173 TSEVLDLIVELKKEGKQFII-VTHHISFARKICDWILFLSEGKVLDSKPTSQFFDHPA 229
Cdd:PRK11144 164 KRELLPYLERLAREINIPILyVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVWASSA 221
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
3-213 |
2.12e-25 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 103.71 E-value: 2.12e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 3 LEITQLEKAYNKQKVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVplifEEKQLRQ---HRLK 79
Cdd:PRK09700 6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNI----NYNKLDHklaAQLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 80 LGILFQSWNLFPHLTALENI---SLPLYRVHGYSKED---ADSQAMTLLNRFELAKHAHKKPAELSGGQCQRVAIIRAIA 153
Cdd:PRK09700 82 IGIIYQELSVIDELTVLENLyigRHLTKKVCGVNIIDwreMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLM 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 154 IQPSMLLFDEPTSALDPLMTSEVLDLIVELKKEGKQFIIVTHHISFARKICDWILFLSEG 213
Cdd:PRK09700 162 LDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDG 221
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
3-241 |
2.62e-25 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 100.00 E-value: 2.62e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 3 LEITQLEKAYNKQKVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNF---DGVPL----IFEEKQLRQ 75
Cdd:PRK11701 7 LSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYrmrDGQLRdlyaLSEAERRRL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 76 HRLKLGILFQswN----LFPHLTALENISLPLYRVHGYSKEDADSQAMTLLNRFEL-AKHAHKKPAELSGGQCQRVAIIR 150
Cdd:PRK11701 87 LRTEWGFVHQ--HprdgLRMQVSAGGNIGERLMAVGARHYGDIRATAGDWLERVEIdAARIDDLPTTFSGGMQQRLQIAR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 151 AIAIQPSMLLFDEPTSALDPLMTSEVLDLIVELKKE-GKQFIIVTHHISFARKICDWILFLSEGKVLDSKPTSQFFDHPA 229
Cdd:PRK11701 165 NLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRElGLAVVIVTHDLAVARLLAHRLLVMKQGRVVESGLTDQVLDDPQ 244
|
250
....*....|..
gi 503691651 230 SPEIQYYLEQVL 241
Cdd:PRK11701 245 HPYTQLLVSSVL 256
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
20-216 |
3.59e-25 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 99.68 E-value: 3.59e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 20 NINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVPLifeeKQLRQHRL-KLGIL--FQSWNLFPHLTAL 96
Cdd:PRK11300 23 NVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHI----EGLPGHQIaRMGVVrtFQHVRLFREMTVI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 97 EN-----------------ISLPLYRvhgYSKEDADSQAMTLLNRFELAKHAHKKPAELSGGQCQRVAIIRAIAIQPSML 159
Cdd:PRK11300 99 ENllvaqhqqlktglfsglLKTPAFR---RAESEALDRAATWLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEIL 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 503691651 160 LFDEPTSALDPLMTSEVLDLIVELKKE-GKQFIIVTHHISFARKICDWILFLSEGKVL 216
Cdd:PRK11300 176 MLDEPAAGLNPKETKELDELIAELRNEhNVTVLLIEHDMKLVMGISDRIYVVNQGTPL 233
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
8-216 |
6.42e-25 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 98.43 E-value: 6.42e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 8 LEKAYNKQKVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVPLIFEEKQLRQHRlKLGILFQSW 87
Cdd:PRK10895 9 LAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARR-GIGYLPQEA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 88 NLFPHLTALENISLPLYRVHGYSKEDADSQAMTLLNRFELAKHAHKKPAELSGGQCQRVAIIRAIAIQPSMLLFDEPTSA 167
Cdd:PRK10895 88 SIFRRLSVYDNLMAVLQIRDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAG 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 503691651 168 LDPLMTSEVLDLIVELKKEGKQFIIVTHHISFARKICDWILFLSEGKVL 216
Cdd:PRK10895 168 VDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLI 216
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
13-225 |
8.89e-25 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 98.80 E-value: 8.89e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 13 NKQKVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVPLifeEKQLRQHRLklGILFQS----WN 88
Cdd:PRK15056 18 NGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPT---RQALQKNLV--AYVPQSeevdWS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 89 lFPHLTAlENISLPLYRVHGYSK--EDADSQAMT-LLNRFELAKHAHKKPAELSGGQCQRVAIIRAIAIQPSMLLFDEPT 165
Cdd:PRK15056 93 -FPVLVE-DVVMMGRYGHMGWLRraKKRDRQIVTaALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPF 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 166 SALDPLMTSEVLDLIVELKKEGKQFIIVTHHISFARKICDWILFLsEGKVLDSKPTSQFF 225
Cdd:PRK15056 171 TGVDVKTEARIISLLRELRDEGKTMLVSTHNLGSVTEFCDYTVMV-KGTVLASGPTETTF 229
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
3-224 |
9.47e-25 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 101.93 E-value: 9.47e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 3 LEITQLEKAYNKQKVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLeSPTC---GRVNFDGVPLIFeeKQLRQ-HRL 78
Cdd:PRK13549 6 LEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGV-YPHGtyeGEIIFEGEELQA--SNIRDtERA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 79 KLGILFQSWNLFPHLTALENISL---PLYrvHGYSKEDA-DSQAMTLLNRFELAKHAHKKPAELSGGQCQRVAIIRAIAI 154
Cdd:PRK13549 83 GIAIIHQELALVKELSVLENIFLgneITP--GGIMDYDAmYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNK 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 155 QPSMLLFDEPTSALDPLMTSEVLDLIVELKKEGKQFIIVTHHISFARKICDWILFLSEGKVLDSKPTSQF 224
Cdd:PRK13549 161 QARLLILDEPTASLTESETAVLLDIIRDLKAHGIACIYISHKLNEVKAISDTICVIRDGRHIGTRPAAGM 230
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
3-220 |
9.65e-25 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 96.83 E-value: 9.65e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 3 LEITQLEKAYNKQKVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLES--PTCGRVNFDGVPLIFEEKQLRQhRLKL 80
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKyeVTEGEILFKGEDITDLPPEERA-RLGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 81 GILFQSwnlfPhltalenislplYRVHGYSKEDadsqAMTLLNrfelakhahkkpAELSGGQCQRVAIIRAIAIQPSMLL 160
Cdd:cd03217 80 FLAFQY----P------------PEIPGVKNAD----FLRYVN------------EGFSGGEKKRNEILQLLLLEPDLAI 127
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 503691651 161 FDEPTSALDPLMTSEVLDLIVELKKEGKQFIIVTHHISFARKI-CDWILFLSEGKVLDSKP 220
Cdd:cd03217 128 LDEPDSGLDIDALRLVAEVINKLREEGKSVLIITHYQRLLDYIkPDRVHVLYDGRIVKSGD 188
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
3-195 |
1.11e-24 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 101.83 E-value: 1.11e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 3 LEITQLEKAY--NKQKVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVPLI-FEEKQLRQHrlk 79
Cdd:PRK11160 339 LTLNNVSFTYpdQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIAdYSEAALRQA--- 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 80 LGILFQSWNLFPHlTALENISLplyrvhgySKEDA-DSQAMTLLNRFELAKHAHKKPA----------ELSGGQCQRVAI 148
Cdd:PRK11160 416 ISVVSQRVHLFSA-TLRDNLLL--------AAPNAsDEALIEVLQQVGLEKLLEDDKGlnawlgeggrQLSGGEQRRLGI 486
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 503691651 149 IRAIAIQPSMLLFDEPTSALDPLMTSEVLDLIVELKKeGKQFIIVTH 195
Cdd:PRK11160 487 ARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQ-NKTVLMITH 532
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
3-214 |
1.20e-24 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 95.21 E-value: 1.20e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 3 LEITQLEKAYNKQKVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDgvplifeekqlrqHRLKLGI 82
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWG-------------STVKIGY 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 83 LFQswnlfphltalenislplyrvhgyskedadsqamtllnrfelakhahkkpaeLSGGQCQRVAIIRAIAIQPSMLLFD 162
Cdd:cd03221 68 FEQ----------------------------------------------------LSGGEKMRLALAKLLLENPNLLLLD 95
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 503691651 163 EPTSALDplMTSeVLDLIVELKKEGKQFIIVTHHISFARKICDWILFLSEGK 214
Cdd:cd03221 96 EPTNHLD--LES-IEALEEALKEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
3-216 |
2.56e-24 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 96.87 E-value: 2.56e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 3 LEITQLEKAYNKQKVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVPlIFEEKQLRQHRLKLGI 82
Cdd:PRK11614 6 LSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKD-ITDWQTAKIMREAVAI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 83 LFQSWNLFPHLTALENISLPLYRVHGYSKEDADSQAMTLLNRfeLAKHAHKKPAELSGGQCQRVAIIRAIAIQPSMLLFD 162
Cdd:PRK11614 85 VPEGRRVFSRMTVEENLAMGGFFAERDQFQERIKWVYELFPR--LHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLD 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 503691651 163 EPTSALDPLMTSEVLDLIVELKKEGKQFIIVTHHISFARKICDWILFLSEGKVL 216
Cdd:PRK11614 163 EPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHVV 216
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
18-231 |
2.84e-24 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 100.70 E-value: 2.84e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 18 LKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVPL-IFEEKQLRQHRLKLGILFQS--WNLFPHLT 94
Cdd:PRK10261 340 VEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIdTLSPGKLQALRRDIQFIFQDpyASLDPRQT 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 95 ALENISLPLyRVHGY-SKEDADSQAMTLLNRFEL-AKHAHKKPAELSGGQCQRVAIIRAIAIQPSMLLFDEPTSALDPLM 172
Cdd:PRK10261 420 VGDSIMEPL-RVHGLlPGKAAAARVAWLLERVGLlPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSI 498
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 173 TSEVLDLIVELKKE-GKQFIIVTHHISFARKICDWILFLSEGKVLDSKPTSQFFDHPASP 231
Cdd:PRK10261 499 RGQIINLLLDLQRDfGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENPQHP 558
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
3-203 |
3.62e-24 |
|
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: 95.50 E-value: 3.62e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 3 LEITQLEKAYNKQKVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVPLIFEEKQLRQHRLKLGi 82
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYLG- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 83 lfQSWNLFPHLTALENISLpLYRVHGYSKEDADsQAMTLLNrfeLAKHAHKKPAELSGGQCQRVAIIRAIAIQPSMLLFD 162
Cdd:TIGR01189 80 --HLPGLKPELSALENLHF-WAAIHGGAQRTIE-DALAAVG---LTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILD 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 503691651 163 EPTSALDPlmtsEVLDLIVELKKE----GKQFIIVTHH---ISFARKI 203
Cdd:TIGR01189 153 EPTTALDK----AGVALLAGLLRAhlarGGIVLLTTHQdlgLVEAREL 196
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
17-216 |
3.80e-24 |
|
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: 96.25 E-value: 3.80e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 17 VLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDG-VPliFEEKqlRQHRLKLGILF-QSWNLFPHLT 94
Cdd:cd03267 36 ALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGlVP--WKRR--KKFLRRIGVVFgQKTQLWWDLP 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 95 ALENISLpLYRVHGYSKEDADSQAMTLLNRFELAKHAHKKPAELSGGQCQRVAIIRAIAIQPSMLLFDEPTSALDPLMTS 174
Cdd:cd03267 112 VIDSFYL-LAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQE 190
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 503691651 175 EVLDLIVELKKEGKQFIIVT-HHISFARKICDWILFLSEGKVL 216
Cdd:cd03267 191 NIRNFLKEYNRERGTTVLLTsHYMKDIEALARRVLVIDKGRLL 233
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
3-196 |
4.60e-24 |
|
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: 95.25 E-value: 4.60e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 3 LEITQLEKAYNKQKVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVPLIFEEKQLRQHRLKLGi 82
Cdd:cd03231 1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLG- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 83 lfqswnlfpHLTALENISLPLYRVHGYSKEDADSQAMTLLNRFELAKHAHKKPAELSGGQCQRVAIIRAIAIQPSMLLFD 162
Cdd:cd03231 80 ---------HAPGIKTTLSVLENLRFWHADHSDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILD 150
|
170 180 190
....*....|....*....|....*....|....
gi 503691651 163 EPTSALDPLMTSEVLDLIVELKKEGKQFIIVTHH 196
Cdd:cd03231 151 EPTTALDKAGVARFAEAMAGHCARGGMVVLTTHQ 184
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1-195 |
5.14e-24 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 95.33 E-value: 5.14e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 1 MKLEITQLEKAYNKQKVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVPLIFEEKQLRQHRL-- 78
Cdd:PRK13539 1 MMLEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACHYLgh 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 79 ----KlgilfqswnlfPHLTALENISLpLYRVHGyskeDADSQAMTLLNRFELAKHAHKKPAELSGGQCQRVAIIRAIAI 154
Cdd:PRK13539 81 rnamK-----------PALTVAENLEF-WAAFLG----GEELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVS 144
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 503691651 155 QPSMLLFDEPTSALDPLMTSEVLDLIVELKKEGKQFIIVTH 195
Cdd:PRK13539 145 NRPIWILDEPTAALDAAAVALFAELIRAHLAQGGIVIAATH 185
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
8-214 |
8.88e-24 |
|
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: 99.24 E-value: 8.88e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 8 LEKAYN-KQKVLKNINLS-IPEAQsLALLGPSGSGKSTLLRILAGLESPtcgrvnFDGvplifeeKQLRQHRLKLGILFQ 85
Cdd:TIGR03719 10 VSKVVPpKKEILKDISLSfFPGAK-IGVLGLNGAGKSTLLRIMAGVDKD------FNG-------EARPQPGIKVGYLPQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 86 SWNLFPHLTALENISLPLYRVHG-----------YSKEDADSQAM-----------------TLLNRFELAKHAHKKP-- 135
Cdd:TIGR03719 76 EPQLDPTKTVRENVEEGVAEIKDaldrfneisakYAEPDADFDKLaaeqaelqeiidaadawDLDSQLEIAMDALRCPpw 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 136 ----AELSGGQCQRVAIIRAIAIQPSMLLFDEPTSALDplmTSEVLDLIVELKKEGKQFIIVTHHISFARKICDWILFLS 211
Cdd:TIGR03719 156 dadvTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLD---AESVAWLERHLQEYPGTVVAVTHDRYFLDNVAGWILELD 232
|
...
gi 503691651 212 EGK 214
Cdd:TIGR03719 233 RGR 235
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
3-227 |
1.12e-23 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 98.83 E-value: 1.12e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 3 LEITQLEKAYNKQKVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVPLIFeekqlRQHRLKLG- 81
Cdd:PRK11288 5 LSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRF-----ASTTAALAa 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 82 ---ILFQSWNLFPHLTALENISL-PLYRVHGY-SKEDADSQAMTLLNRFELAKHAHKKPAELSGGQCQRVAIIRAIAIQP 156
Cdd:PRK11288 80 gvaIIYQELHLVPEMTVAENLYLgQLPHKGGIvNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 503691651 157 SMLLFDEPTSALDPLMTSEVLDLIVELKKEGKQFIIVTHHISFARKICDWILFLSEGKVLDSKPTSQFFDH 227
Cdd:PRK11288 160 RVIAFDEPTSSLSAREIEQLFRVIRELRAEGRVILYVSHRMEEIFALCDAITVFKDGRYVATFDDMAQVDR 230
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
16-218 |
1.35e-23 |
|
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: 99.04 E-value: 1.35e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 16 KVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVPLI-FEEKQLRQHrlkLGILFQSWNLFPHlT 94
Cdd:TIGR01193 488 NILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKdIDRHTLRQF---INYLPQEPYIFSG-S 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 95 ALENISL---------PLYRVHGYSKEDADSQAMTLLNRFELAKHAhkkpAELSGGQCQRVAIIRAIAIQPSMLLFDEPT 165
Cdd:TIGR01193 564 ILENLLLgakenvsqdEIWAACEIAEIKDDIENMPLGYQTELSEEG----SSISGGQKQRIALARALLTDSKVLILDEST 639
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 503691651 166 SALDPLMTSEVLDLIVELKKegKQFIIVTHHISFARKIcDWILFLSEGKVLDS 218
Cdd:TIGR01193 640 SNLDTITEKKIVNNLLNLQD--KTIIFVAHRLSVAKQS-DKIIVLDHGKIIEQ 689
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
20-231 |
2.38e-23 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 95.95 E-value: 2.38e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 20 NINLSIPEAQSLALLGPSGSGKSTLLRILAGLESP---TCGRVNFDGVPLI-FEEKQLRQHRL-KLGILFQ----SWNlf 90
Cdd:PRK09473 34 DLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAAngrIGGSATFNGREILnLPEKELNKLRAeQISMIFQdpmtSLN-- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 91 PHLTALENISLPLYRVHGYSKEDADSQAMTLLNRFELAKhAHKK----PAELSGGQCQRVAIIRAIAIQPSMLLFDEPTS 166
Cdd:PRK09473 112 PYMRVGEQLMEVLMLHKGMSKAEAFEESVRMLDAVKMPE-ARKRmkmyPHEFSGGMRQRVMIAMALLCRPKLLIADEPTT 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 503691651 167 ALDPLMTSEVLDLIVELKKE-GKQFIIVTHHISFARKICDWILFLSEGKVLDSKPTSQFFDHPASP 231
Cdd:PRK09473 191 ALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARDVFYQPSHP 256
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
3-225 |
2.71e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 95.16 E-value: 2.71e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 3 LEITQLEKAYNKQKVLKNIN---LSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVPLIFEekQLRQHRLK 79
Cdd:PRK13642 5 LEVENLVFKYEKESDVNQLNgvsFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAE--NVWNLRRK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 80 LGILFQSW-NLFPHLTALENISLPLYRvHGYSKEDADSQAMTLLNRFELAKHAHKKPAELSGGQCQRVAIIRAIAIQPSM 158
Cdd:PRK13642 83 IGMVFQNPdNQFVGATVEDDVAFGMEN-QGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEI 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 503691651 159 LLFDEPTSALDPLMTSEVLDLIVELKKEGKQFII-VTHHISFARKiCDWILFLSEGKVLDSKPTSQFF 225
Cdd:PRK13642 162 IILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLsITHDLDEAAS-SDRILVMKAGEIIKEAAPSELF 228
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
17-215 |
2.77e-23 |
|
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: 93.69 E-value: 2.77e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 17 VLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVPL-IFEEKQLRQhrlKLGILFQSWNLFPHlTA 95
Cdd:cd03248 29 VLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPIsQYEHKYLHS---KVSLVGQEPVLFAR-SL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 96 LENISLPLYRVHGYSKEDADSQAMTLLNRFELAK----HAHKKPAELSGGQCQRVAIIRAIAIQPSMLLFDEPTSALDpL 171
Cdd:cd03248 105 QDNIAYGLQSCSFECVKEAAQKAHAHSFISELASgydtEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALD-A 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 503691651 172 MTSEVLDLIVELKKEGKQFIIVTHHISFARKiCDWILFLSEGKV 215
Cdd:cd03248 184 ESEQQVQQALYDWPERRTVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
16-215 |
8.95e-23 |
|
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: 91.34 E-value: 8.95e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 16 KVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVPLIFeeKQLRQhRLKLGILF-----QSWNLF 90
Cdd:cd03215 14 GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTR--RSPRD-AIRAGIAYvpedrKREGLV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 91 PHLTALENISLPLYrvhgyskedadsqamtllnrfelakhahkkpaeLSGGQCQRVAIIRAIAIQPSMLLFDEPTSALDP 170
Cdd:cd03215 91 LDLSVAENIALSSL---------------------------------LSGGNQQKVVLARWLARDPRVLILDEPTRGVDV 137
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 503691651 171 LMTSEVLDLIVELKKEGKQFIIVTHHISFARKICDWILFLSEGKV 215
Cdd:cd03215 138 GAKAEIYRLIRELADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
16-215 |
1.00e-22 |
|
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: 96.43 E-value: 1.00e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 16 KVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVPLifeeKQLRQHRLK--LGILFQSWNLFpHL 93
Cdd:COG5265 372 PILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDI----RDVTQASLRaaIGIVPQDTVLF-ND 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 94 TALENIslplyrvhGYSKEDADSQAMTllnrfELAKHAH---------------------KkpaeLSGGQCQRVAIIRAI 152
Cdd:COG5265 447 TIAYNI--------AYGRPDASEEEVE-----AAARAAQihdfieslpdgydtrvgerglK----LSGGEKQRVAIARTL 509
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 503691651 153 AIQPSMLLFDEPTSALDPLMTSEVLDLIVELKKeGKQFIIVTHHISfarKI--CDWILFLSEGKV 215
Cdd:COG5265 510 LKNPPILIFDEATSALDSRTERAIQAALREVAR-GRTTLVIAHRLS---TIvdADEILVLEAGRI 570
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
13-220 |
1.39e-22 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 91.94 E-value: 1.39e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 13 NKQKVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVPLIFEEKqlrqhrlklgilfqswnlfph 92
Cdd:COG2401 41 VERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVDVPDNQFGRE--------------------- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 93 LTALENIslplyrvhgYSKEDADsQAMTLLNRFELAKHA--HKKPAELSGGQCQRVAIIRAIAIQPSMLLFDEPTSALDP 170
Cdd:COG2401 100 ASLIDAI---------GRKGDFK-DAVELLNAVGLSDAVlwLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDR 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 503691651 171 LmTSEVLDLIV--ELKKEGKQFIIVTHHISFARKIC-DWILFLSEGKVLDSKP 220
Cdd:COG2401 170 Q-TAKRVARNLqkLARRAGITLVVATHHYDVIDDLQpDLLIFVGYGGVPEEKR 221
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
3-222 |
1.42e-22 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 95.66 E-value: 1.42e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 3 LEITQLEKAYNKQKVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGL--ESPTCGRVNFDGVPLifEEKQLRQ-HRLK 79
Cdd:TIGR02633 2 LEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVypHGTWDGEIYWSGSPL--KASNIRDtERAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 80 LGILFQSWNLFPHLTALENISLPLYRVHGYSKEDADS---QAMTLLNRFELAKHAHKKP-AELSGGQCQRVAIIRAIAIQ 155
Cdd:TIGR02633 80 IVIIHQELTLVPELSVAENIFLGNEITLPGGRMAYNAmylRAKNLLRELQLDADNVTRPvGDYGGGQQQLVEIAKALNKQ 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 503691651 156 PSMLLFDEPTSALDPLMTSEVLDLIVELKKEGKQFIIVTHHISFARKICDWILFLSEGKVLDSKPTS 222
Cdd:TIGR02633 160 ARLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQHVATKDMS 226
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
17-216 |
1.45e-22 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 92.93 E-value: 1.45e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 17 VLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVPLifEEKQLRQHRLKLGILFQSWNLFPHLTAL 96
Cdd:PRK10575 26 LLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPL--ESWSSKAFARKVAYLPQQLPAAEGMTVR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 97 ENISLPLYRVHG----YSKEDAD--SQAMTLLNrfeLAKHAHKKPAELSGGQCQRVAIIRAIAIQPSMLLFDEPTSALDP 170
Cdd:PRK10575 104 ELVAIGRYPWHGalgrFGAADREkvEEAISLVG---LKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDI 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 503691651 171 LMTSEVLDLIVELKKE-GKQFIIVTHHISFARKICDWILFLSEGKVL 216
Cdd:PRK10575 181 AHQVDVLALVHRLSQErGLTVIAVLHDINMAARYCDYLVALRGGEMI 227
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
21-215 |
2.51e-22 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 95.47 E-value: 2.51e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 21 INLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVPLifeEKQLRQHRLKLGILFQSWNLFPHLTALENIs 100
Cdd:TIGR01257 949 LNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI---ETNLDAVRQSLGMCPQHNILFHHLTVAEHI- 1024
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 101 LPLYRVHGYSKEDADSQAMTLLNRFELAKHAHKKPAELSGGQCQRVAIIRAIAIQPSMLLFDEPTSALDPLMTSEVLDLI 180
Cdd:TIGR01257 1025 LFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLL 1104
|
170 180 190
....*....|....*....|....*....|....*
gi 503691651 181 VELkKEGKQFIIVTHHISFARKICDWILFLSEGKV 215
Cdd:TIGR01257 1105 LKY-RSGRTIIMSTHHMDEADLLGDRIAIISQGRL 1138
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
3-225 |
1.08e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 90.56 E-value: 1.08e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 3 LEITQLEKAYNKQK---VLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVPLifEEKQLRQHRLK 79
Cdd:PRK13650 5 IEVKNLTFKYKEDQekyTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLL--TEENVWDIRHK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 80 LGILFQSW-NLFPHLT-------ALENISLPlyrvHGYSKEDADsQAMTLLNRFELAKhahKKPAELSGGQCQRVAIIRA 151
Cdd:PRK13650 83 IGMVFQNPdNQFVGATveddvafGLENKGIP----HEEMKERVN-EALELVGMQDFKE---REPARLSGGQKQRVAIAGA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 503691651 152 IAIQPSMLLFDEPTSALDPLMTSEVLDLIVELKKE-GKQFIIVTHHISfARKICDWILFLSEGKVLDSKPTSQFF 225
Cdd:PRK13650 155 VAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDyQMTVISITHDLD-EVALSDRVLVMKNGQVESTSTPRELF 228
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
16-237 |
1.68e-21 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 90.96 E-value: 1.68e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 16 KVLKNINLSIPEAQSLALLGPSGSGKS-TLLRILAGLESPtcGRV-----NFDGVPLI-FEEKQLRQH-RLKLGILFQS- 86
Cdd:PRK11022 21 RAVDRISYSVKQGEVVGIVGESGSGKSvSSLAIMGLIDYP--GRVmaeklEFNGQDLQrISEKERRNLvGAEVAMIFQDp 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 87 -WNLFPHLTALENISLPLyRVH-GYSKEDADSQAMTLLNRFELAKHAHK---KPAELSGGQCQRVAIIRAIAIQPSMLLF 161
Cdd:PRK11022 99 mTSLNPCYTVGFQIMEAI-KVHqGGNKKTRRQRAIDLLNQVGIPDPASRldvYPHQLSGGMSQRVMIAMAIACRPKLLIA 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 503691651 162 DEPTSALDPLMTSEVLDLIVEL-KKEGKQFIIVTHHISFARKICDWILFLSEGKVLDSKPTSQFFDHPASPEIQYYL 237
Cdd:PRK11022 178 DEPTTALDVTIQAQIIELLLELqQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDIFRAPRHPYTQALL 254
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
3-240 |
3.24e-21 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 91.84 E-value: 3.24e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 3 LEITQLEKAYNKQK----VLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVPL-----------I 67
Cdd:PRK10261 13 LAVENLNIAFMQEQqkiaAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLrrrsrqvielsE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 68 FEEKQLRQHR-LKLGILFQS--WNLFPHLTALENISLPLyRVH-GYSKEDADSQAMTLLNRFELAKHA---HKKPAELSG 140
Cdd:PRK10261 93 QSAAQMRHVRgADMAMIFQEpmTSLNPVFTVGEQIAESI-RLHqGASREEAMVEAKRMLDQVRIPEAQtilSRYPHQLSG 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 141 GQCQRVAIIRAIAIQPSMLLFDEPTSALDPLMTSEVLDLIVELKKEGKQFII-VTHHISFARKICDWILFLSEGKVLDSK 219
Cdd:PRK10261 172 GMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIfITHDMGVVAEIADRVLVMYQGEAVETG 251
|
250 260
....*....|....*....|.
gi 503691651 220 PTSQFFDHPASPEIQYYLEQV 240
Cdd:PRK10261 252 SVEQIFHAPQHPYTRALLAAV 272
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
5-216 |
7.25e-21 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 91.09 E-value: 7.25e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 5 ITQLEKAYNKQKVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCgrvnFDGVPLIFEEKQLRQHRLKLGILF 84
Cdd:PLN03211 71 ISDETRQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNN----FTGTILANNRKPTKQILKRTGFVT 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 85 QSWNLFPHLTALEN-ISLPLYRV-HGYSKEDADSQAMTLLNRFELAKHAHKKPAE-----LSGGQCQRVAIIRAIAIQPS 157
Cdd:PLN03211 147 QDDILYPHLTVRETlVFCSLLRLpKSLTKQEKILVAESVISELGLTKCENTIIGNsfirgISGGERKRVSIAHEMLINPS 226
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 503691651 158 MLLFDEPTSALDPLMTSEVLDLIVELKKEGKQFIIVTHHISfAR--KICDWILFLSEGKVL 216
Cdd:PLN03211 227 LLILDEPTSGLDATAAYRLVLTLGSLAQKGKTIVTSMHQPS-SRvyQMFDSVLVLSEGRCL 286
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
13-218 |
1.86e-20 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 89.64 E-value: 1.86e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 13 NKQKVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVPL-IFEEKQLRQHrlkLGILFQSWNLFP 91
Cdd:PRK13657 346 NSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIrTVTRASLRRN---IAVVFQDAGLFN 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 92 HLTAlENISLplyrvhgySKEDAD----------SQAMTLLNRFE--LAKHAHKKPAELSGGQCQRVAIIRAIAIQPSML 159
Cdd:PRK13657 423 RSIE-DNIRV--------GRPDATdeemraaaerAQAHDFIERKPdgYDTVVGERGRQLSGGERQRLAIARALLKDPPIL 493
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 503691651 160 LFDEPTSALDPLMTSEVLDLIVELKKEGKQFIIvTHHISFARKiCDWILFLSEGKVLDS 218
Cdd:PRK13657 494 ILDEATSALDVETEAKVKAALDELMKGRTTFII-AHRLSTVRN-ADRILVFDNGRVVES 550
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
3-215 |
3.95e-20 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 88.75 E-value: 3.95e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 3 LEITQLE-KAYNKQKVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLeSPTCGRVNFDGVPL-IFEEKQLRQHrlkL 80
Cdd:PRK11174 350 IEAEDLEiLSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGF-LPYQGSLKINGIELrELDPESWRKH---L 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 81 GILFQSWNLFpHLTALENISLplyrvhgySKEDA-DSQAMTLLNRFELAKHAHKKP-----------AELSGGQCQRVAI 148
Cdd:PRK11174 426 SWVGQNPQLP-HGTLRDNVLL--------GNPDAsDEQLQQALENAWVSEFLPLLPqgldtpigdqaAGLSVGQAQRLAL 496
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 503691651 149 IRAIAIQPSMLLFDEPTSALDplMTSE--VLDLIVELKKeGKQFIIVTHHISFARKiCDWILFLSEGKV 215
Cdd:PRK11174 497 ARALLQPCQLLLLDEPTASLD--AHSEqlVMQALNAASR-RQTTLMVTHQLEDLAQ-WDQIWVMQDGQI 561
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
18-226 |
5.15e-20 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 88.57 E-value: 5.15e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 18 LKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTC---GRVNFDGVPLifeekQLRQHRLKLGILFQSWNLFPHLT 94
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGVkgsGSVLLNGMPI-----DAKEMRAISAYVQQDDLFIPTLT 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 95 ALE--NISLPLYRVHGYSKEDADSQAMTLLNRFELAKHAHKK---PAE---LSGGQCQRVAIIRAIAIQPSMLLFDEPTS 166
Cdd:TIGR00955 116 VREhlMFQAHLRMPRRVTKKEKRERVDEVLQALGLRKCANTRigvPGRvkgLSGGERKRLAFASELLTDPPLLFCDEPTS 195
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 503691651 167 ALDPLMTSEVLDLIVELKKEGKQFIIVTHHISfARKIC--DWILFLSEGKVLDSKPTSQ---FFD 226
Cdd:TIGR00955 196 GLDSFMAYSVVQVLKGLAQKGKTIICTIHQPS-SELFElfDKIILMAEGRVAYLGSPDQavpFFS 259
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
16-216 |
8.56e-20 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 86.29 E-value: 8.56e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 16 KVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDG-VPliFEEKqlRQHRLKLGILF-QSWNLFPHL 93
Cdd:COG4586 36 EAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGyVP--FKRR--KEFARRIGVVFgQRSQLWWDL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 94 TALEniSLPLYR-VHGYSKEDADSQAMTLLNRFELAKHAHKKPAELSGGQCQRVAIIRAIAIQPSMLLFDEPTSALDPLM 172
Cdd:COG4586 112 PAID--SFRLLKaIYRIPDAEYKKRLDELVELLDLGELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVS 189
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 503691651 173 TSEVLDLIVELKKEGKQFIIVT-HHISFARKICDWILFLSEGKVL 216
Cdd:COG4586 190 KEAIREFLKEYNRERGTTILLTsHDMDDIEALCDRVIVIDHGRII 234
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
17-214 |
1.63e-19 |
|
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: 83.29 E-value: 1.63e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 17 VLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDG----VPlifeekqlrQhrlklgilfQSWNLfpH 92
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGsiayVS---------Q---------EPWIQ--N 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 93 LTALENI--SLPlyrvhgYSKE-----------DADSQAMTLLNRFELakhaHKKPAELSGGQCQRVAIIRAIAIQPSML 159
Cdd:cd03250 80 GTIRENIlfGKP------FDEEryekvikacalEPDLEILPDGDLTEI----GEKGINLSGGQKQRISLARAVYSDADIY 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 503691651 160 LFDEPTSALDPLmTSEVL--DLIVELKKEGKQFIIVTHHISFARKiCDWILFLSEGK 214
Cdd:cd03250 150 LLDDPLSAVDAH-VGRHIfeNCILGLLLNNKTRILVTHQLQLLPH-ADQIVVLDNGR 204
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
18-215 |
2.55e-19 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 86.23 E-value: 2.55e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 18 LKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVPLifEEKQLRQHRLKLGILFQSWNLFPHLTAlE 97
Cdd:PRK11176 359 LRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDL--RDYTLASLRNQVALVSQNVHLFNDTIA-N 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 98 NISLPlyRVHGYSKEDAD-----SQAMTLLNRFE--LAKHAHKKPAELSGGQCQRVAIIRAIAIQPSMLLFDEPTSALDp 170
Cdd:PRK11176 436 NIAYA--RTEQYSREQIEeaarmAYAMDFINKMDngLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALD- 512
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 503691651 171 lMTSE-----VLDlivELKKEgKQFIIVTHHISFARKiCDWILFLSEGKV 215
Cdd:PRK11176 513 -TESEraiqaALD---ELQKN-RTSLVIAHRLSTIEK-ADEILVVEDGEI 556
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
11-201 |
2.85e-19 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 83.62 E-value: 2.85e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 11 AYNKQKVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVnfdgvplifeekqLRQHRLKLGILFQSWNLF 90
Cdd:PRK09544 13 SFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI-------------KRNGKLRIGYVPQKLYLD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 91 PhltaleniSLPL-----YRVH-GYSKEDadsqAMTLLNRFElAKHAHKKPAE-LSGGQCQRVAIIRAIAIQPSMLLFDE 163
Cdd:PRK09544 80 T--------TLPLtvnrfLRLRpGTKKED----ILPALKRVQ-AGHLIDAPMQkLSGGETQRVLLARALLNRPQLLVLDE 146
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 503691651 164 PTSALDPLMTSEVLDLIVELKKE-GKQFIIVTH--HISFAR 201
Cdd:PRK09544 147 PTQGVDVNGQVALYDLIDQLRRElDCAVLMVSHdlHLVMAK 187
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
10-214 |
3.29e-19 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 85.94 E-value: 3.29e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 10 KAYNKQK-VLKNINLS-IPEAQsLALLGPSGSGKSTLLRILAGLESPtcgrvnFDGvplifeEKQLrQHRLKLGILFQSW 87
Cdd:PRK11819 14 KVVPPKKqILKDISLSfFPGAK-IGVLGLNGAGKSTLLRIMAGVDKE------FEG------EARP-APGIKVGYLPQEP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 88 NLFPHLTALENISLPLYRVHG-----------YSKEDADSQA----MTLL-------------NRFELAKHAHKKP---- 135
Cdd:PRK11819 80 QLDPEKTVRENVEEGVAEVKAaldrfneiyaaYAEPDADFDAlaaeQGELqeiidaadawdldSQLEIAMDALRCPpwda 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 136 --AELSGGQCQRVAIIRAIAIQPSMLLFDEPTSALDplmtSE-VLDLIVELKKEGKQFIIVTHHISFARKICDWILFLSE 212
Cdd:PRK11819 160 kvTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLD----AEsVAWLEQFLHDYPGTVVAVTHDRYFLDNVAGWILELDR 235
|
..
gi 503691651 213 GK 214
Cdd:PRK11819 236 GR 237
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
18-223 |
6.44e-19 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 82.58 E-value: 6.44e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 18 LKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLeSPTCGRVNFDGVPLI-FEEKQLRQHRlklGILFQSWNLFPHLTAL 96
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGL-LPGQGEILLNGRPLSdWSAAELARHR---AYLSQQQSPPFAMPVF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 97 ENISlpLYRVHGYSKEDADSQAMTLLNRFELAKHAHKKPAELSGGQCQRVAIIRAI-----AIQPS--MLLFDEPTSALD 169
Cdd:COG4138 88 QYLA--LHQPAGASSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLlqvwpTINPEgqLLLLDEPMNSLD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 503691651 170 PLMTSEVLDLIVELKKEGKQFIIVTHHISFARKICDWILFLSEGKVLDSKPTSQ 223
Cdd:COG4138 166 VAQQAALDRLLRELCQQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAE 219
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
5-222 |
1.35e-18 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 84.01 E-value: 1.35e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 5 ITQLEKAYNKQKVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVPLIFEEKQlrqHRLKLGI-- 82
Cdd:PRK10982 1 MSNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSK---EALENGIsm 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 83 LFQSWNLFPHLTALENISLPLYRVHGY----SKEDADSQAmtLLNRFELAKHAHKKPAELSGGQCQRVAIIRAIAIQPSM 158
Cdd:PRK10982 78 VHQELNLVLQRSVMDNMWLGRYPTKGMfvdqDKMYRDTKA--IFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKI 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 503691651 159 LLFDEPTSALDPLMTSEVLDLIVELKKEGKQFIIVTHHISFARKICDWILFLSEGKVLDSKPTS 222
Cdd:PRK10982 156 VIMDEPTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQWIATQPLA 219
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
3-215 |
1.62e-18 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 83.91 E-value: 1.62e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 3 LEITQLekayNKQKVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVPLifeekQLR--QHRLKL 80
Cdd:COG1129 257 LEVEGL----SVGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPV-----RIRspRDAIRA 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 81 GILFQSWN-----LFPHLTALENISLPLYRVHG------YSKEDADSQAMtlLNRFEL-AKHAHKKPAELSGG-QcQRVA 147
Cdd:COG1129 328 GIAYVPEDrkgegLVLDLSIRENITLASLDRLSrgglldRRRERALAEEY--IKRLRIkTPSPEQPVGNLSGGnQ-QKVV 404
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 503691651 148 IIRAIAIQPSMLLFDEPTSALDPLMTSEVLDLIVELKKEGKQFIIVTHHISFARKICDWILFLSEGKV 215
Cdd:COG1129 405 LAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAEGKAVIVISSELPELLGLSDRILVMREGRI 472
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
13-223 |
1.69e-18 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 84.09 E-value: 1.69e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 13 NKQKVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNF-DGVPLIFeekqLRQH-RLKLGILfqswnlf 90
Cdd:COG4178 374 DGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARpAGARVLF----LPQRpYLPLGTL------- 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 91 phltaLENISLPlYRVHGYSkedaDSQAMTLLNRFELAKHAHKKPAE------LSGGQCQRVAIIRAIAIQPSMLLFDEP 164
Cdd:COG4178 443 -----REALLYP-ATAEAFS----DAELREALEAVGLGHLAERLDEEadwdqvLSLGEQQRLAFARLLLHKPDWLFLDEA 512
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 503691651 165 TSALDPLMTSEVLDLIVELKKEGKqFIIVTHHISFARkICDWILFLSEGKVLDSKPTSQ 223
Cdd:COG4178 513 TSALDEENEAALYQLLREELPGTT-VISVGHRSTLAA-FHDRVLELTGDGSWQLLPAEA 569
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
20-196 |
2.20e-18 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 80.23 E-value: 2.20e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 20 NINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVPLIFEEKQLRQHRLKLGilfqswnlfpH------- 92
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQDLLYLG----------Hqpgikte 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 93 LTALENISLpLYRVHGYSKEDADSQAmtlLNRFELAKHAHKKPAELSGGQCQRVAIIRAIAIQPSMLLFDEPTSALDPLM 172
Cdd:PRK13538 89 LTALENLRF-YQRLHGPGDDEALWEA---LAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQG 164
|
170 180
....*....|....*....|....
gi 503691651 173 TSEVLDLIVELKKEGKQFIIVTHH 196
Cdd:PRK13538 165 VARLEALLAQHAEQGGMVILTTHQ 188
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
3-196 |
5.91e-18 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 79.22 E-value: 5.91e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 3 LEITQLEKAYNKQKVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVPLifeEKQLRQHRLKLGI 82
Cdd:PRK13540 2 LDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSI---KKDLCTYQKQLCF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 83 LFQSWNLFPHLTALENIslpLYRVHGYSKEDADSQAMTLlnrFELAKHAHKKPAELSGGQCQRVAIIRAIAIQPSMLLFD 162
Cdd:PRK13540 79 VGHRSGINPYLTLRENC---LYDIHFSPGAVGITELCRL---FSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLD 152
|
170 180 190
....*....|....*....|....*....|....
gi 503691651 163 EPTSALDPLMTSEVLDLIVELKKEGKQFIIVTHH 196
Cdd:PRK13540 153 EPLVALDELSLLTIITKIQEHRAKGGAVLLTSHQ 186
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
16-231 |
1.59e-17 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 79.95 E-value: 1.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 16 KVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESP----TCGRVNFDGVPLI-FEEKQLRQ-HRLKLGILFQ--SW 87
Cdd:COG4170 21 KAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDnwhvTADRFRWNGIDLLkLSPRERRKiIGREIAMIFQepSS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 88 NLFPHLTALENI--SLP-------LYRVHGYSKEdadsQAMTLLNRFELAKHAH---KKPAELSGGQCQRVAIIRAIAIQ 155
Cdd:COG4170 101 CLDPSAKIGDQLieAIPswtfkgkWWQRFKWRKK----RAIELLHRVGIKDHKDimnSYPHELTEGECQKVMIAMAIANQ 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 503691651 156 PSMLLFDEPTSALDPLMTSEVLDLIVELKKEGKQFI-IVTHHISFARKICDWILFLSEGKVLDSKPTSQFFDHPASP 231
Cdd:COG4170 177 PRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSIlLISHDLESISQWADTITVLYCGQTVESGPTEQILKSPHHP 253
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
3-223 |
3.10e-17 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 80.07 E-value: 3.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 3 LEITQLE-KAYNKQKVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVPLifeEKQLRQHRLKLG 81
Cdd:COG3845 258 LEVENLSvRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDI---TGLSPRERRRLG 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 82 ILF-----QSWNLFPHLTALENISLPLYRVHGYSK------EDADSQAMTLLNRFEL-AKHAHKKPAELSGGQCQRVAII 149
Cdd:COG3845 335 VAYipedrLGRGLVPDMSVAENLILGRYRRPPFSRggfldrKAIRAFAEELIEEFDVrTPGPDTPARSLSGGNQQKVILA 414
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 503691651 150 RAIAIQPSMLLFDEPTSALDPLMTSEVLDLIVELKKEGKQFIIVTHHISFARKICDWILFLSEGKVLDSKPTSQ 223
Cdd:COG3845 415 RELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVLLISEDLDEILALSDRIAVMYEGRIVGEVPAAE 488
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
18-230 |
4.24e-17 |
|
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: 80.37 E-value: 4.24e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 18 LKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDG-VPLIFEEKQLRQHRLKLGILFQSwnlfphltAL 96
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGsVAYVPQQAWIQNDSLRENILFGK--------AL 725
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 97 ENislPLYRvhgyskedADSQAMTLLNRFELAKHAHK-----KPAELSGGQCQRVAIIRAIAIQPSMLLFDEPTSALDPL 171
Cdd:TIGR00957 726 NE---KYYQ--------QVLEACALLPDLEILPSGDRteigeKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAH 794
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 503691651 172 MTSEVLDLIVELKK--EGKQFIIVTHHISFARKIcDWILFLSEGKVLDSKPTSQFFDHPAS 230
Cdd:TIGR00957 795 VGKHIFEHVIGPEGvlKNKTRILVTHGISYLPQV-DVIIVMSGGKISEMGSYQELLQRDGA 854
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
15-211 |
5.99e-17 |
|
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: 75.27 E-value: 5.99e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 15 QKVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGL--------ESPTCGRVNFdgVPlifeekqlrQHrlklgilfqs 86
Cdd:cd03223 14 RVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLwpwgsgriGMPEGEDLLF--LP---------QR---------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 87 wNLFPHLTALENISLPLYRVhgyskedadsqamtllnrfelakhahkkpaeLSGGQCQRVAIIRAIAIQPSMLLFDEPTS 166
Cdd:cd03223 73 -PYLPLGTLREQLIYPWDDV-------------------------------LSGGEQQRLAFARLLLHKPKFVFLDEATS 120
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 503691651 167 ALDPLMTSEVLDLiveLKKEGKQFIIVTHHISFaRKICDWILFLS 211
Cdd:cd03223 121 ALDEESEDRLYQL---LKELGITVISVGHRPSL-WKFHDRVLDLD 161
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
16-218 |
6.66e-17 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 79.06 E-value: 6.66e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 16 KVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGL------EsptcGRVNFDGVPLIFeeKQLRQ-HRLKLGILFQSWN 88
Cdd:NF040905 15 KALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVyphgsyE----GEILFDGEVCRF--KDIRDsEALGIVIIHQELA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 89 LFPHLTALENISLPLYRVHG--YSKEDADSQAMTLLNRFELAKHAHKKPAELSGGQCQRVAIIRAIAIQPSMLLFDEPTS 166
Cdd:NF040905 89 LIPYLSIAENIFLGNERAKRgvIDWNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLILDEPTA 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 503691651 167 ALDPLMTSEVLDLIVELKKEGKQFIIVTHHISFARKICDWILFLSEGKVLDS 218
Cdd:NF040905 169 ALNEEDSAALLDLLLELKAQGITSIIISHKLNEIRRVADSITVLRDGRTIET 220
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
23-207 |
9.71e-17 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 77.02 E-value: 9.71e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 23 LSIP-EAQSLALLGPSGSGKSTLLRILAGLESPTCGRV-----------NFDGVPLIFEEKQLRQHRLKLGILFQSWNLF 90
Cdd:cd03236 20 LPVPrEGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFddppdwdeildEFRGSELQNYFTKLLEGDVKVIVKPQYVDLI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 91 PHlTALENISLPLYRVHGYSKEDadsqamTLLNRFELAKHAHKKPAELSGGQCQRVAIIRAIAIQPSMLLFDEPTSALDP 170
Cdd:cd03236 100 PK-AVKGKVGELLKKKDERGKLD------ELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDI 172
|
170 180 190
....*....|....*....|....*....|....*..
gi 503691651 171 LMTSEVLDLIVELKKEGKQFIIVTHHISFARKICDWI 207
Cdd:cd03236 173 KQRLNAARLIRELAEDDNYVLVVEHDLAVLDYLSDYI 209
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
20-218 |
1.54e-16 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 78.24 E-value: 1.54e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 20 NINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVPLifEEKQLrQHRLKLGILFQSWNLFPHLTALENI 99
Cdd:NF033858 284 HVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPV--DAGDI-ATRRRVGYMSQAFSLYGELTVRQNL 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 100 SL--PLYRVhgySKEDADSQAMTLLNRFELAKHAHKKPAELSGGQCQR----VAIIRaiaiQPSMLLFDEPTSALDPLMT 173
Cdd:NF033858 361 ELhaRLFHL---PAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRlslaVAVIH----KPELLILDEPTSGVDPVAR 433
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 503691651 174 SEVLDLIVELKKEGKQFIIVTHHisF----ARkiCDWILFLSEGKVLDS 218
Cdd:NF033858 434 DMFWRLLIELSREDGVTIFISTH--FmneaER--CDRISLMHAGRVLAS 478
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
2-234 |
2.29e-16 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 75.89 E-value: 2.29e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 2 KLEITQLeKAYNKQKVLKNINLSIPEAQSLALLGPSGSGKS----TLLRIL-AGLESpTCGRVNFDGVPLifEEKQLRQh 76
Cdd:PRK10418 4 QIELRNI-ALQAAQPLVHGVSLTLQRGRVLALVGGSGSGKSltcaAALGILpAGVRQ-TAGRVLLDGKPV--APCALRG- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 77 RLKLGILFQSWNLF-PHLTALENISLPLYRVHGYSKEDADSQAMTLLNRFELAKHAHKKPAELSGGQCQRVAIIRAIAIQ 155
Cdd:PRK10418 79 RKIATIMQNPRSAFnPLHTMHTHARETCLALGKPADDATLTAALEAVGLENAARVLKLYPFEMSGGMLQRMMIALALLCE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 156 PSMLLFDEPTSALDPLMTSEVLDLIVEL-KKEGKQFIIVTHHISFARKICDWILFLSEGKVLDSKPTSQFFDHPASPEIQ 234
Cdd:PRK10418 159 APFIIADEPTTDLDVVAQARILDLLESIvQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPKHAVTR 238
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
16-234 |
2.90e-16 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 76.38 E-value: 2.90e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 16 KVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESP----TCGRVNFDGVPLIfeEKQLRQHRLKLG----ILFQSw 87
Cdd:PRK15093 21 KAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDnwrvTADRMRFDDIDLL--RLSPRERRKLVGhnvsMIFQE- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 88 nlfPH--LTALENISLPL-------------YRVHGYSKEdadsQAMTLLNRFELAKH---AHKKPAELSGGQCQRVAII 149
Cdd:PRK15093 98 ---PQscLDPSERVGRQLmqnipgwtykgrwWQRFGWRKR----RAIELLHRVGIKDHkdaMRSFPYELTEGECQKVMIA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 150 RAIAIQPSMLLFDEPTSALDPLMTSEVLDLIVELKKEGKQFI-IVTHHISFARKICDWILFLSEGKVLDSKPTSQFFDHP 228
Cdd:PRK15093 171 IALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTIlLISHDLQMLSQWADKINVLYCGQTVETAPSKELVTTP 250
|
....*.
gi 503691651 229 ASPEIQ 234
Cdd:PRK15093 251 HHPYTQ 256
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
3-196 |
3.86e-16 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 75.10 E-value: 3.86e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 3 LEITQLEKAYNKQKVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLES--PTCGRVNFDGVPLIF---EEkqlrqhR 77
Cdd:COG0396 1 LEIKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPKyeVTSGSILLDGEDILElspDE------R 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 78 LKLGIL--FQSWNLFPHL-------TALENISLPLYRVhgyskEDADSQAMTLLNRFELAKHAHKKP--AELSGGQCQRV 146
Cdd:COG0396 75 ARAGIFlaFQYPVEIPGVsvsnflrTALNARRGEELSA-----REFLKLLKEKMKELGLDEDFLDRYvnEGFSGGEKKRN 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 503691651 147 AIIRAIAIQPSMLLFDEPTSALDPLMTSEVLDLIVELKKEGKQFIIVTHH 196
Cdd:COG0396 150 EILQMLLLEPKLAILDETDSGLDIDALRIVAEGVNKLRSPDRGILIITHY 199
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
3-216 |
4.81e-16 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 75.25 E-value: 4.81e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 3 LEITQLEKAYNKQKVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAG-LESPTC-------GRVNFDGVPLIFEEKQlR 74
Cdd:PRK13547 2 LTADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGdLTGGGAprgarvtGDVTLNGEPLAAIDAP-R 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 75 QHRLKLGILFQSWNLFPhLTALENISLPLY----RVHGYSKEDAD--SQAMTLLNRFELAKhahKKPAELSGGQCQRVAI 148
Cdd:PRK13547 81 LARLRAVLPQAAQPAFA-FSAREIVLLGRYpharRAGALTHRDGEiaWQALALAGATALVG---RDVTTLSGGELARVQF 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 503691651 149 IRAIA---------IQPSMLLFDEPTSALDPLMTSEVLDLIVELKKEGKQFII-VTHHISFARKICDWILFLSEGKVL 216
Cdd:PRK13547 157 ARVLAqlwpphdaaQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLaIVHDPNLAARHADRIAMLADGAIV 234
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
3-216 |
1.28e-15 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 74.77 E-value: 1.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 3 LEITQLEKAYNKQKVLKNINLSIPEAQSLALLGPSGSGKSTLlRILAGLESPTCGRVNFDGVPLIFEEKQLRQ----HRL 78
Cdd:NF000106 14 VEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RG-ALPAHV*GPDAGRRPWRF*TWCANRRALRRtig*HRP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 79 KLGILFQSWnlfphlTALENISLpLYRVHGYSKEDADSQAMTLLNRFELAKHAHKKPAELSGGQCQRVAIIRAIAIQPSM 158
Cdd:NF000106 93 VR*GRRESF------SGRENLYM-IGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAV 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 503691651 159 LLFDEPTSALDPLMTSEVLDLIVELKKEGKQFIIVTHHISFARKICDWILFLSEGKVL 216
Cdd:NF000106 166 LYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVI 223
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
8-170 |
3.08e-15 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 72.19 E-value: 3.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 8 LEKAYNKQKVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVPLIFEEKQlrQHRLKLGILfqsW 87
Cdd:PRK13543 17 LAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRS--RFMAYLGHL---P 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 88 NLFPHLTALENISLpLYRVHGYSKEDADSQAMTLLNrfeLAKHAHKKPAELSGGQCQRVAIIRaIAIQPSML-LFDEPTS 166
Cdd:PRK13543 92 GLKADLSTLENLHF-LCGLHGRRAKQMPGSALAIVG---LAGYEDTLVRQLSAGQKKRLALAR-LWLSPAPLwLLDEPYA 166
|
....
gi 503691651 167 ALDP 170
Cdd:PRK13543 167 NLDL 170
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
21-195 |
9.40e-15 |
|
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: 72.91 E-value: 9.40e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 21 INLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVPLifEEKQLRQHRLKLGILFQSWNLFPHLtalenis 100
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPV--TADNREAYRQLFSAVFSDFHLFDRL------- 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 101 lplyrvHGYSKEDADSQAMTLLNRFELakhAHKKPAE--------LSGGQCQRVAIIRAIAIQPSMLLFDEPTSALDP-- 170
Cdd:COG4615 422 ------LGLDGEADPARARELLERLEL---DHKVSVEdgrfsttdLSQGQRKRLALLVALLEDRPILVFDEWAADQDPef 492
|
170 180
....*....|....*....|....*..
gi 503691651 171 --LMTSEvldLIVELKKEGKQFIIVTH 195
Cdd:COG4615 493 rrVFYTE---LLPELKARGKTVIAISH 516
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
2-217 |
1.34e-14 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 72.44 E-value: 1.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 2 KLEITQLEKAYNKQK-VLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVPL-IFEEKQLRQHrlk 79
Cdd:PRK10790 340 RIDIDNVSFAYRDDNlVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLsSLSHSVLRQG--- 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 80 LGILFQSwnlfPHLTA---LENISLplyrvhgySKEDADSQAMTLLNRFELAKHAHKKPA-----------ELSGGQCQR 145
Cdd:PRK10790 417 VAMVQQD----PVVLAdtfLANVTL--------GRDISEEQVWQALETVQLAELARSLPDglytplgeqgnNLSVGQKQL 484
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503691651 146 VAIIRAIAIQPSMLLFDEPTSALDPlMTSEVLDLIVELKKEGKQFIIVTHHISFARKiCDWILFLSEGKVLD 217
Cdd:PRK10790 485 LALARVLVQTPQILILDEATANIDS-GTEQAIQQALAAVREHTTLVVIAHRLSTIVE-ADTILVLHRGQAVE 554
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
1-228 |
2.74e-14 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 71.67 E-value: 2.74e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 1 MKLEITQLEKAYNKQKVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVPLifEEKQLRQHRLKL 80
Cdd:PRK10789 314 LDVNIRQFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPL--TKLQLDSWRSRL 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 81 GILFQSWNLFPHLTAlENISL--P------------LYRVH--------GYSKEDADSQAMtllnrfelakhahkkpaeL 138
Cdd:PRK10789 392 AVVSQTPFLFSDTVA-NNIALgrPdatqqeiehvarLASVHddilrlpqGYDTEVGERGVM------------------L 452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 139 SGGQCQRVAIIRAIAIQPSMLLFDEPTSALDPLMTSEVLDlivELKK--EGKQFIIVTHHISfARKICDWILFLSEGKVL 216
Cdd:PRK10789 453 SGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILH---NLRQwgEGRTVIISAHRLS-ALTEASEILVMQHGHIA 528
|
250
....*....|..
gi 503691651 217 DSKPTSQFFDHP 228
Cdd:PRK10789 529 QRGNHDQLAQQS 540
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
4-227 |
4.32e-14 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 71.07 E-value: 4.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 4 EITQLEKAYNKQ--KV---------------LKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGvpl 66
Cdd:PRK13545 9 HVTKKYKMYNKPfdKLkdlffrskdgeyhyaLNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKG--- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 67 ifeekqlrqhrlKLGILFQSWNLFPHLTALENISLPLYRVhGYSKEDADSQAMTLLNRFELAKHAHKKPAELSGGQCQRV 146
Cdd:PRK13545 86 ------------SAALIAISSGLNGQLTGIENIELKGLMM-GLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 147 AIIRAIAIQPSMLLFDEPTSALDPLMTSEVLDLIVELKKEGKQFIIVTHHISFARKICDWILFLSEGKVLDSKPTSQFFD 226
Cdd:PRK13545 153 GFAISVHINPDILVIDEALSVGDQTFTKKCLDKMNEFKEQGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEVVD 232
|
.
gi 503691651 227 H 227
Cdd:PRK13545 233 H 233
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
18-215 |
4.35e-14 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 69.84 E-value: 4.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 18 LKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGvplifeekqlrqhrlKLGILFQSWNLFPHLTALE 97
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG---------------EVSVIAISAGLSGQLTGIE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 98 NISLPLYrVHGYSKEDADSQAMTLLNRFELAKHAHKKPAELSGGQCQRVAIIRAIAIQPSMLLFDEPTSALDPLMTSEVL 177
Cdd:PRK13546 105 NIEFKML-CMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKCL 183
|
170 180 190
....*....|....*....|....*....|....*...
gi 503691651 178 DLIVELKKEGKQFIIVTHHISFARKICDWILFLSEGKV 215
Cdd:PRK13546 184 DKIYEFKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKL 221
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
3-218 |
4.93e-14 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 69.43 E-value: 4.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 3 LEITQLEKAYNKQKVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLE--SPTCGRVNFDGVPLIFEEKQLRQHRlkl 80
Cdd:PRK09580 2 LSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLELSPEDRAGE--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 81 GIL--FQSWNLFPHLTALENISLPLYRVHGYSKEDAdsqamtlLNRFELAKHAHKK------PAEL---------SGGQC 143
Cdd:PRK09580 79 GIFmaFQYPVEIPGVSNQFFLQTALNAVRSYRGQEP-------LDRFDFQDLMEEKiallkmPEDLltrsvnvgfSGGEK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 144 QRVAIIRAIAIQPSMLLFDEPTSALDPLMTSEVLDLIVELKKEGKQFIIVTHHisfaRKICDWIL-----FLSEGKVLDS 218
Cdd:PRK09580 152 KRNDILQMAVLEPELCILDESDSGLDIDALKIVADGVNSLRDGKRSFIIVTHY----QRILDYIKpdyvhVLYQGRIVKS 227
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
18-213 |
1.35e-13 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 67.74 E-value: 1.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 18 LKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVPLIFEEKQLRQHRLKLGILF---QSWNLfpHLT 94
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRNRYSVAYaaqKPWLL--NAT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 95 ALENISL--PLYRvhgySKEDADSQAMTLLNRFELAKHAHK-----KPAELSGGQCQRVAIIRAIAIQPSMLLFDEPTSA 167
Cdd:cd03290 95 VEENITFgsPFNK----QRYKAVTDACSLQPDIDLLPFGDQteigeRGINLSGGQRQRICVARALYQNTNIVFLDDPFSA 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 503691651 168 L-----DPLMTSEVLDLiveLKKEGKQFIIVTHHISFARKiCDWILFLSEG 213
Cdd:cd03290 171 LdihlsDHLMQEGILKF---LQDDKRTLVLVTHKLQYLPH-ADWIIAMKDG 217
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
14-215 |
3.14e-13 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 68.27 E-value: 3.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 14 KQKVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVPLifeEKQLRQHRLKLGILFQSWN----- 88
Cdd:PRK09700 275 DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDI---SPRSPLDAVKKGMAYITESrrdng 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 89 LFPHLTALENISL-PLYRVHGYSKedadsqAMTLLNRFELAKHAHKKPA--------------ELSGGQCQRVAIIRAIA 153
Cdd:PRK09700 352 FFPNFSIAQNMAIsRSLKDGGYKG------AMGLFHEVDEQRTAENQREllalkchsvnqnitELSGGNQQKVLISKWLC 425
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503691651 154 IQPSMLLFDEPTSALDPLMTSEVLDLIVELKKEGKQFIIVTHHISFARKICDWILFLSEGKV 215
Cdd:PRK09700 426 CCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRL 487
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
2-195 |
3.23e-13 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 68.46 E-value: 3.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 2 KLEITQLEKAYNKQKV-LKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVPLifEEKQLRQHRLKL 80
Cdd:PRK10522 322 TLELRNVTFAYQDNGFsVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPV--TAEQPEDYRKLF 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 81 GILFQSWNLFPHLTALEnislplyrvhGYSKEDADSQAMtlLNRFELakhAHKKPAE--------LSGGQCQRVAIIRAI 152
Cdd:PRK10522 400 SAVFTDFHLFDQLLGPE----------GKPANPALVEKW--LERLKM---AHKLELEdgrisnlkLSKGQKKRLALLLAL 464
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 503691651 153 AIQPSMLLFDEPTSALDPLMTSEV-LDLIVELKKEGKQFIIVTH 195
Cdd:PRK10522 465 AEERDILLLDEWAADQDPHFRREFyQVLLPLLQEMGKTIFAISH 508
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
13-228 |
3.37e-13 |
|
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: 66.36 E-value: 3.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 13 NKQKVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVPLifeeKQLRQHRL--KLGILFQSWNLF 90
Cdd:cd03244 15 NLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDI----SKIGLHDLrsRISIIPQDPVLF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 91 PHlTALENISlPLyrvHGYSkedaDSQAMTLLNRFELAKHAHKKP-----------AELSGGQCQRVAIIRAIAIQPSML 159
Cdd:cd03244 91 SG-TIRSNLD-PF---GEYS----DEELWQALERVGLKEFVESLPggldtvveeggENLSVGQRQLLCLARALLRKSKIL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 503691651 160 LFDEPTSALDPLMTSEVLDLIVELKKeGKQFIIVTHHIsfaRKI--CDWILFLSEGKVLDskptsqfFDHP 228
Cdd:cd03244 162 VLDEATASVDPETDALIQKTIREAFK-DCTVLTIAHRL---DTIidSDRILVLDKGRVVE-------FDSP 221
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
22-195 |
5.02e-13 |
|
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: 67.89 E-value: 5.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 22 NLSIP-EAQSLALLGPSGSGKSTLLRILAGLESPTCGrvNFDGVPLIfeEKQLRQhrlklgilFQSWNLFPHLTALENIS 100
Cdd:COG1245 92 GLPVPkKGKVTGILGPNGIGKSTALKILSGELKPNLG--DYDEEPSW--DEVLKR--------FRGTELQDYFKKLANGE 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 101 L-----PLY------RVHGYSKE-----DADSQAMTLLNRFELAKHAHKKPAELSGGQCQRVAIIRAIAIQPSMLLFDEP 164
Cdd:COG1245 160 IkvahkPQYvdlipkVFKGTVREllekvDERGKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEP 239
|
170 180 190
....*....|....*....|....*....|.
gi 503691651 165 TSALDPLMTSEVLDLIVELKKEGKQFIIVTH 195
Cdd:COG1245 240 SSYLDIYQRLNVARLIRELAEEGKYVLVVEH 270
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
18-215 |
5.09e-13 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 67.72 E-value: 5.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 18 LKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVPLIFEEKQlrqHRLKLGILFQSWN-----LFPH 92
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQ---DGLANGIVYISEDrkrdgLVLG 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 93 LTALENISLP----LYRVHGYSKEDADSQAMT-LLNRFELAKHAHKKP-AELSGGQCQRVAIIRAIAIQPSMLLFDEPTS 166
Cdd:PRK10762 345 MSVKENMSLTalryFSRAGGSLKHADEQQAVSdFIRLFNIKTPSMEQAiGLLSGGNQQKVAIARGLMTRPKVLILDEPTR 424
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 503691651 167 ALDPLMTSEVLDLIVELKKEGKQFIIVTHHISFARKICDWILFLSEGKV 215
Cdd:PRK10762 425 GVDVGAKKEIYQLINQFKAEGLSIILVSSEMPEVLGMSDRILVMHEGRI 473
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
3-196 |
5.29e-13 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 66.59 E-value: 5.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 3 LEITQLEKAYNKQKVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLES--PTCGRVNFDGVPLIFEEKQLRQHrlkL 80
Cdd:CHL00131 8 LEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPAykILEGDILFKGESILDLEPEERAH---L 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 81 GIL--FQSWNLFPHLTALENISLPLYRVH-GYSKEDADSQA-----MTLLNRFELAKH-AHKKPAE-LSGGQCQRVAIIR 150
Cdd:CHL00131 85 GIFlaFQYPIEIPGVSNADFLRLAYNSKRkFQGLPELDPLEfleiiNEKLKLVGMDPSfLSRNVNEgFSGGEKKRNEILQ 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 503691651 151 AIAIQPSMLLFDEPTSALDPLMTSEVLDLIVELKKEGKQFIIVTHH 196
Cdd:CHL00131 165 MALLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIILITHY 210
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
18-215 |
1.12e-12 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 67.31 E-value: 1.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 18 LKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESP---TC----GRVNF-DGVPLIFEeKQLRQHRLkLGILFQS--- 86
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHaetSSvvirGSVAYvPQVSWIFN-ATVRENIL-FGSDFESery 710
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 87 WNLFpHLTALENiSLPLYRVHgyskedadsqamtllNRFELAKhahkKPAELSGGQCQRVAIIRAIAIQPSMLLFDEPTS 166
Cdd:PLN03232 711 WRAI-DVTALQH-DLDLLPGR---------------DLTEIGE----RGVNISGGQKQRVSMARAVYSNSDIYIFDDPLS 769
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 503691651 167 ALDPLMTSEVLDLIVELKKEGKQFIIVTHHISFARKIcDWILFLSEGKV 215
Cdd:PLN03232 770 ALDAHVAHQVFDSCMKDELKGKTRVLVTNQLHFLPLM-DRIILVSEGMI 817
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
2-201 |
1.94e-12 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 66.59 E-value: 1.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 2 KLEITQLEKAYNKQK---VLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVPLIfEEKQLRQHRL 78
Cdd:PTZ00265 382 KIQFKNVRFHYDTRKdveIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDSHNL-KDINLKWWRS 460
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 79 KLGILFQSWNLFPHlTALENISLPLYRV------HGYSKEDADS-----------------------QAMTLLNRFELAK 129
Cdd:PTZ00265 461 KIGVVSQDPLLFSN-SIKNNIKYSLYSLkdlealSNYYNEDGNDsqenknkrnscrakcagdlndmsNTTDSNELIEMRK 539
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 130 H-----------AHKK---------------------PAELSGGQCQRVAIIRAIAIQPSMLLFDEPTSALDPLMTSEVL 177
Cdd:PTZ00265 540 NyqtikdsevvdVSKKvlihdfvsalpdkyetlvgsnASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQ 619
|
250 260
....*....|....*....|....*
gi 503691651 178 DLIVELK-KEGKQFIIVTHHISFAR 201
Cdd:PTZ00265 620 KTINNLKgNENRITIIIAHRLSTIR 644
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
18-213 |
2.10e-12 |
|
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: 63.50 E-value: 2.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 18 LKNINLSIPEAQSLALLGPSGSGKSTLLriLAGLESPTCGRVN-----FDGVPLIFEeKQLrQHRLKLGIlfqswnlfph 92
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLV--NEGLYASGKARLIsflpkFSRNKLIFI-DQL-QFLIDVGL---------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 93 ltalenislplyrvhGYSKedadsqamtlLNRfelakhahkKPAELSGGQCQRVAIIRAIA--IQPSMLLFDEPTSALDP 170
Cdd:cd03238 77 ---------------GYLT----------LGQ---------KLSTLSGGELQRVKLASELFsePPGTLFILDEPSTGLHQ 122
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 503691651 171 LMTSEVLDLIVELKKEGKQFIIVTHHISFARKiCDWILFLSEG 213
Cdd:cd03238 123 QDINQLLEVIKGLIDLGNTVILIEHNLDVLSS-ADWIIDFGPG 164
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
12-223 |
2.49e-12 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 65.92 E-value: 2.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 12 YNKQKVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVN-FDGvplifeEKQLRQHRLKLG--ILF--QS 86
Cdd:NF033858 11 YGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEvLGG------DMADARHRRAVCprIAYmpQG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 87 W--NLFPHLTALENISLpLYRVHGYSKEDADSQAMTLLNRFELAKHAHKKPAELSGGQCQRVAIIRAIAIQPSMLLFDEP 164
Cdd:NF033858 85 LgkNLYPTLSVFENLDF-FGRLFGQDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCALIHDPDLLILDEP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 503691651 165 TSALDPLMTSEVLDLIVELKKE--GKQFIIVTHHISFARKiCDWILFLSEGKVLDSKPTSQ 223
Cdd:NF033858 164 TTGVDPLSRRQFWELIDRIRAErpGMSVLVATAYMEEAER-FDWLVAMDAGRVLATGTPAE 223
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
3-169 |
4.98e-12 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 64.96 E-value: 4.98e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 3 LEITQLEKAYNKQKVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNF-DGVPLIFEEkQLRQHrlklg 81
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIgETVKLAYVD-QSRDA----- 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 82 ilfqswnLFPHLTALENIS--LPLYRVHGYskeDADSQAMtlLNRFELaKHA--HKKPAELSGGQCQRVAIIRAIAIQPS 157
Cdd:TIGR03719 397 -------LDPNKTVWEEISggLDIIKLGKR---EIPSRAY--VGRFNF-KGSdqQKKVGQLSGGERNRVHLAKTLKSGGN 463
|
170
....*....|..
gi 503691651 158 MLLFDEPTSALD 169
Cdd:TIGR03719 464 VLLLDEPTNDLD 475
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
138-223 |
5.91e-12 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 64.75 E-value: 5.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 138 LSGGQCQRVAIIRAIAIQPSMLLFDEPTSALDPLMTSEVLDLIVELKKEGKQFIIVTHHISFARKICDWILFLSEGKV-- 215
Cdd:PRK10982 392 LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNGLVag 471
|
....*....
gi 503691651 216 -LDSKPTSQ 223
Cdd:PRK10982 472 iVDTKTTTQ 480
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
2-228 |
1.70e-11 |
|
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: 61.66 E-value: 1.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 2 KLEITQLEKAY--NKQKVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVPLifEEKQLRQHRLK 79
Cdd:cd03369 6 EIEVENLSVRYapDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDI--STIPLEDLRSS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 80 LGILFQSWNLFphltaLENISLPLYRVHGYSkedaDSQAMTLLNRFELAKHahkkpaeLSGGQCQRVAIIRAIAIQPSML 159
Cdd:cd03369 84 LTIIPQDPTLF-----SGTIRSNLDPFDEYS----DEEIYGALRVSEGGLN-------LSQGQRQLLCLARALLKRPRVL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 503691651 160 LFDEPTSALDPLMTSEVLDLIVELKKeGKQFIIVTHHIsfaRKI--CDWILFLSEGKVLDskptsqfFDHP 228
Cdd:cd03369 148 VLDEATASIDYATDALIQKTIREEFT-NSTILTIAHRL---RTIidYDKILVMDAGEVKE-------YDHP 207
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
11-215 |
1.94e-11 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 63.05 E-value: 1.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 11 AYNKQKVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFdgvplifeEKQLRQHRLKlgilfQ----- 85
Cdd:PRK11147 12 SFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIY--------EQDLIVARLQ-----Qdpprn 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 86 -SWNLFPHLTA-LENISLPLYRVHGYSKEDADSQAMTLLNRFE------------------------LAKHAHKKPAELS 139
Cdd:PRK11147 79 vEGTVYDFVAEgIEEQAEYLKRYHDISHLVETDPSEKNLNELAklqeqldhhnlwqlenrinevlaqLGLDPDAALSSLS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 140 GGQCQRVAIIRAIAIQPSMLLFDEPTSALDplmtsevLDLIVELKKEGKQF----IIVTHHISFARKICDWILFLSEGKV 215
Cdd:PRK11147 159 GGWLRKAALGRALVSNPDVLLLDEPTNHLD-------IETIEWLEGFLKTFqgsiIFISHDRSFIRNMATRIVDLDRGKL 231
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
3-213 |
2.19e-11 |
|
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: 63.49 E-value: 2.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 3 LEITQLEKAY--NKQKVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVPLIFEEKQLRQHrlkL 80
Cdd:TIGR01257 1938 LRLNELTKVYsgTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISDVHQN---M 2014
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 81 GILFQSWNLFPHLTALENISLpLYRVHGYSKEDADSQAMTLLNRFELAKHAHKKPAELSGGQCQRVAIIRAIAIQPSMLL 160
Cdd:TIGR01257 2015 GYCPQFDAIDDLLTGREHLYL-YARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVL 2093
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 503691651 161 FDEPTSALDPLMTSEVLDLIVELKKEGKQFIIVTHHISFARKICDWILFLSEG 213
Cdd:TIGR01257 2094 LDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKG 2146
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
24-220 |
4.03e-11 |
|
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: 60.88 E-value: 4.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 24 SIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVPLIFEEKQLRQHrlklgilfQSWNLFPHLTALENISLpl 103
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSYKPQYIKAD--------YEGTVRDLLSSITKDFY-- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 104 yrVHGYSKEDadsqamtLLNRFELAKHAHKKPAELSGGQCQRVAIIRAIAIQPSMLLFDEPTSALDP---LMTSEVLDLI 180
Cdd:cd03237 91 --THPYFKTE-------IAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVeqrLMASKVIRRF 161
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 503691651 181 VELKKegKQFIIVTHHISFARKICDWILflsegkVLDSKP 220
Cdd:cd03237 162 AENNE--KTAFVVEHDIIMIDYLADRLI------VFEGEP 193
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
33-223 |
5.29e-11 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 60.72 E-value: 5.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 33 LLGPSGSGKSTLLRILAGLeSPTCGRVNFDGVPLI-FEEKQLRQHRlklGILFQSWN------LFPHLTalenislpLYR 105
Cdd:PRK03695 27 LVGPNGAGKSTLLARMAGL-LPGSGSIQFAGQPLEaWSAAELARHR---AYLSQQQTppfampVFQYLT--------LHQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 106 VHGYSKEDADSQAMTLLNRFELAKHAHKKPAELSGGQCQRV---AIIRAI--AIQPS--MLLFDEPTSALDplMTSEV-L 177
Cdd:PRK03695 95 PDKTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVrlaAVVLQVwpDINPAgqLLLLDEPMNSLD--VAQQAaL 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 503691651 178 D-LIVELKKEGKQFIIVTHHISFARKICDWILFLSEGKVLDSKPTSQ 223
Cdd:PRK03695 173 DrLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDE 219
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
17-213 |
8.49e-11 |
|
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: 60.64 E-value: 8.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 17 VLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGvplifeekqlrqhRLKLGILFqSWnLFPHlTAL 96
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG-------------RISFSSQF-SW-IMPG-TIK 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 97 ENIslplyrVHGYSKEDADSQAMTLLNRFE--LAKHAHKKPA-------ELSGGQCQRVAIIRAIAIQPSMLLFDEPTSA 167
Cdd:cd03291 116 ENI------IFGVSYDEYRYKSVVKACQLEedITKFPEKDNTvlgeggiTLSGGQRARISLARAVYKDADLYLLDSPFGY 189
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 503691651 168 LDPLMTSEVLDLIVELKKEGKQFIIVTHHISFARKiCDWILFLSEG 213
Cdd:cd03291 190 LDVFTEKEIFESCVCKLMANKTRILVTSKMEHLKK-ADKILILHEG 234
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
3-217 |
1.15e-10 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 60.68 E-value: 1.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 3 LEITQLEKAYNKQKVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNfdgvpliFEEKQlrqhrlKLGI 82
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVK-------WSENA------NIGY 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 83 LFQ-SWNLFPH-LTALENISlplyrvhGYSKEDADSQAM-TLLNRFELAKHAHKKPAE-LSGGQCQRVAIIRAIAIQPSM 158
Cdd:PRK15064 387 YAQdHAYDFENdLTLFDWMS-------QWRQEGDDEQAVrGTLGRLLFSQDDIKKSVKvLSGGEKGRMLFGKLMMQKPNV 459
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 159 LLFDEPTSALDplMTS-EVLDLIVElKKEGkQFIIVTHHISFARKICDWILFLSEGKVLD 217
Cdd:PRK15064 460 LVMDEPTNHMD--MESiESLNMALE-KYEG-TLIFVSHDREFVSSLATRIIEITPDGVVD 515
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
21-215 |
2.54e-10 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 59.92 E-value: 2.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 21 INLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVPLIFEEKQlrqHRLKLGILF-----QSWNLFPHLTA 95
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPR---DAIRAGIMLcpedrKAEGIIPVHSV 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 96 LENISLPLYRVH---------GYSKEDADSQAMTLLNRfelAKHAHKKPAELSGGQCQRVAIIRAIAIQPSMLLFDEPTS 166
Cdd:PRK11288 349 ADNINISARRHHlragclinnRWEAENADRFIRSLNIK---TPSREQLIMNLSGGNQQKAILGRWLSEDMKVILLDEPTR 425
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 503691651 167 ALDPLMTSEVLDLIVELKKEGKQFIIVTHHISFARKICDWILFLSEGKV 215
Cdd:PRK11288 426 GIDVGAKHEIYNVIYELAAQGVAVLFVSSDLPEVLGVADRIVVMREGRI 474
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
19-223 |
2.65e-10 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 59.68 E-value: 2.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 19 KNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVPLifeEKQLRQHRLKLGILF-----QSWNLFPHL 93
Cdd:PRK15439 280 RNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEI---NALSTAQRLARGLVYlpedrQSSGLYLDA 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 94 TALENISLPLYRVHGYSKEDADSQAmtLLNRFELA-----KHAHKKPAELSGGQCQRVAIIRAIAIQPSMLLFDEPTSAL 168
Cdd:PRK15439 357 PLAWNVCALTHNRRGFWIKPARENA--VLERYRRAlnikfNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGV 434
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 503691651 169 DPLMTSEVLDLIVELKKEGKQFIIVTHHISFARKICDWILFLSEGKVLDSKPTSQ 223
Cdd:PRK15439 435 DVSARNDIYQLIRSIAAQNVAVLFISSDLEEIEQMADRVLVMHQGEISGALTGAA 489
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
22-195 |
4.71e-10 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 59.05 E-value: 4.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 22 NLSIP-EAQSLALLGPSGSGKSTLLRILAGLESPTCGrvNFDGVPLIfeEKQLRQhrlklgilFQSWNLFPHLTALENIS 100
Cdd:PRK13409 92 GLPIPkEGKVTGILGPNGIGKTTAVKILSGELIPNLG--DYEEEPSW--DEVLKR--------FRGTELQNYFKKLYNGE 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 101 L-----PLY------RVHGYSKE---DADSQAMT--LLNRFELAKHAHKKPAELSGGQCQRVAIIRAIAIQPSMLLFDEP 164
Cdd:PRK13409 160 IkvvhkPQYvdlipkVFKGKVREllkKVDERGKLdeVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEP 239
|
170 180 190
....*....|....*....|....*....|.
gi 503691651 165 TSALDPLMTSEVLDLIVELkKEGKQFIIVTH 195
Cdd:PRK13409 240 TSYLDIRQRLNVARLIREL-AEGKYVLVVEH 269
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
13-215 |
4.89e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 59.37 E-value: 4.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 13 NKQKVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGlESPTC--------GRVNFdgVPLIfeekqlrqhrlklgilf 84
Cdd:PLN03130 628 AERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLG-ELPPRsdasvvirGTVAY--VPQV----------------- 687
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 85 qSWnLFpHLTALENI--SLPLYRVHGYSKEDADS--QAMTLLNRFELAKHAhKKPAELSGGQCQRVAIIRAIAIQPSMLL 160
Cdd:PLN03130 688 -SW-IF-NATVRDNIlfGSPFDPERYERAIDVTAlqHDLDLLPGGDLTEIG-ERGVNISGGQKQRVSMARAVYSNSDVYI 763
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 503691651 161 FDEPTSALDPLMTSEVLDLIVELKKEGKQFIIVTHHISFARKIcDWILFLSEGKV 215
Cdd:PLN03130 764 FDDPLSALDAHVGRQVFDKCIKDELRGKTRVLVTNQLHFLSQV-DRIILVHEGMI 817
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
9-185 |
5.70e-10 |
|
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: 57.27 E-value: 5.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 9 EKAYNKQKVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGL----ESPTcGRVNFDGVP-LIFEEKQLRQhrlklgIL 83
Cdd:cd03233 14 GKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRtegnVSVE-GDIHYNGIPyKEFAEKYPGE------II 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 84 F--QSWNLFPHLTALENIslplyrvhgyskedadsqamtllnRFELAKHAHKKPAELSGGQCQRVAIIRAIAIQPSMLLF 161
Cdd:cd03233 87 YvsEEDVHFPTLTVRETL------------------------DFALRCKGNEFVRGISGGERKRVSIAEALVSRASVLCW 142
|
170 180
....*....|....*....|....
gi 503691651 162 DEPTSALDplmTSEVLDLIVELKK 185
Cdd:cd03233 143 DNSTRGLD---SSTALEILKCIRT 163
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
7-198 |
5.78e-10 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 59.27 E-value: 5.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 7 QLEKAYNKQKV-LKNINlsipeaqSLALLGPSGSGK-STLLRilaglespTCGRVNFDGVPLIfeEKQLRQHRLKLGILF 84
Cdd:PTZ00265 1240 QDYQGDEEQNVgMKNVN-------EFSLTKEGGSGEdSTVFK--------NSGKILLDGVDIC--DYNLKDLRNLFSIVS 1302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 85 QSWNLFpHLTALENISlplyrvhgYSKEDA--------------DSQAMTLLNRFELAKHAHKKpaELSGGQCQRVAIIR 150
Cdd:PTZ00265 1303 QEPMLF-NMSIYENIK--------FGKEDAtredvkrackfaaiDEFIESLPNKYDTNVGPYGK--SLSGGQKQRIAIAR 1371
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 503691651 151 AIAIQPSMLLFDEPTSALDPLMTSEVLDLIVELK-KEGKQFIIVTHHIS 198
Cdd:PTZ00265 1372 ALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKdKADKTIITIAHRIA 1420
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
17-169 |
1.08e-09 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 57.95 E-value: 1.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 17 VLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVnfdgvplifeekqLRQHRLKLGILFQSwnlfpHLTAL 96
Cdd:PLN03073 524 LFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTV-------------FRSAKVRMAVFSQH-----HVDGL 585
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 503691651 97 ENISLP-LYRVHGYSKEdADSQAMTLLNRFELAKHAHKKPA-ELSGGQCQRVAIIRAIAIQPSMLLFDEPTSALD 169
Cdd:PLN03073 586 DLSSNPlLYMMRCFPGV-PEQKLRAHLGSFGVTGNLALQPMyTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLD 659
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
17-213 |
1.87e-09 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 57.61 E-value: 1.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 17 VLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGvplifeekqlrqhRLKLGILFqSWnLFPHlTAL 96
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG-------------RISFSPQT-SW-IMPG-TIK 504
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 97 ENIslplyrVHGYSKEDADSQAMTLLNRFE--LAKHAHKKPA-------ELSGGQCQRVAIIRAIAIQPSMLLFDEPTSA 167
Cdd:TIGR01271 505 DNI------IFGLSYDEYRYTSVIKACQLEedIALFPEKDKTvlgeggiTLSGGQRARISLARAVYKDADLYLLDSPFTH 578
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 503691651 168 LDPLMTSEVLDLIVELKKEGKQFIIVTHHISFARKiCDWILFLSEG 213
Cdd:TIGR01271 579 LDVVTEKEIFESCLCKLMSNKTRILVTSKLEHLKK-ADKILLLHEG 623
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
14-215 |
2.86e-09 |
|
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: 56.76 E-value: 2.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 14 KQKVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTC-GRVNFDGVPLIFE--EKQLRQ-------HRLKLGIL 83
Cdd:TIGR02633 272 HRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKFeGNVFINGKPVDIRnpAQAIRAgiamvpeDRKRHGIV 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 84 fqswnlfPHLTALENISLP-LYRVHGYSKEDADSQAMTLLNRFELAKHAHKKP----AELSGGQCQRVAIIRAIAIQPSM 158
Cdd:TIGR02633 352 -------PILGVGKNITLSvLKSFCFKMRIDAAAELQIIGSAIQRLKVKTASPflpiGRLSGGNQQKAVLAKMLLTNPRV 424
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 503691651 159 LLFDEPTSALDPLMTSEVLDLIVELKKEGKQFIIVTHHISFARKICDWILFLSEGKV 215
Cdd:TIGR02633 425 LILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGKL 481
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
29-202 |
3.44e-09 |
|
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: 53.92 E-value: 3.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 29 QSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVPLIFEEKQLRQHRLKLGIlfqswnlfphltalenislplyrvhg 108
Cdd:smart00382 3 EVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGG-------------------------- 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 109 yskedadsqamtllnrfelakhahkKPAELSGGQCQRVAIIRAIAIQPSMLLFDEPTSALDPLMTSEVLDLIV------E 182
Cdd:smart00382 57 -------------------------KKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEElrllllL 111
|
170 180
....*....|....*....|
gi 503691651 183 LKKEGKQFIIVTHHISFARK 202
Cdd:smart00382 112 KSEKNLTVILTTNDEKDLGP 131
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
96-219 |
7.57e-09 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 55.64 E-value: 7.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 96 LENISLPLYRVHGYSkedADSQAMTLLNRFEL-AKHAHKKPAELSGGQCQRVAIIRAIAIQPSMLLFDEPTSALDplmTS 174
Cdd:PLN03073 305 LEEIYKRLELIDAYT---AEARAASILAGLSFtPEMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLD---LH 378
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 503691651 175 EVLDLIVELKKEGKQFIIVTHHISFARKICDWILFLSEGKVLDSK 219
Cdd:PLN03073 379 AVLWLETYLLKWPKTFIVVSHAREFLNTVVTDILHLHGQKLVTYK 423
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
12-196 |
8.26e-09 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 55.41 E-value: 8.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 12 YNKQKVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGlESPTC--------GRVNFDGvPLIFEEKQlrqHrlklgIL 83
Cdd:PRK10938 270 YNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITG-DHPQGysndltlfGRRRGSG-ETIWDIKK---H-----IG 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 84 FQSWNLfpHL-----TALENI-------SLPLYRvhgySKEDADSQ-AMTLLNRFELAKHAHKKP-AELSGGQcQRVAII 149
Cdd:PRK10938 340 YVSSSL--HLdyrvsTSVRNVilsgffdSIGIYQ----AVSDRQQKlAQQWLDILGIDKRTADAPfHSLSWGQ-QRLALI 412
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 503691651 150 -RAIAIQPSMLLFDEPTSALDPLMTSEVLDLIVELKKEGK-QFIIVTHH 196
Cdd:PRK10938 413 vRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISEGEtQLLFVSHH 461
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
15-215 |
1.53e-08 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 54.78 E-value: 1.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 15 QKVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRV----NFDGVPLifeekqlrqhrlklgilfQSWNLf 90
Cdd:PTZ00243 673 KVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVwaerSIAYVPQ------------------QAWIM- 733
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 91 pHLTALENIslpLYrvhgYSKED-ADSQAMTLLNRFE---------LAKHAHKKPAELSGGQCQRVAIIRAIAIQPSMLL 160
Cdd:PTZ00243 734 -NATVRGNI---LF----FDEEDaARLADAVRVSQLEadlaqlgggLETEIGEKGVNLSGGQKARVSLARAVYANRDVYL 805
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 503691651 161 FDEPTSALDPLMTSEVLDLIVELKKEGKQFIIVTHHISFARKiCDWILFLSEGKV 215
Cdd:PTZ00243 806 LDDPLSALDAHVGERVVEECFLGALAGKTRVLATHQVHVVPR-ADYVVALGDGRV 859
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
3-215 |
2.00e-08 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 54.41 E-value: 2.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 3 LEITQLEKAYNKQKVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNF-DGVPLIFeekqLRQHRLKlg 81
Cdd:PRK10636 313 LKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLaKGIKLGY----FAQHQLE-- 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 82 ilfqswnlfpHLTALENislPLYRVHGYSKEDADSQAMTLLNRFELAKHAHKKPAE-LSGGQCQRVAIIRAIAIQPSMLL 160
Cdd:PRK10636 387 ----------FLRADES---PLQHLARLAPQELEQKLRDYLGGFGFQGDKVTEETRrFSGGEKARLVLALIVWQRPNLLL 453
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 503691651 161 FDEPTSALDPLMTSEVLDLIVELkkEGKqFIIVTHHISFARKICDWILFLSEGKV 215
Cdd:PRK10636 454 LDEPTNHLDLDMRQALTEALIDF--EGA-LVVVSHDRHLLRSTTDDLYLVHDGKV 505
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
7-184 |
2.42e-08 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 54.34 E-value: 2.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 7 QLEKAYNKQKVLKNINLSIPEAQSLALLGPSGSGKSTLLRILA----GLESPTCGRVNFDGVPLIFEEKQLRQHRLKLGi 82
Cdd:TIGR00956 66 KKFRDTKTFDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIAsntdGFHIGVEGVITYDGITPEEIKKHYRGDVVYNA- 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 83 lfQSWNLFPHLTALENISL------PLYRVHGYSKED-ADSQAMTLLNRFELAKHAHKKPAE-----LSGGQCQRVAIIR 150
Cdd:TIGR00956 145 --ETDVHFPHLTVGETLDFaarcktPQNRPDGVSREEyAKHIADVYMATYGLSHTRNTKVGNdfvrgVSGGERKRVSIAE 222
|
170 180 190
....*....|....*....|....*....|....
gi 503691651 151 AIAIQPSMLLFDEPTSALDplmTSEVLDLIVELK 184
Cdd:TIGR00956 223 ASLGGAKIQCWDNATRGLD---SATALEFIRALK 253
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
3-169 |
5.07e-08 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 52.81 E-value: 5.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 3 LEITQLEKAYNKQKVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNF-DGVplifeekqlrqhrlKLG 81
Cdd:PRK11819 325 IEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIgETV--------------KLA 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 82 ILFQSW-NLFPHLTALENISlplyrvhgyskedaDSQAMTLLNRFELAKHAH------------KKPAELSGGQCQRVAI 148
Cdd:PRK11819 391 YVDQSRdALDPNKTVWEEIS--------------GGLDIIKVGNREIPSRAYvgrfnfkggdqqKKVGVLSGGERNRLHL 456
|
170 180
....*....|....*....|.
gi 503691651 149 IRAIAIQPSMLLFDEPTSALD 169
Cdd:PRK11819 457 AKTLKQGGNVLLLDEPTNDLD 477
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
17-171 |
5.32e-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: 5.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 17 VLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESpTCGRVNFDGVPliFEEKQLRQHRLKLGILFQSWNLFPHlTAL 96
Cdd:TIGR01271 1234 VLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVS--WNSVTLQTWRKAFGVIPQKVFIFSG-TFR 1309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 97 ENISlPLYRvhgYSKED----ADSQAM-TLLNRF--ELAKHAHKKPAELSGGQCQRVAIIRAIAIQPSMLLFDEPTSALD 169
Cdd:TIGR01271 1310 KNLD-PYEQ---WSDEEiwkvAEEVGLkSVIEQFpdKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLD 1385
|
..
gi 503691651 170 PL 171
Cdd:TIGR01271 1386 PV 1387
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
2-208 |
6.23e-08 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 52.86 E-value: 6.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 2 KLEITQLEKAYNkqkvlkNINLSIPEAQ-----SLALLGPSGSGKSTLLRILAGLESPTCGRVNFDgvplifeekqlrqh 76
Cdd:COG1245 341 LVEYPDLTKSYG------GFSLEVEGGEiregeVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDED-------------- 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 77 rLKlgilfqswnlfphltalenISL-PLYRVHGYSK------EDADSQAMT-------LLNRFELAKHAHKKPAELSGGQ 142
Cdd:COG1245 401 -LK-------------------ISYkPQYISPDYDGtveeflRSANTDDFGssyykteIIKPLGLEKLLDKNVKDLSGGE 460
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 503691651 143 CQRVAIIRAIAIQPSMLLFDEPTSALD---PLMTSEVLDLIVElkKEGKQFIIVTHHISFARKICDWIL 208
Cdd:COG1245 461 LQRVAIAACLSRDADLYLLDEPSAHLDveqRLAVAKAIRRFAE--NRGKTAMVVDHDIYLIDYISDRLM 527
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
31-199 |
9.35e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 52.12 E-value: 9.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 31 LALLGPSGSGKSTLLRILAGLESPTCGRVNFDgvplifeekqlrqhrLKLGILFQSWNLFPHLTA---LENISlPLYRVH 107
Cdd:PRK13409 368 IGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE---------------LKISYKPQYIKPDYDGTVedlLRSIT-DDLGSS 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 108 GYSKEdadsqamtLLNRFELAKHAHKKPAELSGGQCQRVAIIRAIAIQPSMLLFDEPTSALD---PLMTSEVLDLIVELK 184
Cdd:PRK13409 432 YYKSE--------IIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDveqRLAVAKAIRRIAEER 503
|
170
....*....|....*
gi 503691651 185 KegKQFIIVTHHISF 199
Cdd:PRK13409 504 E--ATALVVDHDIYM 516
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
25-196 |
1.00e-07 |
|
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: 50.26 E-value: 1.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 25 IPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVPLIFEekqlrqhrlklgilfqswnlfphltalenislPLY 104
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITPVYK--------------------------------PQY 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 105 rvhgyskedadsqamtllnrfelakhahkkpAELSGGQCQRVAIIRAIAIQPSMLLFDEPTSALDPLMTSEVLDLIVELK 184
Cdd:cd03222 70 -------------------------------IDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLS 118
|
170
....*....|..
gi 503691651 185 KEGKQFIIVTHH 196
Cdd:cd03222 119 EEGKKTALVVEH 130
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
17-215 |
1.03e-07 |
|
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: 51.39 E-value: 1.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 17 VLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESpTCGRVNFDGVPliFEEKQLRQHRLKLGILFQSWNLFphlTAL 96
Cdd:cd03289 19 VLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVS--WNSVPLQKWRKAFGVIPQKVFIF---SGT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 97 ENISLPLYRVHgyskedADSQAMTLLNRFELAKHAHKKPAE-----------LSGGQCQRVAIIRAIAIQPSMLLFDEPT 165
Cdd:cd03289 93 FRKNLDPYGKW------SDEEIWKVAEEVGLKSVIEQFPGQldfvlvdggcvLSHGHKQLMCLARSVLSKAKILLLDEPS 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 503691651 166 SALDPLmTSEVLDLIVELKKEGKQFIIVTHHISfARKICDWILFLSEGKV 215
Cdd:cd03289 167 AHLDPI-TYQVIRKTLKQAFADCTVILSEHRIE-AMLECQRFLVIEENKV 214
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
17-241 |
1.43e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 51.90 E-value: 1.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 17 VLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVPLifEEKQLRQHRLKLGILFQSWNLFphlTAL 96
Cdd:PLN03232 1251 VLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDV--AKFGLTDLRRVLSIIPQSPVLF---SGT 1325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 97 ENISLPLYRVHGYSK-----EDADSQAMTLLNRFELAKHAHKKPAELSGGQCQRVAIIRAIAIQPSMLLFDEPTSALDPL 171
Cdd:PLN03232 1326 VRFNIDPFSEHNDADlwealERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVR 1405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 172 MTSEVLDLIVELKKEGKQFIIvTHHISFARKiCDWILFLSEGKVLD--------SKPTSQFFD--HPASPEIQYYLEQVL 241
Cdd:PLN03232 1406 TDSLIQRTIREEFKSCTMLVI-AHRLNTIID-CDKILVLSSGQVLEydspqellSRDTSAFFRmvHSTGPANAQYLSNLV 1483
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
14-196 |
2.09e-07 |
|
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: 49.55 E-value: 2.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 14 KQKVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLE--SPTCGRVNFDGVPlifeekqlrqhrlkLGILFQswnlfp 91
Cdd:cd03232 19 KRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKtaGVITGEILINGRP--------------LDKNFQ------ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 92 hltalenislplyRVHGY-SKEDADSQAMTLlnRFELAKHAHKKpaELSGGQCQRVAIIRAIAIQPSMLLFDEPTSALDP 170
Cdd:cd03232 79 -------------RSTGYvEQQDVHSPNLTV--REALRFSALLR--GLSVEQRKRLTIGVELAAKPSILFLDEPTSGLDS 141
|
170 180
....*....|....*....|....*.
gi 503691651 171 LMTSEVLDLIVELKKEGkQFIIVTHH 196
Cdd:cd03232 142 QAAYNIVRFLKKLADSG-QAILCTIH 166
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
135-195 |
9.40e-07 |
|
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: 48.93 E-value: 9.40e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 503691651 135 PAELSGGQCQ---RVAIIRAIAIQPSMLLFDEPTSALDPLMTSEVLDLIVELKKEGKQFIIVTH 195
Cdd:pfam13304 234 AFELSDGTKRllaLLAALLSALPKGGLLLIDEPESGLHPKLLRRLLELLKELSRNGAQLILTTH 297
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
18-195 |
1.38e-06 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 46.97 E-value: 1.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 18 LKNINLSIPEAQSLALLGPSGSGKSTLLRILAglesptcgrvnfdgvpLIFEEKQLRQHRLKLGILfqswnlfPHLTALE 97
Cdd:cd03227 11 FVPNDVTFGEGSLTIITGPNGSGKSTILDAIG----------------LALGGAQSATRRRSGVKA-------GCIVAAV 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 98 NISLpLYRVHGyskedadsqamtllnrfelakhahkkpaeLSGGQCQRVAIIRAIAIQP----SMLLFDEPTSALDPLMT 173
Cdd:cd03227 68 SAEL-IFTRLQ-----------------------------LSGGEKELSALALILALASlkprPLYILDEIDRGLDPRDG 117
|
170 180
....*....|....*....|..
gi 503691651 174 SEVLDLIVELKKEGKQFIIVTH 195
Cdd:cd03227 118 QALAEAILEHLVKGAQVIVITH 139
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
16-215 |
1.61e-06 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 48.39 E-value: 1.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 16 KVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTC-GRVNFDGVPLIFE--EKQLRQH-------RLKLGILfq 85
Cdd:PRK13549 276 KRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPGRWeGEIFIDGKPVKIRnpQQAIAQGiamvpedRKRDGIV-- 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 86 swnlfPHLTALENISLP-LYRVHGYSKEDADSQAMTLlnRFELAKHAHKKP------AELSGGQCQRVAIIRAIAIQPSM 158
Cdd:PRK13549 354 -----PVMGVGKNITLAaLDRFTGGSRIDDAAELKTI--LESIQRLKVKTAspelaiARLSGGNQQKAVLAKCLLLNPKI 426
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 503691651 159 LLFDEPTSALDPLMTSEVLDLIVELKKEGKQFIIVTHHISFARKICDWILFLSEGKV 215
Cdd:PRK13549 427 LILDEPTRGIDVGAKYEIYKLINQLVQQGVAIIVISSELPEVLGLSDRVLVMHEGKL 483
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
18-195 |
4.38e-06 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 46.10 E-value: 4.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 18 LKNINLSIPEAQSLALLGPSGSGKSTLL---------------------RILAGLESPTCGRVNFDGVPLIFEEKQLRQH 76
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSSLAfdtiyaegqrryveslsayarQFLGQMDKPDVDSIEGLSPAIAIDQKTTSRN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 77 -RLKLGILFQSWNLFPHLTALENIS-------------LPLYRvhgyskedadsQAMTLlnrfelakhahkkpaelSGGQ 142
Cdd:cd03270 91 pRSTVGTVTEIYDYLRLLFARVGIRerlgflvdvglgyLTLSR-----------SAPTL-----------------SGGE 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 503691651 143 CQRVAIIRAIAIQPSMLL--FDEPTSALDPLMTSEVLDLIVELKKEGKQFIIVTH 195
Cdd:cd03270 143 AQRIRLATQIGSGLTGVLyvLDEPSIGLHPRDNDRLIETLKRLRDLGNTVLVVEH 197
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
17-208 |
5.04e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 47.09 E-value: 5.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 17 VLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDG---------------VP----LIFEEKQLRQHR 77
Cdd:PRK10636 16 LLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGnwqlawvnqetpalpQPaleyVIDGDREYRQLE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 78 LKLGILFQswnlfphltalENISLPLYRVHGysKEDA------DSQAMTLLNRFELAKHAHKKP-AELSGGQCQRVAIIR 150
Cdd:PRK10636 96 AQLHDANE-----------RNDGHAIATIHG--KLDAidawtiRSRAASLLHGLGFSNEQLERPvSDFSGGWRMRLNLAQ 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503691651 151 AIAIQPSMLLFDEPTSALDplmtsevLDLIVELKKEGKQF----IIVTHHISFARKICDWIL 208
Cdd:PRK10636 163 ALICRSDLLLLDEPTNHLD-------LDAVIWLEKWLKSYqgtlILISHDRDFLDPIVDKII 217
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
17-229 |
6.30e-06 |
|
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: 46.86 E-value: 6.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 17 VLKNINLSIPEAQSLALLGPSGSGKST----LLRILAGLEsptcGRVNFDGVPLifEEKQLRQHRLKLGILFQSWNLFPH 92
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSltlgLFRINESAE----GEIIIDGLNI--AKIGLHDLRFKITIIPQDPVLFSG 1374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 93 ltaleNISLPLYRVHGYSKEDA-DSQAMTLLNRF------ELAKHAHKKPAELSGGQCQRVAIIRAIAIQPSMLLFDEPT 165
Cdd:TIGR00957 1375 -----SLRMNLDPFSQYSDEEVwWALELAHLKTFvsalpdKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEAT 1449
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 503691651 166 SALDpLMTSEVLDLIVELKKEGKQFIIVTHHISfarKICDW--ILFLSEGKVldskptsQFFDHPA 229
Cdd:TIGR00957 1450 AAVD-LETDNLIQSTIRTQFEDCTVLTIAHRLN---TIMDYtrVIVLDKGEV-------AEFGAPS 1504
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
4-183 |
7.42e-06 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 46.48 E-value: 7.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 4 EITQLEKAYNKQKVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVN---------FDgvplifeekqlr 74
Cdd:PRK11147 321 EMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHcgtklevayFD------------ 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 75 QHRLKLGilfqswnlfPHLTALENIslplyrvhGYSKEDA-----DSQAMTLLNRFELA-KHAHKKPAELSGGQCQRVAI 148
Cdd:PRK11147 389 QHRAELD---------PEKTVMDNL--------AEGKQEVmvngrPRHVLGYLQDFLFHpKRAMTPVKALSGGERNRLLL 451
|
170 180 190
....*....|....*....|....*....|....*.
gi 503691651 149 IRaIAIQPSMLL-FDEPTSALDplmtSEVLDLIVEL 183
Cdd:PRK11147 452 AR-LFLKPSNLLiLDEPTNDLD----VETLELLEEL 482
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
13-198 |
1.37e-05 |
|
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: 45.51 E-value: 1.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 13 NKQKVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVPLIFEEKQlRQHrLKLGilfqswnlfph 92
Cdd:TIGR00954 463 NGDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPAKGKLFYVPQ-RPY-MTLG----------- 529
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 93 lTALENISLPL----YRVHGYSkeDADSQAMtlLNRFELaKHAHKKPA----------ELSGGQCQRVAIIRAIAIQPSM 158
Cdd:TIGR00954 530 -TLRDQIIYPDssedMKRRGLS--DKDLEQI--LDNVQL-THILEREGgwsavqdwmdVLSGGEKQRIAMARLFYHKPQF 603
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 503691651 159 LLFDEPTSALDPlmtsEVLDLIVELKKE-GKQFIIVTHHIS 198
Cdd:TIGR00954 604 AILDECTSAVSV----DVEGYMYRLCREfGITLFSVSHRKS 640
|
|
| ABC_SMC3_euk |
cd03272 |
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ... |
137-194 |
1.37e-05 |
|
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: 44.94 E-value: 1.37e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503691651 137 ELSGGQCQRVAIIRAIAIQ----PSMLLFDEPTSALDPLMTSEVLDLIVELKKeGKQFIIVT 194
Cdd:cd03272 158 QLSGGQKSLVALALIFAIQkcdpAPFYLFDEIDAALDAQYRTAVANMIKELSD-GAQFITTT 218
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
15-195 |
2.68e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 43.71 E-value: 2.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 15 QKVLKNINLSIPEAQSLALLGPSGSGKSTLLRILAGLESPTCGRVNFDGVPLIfeekqlRQHRLKLGILFQSWNLFPHLT 94
Cdd:PRK13541 13 QKNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNIN------NIAKPYCTYIGHNLGLKLEMT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 95 ALENISLplyrvhgYSK-EDADSQAMTLLNRFELAKHAHKKPAELSGGQCQRVAIIRAIAIQPSMLLFDEPTSALDPLMT 173
Cdd:PRK13541 87 VFENLKF-------WSEiYNSAETLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENR 159
|
170 180
....*....|....*....|..
gi 503691651 174 SEVLDLIVELKKEGKQFIIVTH 195
Cdd:PRK13541 160 DLLNNLIVMKANSGGIVLLSSH 181
|
|
| COG3910 |
COG3910 |
Predicted ATPase [General function prediction only]; |
160-195 |
3.69e-05 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443116 [Multi-domain] Cd Length: 239 Bit Score: 43.60 E-value: 3.69e-05
10 20 30
....*....|....*....|....*....|....*.
gi 503691651 160 LFDEPTSALDPLMTSEVLDLIVELKKEGKQFIIVTH 195
Cdd:COG3910 157 LLDEPEAALSPSRQLALLALIHDLVREGSQFIIATH 192
|
|
| ABC_SMC_head |
cd03239 |
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural ... |
138-195 |
4.80e-05 |
|
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural maintenance of chromosomes (SMC) proteins are essential for successful chromosome transmission during replication and segregation of the genome in all organisms. SMCs are generally present as single proteins in bacteria, and as at least six distinct proteins in eukaryotes. The proteins range in size from approximately 110 to 170 kDa, and each has five distinct domains: amino- and carboxy-terminal globular domains, which contain sequences characteristic of ATPases, two coiled-coil regions separating the terminal domains , and a central flexible hinge. SMC proteins function together with other proteins in a range of chromosomal transactions, including chromosome condensation, sister-chromatid cohesion, recombination, DNA repair, and epigenetic silencing of gene expression.
Pssm-ID: 213206 [Multi-domain] Cd Length: 178 Bit Score: 42.68 E-value: 4.80e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503691651 138 LSGGQCQRVAIIRAIAIQ---PSML-LFDEPTSALDPLMTSEVLDLIVELKKEGKQFIIVTH 195
Cdd:cd03239 95 LSGGEKSLSALALIFALQeikPSPFyVLDEIDAALDPTNRRRVSDMIKEMAKHTSQFIVITL 156
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
138-203 |
9.99e-05 |
|
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: 42.21 E-value: 9.99e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 503691651 138 LSGGQ------CQRVAIIRAIAIQPSMLLFDEPTSALDPLMTSEVLDLIVELKKEGK--QFIIVTHHISFARKI 203
Cdd:cd03240 116 CSGGEkvlaslIIRLALAETFGSNCGILALDEPTTNLDEENIEESLAEIIEERKSQKnfQLIVITHDEELVDAA 189
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
18-45 |
1.39e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 42.69 E-value: 1.39e-04
10 20
....*....|....*....|....*...
gi 503691651 18 LKNINLSIPEAQSLALLGPSGSGKSTLL 45
Cdd:TIGR00630 624 LKNITVSIPLGLFTCITGVSGSGKSTLI 651
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
136-205 |
1.43e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 42.89 E-value: 1.43e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 503691651 136 AELSGGQCQRVAIIRAIAIQPS--MLLFDEPTSALDPLMTSEVLDLIVELKKEGKQFIIVTHH---ISFARKICD 205
Cdd:PRK00635 475 ATLSGGEQERTALAKHLGAELIgiTYILDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEHDeqmISLADRIID 549
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
18-208 |
3.31e-04 |
|
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: 40.68 E-value: 3.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 18 LKNINLSIPEAQSLALLGPSGSGKSTLL-RILAglesPTCGRVNF--DGVPLIFEEKQLRQHRLKLGILFQS-------- 86
Cdd:cd03271 11 LKNIDVDIPLGVLTCVTGVSGSGKSSLInDTLY----PALARRLHlkKEQPGNHDRIEGLEHIDKVIVIDQSpigrtprs 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 87 -----WNLFPHLTAL------------ENISLplyRVHGysKEDADSQAMTL---LNRFELAKHAHKK------------ 134
Cdd:cd03271 87 npatyTGVFDEIRELfcevckgkrynrETLEV---RYKG--KSIADVLDMTVeeaLEFFENIPKIARKlqtlcdvglgyi 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 135 ----PA-ELSGGQCQRVAIIRAIAIQ---PSMLLFDEPTSALDPLMTSEVLDLIVELKKEGKQFIIVTHHISFArKICDW 206
Cdd:cd03271 162 klgqPAtTLSGGEAQRIKLAKELSKRstgKTLYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIEHNLDVI-KCADW 240
|
..
gi 503691651 207 IL 208
Cdd:cd03271 241 II 242
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
155-203 |
5.80e-04 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 40.37 E-value: 5.80e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 503691651 155 QPSMLLFDEPTSALDPLMTSEVLDLIVELKKEGKQFIIVTHHISFARKI 203
Cdd:COG3593 187 ANPILLIEEPEAHLHPQAQRRLLKLLKELSEKPNQVIITTHSPHLLSEV 235
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
18-48 |
7.47e-04 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 40.39 E-value: 7.47e-04
10 20 30
....*....|....*....|....*....|....*.
gi 503691651 18 LKNINLSIPeaqsLALL----GPSGSGKSTLLR-IL 48
Cdd:COG0178 621 LKNVDVEIP----LGVLtcvtGVSGSGKSTLVNdIL 652
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
18-210 |
7.70e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 40.58 E-value: 7.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 18 LKNINLSIPEAQSLALLGPSGSGKSTLL---------RILAGLESPTC------------------GRVN---------- 60
Cdd:PRK00635 611 LKDLTISLPLGRLTVVTGVSGSGKSSLIndtlvpaveEFIEQGFCSNLsiqwgaisrlvhitrdlpGRSQrsipltyika 690
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 61 FDGVPLIFEEkQLRQHRLKLGILFQSWNL----------FPHLTALEN---ISLPL----------YRVHGYSKEDADSQ 117
Cdd:PRK00635 691 FDDLRELFAE-QPRSKRLGLTKSHFSFNTplgacaecqgLGSITTTDNrtsIPCPSclgkrflpqvLEVRYKGKNIADIL 769
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 118 AMTLL---NRFELAKHAHKK----------------P-AELSGGQCQRVAI---IRAIAIQPSMLLFDEPTSALDPLMTS 174
Cdd:PRK00635 770 EMTAYeaeKFFLDEPSIHEKihalcslgldylplgrPlSSLSGGEIQRLKLayeLLAPSKKPTLYVLDEPTTGLHTHDIK 849
|
250 260 270
....*....|....*....|....*....|....*.
gi 503691651 175 EVLDLIVELKKEGKQFIIVTHHISFArKICDWILFL 210
Cdd:PRK00635 850 ALIYVLQSLTHQGHTVVIIEHNMHVV-KVADYVLEL 884
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
18-44 |
9.19e-04 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 40.01 E-value: 9.19e-04
10 20
....*....|....*....|....*..
gi 503691651 18 LKNINLSIPEAQSLALLGPSGSGKSTL 44
Cdd:COG0178 16 LKNIDVDIPRNKLVVITGLSGSGKSSL 42
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
18-44 |
9.47e-04 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 40.06 E-value: 9.47e-04
10 20
....*....|....*....|....*..
gi 503691651 18 LKNINLSIPEAQSLALLGPSGSGKSTL 44
Cdd:PRK00349 16 LKNIDLDIPRDKLVVFTGLSGSGKSSL 42
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
18-45 |
9.65e-04 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 40.06 E-value: 9.65e-04
10 20 30
....*....|....*....|....*....|..
gi 503691651 18 LKNINLSIPeaqsLALL----GPSGSGKSTLL 45
Cdd:PRK00349 625 LKNVDVEIP----LGKFtcvtGVSGSGKSTLI 652
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
18-44 |
1.13e-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: 40.00 E-value: 1.13e-03
10 20
....*....|....*....|....*..
gi 503691651 18 LKNINLSIPEAQSLALLGPSGSGKSTL 44
Cdd:TIGR00630 12 LKNIDVEIPRDKLVVITGLSGSGKSSL 38
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
135-195 |
2.65e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 38.87 E-value: 2.65e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 503691651 135 PAELSGGQ------CQRVAIIRAIAI-------QPSMLLfDEPTSALDPLMTSEVLDLIVELKKEG-KQFIIVTH 195
Cdd:PRK02224 779 PEQLSGGEralfnlSLRCAIYRLLAEgiegdapLPPLIL-DEPTVFLDSGHVSQLVDLVESMRRLGvEQIVVVSH 852
|
|
| COG1106 |
COG1106 |
ATPase/GTPase, AAA15 family [General function prediction only]; |
146-195 |
3.40e-03 |
|
ATPase/GTPase, AAA15 family [General function prediction only];
Pssm-ID: 440723 [Multi-domain] Cd Length: 330 Bit Score: 38.10 E-value: 3.40e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 503691651 146 VAIIRAIAI---QPSMLLFDEPTSALDPLMTSEVLDLIVEL-KKEGKQFIIVTH 195
Cdd:COG1106 211 LALAGALLDalaKGGVLLIDEIEASLHPSLLRKLLKLFLDLaNKNNAQLIFTTH 264
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
138-215 |
7.63e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 37.08 E-value: 7.63e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 503691651 138 LSGGQCQRVAIIRAIAIQPSMLLFDEPTSALDPLMTSEVLDLIVELKKEGKQFIIVTHHISFARKICDWILFLSEGKV 215
Cdd:NF040905 405 LSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAEGKGVIVISSELPELLGMCDRIYVMNEGRI 482
|
|
| NACHT |
COG5635 |
Predicted NTPase, NACHT family domain [Signal transduction mechanisms]; |
14-49 |
8.29e-03 |
|
Predicted NTPase, NACHT family domain [Signal transduction mechanisms];
Pssm-ID: 444362 [Multi-domain] Cd Length: 935 Bit Score: 37.09 E-value: 8.29e-03
10 20 30
....*....|....*....|....*....|....*.
gi 503691651 14 KQKVLKNINLSIPEAQSLALLGPSGSGKSTLLRILA 49
Cdd:COG5635 166 RIESLKRLELLEAKKKRLLILGEPGSGKTTLLRYLA 201
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
23-61 |
8.57e-03 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 33.73 E-value: 8.57e-03
10 20 30
....*....|....*....|....*....|....*....
gi 503691651 23 LSIPEAQSLALLGPSGSGKSTLLRILAGLESPTcGRVNF 61
Cdd:pfam13555 17 IPIDPRGNTLLTGPSGSGKSTLLDAIQTLLVPA-KRARF 54
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
131-212 |
8.71e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 37.05 E-value: 8.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503691651 131 AHKKPAELSGG---Q---CQRVAIIRAIAIQPSMLLFDEPTSALDPLMTSEVLDLIVELKKEGkQFIIVTHH---ISFAR 201
Cdd:COG4717 552 RTRPVEELSRGtreQlylALRLALAELLAGEPLPLILDDAFVNFDDERLRAALELLAELAKGR-QVIYFTCHeelVELFQ 630
|
90
....*....|.
gi 503691651 202 KICDWILFLSE 212
Cdd:COG4717 631 EEGAHVIELES 641
|
|
| |
