|
Name |
Accession |
Description |
Interval |
E-value |
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
8-229 |
1.54e-133 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 374.77 E-value: 1.54e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 8 LMQLSNIVKSYQNGDQVLKVLKGINLTVYEGEFLAIMGPSGSGKSTLMNIIGLLDRPTSGDYTLHNTKIEILNDRELAKV 87
Cdd:COG1136 4 LLELRNLTKSYGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELARL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 88 RNDEIGFVFQQFFLLAKLTALQNVELPLIYAGVNVSKRREQAKQFLEKVGLGRRIKHLPSELSGGQKQRVAIARALVNDP 167
Cdd:COG1136 84 RRRHIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNRP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2076047389 168 SIILADEPTGALDTKTGQQIMELLTELNKE-GKTIIMVTHEPEIADFATRKIIIRDGDITTDT 229
Cdd:COG1136 164 KLILADEPTGNLDSKTGEEVLELLRELNRElGTTIVMVTHDPELAARADRVIRLRDGRIVSDE 226
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
10-225 |
9.47e-120 |
|
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: 339.85 E-value: 9.47e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 10 QLSNIVKSYQNGDQVLKVLKGINLTVYEGEFLAIMGPSGSGKSTLMNIIGLLDRPTSGDYTLHNTKIEILNDRELAKVRN 89
Cdd:cd03255 2 ELKNLSKTYGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAFRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 90 DEIGFVFQQFFLLAKLTALQNVELPLIYAGVNVSKRREQAKQFLEKVGLGRRIKHLPSELSGGQKQRVAIARALVNDPSI 169
Cdd:cd03255 82 RHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPKI 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2076047389 170 ILADEPTGALDTKTGQQIMELLTELNKE-GKTIIMVTHEPEIADFATRKIIIRDGDI 225
Cdd:cd03255 162 ILADEPTGNLDSETGKEVMELLRELNKEaGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-233 |
1.29e-97 |
|
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: 284.33 E-value: 1.29e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 1 MSHEKKQLMQLSNIVKSYQNGDQVLKVLKGINLTVYEGEFLAIMGPSGSGKSTLMNIIGLLDRPTSGDYTLHNTKIEILN 80
Cdd:COG4181 1 MSSSSAPIIELRGLTKTVGTGAGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 81 DRELAKVRNDEIGFVFQQFFLLAKLTALQNVELPLIYAGVNVSkrREQAKQFLEKVGLGRRIKHLPSELSGGQKQRVAIA 160
Cdd:COG4181 81 EDARARLRARHVGFVFQSFQLLPTLTALENVMLPLELAGRRDA--RARARALLERVGLGHRLDHYPAQLSGGEQQRVALA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2076047389 161 RALVNDPSIILADEPTGALDTKTGQQIMELLTELNKE-GKTIIMVTHEPEIADFATRKIIIRDGDITTDTTASV 233
Cdd:COG4181 159 RAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRErGTTLVLVTHDPALAARCDRVLRLRAGRLVEDTAATA 232
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
8-228 |
9.73e-90 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 277.38 E-value: 9.73e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 8 LMQLSNIVKSYQNGDQVLKVLKGINLTVYEGEFLAIMGPSGSGKSTLMNIIGLLDRPTSGDYTLHNTKIEILNDRELAKV 87
Cdd:PRK10535 4 LLELKDIRRSYPSGEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 88 RNDEIGFVFQQFFLLAKLTALQNVELPLIYAGVNVSKRREQAKQFLEKVGLGRRIKHLPSELSGGQKQRVAIARALVNDP 167
Cdd:PRK10535 84 RREHFGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGG 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2076047389 168 SIILADEPTGALDTKTGQQIMELLTELNKEGKTIIMVTHEPEIADFATRKIIIRDGDITTD 228
Cdd:PRK10535 164 QVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHDPQVAAQAERVIEIRDGEIVRN 224
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
10-233 |
2.79e-84 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 249.97 E-value: 2.79e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 10 QLSNIVKSYQNGdqvLKVLKGINLTVYEGEFLAIMGPSGSGKSTLMNIIGLLDRPTSGDYTLHNTKIEILNDRELAKVRN 89
Cdd:COG2884 3 RFENVSKRYPGG---REALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 90 DeIGFVFQQFFLLAKLTALQNVELPLIYAGVNVSKRREQAKQFLEKVGLGRRIKHLPSELSGGQKQRVAIARALVNDPSI 169
Cdd:COG2884 80 R-IGVVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPEL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2076047389 170 ILADEPTGALDTKTGQQIMELLTELNKEGKTIIMVTHEPEIAD-FATRKIIIRDGDITTDTTASV 233
Cdd:COG2884 159 LLADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLELVDrMPKRVLELEDGRLVRDEARGV 223
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-209 |
2.02e-80 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 241.53 E-value: 2.02e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 1 MSHEKKQLmQLSNIVKSYQNGDQVLKVLKGINLTVYEGEFLAIMGPSGSGKSTLMNIIGLLDRPTSGdytlhntkiEILN 80
Cdd:COG1116 1 MSAAAPAL-ELRGVSKRFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSG---------EVLV 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 81 DRELAKVRNDEIGFVFQQFFLLAKLTALQNVELPLIYAGVNVSKRREQAKQFLEKVGLGRRIKHLPSELSGGQKQRVAIA 160
Cdd:COG1116 71 DGKPVTGPGPDRGVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIA 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2076047389 161 RALVNDPSIILADEPTGALDTKTGQQIMELLTEL-NKEGKTIIMVTHEPE 209
Cdd:COG1116 151 RALANDPEVLLMDEPFGALDALTRERLQDELLRLwQETGKTVLFVTHDVD 200
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
10-212 |
6.62e-80 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 243.06 E-value: 6.62e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 10 QLSNIVKSYQNGDQVLKVLKGINLTVYEGEFLAIMGPSGSGKSTLMNIIGLLDRPTSGDYTLHNTKIEILNDRELAKVRN 89
Cdd:COG1135 3 ELENLSKTFPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRAARR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 90 DeIGFVFQQFFLLAKLTALQNVELPLIYAGVNVSKRREQAKQFLEKVGLGRRIKHLPSELSGGQKQRVAIARALVNDPSI 169
Cdd:COG1135 83 K-IGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPKV 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2076047389 170 ILADEPTGALDTKTGQQIMELLTELNKE-GKTIIMVTHEPE----IAD 212
Cdd:COG1135 162 LLCDEATSALDPETTRSILDLLKDINRElGLTIVLITHEMDvvrrICD 209
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
9-206 |
2.90e-77 |
|
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: 231.98 E-value: 2.90e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 9 MQLSNIVKSYQNGDQVLKVLKGINLTVYEGEFLAIMGPSGSGKSTLMNIIGLLDRPTSGdytlhntkiEILNDRELAKVR 88
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSG---------EVLVDGEPVTGP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 89 NDEIGFVFQQFFLLAKLTALQNVELPLIYAGVNVSKRREQAKQFLEKVGLGRRIKHLPSELSGGQKQRVAIARALVNDPS 168
Cdd:cd03293 72 GPDRGYVFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPD 151
|
170 180 190
....*....|....*....|....*....|....*....
gi 2076047389 169 IILADEPTGALDTKTGQQIMELLTEL-NKEGKTIIMVTH 206
Cdd:cd03293 152 VLLLDEPFSALDALTREQLQEELLDIwRETGKTVLLVTH 190
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
11-225 |
2.30e-75 |
|
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: 227.85 E-value: 2.30e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 11 LSNIVKSYQNGDQVLKVLKGINLTVYEGEFLAIMGPSGSGKSTLMNIIGLLDRPTSGDYTLHNTKIEILNDRELAKVRNd 90
Cdd:cd03258 4 LKNVSKVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKARR- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 91 EIGFVFQQFFLLAKLTALQNVELPLIYAGVNVSKRREQAKQFLEKVGLGRRIKHLPSELSGGQKQRVAIARALVNDPSII 170
Cdd:cd03258 83 RIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKVL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2076047389 171 LADEPTGALDTKTGQQIMELLTELNKE-GKTIIMVTHEPE-IADFATRKIIIRDGDI 225
Cdd:cd03258 163 LCDEATSALDPETTQSILALLRDINRElGLTIVLITHEMEvVKRICDRVAVMEKGEV 219
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
10-232 |
4.92e-75 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 227.25 E-value: 4.92e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 10 QLSNIVKSYQNGDqvlKVLKGINLTVYEGEFLAIMGPSGSGKSTLMNIIGLLDRPTSGDYTLHNTKIEILNDRELAKVRN 89
Cdd:COG3638 4 ELRNLSKRYPGGT---PALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRRLRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 90 DeIGFVFQQFFLLAKLTALQNV------ELPLIYAGVN-VSKR-REQAKQFLEKVGLGRRIKHLPSELSGGQKQRVAIAR 161
Cdd:COG3638 81 R-IGMIFQQFNLVPRLSVLTNVlagrlgRTSTWRSLLGlFPPEdRERALEALERVGLADKAYQRADQLSGGQQQRVAIAR 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2076047389 162 ALVNDPSIILADEPTGALDTKTGQQIMELLTELNKE-GKTIIMVTHEPEIA-DFATRKIIIRDGDITTDTTAS 232
Cdd:COG3638 160 ALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREdGITVVVNLHQVDLArRYADRIIGLRDGRVVFDGPPA 232
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
10-236 |
7.47e-74 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 224.10 E-value: 7.47e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 10 QLSNIVKSYqnGDqvLKVLKGINLTVYEGEFLAIMGPSGSGKSTLMNIIGLLDRPTSGDYTLHNTKIeILNDRELAKVRn 89
Cdd:COG1126 3 EIENLHKSF--GD--LEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDL-TDSKKDINKLR- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 90 DEIGFVFQQFFLLAKLTALQNVELPLIYA-GVNVSKRREQAKQFLEKVGLGRRIKHLPSELSGGQKQRVAIARALVNDPS 168
Cdd:COG1126 77 RKVGMVFQQFNLFPHLTVLENVTLAPIKVkKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPK 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2076047389 169 IILADEPTGALDTKTGQQIMELLTELNKEGKTIIMVTHEPEIA-DFATRKIIIRDGDITTDTTASVVID 236
Cdd:COG1126 157 VMLFDEPTSALDPELVGEVLDVMRDLAKEGMTMVVVTHEMGFArEVADRVVFMDGGRIVEEGPPEEFFE 225
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
11-220 |
9.83e-74 |
|
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: 222.49 E-value: 9.83e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 11 LSNIVKSYQNgdqvLKVLKGINLTVYEGEFLAIMGPSGSGKSTLMNIIGLLDRPTSGDYTLHNTKIEILNDRELAKVRND 90
Cdd:TIGR03608 1 LKNISKKFGD----KVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLNSKKASKFRRE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 91 EIGFVFQQFFLLAKLTALQNVELPLIYAGVNVSKRREQAKQFLEKVGLGRRIKHLPSELSGGQKQRVAIARALVNDPSII 170
Cdd:TIGR03608 77 KLGYLFQNFALIENETVEENLDLGLKYKKLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLI 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2076047389 171 LADEPTGALDTKTGQQIMELLTELNKEGKTIIMVTHEPEIADFATRKIII 220
Cdd:TIGR03608 157 LADEPTGSLDPKNRDEVLDLLLELNDEGKTIIIVTHDPEVAKQADRVIEL 206
|
|
| ABC_ATP_DarD |
NF038007 |
darobactin export ABC transporter ATP-binding protein; |
8-225 |
1.15e-72 |
|
darobactin export ABC transporter ATP-binding protein;
Pssm-ID: 411600 [Multi-domain] Cd Length: 218 Bit Score: 220.36 E-value: 1.15e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 8 LMQLSNIVKSYQNGDQVLKVLKGINLTVYEGEFLAIMGPSGSGKSTLMNIIGLLDRPTSGDYTLHNTKIEILNDRELAKV 87
Cdd:NF038007 1 MLNMQNAEKCYITKTIKTKVLNHLNFSVEKGDFVSIMGPSGSGKSTLLNIIGMFDSLDSGSLTLAGKEVTNLSYSQKIIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 88 RNDEIGFVFQQFFLLAKLTALQNVELPLIYAGVNVSKRREQAKQFLEKVGLGRRIKHLPSELSGGQKQRVAIARALVNDP 167
Cdd:NF038007 81 RRELIGYIFQSFNLIPHLSIFDNVALPLKYRGVAKKERIERVNQVLNLFGIDNRRNHKPMQLSGGQQQRVAIARAMVSNP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2076047389 168 SIILADEPTGALDTKTGQQIMELLTELNKEGKTIIMVTHEPEIADFATRKIIIRDGDI 225
Cdd:NF038007 161 ALLLADEPTGNLDSKNARAVLQQLKYINQKGTTIIMVTHSDEASTYGNRIINMKDGKL 218
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
8-230 |
1.85e-71 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 217.76 E-value: 1.85e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 8 LMQLSNIVKSYQNGDQVLKVLKGINLTVYEGEFLAIMGPSGSGKSTLMNIIGLLDRPTSGDYTLHNTKIEILNDRELAKV 87
Cdd:PRK11629 5 LLQCDNLCKRYQEGSVQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAEL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 88 RNDEIGFVFQQFFLLAKLTALQNVELPLIYAGVNVSKRREQAKQFLEKVGLGRRIKHLPSELSGGQKQRVAIARALVNDP 167
Cdd:PRK11629 85 RNQKLGFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNP 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2076047389 168 SIILADEPTGALDTKTGQQIMELLTELN-KEGKTIIMVTHEPEIADFATRKIIIRDGDITTDTT 230
Cdd:PRK11629 165 RLVLADEPTGNLDARNADSIFQLLGELNrLQGTAFLVVTHDLQLAKRMSRQLEMRDGRLTAELS 228
|
|
| heterocyst_DevA |
TIGR02982 |
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly ... |
11-225 |
2.38e-70 |
|
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly in the Cyanobacteria, but also in the Planctomycetes. Cyanobacterial examples are involved in heterocyst formation, by which some fraction of members of the colony undergo a developmental change and become capable of nitrogen fixation. The DevBCA proteins are thought export of either heterocyst-specific glycolipids or an enzyme essential for formation of the laminated layer found in heterocysts.
Pssm-ID: 274374 [Multi-domain] Cd Length: 220 Bit Score: 214.50 E-value: 2.38e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 11 LSNIVKSYQNGDQVLKVLKGINLTVYEGEFLAIMGPSGSGKSTLMNIIGLLDRPTSGDYTLHNTKIEILNDRELAKVRNd 90
Cdd:TIGR02982 4 IRNLNHYYGHGSLRKQVLFDINLEINPGEIVILTGPSGSGKTTLLTLIGGLRSVQEGSLKVLGQELHGASKKQLVQLRR- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 91 EIGFVFQQFFLLAKLTALQNVELPL-IYAGVNVSKRREQAKQFLEKVGLGRRIKHLPSELSGGQKQRVAIARALVNDPSI 169
Cdd:TIGR02982 83 RIGYIFQAHNLLGFLTARQNVQMALeLQPNLSYQEARERARAMLEAVGLGDHLNYYPHNLSGGQKQRVAIARALVHHPKL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2076047389 170 ILADEPTGALDTKTGQQIMELLTELNKE-GKTIIMVTHEPEIADFATRKIIIRDGDI 225
Cdd:TIGR02982 163 VLADEPTAALDSKSGRDVVELMQKLAKEqGCTILMVTHDNRILDVADRILQMEDGKL 219
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
10-225 |
1.53e-68 |
|
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: 209.69 E-value: 1.53e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 10 QLSNIVKSYqnGDQvlKVLKGINLTVYEGEFLAIMGPSGSGKSTLMNIIGLLDRPTSGDYTLHNTKIEIlNDRELAKVRN 89
Cdd:cd03262 2 EIKNLHKSF--GDF--HVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTD-DKKNINELRQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 90 dEIGFVFQQFFLLAKLTALQNVELPLIYA-GVNVSKRREQAKQFLEKVGLGRRIKHLPSELSGGQKQRVAIARALVNDPS 168
Cdd:cd03262 77 -KVGMVFQQFNLFPHLTVLENITLAPIKVkGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPK 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2076047389 169 IILADEPTGALDTKTGQQIMELLTELNKEGKTIIMVTHEPEIA-DFATRKIIIRDGDI 225
Cdd:cd03262 156 VMLFDEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFArEVADRVIFMDDGRI 213
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
10-223 |
6.95e-67 |
|
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: 205.56 E-value: 6.95e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 10 QLSNIVKSYQNGDQVLKvlkGINLTVYEGEFLAIMGPSGSGKSTLMNIIGLLDRPTSGDYTLHNTKIEILNDRELAKVRN 89
Cdd:TIGR02673 3 EFHNVSKAYPGGVAALH---DVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLRGRQLPLLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 90 dEIGFVFQQFFLLAKLTALQNVELPLIYAGVNVSKRREQAKQFLEKVGLGRRIKHLPSELSGGQKQRVAIARALVNDPSI 169
Cdd:TIGR02673 80 -RIGVVFQDFRLLPDRTVYENVALPLEVRGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPPL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2076047389 170 ILADEPTGALDTKTGQQIMELLTELNKEGKTIIMVTHEPEIAD-FATRKIIIRDG 223
Cdd:TIGR02673 159 LLADEPTGNLDPDLSERILDLLKRLNKRGTTVIVATHDLSLVDrVAHRVIILDDG 213
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
8-223 |
7.71e-67 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 205.78 E-value: 7.71e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 8 LMQLSNIVKSYQNGDQVLKVLKGINLTVYEGEFLAIMGPSGSGKSTLMNIIGLLDRPTSGDYTLHNTKIEILNDRELAKV 87
Cdd:PRK10584 6 IVEVHHLKKSVGQGEHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 88 RNDEIGFVFQQFFLLAKLTALQNVELPLIYAGVNVSKRREQAKQFLEKVGLGRRIKHLPSELSGGQKQRVAIARALVNDP 167
Cdd:PRK10584 86 RAKHVGFVFQSFMLIPTLNALENVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRP 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2076047389 168 SIILADEPTGALDTKTGQQIMELLTELNKE-GKTIIMVTHEPEIADFATRKIIIRDG 223
Cdd:PRK10584 166 DVLFADEPTGNLDRQTGDKIADLLFSLNREhGTTLILVTHDLQLAARCDRRLRLVNG 222
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
10-225 |
1.25e-65 |
|
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: 203.29 E-value: 1.25e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 10 QLSNIVKSYqnGDQVlkVLKGINLTVYEGEFLAIMGPSGSGKSTLMNIIGLLDRPTSGDYTLHNTKIEILNDRELAKVRN 89
Cdd:COG1127 7 EVRNLTKSF--GDRV--VLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 90 dEIGFVFQQFFLLAKLTALQNVELPLI-YAGVNVSKRREQAKQFLEKVGLGRRIKHLPSELSGGQKQRVAIARALVNDPS 168
Cdd:COG1127 83 -RIGMLFQGGALFDSLTVFENVAFPLReHTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDPE 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2076047389 169 IILADEPTGALDTKTGQQIMELLTELNKE-GKTIIMVTHE-PEIADFATRKIIIRDGDI 225
Cdd:COG1127 162 ILLYDEPTAGLDPITSAVIDELIRELRDElGLTSVVVTHDlDSAFAIADRVAVLADGKI 220
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
10-232 |
5.41e-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: 5.41e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 10 QLSNIVKSYQNGDQVLKvlkGINLTVYEGEFLAIMGPSGSGKSTLMNIIGLLDRPTSGDYTLHNTKIEILNDRELAKVRn 89
Cdd:cd03256 2 EVENLSKTYPNGKKALK---DVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLR- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 90 DEIGFVFQQFFLLAKLTALQNV------ELPLIYAGVN-VSKR-REQAKQFLEKVGLGRRIKHLPSELSGGQKQRVAIAR 161
Cdd:cd03256 78 RQIGMIFQQFNLIERLSVLENVlsgrlgRRSTWRSLFGlFPKEeKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIAR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2076047389 162 ALVNDPSIILADEPTGALDTKTGQQIMELLTELNKE-GKTIIMVTHEPEIA-DFATRKIIIRDGDITTDTTAS 232
Cdd:cd03256 158 ALMQQPKLILADEPVASLDPASSRQVMDLLKRINREeGITVIVSLHQVDLArEYADRIVGLKDGRIVFDGPPA 230
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
10-235 |
1.05e-64 |
|
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: 200.64 E-value: 1.05e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 10 QLSNIVKSYQNGDQVLKvlkGINLTVYEGEFLAIMGPSGSGKSTLMNII-GLLdRPTSGDYTLHNTKIEILNDRELAKvr 88
Cdd:COG1122 2 ELENLSFSYPGGTPALD---DVSLSIEKGEFVAIIGPNGSGKSTLLRLLnGLL-KPTSGEVLVDGKDITKKNLRELRR-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 89 ndEIGFVFQ----QFFllaKLTALQNVELPLIYAGVNVSKRREQAKQFLEKVGLGRRIKHLPSELSGGQKQRVAIARALV 164
Cdd:COG1122 76 --KVGLVFQnpddQLF---APTVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2076047389 165 NDPSIILADEPTGALDTKTGQQIMELLTELNKEGKTIIMVTHEPE-IADFATRKIIIRDGDITTDTTASVVI 235
Cdd:COG1122 151 MEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDlVAELADRVIVLDDGRIVADGTPREVF 222
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
10-223 |
3.97e-64 |
|
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: 198.46 E-value: 3.97e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 10 QLSNIVKSYQNGDQvlKVLKGINLTVYEGEFLAIMGPSGSGKSTLMNIIGLLDRPTSGDYTLHNTKIEILNDRELAKvrn 89
Cdd:cd03225 1 ELKNLSFSYPDGAR--PALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRR--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 90 dEIGFVFQ----QFFllaKLTALQNVELPLIYAGVNVSKRREQAKQFLEKVGLGRRIKHLPSELSGGQKQRVAIARALVN 165
Cdd:cd03225 76 -KVGLVFQnpddQFF---GPTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAM 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2076047389 166 DPSIILADEPTGALDTKTGQQIMELLTELNKEGKTIIMVTHEPE-IADFATRKIIIRDG 223
Cdd:cd03225 152 DPDILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDlLLELADRVIVLEDG 210
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
8-236 |
6.64e-64 |
|
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: 207.06 E-value: 6.64e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 8 LMQLSNIVKSY-QNGDQVLKVLKGINLTVYEGEFLAIMGPSGSGKSTLMNIIGLLDRPTSGDYTLHNTKIEILNDRELAK 86
Cdd:COG1123 260 LLEVRNLSKRYpVRGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLRE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 87 VRNDeIGFVFQ----QFFllAKLTALQNVELPL-IYAGVNVSKRREQAKQFLEKVGLGRRIKH-LPSELSGGQKQRVAIA 160
Cdd:COG1123 340 LRRR-VQMVFQdpysSLN--PRMTVGDIIAEPLrLHGLLSRAERRERVAELLERVGLPPDLADrYPHELSGGQRQRVAIA 416
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2076047389 161 RALVNDPSIILADEPTGALDTKTGQQIMELLTELNKE-GKTIIMVTHE-PEIADFATRKIIIRDGDITTDTTASVVID 236
Cdd:COG1123 417 RALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRElGLTYLFISHDlAVVRYIADRVAVMYDGRIVEDGPTEEVFA 494
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
8-225 |
1.55e-63 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 201.48 E-value: 1.55e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 8 LMQLSNIVKSYqnGDQVlkVLKGINLTVYEGEFLAIMGPSGSGKSTLMNIIGLLDRPTSGDytlhntkIeILNDRELAKV 87
Cdd:COG3842 5 ALELENVSKRY--GDVT--ALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGR-------I-LLDGRDVTGL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 88 ----RNdeIGFVFQQFFLLAKLTALQNVELPLIYAGVNVSKRREQAKQFLEKVGLGRRIKHLPSELSGGQKQRVAIARAL 163
Cdd:COG3842 73 ppekRN--VGMVFQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARAL 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2076047389 164 VNDPSIILADEPTGALDTKTGQQIMELLTELNKE-GKTIIMVTHEPE----IADfatRKIIIRDGDI 225
Cdd:COG3842 151 APEPRVLLLDEPLSALDAKLREEMREELRRLQRElGITFIYVTHDQEealaLAD---RIAVMNDGRI 214
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
8-225 |
8.25e-62 |
|
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: 193.11 E-value: 8.25e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 8 LMQLSNIVKSYQNGDQVLKVLKGINLTVYEGEFLAIMGPSGSGKSTLMNIIGLLDRPTSGDYTLHNTKIEILnDRELAKV 87
Cdd:cd03257 1 LLEVKNLSVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKL-SRRLRKI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 88 RNDEIGFVFQQFF--LLAKLTALQNVELPLIYAGVNVSKRREQAKQFLEKVGLG---RRIKHLPSELSGGQKQRVAIARA 162
Cdd:cd03257 80 RRKEIQMVFQDPMssLNPRMTIGEQIAEPLRIHGKLSKKEARKEAVLLLLVGVGlpeEVLNRYPHELSGGQRQRVAIARA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2076047389 163 LVNDPSIILADEPTGALDTKTGQQIMELLTELNKE-GKTIIMVTHEPE-IADFATRKIIIRDGDI 225
Cdd:cd03257 160 LALNPKLLIADEPTSALDVSVQAQILDLLKKLQEElGLTLLFITHDLGvVAKIADRVAVMYAGKI 224
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
8-236 |
1.50e-61 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 193.00 E-value: 1.50e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 8 LMQLSNIVKSYqnGDqvLKVLKGINLTVYEGEFLAIMGPSGSGKSTLMNIIGLLDRPTSGDYTLHNTKIeilNDRElAKV 87
Cdd:PRK09493 1 MIEFKNVSKHF--GP--TQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKV---NDPK-VDE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 88 RN--DEIGFVFQQFFLLAKLTALQNVEL-PLIYAGVNVSKRREQAKQFLEKVGLGRRIKHLPSELSGGQKQRVAIARALV 164
Cdd:PRK09493 73 RLirQEAGMVFQQFYLFPHLTALENVMFgPLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2076047389 165 NDPSIILADEPTGALDTKTGQQIMELLTELNKEGKTIIMVTHEPEIA-DFATRKIIIRDGDITTDTTASVVID 236
Cdd:PRK09493 153 VKPKLMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAeKVASRLIFIDKGRIAEDGDPQVLIK 225
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
10-225 |
2.42e-60 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 193.09 E-value: 2.42e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 10 QLSNIVKSYQNGDQVLKVLKGINLTVYEGEFLAIMGPSGSGKSTLMNIIGLLDRPTSGDYTLHNTKIEILNDRELAKVRN 89
Cdd:PRK11153 3 ELKNISKVFPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKARR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 90 DeIGFVFQQFFLLAKLTALQNVELPLIYAGVNVSKRREQAKQFLEKVGLGRRIKHLPSELSGGQKQRVAIARALVNDPSI 169
Cdd:PRK11153 83 Q-IGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPKV 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2076047389 170 ILADEPTGALDTKTGQQIMELLTELNKE-GKTIIMVTHEPE----IADfatRKIIIRDGDI 225
Cdd:PRK11153 162 LLCDEATSALDPATTRSILELLKDINRElGLTIVLITHEMDvvkrICD---RVAVIDAGRL 219
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
9-225 |
2.46e-60 |
|
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: 188.88 E-value: 2.46e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 9 MQLSNIVKSYqnGDQVlkVLKGINLTVYEGEFLAIMGPSGSGKSTLMNIIGLLDRPTSGDytlhntkIEIlNDRELAKV- 87
Cdd:cd03259 1 LELKGLSKTY--GSVR--ALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGE-------ILI-DGRDVTGVp 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 88 ---RNdeIGFVFQQFFLLAKLTALQNVELPLIYAGVNVSKRREQAKQFLEKVGLGRRIKHLPSELSGGQKQRVAIARALV 164
Cdd:cd03259 69 perRN--IGMVFQDYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2076047389 165 NDPSIILADEPTGALDTKTGQQIMELLTELNKE-GKTIIMVTHEP-EIADFATRKIIIRDGDI 225
Cdd:cd03259 147 REPSLLLLDEPLSALDAKLREELREELKELQRElGITTIYVTHDQeEALALADRIAVMNEGRI 209
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
13-225 |
4.65e-60 |
|
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: 188.00 E-value: 4.65e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 13 NIVKSYQNGdqvLKVLKGINLTVYEGEFLAIMGPSGSGKSTLMNIIGLLDRPTSGDYTLHNTKIEILNDRELAKVRNdEI 92
Cdd:cd03292 5 NVTKTYPNG---TAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYLRR-KI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 93 GFVFQQFFLLAKLTALQNVELPLIYAGVNVSKRREQAKQFLEKVGLGRRIKHLPSELSGGQKQRVAIARALVNDPSIILA 172
Cdd:cd03292 81 GVVFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2076047389 173 DEPTGALDTKTGQQIMELLTELNKEGKTIIMVTHEPEI-ADFATRKIIIRDGDI 225
Cdd:cd03292 161 DEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELvDTTRHRVIALERGKL 214
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
10-230 |
1.36e-59 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 187.58 E-value: 1.36e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 10 QLSNIVKSYqnGDQVlkVLKGINLTVYEGEFLAIMGPSGSGKSTLMNII-GLLdRPTSGDYTLHNTKIeilnDRELAKVR 88
Cdd:COG1131 2 EVRGLTKRY--GDKT--ALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLlGLL-RPTSGEVRVLGEDV----ARDPAEVR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 89 nDEIGFVFQQFFLLAKLTALQNVELPLIYAGVNVSKRREQAKQFLEKVGLGRRIKHLPSELSGGQKQRVAIARALVNDPS 168
Cdd:COG1131 73 -RRIGYVPQEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPE 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2076047389 169 IILADEPTGALDTKTGQQIMELLTELNKEGKTIIMVTHE-PEIADFATRKIIIRDGDITTDTT 230
Cdd:COG1131 152 LLILDEPTSGLDPEARRELWELLRELAAEGKTVLLSTHYlEEAERLCDRVAIIDKGRIVADGT 214
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
10-225 |
1.50e-59 |
|
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: 187.71 E-value: 1.50e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 10 QLSNIVKSYqnGDQVlkVLKGINLTVYEGEFLAIMGPSGSGKSTLMNIIGLLDRPTSGDYTLHNTKIEILNDRELAKVRN 89
Cdd:cd03261 2 ELRGLTKSF--GGRT--VLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 90 dEIGFVFQQFFLLAKLTALQNVELPLIYAGVNVSKR-REQAKQFLEKVGLGRRIKHLPSELSGGQKQRVAIARALVNDPS 168
Cdd:cd03261 78 -RMGMLFQSGALFDSLTVFENVAFPLREHTRLSEEEiREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2076047389 169 IILADEPTGALDTKTGQQIMELLTELNKE-GKTIIMVTHE-PEIADFATRKIIIRDGDI 225
Cdd:cd03261 157 LLLYDEPTAGLDPIASGVIDDLIRSLKKElGLTSIMVTHDlDTAFAIADRIAVLYDGKI 215
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
1-207 |
1.50e-59 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 188.47 E-value: 1.50e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 1 MSHEKKQLMQLSNIVKSYqnGDqvLKVLKGINLTVYEGEFLAIMGPSGSGKSTLMNIIGLLDRPTSGDYTLHNTKIEILN 80
Cdd:COG4598 1 MTDTAPPALEVRDLHKSF--GD--LEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIRLKP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 81 DRELAKVRND---------EIGFVFQQFFLLAKLTALQNV-ELPLIYAGVNVSKRREQAKQFLEKVGLGRRIKHLPSELS 150
Cdd:COG4598 77 DRDGELVPADrrqlqrirtRLGMVFQSFNLWSHMTVLENViEAPVHVLGRPKAEAIERAEALLAKVGLADKRDAYPAHLS 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2076047389 151 GGQKQRVAIARALVNDPSIILADEPTGALDTKTGQQIMELLTELNKEGKTIIMVTHE 207
Cdd:COG4598 157 GGQQQRAAIARALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEEGRTMLVVTHE 213
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
8-236 |
4.68e-59 |
|
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: 186.74 E-value: 4.68e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 8 LMQLSNIVKSYQNGDQVLKvlkGINLTVYEGEFLAIMGPSGSGKSTLMNIIGLLDRPTSGDYTLHNTKIEILNDRELAKV 87
Cdd:TIGR02315 1 MLEVENLSKVYPNGKQALK---NINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKLRKL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 88 RNdEIGFVFQQFFLLAKLTALQNVELPLIYAGVNV--------SKRREQAKQFLEKVGLGRRIKHLPSELSGGQKQRVAI 159
Cdd:TIGR02315 78 RR-RIGMIFQHYNLIERLTVLENVLHGRLGYKPTWrsllgrfsEEDKERALSALERVGLADKAYQRADQLSGGQQQRVAI 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2076047389 160 ARALVNDPSIILADEPTGALDTKTGQQIMELLTELNKE-GKTIIMVTHEPEIA-DFATRKIIIRDGDITTDTTASVVID 236
Cdd:TIGR02315 157 ARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEdGITVIINLHQVDLAkKYADRIVGLKAGEIVFDGAPSELDD 235
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
31-225 |
2.15e-58 |
|
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: 185.92 E-value: 2.15e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 31 INLTVYEGEFLAIMGPSGSGKSTLMNIIGLLDRPTSGDYTLHNTKIEILNDRELAKVRNDEIGFVFQQFFLLAKLTALQN 110
Cdd:cd03294 43 VSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRELRRKKISMVFQSFALLPHRTVLEN 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 111 VELPLIYAGVNVSKRREQAKQFLEKVGLGRRIKHLPSELSGGQKQRVAIARALVNDPSIILADEPTGALDTKTGQQIMEL 190
Cdd:cd03294 123 VAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDE 202
|
170 180 190
....*....|....*....|....*....|....*..
gi 2076047389 191 LTELNKE-GKTIIMVTHEPEIA-DFATRKIIIRDGDI 225
Cdd:cd03294 203 LLRLQAElQKTIVFITHDLDEAlRLGDRIAIMKDGRL 239
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
8-206 |
7.62e-57 |
|
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: 183.33 E-value: 7.62e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 8 LMQLSNIVKSYQNGDQVLKVLKGINLTVYEGEFLAIMGPSGSGKSTLMN-IIGLLDRP--TSGDYTLHNTKIEILNDREL 84
Cdd:COG0444 1 LLEVRNLKVYFPTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARaILGLLPPPgiTSGEILFDGEDLLKLSEKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 85 AKVRNDEIGFVFQqffllAKLTAL--------QNVELPLIYAGVNVSKRREQAKQFLEKVGL---GRRIKHLPSELSGGQ 153
Cdd:COG0444 81 RKIRGREIQMIFQ-----DPMTSLnpvmtvgdQIAEPLRIHGGLSKAEARERAIELLERVGLpdpERRLDRYPHELSGGM 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2076047389 154 KQRVAIARALVNDPSIILADEPTGALDTKTGQQIMELLTELNKE-GKTIIMVTH 206
Cdd:COG0444 156 RQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRElGLAILFITH 209
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
8-232 |
2.49e-56 |
|
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: 179.61 E-value: 2.49e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 8 LMQLSNIVKSYQNGDQVLKVLKGINLTVYEGEFLAIMGPSGSGKSTLMNIIGLLDRPTSGDYTLHNTKIEILNDRELAKv 87
Cdd:COG1124 1 MLEVRNLSVSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRR- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 88 rndEIGFVFQQFF--LLAKLTALQNVELPLIYAGVNVSKRReqAKQFLEKVGLGRRIKH-LPSELSGGQKQRVAIARALV 164
Cdd:COG1124 80 ---RVQMVFQDPYasLHPRHTVDRILAEPLRIHGLPDREER--IAELLEQVGLPPSFLDrYPHQLSGGQRQRVAIARALI 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 165 NDPSIILADEPTGALDTKTGQQIMELLTELNKE-GKTIIMVTHEPEIADF-ATRKIIIRDGDITTDTTAS 232
Cdd:COG1124 155 LEPELLLLDEPTSALDVSVQAEILNLLKDLREErGLTYLFVSHDLAVVAHlCDRVAVMQNGRIVEELTVA 224
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
9-223 |
6.78e-56 |
|
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: 176.22 E-value: 6.78e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 9 MQLSNIVKSYqnGDQvlKVLKGINLTVYEGEFLAIMGPSGSGKSTLMNIIGLLDRPTSGDYTLHNTKIEILNDRELAKVR 88
Cdd:cd03229 1 LELKNVSKRY--GQK--TVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPPLRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 89 NdeIGFVFQQFFLLAKLTALQNVELPLiyagvnvskrreqakqflekvglgrrikhlpselSGGQKQRVAIARALVNDPS 168
Cdd:cd03229 77 R--IGMVFQDFALFPHLTVLENIALGL----------------------------------SGGQQQRVALARALAMDPD 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2076047389 169 IILADEPTGALDTKTGQQIMELLTELNKE-GKTIIMVTHEP-EIADFATRKIIIRDG 223
Cdd:cd03229 121 VLLLDEPTSALDPITRREVRALLKSLQAQlGITVVLVTHDLdEAARLADRVVVLRDG 177
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
17-225 |
1.88e-55 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 176.16 E-value: 1.88e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 17 SYQNGDQVLkvLKGINLTVYEGEFLAIMGPSGSGKSTLMNIIGLLDRPTSGDYTLHNTKIEILNDRELAKvrndEIGFVF 96
Cdd:COG4619 7 SFRVGGKPI--LSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRR----QVAYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 97 QQFFLLAKlTALQNVELPLIYAGVNVSkrREQAKQFLEKVGLGRRIKHLP-SELSGGQKQRVAIARALVNDPSIILADEP 175
Cdd:COG4619 81 QEPALWGG-TVRDNLPFPFQLRERKFD--RERALELLERLGLPPDILDKPvERLSGGERQRLALIRALLLQPDVLLLDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2076047389 176 TGALDTKTGQQIMELLTELNKE-GKTIIMVTHEPE-IADFATRKIIIRDGDI 225
Cdd:COG4619 158 TSALDPENTRRVEELLREYLAEeGRAVLWVSHDPEqIERVADRVLTLEAGRL 209
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-219 |
1.93e-55 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 177.75 E-value: 1.93e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 1 MSHekkqlMQLSNIVKSYQNGDQVLKVLKGINLTVYEGEFLAIMGPSGSGKSTLMNIIGLLDRPTSGDYTLHNTKIEILN 80
Cdd:COG4525 1 MSM-----LTVRHVSVRYPGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 81 -DRelakvrndeiGFVFQQFFLLAKLTALQNVELPLIYAGVNVSKRREQAKQFLEKVGLGRRIKHLPSELSGGQKQRVAI 159
Cdd:COG4525 76 aDR----------GVVFQKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGI 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2076047389 160 ARALVNDPSIILADEPTGALDTKTGQQIMELLTEL-NKEGKTIIMVTHEPEIADF-ATRKII 219
Cdd:COG4525 146 ARALAADPRFLLMDEPFGALDALTREQMQELLLDVwQRTGKGVFLITHSVEEALFlATRLVV 207
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
27-233 |
4.66e-55 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 176.43 E-value: 4.66e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 27 VLKGINLTVYEGEFLAIMGPSGSGKSTLMNII-GLLdRPTSGdytlhntKIEILnDRELAKVRNDeIGFVFQQF-----F 100
Cdd:COG1121 21 VLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAIlGLL-PPTSG-------TVRLF-GKPPRRARRR-IGYVPQRAevdwdF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 101 llaKLTALQNVELPLiYAGVNVSKR-----REQAKQFLEKVGLGRRIKHLPSELSGGQKQRVAIARALVNDPSIILADEP 175
Cdd:COG1121 91 ---PITVRDVVLMGR-YGRRGLFRRpsradREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDPDLLLLDEP 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2076047389 176 TGALDTKTGQQIMELLTELNKEGKTIIMVTHEPE-IADFATRKIIIRDGDITTDTTASV 233
Cdd:COG1121 167 FAGVDAATEEALYELLRELRREGKTILVVTHDLGaVREYFDRVLLLNRGLVAHGPPEEV 225
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
10-225 |
1.49e-54 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 178.42 E-value: 1.49e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 10 QLSNIVKSYQNgdqvLKVLKGINLTVYEGEFLAIMGPSGSGKSTLMNIIGLLDRPTSGdytlhntKIeILNDRELA---K 86
Cdd:COG1118 4 EVRNISKRFGS----FTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSG-------RI-VLNGRDLFtnlP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 87 VRNDEIGFVFQQFFLLAKLTALQNVELPLIYAGVNVSKRREQAKQFLEKVGLGRRIKHLPSELSGGQKQRVAIARALVND 166
Cdd:COG1118 72 PRERRVGFVFQHYALFPHMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVE 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2076047389 167 PSIILADEPTGALDTKTGQQIMELLTELNKE-GKTIIMVTHEPEIA-DFATRKIIIRDGDI 225
Cdd:COG1118 152 PEVLLLDEPFGALDAKVRKELRRWLRRLHDElGGTTVFVTHDQEEAlELADRVVVMNQGRI 212
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
10-225 |
1.51e-54 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 178.34 E-value: 1.51e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 10 QLSNIVKSYqnGDQVlkVLKGINLTVYEGEFLAIMGPSGSGKSTLMNIIGLLDRPTSGDytlhntkIEIlNDRELAKV-- 87
Cdd:COG3839 5 ELENVSKSY--GGVE--ALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGE-------ILI-GGRDVTDLpp 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 88 --RNdeIGFVFQQFFLLAKLTALQNVELPLIYAGVNVSKRREQAKQFLEKVGLGRRIKHLPSELSGGQKQRVAIARALVN 165
Cdd:COG3839 73 kdRN--IAMVFQSYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVR 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2076047389 166 DPSIILADEPTGALDTKTGQQIMELLTELNKE-GKTIIMVTHEP-EIADFATRKIIIRDGDI 225
Cdd:COG3839 151 EPKVFLLDEPLSNLDAKLRVEMRAEIKRLHRRlGTTTIYVTHDQvEAMTLADRIAVMNDGRI 212
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
8-236 |
1.46e-53 |
|
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: 179.71 E-value: 1.46e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 8 LMQLSNIVKSYQNGDQvlKVLKGINLTVYEGEFLAIMGPSGSGKSTL-MNIIGLLDRPTSGDYTLHNTKIEILNDRElaK 86
Cdd:COG1123 4 LLEVRDLSVRYPGGDV--PAVDGVSLTIAPGETVALVGESGSGKSTLaLALMGLLPHGGRISGEVLLDGRDLLELSE--A 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 87 VRNDEIGFVFQQFFL-LAKLTALQNVELPLIYAGVNVSKRREQAKQFLEKVGLGRRIKHLPSELSGGQKQRVAIARALVN 165
Cdd:COG1123 80 LRGRRIGMVFQDPMTqLNPVTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALAL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2076047389 166 DPSIILADEPTGALDTKTGQQIMELLTELNKE-GKTIIMVTHEPE-IADFATRKIIIRDGDITTDTTASVVID 236
Cdd:COG1123 160 DPDLLIADEPTTALDVTTQAEILDLLRELQRErGTTVLLITHDLGvVAEIADRVVVMDDGRIVEDGPPEEILA 232
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
8-236 |
1.31e-51 |
|
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: 167.91 E-value: 1.31e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 8 LMQLSNIVKSYQNGdqvlKVLKGINLTVYEGEFLAIMGPSGSGKSTLMNII-GLLdRPTSGDYTLHNTKIEILNDRELAK 86
Cdd:COG1120 1 MLEAENLSVGYGGR----PVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALaGLL-KPSSGEVLLDGRDLASLSRRELAR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 87 VrndeIGFVFQQFFLLAKLTALQNVEL---PLIYAGVNVSKR-REQAKQFLEKVGL----GRRIkhlpSELSGGQKQRVA 158
Cdd:COG1120 76 R----IAYVPQEPPAPFGLTVRELVALgryPHLGLFGRPSAEdREAVEEALERTGLehlaDRPV----DELSGGERQRVL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 159 IARALVNDPSIILADEPTGALDTKTGQQIMELLTELNKE-GKTIIMVTHEPEIA-DFATRKIIIRDGDITTDTTASVVID 236
Cdd:COG1120 148 IARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARErGRTVVMVLHDLNLAaRYADRLVLLKDGRIVAQGPPEEVLT 227
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
10-232 |
8.39e-51 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 165.57 E-value: 8.39e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 10 QLSNIVKSYQNgdqvLKVLKGINLTVYEGEFLAIMGPSGSGKSTLMNIIGLLDRPTSGDYTLHNTKIEI---LNDRELAK 86
Cdd:COG4161 4 QLKNINCFYGS----HQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFDFsqkPSEKAIRL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 87 VRNDeIGFVFQQFFLLAKLTALQN-VELPLIYAGVNVSKRREQAKQFLEKVGLGRRIKHLPSELSGGQKQRVAIARALVN 165
Cdd:COG4161 80 LRQK-VGMVFQQYNLWPHLTVMENlIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMM 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2076047389 166 DPSIILADEPTGALDTKTGQQIMELLTELNKEGKTIIMVTHEPEIA-DFATRKIIIRDGDITTDTTAS 232
Cdd:COG4161 159 EPQVLLFDEPTAALDPEITAQVVEIIRELSQTGITQVIVTHEVEFArKVASQVVYMEKGRIIEQGDAS 226
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
11-211 |
3.68e-50 |
|
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: 163.56 E-value: 3.68e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 11 LSNIVKSYqnGDQVlkVLKGINLTVYEGEFLAIMGPSGSGKSTLMNIIGLLDRPTSGDYTLHntkieilnDRELAKV--- 87
Cdd:cd03300 3 LENVSKFY--GGFV--ALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLD--------GKDITNLpph 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 88 -RNdeIGFVFQQFFLLAKLTALQNVELPLIYAGVNVSKRREQAKQFLEKVGLGRRIKHLPSELSGGQKQRVAIARALVND 166
Cdd:cd03300 71 kRP--VNTVFQNYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNE 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2076047389 167 PSIILADEPTGALDTKTGQQIMELLTELNKE-GKTIIMVTHEPEIA 211
Cdd:cd03300 149 PKVLLLDEPLGALDLKLRKDMQLELKRLQKElGITFVFVTHDQEEA 194
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
9-232 |
6.34e-50 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 163.26 E-value: 6.34e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 9 MQLSNIVKSYQNGdqvlKVLKGINLTVYEGEFLAIMGPSGSGKSTLMNIIGLLDRPTSGDYTLHNTKIEI---LNDRELA 85
Cdd:PRK11124 3 IQLNGINCFYGAH----QALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFDFsktPSDKAIR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 86 KVRNDeIGFVFQQFFLLAKLTALQN-VELPLIYAGVNVSKRREQAKQFLEKVGLGRRIKHLPSELSGGQKQRVAIARALV 164
Cdd:PRK11124 79 ELRRN-VGMVFQQYNLWPHLTVQQNlIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALM 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2076047389 165 NDPSIILADEPTGALDTKTGQQIMELLTELNKEGKTIIMVTHEPEIA-DFATRKIIIRDGDITTDTTAS 232
Cdd:PRK11124 158 MEPQVLLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTHEVEVArKTASRVVYMENGHIVEQGDAS 226
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
10-219 |
2.06e-49 |
|
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: 160.78 E-value: 2.06e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 10 QLSNIVKSYQNGdqvlKVLKGINLTVYEGEFLAIMGPSGSGKSTLMN-IIGLLdRPTSGdytlhntKIEILnDRELAKVR 88
Cdd:cd03235 1 EVEDLTVSYGGH----PVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKaILGLL-KPTSG-------SIRVF-GKPLEKER 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 89 NDeIGFVFQQFFLLAK--LTALQNVELPLiYAGVNVSKR-----REQAKQFLEKVGLG----RRIkhlpSELSGGQKQRV 157
Cdd:cd03235 68 KR-IGYVPQRRSIDRDfpISVRDVVLMGL-YGHKGLFRRlskadKAKVDEALERVGLSeladRQI----GELSGGQQQRV 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2076047389 158 AIARALVNDPSIILADEPTGALDTKTGQQIMELLTELNKEGKTIIMVTHEPEIADFATRKII 219
Cdd:cd03235 142 LLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRVL 203
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
9-225 |
2.59e-49 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 161.84 E-value: 2.59e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 9 MQLSNIVKSYqNGDQVLKvlkGINLTVYEGEFLAIMGPSGSGKSTLMNIIGLLDRPTSGdyTLHNTKIEILNDRELAKVR 88
Cdd:PRK11264 4 IEVKNLVKKF-HGQTVLH---GIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAG--TIRVGDITIDTARSLSQQK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 89 N------DEIGFVFQQFFLLAKLTALQNV-ELPLIYAGVNVSKRREQAKQFLEKVGLGRRIKHLPSELSGGQKQRVAIAR 161
Cdd:PRK11264 78 GlirqlrQHVGFVFQNFNLFPHRTVLENIiEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIAR 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2076047389 162 ALVNDPSIILADEPTGALDTKTGQQIMELLTELNKEGKTIIMVTHEPEIA-DFATRKIIIRDGDI 225
Cdd:PRK11264 158 ALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFArDVADRAIFMDQGRI 222
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
11-225 |
4.17e-49 |
|
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: 160.93 E-value: 4.17e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 11 LSNIVKSYQNGDqvlKVLKGINLTVYEGEFLAIMGPSGSGKSTLMNIIGLLDRPTSGDYTLHNTKIEILNDRELAKvrnd 90
Cdd:cd03295 3 FENVTKRYGGGK---KAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRR---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 91 EIGFVFQQFFLLAKLTALQNVELPLIYAGVNVSKRREQAKQFLEKVGLGrrIKHL----PSELSGGQKQRVAIARALVND 166
Cdd:cd03295 76 KIGYVIQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLD--PAEFadryPHELSGGQQQRVGVARALAAD 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2076047389 167 PSIILADEPTGALDTKTGQQIMELLTELNKE-GKTIIMVTHEPEIA-DFATRKIIIRDGDI 225
Cdd:cd03295 154 PPLLLMDEPFGALDPITRDQLQEEFKRLQQElGKTIVFVTHDIDEAfRLADRIAIMKNGEI 214
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
10-225 |
6.47e-49 |
|
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: 158.33 E-value: 6.47e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 10 QLSNIVKSYQNGdqvlKVLKGINLTVYEGEFLAIMGPSGSGKSTLMNII-GLLdRPTSGDYTLHNTKIeilnDRELAKVR 88
Cdd:cd03230 2 EVRNLSKRYGKK----TALDDISLTVEKGEIYGLLGPNGAGKTTLIKIIlGLL-KPDSGEIKVLGKDI----KKEPEEVK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 89 NdEIGFVFQQFFLLAKLTALQNVELpliyagvnvskrreqakqflekvglgrrikhlpselSGGQKQRVAIARALVNDPS 168
Cdd:cd03230 73 R-RIGYLPEEPSLYENLTVRENLKL------------------------------------SGGMKQRLALAQALLHDPE 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2076047389 169 IILADEPTGALDTKTGQQIMELLTELNKEGKTIIMVTH-EPEIADFATRKIIIRDGDI 225
Cdd:cd03230 116 LLILDEPTSGLDPESRREFWELLRELKKEGKTILLSSHiLEEAERLCDRVAILNNGRI 173
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
9-223 |
3.80e-48 |
|
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: 156.39 E-value: 3.80e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 9 MQLSNIVKSYQNGDQvlKVLKGINLTVYEGEFLAIMGPSGSGKSTLMNIIGLLDRPTSGDYTLHNTKIEILNDRELAKVr 88
Cdd:cd03228 1 IEFKNVSFSYPGRPK--PVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKN- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 89 ndeIGFVFQQFFLLAKlTALQNVelpliyagvnvskrreqakqflekvglgrrikhlpseLSGGQKQRVAIARALVNDPS 168
Cdd:cd03228 78 ---IAYVPQDPFLFSG-TIRENI-------------------------------------LSGGQRQRIAIARALLRDPP 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2076047389 169 IILADEPTGALDTKTGQQIMELLTELnKEGKTIIMVTHEPEIADFATRKIIIRDG 223
Cdd:cd03228 117 ILILDEATSALDPETEALILEALRAL-AKGKTVIVIAHRLSTIRDADRIIVLDDG 170
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
26-230 |
4.37e-48 |
|
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: 159.54 E-value: 4.37e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 26 KVLKGINLTVYEGEFLAIMGPSGSGKSTLMNII-GLLdRPTSGDYTLHNTKIEILNDRELAKVRNdEIGFVFQ----QFF 100
Cdd:TIGR04521 19 KALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLnGLL-KPTSGTVTIDGRDITAKKKKKLKDLRK-KVGLVFQfpehQLF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 101 llaKLTALQNVELPLIYAGVNVSKRREQAKQFLEKVGLGRRIKHL-PSELSGGQKQRVAIARALVNDPSIILADEPTGAL 179
Cdd:TIGR04521 97 ---EETVYKDIAFGPKNLGLSEEEAEERVKEALELVGLDEEYLERsPFELSGGQMRRVAIAGVLAMEPEVLILDEPTAGL 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2076047389 180 DTKTGQQIMELLTELNKE-GKTIIMVTHEPE-IADFATRKIIIRDGDITTDTT 230
Cdd:TIGR04521 174 DPKGRKEILDLFKRLHKEkGLTVILVTHSMEdVAEYADRVIVMHKGKIVLDGT 226
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
10-220 |
5.19e-48 |
|
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: 155.48 E-value: 5.19e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 10 QLSNIVKSYQNGdqvlKVLKGINLTVYEGEFLAIMGPSGSGKSTLMNIIGLLDRPTSGDYTLHNTKIEILNDRELAKvrn 89
Cdd:cd00267 1 EIENLSFRYGGR----TALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRR--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 90 dEIGFVFQqffllakltalqnvelpliyagvnvskrreqakqflekvglgrrikhlpseLSGGQKQRVAIARALVNDPSI 169
Cdd:cd00267 74 -RIGYVPQ---------------------------------------------------LSGGQRQRVALARALLLNPDL 101
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2076047389 170 ILADEPTGALDTKTGQQIMELLTELNKEGKTIIMVTHEPEIADFATRKIII 220
Cdd:cd00267 102 LLLDEPTSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIV 152
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
8-223 |
4.02e-47 |
|
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: 155.67 E-value: 4.02e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 8 LMQLSNIVKS---YQNGDQVLKVLKGINLTVYEGEFLAIMGPSGSGKSTLMNIIGLLDRPTSGD--YTLHNTKIEI--LN 80
Cdd:COG4778 4 LLEVENLSKTftlHLQGGKRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSilVRHDGGWVDLaqAS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 81 DRELAKVRNDEIGFVFQqfFL--LAKLTALQNVELPLIYAGVNVSKRREQAKQFLEKVGLGRRIKHL-PSELSGGQKQRV 157
Cdd:COG4778 84 PREILALRRRTIGYVSQ--FLrvIPRVSALDVVAEPLLERGVDREEARARARELLARLNLPERLWDLpPATFSGGEQQRV 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2076047389 158 AIARALVNDPSIILADEPTGALDTKTGQQIMELLTELNKEGKTIIMVTHEPEIAD-FATRKIIIRDG 223
Cdd:COG4778 162 NIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVREaVADRVVDVTPF 228
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
10-226 |
8.31e-47 |
|
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: 163.01 E-value: 8.31e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 10 QLSNIVKSYQNGDQvlKVLKGINLTVYEGEFLAIMGPSGSGKSTLMNII-GLLDrPTSGDYTLHNTKIEILNDRELAKVr 88
Cdd:COG4987 335 ELEDVSFRYPGAGR--PVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLlRFLD-PQSGSITLGGVDLRDLDEDDLRRR- 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 89 ndeIGFVFQQFFLLAKlTALQNvelpLIYAGVNVSkrREQAKQFLEKVGLGRRIKHLP-----------SELSGGQKQRV 157
Cdd:COG4987 411 ---IAVVPQRPHLFDT-TLREN----LRLARPDAT--DEELWAALERVGLGDWLAALPdgldtwlgeggRRLSGGERRRL 480
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2076047389 158 AIARALVNDPSIILADEPTGALDTKTGQQIMELLTELNKeGKTIIMVTHEPEIADFATRKIIIRDGDIT 226
Cdd:COG4987 481 ALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALA-GRTVLLITHRLAGLERMDRILVLEDGRIV 548
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
11-230 |
1.75e-46 |
|
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: 155.28 E-value: 1.75e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 11 LSNIVKSYQNGDQvlKVLKGINLTVYEGEFLAIMGPSGSGKSTLM-NIIGLLdRPTSGDYTLHNtkIEILNDRELAKVRN 89
Cdd:TIGR04520 3 VENVSFSYPESEK--PALKNVSLSIEKGEFVAIIGHNGSGKSTLAkLLNGLL-LPTSGKVTVDG--LDTLDEENLWEIRK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 90 dEIGFVFQ----QF----------FllakltALQNvelpliyAGVNVSKRREQAKQFLEKVGLGRRIKHLPSELSGGQKQ 155
Cdd:TIGR04520 78 -KVGMVFQnpdnQFvgatveddvaF------GLEN-------LGVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQ 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2076047389 156 RVAIARALVNDPSIILADEPTGALDTKTGQQIMELLTELNKE-GKTIIMVTHEPEIADFATRKIIIRDGDITTDTT 230
Cdd:TIGR04520 144 RVAIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEeGITVISITHDMEEAVLADRVIVMNKGKIVAEGT 219
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
8-225 |
6.73e-46 |
|
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: 159.85 E-value: 6.73e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 8 LMQLSNIVKSYQNGDQVLKVLKGINLTVYEGEFLAIMGPSGSGKS-TLMNIIGLLDRP---TSGDYTLHNTKIEILNDRE 83
Cdd:COG4172 6 LLSVEDLSVAFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvTALSILRLLPDPaahPSGSILFDGQDLLGLSERE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 84 LAKVRNDEIGFVFQQffllaKLTAL--------QNVELPLIYAGVNVSKRREQAKQFLEKVGL---GRRIKHLPSELSGG 152
Cdd:COG4172 86 LRRIRGNRIAMIFQE-----PMTSLnplhtigkQIAEVLRLHRGLSGAAARARALELLERVGIpdpERRLDAYPHQLSGG 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2076047389 153 QKQRVAIARALVNDPSIILADEPTGALDTKTGQQIMELLTELNKE-GKTIIMVTHEPEI-ADFATRKIIIRDGDI 225
Cdd:COG4172 161 QRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRElGMALLLITHDLGVvRRFADRVAVMRQGEI 235
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
9-225 |
8.04e-46 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 156.01 E-value: 8.04e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 9 MQLSNIVKSYQNgdqvLKVLKGINLTVYEGEFLAIMGPSGSGKSTLMNIIGLLDRPTSGDYTLHNTKIEILNDRElakvR 88
Cdd:PRK10851 3 IEIANIKKSFGR----TQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARD----R 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 89 NdeIGFVFQQFFLLAKLTALQNVELpliyaGVNVSKRRE---------QAKQFLEKVGLGRRIKHLPSELSGGQKQRVAI 159
Cdd:PRK10851 75 K--VGFVFQHYALFRHMTVFDNIAF-----GLTVLPRRErpnaaaikaKVTQLLEMVQLAHLADRYPAQLSGGQKQRVAL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2076047389 160 ARALVNDPSIILADEPTGALDTKTGQQIMELLTELNKEGK-TIIMVTHEPEIA-DFATRKIIIRDGDI 225
Cdd:PRK10851 148 ARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKfTSVFVTHDQEEAmEVADRVVVMSQGNI 215
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
8-223 |
1.78e-45 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 152.16 E-value: 1.78e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 8 LMQLSNIVKSYQNGdqvlKVLKGINLTVYEGEFLAIMGPSGSGKSTLMNIIGLLDRPTSGDYTLHNTKIEilndrelakV 87
Cdd:PRK11248 1 MLQISHLYADYGGK----PALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVE---------G 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 88 RNDEIGFVFQQFFLLAKLTALQNVELPLIYAGVNVSKRREQAKQFLEKVGLGRRIKHLPSELSGGQKQRVAIARALVNDP 167
Cdd:PRK11248 68 PGAERGVVFQNEGLLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANP 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2076047389 168 SIILADEPTGALDTKTGQQIMELLTELNKE-GKTIIMVTHEPEIADF-ATRKIIIRDG 223
Cdd:PRK11248 148 QLLLLDEPFGALDAFTREQMQTLLLKLWQEtGKQVLLITHDIEEAVFmATELVLLSPG 205
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
10-225 |
1.96e-45 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 151.45 E-value: 1.96e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 10 QLSNIvkSYQNGDQVLKvlkgINLTVYEGEFLAIMGPSGSGKSTLMNIIGLLDRPTSGDYtlhntkieILNDRELAKVRN 89
Cdd:COG3840 3 RLDDL--TYRYGDFPLR----FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRI--------LWNGQDLTALPP 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 90 DE--IGFVFQQFFLLAKLTALQNVELpliyaGVNVSKR-----REQAKQFLEKVGLGRRIKHLPSELSGGQKQRVAIARA 162
Cdd:COG3840 69 AErpVSMLFQENNLFPHLTVAQNIGL-----GLRPGLKltaeqRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARC 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2076047389 163 LVNDPSIILADEPTGALDTKTGQQIMELLTELNKE-GKTIIMVTHEPE-IADFATRKIIIRDGDI 225
Cdd:COG3840 144 LVRKRPILLLDEPFSALDPALRQEMLDLVDELCRErGLTVLMVTHDPEdAARIADRVLLVADGRI 208
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
10-235 |
4.00e-45 |
|
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: 160.00 E-value: 4.00e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 10 QLSNIVKSYQNGDQvlKVLKGINLTVYEGEFLAIMGPSGSGKSTLMNII-GLLDrPTSGDYTLHNTKIEILNDRELAKvr 88
Cdd:COG2274 475 ELENVSFRYPGDSP--PVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLlGLYE-PTSGRILIDGIDLRQIDPASLRR-- 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 89 ndEIGFVFQQFFLLAKlTALQNvelpLIYAGVNVSkrREQAKQFLEKVGLGRRIKHLP-----------SELSGGQKQRV 157
Cdd:COG2274 550 --QIGVVLQDVFLFSG-TIREN----ITLGDPDAT--DEEIIEAARLAGLHDFIEALPmgydtvvgeggSNLSGGQRQRL 620
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2076047389 158 AIARALVNDPSIILADEPTGALDTKTGQQIMELLTELNKeGKTIIMVTHEPEIADFATRKIIIRDGDITTDTTASVVI 235
Cdd:COG2274 621 AIARALLRNPRILILDEATSALDAETEAIILENLRRLLK-GRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEELL 697
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
8-207 |
7.11e-45 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 149.64 E-value: 7.11e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 8 LMQLSNIVKSYQNGDQVLKvlkGINLTVYEGEFLAIMGPSGSGKSTLMNIIGLLDRPTSGDYTLHNTKIEILNDRELAKV 87
Cdd:PRK10908 1 MIRFEHVSKAYLGGRQALQ---GVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPFL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 88 RNdEIGFVFQQFFLLAKLTALQNVELPLIYAGVNVSKRREQAKQFLEKVGLGRRIKHLPSELSGGQKQRVAIARALVNDP 167
Cdd:PRK10908 78 RR-QIGMIFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKP 156
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2076047389 168 SIILADEPTGALDTKTGQQIMELLTELNKEGKTIIMVTHE 207
Cdd:PRK10908 157 AVLLADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHD 196
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
9-213 |
1.08e-44 |
|
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: 149.25 E-value: 1.08e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 9 MQLSNIVKSYqnGDqvLKVLKGINLTVYEGEFLAIMGPSGSGKSTLMNII-GLLD----RPTSGDYTLHNTKIEILNDRE 83
Cdd:cd03260 1 IELRDLNVYY--GD--KHALKDISLDIPKGEITALIGPSGCGKSTLLRLLnRLNDlipgAPDEGEVLLDGKDIYDLDVDV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 84 LAKVRndEIGFVFQQFFLLAKlTALQNVELPLIYAGVNVSKRREQ-AKQFLEKVGLGRRIK-HL-PSELSGGQKQRVAIA 160
Cdd:cd03260 77 LELRR--RVGMVFQKPNPFPG-SIYDNVAYGLRLHGIKLKEELDErVEEALRKAALWDEVKdRLhALGLSGGQQQRLCLA 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2076047389 161 RALVNDPSIILADEPTGALDTKTGQQIMELLTELNKEgKTIIMVTHEPE----IADF 213
Cdd:cd03260 154 RALANEPEVLLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTHNMQqaarVADR 209
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
10-223 |
1.58e-44 |
|
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: 149.24 E-value: 1.58e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 10 QLSNIVKSYQNGdqvlKVLKGINLTVYEGEFLAIMGPSGSGKSTLMNIIGLLDRPTSGdytlhntKIEILND---RELAK 86
Cdd:COG4555 3 EVENLSKKYGKV----PALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSG-------SILIDGEdvrKEPRE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 87 VRNdEIGFVFQQFFLLAKLTALQNVELPLIYAGVNVSKRREQAKQFLEKVGLGRRIKHLPSELSGGQKQRVAIARALVND 166
Cdd:COG4555 72 ARR-QIGVLPDERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHD 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2076047389 167 PSIILADEPTGALDTKTGQQIMELLTELNKEGKTIIMVTHEP-EIADFATRKIIIRDG 223
Cdd:COG4555 151 PKVLLLDEPTNGLDVMARRLLREILRALKKEGKTVLFSSHIMqEVEALCDRVVILHKG 208
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
10-226 |
3.53e-44 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 146.43 E-value: 3.53e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 10 QLSNIVKSYQNGdqvlKVLKGINLTVYEGEFLAIMGPSGSGKSTLMNIIGLLDRPTSGDYTLHNTKIEILNDRELAKvrn 89
Cdd:cd03214 1 EVENLSVGYGGR----TVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELAR--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 90 dEIGFVFQqffllakltALQNVELpliyagvnvskrreqaKQFLEkvglgRRIkhlpSELSGGQKQRVAIARALVNDPSI 169
Cdd:cd03214 74 -KIAYVPQ---------ALELLGL----------------AHLAD-----RPF----NELSGGERQRVLLARALAQEPPI 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2076047389 170 ILADEPTGALDTKTGQQIMELLTELNKE-GKTIIMVTHEPEIA-DFATRKIIIRDGDIT 226
Cdd:cd03214 119 LLLDEPTSHLDIAHQIELLELLRRLARErGKTVVMVLHDLNLAaRYADRVILLKDGRIV 177
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
9-225 |
5.62e-44 |
|
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: 147.87 E-value: 5.62e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 9 MQLSNIVKSYQNgdqvLKVLKGINLTVYEGEFLAIMGPSGSGKSTLMNIIGLLDRPTSGDYTLHNtkieilNDRELAKVR 88
Cdd:cd03296 3 IEVRNVSKRFGD----FVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGG------EDATDVPVQ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 89 NDEIGFVFQQFFLLAKLTALQNVELpliyaGVNVSKR---------REQAKQFLEKVGLGRRIKHLPSELSGGQKQRVAI 159
Cdd:cd03296 73 ERNVGFVFQHYALFRHMTVFDNVAF-----GLRVKPRserppeaeiRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVAL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2076047389 160 ARALVNDPSIILADEPTGALDTKTGQQIMELLTELNKE-GKTIIMVTHEPEIA-DFATRKIIIRDGDI 225
Cdd:cd03296 148 ARALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDElHVTTVFVTHDQEEAlEVADRVVVMNKGRI 215
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
8-216 |
6.23e-44 |
|
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: 146.47 E-value: 6.23e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 8 LMQLSNIVKSYqnGDQVLkvLKGINLTVYEGEFLAIMGPSGSGKSTLMNIIGLLDRPTSGDYTLHNTKIEILNDRelakv 87
Cdd:COG4133 2 MLEAENLSCRR--GERLL--FSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDARED----- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 88 RNDEIGFVFQQFFLLAKLTALQNVELpliYAGV-NVSKRREQAKQFLEKVGLGRRIKHLPSELSGGQKQRVAIARALVND 166
Cdd:COG4133 73 YRRRLAYLGHADGLKPELTVRENLRF---WAALyGLRADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSP 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2076047389 167 PSIILADEPTGALDTKTGQQIMELLTELNKEGKTIIMVTHEPEIADFATR 216
Cdd:COG4133 150 APLWLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTTHQPLELAAARV 199
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
26-219 |
1.93e-43 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 147.04 E-value: 1.93e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 26 KVLKGINLTVYEGEFLAIMGPSGSGKSTLMNIIGLLDRPTSGDYTLHNTKIEILND----------RELAKVRNdEIGFV 95
Cdd:PRK10619 19 EVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDkdgqlkvadkNQLRLLRT-RLTMV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 96 FQQFFLLAKLTALQNV-ELPLIYAGVNVSKRREQAKQFLEKVGLGRRIK-HLPSELSGGQKQRVAIARALVNDPSIILAD 173
Cdd:PRK10619 98 FQHFNLWSHMTVLENVmEAPIQVLGLSKQEARERAVKYLAKVGIDERAQgKYPVHLSGGQQQRVSIARALAMEPEVLLFD 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2076047389 174 EPTGALDTKTGQQIMELLTELNKEGKTIIMVTHEPEIADFATRKII 219
Cdd:PRK10619 178 EPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVI 223
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
28-176 |
2.50e-43 |
|
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: 143.17 E-value: 2.50e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 28 LKGINLTVYEGEFLAIMGPSGSGKSTLMNIIGLLDRPTSGDYTLHNTKIEILNDRELAKvrndEIGFVFQQFFLLAKLTA 107
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRK----EIGYVFQDPQLFPRLTV 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2076047389 108 LQNVELPLIYAGVNVSKRREQAKQFLEKVGLG----RRIKHLPSELSGGQKQRVAIARALVNDPSIILADEPT 176
Cdd:pfam00005 77 RENLRLGLLLKGLSKREKDARAEEALEKLGLGdladRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
9-225 |
2.54e-43 |
|
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: 145.48 E-value: 2.54e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 9 MQLSNIVKSYQNgdqvLKVLKGINLTVYEGEFLAIMGPSGSGKSTLMNIIGLLDRPTSGDYtlhntkieILNDRELAKVR 88
Cdd:cd03301 1 VELENVTKRFGN----VTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRI--------YIGGRDVTDLP 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 89 NDE--IGFVFQQFFLLAKLTALQNVELPLIYAGVNVSKRREQAKQFLEKVGLGRRIKHLPSELSGGQKQRVAIARALVND 166
Cdd:cd03301 69 PKDrdIAMVFQNYALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVRE 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2076047389 167 PSIILADEPTGALDTKTGQQIMELLTELNKE-GKTIIMVTHEP-EIADFATRKIIIRDGDI 225
Cdd:cd03301 149 PKVFLMDEPLSNLDAKLRVQMRAELKRLQQRlGTTTIYVTHDQvEAMTMADRIAVMNDGQI 209
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
9-225 |
2.93e-43 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 145.34 E-value: 2.93e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 9 MQLSNIVKSYQNGDQVlkVLKGINLTVYEGEFLAIMGPSGSGKSTLMNIIGLLDRPTSGDYTLHntKIEILNDRELAKVR 88
Cdd:cd03263 1 LQIRNLTKTYKKGTKP--AVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYIN--GYSIRTDRKAARQS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 89 ndeIGFVFQQFFLLAKLTALQNVELPLIYAGVNVSKRREQAKQFLEKVGLGRRIKHLPSELSGGQKQRVAIARALVNDPS 168
Cdd:cd03263 77 ---LGYCPQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPS 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2076047389 169 IILADEPTGALDTKTGQQIMELLTELnKEGKTIIMVTHEPEIADF-ATRKIIIRDGDI 225
Cdd:cd03263 154 VLLLDEPTSGLDPASRRAIWDLILEV-RKGRSIILTTHSMDEAEAlCDRIAIMSDGKL 210
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
10-206 |
1.05e-42 |
|
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: 144.50 E-value: 1.05e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 10 QLSNIVKSYqnGDqvLKVLKGINLTVYEGEFLAIMGPSGSGKSTLMNII-GLLdRPTSGDYTLHNTKIEILNDRELAKVR 88
Cdd:cd03219 2 EVRGLTKRF--GG--LVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLIsGFL-RPTSGSVLFDGEDITGLPPHEIARLG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 89 ndeIGFVFQQFFLLAKLTALQNVEL------PLIYAGVNVSKR----REQAKQFLEKVGLGRRIKHLPSELSGGQKQRVA 158
Cdd:cd03219 77 ---IGRTFQIPRLFPELTVLENVMVaaqartGSGLLLARARREereaRERAEELLERVGLADLADRPAGELSYGQQRRLE 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2076047389 159 IARALVNDPSIILADEPTGALDTKTGQQIMELLTELNKEGKTIIMVTH 206
Cdd:cd03219 154 IARALATDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEH 201
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
33-228 |
1.07e-42 |
|
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: 143.79 E-value: 1.07e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 33 LTVYEGEFLAIMGPSGSGKSTLMNIIGLLDRPTSGDYTLHNTkieilnDRELAKVRNDEIGFVFQQFFLLAKLTALQNVE 112
Cdd:cd03298 19 LTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGV------DVTAAPPADRPVSMLFQENNLFAHLTVEQNVG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 113 LpliyaGVNVSKR-----REQAKQFLEKVGLGRRIKHLPSELSGGQKQRVAIARALVNDPSIILADEPTGALDTKTGQQI 187
Cdd:cd03298 93 L-----GLSPGLKltaedRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEM 167
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2076047389 188 MELLTELNKE-GKTIIMVTHEPE-IADFATRKIIIRDGDITTD 228
Cdd:cd03298 168 LDLVLDLHAEtKMTVLMVTHQPEdAKRLAQRVVFLDNGRIAAQ 210
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
10-226 |
2.45e-42 |
|
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: 150.68 E-value: 2.45e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 10 QLSNIVKSYQNGDQVLKvlkGINLTVYEGEFLAIMGPSGSGKSTLMNIIGLLDRPTSGdytlhntKIEIlNDRELAKVRN 89
Cdd:COG4988 338 ELEDVSFSYPGGRPALD---GLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSG-------SILI-NGVDLSDLDP 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 90 DE----IGFVFQQFFLLAkLTALQNVELpliyAGVNVSkrREQAKQFLEKVGLGRRIKHLP-----------SELSGGQK 154
Cdd:COG4988 407 ASwrrqIAWVPQNPYLFA-GTIRENLRL----GRPDAS--DEELEAALEAAGLDEFVAALPdgldtplgeggRGLSGGQA 479
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2076047389 155 QRVAIARALVNDPSIILADEPTGALDTKTGQQIMELLTELnKEGKTIIMVTHEPEIADFATRKIIIRDGDIT 226
Cdd:COG4988 480 QRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRL-AKGRTVILITHRLALLAQADRILVLDDGRIV 550
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
11-230 |
2.65e-42 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 144.05 E-value: 2.65e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 11 LSNIVKSYqnGDQvlKVLKGINLTVYEGEFLAIMGPSGSGKSTLMNIIGLLDRPTSGDYTLHNTKieilndreLAKVRnD 90
Cdd:PRK11247 15 LNAVSKRY--GER--TVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAP--------LAEAR-E 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 91 EIGFVFQQFFLLAKLTALQNVELPLiyagvnVSKRREQAKQFLEKVGLGRRIKHLPSELSGGQKQRVAIARALVNDPSII 170
Cdd:PRK11247 82 DTRLMFQDARLLPWKKVIDNVGLGL------KGQWRDAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2076047389 171 LADEPTGALDTKTGQQIMELLTELNKE-GKTIIMVTHE-PEIADFATRKIIIRDGDITTDTT 230
Cdd:PRK11247 156 LLDEPLGALDALTRIEMQDLIESLWQQhGFTVLLVTHDvSEAVAMADRVLLIEEGKIGLDLT 217
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
10-226 |
1.78e-41 |
|
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: 140.41 E-value: 1.78e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 10 QLSNIVKSYQNGdqvlKVLKGINLTVYEGeFLAIMGPSGSGKSTLMNIIGLLDRPTSGDYTLHNtkIEILNDRElaKVRn 89
Cdd:cd03264 2 QLENLTKRYGKK----RALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDG--QDVLKQPQ--KLR- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 90 DEIGFVFQQFFLLAKLTALQNVELPLIYAGVNVSKRREQAKQFLEKVGLGRRIKHLPSELSGGQKQRVAIARALVNDPSI 169
Cdd:cd03264 72 RRIGYLPQEFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSI 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2076047389 170 ILADEPTGALDTKTGQQIMELLTELNkEGKTIIMVTHEPE-IADFATRKIIIRDGDIT 226
Cdd:cd03264 152 LIVDEPTAGLDPEERIRFRNLLSELG-EDRIVILSTHIVEdVESLCNQVAVLNKGKLV 208
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
10-226 |
2.54e-41 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 140.08 E-value: 2.54e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 10 QLSNIVKSYQNGDqvlKVLKGINLTVYEGEFLAIMGPSGSGKSTLMNIIGLLDRPTSGdytlhntKIEILNDRELAKVRN 89
Cdd:cd03226 1 RIENISFSYKKGT---EILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSG-------SILLNGKPIKAKERR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 90 DEIGFVFQ----QFFLlakltalQNVELPLIYAGVNVSKRREQAKQFLEKVGLGRRIKHLPSELSGGQKQRVAIARALVN 165
Cdd:cd03226 71 KSIGYVMQdvdyQLFT-------DSVREELLLGLKELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLS 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2076047389 166 DPSIILADEPTGALDTKTGQQIMELLTELNKEGKTIIMVTHEPE-IADFATRKIIIRDGDIT 226
Cdd:cd03226 144 GKDLLIFDEPTSGLDYKNMERVGELIRELAAQGKAVIVITHDYEfLAKVCDRVLLLANGAIV 205
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
8-236 |
6.45e-41 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 145.93 E-value: 6.45e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 8 LMQLSNIVKSYqNGdqVlKVLKGINLTVYEGEFLAIMGPSGSGKSTLMNIIGLLDRPTSGDYTLHNTKIEILNDRELAKV 87
Cdd:COG1129 4 LLEMRGISKSF-GG--V-KALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDAQAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 88 RndeIGFVFQQFFLLAKLTALQNV---ELPLIYAGVNVSKRREQAKQFLEKVGLGRRIKHLPSELSGGQKQRVAIARALV 164
Cdd:COG1129 80 G---IAIIHQELNLVPNLSVAENIflgREPRRGGLIDWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALS 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2076047389 165 NDPSIILADEPTGALDTKTGQQIMELLTELNKEGKTIIMVTHE-PEIADFATRKIIIRDG-DITTDTTASVVID 236
Cdd:COG1129 157 RDARVLILDEPTASLTEREVERLFRIIRRLKAQGVAIIYISHRlDEVFEIADRVTVLRDGrLVGTGPVAELTED 230
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
28-220 |
9.15e-41 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 139.14 E-value: 9.15e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 28 LKGINLTVYEGEFLAIMGPSGSGKSTLMNIIGLLDRPTSGDYtlhntkieILNDRELAKVRNDEIgFVFQQFFLLAKLTA 107
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGV--------ILEGKQITEPGPDRM-VVFQNYSLLPWLTV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 108 LQNVELPL--IYAGVNVSKRREQAKQFLEKVGLGRRIKHLPSELSGGQKQRVAIARALVNDPSIILADEPTGALDTKTGQ 185
Cdd:TIGR01184 72 RENIALAVdrVLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRG 151
|
170 180 190
....*....|....*....|....*....|....*.
gi 2076047389 186 QIMELLTELNKE-GKTIIMVTHEPEIADFATRKIII 220
Cdd:TIGR01184 152 NLQEELMQIWEEhRVTVLMVTHDVDEALLLSDRVVM 187
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
4-230 |
1.30e-40 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 142.78 E-value: 1.30e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 4 EKKQLMQLSNIVKSYqnGDQvlKVLKGINLTVYEGEFLAIMGPSGSGKSTLMNIIGLLDRPTSGDYtlhntkieILNDRE 83
Cdd:PRK09452 10 SLSPLVELRGISKSF--DGK--EVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRI--------MLDGQD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 84 LAKV--RNDEIGFVFQQFFLLAKLTALQNVELPLIYAGVNVSKRREQAKQFLEKVGLGRRIKHLPSELSGGQKQRVAIAR 161
Cdd:PRK09452 78 ITHVpaENRHVNTVFQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIAR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2076047389 162 ALVNDPSIILADEPTGALDTKTGQQIMELLTELNKE-GKTIIMVTHEPEIA-DFATRKIIIRDGDITTDTT 230
Cdd:PRK09452 158 AVVNKPKVLLLDESLSALDYKLRKQMQNELKALQRKlGITFVFVTHDQEEAlTMSDRIVVMRDGRIEQDGT 228
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
8-206 |
6.68e-40 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 139.87 E-value: 6.68e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 8 LMQLSNIVKSY-------QNGDQVLKVLKGINLTVYEGEFLAIMGPSGSGKSTLMNIIGLLDRPTSGDYTLHNTKIEILN 80
Cdd:COG4608 7 LLEVRDLKKHFpvrgglfGRTVGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 81 DRELAKVRNDeIGFVFQQFF--LLAKLTALQNVELPLIYAGV-NVSKRREQAKQFLEKVGLGRRikHL---PSELSGGQK 154
Cdd:COG4608 87 GRELRPLRRR-MQMVFQDPYasLNPRMTVGDIIAEPLRIHGLaSKAERRERVAELLELVGLRPE--HAdryPHEFSGGQR 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2076047389 155 QRVAIARALVNDPSIILADEPTGALDTKTGQQIMELLTELNKE-GKTIIMVTH 206
Cdd:COG4608 164 QRIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDElGLTYLFISH 216
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
10-223 |
1.30e-39 |
|
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: 134.09 E-value: 1.30e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 10 QLSNIVKSYQNGdqvlKVLKGINLTVYEGEFLAIMGPSGSGKSTLMNII-GLLdRPTSGDYTLHNTKIEILNDRElakVR 88
Cdd:cd03216 2 ELRGITKRFGGV----KALDGVSLSVRRGEVHALLGENGAGKSTLMKILsGLY-KPDSGEILVDGKEVSFASPRD---AR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 89 NDEIGFVFQqffllakltalqnvelpliyagvnvskrreqakqflekvglgrrikhlpseLSGGQKQRVAIARALVNDPS 168
Cdd:cd03216 74 RAGIAMVYQ---------------------------------------------------LSVGERQMVEIARALARNAR 102
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2076047389 169 IILADEPTGALDTKTGQQIMELLTELNKEGKTIIMVTH-EPEIADFATRKIIIRDG 223
Cdd:cd03216 103 LLILDEPTAALTPAEVERLFKVIRRLRAQGVAVIFISHrLDEVFEIADRVTVLRDG 158
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
17-206 |
1.79e-39 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 143.00 E-value: 1.79e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 17 SYQNGDQVLKvlkGINLTVYEGEFLAIMGPSGSGKSTLMNII-GLLDrPTSGdytlhntKIEI----LNDRELAKVRNdE 91
Cdd:COG1132 348 SYPGDRPVLK---DISLTIPPGETVALVGPSGSGKSTLVNLLlRFYD-PTSG-------RILIdgvdIRDLTLESLRR-Q 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 92 IGFVFQQFFLLAkLTALQNvelpLIYAGVNVSkrREQAKQFLEKVGLGRRIKHLP-----------SELSGGQKQRVAIA 160
Cdd:COG1132 416 IGVVPQDTFLFS-GTIREN----IRYGRPDAT--DEEVEEAAKAAQAHEFIEALPdgydtvvgergVNLSGGQRQRIAIA 488
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2076047389 161 RALVNDPSIILADEPTGALDTKTGQQIMELLTELNKeGKTIIMVTH 206
Cdd:COG1132 489 RALLKDPPILILDEATSALDTETEALIQEALERLMK-GRTTIVIAH 533
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
43-230 |
1.04e-38 |
|
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: 136.47 E-value: 1.04e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 43 IMGPSGSGKSTLMNIIGLLDRPTSGDYTLHNTKIEilndreLAKVRNDEIGFVFQQFFLLAKLTALQNVELPLIYAGVNV 122
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVT------NVPPHLRHINMVFQSYALFPHMTVEENVAFGLKMRKVPR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 123 SKRREQAKQFLEKVGLGRRIKHLPSELSGGQKQRVAIARALVNDPSIILADEPTGALDTKTGQQI-MELLTELNKEGKTI 201
Cdd:TIGR01187 75 AEIKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMqLELKTIQEQLGITF 154
|
170 180 190
....*....|....*....|....*....|
gi 2076047389 202 IMVTHEPEIA-DFATRKIIIRDGDITTDTT 230
Cdd:TIGR01187 155 VFVTHDQEEAmTMSDRIAIMRKGKIAQIGT 184
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
27-225 |
1.31e-38 |
|
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: 134.00 E-value: 1.31e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 27 VLKGINLTVYEGEFLAIMGPSGSGKSTLMNIIGLLDRPTSGDYTLHNTKIEILNDRElakvRNdeIGFVFQQFFLLAKLT 106
Cdd:cd03299 14 KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEK----RD--ISYVPQNYALFPHMT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 107 ALQNVELPLIYAGVNVSKRREQAKQFLEKVGLGRRIKHLPSELSGGQKQRVAIARALVNDPSIILADEPTGALDTKTGQQ 186
Cdd:cd03299 88 VYKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEK 167
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2076047389 187 IMELLTELNKE-GKTIIMVTHE-PEIADFATRKIIIRDGDI 225
Cdd:cd03299 168 LREELKKIRKEfGVTVLHVTHDfEEAWALADKVAIMLNGKL 208
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
19-222 |
1.48e-38 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 132.99 E-value: 1.48e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 19 QNGDQVLkvLKGINLTVYEGEFLAIMGPSGSGKSTLMN-IIGLLDRP--TSGDYTLHNTKIEILNdrelAKVRNdeIGFV 95
Cdd:COG4136 10 TLGGRPL--LAPLSLTVAPGEILTLMGPSGSGKSTLLAaIAGTLSPAfsASGEVLLNGRRLTALP----AEQRR--IGIL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 96 FQQFFLLAKLTALQNV--ELPliyAGVNVSKRREQAKQFLEKVGLGRRIKHLPSELSGGQKQRVAIARALVNDPSIILAD 173
Cdd:COG4136 82 FQDDLLFPHLSVGENLafALP---PTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLD 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2076047389 174 EPTGALDTKTGQQIMEL-LTELNKEGKTIIMVTHEPEIADFATRKIIIRD 222
Cdd:COG4136 159 EPFSKLDAALRAQFREFvFEQIRQRGIPALLVTHDEEDAPAAGRVLDLGN 208
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
9-231 |
2.94e-38 |
|
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: 132.49 E-value: 2.94e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 9 MQLSNIVKSYqngDQVLKVlKGINLTVYEGEFLAIMGPSGSGKSTLMNIIGLLDRPTSGDYTLHNTKIEilndRELAKVR 88
Cdd:cd03265 1 IEVENLVKKY---GDFEAV-RGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVV----REPREVR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 89 NdEIGFVFQQFFLLAKLTALQNVELPLIYAGVNVSKRREQAKQFLEKVGLGRRIKHLPSELSGGQKQRVAIARALVNDPS 168
Cdd:cd03265 73 R-RIGIVFQDLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPE 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2076047389 169 IILADEPTGALDTKTGQQIMELLTELNKE-GKTIIMVTHEPEIAD-FATRKIIIRDGDITTDTTA 231
Cdd:cd03265 152 VLFLDEPTIGLDPQTRAHVWEYIEKLKEEfGMTILLTTHYMEEAEqLCDRVAIIDHGRIIAEGTP 216
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
26-223 |
4.23e-38 |
|
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: 132.03 E-value: 4.23e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 26 KVLKGINL---TVYEGEFLAIMGPSGSGKSTLMNIIGLLDRPTSGDYTLHNTkieILNDRELA---KVRNDEIGFVFQQF 99
Cdd:cd03297 8 KRLPDFTLkidFDLNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGT---VLFDSRKKinlPPQQRKIGLVFQQY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 100 FLLAKLTALQNVELPLiyAGVNVSKRREQAKQFLEKVGLGRRIKHLPSELSGGQKQRVAIARALVNDPSIILADEPTGAL 179
Cdd:cd03297 85 ALFPHLNVRENLAFGL--KRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSAL 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2076047389 180 DTKTGQQIMELLTELNKE-GKTIIMVTHEP-EIADFATRKIIIRDG 223
Cdd:cd03297 163 DRALRLQLLPELKQIKKNlNIPVIFVTHDLsEAEYLADRIVVMEDG 208
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
25-225 |
5.35e-38 |
|
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: 138.66 E-value: 5.35e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 25 LKVLKGINLTVYEGEFLAIMGPSGSGKSTL-MNIIGLLdrPTSGDYTLHNTKIEILNDRELAKVRNDeIGFVFQQFF--L 101
Cdd:COG4172 299 VKAVDGVSLTLRRGETLGLVGESGSGKSTLgLALLRLI--PSEGEIRFDGQDLDGLSRRALRPLRRR-MQVVFQDPFgsL 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 102 LAKLTALQNVELPLIYAGVNVSK--RREQAKQFLEKVGLGRRIKH-LPSELSGGQKQRVAIARALVNDPSIILADEPTGA 178
Cdd:COG4172 376 SPRMTVGQIIAEGLRVHGPGLSAaeRRARVAEALEEVGLDPAARHrYPHEFSGGQRQRIAIARALILEPKLLVLDEPTSA 455
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2076047389 179 LDTKTGQQIMELLTELNKE-GKTIIMVTHE----PEIADfatRKIIIRDGDI 225
Cdd:COG4172 456 LDVSVQAQILDLLRDLQREhGLAYLFISHDlavvRALAH---RVMVMKDGKV 504
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
26-228 |
5.89e-38 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 132.52 E-value: 5.89e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 26 KVLKGINLTVYEGEFLAIMGPSGSGKSTLMNIIGLLDRPTSGDytlhntKIEILnDRELAKVRNDE----IGFV---FQQ 98
Cdd:COG1119 17 TILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGN------DVRLF-GERRGGEDVWElrkrIGLVspaLQL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 99 FFLlAKLTALqNVELPLIYAGVNVSKR-----REQAKQFLEKVGLGRRIKHLPSELSGGQKQRVAIARALVNDPSIILAD 173
Cdd:COG1119 90 RFP-RDETVL-DVVLSGFFDSIGLYREptdeqRERARELLELLGLAHLADRPFGTLSQGEQRRVLIARALVKDPELLILD 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2076047389 174 EPTGALDTKTGQQIMELLTELNKEG-KTIIMVTHEPE-IADFATRKIIIRDGDITTD 228
Cdd:COG1119 168 EPTAGLDLGARELLLALLDKLAAEGaPTLVLVTHHVEeIPPGITHVLLLKDGRVVAA 224
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
10-228 |
9.76e-38 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 131.17 E-value: 9.76e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 10 QLSNIVKSYQNGDQvlKVLKGINLTVYEGEFLAIMGPSGSGKSTLMNIIGLLDRPTSGDYTLHNTKIEILNDRELAKVrn 89
Cdd:cd03245 4 EFRNVSFSYPNQEI--PALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRN-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 90 deIGFVFQQFFLLAKlTALQNVEL--PLI----------YAGVNvskrreqakQFLEK--VGLGRRIKHLPSELSGGQKQ 155
Cdd:cd03245 80 --IGYVPQDVTLFYG-TLRDNITLgaPLAdderilraaeLAGVT---------DFVNKhpNGLDLQIGERGRGLSGGQRQ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2076047389 156 RVAIARALVNDPSIILADEPTGALDTKTGQQIMELLTELnKEGKTIIMVTHEPEIADFATRKIIIRDGDITTD 228
Cdd:cd03245 148 AVALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQL-LGDKTLIIITHRPSLLDLVDRIIVMDSGRIVAD 219
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
8-206 |
1.07e-37 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 132.08 E-value: 1.07e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 8 LMQLSNIVKSYqnGDqvLKVLKGINLTVYEGEFLAIMGPSGSGKSTLMNII-GLLdRPTSGDYTLHNTKIEILNDRELAK 86
Cdd:COG0411 4 LLEVRGLTKRF--GG--LVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLItGFY-RPTSGRILFDGRDITGLPPHRIAR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 87 ---VRndeigfVFQQFFLLAKLTALQNVEL--------PLIYAGVNVSKR-------REQAKQFLEKVGLGRRIKHLPSE 148
Cdd:COG0411 79 lgiAR------TFQNPRLFPELTVLENVLVaaharlgrGLLAALLRLPRArreereaRERAEELLERVGLADRADEPAGN 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2076047389 149 LSGGQKQRVAIARALVNDPSIILADEPTGALDTKTGQQIMELLTELNKE-GKTIIMVTH 206
Cdd:COG0411 153 LSYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDErGITILLIEH 211
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
9-228 |
1.11e-37 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 133.29 E-value: 1.11e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 9 MQ--LSNIVKSYQNG-DQVLKVLKGINLTVYEGEFLAIMGPSGSGKSTLMNIIGLLDRPTSG--DYTLHNTKIE------ 77
Cdd:PRK13651 1 MQikVKNIVKIFNKKlPTELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGtiEWIFKDEKNKkktkek 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 78 -------ILNDRELAKVRN-----DEIGFVFQ----QFFllaKLTALQNVELPLIYAGVNVSKRREQAKQFLEKVGLGRR 141
Cdd:PRK13651 81 ekvleklVIQKTRFKKIKKikeirRRVGVVFQfaeyQLF---EQTIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLDES 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 142 -IKHLPSELSGGQKQRVAIARALVNDPSIILADEPTGALDTKTGQQIMELLTELNKEGKTIIMVTHEPE-IADFATRKII 219
Cdd:PRK13651 158 yLQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDnVLEWTKRTIF 237
|
....*....
gi 2076047389 220 IRDGDITTD 228
Cdd:PRK13651 238 FKDGKIIKD 246
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
13-230 |
2.22e-37 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 131.74 E-value: 2.22e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 13 NIVKSYQNGDQVLKvlkGINLTVYEGEFLAIMGPSGSGKSTL-MNIIGLLdRPTSGDYTLHNTKIEiLNDRELAKVRNdE 91
Cdd:PRK13639 6 DLKYSYPDGTEALK---GINFKAEKGEMVALLGPNGAGKSTLfLHFNGIL-KPTSGEVLIKGEPIK-YDKKSLLEVRK-T 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 92 IGFVFQ----QFFllaKLTALQNVELPLIYAGVNVSKRREQAKQFLEKVGLGRRIKHLPSELSGGQKQRVAIARALVNDP 167
Cdd:PRK13639 80 VGIVFQnpddQLF---APTVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2076047389 168 SIILADEPTGALDTKTGQQIMELLTELNKEGKTIIMVTHEPEIAD-FATRKIIIRDGDITTDTT 230
Cdd:PRK13639 157 EIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPvYADKVYVMSDGKIIKEGT 220
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
32-228 |
7.49e-37 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 129.32 E-value: 7.49e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 32 NLTVYEGEFLAIMGPSGSGKSTLMNIIGLLDRPTSGDYTLHNtkieilNDRELAKVRNDEIGFVFQQFFLLAKLTALQNV 111
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNG------QDHTTTPPSRRPVSMLFQENNLFSHLTVAQNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 112 ELPLiYAGVNVS-KRREQAKQFLEKVGLGRRIKHLPSELSGGQKQRVAIARALVNDPSIILADEPTGALDTKTGQQIMEL 190
Cdd:PRK10771 93 GLGL-NPGLKLNaAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTL 171
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2076047389 191 LTELNKEGK-TIIMVTHEPE-IADFATRKIIIRDGDITTD 228
Cdd:PRK10771 172 VSQVCQERQlTLLMVSHSLEdAARIAPRSLVVADGRIAWD 211
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
31-226 |
8.02e-37 |
|
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: 132.15 E-value: 8.02e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 31 INLTVYEGEFLAIMGPSGSGKSTLMNIIGLLDRPTSGDYTLHNtkiEILNDRElAKV------RNdeIGFVFQQFFLLAK 104
Cdd:COG4148 18 VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGG---EVLQDSA-RGIflpphrRR--IGYVFQEARLFPH 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 105 LTALQNVElpliYaGVNVSKRREQAKQFLEKV---GLGRRIKHLPSELSGGQKQRVAIARALVNDPSIILADEPTGALDT 181
Cdd:COG4148 92 LSVRGNLL----Y-GRKRAPRAERRISFDEVVellGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDL 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2076047389 182 KTGQQIMELLTELNKEGKT-IIMVTHEP-EIADFATRKIIIRDGDIT 226
Cdd:COG4148 167 ARKAEILPYLERLRDELDIpILYVSHSLdEVARLADHVVLLEQGRVV 213
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
25-213 |
1.69e-36 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 127.28 E-value: 1.69e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 25 LKVLKGINLTVYEGEFLAIMGPSGSGKSTLMNII-GLLDRP-TSGDYTLHNTKIEILNDRELakvrndeIGFVFQQFFLL 102
Cdd:cd03213 22 KQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALaGRRTGLgVSGEVLINGRPLDKRSFRKI-------IGYVPQDDILH 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 103 AKLTALQNvelpLIYAGvnvskrreqakqflekvglgrrikHLPSeLSGGQKQRVAIARALVNDPSIILADEPTGALDTK 182
Cdd:cd03213 95 PTLTVRET----LMFAA------------------------KLRG-LSGGERKRVSIALELVSNPSLLFLDEPTSGLDSS 145
|
170 180 190
....*....|....*....|....*....|.
gi 2076047389 183 TGQQIMELLTELNKEGKTIIMVTHEPEIADF 213
Cdd:cd03213 146 SALQVMSLLRRLADTGRTIICSIHQPSSEIF 176
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
11-223 |
2.18e-36 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 131.31 E-value: 2.18e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 11 LSNIVKSYqnGDQVLKvlKGINLTVYEGEFLAIMGPSGSGKSTLMNIIGLLDRPTSGDYTLHNTKieiLNDRELAKvRNd 90
Cdd:PRK11000 6 LRNVTKAY--GDVVIS--KDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKR---MNDVPPAE-RG- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 91 eIGFVFQQFFLLAKLTALQNVELPLIYAGVNVSKRREQAKQFLEKVGLGRRIKHLPSELSGGQKQRVAIARALVNDPSII 170
Cdd:PRK11000 77 -VGMVFQSYALYPHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVF 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2076047389 171 LADEPTGALDTKTGQQIMELLTELNKE-GKTIIMVTHEPEIADFATRKIIIRDG 223
Cdd:PRK11000 156 LLDEPLSNLDAALRVQMRIEISRLHKRlGRTMIYVTHDQVEAMTLADKIVVLDA 209
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
9-235 |
4.09e-36 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 133.39 E-value: 4.09e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 9 MQLSNIVKSYQNgdqvLKVLKGINLTVYEGEFLAIMGPSGSGKSTLMNIIGLLD--RPTSGDYTLHN------------- 73
Cdd:TIGR03269 1 IEVKNLTKKFDG----KEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDqyEPTSGRIIYHValcekcgyverps 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 74 -------------TKIEI----LNDRELAKVRNdEIGFVFQQFF-LLAKLTALQNVELPLIYAGVNVSKRREQAKQFLEK 135
Cdd:TIGR03269 77 kvgepcpvcggtlEPEEVdfwnLSDKLRRRIRK-RIAIMLQRTFaLYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 136 VGLGRRIKHLPSELSGGQKQRVAIARALVNDPSIILADEPTGALDTKTGQQIMELLTELNKE-GKTIIMVTHEPE-IADF 213
Cdd:TIGR03269 156 VQLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKAsGISMVLTSHWPEvIEDL 235
|
250 260
....*....|....*....|..
gi 2076047389 214 ATRKIIIRDGDITTDTTASVVI 235
Cdd:TIGR03269 236 SDKAIWLENGEIKEEGTPDEVV 257
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
32-225 |
4.18e-36 |
|
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: 126.90 E-value: 4.18e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 32 NLTVYEGEFLAIMGPSGSGKSTLMNIIGLLDRPTSGDYTLHNTkieilNDRELAKVRNdEIGFVFQQFFLLAKLTALQNV 111
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQ-----SHTGLAPYQR-PVSMLFQENNLFAHLTVRQNI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 112 ELPLIYAGVNVSKRREQAKQFLEKVGLGRRIKHLPSELSGGQKQRVAIARALVNDPSIILADEPTGALDTKTGQQIMELL 191
Cdd:TIGR01277 92 GLGLHPGLKLNAEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALV 171
|
170 180 190
....*....|....*....|....*....|....*.
gi 2076047389 192 TELNKEGK-TIIMVTHEP-EIADFATRKIIIRDGDI 225
Cdd:TIGR01277 172 KQLCSERQrTLLMVTHHLsDARAIASQIAVVSQGKI 207
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
8-223 |
4.45e-36 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 132.84 E-value: 4.45e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 8 LMQLSNIVKSYqnGDqvLKVLKGINLTVYEGEFLAIMGPSGSGKSTLMNII-GLLdRPTSGDYTLHNTKIEILNDRELAK 86
Cdd:COG3845 5 ALELRGITKRF--GG--VVANDDVSLTVRPGEIHALLGENGAGKSTLMKILyGLY-QPDSGEILIDGKPVRIRSPRDAIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 87 VRndeIGFVFQQFFLLAKLTALQNVEL---PLIYAGVNVSKRREQAKQFLEKVGL----GRRIkhlpSELSGGQKQRVAI 159
Cdd:COG3845 80 LG---IGMVHQHFMLVPNLTVAENIVLglePTKGGRLDRKAARARIRELSERYGLdvdpDAKV----EDLSVGEQQRVEI 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2076047389 160 ARALVNDPSIILADEPTGALdtkTGQQI---MELLTELNKEGKTIIMVTHE-PEIADFATRKIIIRDG 223
Cdd:COG3845 153 LKALYRGARILILDEPTAVL---TPQEAdelFEILRRLAAEGKSIIFITHKlREVMAIADRVTVLRRG 217
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
5-230 |
4.77e-36 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 128.59 E-value: 4.77e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 5 KKQLMQLSNIVKSYQNGDQvlKVLKGINLTVYEGEFLAIMGPSGSGKSTLM-NIIGLLdRPTSGDYTLHNTKieiLNDRE 83
Cdd:PRK13635 2 KEEIIRVEHISFRYPDAAT--YALKDVSFSVYEGEWVAIVGHNGSGKSTLAkLLNGLL-LPEAGTITVGGMV---LSEET 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 84 LAKVRNdEIGFVFQ----QFfllAKLTALQNVELPLIYAGVNVSKRREQAKQFLEKVGLGRRIKHLPSELSGGQKQRVAI 159
Cdd:PRK13635 76 VWDVRR-QVGMVFQnpdnQF---VGATVQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAI 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2076047389 160 ARALVNDPSIILADEPTGALDTKTGQQIMELLTELNKEGK-TIIMVTHEPEIADFATRKIIIRDGDITTDTT 230
Cdd:PRK13635 152 AGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGiTVLSITHDLDEAAQADRVIVMNKGEILEEGT 223
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
10-225 |
4.86e-36 |
|
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: 125.41 E-value: 4.86e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 10 QLSNIVKSYQNGDQVlkVLKGINLTVYEGEFLAIMGPSGSGKSTLMNIIGLLDRPTSGDYTLHNTKIEILNDRELAkvrn 89
Cdd:cd03246 2 EVENVSFRYPGAEPP--VLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELG---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 90 DEIGFVFQQFFLLAKlTALQNVelpliyagvnvskrreqakqflekvglgrrikhlpseLSGGQKQRVAIARALVNDPSI 169
Cdd:cd03246 76 DHVGYLPQDDELFSG-SIAENI-------------------------------------LSGGQRQRLGLARALYGNPRI 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2076047389 170 ILADEPTGALDTKTGQQIMELLTELNKEGKTIIMVTHEPEIADFATRKIIIRDGDI 225
Cdd:cd03246 118 LVLDEPNSHLDVEGERALNQAIAALKAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
26-223 |
1.02e-35 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 128.02 E-value: 1.02e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 26 KVLKGINLTVYEGEFLAIMGPSGSGKSTLMNIIGLLDRPTSGDYTLHNTKIEI-LNDRELAKVRNdEIGFVFQqfFLLAK 104
Cdd:PRK13641 21 KGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPeTGNKNLKKLRK-KVSLVFQ--FPEAQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 105 L---TALQNVELPLIYAGVNVSKRREQAKQFLEKVGLGRR-IKHLPSELSGGQKQRVAIARALVNDPSIILADEPTGALD 180
Cdd:PRK13641 98 LfenTVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLSEDlISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLD 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2076047389 181 TKTGQQIMELLTELNKEGKTIIMVTHE-PEIADFATRKIIIRDG 223
Cdd:PRK13641 178 PEGRKEMMQLFKDYQKAGHTVILVTHNmDDVAEYADDVLVLEHG 221
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
9-230 |
2.51e-35 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 126.82 E-value: 2.51e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 9 MQLSNIVKSYQNGDQV-LKVLKGINLTVYEGEFLAIMGPSGSGKSTLMNIIGLLDRPTSGDYTLHNTKI-EILNDRELAK 86
Cdd:PRK13646 3 IRFDNVSYTYQKGTPYeHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITItHKTKDKYIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 87 VRNdEIGFVFQqfFLLAKLTAlQNVELPLIYA----GVNVSKRREQAKQFLEKVGLGRRIKHL-PSELSGGQKQRVAIAR 161
Cdd:PRK13646 83 VRK-RIGMVFQ--FPESQLFE-DTVEREIIFGpknfKMNLDEVKNYAHRLLMDLGFSRDVMSQsPFQMSGGQMRKIAIVS 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2076047389 162 ALVNDPSIILADEPTGALDTKTGQQIMELLTELN-KEGKTIIMVTHE-PEIADFATRKIIIRDGDITTDTT 230
Cdd:PRK13646 159 ILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQtDENKTIILVSHDmNEVARYADEVIVMKEGSIVSQTS 229
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
26-206 |
3.38e-35 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 125.53 E-value: 3.38e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 26 KVLKGINLTVYEGEFLAIMGPSGSGKSTL------MN--IIGLldRpTSGDYTLHNTkiEILN-DRELAKVRNdEIGFVF 96
Cdd:COG1117 25 QALKDINLDIPENKVTALIGPSGCGKSTLlrclnrMNdlIPGA--R-VEGEILLDGE--DIYDpDVDVVELRR-RVGMVF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 97 QQFFLLAKlTALQNVELPLIYAGVNvSKRR-----EQAkqfLEKVGL----GRRIKHLPSELSGGQKQRVAIARALVNDP 167
Cdd:COG1117 99 QKPNPFPK-SIYDNVAYGLRLHGIK-SKSEldeivEES---LRKAALwdevKDRLKKSALGLSGGQQQRLCIARALAVEP 173
|
170 180 190
....*....|....*....|....*....|....*....
gi 2076047389 168 SIILADEPTGALDTKTGQQIMELLTELnKEGKTIIMVTH 206
Cdd:COG1117 174 EVLLMDEPTSALDPISTAKIEELILEL-KKDYTIVIVTH 211
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
27-214 |
1.12e-34 |
|
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: 123.31 E-value: 1.12e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 27 VLKGINLTVYEGEFLAIMGPSGSGKSTLMN-IIGLLdRPTSGdytlhntKIeILNDRELAKVRNDE-----IGFVFQQFF 100
Cdd:cd03224 15 ILFGVSLTVPEGEIVALLGRNGAGKTTLLKtIMGLL-PPRSG-------SI-RFDGRDITGLPPHEraragIGYVPEGRR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 101 LLAKLTALQNVELPLiYAGvnvskRREQAKQFLEKV-----GLGRRIKHLPSELSGGQKQRVAIARALVNDPSIILADEP 175
Cdd:cd03224 86 IFPELTVEENLLLGA-YAR-----RRAKRKARLERVyelfpRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEP 159
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2076047389 176 TGALDTKTGQQIMELLTELNKEGKTIIMV----THEPEIADFA 214
Cdd:cd03224 160 SEGLAPKIVEEIFEAIRELRDEGVTILLVeqnaRFALEIADRA 202
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
27-208 |
1.30e-34 |
|
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: 129.40 E-value: 1.30e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 27 VLKGINLTVYEGEFLAIMGPSGSGKSTL-MNIIGLLDrPTSGDYTLHNTKIEILNDRELAKVrndeIGFVFQQFFLLAKl 105
Cdd:TIGR02868 350 VLDGVSLDLPPGERVAILGPSGSGKSTLlATLAGLLD-PLQGEVTLDGVPVSSLDQDEVRRR----VSVCAQDAHLFDT- 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 106 TALQNVELpliyAGVNVSKrrEQAKQFLEKVGLGRRIKHLP-----------SELSGGQKQRVAIARALVNDPSIILADE 174
Cdd:TIGR02868 424 TVRENLRL----ARPDATD--EELWAALERVGLADWLRALPdgldtvlgeggARLSGGERQRLALARALLADAPILLLDE 497
|
170 180 190
....*....|....*....|....*....|....
gi 2076047389 175 PTGALDTKTGQQIMELLTELNkEGKTIIMVTHEP 208
Cdd:TIGR02868 498 PTEHLDAETADELLEDLLAAL-SGRTVVLITHHL 530
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
8-225 |
1.64e-34 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 122.86 E-value: 1.64e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 8 LMQLSNIVKSYQNGDQVLKVLKGINLTVYEGEFLAIMGPSGSGKSTLMNIIGLLDRPTSGDYTLHNtkIEILNDRELAKV 87
Cdd:cd03266 1 MITADALTKRFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDG--FDVVKEPAEARR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 88 RndeIGFVFQQFFLLAKLTALQNVELpliYAGVNVSKRREqAKQFLEKVGLGRRIKHL----PSELSGGQKQRVAIARAL 163
Cdd:cd03266 79 R---LGFVSDSTGLYDRLTARENLEY---FAGLYGLKGDE-LTARLEELADRLGMEELldrrVGGFSTGMRQKVAIARAL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2076047389 164 VNDPSIILADEPTGALDTKTGQQIMELLTELNKEGKTIIMVTHE-PEIADFATRKIIIRDGDI 225
Cdd:cd03266 152 VHDPPVLLLDEPTTGLDVMATRALREFIRQLRALGKCILFSTHImQEVERLCDRVVVLHRGRV 214
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
26-228 |
1.89e-34 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 123.97 E-value: 1.89e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 26 KVLKGINLTVYEGEFLAIMGPSGSGKSTLM-NIIGLLdrptSGDYTLhNTKIEILND---------RELAKVRNdEIGFV 95
Cdd:PRK09984 18 QALHAVDLNIHHGEMVALLGPSGSGKSTLLrHLSGLI----TGDKSA-GSHIELLGRtvqregrlaRDIRKSRA-NTGYI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 96 FQQFFLLAKLTALQNVEL------PLIYAGVN--VSKRREQAKQFLEKVGLGRRIKHLPSELSGGQKQRVAIARALVNDP 167
Cdd:PRK09984 92 FQQFNLVNRLSVLENVLIgalgstPFWRTCFSwfTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAIARALMQQA 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2076047389 168 SIILADEPTGALDTKTGQQIMELLTELNK-EGKTIIMVTHEPEIA-DFATRKIIIRDGDITTD 228
Cdd:PRK09984 172 KVILADEPIASLDPESARIVMDTLRDINQnDGITVVVTLHQVDYAlRYCERIVALRQGHVFYD 234
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
27-220 |
1.93e-34 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 121.57 E-value: 1.93e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 27 VLKGINLTVYEGEFLAIMGPSGSGKSTLMNII-GLLdRPTSGdytlhntkieilndrELAKVRNDEIGFVFQQFFLLAKL 105
Cdd:NF040873 7 VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLaGVL-RPTSG---------------TVRRAGGARVAYVPQRSEVPDSL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 106 --TALQNVELPLiYAGVNVSKR-----REQAKQFLEKVGL----GRRIkhlpSELSGGQKQRVAIARALVNDPSIILADE 174
Cdd:NF040873 71 plTVRDLVAMGR-WARRGLWRRltrddRAAVDDALERVGLadlaGRQL----GELSGGQRQRALLAQGLAQEADLLLLDE 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2076047389 175 PTGALDTKTGQQIMELLTELNKEGKTIIMVTHEPEIADFATRKIII 220
Cdd:NF040873 146 PTTGLDAESRERIIALLAEEHARGATVVVVTHDLELVRRADPCVLL 191
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
10-225 |
1.93e-34 |
|
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: 122.72 E-value: 1.93e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 10 QLSNIVKSYQNGDQVLKvlkGINLTVYEGEFLAIMGPSGSGKSTLMNIIGLLDRPTSGDYTLHNTKIeilNDRELAKVRN 89
Cdd:cd03254 4 EFENVNFSYDEKKPVLK---DINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDI---RDISRKSLRS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 90 dEIGFVFQQFFLLAKlTALQNVELPLIYAgvnvskRREQAKQFLEKVGLGRRIKHLP-----------SELSGGQKQRVA 158
Cdd:cd03254 78 -MIGVVLQDTFLFSG-TIMENIRLGRPNA------TDEEVIEAAKEAGAHDFIMKLPngydtvlgengGNLSQGERQLLA 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2076047389 159 IARALVNDPSIILADEPTGALDTKTGQQIMELLTELNKeGKTIIMVTHEPEIADFATRKIIIRDGDI 225
Cdd:cd03254 150 IARAMLRDPKILILDEATSNIDTETEKLIQEALEKLMK-GRTSIIIAHRLSTIKNADKILVLDDGKI 215
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
28-225 |
2.21e-34 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 124.36 E-value: 2.21e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 28 LKGINLTVYEGEFLAIMGPSGSGKSTLMNIIGLLDRPTSGDYTLHNTKIEI-LNDRELAKVRNdEIGFVFQ----QFFll 102
Cdd:PRK13634 23 LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAgKKNKKLKPLRK-KVGIVFQfpehQLF-- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 103 aKLTALQNVELPLIYAGVNVSKRREQAKQFLEKVGLGRRI-KHLPSELSGGQKQRVAIARALVNDPSIILADEPTGALDT 181
Cdd:PRK13634 100 -EETVEKDICFGPMNFGVSEEDAKQKAREMIELVGLPEELlARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDP 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2076047389 182 KTGQQIMELLTELNKE-GKTIIMVTHEPE-IADFATRKIIIRDGDI 225
Cdd:PRK13634 179 KGRKEMMEMFYKLHKEkGLTTVLVTHSMEdAARYADQIVVMHKGTV 224
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
8-207 |
2.26e-34 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 125.22 E-value: 2.26e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 8 LMQLSNIVKSYQNGDQVLKVLKGINLTVYEGEFLAIMGPSGSGKS-TLMNIIGLLDRP--TSGDYTLHNTKIEILNDREL 84
Cdd:PRK09473 12 LLDVKDLRVTFSTPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSqTAFALMGLLAANgrIGGSATFNGREILNLPEKEL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 85 AKVRNDEIGFVFQQffllaKLTAL--------QNVELPLIYAGVNVSKRREQAKQFLEKVGLG---RRIKHLPSELSGGQ 153
Cdd:PRK09473 92 NKLRAEQISMIFQD-----PMTSLnpymrvgeQLMEVLMLHKGMSKAEAFEESVRMLDAVKMPearKRMKMYPHEFSGGM 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2076047389 154 KQRVAIARALVNDPSIILADEPTGALDTKTGQQIMELLTELNKEGKT-IIMVTHE 207
Cdd:PRK09473 167 RQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTaIIMITHD 221
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
8-220 |
2.68e-34 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 123.41 E-value: 2.68e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 8 LMQLSNIVKSYQNGD-----QVLKVLKGINLTVYEGEFLAIMGPSGSGKSTLMNIIGLLDRPTSGDYTLHNTKIEILNDR 82
Cdd:COG4167 4 LLEVRNLSKTFKYRTglfrrQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYGDYK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 83 ELAKVrndeIGFVFQ--QFFLLAKLTALQNVELPLIYA-GVNVSKRREQAKQFLEKVGLGRriKHL---PSELSGGQKQR 156
Cdd:COG4167 84 YRCKH----IRMIFQdpNTSLNPRLNIGQILEEPLRLNtDLTAEEREERIFATLRLVGLLP--EHAnfyPHMLSSGQKQR 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2076047389 157 VAIARALVNDPSIILADEPTGALDTKTGQQIMELLTELNKE-GKTIIMVTHEPEIADFATRKIII 220
Cdd:COG4167 158 VALARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKlGISYIYVSQHLGIVKHISDKVLV 222
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
10-206 |
4.45e-34 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 124.96 E-value: 4.45e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 10 QLSNIVKSYQNGDQVLKvlkGINLTVYEGEFLAIMGPSGSGKSTLMNIIGLLDRPTSGDytlhntkIEI----LNDRELA 85
Cdd:PRK11650 5 KLQAVRKSYDGKTQVIK---GIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGE-------IWIggrvVNELEPA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 86 KvRNdeIGFVFQQFFLLAKLTALQNVELPLIYAGV---NVSKRREQAKQFLEkvgLGRRIKHLPSELSGGQKQRVAIARA 162
Cdd:PRK11650 75 D-RD--IAMVFQNYALYPHMSVRENMAYGLKIRGMpkaEIEERVAEAARILE---LEPLLDRKPRELSGGQRQRVAMGRA 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2076047389 163 LVNDPSIILADEPTGALDTKTGQQ----IMELLTELnkeGKTIIMVTH 206
Cdd:PRK11650 149 IVREPAVFLFDEPLSNLDAKLRVQmrleIQRLHRRL---KTTSLYVTH 193
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
10-236 |
9.28e-34 |
|
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: 128.06 E-value: 9.28e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 10 QLSNIVKSYQNGDQvlKVLKGINLTVYEGEFLAIMGPSGSGKSTLMNIIGLLDRPTSGDYTLHNTKIEILNDRELAkvRN 89
Cdd:TIGR03375 465 EFRNVSFAYPGQET--PALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQIDPADLR--RN 540
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 90 deIGFVFQQFFLLAKlTALQNvelpLIYAGVNVSKRREQAKqfLEKVGLGRRIKHLPS-----------ELSGGQKQRVA 158
Cdd:TIGR03375 541 --IGYVPQDPRLFYG-TLRDN----IALGAPYADDEEILRA--AELAGVTEFVRRHPDgldmqigergrSLSGGQRQAVA 611
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2076047389 159 IARALVNDPSIILADEPTGALDTKTGQQIMELLTELnKEGKTIIMVTHEPEIADFATRKIIIRDGDITTDTTASVVID 236
Cdd:TIGR03375 612 LARALLRDPPILLLDEPTSAMDNRSEERFKDRLKRW-LAGKTLVLVTHRTSLLDLVDRIIVMDNGRIVADGPKDQVLE 688
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
5-225 |
1.90e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 121.64 E-value: 1.90e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 5 KKQLMQLSNIVKSYQNGDQvlKVLKGINLTVYEGEFLAIMGPSGSGKSTLMNIIGLLDRPTSGDYTLHNTKIEILNDREL 84
Cdd:PRK13632 4 KSVMIKVENVSFSYPNSEN--NALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 85 AKvrndEIGFVFQ----QFFllaKLTALQNVELPLIYAGVNVSKRREQAKQFLEKVGLGRRIKHLPSELSGGQKQRVAIA 160
Cdd:PRK13632 82 RK----KIGIIFQnpdnQFI---GATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2076047389 161 RALVNDPSIILADEPTGALDTKTGQQIMELLTELNKEG-KTIIMVTHEPEIADFATRKIIIRDGDI 225
Cdd:PRK13632 155 SVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRkKTLISITHDMDEAILADKVIVFSEGKL 220
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
8-206 |
2.35e-33 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 126.09 E-value: 2.35e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 8 LMQLSNIVKSYQNGDQvlKVLKGINLTVYEGEFLAIMGPSGSGKSTLMNiigLLDR---PTSGDYTLHNTKIEILNDREL 84
Cdd:PRK11160 338 SLTLNNVSFTYPDQPQ--PVLKGLSLQIKAGEKVALLGRTGCGKSTLLQ---LLTRawdPQQGEILLNGQPIADYSEAAL 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 85 akvRNdEIGFVFQQFFLLAKlTALQNvelpLIYAGVNVSKrrEQAKQFLEKVGLGrriKHLPSE-------------LSG 151
Cdd:PRK11160 413 ---RQ-AISVVSQRVHLFSA-TLRDN----LLLAAPNASD--EALIEVLQQVGLE---KLLEDDkglnawlgeggrqLSG 478
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2076047389 152 GQKQRVAIARALVNDPSIILADEPTGALDTKTGQQIMELLTELNKeGKTIIMVTH 206
Cdd:PRK11160 479 GEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQ-NKTVLMITH 532
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
8-197 |
2.49e-33 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 122.38 E-value: 2.49e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 8 LMQLSNIVKSYQ------NGDQVLKVLKGINLTVYEGEFLAIMGPSGSGKSTLMNIIGLLDRPTSGDYTLHNTKIeILND 81
Cdd:PRK11308 5 LLQAIDLKKHYPvkrglfKPERLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDL-LKAD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 82 RELAKVRNDEIGFVFQQFFllAKLTALQNV----ELPL-IYAGVNVSKRREQAKQFLEKVGLgrRIKH---LPSELSGGQ 153
Cdd:PRK11308 84 PEAQKLLRQKIQIVFQNPY--GSLNPRKKVgqilEEPLlINTSLSAAERREKALAMMAKVGL--RPEHydrYPHMFSGGQ 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2076047389 154 KQRVAIARALVNDPSIILADEPTGALDTKTGQQIMELLTELNKE 197
Cdd:PRK11308 160 RQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQE 203
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
11-211 |
3.99e-33 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 125.09 E-value: 3.99e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 11 LSNIVKSYQNGDqvlKVLKGINLTVYEGEFLAIMGPSGSGKSTLMNII-GLLDrPTSGdytlhntkiEI-LNDRELA--- 85
Cdd:TIGR02857 324 FSGVSVAYPGRR---PALRPVSFTVPPGERVALVGPSGAGKSTLLNLLlGFVD-PTEG---------SIaVNGVPLAdad 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 86 -KVRNDEIGFVFQQFFLLAKlTALQNVELPLIYAGvnvskrREQAKQFLEKVGLGRRIKHLP-----------SELSGGQ 153
Cdd:TIGR02857 391 aDSWRDQIAWVPQHPFLFAG-TIAENIRLARPDAS------DAEIREALERAGLDEFVAALPqgldtpigeggAGLSGGQ 463
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2076047389 154 KQRVAIARALVNDPSIILADEPTGALDTKTGQQIMELLTELnKEGKTIIMVTHEPEIA 211
Cdd:TIGR02857 464 AQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRAL-AQGRTVLLVTHRLALA 520
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
28-236 |
4.16e-33 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 123.60 E-value: 4.16e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 28 LKGINLTVYEGEFLAIMGPSGSGKSTLMNIIGLLDRPTSGDYTLHNTKIEILNDRELAKVRNDEIGFVFQQFFLLAKLTA 107
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVRRKKIAMVFQSFALMPHMTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 108 LQNVELPLIYAGVNVSKRREQAKQFLEKVGLGRRIKHLPSELSGGQKQRVAIARALVNDPSIILADEPTGALDTKTGQQI 187
Cdd:PRK10070 124 LDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEM 203
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2076047389 188 MELLTELN-KEGKTIIMVTHE-PEIADFATRKIIIRDGDITTDTTASVVID 236
Cdd:PRK10070 204 QDELVKLQaKHQRTIVFISHDlDEAMRIGDRIAIMQNGEVVQVGTPDEILN 254
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
8-235 |
6.22e-33 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 119.84 E-value: 6.22e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 8 LMQLSNIvkSYQNGDQVLkvLKGINLTVYEGEFLAIMGPSGSGKSTLMNII-GLLdRPTSGDYTLHNTKIEILNDRELAK 86
Cdd:COG4559 1 MLEAENL--SVRLGGRTL--LDDVSLTLRPGELTAIIGPNGAGKSTLLKLLtGEL-TPSSGEVRLNGRPLAAWSPWELAR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 87 VR-----NDEIGFVFqqffllaklTALQNVELPLIYAGVNVSKRREQAKQFLEKVGLGRRIKHLPSELSGGQKQRVAIAR 161
Cdd:COG4559 76 RRavlpqHSSLAFPF---------TVEEVVALGRAPHGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLAR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 162 ALV-------NDPSIILADEPTGALDTKTGQQIMELLTELNKEGKTIIMVTHEPEI-ADFATRKIIIRDGDITTDTTASV 233
Cdd:COG4559 147 VLAqlwepvdGGPRWLFLDEPTSALDLAHQHAVLRLARQLARRGGGVVAVLHDLNLaAQYADRILLLHQGRLVAQGTPEE 226
|
..
gi 2076047389 234 VI 235
Cdd:COG4559 227 VL 228
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
26-206 |
6.81e-33 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 119.18 E-value: 6.81e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 26 KVLKGINLTVYEGEFLAIMGPSGSGKSTlmnIIGLLDR---PTSGDYTLHNTKIEILNDRELakvrNDEIGFVFQQFFLL 102
Cdd:cd03249 17 PILKGLSLTIPPGKTVALVGSSGCGKST---VVSLLERfydPTSGEILLDGVDIRDLNLRWL----RSQIGLVSQEPVLF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 103 AKlTALQNVELPLIYAGVnvskrrEQAKQFLEKVGLGRRIKHLP-----------SELSGGQKQRVAIARALVNDPSIIL 171
Cdd:cd03249 90 DG-TIAENIRYGKPDATD------EEVEEAAKKANIHDFIMSLPdgydtlvgergSQLSGGQKQRIAIARALLRNPKILL 162
|
170 180 190
....*....|....*....|....*....|....*
gi 2076047389 172 ADEPTGALDTKTGQQIMELLTELnKEGKTIIMVTH 206
Cdd:cd03249 163 LDEATSALDAESEKLVQEALDRA-MKGRTTIVIAH 196
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
19-225 |
1.07e-32 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 118.14 E-value: 1.07e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 19 QNGDQVLKVLKGINLTVYEGEFLAIMGPSGSGKSTLMNII-GLLDRP--TSGDYTLHNTKIEIlndrelAKVRnDEIGFV 95
Cdd:cd03234 14 KNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAIsGRVEGGgtTSGQILFNGQPRKP------DQFQ-KCVAYV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 96 FQQFFLLAKLTalqnVELPLIYAgVNVSKRREQAKQFLEKVGLGRRIKHLPSE---------LSGGQKQRVAIARALVND 166
Cdd:cd03234 87 RQDDILLPGLT----VRETLTYT-AILRLPRKSSDAIRKKRVEDVLLRDLALTriggnlvkgISGGERRRVSIAVQLLWD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2076047389 167 PSIILADEPTGALDTKTGQQIMELLTELNKEGKTIIMVTHEP--EIADFATRKIIIRDGDI 225
Cdd:cd03234 162 PKVLILDEPTSGLDSFTALNLVSTLSQLARRNRIVILTIHQPrsDLFRLFDRILLLSSGEI 222
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
10-225 |
1.10e-32 |
|
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: 117.70 E-value: 1.10e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 10 QLSNIVKSYQNGdqvlKVLKGINLTVYEGEFLAIMGPSGSGKSTLMNIIGLLDRPTSGDYTlhntkIEILNDRELAKVRN 89
Cdd:cd03268 2 KTNDLTKTYGKK----RVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEIT-----FDGKSYQKNIEALR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 90 dEIGFVFQQFFLLAKLTALQNVELPLIYAGVnvskRREQAKQFLEKVGLGRRIKHLPSELSGGQKQRVAIARALVNDPSI 169
Cdd:cd03268 73 -RIGALIEAPGFYPNLTARENLRLLARLLGI----RKKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDL 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2076047389 170 ILADEPTGALDTKTGQQIMELLTELNKEGKTIIMVTHE-PEIADFATRKIIIRDGDI 225
Cdd:cd03268 148 LILDEPTNGLDPDGIKELRELILSLRDQGITVLISSHLlSEIQKVADRIGIINKGKL 204
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
9-228 |
1.39e-32 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 119.03 E-value: 1.39e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 9 MQLSNIVKSYQNG--DQVlKVLKGINLTVYEGEFLAIMGPSGSGKSTLMNIIglldrptSGDYTLHNTKIEIlNDRELAK 86
Cdd:COG1101 2 LELKNLSKTFNPGtvNEK-RALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAI-------AGSLPPDSGSILI-DGKDVTK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 87 V----RNDEIGFVFQQFFL--LAKLTALQNveLPLIYA---------GVNvSKRREQAKQFLEKVGLG--RRIKHLPSEL 149
Cdd:COG1101 73 LpeykRAKYIGRVFQDPMMgtAPSMTIEEN--LALAYRrgkrrglrrGLT-KKRRELFRELLATLGLGleNRLDTKVGLL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 150 SGGQKQRVAIARALVNDPSIILADEPTGALDTKTGQQIMELLTELNKEGK-TIIMVTHEPEIA-DFATRKIIIRDGDITT 227
Cdd:COG1101 150 SGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNlTTLMVTHNMEQAlDYGNRLIMMHEGRIIL 229
|
.
gi 2076047389 228 D 228
Cdd:COG1101 230 D 230
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
8-204 |
3.18e-32 |
|
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: 117.39 E-value: 3.18e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 8 LMQLSNIVKSYqnGDqvLKVLKGINLTVYEGEFLAIMGPSGSGKSTLMN-IIGLLdRPTSGDYTLhntkieilNDRELAK 86
Cdd:COG0410 3 MLEVENLHAGY--GG--IHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKaISGLL-PPRSGSIRF--------DGEDITG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 87 VRNDE-----IGFVFQQFFLLAKLTALQNVELpliyaGVNVSKRREQAKQFLEKVG-----LGRRIKHLPSELSGGQKQR 156
Cdd:COG0410 70 LPPHRiarlgIGYVPEGRRIFPSLTVEENLLL-----GAYARRDRAEVRADLERVYelfprLKERRRQRAGTLSGGEQQM 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2076047389 157 VAIARALVNDPSIILADEPTGALDTKTGQQIMELLTELNKEGKTIIMV 204
Cdd:COG0410 145 LAIGRALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNREGVTILLV 192
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
8-222 |
3.48e-32 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 120.71 E-value: 3.48e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 8 LMQLSNIVKSYQNGDQVLKVlkgiNLTVYEGEFLAIMGPSGSGKSTLMNIIGLLDRPTSGDYtlhntkieILNDRELAKV 87
Cdd:PRK11607 19 LLEIRNLTKSFDGQHAVDDV----SLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQI--------MLDGVDLSHV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 88 --RNDEIGFVFQQFFLLAKLTALQNVELPLIYAGVNVSKRREQAKQFLEKVGLGRRIKHLPSELSGGQKQRVAIARALVN 165
Cdd:PRK11607 87 ppYQRPINMMFQSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAK 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2076047389 166 DPSIILADEPTGALDTKTGQQI-MELLTELNKEGKTIIMVTHEPEIADFATRKIIIRD 222
Cdd:PRK11607 167 RPKLLLLDEPMGALDKKLRDRMqLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMN 224
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
8-223 |
4.14e-32 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 122.51 E-value: 4.14e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 8 LMQLSNIVKSYQNGDQVLKVLKGINLTVYEGEFLAIMGPSGSGKS-TLMNIIGLLDRP----TSGDYTLHNTKIEILNDR 82
Cdd:PRK15134 5 LLAIENLSVAFRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPpvvyPSGDIRFHGESLLHASEQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 83 ELAKVRNDEIGFVFQQffLLAKLTALQNVELPL-----IYAGVnvskRREQAK----QFLEKVGL---GRRIKHLPSELS 150
Cdd:PRK15134 85 TLRGVRGNKIAMIFQE--PMVSLNPLHTLEKQLyevlsLHRGM----RREAARgeilNCLDRVGIrqaAKRLTDYPHQLS 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2076047389 151 GGQKQRVAIARALVNDPSIILADEPTGALDTKTGQQIMELLTELNKE-GKTIIMVTHEPEIA-DFATRKIIIRDG 223
Cdd:PRK15134 159 GGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQElNMGLLFITHNLSIVrKLADRVAVMQNG 233
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
1-207 |
6.15e-32 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 119.04 E-value: 6.15e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 1 MSHEKKQLMQLSNIVKSYQNGD---------QVLKVLKGINLTVYEGEFLAIMGPSGSGKSTLMN-IIGLLdRPTSGDYT 70
Cdd:PRK15079 1 VTEGKKVLLEVADLKVHFDIKDgkqwfwqppKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARaIIGLV-KATDGEVA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 71 LHNTKIEILNDRELAKVRNDeIGFVFQQffLLAKLTALQNV------ELPLIYAGVNVSKRREQAKQFLEKVGL-GRRIK 143
Cdd:PRK15079 80 WLGKDLLGMKDDEWRAVRSD-IQMIFQD--PLASLNPRMTIgeiiaePLRTYHPKLSRQEVKDRVKAMMLKVGLlPNLIN 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2076047389 144 HLPSELSGGQKQRVAIARALVNDPSIILADEPTGALDTKTGQQIMELLTELNKE-GKTIIMVTHE 207
Cdd:PRK15079 157 RYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREmGLSLIFIAHD 221
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
11-225 |
1.49e-31 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 115.33 E-value: 1.49e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 11 LSNIVKSYQNGdqvlKVLKGINLTVYEGEFLAIMGPSGSGKSTLMNIIGLLDRPTSGdytlhntKIeILNDRELAKVRND 90
Cdd:cd03218 3 AENLSKRYGKR----KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSG-------KI-LLDGQDITKLPMH 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 91 E-----IGFVFQQFFLLAKLTALQNVELPLIYAGVNVSKRREQAKQFLEKVGLGRRIKHLPSELSGGQKQRVAIARALVN 165
Cdd:cd03218 71 KrarlgIGYLPQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALAT 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2076047389 166 DPSIILADEPTGALDTKTGQQIMELLTELNKEGKTIIMVTHE-PEIADFATRKIIIRDGDI 225
Cdd:cd03218 151 NPKFLLLDEPFAGVDPIAVQDIQKIIKILKDRGIGVLITDHNvRETLSITDRAYIIYEGKV 211
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
9-226 |
2.01e-31 |
|
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: 113.56 E-value: 2.01e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 9 MQLSNIVKSYQNGDQvlKVLKGINLTVYEGEFLAIMGPSGSGKSTLMNII-GLLDrPTSGDYTLHNTKIEilndrELAKV 87
Cdd:cd03247 1 LSINNVSFSYPEQEQ--QVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLtGDLK-PQQGEITLDGVPVS-----DLEKA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 88 RNDEIGFVFQQFFLLAKlTALQNvelpliyagvnvskrreqakqflekvgLGRRikhlpseLSGGQKQRVAIARALVNDP 167
Cdd:cd03247 73 LSSLISVLNQRPYLFDT-TLRNN---------------------------LGRR-------FSGGERQRLALARILLQDA 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2076047389 168 SIILADEPTGALDTKTGQQIMELLTELNKEgKTIIMVTHEPEIADFATRKIIIRDGDIT 226
Cdd:cd03247 118 PIVLLDEPTVGLDPITERQLLSLIFEVLKD-KTLIWITHHLTGIEHMDKILFLENGKII 175
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
6-223 |
3.98e-31 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 119.50 E-value: 3.98e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 6 KQLMQLSNIVKSYQngdqVLKVLKGINLTVYEGEFLAIMGPSGSGKSTLMNIIGLLDRPTSGDYTLHNTKIEILNDRELA 85
Cdd:PRK09700 3 TPYISMAGIGKSFG----PVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 86 KVrndEIGFVFQQFFLLAKLTALQNV---ELPL-IYAGVNV---SKRREQAKQFLEKVGLGRRIKHLPSELSGGQKQRVA 158
Cdd:PRK09700 79 QL---GIGIIYQELSVIDELTVLENLyigRHLTkKVCGVNIidwREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLE 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2076047389 159 IARALVNDPSIILADEPTGALDTKTGQQIMELLTELNKEGKTIIMVTHE-PEIADFATRKIIIRDG 223
Cdd:PRK09700 156 IAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKlAEIRRICDRYTVMKDG 221
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
5-230 |
4.16e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 115.57 E-value: 4.16e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 5 KKQLMQLSNIVKSYQNGDQVLK--VLKGINLTVYEGEFLAIMGPSGSGKSTLMNIIGLLDRPTSGdyTLHNTKIEILNDR 82
Cdd:PRK13633 1 MNEMIKCKNVSYKYESNEESTEklALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEG--KVYVDGLDTSDEE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 83 ELAKVRNdEIGFVFQ----QffLLAKLtalqnVELPLIYA----GVNVSKRREQAKQFLEKVGLGRRIKHLPSELSGGQK 154
Cdd:PRK13633 79 NLWDIRN-KAGMVFQnpdnQ--IVATI-----VEEDVAFGpenlGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQK 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2076047389 155 QRVAIARALVNDPSIILADEPTGALDTKTGQQIMELLTELNKE-GKTIIMVTHEPEIADFATRKIIIRDGDITTDTT 230
Cdd:PRK13633 151 QRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKyGITIILITHYMEEAVEADRIIVMDSGKVVMEGT 227
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
9-231 |
6.05e-31 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 114.86 E-value: 6.05e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 9 MQLSNIVK----SYQNGDQvlKVLKGINLTVYEGEFLAIMGPSGSGKSTLMNIIGLLDRPTSGDYTLHNTKIEILNDREL 84
Cdd:PRK11831 2 QSVANLVDmrgvSFTRGNR--CIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 85 AKVRNdEIGFVFQQFFLLAKLTALQNVELPLiyagvnvskrREQAK-----------QFLEKVGLGRRIKHLPSELSGGQ 153
Cdd:PRK11831 80 YTVRK-RMSMLFQSGALFTDMNVFDNVAYPL----------REHTQlpapllhstvmMKLEAVGLRGAAKLMPSELSGGM 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 154 KQRVAIARALVNDPSIILADEPTGALDTKTGQQIMELLTELNKE-GKTIIMVTHE-PEIADFATRKIIIRDGDITTDTTA 231
Cdd:PRK11831 149 ARRAALARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSAlGVTCVVVSHDvPEVLSIADHAYIVADKKIVAHGSA 228
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
28-208 |
6.90e-31 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 119.38 E-value: 6.90e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 28 LKGINLTVYEGEFLAIMGPSGSGKSTLMNIIGLLDRP---TSGDYTLHNTKIeilnDRELAKVRNdeiGFVFQQFFLLAK 104
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKgvkGSGSVLLNGMPI----DAKEMRAIS---AYVQQDDLFIPT 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 105 LTALQNvelpLIY-------AGVNVSKRREQAKQFLEKVGLGR----RI--KHLPSELSGGQKQRVAIARALVNDPSIIL 171
Cdd:TIGR00955 114 LTVREH----LMFqahlrmpRRVTKKEKRERVDEVLQALGLRKcantRIgvPGRVKGLSGGERKRLAFASELLTDPPLLF 189
|
170 180 190
....*....|....*....|....*....|....*..
gi 2076047389 172 ADEPTGALDTKTGQQIMELLTELNKEGKTIIMVTHEP 208
Cdd:TIGR00955 190 CDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQP 226
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
26-234 |
9.22e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 114.76 E-value: 9.22e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 26 KVLKGINLTVYEGEFLAIMGPSGSGKSTLMNIIGLLDRPTSGDYTLHNTKI--EILNDRELAKvrndEIGFVFQ----QF 99
Cdd:PRK13637 21 KALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDItdKKVKLSDIRK----KVGLVFQypeyQL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 100 FllaKLTALQNVELPLIYAGVNVSKRREQAKQFLEKVGLGRRI--KHLPSELSGGQKQRVAIARALVNDPSIILADEPTG 177
Cdd:PRK13637 97 F---EETIEKDIAFGPINLGLSEEEIENRVKRAMNIVGLDYEDykDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTA 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2076047389 178 ALDTKTGQQIMELLTELNKEGK-TIIMVTHEPE-IADFATRKIIIRDGDITTDTTASVV 234
Cdd:PRK13637 174 GLDPKGRDEILNKIKELHKEYNmTIILVSHSMEdVAKLADRIIVMNKGKCELQGTPREV 232
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
26-225 |
1.76e-30 |
|
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: 112.71 E-value: 1.76e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 26 KVLKGINLTVYEGEFLAIMGPSGSGKSTLMNIIGLLDRPTSGdytlhntKIEIlNDRELAKVRND----EIGFVFQQFFL 101
Cdd:cd03253 15 PVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSG-------SILI-DGQDIREVTLDslrrAIGVVPQDTVL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 102 LAKlTALQNVElpliYAGVNVSKrrEQAKQFLEKVGLGRRIKHLPS-----------ELSGGQKQRVAIARALVNDPSII 170
Cdd:cd03253 87 FND-TIGYNIR----YGRPDATD--EEVIEAAKAAQIHDKIMRFPDgydtivgerglKLSGGEKQRVAIARAILKNPPIL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2076047389 171 LADEPTGALDTKTGQQIMELLTELNKeGKTIIMVTHE-PEIADfATRKIIIRDGDI 225
Cdd:cd03253 160 LLDEATSALDTHTEREIQAALRDVSK-GRTTIVIAHRlSTIVN-ADKIIVLKDGRI 213
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
31-226 |
1.92e-30 |
|
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: 115.59 E-value: 1.92e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 31 INLTVYEGEFLAIMGPSGSGKSTLMNIIGLLDRPTSGdytlhntkiEI-LNDRELAKVRND--------EIGFVFQQFFL 101
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEG---------EIvLNGRTLFDSRKGiflppekrRIGYVFQEARL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 102 LAKLTALQNVELPliYAGVNVSKRREQAKQFLEKVGLGRRIKHLPSELSGGQKQRVAIARALVNDPSIILADEPTGALDT 181
Cdd:TIGR02142 87 FPHLSVRGNLRYG--MKRARPSERRISFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDD 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2076047389 182 KTGQQIMELLTELNKE-GKTIIMVTHEP-EIADFATRKIIIRDGDIT 226
Cdd:TIGR02142 165 PRKYEILPYLERLHAEfGIPILYVSHSLqEVLRLADRVVVLEDGRVA 211
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
26-225 |
2.08e-30 |
|
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: 112.71 E-value: 2.08e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 26 KVLKGINLTVYEGEFLAIMGPSGSGKSTLMNIIGLLDRPTSGDYTLHNTKIEilnDRELAKVRNdEIGFVFQQFFLLAKl 105
Cdd:cd03251 16 PVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVR---DYTLASLRR-QIGLVSQDVFLFND- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 106 TALQNVElpliYAGVNVSK-------RREQAKQFLEKV--GLGRRIKHLPSELSGGQKQRVAIARALVNDPSIILADEPT 176
Cdd:cd03251 91 TVAENIA----YGRPGATReeveeaaRAANAHEFIMELpeGYDTVIGERGVKLSGGQRQRIAIARALLKDPPILILDEAT 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2076047389 177 GALDTKTGQQIMELLTELNKeGKTIIMVTHEPEIADFATRKIIIRDGDI 225
Cdd:cd03251 167 SALDTESERLVQAALERLMK-NRTTFVIAHRLSTIENADRIVVLEDGKI 214
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
8-230 |
3.28e-30 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 112.86 E-value: 3.28e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 8 LMQLSNIVKSYQNG-----DQVLKVLKGINLTVYEGEFLAIMGPSGSGKSTLMNIIGLLDRPTSGDYTLHNTKIEILNDR 82
Cdd:PRK10419 3 LLNVSGLSHHYAHGglsgkHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 83 ELAKVRNDeIGFVFQQFF--LLAKLTALQNVELPLIY-AGVNVSKRREQAKQFLEKVGLGRRI-KHLPSELSGGQKQRVA 158
Cdd:PRK10419 83 QRKAFRRD-IQMVFQDSIsaVNPRKTVREIIREPLRHlLSLDKAERLARASEMLRAVDLDDSVlDKRPPQLSGGQLQRVC 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2076047389 159 IARALVNDPSIILADEPTGALDTKTGQQIMELLTELNKEGKT-IIMVTHEPEIAD-FATRKIIIRDGDITTDTT 230
Cdd:PRK10419 162 LARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTaCLFITHDLRLVErFCQRVMVMDNGQIVETQP 235
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
9-223 |
9.41e-30 |
|
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: 110.06 E-value: 9.41e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 9 MQLSNIVKSYqnGDQvlKVLKGINLTVYEGEFLAIMGPSGSGKSTLMNIIGLLDRPTSGdytlhntKIEILNDRELAKVR 88
Cdd:cd03269 1 LEVENVTKRF--GRV--TALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSG-------EVLFDGKPLDIAAR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 89 NDeIGFVFQQFFLLAKLTALQNvelpLIY----AGVNVSKRREQAKQFLEKVGLGRRIKHLPSELSGGQKQRVAIARALV 164
Cdd:cd03269 70 NR-IGYLPEERGLYPKMKVIDQ----LVYlaqlKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVI 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 165 NDPSIILADEPTGALDTKTGQQIMELLTELNKEGKTIIMVTHEPE-IADFATRKIIIRDG 223
Cdd:cd03269 145 HDPELLILDEPFSGLDPVNVELLKDVIRELARAGKTVILSTHQMElVEELCDRVLLLNKG 204
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
25-230 |
1.07e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 112.64 E-value: 1.07e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 25 LKVLKGINLTVYEGEFLAIMGPSGSGKSTLMNIIGLLDRPTSGDYTLHNTKI----------------EILNDRELAKVr 88
Cdd:PRK13631 39 LVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIgdkknnhelitnpyskKIKNFKELRRR- 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 89 ndeIGFVFQ----QFFllaKLTALQNVELPLIYAGVNVSKRREQAKQFLEKVGLGRR-IKHLPSELSGGQKQRVAIARAL 163
Cdd:PRK13631 118 ---VSMVFQfpeyQLF---KDTIEKDIMFGPVALGVKKSEAKKLAKFYLNKMGLDDSyLERSPFGLSGGQKRRVAIAGIL 191
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2076047389 164 VNDPSIILADEPTGALDTKTGQQIMELLTELNKEGKTIIMVTHEP----EIADFAtrkIIIRDGDITTDTT 230
Cdd:PRK13631 192 AIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMehvlEVADEV---IVMDKGKILKTGT 259
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
26-211 |
1.19e-29 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 111.16 E-value: 1.19e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 26 KVLKGINLTVYEGEFLAIMGPSGSGKSTLMNIIGLL-----DRPTSGDYTLHNTKIEILNDRELAKvrndEIGFVFQQFF 100
Cdd:PRK14247 17 EVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQDIFKMDVIELRR----RVQMVFQIPN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 101 LLAKLTALQNVELPLIYAGVNVSKR--REQAKQFLEKVGLGRRIKH---LPS-ELSGGQKQRVAIARALVNDPSIILADE 174
Cdd:PRK14247 93 PIPNLSIFENVALGLKLNRLVKSKKelQERVRWALEKAQLWDEVKDrldAPAgKLSGGQQQRLCIARALAFQPEVLLADE 172
|
170 180 190
....*....|....*....|....*....|....*..
gi 2076047389 175 PTGALDTKTGQQIMELLTELNKEgKTIIMVTHEPEIA 211
Cdd:PRK14247 173 PTANLDPENTAKIESLFLELKKD-MTIVLVTHFPQQA 208
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
11-226 |
4.20e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 110.22 E-value: 4.20e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 11 LSNIVKSYQNGDQVL-KVLKGINLTVYEGEFLAIMGPSGSGKSTLMNIIGLLDRPTSGDYTLHNTKIEILN-DRELAKVR 88
Cdd:PRK13649 5 LQNVSYTYQAGTPFEgRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSkNKDIKQIR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 89 NdEIGFVFQ----QFFllaKLTALQNVELPLIYAGVNVSKRREQAKQFLEKVGLGRRI-KHLPSELSGGQKQRVAIARAL 163
Cdd:PRK13649 85 K-KVGLVFQfpesQLF---EETVLKDVAFGPQNFGVSQEEAEALAREKLALVGISESLfEKNPFELSGGQMRRVAIAGIL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2076047389 164 VNDPSIILADEPTGALDTKTGQQIMELLTELNKEGKTIIMVTH-EPEIADFATRKIIIRDGDIT 226
Cdd:PRK13649 161 AMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTHlMDDVANYADFVYVLEKGKLV 224
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
27-211 |
5.85e-29 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 109.16 E-value: 5.85e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 27 VLKGINLTVYEGEFLAIMGPSGSGKSTLMNIIGLL-----DRPTSGDYTLHNTKIeILNDRELAKVRNdEIGFVFQQFFL 101
Cdd:PRK14267 19 VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLlelneEARVEGEVRLFGRNI-YSPDVDPIEVRR-EVGMVFQYPNP 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 102 LAKLTALQNVELPLIYAGVNVSKRR--EQAKQFLEKVGL----GRRIKHLPSELSGGQKQRVAIARALVNDPSIILADEP 175
Cdd:PRK14267 97 FPHLTIYDNVAIGVKLNGLVKSKKEldERVEWALKKAALwdevKDRLNDYPSNLSGGQRQRLVIARALAMKPKILLMDEP 176
|
170 180 190
....*....|....*....|....*....|....*.
gi 2076047389 176 TGALDTKTGQQIMELLTELNKEgKTIIMVTHEPEIA 211
Cdd:PRK14267 177 TANIDPVGTAKIEELLFELKKE-YTIVLVTHSPAQA 211
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
4-225 |
6.24e-29 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 111.35 E-value: 6.24e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 4 EKKQLMQLSNIVKSYqnGDQVlkVLKGINLTVYEGEFLAIMGPSGSGKSTLMNIIGLLDRPTSGdytlhntkiEILNDRE 83
Cdd:PRK11432 2 TQKNFVVLKNITKRF--GSNT--VIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEG---------QIFIDGE 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 84 ---LAKVRNDEIGFVFQQFFLLAKLTALQNVELPLIYAGVNVSKRREQAKQFLEKVGLGRRIKHLPSELSGGQKQRVAIA 160
Cdd:PRK11432 69 dvtHRSIQQRDICMVFQSYALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALA 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2076047389 161 RALVNDPSIILADEPTGALDTKTGQQIMELLTELNKE-GKTIIMVTHEPEIAdFATRK--IIIRDGDI 225
Cdd:PRK11432 149 RALILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQfNITSLYVTHDQSEA-FAVSDtvIVMNKGKI 215
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
9-223 |
8.14e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 109.44 E-value: 8.14e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 9 MQLSNIVKSYQNGDqvlKVLKGINLTVYEGEFLAIMGPSGSGKSTLMNIIGLLDRPTSGDYTLHNTKIEILNDRElakVR 88
Cdd:PRK13647 5 IEVEDLHFRYKDGT---KALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKW---VR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 89 NdEIGFVFQ----QFFllaKLTALQNVELPLIYAGVNVSKRREQAKQFLEKVGLGRRIKHLPSELSGGQKQRVAIARALV 164
Cdd:PRK13647 79 S-KVGLVFQdpddQVF---SSTVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 165 NDPSIILADEPTGALDTKTGQQIMELLTELNKEGKTIIMVTHEPEIA-DFATRKIIIRDG 223
Cdd:PRK13647 155 MDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAaEWADQVIVLKEG 214
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
8-225 |
8.66e-29 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 108.86 E-value: 8.66e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 8 LMQLSNIVKSYQNGdqvlKVLKGINLTVYEGEFLAIMGPSGSGKSTLMNIIGLLDRPTSG--DYTLHNTKIEILNDRELA 85
Cdd:PRK11701 6 LLSVRGLTKLYGPR----KGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGevHYRMRDGQLRDLYALSEA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 86 KVR---NDEIGFVFQQffllakltALQNVElPLIYAGVNVSKR------------REQAKQFLEKVGLGR-RIKHLPSEL 149
Cdd:PRK11701 82 ERRrllRTEWGFVHQH--------PRDGLR-MQVSAGGNIGERlmavgarhygdiRATAGDWLERVEIDAaRIDDLPTTF 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2076047389 150 SGGQKQRVAIARALVNDPSIILADEPTGALDTKTGQQIMELLTELNKE-GKTIIMVTHEPEIAD-FATRKIIIRDGDI 225
Cdd:PRK11701 153 SGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRElGLAVVIVTHDLAVARlLAHRLLVMKQGRV 230
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
19-223 |
1.83e-28 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 106.78 E-value: 1.83e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 19 QNGDQVLKVLKGINLTVYEGEFLAIMGPSGSGKSTLMN-IIGLLDRpTSGDYTLHNTkieilndrelakvrndeIGFVFQ 97
Cdd:cd03250 12 SGEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSaLLGELEK-LSGSVSVPGS-----------------IAYVSQ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 98 QFFLLaKLTALQNvelplIYAGVNVSKRReqAKQFLEKVGLGRRIKHLP-----------SELSGGQKQRVAIARALVND 166
Cdd:cd03250 74 EPWIQ-NGTIREN-----ILFGKPFDEER--YEKVIKACALEPDLEILPdgdlteigekgINLSGGQKQRISLARAVYSD 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2076047389 167 PSIILADEPTGALDTKTGQQIME-LLTELNKEGKTIIMVTHEPEIADFATRKIIIRDG 223
Cdd:cd03250 146 ADIYLLDDPLSAVDAHVGRHIFEnCILGLLLNNKTRILVTHQLQLLPHADQIVVLDNG 203
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
10-223 |
1.85e-28 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 109.04 E-value: 1.85e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 10 QLSNIVKSYqnGDQvlKVLKGINLTVYEGEFLAIMGPSGSGKSTLMNII-GLLDrPTSGdytlhntkiEIL-NDRELAKV 87
Cdd:COG4152 3 ELKGLTKRF--GDK--TAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIIlGILA-PDSG---------EVLwDGEPLDPE 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 88 RNDEIGF------------VFQQFFLLAKLTalqnvelpliyaGVNVSKRREQAKQFLEKVGLGRRIKHLPSELSGGQKQ 155
Cdd:COG4152 69 DRRRIGYlpeerglypkmkVGEQLVYLARLK------------GLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQ 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2076047389 156 RVAIARALVNDPSIILADEPTGALDTKTGQQIMELLTELNKEGKTIIMVTHEPEIAD-FATRKIIIRDG 223
Cdd:COG4152 137 KVQLIAALLHDPELLILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQMELVEeLCDRIVIINKG 205
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
2-228 |
3.81e-28 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 106.46 E-value: 3.81e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 2 SHEKKQLMQLSNIvKSYQNGDQVLKVLKGINLTVYEGEFLAIMGPSGSGKSTLMNIIGLLDRPTSGDYTLHNTKIEILnd 81
Cdd:cd03220 13 YKGGSSSLKKLGI-LGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSLL-- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 82 relakvrndEIGFVFQqffllAKLTALQNVELPLIYAGVNVSKRREQAKQFLEKVGLGRRIkHLP-SELSGGQKQRVAIA 160
Cdd:cd03220 90 ---------GLGGGFN-----PELTGRENIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFI-DLPvKTYSSGMKARLAFA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2076047389 161 RALVNDPSIILADEPTGALDTKTGQQIMELLTELNKEGKTIIMVTHEPE-IADFATRKIIIRDGDITTD 228
Cdd:cd03220 155 IATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQGKTVILVSHDPSsIKRLCDRALVLEKGKIRFD 223
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
17-235 |
4.88e-28 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 106.78 E-value: 4.88e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 17 SYQNGDQVlkVLKGINLTVYEGEFLAIMGPSGSGKSTLMNII-GLLdRPTSGDYTLHNTKIEILNDRELAKVRndeiGFV 95
Cdd:PRK13548 9 SVRLGGRT--LLDDVSLTLRPGEVVAILGPNGAGKSTLLRALsGEL-SPDSGEVRLNGRPLADWSPAELARRR----AVL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 96 FQQFFLLAKLTALQNVELPLiYAGVNVSKRREQA-KQFLEKVGL----GRRIkhlpSELSGGQKQRVAIARALV------ 164
Cdd:PRK13548 82 PQHSSLSFPFTVEEVVAMGR-APHGLSRAEDDALvAAALAQVDLahlaGRDY----PQLSGGEQQRVQLARVLAqlwepd 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2076047389 165 NDPSIILADEPTGALDTKTGQQIMELLTEL-NKEGKTIIMVTHEPEIAD-FATRKIIIRDGDITTDTTASVVI 235
Cdd:PRK13548 157 GPPRWLLLDEPTSALDLAHQHHVLRLARQLaHERGLAVIVVLHDLNLAArYADRIVLLHQGRLVADGTPAEVL 229
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
9-235 |
5.25e-28 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 106.64 E-value: 5.25e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 9 MQL--SNIVKSYQNGdqvlKVLKGINLTVYEGEFLAIMGPSGSGKSTLMNIIGLLDRPTSGDYTLHNTKIEILNDRELAK 86
Cdd:PRK11231 1 MTLrtENLTVGYGTK----RILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLAR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 87 vrndEIGFVFQQFFLLAKLTALQNVEL---P-LIYAGVNVSKRREQAKQFLEKVGLGRRIKHLPSELSGGQKQRVAIARA 162
Cdd:PRK11231 77 ----RLALLPQHHLTPEGITVRELVAYgrsPwLSLWGRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMV 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2076047389 163 LVNDPSIILADEPTGALDTKTGQQIMELLTELNKEGKTIIMVTHEPEIAD-FATRKIIIRDGDITTDTTASVVI 235
Cdd:PRK11231 153 LAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNQASrYCDHLVVLANGHVMAQGTPEEVM 226
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
27-224 |
7.83e-28 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 110.67 E-value: 7.83e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 27 VLKGINLTVYEGEFLAIMGPSGSGKSTLMNII--------GLLDRPtsgdytlhntkieilndrelakvRNDEIGFVFQQ 98
Cdd:COG4178 378 LLEDLSLSLKPGERLLITGPSGSGKSTLLRAIaglwpygsGRIARP-----------------------AGARVLFLPQR 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 99 -FFLLAKLTALqnvelpLIYAGVNVSKRREQAKQFLEKVGLGRRIKHL------PSELSGGQKQRVAIARALVNDPSIIL 171
Cdd:COG4178 435 pYLPLGTLREA------LLYPATAEAFSDAELREALEAVGLGHLAERLdeeadwDQVLSLGEQQRLAFARLLLHKPDWLF 508
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2076047389 172 ADEPTGALDTKTGQQIMELLTELNKEGkTIIMVTHEPEIADFATRKIIIRDGD 224
Cdd:COG4178 509 LDEATSALDEENEAALYQLLREELPGT-TVISVGHRSTLAAFHDRVLELTGDG 560
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
8-234 |
1.01e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 106.74 E-value: 1.01e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 8 LMQLSNIVKSYQ-NGDQVLKVLKGINLTVYEGEFLAIMGPSGSGKSTLMNIIGLLDRPTSGDYTLHNTKIEILNDRELAK 86
Cdd:PRK13643 1 MIKFEKVNYTYQpNSPFASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKEIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 87 VRNDEIGFVFQ----QFFllaKLTALQNVELPLIYAGVNVSKRREQAKQFLEKVGLGRRI-KHLPSELSGGQKQRVAIAR 161
Cdd:PRK13643 81 PVRKKVGVVFQfpesQLF---EETVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLADEFwEKSPFELSGGQMRRVAIAG 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2076047389 162 ALVNDPSIILADEPTGALDTKTGQQIMELLTELNKEGKTIIMVTH-EPEIADFATRKIIIRDGDITTDTTASVV 234
Cdd:PRK13643 158 ILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSGQTVVLVTHlMDDVADYADYVYLLEKGHIISCGTPSDV 231
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
27-226 |
2.11e-27 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 109.45 E-value: 2.11e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 27 VLKGINLTVYEGEFLAIMGPSGSGKSTLMNII-GLLdRPTSGDYTLHNTKIEILNDRELAKVrndeIGFvfqqfflLAkl 105
Cdd:COG4618 347 ILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLvGVW-PPTAGSVRLDGADLSQWDREELGRH----IGY-------LP-- 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 106 talQNVELpliYAG-----------VNVSKRREQAKqfleKVGLGRRIKHLP-----------SELSGGQKQRVAIARAL 163
Cdd:COG4618 413 ---QDVEL---FDGtiaeniarfgdADPEKVVAAAK----LAGVHEMILRLPdgydtrigeggARLSGGQRQRIGLARAL 482
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2076047389 164 VNDPSIILADEPTGALDTKTGQQIMELLTELNKEGKTIIMVTHEPEIADFATRKIIIRDGDIT 226
Cdd:COG4618 483 YGDPRLVVLDEPNSNLDDEGEAALAAAIRALKARGATVVVITHRPSLLAAVDKLLVLRDGRVQ 545
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
8-235 |
2.96e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 105.45 E-value: 2.96e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 8 LMQLSNIVKSYQNGDqvlKVLKGINLTVYEGEFLAIMGPSGSGKSTL-MNIIGLLdRPTSGDYTLHNtkIEILNDRELAK 86
Cdd:PRK13644 1 MIRLENVSYSYPDGT---PALENINLVIKKGEYIGIIGKNGSGKSTLaLHLNGLL-RPQKGKVLVSG--IDTGDFSKLQG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 87 VRNdEIGFVFQ----QFFLLAKLTAL----QNVELPLIyagvNVSKRREQAkqfLEKVGLGRRIKHLPSELSGGQKQRVA 158
Cdd:PRK13644 75 IRK-LVGIVFQnpetQFVGRTVEEDLafgpENLCLPPI----EIRKRVDRA---LAEIGLEKYRHRSPKTLSGGQGQCVA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2076047389 159 IARALVNDPSIILADEPTGALDTKTGQQIMELLTELNKEGKTIIMVTHEPEIADFATRKIIIRDGDITTDTTASVVI 235
Cdd:PRK13644 147 LAGILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVL 223
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
8-220 |
3.16e-27 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 106.36 E-value: 3.16e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 8 LMQLSNIVKSYQNGDQVLKVLKGINLTVYEGEFLAIMGPSGSGKS-TLMNIIGLLDRP---TSGDYTLHNTKIEILNDRE 83
Cdd:PRK11022 3 LLNVDKLSVHFGDESAPFRAVDRISYSVKQGEVVGIVGESGSGKSvSSLAIMGLIDYPgrvMAEKLEFNGQDLQRISEKE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 84 LAKVRNDEIGFVFQQffllaKLTAL--------QNVELPLIYAGVNVSKRREQAKQFLEKVGL---GRRIKHLPSELSGG 152
Cdd:PRK11022 83 RRNLVGAEVAMIFQD-----PMTSLnpcytvgfQIMEAIKVHQGGNKKTRRQRAIDLLNQVGIpdpASRLDVYPHQLSGG 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2076047389 153 QKQRVAIARALVNDPSIILADEPTGALDTKTGQQIMELLTELN-KEGKTIIMVTHEPEIADFATRKIII 220
Cdd:PRK11022 158 MSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQqKENMALVLITHDLALVAEAAHKIIV 226
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
5-234 |
4.23e-27 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 108.35 E-value: 4.23e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 5 KKQLMQLSNIVKSYQNGDQ-VLKVLKGINLTVYEGEFLAIMGPSGSGKSTLMNIIGLLDRPTSGDYT--LHNTKIEILND 81
Cdd:TIGR03269 276 GEPIIKVRNVSKRYISVDRgVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNvrVGDEWVDMTKP 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 82 RELAKVRNDE-IGFVFQQFFLLAKLTALQN------VELP-------LIYAGVNVSKRREQAKQFLEKvglgrrikhLPS 147
Cdd:TIGR03269 356 GPDGRGRAKRyIGILHQEYDLYPHRTVLDNlteaigLELPdelarmkAVITLKMVGFDEEKAEEILDK---------YPD 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 148 ELSGGQKQRVAIARALVNDPSIILADEPTGALDTKTGQQIMELLTELNKE-GKTIIMVTHEPE-IADFATRKIIIRDGDI 225
Cdd:TIGR03269 427 ELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEmEQTFIIVSHDMDfVLDVCDRAALMRDGKI 506
|
250
....*....|
gi 2076047389 226 T-TDTTASVV 234
Cdd:TIGR03269 507 VkIGDPEEIV 516
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
42-227 |
5.84e-27 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 106.11 E-value: 5.84e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 42 AIMGPSGSGKSTLMNIIGLLDRPTSGdytlhntKIeILNDRELAKVRND--------EIGFVFQQffllAKLTALQNVEL 113
Cdd:PRK11144 28 AIFGRSGAGKTSLINAISGLTRPQKG-------RI-VLNGRVLFDAEKGiclppekrRIGYVFQD----ARLFPHYKVRG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 114 PLIYaGVnvskRREQAKQFLEKVG-LGrrIKHL----PSELSGGQKQRVAIARALVNDPSIILADEPTGALDTKTGQQIM 188
Cdd:PRK11144 96 NLRY-GM----AKSMVAQFDKIVAlLG--IEPLldryPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELL 168
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2076047389 189 ELLTELNKEGKT-IIMVTHE-PEIADFATRKIIIRDGDITT 227
Cdd:PRK11144 169 PYLERLAREINIpILYVSHSlDEILRLADRVVVLEQGKVKA 209
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
9-212 |
1.10e-26 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 105.30 E-value: 1.10e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 9 MQLSNIVKSYqnGDQVlkVLKGINLTVYEGEFLAIMGPSGSGKSTLMNIIGLLDRPTSGdytlhntKIEILNDRELAKVR 88
Cdd:PRK13536 42 IDLAGVSKSY--GDKA--VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAG-------KITVLGVPVPARAR 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 89 --NDEIGFVFQQFFLLAKLTALQNVELPLIYAGVNVSKRREQAKQFLEKVGLGRRIKHLPSELSGGQKQRVAIARALVND 166
Cdd:PRK13536 111 laRARIGVVPQFDNLDLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALIND 190
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2076047389 167 PSIILADEPTGALDTKTGQQIMELLTELNKEGKTIIMVTHEPEIAD 212
Cdd:PRK13536 191 PQLLILDEPTTGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAE 236
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
27-225 |
2.38e-26 |
|
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: 106.28 E-value: 2.38e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 27 VLKGINLTVYEGEFLAIMGPSGSGKSTLMNIIGLLDRPTSGDYTLHNTKIEILNDRELAKvrndEIGFVFQQffllaklt 106
Cdd:TIGR01842 333 TLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGK----HIGYLPQD-------- 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 107 alqnVELpliYAGV---NVSKRREQAKQflEKV-------GLGRRIKHLP-----------SELSGGQKQRVAIARALVN 165
Cdd:TIGR01842 401 ----VEL---FPGTvaeNIARFGENADP--EKIieaaklaGVHELILRLPdgydtvigpggATLSGGQRQRIALARALYG 471
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 166 DPSIILADEPTGALDTKTGQQIMELLTELNKEGKTIIMVTHEPEIADFATRKIIIRDGDI 225
Cdd:TIGR01842 472 DPKLVVLDEPNSNLDEEGEQALANAIKALKARGITVVVITHRPSLLGCVDKILVLQDGRI 531
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
27-210 |
4.51e-26 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 105.56 E-value: 4.51e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 27 VLKGINLTVYEGEFLAIMGPSGSGKST----LMNIIglldrPTSGDYTLHNTKIEILNDRELAKVRNdEIGFVFQQFF-- 100
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLI-----NSQGEIWFDGQPLHNLNRRQLLPVRH-RIQVVFQDPNss 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 101 LLAKLTALQNVE--LPLIYAGVNVSKRREQAKQFLEKVGLGRRIKH-LPSELSGGQKQRVAIARALVNDPSIILADEPTG 177
Cdd:PRK15134 375 LNPRLNVLQIIEegLRVHQPTLSAAQREQQVIAVMEEVGLDPETRHrYPAEFSGGQRQRIAIARALILKPSLIILDEPTS 454
|
170 180 190
....*....|....*....|....*....|....
gi 2076047389 178 ALDTKTGQQIMELLTEL-NKEGKTIIMVTHEPEI 210
Cdd:PRK15134 455 SLDKTVQAQILALLKSLqQKHQLAYLFISHDLHV 488
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
9-206 |
6.47e-26 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 101.31 E-value: 6.47e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 9 MQLSNIVKSYQNgdqvLKVLKGINLTVYEGEFLAIMGPSGSGKSTLMNIIGLLDRPTSGDYTLHNTKIEILNDRELAKVr 88
Cdd:COG4604 2 IEIKNVSKRYGG----KVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKR- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 89 ndeIGFVFQQFFLLAKLTALQNVEL---PliYagvnvSKRR---------EQAKQFLEKVGLGRRikHLpSELSGGQKQR 156
Cdd:COG4604 77 ---LAILRQENHINSRLTVRELVAFgrfP--Y-----SKGRltaedreiiDEAIAYLDLEDLADR--YL-DELSGGQRQR 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2076047389 157 VAIARALVNDPSIILADEPTGALDTKTGQQIMELLTELNKE-GKTIIMVTH 206
Cdd:COG4604 144 AFIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADElGKTVVIVLH 194
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
27-225 |
8.04e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 101.80 E-value: 8.04e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 27 VLKGINLTVYEGEFLAIMGPSGSGKSTLMNIIGLLDRPTSGDYTLHNTKIEILNDRELAKVRnDEIGFVFQ----QFfll 102
Cdd:PRK13640 22 ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPNSKITVDGITLTAKTVWDIR-EKVGIVFQnpdnQF--- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 103 AKLTALQNVELPLIYAGVNVSKRREQAKQFLEKVGLGRRIKHLPSELSGGQKQRVAIARALVNDPSIILADEPTGALDTK 182
Cdd:PRK13640 98 VGATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPA 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2076047389 183 TGQQIMELLTELNKE-GKTIIMVTHEPEIADFATRKIIIRDGDI 225
Cdd:PRK13640 178 GKEQILKLIRKLKKKnNLTVISITHDIDEANMADQVLVLDDGKL 221
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
26-225 |
9.87e-26 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 104.80 E-value: 9.87e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 26 KVLKGINLTVYEGEFLAIMGPSGSGKSTLMNIIGLLDRPTSGDYTLHNTKIEilnDRELAKVRNdEIGFVFQQFFLLAKl 105
Cdd:TIGR02203 346 PALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLA---DYTLASLRR-QVALVSQDVVLFND- 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 106 TALQNVElpliYAGVNVSKRRE--------QAKQFLEKV--GLGRRIKHLPSELSGGQKQRVAIARALVNDPSIILADEP 175
Cdd:TIGR02203 421 TIANNIA----YGRTEQADRAEieralaaaYAQDFVDKLplGLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEA 496
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2076047389 176 TGALDTKTGQQIMELLTELnKEGKTIIMVTHEPEIADFATRKIIIRDGDI 225
Cdd:TIGR02203 497 TSALDNESERLVQAALERL-MQGRTTLVIAHRLSTIEKADRIVVMDDGRI 545
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
26-206 |
1.04e-25 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 100.62 E-value: 1.04e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 26 KVLKGINLTVYEGEFLAIMGPSGSGKSTLMNIIGLLD--RPT-----SGDYTLHNTKIEILNDRELAKvrndEIGFVFQQ 98
Cdd:PRK14239 19 KALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNdlNPEvtitgSIVYNGHNIYSPRTDTVDLRK----EIGMVFQQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 99 ---FfllaKLTALQNVELPLIYAGVnvsKRREQAKQFLEKVGLGRRI-----KHLPSE---LSGGQKQRVAIARALVNDP 167
Cdd:PRK14239 95 pnpF----PMSIYENVVYGLRLKGI---KDKQVLDEAVEKSLKGASIwdevkDRLHDSalgLSGGQQQRVCIARVLATSP 167
|
170 180 190
....*....|....*....|....*....|....*....
gi 2076047389 168 SIILADEPTGALDTKTGQQIMELLTELnKEGKTIIMVTH 206
Cdd:PRK14239 168 KIILLDEPTSALDPISAGKIEETLLGL-KDDYTMLLVTR 205
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
27-213 |
1.22e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 100.51 E-value: 1.22e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 27 VLKGINLTVYEGEFLAIMGPSGSGKSTLMNIIGLLdrptsgdYTLHNTKIEI----------LNDRELAKVRNdEIGFVF 96
Cdd:PRK14246 25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRL-------IEIYDSKIKVdgkvlyfgkdIFQIDAIKLRK-EVGMVF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 97 QQFFLLAKLTALQNVELPLIYAGVNvsKRREQAK---QFLEKVGLGR----RIKHLPSELSGGQKQRVAIARALVNDPSI 169
Cdd:PRK14246 97 QQPNPFPHLSIYDNIAYPLKSHGIK--EKREIKKiveECLRKVGLWKevydRLNSPASQLSGGQQQRLTIARALALKPKV 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2076047389 170 ILADEPTGALDTKTGQQIMELLTELNKEgKTIIMVTHEPE----IADF 213
Cdd:PRK14246 175 LLMDEPTSMIDIVNSQAIEKLITELKNE-IAIVIVSHNPQqvarVADY 221
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
30-218 |
2.01e-25 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 98.72 E-value: 2.01e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 30 GINLTVYEGEFLAIMGPSGSGKSTLMNIIGLLDRPTSGdytlhntkiEIL-NDRELAKVRNDeigfvFQQ--FFL--LA- 103
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAG---------EVLwQGEPIRRQRDE-----YHQdlLYLghQPg 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 104 ---KLTALQNVelpLIYAGVNVSKRREQAKQFLEKVGLGRRiKHLP-SELSGGQKQRVAIARALVNDPSIILADEPTGAL 179
Cdd:PRK13538 85 iktELTALENL---RFYQRLHGPGDDEALWEALAQVGLAGF-EDVPvRQLSAGQQRRVALARLWLTRAPLWILDEPFTAI 160
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2076047389 180 DTKTGQQIMELLTELNKEGKTIIMVTHEP-EIADFATRKI 218
Cdd:PRK13538 161 DKQGVARLEALLAQHAEQGGMVILTTHQDlPVASDKVRKL 200
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
27-225 |
2.27e-25 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 104.03 E-value: 2.27e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 27 VLKGINLTVYEGEFLAIMGPSGSGKSTlmnIIGLLDR---PTSGDYTLHNTKIEILNDRELAKvrndEIGFVFQQFFLLA 103
Cdd:TIGR00958 496 VLKGLTFTLHPGEVVALVGPSGSGKST---VAALLQNlyqPTGGQVLLDGVPLVQYDHHYLHR----QVALVGQEPVLFS 568
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 104 KlTALQNVELPLIY---AGVNVSKRREQAKQFLEKV--GLGRRIKHLPSELSGGQKQRVAIARALVNDPSIILADEPTGA 178
Cdd:TIGR00958 569 G-SVRENIAYGLTDtpdEEIMAAAKAANAHDFIMEFpnGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSA 647
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2076047389 179 LDTktgqQIMELLTELNK-EGKTIIMVTHEPEIADFATRKIIIRDGDI 225
Cdd:TIGR00958 648 LDA----ECEQLLQESRSrASRTVLLIAHRLSTVERADQILVLKKGSV 691
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
26-206 |
2.28e-25 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 103.77 E-value: 2.28e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 26 KVLKG-INLTVYEGEFLAIMGPSGSGKSTLMN-IIGLLdrPTSGDYTLHNtkIEiLNDRELAKVRNdEIGFVFQQFFLLA 103
Cdd:PRK11174 363 KTLAGpLNFTLPAGQRIALVGPSGAGKTSLLNaLLGFL--PYQGSLKING--IE-LRELDPESWRK-HLSWVGQNPQLPH 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 104 KlTALQNVELPLIYAG---VNVSKRREQAKQFLEKV--GLGRRIKHLPSELSGGQKQRVAIARALVNDPSIILADEPTGA 178
Cdd:PRK11174 437 G-TLRDNVLLGNPDASdeqLQQALENAWVSEFLPLLpqGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTAS 515
|
170 180
....*....|....*....|....*...
gi 2076047389 179 LDTKTGQQIMELLTElNKEGKTIIMVTH 206
Cdd:PRK11174 516 LDAHSEQLVMQALNA-ASRRQTTLMVTH 542
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
11-206 |
2.41e-25 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 103.22 E-value: 2.41e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 11 LSNIVKSYqnGDQVLkvLKGINLTVYEGEFLAIMGPSGSGKSTLMNIIGLLDRPTSGDYTLHntkieilndrelakvRND 90
Cdd:COG0488 1 LENLSKSF--GGRPL--LDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIP---------------KGL 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 91 EIGFVFQQFFLLAKLTALQNV------------ELPLIYAGVNVSKRRE--------------------QAKQFLEKVGL 138
Cdd:COG0488 62 RIGYLPQEPPLDDDLTVLDTVldgdaelraleaELEELEAKLAEPDEDLerlaelqeefealggweaeaRAEEILSGLGF 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2076047389 139 GRRIKHLP-SELSGGQKQRVAIARALVNDPSIILADEPTGALDTKTgqqIMELLTELNKEGKTIIMVTH 206
Cdd:COG0488 142 PEEDLDRPvSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLES---IEWLEEFLKNYPGTVLVVSH 207
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
9-206 |
2.82e-25 |
|
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 represents the family of all lantibiotics related to gallidermin, including epidermin, mutatin, and nisin. This protein family describes the ATP-binding subunit of a gallidermin/epidermin class lantibiotic protection transporter. It is largely restricted to gallidermin-family lantibiotic biosynthesis and export cassettes, but also occurs in orphan transporter cassettes in species that lack candidate lantibiotic precursor and synthetase genes.
Pssm-ID: 163452 [Multi-domain] Cd Length: 223 Bit Score: 99.01 E-value: 2.82e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 9 MQLSNIVKSYQNGDqvlkVLKGINLTVYEGEFLAIMGPSGSGKSTLMNIIGLLDRPTSGDYtlhntkieILNDRELAKVR 88
Cdd:TIGR03740 1 LETKNLSKRFGKQT----AVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEI--------IFDGHPWTRKD 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 89 NDEIGFVFQQFFLLAKLTALQNVELPLIYAGVNVSKRREqakqFLEKVGLGRRIKHLPSELSGGQKQRVAIARALVNDPS 168
Cdd:TIGR03740 69 LHKIGSLIESPPLYENLTARENLKVHTTLLGLPDSRIDE----VLNIVDLTNTGKKKAKQFSLGMKQRLGIAIALLNHPK 144
|
170 180 190
....*....|....*....|....*....|....*...
gi 2076047389 169 IILADEPTGALDTKTGQQIMELLTELNKEGKTIIMVTH 206
Cdd:TIGR03740 145 LLILDEPTNGLDPIGIQELRELIRSFPEQGITVILSSH 182
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
26-225 |
3.10e-25 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 97.98 E-value: 3.10e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 26 KVLKGINLTVYEGEFLAIMGPSGSGKSTLMNII-GLLD-RPTSGDYTLHNTKIEILNDRELAKVrndEIGFVFQQfflla 103
Cdd:cd03217 14 EILKGVNLTIKKGEVHALMGPNGSGKSTLAKTImGHPKyEVTEGEILFKGEDITDLPPEERARL---GIFLAFQY----- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 104 kltalqnvelPLIYAGVNVskrreqaKQFLEKVGLGrrikhlpseLSGGQKQRVAIARALVNDPSIILADEPTGALDTKT 183
Cdd:cd03217 86 ----------PPEIPGVKN-------ADFLRYVNEG---------FSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDA 139
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2076047389 184 GQQIMELLTELNKEGKTIIMVTHEPEIADF--ATRKIIIRDGDI 225
Cdd:cd03217 140 LRLVAEVINKLREEGKSVLIITHYQRLLDYikPDRVHVLYDGRI 183
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
21-225 |
3.16e-25 |
|
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: 97.50 E-value: 3.16e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 21 GDQVLKV--------LKGINLTVYEGEFLAIMGPSGSGKSTLMNIIGLLDRPTSGDYTLHNTKIEILNDRELakvRNDEI 92
Cdd:cd03215 1 GEPVLEVrglsvkgaVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDA---IRAGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 93 GFV---FQQFFLLAKLTALQNVELPLIyagvnvskrreqakqflekvglgrrikhlpseLSGGQKQRVAIARALVNDPSI 169
Cdd:cd03215 78 AYVpedRKREGLVLDLSVAENIALSSL--------------------------------LSGGNQQKVVLARWLARDPRV 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2076047389 170 ILADEPTGALDTKTGQQIMELLTELNKEGKTIIMVTHE-PEIADFATRKIIIRDGDI 225
Cdd:cd03215 126 LILDEPTRGVDVGAKAEIYRLIRELADAGKAVLLISSElDELLGLCDRILVMYEGRI 182
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
11-228 |
3.18e-25 |
|
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: 98.94 E-value: 3.18e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 11 LSNIVKSYQNGDQVLKV-LKGINLTVYEGEFLAIMGPSGSGKSTLMNIIGLLDRPTSGDYTLHNtkiEILNDRELAKVRN 89
Cdd:cd03267 19 LIGSLKSLFKRKYREVEaLKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAG---LVPWKRRKKFLRR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 90 deIGFVFQQFFLLA-KLTALQNVEL-PLIYaGVNVSKRREQAKQFLEKVGLGRRIKHLPSELSGGQKQRVAIARALVNDP 167
Cdd:cd03267 96 --IGVVFGQKTQLWwDLPVIDSFYLlAAIY-DLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEP 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2076047389 168 SIILADEPTGALDTKTGQQIMELLTELNKE-GKTIIMVTHE-PEIADFATRKIIIRDGDITTD 228
Cdd:cd03267 173 EILFLDEPTIGLDVVAQENIRNFLKEYNRErGTTVLLTSHYmKDIEALARRVLVIDKGRLLYD 235
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
6-231 |
4.73e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 99.42 E-value: 4.73e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 6 KQLMQLSNIVKSYQNgDQVLKVLKGINLTVYEGEFLAIMGPSGSGKSTLMNIIGLLDRPTSGDYTLHNTKIEILNDRELa 85
Cdd:PRK13650 2 SNIIEVKNLTFKYKE-DQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDI- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 86 kvrNDEIGFVFQ----QFfllAKLTALQNVELPLIYAGVNVSKRREQAKQFLEKVGLGRRIKHLPSELSGGQKQRVAIAR 161
Cdd:PRK13650 80 ---RHKIGMVFQnpdnQF---VGATVEDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2076047389 162 ALVNDPSIILADEPTGALDTKTGQQIMELLTELNKE-GKTIIMVTHEPEIADFATRKIIIRDGDITTDTTA 231
Cdd:PRK13650 154 AVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDyQMTVISITHDLDEVALSDRVLVMKNGQVESTSTP 224
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
8-223 |
4.94e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 99.54 E-value: 4.94e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 8 LMQLSNIVKSYQNGDQVLKvlkGINLTVYEGEFLAIMGPSGSGKSTLMNIIGLLDRPTSGDYTLHNTKIEiLNDRELAKV 87
Cdd:PRK13636 5 ILKVEELNYNYSDGTHALK---GININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPID-YSRKGLMKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 88 RNDeIGFVFQ----QFFllaKLTALQNVELPLIYAGVNVSKRREQAKQFLEKVGLGRrIKHLPSE-LSGGQKQRVAIARA 162
Cdd:PRK13636 81 RES-VGMVFQdpdnQLF---SASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEH-LKDKPTHcLSFGQKKRVAIAGV 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2076047389 163 LVNDPSIILADEPTGALDTKTGQQIMELLTELNKE-GKTIIMVTHEPEI-ADFATRKIIIRDG 223
Cdd:PRK13636 156 LVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKElGLTIIIATHDIDIvPLYCDNVFVMKEG 218
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
14-236 |
5.58e-25 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 98.62 E-value: 5.58e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 14 IVKSYQNGDQVLKVLKGINLTVYEGEFLAIMGPSGSGKSTLMNIIGLLDRPTSGDYTLHNTKIEILndrelakvrndEIG 93
Cdd:COG1134 28 LLRRRRTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRVSALL-----------ELG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 94 FVFQqffllAKLTALQNVELP-LIYaGVNvskrREQAKQFLEKV----GLGRRIkHLP-SELSGGQKQRVAIARALVNDP 167
Cdd:COG1134 97 AGFH-----PELTGRENIYLNgRLL-GLS----RKEIDEKFDEIvefaELGDFI-DQPvKTYSSGMRARLAFAVATAVDP 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 168 SIILADEPTGALDTKTGQQIMELLTELNKEGKTIIMVTHEPE-IADFATRKIIIRDGDITTDTTASVVID 236
Cdd:COG1134 166 DILLVDEVLAVGDAAFQKKCLARIRELRESGRTVIFVSHSMGaVRRLCDRAIWLEKGRLVMDGDPEEVIA 235
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
9-236 |
7.34e-25 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 102.51 E-value: 7.34e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 9 MQLSNIVKSYQNGDqvlKVLKGINLTVYEGEFLAIMGPSGSGKSTLMNIIGLLDRPTSGDYTLHNTKIEILNDRELAKVr 88
Cdd:TIGR01193 474 IVINDVSYSYGYGS---NILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQF- 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 89 ndeIGFVFQQFFLLAK-------LTALQNVELPLIYAGVNVSKRREQAKQFleKVGLGRRIKHLPSELSGGQKQRVAIAR 161
Cdd:TIGR01193 550 ---INYLPQEPYIFSGsilenllLGAKENVSQDEIWAACEIAEIKDDIENM--PLGYQTELSEEGSSISGGQKQRIALAR 624
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2076047389 162 ALVNDPSIILADEPTGALDTKTGQQIMELLTELNKegKTIIMVTHEPEIADFATRKIIIRDGDITTDTTASVVID 236
Cdd:TIGR01193 625 ALLTDSKVLILDESTSNLDTITEKKIVNNLLNLQD--KTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDELLD 697
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
27-218 |
8.75e-25 |
|
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: 97.18 E-value: 8.75e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 27 VLKGINLTVYEGEFLAIMGPSGSGKSTLMNIIGLLDRPTSGDYTLHNTKIEILNDrELAKvrndEIGFVFQQFFLLAKLT 106
Cdd:cd03231 15 LFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRD-SIAR----GLLYLGHAPGIKTTLS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 107 ALQNVELpliYAGVNvskRREQAKQFLEKVGLGRrIKHLP-SELSGGQKQRVAIARALVNDPSIILADEPTGALDTKTGQ 185
Cdd:cd03231 90 VLENLRF---WHADH---SDEQVEEALARVGLNG-FEDRPvAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVA 162
|
170 180 190
....*....|....*....|....*....|....
gi 2076047389 186 QIMELLTELNKEGKTIIMVTHEP-EIADFATRKI 218
Cdd:cd03231 163 RFAEAMAGHCARGGMVVLTTHQDlGLSEAGAREL 196
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
17-225 |
1.63e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 97.90 E-value: 1.63e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 17 SYQ-NGDQVLkVLKGINLTVYEGEFLAIMGPSGSGKSTLMNIIGLLDRPTSGDYTLHNTKIeilNDRELAKVRNDeIGFV 95
Cdd:PRK13648 14 SFQyQSDASF-TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAI---TDDNFEKLRKH-IGIV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 96 FQ----QFfllAKLTALQNVELPLIYAGVNVSKRREQAKQFLEKVGLGRRIKHLPSELSGGQKQRVAIARALVNDPSIIL 171
Cdd:PRK13648 89 FQnpdnQF---VGSIVKYDVAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVII 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2076047389 172 ADEPTGALDTKTGQQIMELLTELNKEGK-TIIMVTHEPEIADFATRKIIIRDGDI 225
Cdd:PRK13648 166 LDEATSMLDPDARQNLLDLVRKVKSEHNiTIISITHDLSEAMEADHVIVMNKGTV 220
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
26-226 |
1.77e-24 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 100.86 E-value: 1.77e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 26 KVLKGINLTVYEGEFLAIMGPSGSGKSTLMN-IIGLlDRPTSGDYTLHNTKIEILNDRElAkVRNdeiGFVF-----QQF 99
Cdd:COG1129 266 GVVRDVSFSVRAGEILGIAGLVGAGRTELARaLFGA-DPADSGEIRLDGKPVRIRSPRD-A-IRA---GIAYvpedrKGE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 100 FLLAKLTALQNVELPLI----YAGVnVSKRREQ--AKQFLEKVGL-GRRIKHLPSELSGGQKQRVAIARALVNDPSIILA 172
Cdd:COG1129 340 GLVLDLSIRENITLASLdrlsRGGL-LDRRRERalAEEYIKRLRIkTPSPEQPVGNLSGGNQQKVVLAKWLATDPKVLIL 418
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2076047389 173 DEPTGALDTKTGQQIMELLTELNKEGKTIIMVTHE-PEIADFATRKIIIRDGDIT 226
Cdd:COG1129 419 DEPTRGIDVGAKAEIYRLIRELAAEGKAVIVISSElPELLGLSDRILVMREGRIV 473
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
9-212 |
2.07e-24 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 98.34 E-value: 2.07e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 9 MQLSNIVKSYqnGDQVlkVLKGINLTVYEGEFLAIMGPSGSGKSTLMNIIGLLDRPTSGDYTLHNTKIEilndrELAKVR 88
Cdd:PRK13537 8 IDFRNVEKRY--GDKL--VVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVP-----SRARHA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 89 NDEIGFVFQQFFLLAKLTALQNVELPLIYAGVNVSKRREQAKQFLEKVGLGRRIKHLPSELSGGQKQRVAIARALVNDPS 168
Cdd:PRK13537 79 RQRVGVVPQFDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPD 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2076047389 169 IILADEPTGALDTKTGQQIMELLTELNKEGKTIIMVTHEPEIAD 212
Cdd:PRK13537 159 VLVLDEPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAE 202
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
25-225 |
2.08e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 98.16 E-value: 2.08e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 25 LKVLKGINLTVYEGEFLAIMGPSGSGKSTLMNII-GLLDRPTS----GDYTLHNTKIEIlndRELAKVRNdEIGFVFQ-Q 98
Cdd:PRK13645 24 FKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTnGLIISETGqtivGDYAIPANLKKI---KEVKRLRK-EIGLVFQfP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 99 FFLLAKLTALQNVELPLIYAGVNVSKRREQAKQFLEKVGLGRR-IKHLPSELSGGQKQRVAIARALVNDPSIILADEPTG 177
Cdd:PRK13645 100 EYQLFQETIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLPEDyVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTG 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2076047389 178 ALDTKTGQQIMELLTELNKE-GKTIIMVTHE-PEIADFATRKIIIRDGDI 225
Cdd:PRK13645 180 GLDPKGEEDFINLFERLNKEyKKRIIMVTHNmDQVLRIADEVIVMHEGKV 229
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
8-223 |
2.83e-24 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 100.08 E-value: 2.83e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 8 LMQLSNIVKSYQNgdqvLKVLKGINLTVYEGEFLAIMGPSGSGKSTLMNIIglldrptSGDYTLHNTKIEILNDRELAKV 87
Cdd:PRK10762 4 LLQLKGIDKAFPG----VKALSGAALNVYPGRVMALVGENGAGKSTMMKVL-------TGIYTRDAGSILYLGKEVTFNG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 88 RNDE----IGFVFQQFFLLAKLTALQNV----ELPLIYAGVNVSKRREQAKQFLEKVGLGRRIKHLPSELSGGQKQRVAI 159
Cdd:PRK10762 73 PKSSqeagIGIIHQELNLIPQLTIAENIflgrEFVNRFGRIDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEI 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2076047389 160 ARALVNDPSIILADEPTGAL-DTKTgQQIMELLTELNKEGKTIIMVTHE-PEIADFATRKIIIRDG 223
Cdd:PRK10762 153 AKVLSFESKVIIMDEPTDALtDTET-ESLFRVIRELKSQGRGIVYISHRlKEIFEICDDVTVFRDG 217
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
6-225 |
4.55e-24 |
|
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: 95.62 E-value: 4.55e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 6 KQLMQLSNIVKSYQNGDQVLkVLKGINLTVYEGEFLAIMGPSGSGKSTLMNIIGLLDRPTSGDYTLHNTKIEILNDRELA 85
Cdd:cd03248 9 KGIVKFQNVTFAYPTRPDTL-VLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLH 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 86 KVrndeIGFVFQQFFLLAKLTA------LQNVELPLIYAGVNVSkrreQAKQFLEKVGLG--RRIKHLPSELSGGQKQRV 157
Cdd:cd03248 88 SK----VSLVGQEPVLFARSLQdniaygLQSCSFECVKEAAQKA----HAHSFISELASGydTEVGEKGSQLSGGQKQRV 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2076047389 158 AIARALVNDPSIILADEPTGALDTKTGQQIMELLTELNkEGKTIIMVTHEPEIADFATRKIIIRDGDI 225
Cdd:cd03248 160 AIARALIRNPQVLILDEATSALDAESEQQVQQALYDWP-ERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
9-211 |
6.41e-24 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 98.38 E-value: 6.41e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 9 MQLSNIVKSYqnGDQvlKVLKGINLTVYEGEFLAIMGPSGSGKSTLMNIIGLLDRPTSGDYTLHNTKIEILNDRELAKvr 88
Cdd:PRK09536 4 IDVSDLSVEF--GDT--TVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASR-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 89 ndEIGFVFQQFFLLAKLTALQNVEL---PLI--YAGVNVSKRR--EQAkqfLEKVGLGRRIKHLPSELSGGQKQRVAIAR 161
Cdd:PRK09536 78 --RVASVPQDTSLSFEFDVRQVVEMgrtPHRsrFDTWTETDRAavERA---MERTGVAQFADRPVTSLSGGERQRVLLAR 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2076047389 162 ALVNDPSIILADEPTGALDTKTGQQIMELLTELNKEGKTIIMVTHEPEIA 211
Cdd:PRK09536 153 ALAQATPVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLA 202
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
27-208 |
7.16e-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: 94.35 E-value: 7.16e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 27 VLKGINLTVYEGEFLAIMGPSGSGKSTLMNIIGLLDRPTSGDYtlhntkieILNDRELAKVRN---DEIGFVFQQFFLLA 103
Cdd:TIGR01189 15 LFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEV--------RWNGTPLAEQRDephENILYLGHLPGLKP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 104 KLTALQNVELpliYAGVNVSKRREqAKQFLEKVGLgRRIKHLP-SELSGGQKQRVAIARALVNDPSIILADEPTGALDTK 182
Cdd:TIGR01189 87 ELSALENLHF---WAAIHGGAQRT-IEDALAAVGL-TGFEDLPaAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKA 161
|
170 180
....*....|....*....|....*.
gi 2076047389 183 TGQQIMELLTELNKEGKTIIMVTHEP 208
Cdd:TIGR01189 162 GVALLAGLLRAHLARGGIVLLTTHQD 187
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
10-175 |
9.02e-24 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 95.10 E-value: 9.02e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 10 QLSNIVKSYQNgdqvLKVLKGINLTVYEGEFLAIMGPSGSGKSTLMNII-GLLdRPTSGdytlhntKIeILNDRELAKVR 88
Cdd:COG1137 5 EAENLVKSYGK----RTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIvGLV-KPDSG-------RI-FLDGEDITHLP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 89 NDE-----IGFVFQQFFLLAKLTALQNVELPLIYAGVNVSKRREQAKQFLEKVGLGRRIKHLPSELSGGQKQRVAIARAL 163
Cdd:COG1137 72 MHKrarlgIGYLPQEASIFRKLTVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARAL 151
|
170
....*....|..
gi 2076047389 164 VNDPSIILADEP 175
Cdd:COG1137 152 ATNPKFILLDEP 163
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
27-228 |
9.80e-24 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 95.82 E-value: 9.80e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 27 VLKGINLTVYEGEFLAIMGPSGSGKSTLMNIIGLLDRPTSGDYTLHNTKIEILNDRELAKvrndEIGFVFQQFFLLAKLT 106
Cdd:PRK10253 22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVAR----RIGLLAQNATTPGDIT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 107 ALQNV------ELPLIyagvnvSKRREQAKQFLEKVGLGRRIKHLPSE----LSGGQKQRVAIARALVNDPSIILADEPT 176
Cdd:PRK10253 98 VQELVargrypHQPLF------TRWRKEDEEAVTKAMQATGITHLADQsvdtLSGGQRQRAWIAMVLAQETAIMLLDEPT 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2076047389 177 GALDTKTGQQIMELLTELNKE-GKTIIMVTHEPEIA-DFATRKIIIRDGDITTD 228
Cdd:PRK10253 172 TWLDISHQIDLLELLSELNREkGYTLAAVLHDLNQAcRYASHLIALREGKIVAQ 225
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
8-205 |
2.15e-23 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 94.86 E-value: 2.15e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 8 LMQLSNIVKS--YQNG---DQVLKVLKGINLTVYEGEFLAIMGPSGSGKSTLMNIIGLLDRPTSGDYtlhntkieILNDR 82
Cdd:PRK15112 4 LLEVRNLSKTfrYRTGwfrRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGEL--------LIDDH 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 83 ELA----KVRNDEIGFVFQQffllaKLTAL-------QNVELPLIY-AGVNVSKRREQAKQFLEKVGLGR-RIKHLPSEL 149
Cdd:PRK15112 76 PLHfgdySYRSQRIRMIFQD-----PSTSLnprqrisQILDFPLRLnTDLEPEQREKQIIETLRQVGLLPdHASYYPHML 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2076047389 150 SGGQKQRVAIARALVNDPSIILADEPTGALDTKTGQQIMELLTELN-KEGKTIIMVT 205
Cdd:PRK15112 151 APGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQeKQGISYIYVT 207
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
27-208 |
2.24e-23 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 93.40 E-value: 2.24e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 27 VLKGINLTVYEGEFLAIMGPSGSGKSTLMNIIGLLDRPTSGDYTLHNTKIEILNDRELakvrndeIGFVFQQFFLLAKLT 106
Cdd:PRK13539 17 LFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEA-------CHYLGHRNAMKPALT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 107 ALQNVELpliYAGVNvSKRREQAKQFLEKVGLGRrIKHLP-SELSGGQKQRVAIARALVNDPSIILADEPTGALDTKTGQ 185
Cdd:PRK13539 90 VAENLEF---WAAFL-GGEELDIAAALEAVGLAP-LAHLPfGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVA 164
|
170 180
....*....|....*....|...
gi 2076047389 186 QIMELLTELNKEGKTIIMVTHEP 208
Cdd:PRK13539 165 LFAELIRAHLAQGGIVIAATHIP 187
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
27-236 |
2.33e-23 |
|
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: 94.09 E-value: 2.33e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 27 VLKGINLTVYEGEFLAIMGPSGSGKSTLMNIIGLLDRPTSGDYTLHNTKIEILNDRELAKvrndEIGFVFQQFFLLAKLT 106
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRR----QVGVVLQENVLFNRSI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 107 ----ALQNVELPL---IYAGvnvskRREQAKQFLEKV--GLGRRIKHLPSELSGGQKQRVAIARALVNDPSIILADEPTG 177
Cdd:cd03252 93 rdniALADPGMSMervIEAA-----KLAGAHDFISELpeGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATS 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2076047389 178 ALDTKTGQQIMELLTELNKeGKTIIMVTHEPEIADFATRKIIIRDGDITTDTTASVVID 236
Cdd:cd03252 168 ALDYESEHAIMRNMHDICA-GRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLA 225
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
6-226 |
3.11e-23 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 97.44 E-value: 3.11e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 6 KQLMQLSNIVKSYqnGDQVlkVLKGINLTVYEGEFLAIMGPSGSGKSTLMNII-GLLdRPTSGDYTL-HNTKieilndre 83
Cdd:COG0488 313 KKVLELEGLSKSY--GDKT--LLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLaGEL-EPDSGTVKLgETVK-------- 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 84 lakvrndeIGFVFQ-QFFLLAKLTALQNVelpliyAGVNVSKRREQAKQFLEKVGL-GRRIKHLPSELSGGQKQRVAIAR 161
Cdd:COG0488 380 --------IGYFDQhQEELDPDKTVLDEL------RDGAPGGTEQEVRGYLGRFLFsGDDAFKPVGVLSGGEKARLALAK 445
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2076047389 162 ALVNDPSIILADEPTGALDTKTGQQIMELLTELnkEGkTIIMVTHEPEIAD-FATRKIIIRDGDIT 226
Cdd:COG0488 446 LLLSPPNVLLLDEPTNHLDIETLEALEEALDDF--PG-TVLLVSHDRYFLDrVATRILEFEDGGVR 508
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
9-223 |
3.59e-23 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 96.90 E-value: 3.59e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 9 MQLSNIVKSYQNgdqvLKVLKGINLTVYEGEFLAIMGPSGSGKSTLMNIIGLLDRPTSGDYTLHNTKIEILNDRElakVR 88
Cdd:PRK11288 5 LSFDGIGKTFPG----VKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTA---AL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 89 NDEIGFVFQQFFLLAKLTALQNV---ELPLIYAGVNVSKRREQAKQFLEKVGL----GRRIKHLpselSGGQKQRVAIAR 161
Cdd:PRK11288 78 AAGVAIIYQELHLVPEMTVAENLylgQLPHKGGIVNRRLLNYEAREQLEHLGVdidpDTPLKYL----SIGQRQMVEIAK 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2076047389 162 ALVNDPSIILADEPTGALDTKTGQQIMELLTELNKEGKTIIMVTHE-PEIADFATRKIIIRDG 223
Cdd:PRK11288 154 ALARNARVIAFDEPTSSLSAREIEQLFRVIRELRAEGRVILYVSHRmEEIFALCDAITVFKDG 216
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
25-207 |
4.63e-23 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 94.97 E-value: 4.63e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 25 LKVLKGINLTVYEGEFLAIMGPSGSGKSTLMN-IIGLLD---RPTSGDYTLHNTKIEILNDRELAKVRNDEIGFVFQQff 100
Cdd:COG4170 20 VKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKaICGITKdnwHVTADRFRWNGIDLLKLSPRERRKIIGREIAMIFQE-- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 101 LLAKLTALQNVELPLIYAGVNVS----------KRREQAKQFLEKVGLG--RRI-KHLPSELSGGQKQRVAIARALVNDP 167
Cdd:COG4170 98 PSSCLDPSAKIGDQLIEAIPSWTfkgkwwqrfkWRKKRAIELLHRVGIKdhKDImNSYPHELTEGECQKVMIAMAIANQP 177
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2076047389 168 SIILADEPTGALDTKTGQQIMELLTELNK-EGKTIIMVTHE 207
Cdd:COG4170 178 RLLIADEPTNAMESTTQAQIFRLLARLNQlQGTSILLISHD 218
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
26-216 |
5.32e-23 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 93.26 E-value: 5.32e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 26 KVLKGINLTVYEGEFLAIMGPSGSGKSTLMNIIGLLDRPTSGDYTLHNTKIEILNDRELAKVRndeIGFVFQQFFLLAKL 105
Cdd:COG4674 24 KALNDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTRPDSGSVLFGGTDLTGLDEHEIARLG---IGRKFQKPTVFEEL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 106 TALQNVELPLIyAGVNV---------SKRREQAKQFLEKVGLGRRIKHLPSELSGGQKQRVAIARALVNDPSIILADEPT 176
Cdd:COG4674 101 TVFENLELALK-GDRGVfaslfarltAEERDRIEEVLETIGLTDKADRLAGLLSHGQKQWLEIGMLLAQDPKLLLLDEPV 179
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2076047389 177 -GALDTKTgQQIMELLTELNKEgKTIIMVTHEPE-IADFATR 216
Cdd:COG4674 180 aGMTDAET-ERTAELLKSLAGK-HSVVVVEHDMEfVRQIARK 219
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
4-207 |
1.08e-22 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 92.08 E-value: 1.08e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 4 EKKQLMQLSNIvkSYQNGDQvlKVLKGINLTVYEGEFLAIMGPSGSGKSTLMNIIGLLDRPTSGDYTLHNTKIEILNDRE 83
Cdd:PRK10247 3 ENSPLLQLQNV--GYLAGDA--KILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 84 LAKvrndEIGFVFQQFFLLAKlTALQNVELPLiyagvNVSKRREQAKQF---LEKVGLGRRIKHLP-SELSGGQKQRVAI 159
Cdd:PRK10247 79 YRQ----QVSYCAQTPTLFGD-TVYDNLIFPW-----QIRNQQPDPAIFlddLERFALPDTILTKNiAELSGGEKQRISL 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2076047389 160 ARALVNDPSIILADEPTGALDTKTGQQIMELLTELNKE-GKTIIMVTHE 207
Cdd:PRK10247 149 IRNLQFMPKVLLLDEITSALDESNKHNVNEIIHRYVREqNIAVLWVTHD 197
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
30-207 |
2.16e-22 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 91.98 E-value: 2.16e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 30 GINLTVYEGEFLAIMGPSGSGKSTLMNIIGLLDRPTSGDYTLHNTKIEILNDRELAK---VRndeigfVFQQFFLLAKLT 106
Cdd:PRK11300 23 NVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIARmgvVR------TFQHVRLFREMT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 107 ALQN--------VELPLIyAGV--NVSKRR------EQAKQFLEKVGLGRRIKHLPSELSGGQKQRVAIARALVNDPSII 170
Cdd:PRK11300 97 VIENllvaqhqqLKTGLF-SGLlkTPAFRRaesealDRAATWLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEIL 175
|
170 180 190
....*....|....*....|....*....|....*...
gi 2076047389 171 LADEPTGALDTKTGQQIMELLTELNKE-GKTIIMVTHE 207
Cdd:PRK11300 176 MLDEPAAGLNPKETKELDELIAELRNEhNVTVLLIEHD 213
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
27-220 |
3.71e-22 |
|
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: 89.14 E-value: 3.71e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 27 VLKGINLTVYEGEFLAIMGPSGSGKSTLMNIIGlldrptsGDYTLHNTKIEILNDRELAkvrndeigFVFQQffllaklt 106
Cdd:cd03223 16 LLKDLSFEIKPGDRLLITGPSGTGKSSLFRALA-------GLWPWGSGRIGMPEGEDLL--------FLPQR-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 107 alqnvelPLIYAGVnvskRREQAkqflekvglgrrIKHLPSELSGGQKQRVAIARALVNDPSIILADEPTGALDTKTGQQ 186
Cdd:cd03223 73 -------PYLPLGT----LREQL------------IYPWDDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDR 129
|
170 180 190
....*....|....*....|....*....|....
gi 2076047389 187 IMELLTElnkEGKTIIMVTHEPEIADFATRKIII 220
Cdd:cd03223 130 LYQLLKE---LGITVISVGHRPSLWKFHDRVLDL 160
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
4-236 |
3.80e-22 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 94.35 E-value: 3.80e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 4 EKKQLMQLSNIVKSYQNgdqvLKVLKGINLTVYEGEFLAIMGPSGSGKSTLMNIIGLLDRPTSGDYTLHNTKIEILNDre 83
Cdd:PRK15439 7 TAPPLLCARSISKQYSG----VEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTP-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 84 lAKVRNDEIGFVFQQFFLLAKLTALQNVELPLiyAGVNVSKRREQAKqfLEKVGLGRRIKHLPSELSGGQKQRVAIARAL 163
Cdd:PRK15439 81 -AKAHQLGIYLVPQEPLLFPNLSVKENILFGL--PKRQASMQKMKQL--LAALGCQLDLDSSAGSLEVADRQIVEILRGL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2076047389 164 VNDPSIILADEPTGALDTKTGQQIMELLTELNKEGKTIIMVTHE-PEIADFATRKIIIRDGDI-----TTDTTASVVID 236
Cdd:PRK15439 156 MRDSRILILDEPTASLTPAETERLFSRIRELLAQGVGIVFISHKlPEIRQLADRISVMRDGTIalsgkTADLSTDDIIQ 234
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
26-206 |
5.02e-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: 94.12 E-value: 5.02e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 26 KVLKGINLTVYEGEFLAIMGPSGSGKSTlmnIIGLLDR---PTSGDYTLHNTKIeilndREL--AKVRNDeIGFVFQQff 100
Cdd:COG5265 372 PILKGVSFEVPAGKTVAIVGPSGAGKST---LARLLFRfydVTSGRILIDGQDI-----RDVtqASLRAA-IGIVPQD-- 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 101 llaklTALQN--VELPLIYAGVNVSkrREQAKQFLEKVGLGRRIKHLPS-----------ELSGGQKQRVAIARALVNDP 167
Cdd:COG5265 441 -----TVLFNdtIAYNIAYGRPDAS--EEEVEAAARAAQIHDFIESLPDgydtrvgerglKLSGGEKQRVAIARTLLKNP 513
|
170 180 190
....*....|....*....|....*....|....*....
gi 2076047389 168 SIILADEPTGALDTKTGQQIMELLTELNKeGKTIIMVTH 206
Cdd:COG5265 514 PILIFDEATSALDSRTERAIQAALREVAR-GRTTLVIAH 551
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
31-207 |
5.53e-22 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 94.15 E-value: 5.53e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 31 INLTVYEGEFLAIMGPSGSGKSTLMNIIGLLDRPTSGDYTLHNTKIEILNDRELAKVRNDeIGFVFQQFF--LLAKLTAL 108
Cdd:PRK10261 343 VSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQALRRD-IQFIFQDPYasLDPRQTVG 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 109 QNVELPLIYAGV-NVSKRREQAKQFLEKVGLgrRIKH---LPSELSGGQKQRVAIARALVNDPSIILADEPTGALDTKTG 184
Cdd:PRK10261 422 DSIMEPLRVHGLlPGKAAAARVAWLLERVGL--LPEHawrYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIR 499
|
170 180
....*....|....*....|....
gi 2076047389 185 QQIMELLTELNKE-GKTIIMVTHE 207
Cdd:PRK10261 500 GQIINLLLDLQRDfGIAYLFISHD 523
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
26-213 |
6.78e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 91.02 E-value: 6.78e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 26 KVLKGINLTVYEGEFLAIMGPSGSGKSTLMNIIGLLDRPTSGDYTLHNTKIEILNDRELAKVrndeIGFVFQ----QFFl 101
Cdd:PRK13652 18 EALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKF----VGLVFQnpddQIF- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 102 laKLTALQNVELPLIYAGVNVSKRREQAKQFLEKVGLGRRIKHLPSELSGGQKQRVAIARALVNDPSIILADEPTGALDT 181
Cdd:PRK13652 93 --SPTVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDP 170
|
170 180 190
....*....|....*....|....*....|....*..
gi 2076047389 182 KTGQQIMELLTELNKE-GKTIIMVTHE----PEIADF 213
Cdd:PRK13652 171 QGVKELIDFLNDLPETyGMTVIFSTHQldlvPEMADY 207
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
13-225 |
7.50e-22 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 93.54 E-value: 7.50e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 13 NIVKSYQNGDQvlKVLKGINLTVYEGEFLAIMGPSGSGKSTLMNIIGLLDRPTSGDYTL--HNtkieiLNDRELAKVRNd 90
Cdd:PRK11176 346 NVTFTYPGKEV--PALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLdgHD-----LRDYTLASLRN- 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 91 EIGFVFQQFFLLAKLTAlQNVElpliYAGVNVSKRRE--------QAKQFLEKV--GLGRRIKHLPSELSGGQKQRVAIA 160
Cdd:PRK11176 418 QVALVSQNVHLFNDTIA-NNIA----YARTEQYSREQieeaarmaYAMDFINKMdnGLDTVIGENGVLLSGGQRQRIAIA 492
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2076047389 161 RALVNDPSIILADEPTGALDTKTGQQIMELLTELNKEgKTIIMVTHEPEIADFATRKIIIRDGDI 225
Cdd:PRK11176 493 RALLRDSPILILDEATSALDTESERAIQAALDELQKN-RTSLVIAHRLSTIEKADEILVVEDGEI 556
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
27-226 |
9.72e-22 |
|
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: 89.51 E-value: 9.72e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 27 VLKGINLTVYEGEFLAIMGPSGSGKSTLMN-IIGLLdRPTSGDYTLHNTKIEILNDRELAKVrndEIGFVFQQFFLLAKL 105
Cdd:TIGR03410 15 ILRGVSLEVPKGEVTCVLGRNGVGKTTLLKtLMGLL-PVKSGSIRLDGEDITKLPPHERARA---GIAYVPQGREIFPRL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 106 TALQNVELpliyaGVNVSKRREQA------------KQFLekvglGRRikhlPSELSGGQKQRVAIARALVNDPSIILAD 173
Cdd:TIGR03410 91 TVEENLLT-----GLAALPRRSRKipdeiyelfpvlKEML-----GRR----GGDLSGGQQQQLAIARALVTRPKLLLLD 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2076047389 174 EPTGALDTKTGQQIMELLTELNKEGK-TIIMVTHEPEIA-DFATRKIIIRDGDIT 226
Cdd:TIGR03410 157 EPTEGIQPSIIKDIGRVIRRLRAEGGmAILLVEQYLDFArELADRYYVMERGRVV 211
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
10-223 |
1.22e-21 |
|
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: 87.12 E-value: 1.22e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 10 QLSNIVKSYqnGDQVLkvLKGINLTVYEGEFLAIMGPSGSGKSTLMNIIGLLDRPTSGDYTLHntkieilndrelakvRN 89
Cdd:cd03221 2 ELENLSKTY--GGKLL--LKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWG---------------ST 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 90 DEIGFVFQqffllakltalqnvelpliyagvnvskrreqakqflekvglgrrikhlpseLSGGQKQRVAIARALVNDPSI 169
Cdd:cd03221 63 VKIGYFEQ---------------------------------------------------LSGGEKMRLALAKLLLENPNL 91
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2076047389 170 ILADEPTGALDTKTGQQIMELLTELNkegKTIIMVTHEPE-IADFATRKIIIRDG 223
Cdd:cd03221 92 LLLDEPTNHLDLESIEALEEALKEYP---GTVILVSHDRYfLDQVATKIIELEDG 143
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
28-206 |
2.60e-21 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 91.95 E-value: 2.60e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 28 LKGINLTVYEGEFLAIMGPSGSGKSTLmniIGLLDR---PTSGDYTLHNTKIEILNdreLAKVRNDeIGFVFQQFFLLAK 104
Cdd:PRK13657 351 VEDVSFEAKPGQTVAIVGPTGAGKSTL---INLLQRvfdPQSGRILIDGTDIRTVT---RASLRRN-IAVVFQDAGLFNR 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 105 LTAlQNVEL---PLIYAGVNVSKRREQAKQFLEK--VGLGRRIKHLPSELSGGQKQRVAIARALVNDPSIILADEPTGAL 179
Cdd:PRK13657 424 SIE-DNIRVgrpDATDEEMRAAAERAQAHDFIERkpDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSAL 502
|
170 180
....*....|....*....|....*..
gi 2076047389 180 DTKTGQQIMELLTELNKeGKTIIMVTH 206
Cdd:PRK13657 503 DVETEAKVKAALDELMK-GRTTFIIAH 528
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
4-224 |
2.70e-21 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 91.84 E-value: 2.70e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 4 EKKQLMQLSNIVKSYQNGDQVLKVLKGINLTVYEGEFLAIMGPSGSGKS-TLMNIIGLLDRP----TSGDYTLHNTKIEI 78
Cdd:PRK10261 8 DARDVLAVENLNIAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSvTALALMRLLEQAgglvQCDKMLLRRRSRQV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 79 L-----NDRELAKVRNDEIGFVFQQffllaKLTALQNV--------ELPLIYAGVNVSKRREQAKQFLEKVGLGRR---I 142
Cdd:PRK10261 88 IelseqSAAQMRHVRGADMAMIFQE-----PMTSLNPVftvgeqiaESIRLHQGASREEAMVEAKRMLDQVRIPEAqtiL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 143 KHLPSELSGGQKQRVAIARALVNDPSIILADEPTGALDTKTGQQIMELLTELNKE-GKTIIMVTHE-PEIADFATRKIII 220
Cdd:PRK10261 163 SRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEmSMGVIFITHDmGVVAEIADRVLVM 242
|
....
gi 2076047389 221 RDGD 224
Cdd:PRK10261 243 YQGE 246
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
26-225 |
4.05e-21 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 89.76 E-value: 4.05e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 26 KVLKGINLTVYEGEFLAIMGPSGSGKSTLMNII-GLLdRPTSGdytlhntKIEIL------NDRELAKvrndEIGFVF-- 96
Cdd:COG4586 36 EAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLtGIL-VPTSG-------EVRVLgyvpfkRRKEFAR----RIGVVFgq 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 97 -QQffLLAKLTALQNVEL-PLIYaGVNVSKRREQAKQFLEKVGLGRRIKHLPSELSGGQKQRVAIARALVNDPSIILADE 174
Cdd:COG4586 104 rSQ--LWWDLPAIDSFRLlKAIY-RIPDAEYKKRLDELVELLDLGELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDE 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2076047389 175 PTGALDTKTGQQIMELLTELNKE-GKTIIMVTHEPE-IADFATRKIIIRDGDI 225
Cdd:COG4586 181 PTIGLDVVSKEAIREFLKEYNRErGTTILLTSHDMDdIEALCDRVIVIDHGRI 233
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
8-236 |
5.04e-21 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 90.76 E-value: 5.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 8 LMQLSNIVKSYQngdqVLKVLKGINLTVYEGEFLAIMGPSGSGKSTLMNIIglldrptSGDYTLHNTKIEILNDRELAK- 86
Cdd:PRK13549 5 LLEMKNITKTFG----GVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVL-------SGVYPHGTYEGEIIFEGEELQa 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 87 --VRNDE---IGFVFQQFFLLAKLTALQNVEL--PLIYAGV-NVSKRREQAKQFLEKVGLGRRIKHLPSELSGGQKQRVA 158
Cdd:PRK13549 74 snIRDTEragIAIIHQELALVKELSVLENIFLgnEITPGGImDYDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 159 IARALVNDPSIILADEPTGALDTKTGQQIMELLTELNKEGKTIIMVTHE----PEIADFATrkiIIRDGD-ITTDTTASV 233
Cdd:PRK13549 154 IAKALNKQARLLILDEPTASLTESETAVLLDIIRDLKAHGIACIYISHKlnevKAISDTIC---VIRDGRhIGTRPAAGM 230
|
...
gi 2076047389 234 VID 236
Cdd:PRK13549 231 TED 233
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
27-208 |
8.84e-21 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 90.32 E-value: 8.84e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 27 VLKGINLTVYEGEFLAIMGPSGSGKSTLMNIIglldrptSGDYTLHNTKIEIL-NDRELAKVRNDEIGFVFQQFFLLAKL 105
Cdd:PLN03211 83 ILNGVTGMASPGEILAVLGPSGSGKSTLLNAL-------AGRIQGNNFTGTILaNNRKPTKQILKRTGFVTQDDILYPHL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 106 TALQN-VELPLIYAGVNVSKRREQ--AKQFLEKVGLGRRIKHLPSE-----LSGGQKQRVAIARALVNDPSIILADEPTG 177
Cdd:PLN03211 156 TVRETlVFCSLLRLPKSLTKQEKIlvAESVISELGLTKCENTIIGNsfirgISGGERKRVSIAHEMLINPSLLILDEPTS 235
|
170 180 190
....*....|....*....|....*....|.
gi 2076047389 178 ALDTKTGQQIMELLTELNKEGKTIIMVTHEP 208
Cdd:PLN03211 236 GLDATAAYRLVLTLGSLAQKGKTIVTSMHQP 266
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
31-220 |
9.30e-21 |
|
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: 90.84 E-value: 9.30e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 31 INLTVYEGEFLAIMGPSGSGKSTLMNIIGLLDRPTSGDYTLHNTKIEIlndrELAKVRNdEIGFVFQQFFLLAKLTALQN 110
Cdd:TIGR01257 949 LNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIET----NLDAVRQ-SLGMCPQHNILFHHLTVAEH 1023
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 111 VelpLIYAGVNvSKRREQAK----QFLEKVGLGRRIKHLPSELSGGQKQRVAIARALVNDPSIILADEPTGALDTKTGQQ 186
Cdd:TIGR01257 1024 I---LFYAQLK-GRSWEEAQlemeAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRS 1099
|
170 180 190
....*....|....*....|....*....|....
gi 2076047389 187 IMELLTELnKEGKTIIMVTHEPEIADFATRKIII 220
Cdd:TIGR01257 1100 IWDLLLKY-RSGRTIIMSTHHMDEADLLGDRIAI 1132
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
8-223 |
1.18e-20 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 89.85 E-value: 1.18e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 8 LMQLSNIVKSYQNgdqvLKVLKGINLTVYEGEFLAIMGPSGSGKSTLMNIIglldrptSGDYTLHNTKIEILNDRELAKV 87
Cdd:NF040905 1 ILEMRGITKTFPG----VKALDDVNLSVREGEIHALCGENGAGKSTLMKVL-------SGVYPHGSYEGEILFDGEVCRF 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 88 RN----DEIGFVF--QQFFLLAKLTALQNvelplIYAGVNVSKR--------REQAKQFLEKVGLGRRIKHLPSELSGGQ 153
Cdd:NF040905 70 KDirdsEALGIVIihQELALIPYLSIAEN-----IFLGNERAKRgvidwnetNRRARELLAKVGLDESPDTLVTDIGVGK 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2076047389 154 KQRVAIARALVNDPSIILADEPTGALDTKTGQQIMELLTELNKEGKTIIMVTHE-PEIADFATRKIIIRDG 223
Cdd:NF040905 145 QQLVEIAKALSKDVKLLILDEPTAALNEEDSAALLDLLLELKAQGITSIIISHKlNEIRRVADSITVLRDG 215
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
26-225 |
2.11e-20 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 86.27 E-value: 2.11e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 26 KVLKGINLTVYEGEFLAIMGPSGSGKSTLMNII-GLLD-RPTSGDYTLHN---TKIEIlndrelakvrnDE-----IGFV 95
Cdd:COG0396 14 EILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLmGHPKyEVTSGSILLDGediLELSP-----------DEraragIFLA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 96 FQQ----------FFLLAKLTALQNVELPLIyagvnvsKRREQAKQFLEKVGLGRriKHLPSEL----SGGQKQRVAIAR 161
Cdd:COG0396 83 FQYpveipgvsvsNFLRTALNARRGEELSAR-------EFLKLLKEKMKELGLDE--DFLDRYVnegfSGGEKKRNEILQ 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2076047389 162 ALVNDPSIILADEPTGALDTKTGQQIMELLTELNKEGKTIIMVTHEPEIADF--ATRKIIIRDGDI 225
Cdd:COG0396 154 MLLLEPKLAILDETDSGLDIDALRIVAEGVNKLRSPDRGILIITHYQRILDYikPDFVHVLVDGRI 219
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
8-207 |
3.15e-20 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 87.55 E-value: 3.15e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 8 LMQLSNIVKSYQNGDQVLKVLKGINLTVYEGEFLAIMGPSGSGKSTLMN-IIGLLD---RPTSGDYTLHNTKIEILNDRE 83
Cdd:PRK15093 3 LLDIRNLTIEFKTSDGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKaICGVTKdnwRVTADRMRFDDIDLLRLSPRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 84 LAKVRNDEIGFVFQQffLLAKLTALQNVELPLI-------YAG-----VNVSKRReqAKQFLEKVGLGRR---IKHLPSE 148
Cdd:PRK15093 83 RRKLVGHNVSMIFQE--PQSCLDPSERVGRQLMqnipgwtYKGrwwqrFGWRKRR--AIELLHRVGIKDHkdaMRSFPYE 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 149 LSGGQKQRVAIARALVNDPSIILADEPTGALDTKTGQQIMELLTELNK-EGKTIIMVTHE 207
Cdd:PRK15093 159 LTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQnNNTTILLISHD 218
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
9-206 |
8.06e-20 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 87.47 E-value: 8.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 9 MQLSNIVKSYQNGDqvlKVLKGINLTVYEGEFLAIMGPSGSGKSTLMNIIGLLDRPTSGDYTLHNTKIEILNDRELakvR 88
Cdd:PRK10790 341 IDIDNVSFAYRDDN---LVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVL---R 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 89 NDeIGFVFQQFFLLAKlTALQNVELpliyaGVNVSKrrEQAKQFLEKVGLGRRIKHLP-----------SELSGGQKQRV 157
Cdd:PRK10790 415 QG-VAMVQQDPVVLAD-TFLANVTL-----GRDISE--EQVWQALETVQLAELARSLPdglytplgeqgNNLSVGQKQLL 485
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2076047389 158 AIARALVNDPSIILADEPTGALDTKTGQQIMELLTELnKEGKTIIMVTH 206
Cdd:PRK10790 486 ALARVLVQTPQILILDEATANIDSGTEQAIQQALAAV-REHTTLVVIAH 533
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
13-225 |
1.38e-19 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 84.17 E-value: 1.38e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 13 NIVKSYQNgdqvLKVLKGINLTVYEGEFLAIMGPSGSGKST-LMNIIGLLDRpTSGDYTLHNTKIEILNDRELAKvrnDE 91
Cdd:PRK10895 8 NLAKAYKG----RRVVEDVSLTVNSGEIVGLLGPNGAGKTTtFYMVVGIVPR-DAGNIIIDDEDISLLPLHARAR---RG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 92 IGFVFQQFFLLAKLTALQNVELPL-IYAGVNVSKRREQAKQFLEKVGLGRRIKHLPSELSGGQKQRVAIARALVNDPSII 170
Cdd:PRK10895 80 IGYLPQEASIFRRLSVYDNLMAVLqIRDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFI 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2076047389 171 LADEPTGALDTKTGQQIMELLTELNKEGKTIIMVTHE-PEIADFATRKIIIRDGDI 225
Cdd:PRK10895 160 LLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNvRETLAVCERAYIVSQGHL 215
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
27-206 |
3.60e-19 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 83.29 E-value: 3.60e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 27 VLKGINLTVYEGEFLAI---------------MGPSGSGKSTLMNIIGLLDR--PT---SGDYTLHNTKieiLNDREL-- 84
Cdd:PRK14243 10 VLRTENLNVYYGSFLAVknvwldipknqitafIGPSGCGKSTILRCFNRLNDliPGfrvEGKVTFHGKN---LYAPDVdp 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 85 AKVRNdEIGFVFQQFFLLAKlTALQNVEL-PLI--YAG-----VNVSKRR----EQAKQFLEKVGLGrrikhlpseLSGG 152
Cdd:PRK14243 87 VEVRR-RIGMVFQKPNPFPK-SIYDNIAYgARIngYKGdmdelVERSLRQaalwDEVKDKLKQSGLS---------LSGG 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2076047389 153 QKQRVAIARALVNDPSIILADEPTGALDTKTGQQIMELLTELnKEGKTIIMVTH 206
Cdd:PRK14243 156 QQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHEL-KEQYTIIIVTH 208
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
26-232 |
1.27e-18 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 84.07 E-value: 1.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 26 KVLKGINLTVYEGEFLAIMGPSGSGKSTLMNIIGLLDRPTSGDYTLHNTKIEILNdrELAKVRND---------EIGFvF 96
Cdd:PRK09700 277 KKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRS--PLDAVKKGmayitesrrDNGF-F 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 97 QQFFL---LAKLTALQNVELPLIYAGVNVSKRREQAKQFLEKVGLG-RRIKHLPSELSGGQKQRVAIARALVNDPSIILA 172
Cdd:PRK09700 354 PNFSIaqnMAISRSLKDGGYKGAMGLFHEVDEQRTAENQRELLALKcHSVNQNITELSGGNQQKVLISKWLCCCPEVIIF 433
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2076047389 173 DEPTGALDTKTGQQIMELLTELNKEGKTIIMVTHE-PEIADFATRKIIIRDGDITTDTTAS 232
Cdd:PRK09700 434 DEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSElPEIITVCDRIAVFCEGRLTQILTNR 494
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
7-232 |
2.38e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 81.68 E-value: 2.38e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 7 QLMQLSNIVKSYQNGDQVLKvLKGINLTVYEGEFLAIMGPSGSGKSTLMNIIGLLDRPTSGDYTLHNTKIEILNDRELAK 86
Cdd:PRK13642 3 KILEVENLVFKYEKESDVNQ-LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 87 vrndEIGFVFQ----QFfllAKLTALQNVELPLIYAGVNVSKRREQAKQFLEKVGLGRRIKHLPSELSGGQKQRVAIARA 162
Cdd:PRK13642 82 ----KIGMVFQnpdnQF---VGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGI 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2076047389 163 LVNDPSIILADEPTGALDTKTGQQIMELLTEL-NKEGKTIIMVTHEPEIADFATRKIIIRDGDITTDTTAS 232
Cdd:PRK13642 155 IALRPEIIILDESTSMLDPTGRQEIMRVIHEIkEKYQLTVLSITHDLDEAASSDRILVMKAGEIIKEAAPS 225
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
22-213 |
2.59e-18 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 80.39 E-value: 2.59e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 22 DQVLKVLKGINLTVYEGEFLAIMGPSGSGKSTLMN-IIG-LLDRPTSGdytlhntkieilndreLAKVRNDEIGfvfqqf 99
Cdd:COG2401 40 VVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRlLAGaLKGTPVAG----------------CVDVPDNQFG------ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 100 fllakltalqnVELPLIYagvNVSKRRE--QAKQFLEKVGLG------RRikhlPSELSGGQKQRVAIARALVNDPSIIL 171
Cdd:COG2401 98 -----------REASLID---AIGRKGDfkDAVELLNAVGLSdavlwlRR----FKELSTGQKFRFRLALLLAERPKLLV 159
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2076047389 172 ADEPTGALDTKTGQQIMELLTELNKE-GKTIIMVTHEPEIADF 213
Cdd:COG2401 160 IDEFCSHLDRQTAKRVARNLQKLARRaGITLVVATHHYDVIDD 202
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
23-213 |
2.75e-18 |
|
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: 79.59 E-value: 2.75e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 23 QVLKVLKGINLTVYEGEFLAIMGPSGSGKSTLMNIigLLDRPTSGDytlhnTKIEIL-NDRELAKVRNDEIGFVFQQFFL 101
Cdd:cd03232 18 GKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDV--LAGRKTAGV-----ITGEILiNGRPLDKNFQRSTGYVEQQDVH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 102 LAKLTalqnVELPLIYAGVNvskrreqakqflekvglgrrikhlpSELSGGQKQRVAIARALVNDPSIILADEPTGALDT 181
Cdd:cd03232 91 SPNLT----VREALRFSALL-------------------------RGLSVEQRKRLTIGVELAAKPSILFLDEPTSGLDS 141
|
170 180 190
....*....|....*....|....*....|..
gi 2076047389 182 KTGQQIMELLTELNKEGKTIIMVTHEPEIADF 213
Cdd:cd03232 142 QAAYNIVRFLKKLADSGQAILCTIHQPSASIF 173
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
25-235 |
2.87e-18 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 80.69 E-value: 2.87e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 25 LKVLKGINLTVYEGEFLAIMGPSGSGKSTLMNIIGLLDRPTSGDYTLHNTKIeilNDRELAKVRNDEIGFVFQQFFLLAK 104
Cdd:PRK11614 18 IQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDI---TDWQTAKIMREAVAIVPEGRRVFSR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 105 LTALQNVELPLIYAgvnvskRREQAKQFLEKV-----GLGRRIKHLPSELSGGQKQRVAIARALVNDPSIILADEPTGAL 179
Cdd:PRK11614 95 MTVEENLAMGGFFA------ERDQFQERIKWVyelfpRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGL 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2076047389 180 DTKTGQQIMELLTELNKEGKTIIMVTHEPEIA-DFATRKIIIRDGDITTDTTASVVI 235
Cdd:PRK11614 169 APIIIQQIFDTIEQLREQGMTIFLVEQNANQAlKLADRGYVLENGHVVLEDTGDALL 225
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
11-206 |
1.30e-17 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 79.54 E-value: 1.30e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 11 LSNIVKSYQNGDQVLKvlkGINLTVYEGEFLAIMGPSGSGKSTLMNIIGLLDRPTSGDytlhntkIEILNDRELAKVRND 90
Cdd:PRK15056 9 VNDVTVTWRNGHTALR---DASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGK-------ISILGQPTRQALQKN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 91 EIGFVFQQ------FFLLAKLTALQNVELPLIYAGVNVSKRREQAKQFLEKVGLGRRIKHLPSELSGGQKQRVAIARALV 164
Cdd:PRK15056 79 LVAYVPQSeevdwsFPVLVEDVVMMGRYGHMGWLRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIA 158
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2076047389 165 NDPSIILADEPTGALDTKTGQQIMELLTELNKEGKTIIMVTH 206
Cdd:PRK15056 159 QQGQVILLDEPFTGVDVKTEARIISLLRELRDEGKTMLVSTH 200
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
8-236 |
1.34e-17 |
|
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: 81.02 E-value: 1.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 8 LMQLSNIVKSYQNgdqvLKVLKGINLTVYEGEFLAIMGPSGSGKSTLMNIIglldrptSGDYTLHNTKIEILNDRELAK- 86
Cdd:TIGR02633 1 LLEMKGIVKTFGG----VKALDGIDLEVRPGECVGLCGENGAGKSTLMKIL-------SGVYPHGTWDGEIYWSGSPLKa 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 87 --VRNDE---IGFVFQQFFLLAKLTALQNV----ELPLIYAGVNVSKRREQAKQFLEKVGLGRRIKHLP-SELSGGQKQR 156
Cdd:TIGR02633 70 snIRDTEragIVIIHQELTLVPELSVAENIflgnEITLPGGRMAYNAMYLRAKNLLRELQLDADNVTRPvGDYGGGQQQL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 157 VAIARALVNDPSIILADEPTGALDTKTGQQIMELLTELNKEGKTIIMVTHE-PEIADFATRKIIIRDGD-ITTDTTASVV 234
Cdd:TIGR02633 150 VEIAKALNKQARLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKlNEVKAVCDTICVIRDGQhVATKDMSTMS 229
|
..
gi 2076047389 235 ID 236
Cdd:TIGR02633 230 ED 231
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
8-234 |
2.59e-17 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 78.23 E-value: 2.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 8 LMQLSNIVKSYQNGdqvlKVLKGINLTVYEGEFLAIMGPSGSGKSTLMNIIGLLDRPTSGdytlhntkiEILNDRELakv 87
Cdd:PRK09544 4 LVSLENVSVSFGQR----RVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEG---------VIKRNGKL--- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 88 rndEIGFVFQQFFLLAKLtALQNVELPLIYAGVnvskRREQAKQFLEKVGLGRRIKHLPSELSGGQKQRVAIARALVNDP 167
Cdd:PRK09544 68 ---RIGYVPQKLYLDTTL-PLTVNRFLRLRPGT----KKEDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRP 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2076047389 168 SIILADEPTGALDTKTGQQIMELLTELNKE-GKTIIMVTHEPEIADFATRKIIIRDGDITTDTTASVV 234
Cdd:PRK09544 140 QLLVLDEPTQGVDVNGQVALYDLIDQLRRElDCAVLMVSHDLHLVMAKTDEVLCLNHHICCSGTPEVV 207
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
27-206 |
2.78e-17 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 80.14 E-value: 2.78e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 27 VLKGINLTVYEGEFLAIMGPSGSGKSTLMNIIGLLDRPTSGDYTLHntkieilnDRELAKVRNDE----IGFVFQQFFLL 102
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFH--------DIPLTKLQLDSwrsrLAVVSQTPFLF 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 103 AKLTAlQNVELpliyagvnvsKRREQAKQFLEKVG----LGRRIKHLPS-----------ELSGGQKQRVAIARALVNDP 167
Cdd:PRK10789 402 SDTVA-NNIAL----------GRPDATQQEIEHVArlasVHDDILRLPQgydtevgergvMLSGGQKQRISIARALLLNA 470
|
170 180 190
....*....|....*....|....*....|....*....
gi 2076047389 168 SIILADEPTGALDTKTGQQIMELLTELnKEGKTIIMVTH 206
Cdd:PRK10789 471 EILILDDALSAVDGRTEHQILHNLRQW-GEGRTVIISAH 508
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
27-211 |
4.20e-17 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 77.91 E-value: 4.20e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 27 VLKGINLTVYEGEFLAIMGPSGSGKSTLMNIIGLLDRPTSGDYTLHNTKIEILNDRELAKvrndEIGFVFQQFFLLAKLT 106
Cdd:PRK10575 26 LLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFAR----KVAYLPQQLPAAEGMT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 107 ALQNVEL---PLIYA-GVNVSKRREQAKQFLEKVGLGRRIKHLPSELSGGQKQRVAIARALVNDPSIILADEPTGALDTK 182
Cdd:PRK10575 102 VRELVAIgryPWHGAlGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIA 181
|
170 180 190
....*....|....*....|....*....|
gi 2076047389 183 TGQQIMELLTELNKE-GKTIIMVTHEPEIA 211
Cdd:PRK10575 182 HQVDVLALVHRLSQErGLTVIAVLHDINMA 211
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
9-206 |
4.63e-17 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 77.57 E-value: 4.63e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 9 MQLSNIvksyqngdQVLKVLKGINLTVYEGEFLAIMGPSGSGKSTLMNII-GLLdrPTSGDYTLHNTKIEILNDRELAKV 87
Cdd:COG4138 1 LQLNDV--------AVAGRLGPISAQVNAGELIHLIGPNGAGKSTLLARMaGLL--PGQGEILLNGRPLSDWSAAELARH 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 88 RndeiGFVFQQFFLLAKLTALQnvELPLIYAGVNVSKRREQAKQFL-EKVG----LGRRIKHLpselSGGQKQRVAIARA 162
Cdd:COG4138 71 R----AYLSQQQSPPFAMPVFQ--YLALHQPAGASSEAVEQLLAQLaEALGledkLSRPLTQL----SGGEWQRVRLAAV 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2076047389 163 LVN-DPSI------ILADEPTGALDtkTGQQIM--ELLTELNKEGKTIIMVTH 206
Cdd:COG4138 141 LLQvWPTInpegqlLLLDEPMNSLD--VAQQAAldRLLRELCQQGITVVMSSH 191
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
42-228 |
1.18e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 76.67 E-value: 1.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 42 AIMGPSGSGKSTLMNIIGLLDRPTSG-----DYTLHNTkiEILNDRELAKVRNdEIGFVFQQFFLLAkLTALQNVelpli 116
Cdd:PRK14271 51 SLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGR--SIFNYRDVLEFRR-RVGMLFQRPNPFP-MSIMDNV----- 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 117 YAGVNVSK---RRE---QAKQFLEKVGL----GRRIKHLPSELSGGQKQRVAIARALVNDPSIILADEPTGALDTKTGQQ 186
Cdd:PRK14271 122 LAGVRAHKlvpRKEfrgVAQARLTEVGLwdavKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEK 201
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2076047389 187 IMELLTELnKEGKTIIMVTHE-PEIADFATRKIIIRDGDITTD 228
Cdd:PRK14271 202 IEEFIRSL-ADRLTVIIVTHNlAQAARISDRAALFFDGRLVEE 243
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
26-227 |
1.51e-16 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 76.58 E-value: 1.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 26 KVLKGINLTVYEGEFLAIMGPSGSGKSTL-MNIIGLLdRPTSGDYTLHNTKIEiLNDRELAKVRNdEIGFVFQ----QFF 100
Cdd:PRK13638 15 PVLKGLNLDFSLSPVTGLVGANGCGKSTLfMNLSGLL-RPQKGAVLWQGKPLD-YSKRGLLALRQ-QVATVFQdpeqQIF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 101 LlaklTAL-QNVELPLIYAGV---NVSKRREQAKQFLEkvglGRRIKHLPSE-LSGGQKQRVAIARALVNDPSIILADEP 175
Cdd:PRK13638 92 Y----TDIdSDIAFSLRNLGVpeaEITRRVDEALTLVD----AQHFRHQPIQcLSHGQKKRVAIAGALVLQARYLLLDEP 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2076047389 176 TGALDTKTGQQIMELLTELNKEGKTIIMVTHEPE-IADFATRKIIIRDGDITT 227
Cdd:PRK13638 164 TAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDlIYEISDAVYVLRQGQILT 216
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
19-232 |
3.03e-16 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 76.97 E-value: 3.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 19 QNGDQVLKV-------LKGINLTVYEGEFLAIMGPSGSGKSTLMNII-GLLDRpTSGDYTLHNTKIEILNDRE-----LA 85
Cdd:PRK10762 252 APGEVRLKVdnlsgpgVNDVSFTLRKGEILGVSGLMGAGRTELMKVLyGALPR-TSGYVTLDGHEVVTRSPQDglangIV 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 86 KVRNDEIGFvfqqfFLLAKLTALQNVELP----LIYAGVNVSKRREQ--AKQFLEKVglgrRIKhLPS------ELSGGQ 153
Cdd:PRK10762 331 YISEDRKRD-----GLVLGMSVKENMSLTalryFSRAGGSLKHADEQqaVSDFIRLF----NIK-TPSmeqaigLLSGGN 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 154 KQRVAIARALVNDPSIILADEPTGALDTKTGQQIMELLTELNKEGKTIIMVTHE-PEIADFATRKIIIRDGDITTDTTAS 232
Cdd:PRK10762 401 QQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAEGLSIILVSSEmPEVLGMSDRILVMHEGRISGEFTRE 480
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
27-206 |
3.15e-16 |
|
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: 74.45 E-value: 3.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 27 VLKGINLTVYEGEFLAIMGPSGSGKSTLMNIIGLLDRPTSGDYTLHNTKIEILNdreLAKVRNdEIGFVFQQFFLLAKlT 106
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIG---LHDLRS-RISIIPQDPVLFSG-T 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 107 ALQNVElPLiyaGVNVSKRREQAkqfLEKVGLGRRIKHLP-----------SELSGGQKQRVAIARALVNDPSIILADEP 175
Cdd:cd03244 94 IRSNLD-PF---GEYSDEELWQA---LERVGLKEFVESLPggldtvveeggENLSVGQRQLLCLARALLRKSKILVLDEA 166
|
170 180 190
....*....|....*....|....*....|.
gi 2076047389 176 TGALDTKTGQQIMELLTELNKeGKTIIMVTH 206
Cdd:cd03244 167 TASVDPETDALIQKTIREAFK-DCTVLTIAH 196
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
25-214 |
3.56e-16 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 77.07 E-value: 3.56e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 25 LKVLKGINLTVYEGEFLAIMGPSGSGKSTLMNIigLLDRPTSGDYTlhnTKIEILNDRELAKVRNDEIGFVFQQFFLLAK 104
Cdd:TIGR00956 776 RVILNNVDGWVKPGTLTALMGASGAGKTTLLNV--LAERVTTGVIT---GGDRLVNGRPLDSSFQRSIGYVQQQDLHLPT 850
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 105 LTalqnVELPLIYAGV-----NVSKrrEQAKQFLEKVglgrrIKHLPSE-------------LSGGQKQRVAIARALVND 166
Cdd:TIGR00956 851 ST----VRESLRFSAYlrqpkSVSK--SEKMEYVEEV-----IKLLEMEsyadavvgvpgegLNVEQRKRLTIGVELVAK 919
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2076047389 167 P-SIILADEPTGALDTKTGQQIMELLTELNKEGKTIIMVTHEPEIADFA 214
Cdd:TIGR00956 920 PkLLLFLDEPTSGLDSQTAWSICKLMRKLADHGQAILCTIHQPSAILFE 968
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
7-207 |
8.36e-16 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 73.97 E-value: 8.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 7 QLMQLSNIVKSyqnGDQVLkvLKGINLTVYEGEFLAIMGPSGSGKStlMNIIGLLD------RPTSGDYTLHNTKIEiln 80
Cdd:PRK10418 3 QQIELRNIALQ---AAQPL--VHGVSLTLQRGRVLALVGGSGSGKS--LTCAAALGilpagvRQTAGRVLLDGKPVA--- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 81 dreLAKVRNDEIGFVFQQ----FFLLAKLTAlQNVElplIYAGVNVSKRREQAKQFLEKVGLG---RRIKHLPSELSGGQ 153
Cdd:PRK10418 73 ---PCALRGRKIATIMQNprsaFNPLHTMHT-HARE---TCLALGKPADDATLTAALEAVGLEnaaRVLKLYPFEMSGGM 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2076047389 154 KQRVAIARALVNDPSIILADEPTGALDTKTGQQIMELLTELNKE-GKTIIMVTHE 207
Cdd:PRK10418 146 LQRMMIALALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKrALGMLLVTHD 200
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
26-212 |
9.60e-16 |
|
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six proteins and believed to act in Fe-S cluster formation during oxidative stress. SufC forms a complex with SufB and SufD. SufC belongs to the ATP-binding cassette transporter family (pfam00005) but is no longer thought to be part of a transporter. The complex is reported as cytosolic () or associated with the membrane (). The SUF system also includes a cysteine desulfurase (SufS, enhanced by SufE) and a probable iron-sulfur cluster assembly scaffold protein, SufA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 273907 [Multi-domain] Cd Length: 243 Bit Score: 73.83 E-value: 9.60e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 26 KVLKGINLTVYEGEFLAIMGPSGSGKSTLMNIIglldrptSGDYTLHNTKIEI-LNDRELAKVRNDEIG----FV-FQ-- 97
Cdd:TIGR01978 14 EILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTI-------AGHPSYEVTSGTIlFKGQDLLELEPDERAraglFLaFQyp 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 98 --------QFFLLAKLTAL--QNVELPLiyagvNVSKRREQAKQFLEKVGLGRRIKH--LPSELSGGQKQRVAIARALVN 165
Cdd:TIGR01978 87 eeipgvsnLEFLRSALNARrsARGEEPL-----DLLDFEKLLKEKLALLDMDEEFLNrsVNEGFSGGEKKRNEILQMALL 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2076047389 166 DPSIILADEPTGALDTKTGQQIMELLTELNKEGKTIIMVTHEPEIAD 212
Cdd:TIGR01978 162 EPKLAILDEIDSGLDIDALKIVAEGINRLREPDRSFLIITHYQRLLN 208
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
21-226 |
1.60e-15 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 75.06 E-value: 1.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 21 GDQVLKVLKGINLTVYEGEFLAIMGPSGSGKSTLMNIIGLLDRPTSGDYTLHNTKIEILNDRELakvRNDEIGFV---FQ 97
Cdd:COG3845 267 DDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRER---RRLGVAYIpedRL 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 98 QFFLLAKLTALQNVELPLIYAG-------VNVSKRREQAKQFLEK-----VGLGRRIKHLpselSGGQKQRVAIARALVN 165
Cdd:COG3845 344 GRGLVPDMSVAENLILGRYRRPpfsrggfLDRKAIRAFAEELIEEfdvrtPGPDTPARSL----SGGNQQKVILARELSR 419
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2076047389 166 DPSIILADEPTGALDTKTGQQIMELLTELNKEGKTIIMVTHE-PEIADFATRKIIIRDGDIT 226
Cdd:COG3845 420 DPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVLLISEDlDEILALSDRIAVMYEGRIV 481
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
26-213 |
1.65e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 73.53 E-value: 1.65e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 26 KVLKGINLTVYEGEFLAIMGPSGSGKSTLMNIIGLLDRpTSGDYTLHNtKIEILNDR------ELAKVRNdEIGFVFQQF 99
Cdd:PRK14258 21 KILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNE-LESEVRVEG-RVEFFNQNiyerrvNLNRLRR-QVSMVHPKP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 100 FLLAkLTALQNVELPLIYAG----VNVSKRREQAkqfLEKVGLGRRIKHL----PSELSGGQKQRVAIARALVNDPSIIL 171
Cdd:PRK14258 98 NLFP-MSVYDNVAYGVKIVGwrpkLEIDDIVESA---LKDADLWDEIKHKihksALDLSGGQQQRLCIARALAVKPKVLL 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2076047389 172 ADEPTGALDTKTGQQIMELLTELNKEGK-TIIMVTHE----PEIADF 213
Cdd:PRK14258 174 MDEPCFGLDPIASMKVESLIQSLRLRSElTMVIVSHNlhqvSRLSDF 220
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
8-225 |
2.32e-15 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 74.67 E-value: 2.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 8 LMQLSNIVKSYqnGDQVlkVLKGINLTVYEGEFLAIMGPSGSGKSTLMNII-GllDRPT--SGDYTLHNTKI---EILND 81
Cdd:PRK10938 260 RIVLNNGVVSY--NDRP--ILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLItG--DHPQgySNDLTLFGRRRgsgETIWD 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 82 RElakvrnDEIGFVFQQFFLLAKL-TALQNVELPL------IYAGVNvSKRREQAKQFLEKVGLGRRIKHLP-SELSGGQ 153
Cdd:PRK10938 334 IK------KHIGYVSSSLHLDYRVsTSVRNVILSGffdsigIYQAVS-DRQQKLAQQWLDILGIDKRTADAPfHSLSWGQ 406
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2076047389 154 KQRVAIARALVNDPSIILADEPTGALDTKTGQQIMELLTELNKEGKT-IIMVTHEPEIAD--FATRKIIIRDGDI 225
Cdd:PRK10938 407 QRLALIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISEGETqLLFVSHHAEDAPacITHRLEFVPDGDI 481
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
7-226 |
3.11e-15 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 74.24 E-value: 3.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 7 QLMQLSNIVKSYQngDQVLKVlKGINLTVYEGEFLAIMGPSGSGKSTLMNIIGLLDRPTSGDYTLHNTKIEILNDRELAK 86
Cdd:PRK10522 321 QTLELRNVTFAYQ--DNGFSV-GPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRK 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 87 VrndeIGFVFQQFFLLAKLTALQNVElpliyagvnvsKRREQAKQFLEKVGLGRRIKH-----LPSELSGGQKQRVAIAR 161
Cdd:PRK10522 398 L----FSAVFTDFHLFDQLLGPEGKP-----------ANPALVEKWLERLKMAHKLELedgriSNLKLSKGQKKRLALLL 462
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2076047389 162 ALVNDPSIILADEPTGALDTKTGQQI-MELLTELNKEGKTIIMVTHEPEIADFATRKIIIRDGDIT 226
Cdd:PRK10522 463 ALAEERDILLLDEWAADQDPHFRREFyQVLLPLLQEMGKTIFAISHDDHYFIHADRLLEMRNGQLS 528
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
26-213 |
5.79e-15 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 71.60 E-value: 5.79e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 26 KVLKGINLTVYEGEFLAIMGPSGSGKSTLMNIIGllDRP----TSGDYTLHNTKIEILNDRELAKVrndEIGFVFQ---- 97
Cdd:CHL00131 21 EILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIA--GHPaykiLEGDILFKGESILDLEPEERAHL---GIFLAFQypie 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 98 -------QFFLLA---KLTALQNVEL-PLIYAGVNVSKrreqakqfLEKVGLGRRIKH--LPSELSGGQKQRVAIARALV 164
Cdd:CHL00131 96 ipgvsnaDFLRLAynsKRKFQGLPELdPLEFLEIINEK--------LKLVGMDPSFLSrnVNEGFSGGEKKRNEILQMAL 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2076047389 165 NDPSIILADEPTGALDTKTGQQIMELLTELNKEGKTIIMVTHEPEIADF 213
Cdd:CHL00131 168 LDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIILITHYQRLLDY 216
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
9-206 |
9.58e-15 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 71.12 E-value: 9.58e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 9 MQLSNIvksyqngdQVLKVLKGINLTVYEGEFLAIMGPSGSGKSTLMN-IIGLLdrPTSGDYTLHNTKIEILNDRELAKV 87
Cdd:PRK03695 1 MQLNDV--------AVSTRLGPLSAEVRAGEILHLVGPNGAGKSTLLArMAGLL--PGSGSIQFAGQPLEAWSAAELARH 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 88 RndeiGFVFQQFFLLAKLTALQNVELPLiYAGVNVSKRREQAKQFLEKVGLGRRIKHLPSELSGGQKQRVAIARALVN-D 166
Cdd:PRK03695 71 R----AYLSQQQTPPFAMPVFQYLTLHQ-PDKTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVLQvW 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2076047389 167 PSI------ILADEPTGALDtkTGQQIM--ELLTELNKEGKTIIMVTH 206
Cdd:PRK03695 146 PDInpagqlLLLDEPMNSLD--VAQQAAldRLLSELCQQGIAVVMSSH 191
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
28-223 |
1.52e-14 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 70.62 E-value: 1.52e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 28 LKGINLTVYEGEFLAIMGPSGSGKSTLMNIIGLLDRPTSGDYTlhntkieilndrelakvRNDEIGFVFQQFFLLAKLTA 107
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVD-----------------RNGEVSVIAISAGLSGQLTG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 108 LQNVELPLIYAGVNVSKRREQAKQFLEKVGLGRRIKHLPSELSGGQKQRVAIARALVNDPSIILADEPTGALDTKTGQQI 187
Cdd:PRK13546 103 IENIEFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKC 182
|
170 180 190
....*....|....*....|....*....|....*..
gi 2076047389 188 MELLTELNKEGKTIIMVTHE-PEIADFATRKIIIRDG 223
Cdd:PRK13546 183 LDKIYEFKEQNKTIFFVSHNlGQVRQFCTKIAWIEGG 219
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
26-207 |
2.28e-14 |
|
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: 71.50 E-value: 2.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 26 KVLKGINLTVYEGEFLAIMGPSGSGKSTLMNIIGLLDRPTSGDYTLH-NTKIEIL----------NDRE-----LAKVRN 89
Cdd:TIGR03719 19 EILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQpGIKVGYLpqepqldptkTVREnveegVAEIKD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 90 --DEIGFVFQQF--------FLLAKLTALQNvelpLIYA--GVNVSKRREQAKQFLEkvglgrrikhLP------SELSG 151
Cdd:TIGR03719 99 alDRFNEISAKYaepdadfdKLAAEQAELQE----IIDAadAWDLDSQLEIAMDALR----------CPpwdadvTKLSG 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2076047389 152 GQKQRVAIARALVNDPSIILADEPTGALDTKTGQQIMELLTELnkEGkTIIMVTHE 207
Cdd:TIGR03719 165 GERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEY--PG-TVVAVTHD 217
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
21-226 |
2.71e-14 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 71.48 E-value: 2.71e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 21 GDQVLKV--LKG------INLTVYEGEFLAIMGPSGSGKSTLMNIIGLLDRPTSGDYTLHNTKIEILN------------ 80
Cdd:PRK11288 254 GEVRLRLdgLKGpglrepISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSprdairagimlc 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 81 --DRE------LAKVRnDEIGFVFQQFFLLAKLTalqnvelpliyagVNVSKRREQAKQFLEKVglgrRIKhLPS----- 147
Cdd:PRK11288 334 peDRKaegiipVHSVA-DNINISARRHHLRAGCL-------------INNRWEAENADRFIRSL----NIK-TPSreqli 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 148 -ELSGGQKQRVAIARALVNDPSIILADEPTGALDTKTGQQIMELLTELNKEGKTIIMVTHE-PEIADFATRKIIIRDGDI 225
Cdd:PRK11288 395 mNLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYELAAQGVAVLFVSSDlPEVLGVADRIVVMREGRI 474
|
.
gi 2076047389 226 T 226
Cdd:PRK11288 475 A 475
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
37-213 |
2.97e-14 |
|
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: 71.35 E-value: 2.97e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 37 EGEFLAIMGPSGSGKSTLMNII-GLLdRPTSGDYTLHNTKIEILNdrelaKVRNDEIGFVFQQfflLA--KLTA---LQN 110
Cdd:COG1245 98 KGKVTGILGPNGIGKSTALKILsGEL-KPNLGDYDEEPSWDEVLK-----RFRGTELQDYFKK---LAngEIKVahkPQY 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 111 VEL-PLIYAGvNVS---KR---REQAKQFLEKVGLGRRIKHLPSELSGGQKQRVAIARALVNDPSIILADEPTGALDTKT 183
Cdd:COG1245 169 VDLiPKVFKG-TVRellEKvdeRGKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIYQ 247
|
170 180 190
....*....|....*....|....*....|
gi 2076047389 184 GQQIMELLTELNKEGKTIIMVTHEPEIADF 213
Cdd:COG1245 248 RLNVARLIRELAEEGKYVLVVEHDLAILDY 277
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
21-213 |
3.02e-14 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 71.42 E-value: 3.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 21 GDQVLKVLKGINLTVYEGEFLAIMGPSGSGKSTLMNIigLLDRPTSGdYTLHNTKIEILNDRE--LAKVRndeiGFVFQQ 98
Cdd:PLN03140 889 TEDRLQLLREVTGAFRPGVLTALMGVSGAGKTTLMDV--LAGRKTGG-YIEGDIRISGFPKKQetFARIS----GYCEQN 961
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 99 FFLLAKLTalqnVELPLIYAGV-----NVSKRR-----EQAKQFLEKVGLGRRIKHLP--SELSGGQKQRVAIARALVND 166
Cdd:PLN03140 962 DIHSPQVT----VRESLIYSAFlrlpkEVSKEEkmmfvDEVMELVELDNLKDAIVGLPgvTGLSTEQRKRLTIAVELVAN 1037
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2076047389 167 PSIILADEPTGALDTKTGQQIMELLTELNKEGKTIIMVTHEPEIADF 213
Cdd:PLN03140 1038 PSIIFMDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQPSIDIF 1084
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
9-236 |
3.87e-14 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 71.21 E-value: 3.87e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 9 MQLSNIVKSYQNGDQVlKVLKGINLTVYEGEFLAIMGPSGSGKSTLMNIIGLLDRPTSGDYTLHNTkiEILNDRELAKVR 88
Cdd:PTZ00265 383 IQFKNVRFHYDTRKDV-EIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDS--HNLKDINLKWWR 459
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 89 NdEIGFVFQQFFLLAK---------LTALQNVELPLIYAGVNVSKRRE-----------------------------QAK 130
Cdd:PTZ00265 460 S-KIGVVSQDPLLFSNsiknnikysLYSLKDLEALSNYYNEDGNDSQEnknkrnscrakcagdlndmsnttdsneliEMR 538
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 131 QFLE------------KVGLGRRIKHLP-----------SELSGGQKQRVAIARALVNDPSIILADEPTGALDTKTGQQI 187
Cdd:PTZ00265 539 KNYQtikdsevvdvskKVLIHDFVSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLV 618
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 2076047389 188 MELLTELN-KEGKTIIMVTHEPEIADFATRKIIIRDGDITTDTTASVVID 236
Cdd:PTZ00265 619 QKTINNLKgNENRITIIIAHRLSTIRYANTIFVLSNRERGSTVDVDIIGE 668
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
27-223 |
5.17e-14 |
|
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: 69.50 E-value: 5.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 27 VLKGINLTVYEGEFLAIMGPSGSGKSTL-MNIIGLLDrPTSGDYTlHNTKIEILNDREL---AKVRNDEI-GFVFQQFFL 101
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLlMLILGELE-PSEGKIK-HSGRISFSSQFSWimpGTIKENIIfGVSYDEYRY 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 102 LAKLTALQNVElpliyagvNVSKRREQAKQFLEKVGLgrrikhlpsELSGGQKQRVAIARALVNDPSIILADEPTGALDT 181
Cdd:cd03291 130 KSVVKACQLEE--------DITKFPEKDNTVLGEGGI---------TLSGGQRARISLARAVYKDADLYLLDSPFGYLDV 192
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2076047389 182 KTGQQIMELLTELNKEGKTIIMVTHEPEIADFATRKIIIRDG 223
Cdd:cd03291 193 FTEKEIFESCVCKLMANKTRILVTSKMEHLKKADKILILHEG 234
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
32-216 |
1.07e-13 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 69.66 E-value: 1.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 32 NLTVYEGEFLAIMGPSGSGKSTLMNIIGLLDRPTSGDYTLHNTKIEILNDRELAKVRNDEigfvFQQFF--LLAK----- 104
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLSFEQLQKLVSDE----WQRNNtdMLSPgeddt 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 105 -LTALQnvelpLIYAGVNVSKRREQ-AKQFLEKVGLGRRIKHLpselSGGQKQRVAIARALVNDPSIILADEPTGALDTK 182
Cdd:PRK10938 99 gRTTAE-----IIQDEVKDPARCEQlAQQFGITALLDRRFKYL----STGETRKTLLCQALMSEPDLLILDEPFDGLDVA 169
|
170 180 190
....*....|....*....|....*....|....*
gi 2076047389 183 TGQQIMELLTELNKEGKTIIMVTHE-PEIADFATR 216
Cdd:PRK10938 170 SRQQLAELLASLHQSGITLVLVLNRfDEIPDFVQF 204
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
28-226 |
1.11e-13 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 69.97 E-value: 1.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 28 LKGINLTVYEGEFLAIMGPSGSGKSTLMN-IIGLLDRpTSGDYTLHNTkieilndrelakvrndeIGFVFQQFFLlaklt 106
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSaLLAEMDK-VEGHVHMKGS-----------------VAYVPQQAWI----- 710
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 107 alQNVEL-PLIYAGVNVSKRREQakQFLEKVGLGRRIKHLPS-----------ELSGGQKQRVAIARALVNDPSIILADE 174
Cdd:TIGR00957 711 --QNDSLrENILFGKALNEKYYQ--QVLEACALLPDLEILPSgdrteigekgvNLSGGQKQRVSLARAVYSNADIYLFDD 786
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2076047389 175 PTGALDTKTGQQIMELLT--ELNKEGKTIIMVTHE----PEIaDFAtrkIIIRDGDIT 226
Cdd:TIGR00957 787 PLSAVDAHVGKHIFEHVIgpEGVLKNKTRILVTHGisylPQV-DVI---IVMSGGKIS 840
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
25-223 |
1.33e-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: 67.36 E-value: 1.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 25 LKVLKGINLTVYEGEFLAIMGPSGSGKSTLMNIIgLLDRPTSGDYTLHNTKIEILNDRELAKVRND-EIGFVFQQFFLLa 103
Cdd:cd03290 14 LATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAI-LGEMQTLEGKVHWSNKNESEPSFEATRSRNRySVAYAAQKPWLL- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 104 KLTALQNVELpliyaGVNVSKRREQAkqFLEKVGLGRRIKHLPS-----------ELSGGQKQRVAIARALVNDPSIILA 172
Cdd:cd03290 92 NATVEENITF-----GSPFNKQRYKA--VTDACSLQPDIDLLPFgdqteigergiNLSGGQRQRICVARALYQNTNIVFL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2076047389 173 DEPTGALDTKTGQQIME--LLTELNKEGKTIIMVTHEPEIADFATRKIIIRDG 223
Cdd:cd03290 165 DDPFSALDIHLSDHLMQegILKFLQDDKRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
28-225 |
1.42e-13 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 69.53 E-value: 1.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 28 LKGINLTVYEGEFLAIMGPSGSGKSTLMNIIGLLDRPTSGdytlhntKIEILNDRELAKVRNDeigfvfqqffLLAKLTA 107
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKG-------TVDIKGSAALIAISSG----------LNGQLTG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 108 LQNVELPLIYAGVNVSKRREQAKQFLEKVGLGRRIKHLPSELSGGQKQRVAIARALVNDPSIILADEPTGALDTKTGQQI 187
Cdd:PRK13545 103 IENIELKGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKC 182
|
170 180 190
....*....|....*....|....*....|....*....
gi 2076047389 188 MELLTELNKEGKTIIMVTHE-PEIADFATRKIIIRDGDI 225
Cdd:PRK13545 183 LDKMNEFKEQGKTIFFISHSlSQVKSFCTKALWLHYGQV 221
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
7-226 |
1.70e-13 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 66.90 E-value: 1.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 7 QLMQLSNIVKSYQNGDQVLKVLKGINLTVYEGEFLAIMGPSGSGKSTLMNII-GLLDRPTSGDYTLHNTKIEILndrELA 85
Cdd:cd03233 2 STLSWRNISFTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALaNRTEGNVSVEGDIHYNGIPYK---EFA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 86 KVRNDEIGFVFQQFFLLAKLTALQNVELPLiyagvnvskrREQAKQFLEKVglgrrikhlpselSGGQKQRVAIARALVN 165
Cdd:cd03233 79 EKYPGEIIYVSEEDVHFPTLTVRETLDFAL----------RCKGNEFVRGI-------------SGGERKRVSIAEALVS 135
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2076047389 166 DPSIILADEPTGALDTKTGQQIMELLTELNKEGKTIIMVT---HEPEIADFATRKIIIRDGDIT 226
Cdd:cd03233 136 RASVLCWDNSTRGLDSSTALEILKCIRTMADVLKTTTFVSlyqASDEIYDLFDKVLVLYEGRQI 199
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
16-232 |
2.64e-13 |
|
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: 67.05 E-value: 2.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 16 KSYQNGDQVLKVLKGinlTVYEGEFLAIMGPSGSGKSTLMNIIGLLDRPTSGDytlhntkIEILNDRELAKVRNDEIGFV 95
Cdd:cd03237 6 MKKTLGEFTLEVEGG---SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGD-------IEIELDTVSYKPQYIKADYE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 96 FQQFFLLAKLTALqnvelpliyAGVNVSKRREQAKQF-LEKVgLGRRIkhlpSELSGGQKQRVAIARALVNDPSIILADE 174
Cdd:cd03237 76 GTVRDLLSSITKD---------FYTHPYFKTEIAKPLqIEQI-LDREV----PELSGGELQRVAIAACLSKDADIYLLDE 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2076047389 175 PTGALDTKtgQQIM-----ELLTELNKegKTIIMVTHEPEIADFATRKIIIRDGDITTDTTAS 232
Cdd:cd03237 142 PSAYLDVE--QRLMaskviRRFAENNE--KTAFVVEHDIIMIDYLADRLIVFEGEPSVNGVAN 200
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
8-216 |
5.06e-13 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 67.67 E-value: 5.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 8 LMQLSNIVKSYqnGDQVLkvLKGINLTVYEGEFLAIMGPSGSGKSTLMNIIglldrptSGDYTLHNTKIEILNDRELAKV 87
Cdd:PRK11147 3 LISIHGAWLSF--SDAPL--LDNAELHIEDNERVCLVGRNGAGKSTLMKIL-------NGEVLLDDGRIIYEQDLIVARL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 88 RND------------------EIGFVFQQFFLLAKLTALQNVELPLiyagvnvsKRREQAKQFLEKVGLGR---RIK--- 143
Cdd:PRK11147 72 QQDpprnvegtvydfvaegieEQAEYLKRYHDISHLVETDPSEKNL--------NELAKLQEQLDHHNLWQlenRINevl 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 144 ---HLP-----SELSGGQKQRVAIARALVNDPSIILADEPTGALDTKTgqqiMELLTELNKEGK-TIIMVTHEPE-IADF 213
Cdd:PRK11147 144 aqlGLDpdaalSSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIET----IEWLEGFLKTFQgSIIFISHDRSfIRNM 219
|
...
gi 2076047389 214 ATR 216
Cdd:PRK11147 220 ATR 222
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
31-230 |
7.07e-13 |
|
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: 67.13 E-value: 7.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 31 INLTVYEGEFLAIMGPSGSGKSTLMNIIGLLDRPTSGdytlhntkiEI-LNDRELAKVRNDE----IGFVFQQFFLLAKL 105
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESG---------EIlLDGQPVTADNREAyrqlFSAVFSDFHLFDRL 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 106 TALQNVELPliyagvnvskrrEQAKQFLEKVGLGRRIKH-----LPSELSGGQKQRVAIARALVNDPSIILADEptGALD 180
Cdd:COG4615 422 LGLDGEADP------------ARARELLERLELDHKVSVedgrfSTTDLSQGQRKRLALLVALLEDRPILVFDE--WAAD 487
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2076047389 181 tktgQ-----QI--MELLTELNKEGKTIIMVTHEPEIADFATRKIIIRDGDITTDTT 230
Cdd:COG4615 488 ----QdpefrRVfyTELLPELKARGKTVIAISHDDRYFDLADRVLKMDYGKLVELTG 540
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
4-223 |
7.08e-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: 67.12 E-value: 7.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 4 EKKQLMQLSNIVKSYqnGDQVLKVLKGinlTVYEGEFLAIMGPSGSGKSTLMNIIGLLDRPTSGDYTLhNTKI-----EI 78
Cdd:COG1245 337 EEETLVEYPDLTKSY--GGFSLEVEGG---EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDE-DLKIsykpqYI 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 79 LNDRE------LAKVRNDEIGfvfqqffllaklTALQNVELpliyagvnvskrreqakqfLEKVGLGRRIKHLPSELSGG 152
Cdd:COG1245 411 SPDYDgtveefLRSANTDDFG------------SSYYKTEI-------------------IKPLGLEKLLDKNVKDLSGG 459
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2076047389 153 QKQRVAIARALVNDPSIILADEPTGALD-------TKTGQQIMElltelnKEGKTIIMVTHEPEIADFATRKIIIRDG 223
Cdd:COG1245 460 ELQRVAIAACLSRDADLYLLDEPSAHLDveqrlavAKAIRRFAE------NRGKTAMVVDHDIYLIDYISDRLMVFEG 531
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
27-235 |
7.62e-13 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 66.00 E-value: 7.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 27 VLKGINLTVYEGEFLAIMGPSGSGKSTLMNII-GLLDRP-------TSGDYTLHNTKIEILNDRELAKVR-----NDEIG 93
Cdd:PRK13547 16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALaGDLTGGgaprgarVTGDVTLNGEPLAAIDAPRLARLRavlpqAAQPA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 94 FVF--QQFFLLAKLTALQNvelpliyAGVNVSKRREQAKQFLEKVGLGRRIKHLPSELSGGQKQRVAIARALVN------ 165
Cdd:PRK13547 96 FAFsaREIVLLGRYPHARR-------AGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLAQlwpphd 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2076047389 166 ---DPSIILADEPTGALDTKTGQQIMELLTELNKEGKT-IIMVTHEPEI-ADFATRKIIIRDGDITTDTTASVVI 235
Cdd:PRK13547 169 aaqPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLgVLAIVHDPNLaARHADRIAMLADGAIVAHGAPADVL 243
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
27-206 |
9.90e-13 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 66.98 E-value: 9.90e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 27 VLKGINLTVYEGEFLAIMGPSGSGKSTLMNII--------------------------------------------GLLD 62
Cdd:PTZ00265 1183 IYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLmrfydlkndhhivfknehtndmtneqdyqgdeeqnvgmknvnefSLTK 1262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 63 RPTSG-DYTLHNTKIEIL------NDRELAKVRNdeigfvfqQFFLLAKLTALQNVElplIYAGVNVSKR---REQAKQF 132
Cdd:PTZ00265 1263 EGGSGeDSTVFKNSGKILldgvdiCDYNLKDLRN--------LFSIVSQEPMLFNMS---IYENIKFGKEdatREDVKRA 1331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 133 LEKVGLGRRIKHLPSE-----------LSGGQKQRVAIARALVNDPSIILADEPTGALDTKTGQQIMELLTEL-NKEGKT 200
Cdd:PTZ00265 1332 CKFAAIDEFIESLPNKydtnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIkDKADKT 1411
|
....*.
gi 2076047389 201 IIMVTH 206
Cdd:PTZ00265 1412 IITIAH 1417
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
26-228 |
1.12e-12 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 66.49 E-value: 1.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 26 KVLKGINLTVYEGEFLAIMGPSGSGKSTLMN-IIGLLDRPTSGDYTLHNTKIEILNDRE-----LAKVRNDEigfvfQQF 99
Cdd:PRK13549 276 KRVDDVSFSLRRGEILGIAGLVGAGRTELVQcLFGAYPGRWEGEIFIDGKPVKIRNPQQaiaqgIAMVPEDR-----KRD 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 100 FLLAKLTALQNVELPLI--YAG---VNVSKRREQAKQFLEKVglgrRIK----HLP-SELSGGQKQRVAIARALVNDPSI 169
Cdd:PRK13549 351 GIVPVMGVGKNITLAALdrFTGgsrIDDAAELKTILESIQRL----KVKtaspELAiARLSGGNQQKAVLAKCLLLNPKI 426
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 170 ILADEPTGALDTKTGQQIMELLTELNKEGKTIIMVTHE-PEIADFATRKIIIRDGDITTD 228
Cdd:PRK13549 427 LILDEPTRGIDVGAKYEIYKLINQLVQQGVAIIVISSElPEVLGLSDRVLVMHEGKLKGD 486
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
24-223 |
1.37e-12 |
|
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: 66.86 E-value: 1.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 24 VLKVLKGINLTVYEGEFLAIMGPSGSGKSTL-MNIIGLLDrPTSGDYTlHNTKIEILNDREL---AKVRNDEI-GFVFQQ 98
Cdd:TIGR01271 438 VTPVLKNISFKLEKGQLLAVAGSTGSGKSSLlMMIMGELE-PSEGKIK-HSGRISFSPQTSWimpGTIKDNIIfGLSYDE 515
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 99 FFLLAKLTALQNVElpliyagvNVSKRREQAKQFLEKVGLgrrikhlpsELSGGQKQRVAIARALVNDPSIILADEPTGA 178
Cdd:TIGR01271 516 YRYTSVIKACQLEE--------DIALFPEKDKTVLGEGGI---------TLSGGQRARISLARAVYKDADLYLLDSPFTH 578
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2076047389 179 LDTKTGQQIMELLTELNKEGKTIIMVTHEPEIADFATRKIIIRDG 223
Cdd:TIGR01271 579 LDVVTEKEIFESCLCKLMSNKTRILVTSKLEHLKKADKILLLHEG 623
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
37-213 |
1.53e-12 |
|
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: 65.08 E-value: 1.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 37 EGEFLAIMGPSGSGKSTLMNIIGLLDRPTSGDYTLHNTKIEILND---REL----AKVRNDEIGFVFQQffllakltalQ 109
Cdd:cd03236 25 EGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFDDPPDWDEILDEfrgSELqnyfTKLLEGDVKVIVKP----------Q 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 110 NVEL-PLIYAG-----VNVSKRREQAKQFLEKVGLGRRIKHLPSELSGGQKQRVAIARALVNDPSIILADEPTGALDTKT 183
Cdd:cd03236 95 YVDLiPKAVKGkvgelLKKKDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQ 174
|
170 180 190
....*....|....*....|....*....|
gi 2076047389 184 GQQIMELLTELNKEGKTIIMVTHEPEIADF 213
Cdd:cd03236 175 RLNAARLIRELAEDDNYVLVVEHDLAVLDY 204
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
26-222 |
2.05e-12 |
|
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: 63.97 E-value: 2.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 26 KVLKGINLTVYEGEFLAIMGPSGSGKSTLMNIIGLLDRPTSGDYTLHNTKIEILndrELAKVRNdEIGFVFQQffllakl 105
Cdd:cd03369 22 PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTI---PLEDLRS-SLTIIPQD------- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 106 talqnvelPLIYAGVNVSKRREQAKQFLEKVGLGRRIKHLPSELSGGQKQRVAIARALVNDPSIILADEPTGALDTKTGQ 185
Cdd:cd03369 91 --------PTLFSGTIRSNLDPFDEYSDEEIYGALRVSEGGLNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDA 162
|
170 180 190
....*....|....*....|....*....|....*...
gi 2076047389 186 QIMELLTELNKeGKTIIMVTHE-PEIADFAtrKIIIRD 222
Cdd:cd03369 163 LIQKTIREEFT-NSTILTIAHRlRTIIDYD--KILVMD 197
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
4-223 |
2.79e-12 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 65.60 E-value: 2.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 4 EKKQLMQLSNIVKSYqnGDQVLKVLKGinlTVYEGEFLAIMGPSGSGKSTLMNIIGLLDRPTSGdytlhntkiEILNDRE 83
Cdd:PRK13409 336 ERETLVEYPDLTKKL--GDFSLEVEGG---EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEG---------EVDPELK 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 84 LA----KVRNDEIGFVFQqffLLAKLTAlqNVELPLIYAgvnvskrreqakQFLEKVGLGRRIKHLPSELSGGQKQRVAI 159
Cdd:PRK13409 402 ISykpqYIKPDYDGTVED---LLRSITD--DLGSSYYKS------------EIIKPLQLERLLDKNVKDLSGGELQRVAI 464
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2076047389 160 ARALVNDPSIILADEPTGALD-------TKTGQQIMElltelnKEGKTIIMVTHEPEIADFATRKIIIRDG 223
Cdd:PRK13409 465 AACLSRDADLYLLDEPSAHLDveqrlavAKAIRRIAE------EREATALVVDHDIYMIDYISDRLMVFEG 529
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
11-223 |
2.97e-12 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 65.52 E-value: 2.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 11 LSNIVKSYQNgdqvLKVLKGINLTVYEGEFLAIMGPSGSGKSTLMNIIGLLDRPTSGDYTLHNTKIEILNDRELAKvrnD 90
Cdd:PRK10982 1 MSNISKSFPG----VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEALE---N 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 91 EIGFVFQQFFLLAKLTALQNVEL---PLIYAGVNVSKRREQAKQFLEKVGLGRRIKHLPSELSGGQKQRVAIARALVNDP 167
Cdd:PRK10982 74 GISMVHQELNLVLQRSVMDNMWLgryPTKGMFVDQDKMYRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNA 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2076047389 168 SIILADEPTGALDTKTGQQIMELLTELNKEGKTIIMVTHE-PEIADFATRKIIIRDG 223
Cdd:PRK10982 154 KIVIMDEPTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKmEEIFQLCDEITILRDG 210
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
26-225 |
7.30e-12 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 64.41 E-value: 7.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 26 KVLKGINLTVYEGEFLAIMGPSGSGKSTLMNiiGLLdrptsgdytlhnTKIEILNDRELAKvrnDEIGFVFQQ------- 98
Cdd:PTZ00243 674 VLLRDVSVSVPRGKLTVVLGATGSGKSTLLQ--SLL------------SQFEISEGRVWAE---RSIAYVPQQawimnat 736
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 99 ------FFLLAKLTALQNVelpliyagVNVSKRREQAKQFleKVGLGRRIKHLPSELSGGQKQRVAIARALVNDPSIILA 172
Cdd:PTZ00243 737 vrgnilFFDEEDAARLADA--------VRVSQLEADLAQL--GGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLL 806
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2076047389 173 DEPTGALDTKTGQQIME--LLTELnkEGKTIIMVTHEPEIADFATRKIIIRDGDI 225
Cdd:PTZ00243 807 DDPLSALDAHVGERVVEecFLGAL--AGKTRVLATHQVHVVPRADYVVALGDGRV 859
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
26-206 |
8.38e-12 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 63.98 E-value: 8.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 26 KVLKGINLTVYEGEFLAIMGPSGSGKSTLMNIIGLLDRPTSGDYTLH-NTKIEIL----------NDRE-----LAKVRN 89
Cdd:PRK11819 21 QILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPApGIKVGYLpqepqldpekTVREnveegVAEVKA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 90 -----DEIGFVF---QQFF--LLAKLTALQNvelpLIYA--GVNVSKRREQAKQFLekvglgrrikHLP------SELSG 151
Cdd:PRK11819 101 aldrfNEIYAAYaepDADFdaLAAEQGELQE----IIDAadAWDLDSQLEIAMDAL----------RCPpwdakvTKLSG 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2076047389 152 GQKQRVAIARALVNDPSIILADEPTGALDTKTGQQIMELLTELnkEGkTIIMVTH 206
Cdd:PRK11819 167 GERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLEQFLHDY--PG-TVVAVTH 218
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
28-230 |
1.10e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 63.99 E-value: 1.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 28 LKGINLTVYEGEFLAIMGPSGSGKSTLMN-IIGLLDRPTSGDYTLHNT-----KIE-ILNdrelAKVRnDEI--GFVFQQ 98
Cdd:PLN03130 633 LSNINLDVPVGSLVAIVGSTGEGKTSLISaMLGELPPRSDASVVIRGTvayvpQVSwIFN----ATVR-DNIlfGSPFDP 707
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 99 --FFLLAKLTALQNvELPLIYAGvnvskrreqakqflEKVGLGRRikhlPSELSGGQKQRVAIARALVNDPSIILADEPT 176
Cdd:PLN03130 708 erYERAIDVTALQH-DLDLLPGG--------------DLTEIGER----GVNISGGQKQRVSMARAVYSNSDVYIFDDPL 768
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2076047389 177 GALDTKTGQQIMELLTELNKEGKTIIMVTHEPEIADFATRKIIIRDGDITTDTT 230
Cdd:PLN03130 769 SALDAHVGRQVFDKCIKDELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGT 822
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
22-207 |
1.14e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 61.89 E-value: 1.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 22 DQVLkvLKGINLTVYEGEFLAIMGPSGSGKSTLMNIIGLLDRPTSGDYTLHNTKIeilnDRELAKVRNdEIGFVFQQFFL 101
Cdd:PRK13540 13 DQPL--LQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSI----KKDLCTYQK-QLCFVGHRSGI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 102 LAKLTALQNVelpliYAGVNVSKRREQAKQFLEKVGLGRRIKHLPSELSGGQKQRVAIARALVNDPSIILADEPTGALDT 181
Cdd:PRK13540 86 NPYLTLRENC-----LYDIHFSPGAVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDE 160
|
170 180
....*....|....*....|....*.
gi 2076047389 182 KTGQQIMELLTELNKEGKTIIMVTHE 207
Cdd:PRK13540 161 LSLLTIITKIQEHRAKGGAVLLTSHQ 186
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
31-206 |
1.47e-11 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 63.61 E-value: 1.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 31 INLTVYEGE---FLaimGPSGSGKSTLMNII-GLLDrPTSGDYTLHNTKIEIlNDRELAKvrndEIGFVFQQFFLLAKLT 106
Cdd:NF033858 285 VSFRIRRGEifgFL---GSNGCGKSTTMKMLtGLLP-ASEGEAWLFGQPVDA-GDIATRR----RVGYMSQAFSLYGELT 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 107 ALQNVELpliYA---GVNVSKRREQAKQFLEKVGLGRRIKHLPSELSGGQKQRVAIARALVNDPSIILADEPTGALDTKT 183
Cdd:NF033858 356 VRQNLEL---HArlfHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVA 432
|
170 180
....*....|....*....|....
gi 2076047389 184 GQQIMELLTELNKE-GKTIIMVTH 206
Cdd:NF033858 433 RDMFWRLLIELSREdGVTIFISTH 456
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
27-213 |
1.54e-11 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 62.12 E-value: 1.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 27 VLKGINLTVYEGEFLAIMGPSGSGKSTLMNIIGLLD--RPTSGDYTLHNTKIEILNDRE-------LAKVRNDEIGFVFQ 97
Cdd:PRK09580 16 ILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLELSPEDragegifMAFQYPVEIPGVSN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 98 QFFLLAKLTALQNvelpliYAGVNVSKRREQAKQFLEKVglgrRIKHLPSEL---------SGGQKQRVAIARALVNDPS 168
Cdd:PRK09580 96 QFFLQTALNAVRS------YRGQEPLDRFDFQDLMEEKI----ALLKMPEDLltrsvnvgfSGGEKKRNDILQMAVLEPE 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2076047389 169 IILADEPTGALDTKTGQQIMELLTELNKEGKTIIMVTHEPEIADF 213
Cdd:PRK09580 166 LCILDESDSGLDIDALKIVADGVNSLRDGKRSFIIVTHYQRILDY 210
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
34-213 |
3.92e-11 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 62.13 E-value: 3.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 34 TVYEGEFLAIMGPSGSGKSTLMNII-GLLdRPTSGDYTLHNTKIEILnDR----EL----AKVRNDEIGFVFQqffllak 104
Cdd:PRK13409 95 IPKEGKVTGILGPNGIGKTTAVKILsGEL-IPNLGDYEEEPSWDEVL-KRfrgtELqnyfKKLYNGEIKVVHK------- 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 105 ltaLQNVEL-PLIYAGvNVS----------KRREQAKQF-LEKVgLGRRIkhlpSELSGGQKQRVAIARALVNDPSIILA 172
Cdd:PRK13409 166 ---PQYVDLiPKVFKG-KVRellkkvdergKLDEVVERLgLENI-LDRDI----SELSGGELQRVAIAAALLRDADFYFF 236
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2076047389 173 DEPTGALDTKTGQQIMELLTELNkEGKTIIMVTHEPEIADF 213
Cdd:PRK13409 237 DEPTSYLDIRQRLNVARLIRELA-EGKYVLVVEHDLAVLDY 276
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
37-221 |
4.40e-11 |
|
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: 59.30 E-value: 4.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 37 EGEFLAIMGPSGSGKSTLMNIIGLLdrptsgdytlhntkieilndrelakvrndeigFVFQQFFLLAKLTALQNVELPLI 116
Cdd:cd03227 20 EGSLTIITGPNGSGKSTILDAIGLA--------------------------------LGGAQSATRRRSGVKAGCIVAAV 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 117 YAGVNVSkrREQakqflekvglgrrikhlpseLSGGQKQRVAIARAL----VNDPSIILADEPTGALDTKTGQQIMELLT 192
Cdd:cd03227 68 SAELIFT--RLQ--------------------LSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALAEAIL 125
|
170 180
....*....|....*....|....*....
gi 2076047389 193 ELNKEGKTIIMVTHEPEIADFATRKIIIR 221
Cdd:cd03227 126 EHLVKGAQVIVITHLPELAELADKLIHIK 154
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
5-223 |
5.24e-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: 61.95 E-value: 5.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 5 KKQLMQLSNIVKSYQNGDQvlKVLKGINLTVYEGEFLAIMGPSGSGKSTLMNIIGLLDRPTSGDYTLHNTKIeILNDREL 84
Cdd:TIGR01257 1934 KTDILRLNELTKVYSGTSS--PAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSI-LTNISDV 2010
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 85 akvrNDEIGFVFQQFFLLAKLTALQNVELPLIYAGVNVSKRREQAKQFLEKVGLGRRIKHLPSELSGGQKQRVAIARALV 164
Cdd:TIGR01257 2011 ----HQNMGYCPQFDAIDDLLTGREHLYLYARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALI 2086
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 165 NDPSIILADEPTGALDTKTGQQIMELLTELNKEGKTIIMVTHEPEIAD-FATRKIIIRDG 223
Cdd:TIGR01257 2087 GCPPLVLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEaLCTRLAIMVKG 2146
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
28-230 |
1.46e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 60.76 E-value: 1.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 28 LKGINLTVYEGEFLAIMGPSGSGKSTLMN-IIGLLDRPTSGDYTLHNTKIE------ILNdrelAKVRNDEI---GFVFQ 97
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISaMLGELSHAETSSVVIRGSVAYvpqvswIFN----ATVRENILfgsDFESE 708
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 98 QFFLLAKLTALQNvELPLiYAGVNVSKrreqakqflekvgLGRRikhlPSELSGGQKQRVAIARALVNDPSIILADEPTG 177
Cdd:PLN03232 709 RYWRAIDVTALQH-DLDL-LPGRDLTE-------------IGER----GVNISGGQKQRVSMARAVYSNSDIYIFDDPLS 769
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2076047389 178 ALDTKTGQQIMELLTELNKEGKTIIMVTHEPEIADFATRKIIIRDGDITTDTT 230
Cdd:PLN03232 770 ALDAHVAHQVFDSCMKDELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGT 822
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
45-206 |
1.87e-10 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 59.91 E-value: 1.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 45 GPSGSGKSTLMNIIGLLDRPTSGDYTLHNtkieilNDReLAKVRNDEigFVFQQFFLL-------AKLTALqNVELPLIY 117
Cdd:PRK15064 34 GANGCGKSTFMKILGGDLEPSAGNVSLDP------NER-LGKLRQDQ--FAFEEFTVLdtvimghTELWEV-KQERDRIY 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 118 AGVNVS-----KRREQAKQFLEKVG-----------LGRRI---KH--LPSELSGGQKQRVAIARALVNDPSIILADEPT 176
Cdd:PRK15064 104 ALPEMSeedgmKVADLEVKFAEMDGytaearagellLGVGIpeeQHygLMSEVAPGWKLRVLLAQALFSNPDILLLDEPT 183
|
170 180 190
....*....|....*....|....*....|
gi 2076047389 177 GALDTKTgqqIMELLTELNKEGKTIIMVTH 206
Cdd:PRK15064 184 NNLDINT---IRWLEDVLNERNSTMIIISH 210
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
149-223 |
4.07e-10 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 58.97 E-value: 4.07e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2076047389 149 LSGGQKQRVAIARALVNDPSIILADEPTGALDTKTGQQIMELLTELNKEGKTIIMVTHE-PEIADFATRKIIIRDG 223
Cdd:PRK10982 392 LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEmPELLGITDRILVMSNG 467
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
131-218 |
6.28e-10 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 56.56 E-value: 6.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 131 QFLEKVGLGR-RIKHLPSELSGGQKQRVAIARALVNDP--SIILADEPTGALDTKTGQQIMELLTELNKEGKTIIMVTHE 207
Cdd:cd03238 69 QFLIDVGLGYlTLGQKLSTLSGGELQRVKLASELFSEPpgTLFILDEPSTGLHQQDINQLLEVIKGLIDLGNTVILIEHN 148
|
90
....*....|.
gi 2076047389 208 PEIADFATRKI 218
Cdd:cd03238 149 LDVLSSADWII 159
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
26-228 |
1.08e-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: 57.91 E-value: 1.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 26 KVLKGINLTVYEGEFLAIMGPSGSGKSTLMN-IIGLLDRPTSGDYTLHNTKIEILNDRE-----LAKVRNDEigfvfQQF 99
Cdd:TIGR02633 274 KRVDDVSFSLRRGEILGVAGLVGAGRTELVQaLFGAYPGKFEGNVFINGKPVDIRNPAQairagIAMVPEDR-----KRH 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 100 FLLAKLTALQNVELPLIYAGVNVSKRREQAkqflEKVGLGRRIKHLP----------SELSGGQKQRVAIARALVNDPSI 169
Cdd:TIGR02633 349 GIVPILGVGKNITLSVLKSFCFKMRIDAAA----ELQIIGSAIQRLKvktaspflpiGRLSGGNQQKAVLAKMLLTNPRV 424
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 170 ILADEPTGALDTKTGQQIMELLTELNKEGKTIIMVTHE-PEIADFATRKIIIRDGDITTD 228
Cdd:TIGR02633 425 LILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSElAEVLGLSDRVLVIGEGKLKGD 484
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
27-206 |
1.64e-09 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 56.01 E-value: 1.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 27 VLKGINLTVYEGEFLAIMGPSGSGKSTLMNIIGLLDRPTSGDY---TLHNTKIEilndrelakvRNDEIGFVFQQFFLLA 103
Cdd:PRK13543 26 VFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIqidGKTATRGD----------RSRFMAYLGHLPGLKA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 104 KLTALQNVELpliYAGVNVSKRREQAKQFLEKVGLGRRIKHLPSELSGGQKQRVAIARALVNDPSIILADEPTGALDTKT 183
Cdd:PRK13543 96 DLSTLENLHF---LCGLHGRRAKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEG 172
|
170 180
....*....|....*....|...
gi 2076047389 184 GQQIMELLTELNKEGKTIIMVTH 206
Cdd:PRK13543 173 ITLVNRMISAHLRGGGAALVTTH 195
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
1-228 |
2.38e-09 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 56.67 E-value: 2.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 1 MSHEKKQLMQLSNIVKSYQNgdqvLKVLKGINLTVYEGEFLAIMGPSGSGK---STLMNIIGlldrPTSGDYTLHnTKIE 77
Cdd:NF000106 6 ISNGARNAVEVRGLVKHFGE----VKAVDGVDLDVREGTVLGVLGP*GAA**rgALPAHV*G----PDAGRRPWR-F*TW 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 78 ILNDRELAKVrndeIGFvfQQFFLLAKLTALQNVE-LPLIYAGVNVSKR--REQAKQFLEKVGLGRRIKHLPSELSGGQK 154
Cdd:NF000106 77 CANRRALRRT----IG*--HRPVR*GRRESFSGREnLYMIGR*LDLSRKdaRARADELLERFSLTEAAGRAAAKYSGGMR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2076047389 155 QRVAIARALVNDPSIILADEPTGALDTKTGQQIMELLTELNKEGKTIIMVTHEPEIAD-FATRKIIIRDGDITTD 228
Cdd:NF000106 151 RRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEqLAHELTVIDRGRVIAD 225
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
28-213 |
3.13e-09 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 55.34 E-value: 3.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 28 LKGINLTVYEGEFLAIMGPSGSGKSTLM---------------------NIIGLLDRPtsgDYTlhntKIE------ILN 80
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSSLAfdtiyaegqrryveslsayarQFLGQMDKP---DVD----SIEglspaiAID 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 81 DRELAKVRNDEIGFVfqqffllaklTALQNVeLPLIYAGVNVSKRReqakQFLEKVGLG-----RRIkhlpSELSGGQKQ 155
Cdd:cd03270 84 QKTTSRNPRSTVGTV----------TEIYDY-LRLLFARVGIRERL----GFLVDVGLGyltlsRSA----PTLSGGEAQ 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2076047389 156 RVAIARALVNDPSIIL--ADEPTGALDTKTGQQIMELLTELNKEGKTIIMVTHEPEI---ADF 213
Cdd:cd03270 145 RIRLATQIGSGLTGVLyvLDEPSIGLHPRDNDRLIETLKRLRDLGNTVLVVEHDEDTiraADH 207
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
38-224 |
3.34e-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: 3.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 38 GEFLAIMGPSGSGKSTLMNIIGlldrptsgdytlhntkieilndRELAKvrnDEIGFVFqqffllakltalqnvelpliy 117
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALA----------------------RELGP---PGGGVIY--------------------- 35
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 118 agVNVSKRREQAKQFLEKVGLGRRikhlPSELSGGQKQRVAIARALVNDPSIILADEPTGALDTKTGQQIMELLT----- 192
Cdd:smart00382 36 --IDGEDILEEVLDQLLLIIVGGK----KASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEElrlll 109
|
170 180 190
....*....|....*....|....*....|....*....
gi 2076047389 193 -ELNKEGKTIIMVTH------EPEIADFATRKIIIRDGD 224
Cdd:smart00382 110 lLKSEKNLTVILTTNdekdlgPALLRRRFDRRIVLLLIL 148
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
41-207 |
4.27e-09 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 56.02 E-value: 4.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 41 LAIMGPSGSGKSTLMNIIGLLDRPTSGdyTLHNTkieilndrelAKVRNDeigfVFQQFfllaKLTALQNVELPLIY--- 117
Cdd:PLN03073 538 IAMVGPNGIGKSTILKLISGELQPSSG--TVFRS----------AKVRMA----VFSQH----HVDGLDLSSNPLLYmmr 597
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 118 --AGVNVSKRREQAKQFlekvGLGRRIKHLPS-ELSGGQKQRVAIARALVNDPSIILADEPTGALDTKTGQQIMELLTeL 194
Cdd:PLN03073 598 cfPGVPEQKLRAHLGSF----GVTGNLALQPMyTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEALIQGLV-L 672
|
170
....*....|...
gi 2076047389 195 NKEGktIIMVTHE 207
Cdd:PLN03073 673 FQGG--VLMVSHD 683
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1-226 |
5.42e-09 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 55.83 E-value: 5.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 1 MSHEKKQLMQLSNIVKSYQNGDQVLKV--LKG-----INLTVYEGEFLAIMGPSGSGKSTLMNIIGLLDRPTSGDYTLHN 73
Cdd:PRK15439 245 LSASQKLWLELPGNRRQQAAGAPVLTVedLTGegfrnISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNG 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 74 TKIEILNDRE-LAKvrndeiGFVF-----QQ--FFLLAKLT----ALQNVELPLIYAGVNVSKRREQAKQflekvGLGRR 141
Cdd:PRK15439 325 KEINALSTAQrLAR------GLVYlpedrQSsgLYLDAPLAwnvcALTHNRRGFWIKPARENAVLERYRR-----ALNIK 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 142 IKHLPSE---LSGGQKQRVAIARALVNDPSIILADEPTGALDTKTGQQIMELLTELNKEGKTIIMVTHE-PEIADFATRK 217
Cdd:PRK15439 394 FNHAEQAartLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIAAQNVAVLFISSDlEEIEQMADRV 473
|
....*....
gi 2076047389 218 IIIRDGDIT 226
Cdd:PRK15439 474 LVMHQGEIS 482
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
7-183 |
8.22e-09 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 55.33 E-value: 8.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 7 QLMQLSNIVKSYqnGDQVLkvLKGINLTVYEGEFLAIMGPSGSGKSTLMNIIGLLDRPTSGDYTLHNTkieilndrelak 86
Cdd:TIGR03719 321 KVIEAENLTKAF--GDKLL--IDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGET------------ 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 87 VRndeIGFVFQQfflLAKLTALQNVeLPLIYAG---VNVSKRREQAKQFLEKVGL-GRRIKHLPSELSGGQKQRVAIARA 162
Cdd:TIGR03719 385 VK---LAYVDQS---RDALDPNKTV-WEEISGGldiIKLGKREIPSRAYVGRFNFkGSDQQKKVGQLSGGERNRVHLAKT 457
|
170 180
....*....|....*....|.
gi 2076047389 163 LVNDPSIILADEPTGALDTKT 183
Cdd:TIGR03719 458 LKSGGNVLLLDEPTNDLDVET 478
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
148-232 |
1.02e-08 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 52.96 E-value: 1.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 148 ELSGGQKQRVAIARALVNDPSIILADEPTGALDTKTGQQIMELLTELNKEG-KTIIMVTHEPEIADFATRKIIIRDGDIT 226
Cdd:cd03222 71 DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGkKTALVVEHDLAVLDYLSDRIHVFEGEPG 150
|
....*.
gi 2076047389 227 TDTTAS 232
Cdd:cd03222 151 VYGIAS 156
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
9-209 |
1.78e-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: 54.53 E-value: 1.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 9 MQLSNIVKSYQNGDQvlKVLKGINLTVYEGEFLAIMGPSGSGKSTLMniiglldrptSGDYTLHNTKIEI------LNDR 82
Cdd:TIGR01271 1218 MDVQGLTAKYTEAGR--AVLQDLSFSVEGGQRVGLLGRTGSGKSTLL----------SALLRLLSTEGEIqidgvsWNSV 1285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 83 ELAKVRNdEIGFVFQQFFLLAKlTALQNVELPLIYAGvnvskrrEQAKQFLEKVGLGRRIKHLPSEL-----------SG 151
Cdd:TIGR01271 1286 TLQTWRK-AFGVIPQKVFIFSG-TFRKNLDPYEQWSD-------EEIWKVAEEVGLKSVIEQFPDKLdfvlvdggyvlSN 1356
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2076047389 152 GQKQRVAIARALVNDPSIILADEPTGALDTKTGQQIMELLTELNKEGkTIIMVTHEPE 209
Cdd:TIGR01271 1357 GHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNC-TVILSEHRVE 1413
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
9-227 |
2.08e-08 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 53.32 E-value: 2.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 9 MQLSNIVKSYQNGDQVlkVLKGINLTVYEGEFLAIMGPSGSGKSTLMN-IIGLLDrpTSGDYTLHNTKieiLNDRELAKV 87
Cdd:cd03289 3 MTVKDLTAKYTEGGNA--VLENISFSISPGQRVGLLGRTGSGKSTLLSaFLRLLN--TEGDIQIDGVS---WNSVPLQKW 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 88 RNdEIGFVFQQFFLLAKlTALQNVElpliyagVNVSKRREQAKQFLEKVGLGRRIKHLPSEL-----------SGGQKQR 156
Cdd:cd03289 76 RK-AFGVIPQKVFIFSG-TFRKNLD-------PYGKWSDEEIWKVAEEVGLKSVIEQFPGQLdfvlvdggcvlSHGHKQL 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2076047389 157 VAIARALVNDPSIILADEPTGALDTKTGQQIMELLTElNKEGKTIIMVTHEPEIADFATRKIIIRDGDITT 227
Cdd:cd03289 147 MCLARSVLSKAKILLLDEPSAHLDPITYQVIRKTLKQ-AFADCTVILSEHRIEAMLECQRFLVIEENKVRQ 216
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
26-210 |
2.45e-08 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 53.64 E-value: 2.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 26 KVLKGINLTVYEGEFLAIMGPSGSGKSTL-MNIIG-LLDRPTSGDYTLHNTKIEILNDRE-----LAKVRND--EIGFVF 96
Cdd:NF040905 274 KVVDDVSLNVRRGEIVGIAGLMGAGRTELaMSVFGrSYGRNISGTVFKDGKEVDVSTVSDaidagLAYVTEDrkGYGLNL 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 97 ----QQFFLLAKLTALQNvelpliyAGVnVSKRREQ--AKQFLEKVglgrRIKHlPS------ELSGGQKQRVAIARALV 164
Cdd:NF040905 354 iddiKRNITLANLGKVSR-------RGV-IDENEEIkvAEEYRKKM----NIKT-PSvfqkvgNLSGGNQQKVVLSKWLF 420
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2076047389 165 NDPSIILADEPTGALDTKTGQQIMELLTELNKEGKTIIMVTHE-PEI 210
Cdd:NF040905 421 TDPDVLILDEPTRGIDVGAKYEIYTIINELAAEGKGVIVISSElPEL 467
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
4-226 |
3.41e-08 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 53.36 E-value: 3.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 4 EKK---QLMQLSNIVKSYQNGdqvlKVLKGINLTVYEGEFLAIMGPSGSGKSTLMNiiglldrptsgdyTLHNtkiEILN 80
Cdd:PRK15064 312 DKKlhrNALEVENLTKGFDNG----PLFKNLNLLLEAGERLAIIGENGVGKTTLLR-------------TLVG---ELEP 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 81 DRELAK-VRNDEIGFVFQ----QFfllakltalqnvelpliYAGVNVSKRREQAKQflEKVG-------LGR------RI 142
Cdd:PRK15064 372 DSGTVKwSENANIGYYAQdhayDF-----------------ENDLTLFDWMSQWRQ--EGDDeqavrgtLGRllfsqdDI 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 143 KHLPSELSGGQKQRVAIARALVNDPSIILADEPTGALDtktgqqiMELLTELNK-----EGkTIIMVTHEPE-IADFATR 216
Cdd:PRK15064 433 KKSVKVLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMD-------MESIESLNMalekyEG-TLIFVSHDREfVSSLATR 504
|
250
....*....|
gi 2076047389 217 KIIIRDGDIT 226
Cdd:PRK15064 505 IIEITPDGVV 514
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
27-225 |
6.88e-08 |
|
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: 52.64 E-value: 6.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 27 VLKGINLTVYEGEFLAIMGPSGSGKSTLMniIGLLDrptsgdyTLHNTKIEILNDR-ELAKVRNDEIGFvfqqffllaKL 105
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSLT--LGLFR-------INESAEGEIIIDGlNIAKIGLHDLRF---------KI 1362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 106 TALQnvELPLIYAG---VNV----SKRREQAKQFLEKVGLGRRIKHLPSEL-----------SGGQKQRVAIARALVNDP 167
Cdd:TIGR00957 1363 TIIP--QDPVLFSGslrMNLdpfsQYSDEEVWWALELAHLKTFVSALPDKLdhecaeggenlSVGQRQLVCLARALLRKT 1440
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 168 SIILADEPTGALDTKTGQQIMELL-TELnkEGKTIIMVTHE-PEIADFaTRKIIIRDGDI 225
Cdd:TIGR00957 1441 KILVLDEATAAVDLETDNLIQSTIrTQF--EDCTVLTIAHRlNTIMDY-TRVIVLDKGEV 1497
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
17-212 |
7.61e-08 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 52.26 E-value: 7.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 17 SYQNGDQVLkvLKGINLTVYEGEFLAIMGPSGSGKSTLMNI-IGLLdRPTSGdyTLH-NTKIEILndrelakvrndeigf 94
Cdd:PRK11147 326 NYQIDGKQL--VKDFSAQVQRGDKIALIGPNGCGKTTLLKLmLGQL-QADSG--RIHcGTKLEVA--------------- 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 95 VFQQFflLAKLTALQNVElpliyagVNVSkrreQAKQfleKVGLGRRIKHLPS-----------------ELSGGQKQRV 157
Cdd:PRK11147 386 YFDQH--RAELDPEKTVM-------DNLA----EGKQ---EVMVNGRPRHVLGylqdflfhpkramtpvkALSGGERNRL 449
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2076047389 158 AIARALVNDPSIILADEPTGALDTKTgqqiMELLTEL--NKEGkTIIMVTHEPEIAD 212
Cdd:PRK11147 450 LLARLFLKPSNLLILDEPTNDLDVET----LELLEELldSYQG-TVLLVSHDRQFVD 501
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
20-208 |
5.09e-07 |
|
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: 49.75 E-value: 5.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 20 NGDqvlKVLKGINLTVYEGEFLAIMGPSGSGKSTLMNIIGLLdRPTSGDytlhntkieilndrELAKVRNDEIGFVFQQF 99
Cdd:TIGR00954 463 NGD---VLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGEL-WPVYGG--------------RLTKPAKGKLFYVPQRP 524
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 100 FLlakltALQNVELPLIYA-GVNVSKRR----EQAKQFLEKVGLGRRIKHLPS---------ELSGGQKQRVAIARALVN 165
Cdd:TIGR00954 525 YM-----TLGTLRDQIIYPdSSEDMKRRglsdKDLEQILDNVQLTHILEREGGwsavqdwmdVLSGGEKQRIAMARLFYH 599
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2076047389 166 DPSIILADEPTGALDTKTGQQIMELLTELnkeGKTIIMVTHEP 208
Cdd:TIGR00954 600 KPQFAILDECTSAVSVDVEGYMYRLCREF---GITLFSVSHRK 639
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
28-206 |
5.69e-07 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 50.01 E-value: 5.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 28 LKGINLTVYEGEFLAIMGPSGSGKSTLMN-----------------------IIGL--LDR------------PTS--GD 68
Cdd:TIGR00630 624 LKNITVSIPLGLFTCITGVSGSGKSTLINdtlypalanrlngaktvpgrytsIEGLehLDKvihidqspigrtPRSnpAT 703
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 69 YTLHNTKIeilndREL------AKVRndeiGFVFQQFFLLAKLTALQ--------NVE---LPLIYAGVNVSKRR----- 126
Cdd:TIGR00630 704 YTGVFDEI-----RELfaetpeAKVR----GYTPGRFSFNVKGGRCEacqgdgviKIEmhfLPDVYVPCEVCKGKrynre 774
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 127 -------------------EQAKQFLEK-------------VGLGR-RIKHLPSELSGGQKQRVAIARAL---VNDPSII 170
Cdd:TIGR00630 775 tlevkykgkniadvldmtvEEAYEFFEAvpsisrklqtlcdVGLGYiRLGQPATTLSGGEAQRIKLAKELskrSTGRTLY 854
|
250 260 270
....*....|....*....|....*....|....*.
gi 2076047389 171 LADEPTGALDTKTGQQIMELLTELNKEGKTIIMVTH 206
Cdd:TIGR00630 855 ILDEPTTGLHFDDIKKLLEVLQRLVDKGNTVVVIEH 890
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
150-209 |
6.28e-07 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 49.47 E-value: 6.28e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 150 SGGQKQRVAIARALVNDPSIILADEPTGALDTktgQQIMELLTELNKEGKTIIMVTHEPE 209
Cdd:PLN03073 346 SGGWRMRIALARALFIEPDLLLLDEPTNHLDL---HAVLWLETYLLKWPKTFIVVSHARE 402
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
141-214 |
2.24e-06 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 48.29 E-value: 2.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 141 RIKHLP-----SELSGGQKQRVAIARALVN---DPSIILADEPTGALDTKTGQQIMELLTELNKEGKTIIMVTHEPEIAD 212
Cdd:PRK00635 797 GLDYLPlgrplSSLSGGEIQRLKLAYELLApskKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVVIIEHNMHVVK 876
|
..
gi 2076047389 213 FA 214
Cdd:PRK00635 877 VA 878
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
8-207 |
2.26e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 47.86 E-value: 2.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 8 LMQLSNIVKSYqnGDQVlkVLKGINLTVYEGEFLAIMGPSGSGKSTLMNIIGLLDRPTSGDYTL-HNTKIEILNDRELAK 86
Cdd:PRK10636 312 LLKMEKVSAGY--GDRI--ILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLaKGIKLGYFAQHQLEF 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 87 VRNDEIGfvfqqfflLAKLTALQNVELpliyagvnvskrREQAKQFLEKVGL-GRRIKHLPSELSGGQKQRVAIARALVN 165
Cdd:PRK10636 388 LRADESP--------LQHLARLAPQEL------------EQKLRDYLGGFGFqGDKVTEETRRFSGGEKARLVLALIVWQ 447
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2076047389 166 DPSIILADEPTGALDTKTGQQIMELLTELnkEGkTIIMVTHE 207
Cdd:PRK10636 448 RPNLLLLDEPTNHLDLDMRQALTEALIDF--EG-ALVVVSHD 486
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
149-223 |
4.01e-06 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 47.52 E-value: 4.01e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2076047389 149 LSGGQKQRVAIARALVNDPSII--LADEPTGALDTKTGQQIMELLTELNKEGKTIIMVTHEPEIADFATRKIIIRDG 223
Cdd:PRK00635 477 LSGGEQERTALAKHLGAELIGItyILDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEHDEQMISLADRIIDIGPG 553
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
9-224 |
5.91e-06 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 45.68 E-value: 5.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 9 MQLSNIvKSYQNgDQVLKVLKGINLtvyegeflaIMGPSGSGKSTlmnIIGLLDRPTSGDytLHNTKIEILNDRELAKVr 88
Cdd:cd03240 4 LSIRNI-RSFHE-RSEIEFFSPLTL---------IVGQNGAGKTT---IIEALKYALTGE--LPPNSKGGAHDPKLIRE- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 89 NDEIGFVFQQFFLLA--KLTALQNVElplIYAGVNVSKRREQAKQFLEKVGLgrrikhlpseLSGGQKQ------RVAIA 160
Cdd:cd03240 67 GEVRAQVKLAFENANgkKYTITRSLA---ILENVIFCHQGESNWPLLDMRGR----------CSGGEKVlasliiRLALA 133
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2076047389 161 RALVNDPSIILADEPTGALDT-KTGQQIMELLTELNKEG-KTIIMVTHEPEIADFATRKI-IIRDGD 224
Cdd:cd03240 134 ETFGSNCGILALDEPTTNLDEeNIEESLAEIIEERKSQKnFQLIVITHDEELVDAADHIYrVEKDGR 200
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
28-207 |
6.68e-06 |
|
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: 45.68 E-value: 6.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 28 LKGINLTVYEGEFLAIMGPSGSGKSTLMNII--GLLDRPTSGDYTLHNTKIEILNDRELAKVRN---DEIGF-------- 94
Cdd:cd03271 11 LKNIDVDIPLGVLTCVTGVSGSGKSSLINDTlyPALARRLHLKKEQPGNHDRIEGLEHIDKVIVidqSPIGRtprsnpat 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 95 ---VF---QQFFLLAKLTALQNVE-LPLIYAGVNVSK----RREQAKQFLEKV-GLGRRIKHL------------PS-EL 149
Cdd:cd03271 91 ytgVFdeiRELFCEVCKGKRYNREtLEVRYKGKSIADvldmTVEEALEFFENIpKIARKLQTLcdvglgyiklgqPAtTL 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2076047389 150 SGGQKQRVAIARAL---VNDPSIILADEPTGALDTKTGQQIMELLTELNKEGKTIIMVTHE 207
Cdd:cd03271 171 SGGEAQRIKLAKELskrSTGKTLYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIEHN 231
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
37-221 |
1.07e-05 |
|
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini.
Pssm-ID: 213246 [Multi-domain] Cd Length: 213 Bit Score: 44.95 E-value: 1.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 37 EGEFLAIMGPSGSGKSTLMNIIglldrptsgDYTLHNTKIEILNDRELAKVRND-----EIGFVFQQFFLLAKLTAlqnv 111
Cdd:cd03279 27 NNGLFLICGPTGAGKSTILDAI---------TYALYGKTPRYGRQENLRSVFAPgedtaEVSFTFQLGGKKYRVER---- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 112 elpliYAGVNvskrreqAKQFlekvglgRRIKHLP------------SELSGGQKQRVAIARAL-----------VNDPS 168
Cdd:cd03279 94 -----SRGLD-------YDQF-------TRIVLLPqgefdrflarpvSTLSGGETFLASLSLALalsevlqnrggARLEA 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2076047389 169 IILaDEPTGALDTKTGQQIMELLTELNKEGKTIIMVTHEPEIADFATRKIIIR 221
Cdd:cd03279 155 LFI-DEGFGTLDPEALEAVATALELIRTENRMVGVISHVEELKERIPQRLEVI 206
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
13-183 |
1.64e-05 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 45.11 E-value: 1.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 13 NIVKSYqnGDQVLkvLKGINLTVYEGEFLAIMGPSGSGKSTLMNIIGLLDRPTSGDYTLHNTkieilndrelakVRndeI 92
Cdd:PRK11819 329 NLSKSF--GDRLL--IDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGET------------VK---L 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 93 GFVFQQfflLAKLTALQNV------ELPLIYAG---VN----VS----KRREQAKqfleKVGlgrrikhlpsELSGGQKQ 155
Cdd:PRK11819 390 AYVDQS---RDALDPNKTVweeisgGLDIIKVGnreIPsrayVGrfnfKGGDQQK----KVG----------VLSGGERN 452
|
170 180
....*....|....*....|....*...
gi 2076047389 156 RVAIARALVNDPSIILADEPTGALDTKT 183
Cdd:PRK11819 453 RLHLAKTLKQGGNVLLLDEPTNDLDVET 480
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
26-208 |
4.28e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 42.94 E-value: 4.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 26 KVLKGINLTVYEGEFLAIMGPSGSGKSTLMNIIGLLDRPTSGDYTLHNTKIEilndrelaKVRNDEIGFVFQQFFLLAKL 105
Cdd:PRK13541 14 KNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNIN--------NIAKPYCTYIGHNLGLKLEM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 106 TALQNVEL--------PLIYAGVNVSKRREqakqFL-EKVglgrrikhlpSELSGGQKQRVAIARALVNDPSIILADEPT 176
Cdd:PRK13541 86 TVFENLKFwseiynsaETLYAAIHYFKLHD----LLdEKC----------YSLSSGMQKIVAIARLIACQSDLWLLDEVE 151
|
170 180 190
....*....|....*....|....*....|..
gi 2076047389 177 GALDTKTGQQIMELLTELNKEGKTIIMVTHEP 208
Cdd:PRK13541 152 TNLSKENRDLLNNLIVMKANSGGIVLLSSHLE 183
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
124-213 |
9.14e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 43.28 E-value: 9.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 124 KRREQAKQFLEKVGLGrrikHLP-----SELSGGQKQRVAIARALV---NDPSIILADEPTGALDTKTGQQIMELLTELN 195
Cdd:PRK00635 1674 KKIQKPLQALIDNGLG----YLPlgqnlSSLSLSEKIAIKIAKFLYlppKHPTLFLLDEIATSLDNQQKSALLVQLRTLV 1749
|
90 100
....*....|....*....|.
gi 2076047389 196 KEGKTIIMVTHEPEI---ADF 213
Cdd:PRK00635 1750 SLGHSVIYIDHDPALlkqADY 1770
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
10-194 |
1.07e-04 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 41.92 E-value: 1.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 10 QLSNIvKSYQnGDQVLKVLKGINLtvyegeflaIMGPSGSGKSTLMNIIGL-LDRPTSGDYTLHNTKIEILND------- 81
Cdd:COG0419 6 RLENF-RSYR-DTETIDFDDGLNL---------IVGPNGAGKSTILEAIRYaLYGKARSRSKLRSDLINVGSEeasvele 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 82 -----------------RELAKVRNDEIGFVFQQFFLLAKLTALQNvELPLIYAGVNVSKRREQAKQFLEKVGLGRRIKH 144
Cdd:COG0419 75 fehggkryrierrqgefAEFLEAKPSERKEALKRLLGLEIYEELKE-RLKELEEALESALEELAELQKLKQEILAQLSGL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2076047389 145 LPSE-LSGGQKQRVAIARALvndpSIILaDepTGALDTKTGQQIMELLTEL 194
Cdd:COG0419 154 DPIEtLSGGERLRLALADLL----SLIL-D--FGSLDEERLERLLDALEEL 197
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
28-56 |
2.31e-04 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 41.98 E-value: 2.31e-04
10 20
....*....|....*....|....*....
gi 2076047389 28 LKGINLTVYEGEFLAIMGPSGSGKSTLMN 56
Cdd:PRK00349 625 LKNVDVEIPLGKFTCVTGVSGSGKSTLIN 653
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
11-205 |
2.33e-04 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 42.02 E-value: 2.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 11 LSNIVKSYQNGDQVLKV--LKGINLTVYEGEFLAIMGPSGSGKSTLMNII---------GLLDRPTSGDYTLHntkiEIL 79
Cdd:TIGR00956 58 LTRGFRKLKKFRDTKTFdiLKPMDGLIKPGELTVVLGRPGSGCSTLLKTIasntdgfhiGVEGVITYDGITPE----EIK 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 80 NDR--ELAKVRNDEIGF----VFQQFFLLAKLTALQNvelpliyAGVNVSkRREQAKQFLE--------------KVG-- 137
Cdd:TIGR00956 134 KHYrgDVVYNAETDVHFphltVGETLDFAARCKTPQN-------RPDGVS-REEYAKHIADvymatyglshtrntKVGnd 205
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2076047389 138 LGRRIkhlpselSGGQKQRVAIARALVNDPSIILADEPTGALDTKTGQQIMELLTELNKEGKTIIMVT 205
Cdd:TIGR00956 206 FVRGV-------SGGERKRVSIAEASLGGAKIQCWDNATRGLDSATALEFIRALKTSANILDTTPLVA 266
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
87-221 |
3.72e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. 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: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 41.49 E-value: 3.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 87 VRNDEIGFVFQQFflLAKLTALQNVELP--------LIYAGVNVSKRREQAKQFL--EKVGLGRRikhlPSE-LSGGQKQ 155
Cdd:TIGR00618 884 IKIQFDGDALIKF--LHEITLYANVRLAnqsegrfhGRYADSHVNARKYQGLALLvaDAYTGSVR----PSAtLSGGETF 957
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2076047389 156 RVAIARAL-----------VNDPSIILaDEPTGALDTKTGQQIMELLTELNKEGKTIIMVTHEPEIADFATRKIIIR 221
Cdd:TIGR00618 958 LASLSLALaladllstsggTVLDSLFI-DEGFGSLDEDSLDRAIGILDAIREGSKMIGIISHVPEFRERIPHRILVK 1033
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
132-213 |
7.88e-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: 40.38 E-value: 7.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 132 FLEKVGLG-----RRIkhlpSELSGGQKQRVAIARALVNDPSIIL--ADEPTGALDTKTGQQIMELLTELNKEGKTIIMV 204
Cdd:TIGR00630 471 FLIDVGLDylslsRAA----GTLSGGEAQRIRLATQIGSGLTGVLyvLDEPSIGLHQRDNRRLINTLKRLRDLGNTLIVV 546
|
90
....*....|..
gi 2076047389 205 THEPEI---ADF 213
Cdd:TIGR00630 547 EHDEDTiraADY 558
|
|
| COG4938 |
COG4938 |
Predicted ATPase [General function prediction only]; |
45-210 |
8.22e-04 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443965 [Multi-domain] Cd Length: 277 Bit Score: 39.57 E-value: 8.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 45 GPSGSGKSTLMNIIGLL----------DR-----------------PTSGDYTLHntkieILNDRELAKVRNDEIGFVFQ 97
Cdd:COG4938 27 GPNGSGKSTLIQALLLLlqsnfiylpaERsgparlypslvrelsdlGSRGEYTAD-----FLAELENLEILDDKSKELLE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 98 QFF-LLAKLTAlqnvelpliyAGVNVSKRREQAKQFLEKVGLGRRIKhlPSELSGGQKQRVAI---ARALVNDPSIILAD 173
Cdd:COG4938 102 QVEeWLEKIFP----------GKVEVDASSDLVRLVFRPSGNGKRIP--LSNVGSGVSELLPIllaLLSAAKPGSLLIIE 169
|
170 180 190
....*....|....*....|....*....|....*..
gi 2076047389 174 EPTGALDTKTGQQIMELLTELNKEGKTIIMVTHEPEI 210
Cdd:COG4938 170 EPEAHLHPKAQSALAELLAELANSGVQVIIETHSDYI 206
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
28-56 |
9.60e-04 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 40.01 E-value: 9.60e-04
10 20
....*....|....*....|....*....
gi 2076047389 28 LKGINLTVYEGEFLAIMGPSGSGKSTLMN 56
Cdd:COG0178 621 LKNVDVEIPLGVLTCVTGVSGSGKSTLVN 649
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
56-212 |
1.61e-03 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 38.91 E-value: 1.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 56 NIIGLLDRPTSGDYTLHNTKIEILNDRELAKVRNDEIGFVFQqfFLLAKLTALQNVELPLIYAGVNVSKRREQAKQFLEK 135
Cdd:pfam13304 146 SIISPLSFLLLLDEGLLLEDWAVLDLAADLALFPDLKELLQR--LVRGLKLADLNLSDLGEGIEKSLLVDDRLRERGLIL 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 136 VGLGRRIKHLPSELSGGQKQ---RVAIARALVNDPSIILADEPTGALDTKTGQQIMELLTELNKEGKTIIMVTHEPEIAD 212
Cdd:pfam13304 224 LENGGGGELPAFELSDGTKRllaLLAALLSALPKGGLLLIDEPESGLHPKLLRRLLELLKELSRNGAQLILTTHSPLLLD 303
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
10-176 |
1.74e-03 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 39.34 E-value: 1.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 10 QLSNIVKSYqnGDQVlkVLKGINLTVYEGEFLAIMGPSGSGKSTLMNIIglldrptSGDYTLHNTKIEILN-DRELAKVR 88
Cdd:NF033858 3 RLEGVSHRY--GKTV--ALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLI-------AGARKIQQGRVEVLGgDMADARHR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 89 ND---EIGF--------------VFQ--QFFllAKLTalqnvelpliyaGVNVSKRREQAKQFLEKVGLGRRIKHLPSEL 149
Cdd:NF033858 72 RAvcpRIAYmpqglgknlyptlsVFEnlDFF--GRLF------------GQDAAERRRRIDELLRATGLAPFADRPAGKL 137
|
170 180
....*....|....*....|....*..
gi 2076047389 150 SGGQKQRVAIARALVNDPSIILADEPT 176
Cdd:NF033858 138 SGGMKQKLGLCCALIHDPDLLILDEPT 164
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
9-232 |
2.76e-03 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 37.97 E-value: 2.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 9 MQLSNIVKSYQNGdqvLK-VLKGINLTVYEGEFLAIMGPSGSGKSTL----MNIIGLLDrptsGDYTLHNTKIEILndrE 83
Cdd:cd03288 20 IKIHDLCVRYENN---LKpVLKHVKAYIKPGQKVGICGRTGSGKSSLslafFRMVDIFD----GKIVIDGIDISKL---P 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 84 LAKVRNdEIGFVFQQffllakltalqnvelPLIYAG---VNVSKRR----EQAKQFLEKVGLGRRIKHLPSEL------- 149
Cdd:cd03288 90 LHTLRS-RLSIILQD---------------PILFSGsirFNLDPECkctdDRLWEALEIAQLKNMVKSLPGGLdavvteg 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 150 ----SGGQKQRVAIARALVNDPSIILADEPTGALDTKTgQQIMELLTELNKEGKTIIMVTHEPEIADFATRKIIIRDGDI 225
Cdd:cd03288 154 genfSVGQRQLFCLARAFVRKSSILIMDEATASIDMAT-ENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGIL 232
|
....*..
gi 2076047389 226 TTDTTAS 232
Cdd:cd03288 233 VECDTPE 239
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
28-54 |
3.12e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 38.47 E-value: 3.12e-03
10 20
....*....|....*....|....*..
gi 2076047389 28 LKGINLTVYEGEFLAIMGPSGSGKSTL 54
Cdd:COG0178 16 LKNIDVDIPRNKLVVITGLSGSGKSSL 42
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
9-230 |
3.37e-03 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 38.06 E-value: 3.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 9 MQLSNI-VKSYQN-GDQVLKVLKGINltvyegeflAIMGPSGSGKSTLMNIIGLL------------DRPTSGDYTLHNT 74
Cdd:COG3593 1 MKLEKIkIKNFRSiKDLSIELSDDLT---------VLVGENNSGKSSILEALRLLlgpsssrkfdeeDFYLGDDPDLPEI 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 75 KIEI--------LNDRELAKVRNDEIGFVFQQF--FLLAKLTALQN-----VELPLIYAGVNVSKRREQAKQFLE--KVG 137
Cdd:COG3593 72 EIELtfgsllsrLLRLLLKEEDKEELEEALEELneELKEALKALNEllseyLKELLDGLDLELELSLDELEDLLKslSLR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 138 LGRRIKHLPSELSGGQKQRVAIA--RALV-----NDPSIILADEPTGALDTKTGQQIMELLTELNKEGKTIIMVTHEPEI 210
Cdd:COG3593 152 IEDGKELPLDRLGSGFQRLILLAllSALAelkraPANPILLIEEPEAHLHPQAQRRLLKLLKELSEKPNQVIITTHSPHL 231
|
250 260
....*....|....*....|...
gi 2076047389 211 AD-FATRKIII--RDGDITTDTT 230
Cdd:COG3593 232 LSeVPLENIRRlrRDSGGTTSTK 254
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
25-225 |
3.83e-03 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 38.29 E-value: 3.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 25 LKVLKGINLTVYEGEFLAIMGPSGSGKSTLM-NIIGLLDRP--TSGDYT----------------------LH------- 72
Cdd:PLN03140 178 LTILKDASGIIKPSRMTLLLGPPSSGKTTLLlALAGKLDPSlkVSGEITyngyrlnefvprktsayisqndVHvgvmtvk 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 73 ------------NTKIEILNdrELAKVRNDEIGFVFQQFFLLAKLTALQNVELPLI--YA----GVNVSKRREQAKQFLE 134
Cdd:PLN03140 258 etldfsarcqgvGTRYDLLS--ELARREKDAGIFPEAEVDLFMKATAMEGVKSSLItdYTlkilGLDICKDTIVGDEMIR 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076047389 135 KVglgrrikhlpselSGGQKQRVAIARALVNDPSIILADEPTGALDTKTGQQIMELLTEL-NKEGKTIIM--VTHEPEIA 211
Cdd:PLN03140 336 GI-------------SGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQQIvHLTEATVLMslLQPAPETF 402
|
250
....*....|....
gi 2076047389 212 DFATRKIIIRDGDI 225
Cdd:PLN03140 403 DLFDDIILLSEGQI 416
|
|
| PhnN |
COG3709 |
Ribose 1,5-bisphosphate kinase PhnN [Carbohydrate transport and metabolism]; |
38-56 |
4.82e-03 |
|
Ribose 1,5-bisphosphate kinase PhnN [Carbohydrate transport and metabolism];
Pssm-ID: 442923 Cd Length: 188 Bit Score: 36.71 E-value: 4.82e-03
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
149-210 |
6.08e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 37.57 E-value: 6.08e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2076047389 149 LSGGQKQ------RVAIARALVNDPSIILADEPTGALDTKTGQQIMELLTELNKEGKTI---IMVTHEPEI 210
Cdd:PRK01156 802 LSGGEKTavafalRVAVAQFLNNDKSLLIMDEPTAFLDEDRRTNLKDIIEYSLKDSSDIpqvIMISHHREL 872
|
|
| |
