|
Name |
Accession |
Description |
Interval |
E-value |
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
16-352 |
1.10e-172 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 483.43 E-value: 1.10e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 16 HIKIRGLNKFYQSQGQKLHALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQNIAELSHSELIQT 95
Cdd:COG1135 1 MIELENLSKTFPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 96 RQRIGMIFQHFNLMSAKTVWENVALPLKVSNYNKADIDQRVNEVLALVGLADKSNYYPSQLSGGQKQRVGIARALVHHPE 175
Cdd:COG1135 81 RRKIGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 176 ILLCDEATSALDPESTATILALLKKINQELGLTIVLITHEMQVIREICDQVVVIDQGEIVEAGQVWSVFSRPEQQITQEL 255
Cdd:COG1135 161 VLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVLDVFANPQSELTRRF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 256 LN-LEQITLP-FKINPLPDEDSTHIIVKLKYEAEAHQVPDIQELLARFKAPVNLYQSQVDTIQGHIIGSLLVGIPNVEID 333
Cdd:COG1135 241 LPtVLNDELPeELLARLREAAGGGRLVRLTFVGESADEPLLSELARRFGVDVNILSGGIEEIQGTPVGRLIVELEGDDAA 320
|
330 340
....*....|....*....|...
gi 1194606020 334 LssiqQDALTAIAQ----FEVLG 352
Cdd:COG1135 321 I----DAALAYLREqgvvVEVLG 339
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
17-353 |
1.29e-146 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 417.66 E-value: 1.29e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 17 IKIRGLNKFYQSQGQKLHALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQNIAELSHSELIQTR 96
Cdd:PRK11153 2 IELKNISKVFPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 97 QRIGMIFQHFNLMSAKTVWENVALPLKVSNYNKADIDQRVNEVLALVGLADKSNYYPSQLSGGQKQRVGIARALVHHPEI 176
Cdd:PRK11153 82 RQIGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPKV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 177 LLCDEATSALDPESTATILALLKKINQELGLTIVLITHEMQVIREICDQVVVIDQGEIVEAGQVWSVFSRPEQQITQELL 256
Cdd:PRK11153 162 LLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHPKHPLTREFI 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 257 -NLEQITLP----FKINPLPDEDSTHIIvKLKYEAEAHQVPDIQELLARFKAPVNLYQSQVDTIQGHIIGSLLVGipnve 331
Cdd:PRK11153 242 qSTLHLDLPedylARLQAEPTTGSGPLL-RLEFTGESVDAPLLSETARRFGVDFNILSGQIDYIGGVKFGSLLVE----- 315
|
330 340
....*....|....*....|....*....
gi 1194606020 332 idLSSIQQDALTAIAQF-------EVLGY 353
Cdd:PRK11153 316 --LTGDPGDIQAAIAYLqehgvkvEVLGY 342
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
17-248 |
7.73e-132 |
|
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: 376.15 E-value: 7.73e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 17 IKIRGLNKFYQSQGQKLHALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQNIAELSHSELIQTR 96
Cdd:cd03258 2 IELKNVSKVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 97 QRIGMIFQHFNLMSAKTVWENVALPLKVSNYNKADIDQRVNEVLALVGLADKSNYYPSQLSGGQKQRVGIARALVHHPEI 176
Cdd:cd03258 82 RRIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKV 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1194606020 177 LLCDEATSALDPESTATILALLKKINQELGLTIVLITHEMQVIREICDQVVVIDQGEIVEAGQVWSVFSRPE 248
Cdd:cd03258 162 LLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFANPQ 233
|
|
| ABC_MetN |
TIGR02314 |
D-methionine ABC transporter, ATP-binding protein; Members of this family are the ATP-binding ... |
17-353 |
1.85e-105 |
|
D-methionine ABC transporter, ATP-binding protein; Members of this family are the ATP-binding protein of the D-methionine ABC transporter complex. Known members belong to the Proteobacteria.
Pssm-ID: 131367 [Multi-domain] Cd Length: 343 Bit Score: 313.36 E-value: 1.85e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 17 IKIRGLNKFYQSQGQKLHALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQNIAELSHSELIQTR 96
Cdd:TIGR02314 2 IKLSNITKVFHQGTKTIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTSGSVIVDGQDLTTLSNSELTKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 97 QRIGMIFQHFNLMSAKTVWENVALPLKVSNYNKADIDQRVNEVLALVGLADKSNYYPSQLSGGQKQRVGIARALVHHPEI 176
Cdd:TIGR02314 82 RQIGMIFQHFNLLSSRTVFGNVALPLELDNTPKDEIKRKVTELLALVGLGDKHDSYPSNLSGGQKQRVAIARALASNPKV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 177 LLCDEATSALDPESTATILALLKKINQELGLTIVLITHEMQVIREICDQVVVIDQGEIVEAGQVWSVFSRPEQQITQELL 256
Cdd:TIGR02314 162 LLCDEATSALDPATTQSILELLKEINRRLGLTILLITHEMDVVKRICDCVAVISNGELIEQGTVSEIFSHPKTPLAQKFI 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 257 -NLEQITLP----FKINPLPDEDStHIIVKLKYEAEAHQVPDIQELLARFKAPVNLYQSQVDTIQGHIIGSLLVgipnve 331
Cdd:TIGR02314 242 rSTLHLSIPedyqERLQATPFADS-VPMVRLEFTGQTVDAPLLSQTARRFNVDNSILSSQMDYAGGVKFGIMLA------ 314
|
330 340
....*....|....*....|....*....
gi 1194606020 332 iDLSSIQQDALTAIA-------QFEVLGY 353
Cdd:TIGR02314 315 -EMHGTQQDTQAAIAylqehnvKVEVLGY 342
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
17-257 |
1.85e-98 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 291.51 E-value: 1.85e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 17 IKIRGLNKFYQSqgqkLHALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQNIAeLSHSELIQTR 96
Cdd:COG1126 2 IEIENLHKSFGD----LEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLT-DSKKDINKLR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 97 QRIGMIFQHFNLMSAKTVWENVAL-PLKVSNYNKADIDQRVNEVLALVGLADKSNYYPSQLSGGQKQRVGIARALVHHPE 175
Cdd:COG1126 77 RKVGMVFQQFNLFPHLTVLENVTLaPIKVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 176 ILLCDEATSALDPESTATILALLKKINQElGLTIVLITHEMQVIREICDQVVVIDQGEIVEAGQVWSVFSRPEQQITQEL 255
Cdd:COG1126 157 VMLFDEPTSALDPELVGEVLDVMRDLAKE-GMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFENPQHERTRAF 235
|
..
gi 1194606020 256 LN 257
Cdd:COG1126 236 LS 237
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
15-238 |
7.82e-92 |
|
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: 274.55 E-value: 7.82e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 15 PHIKIRGLNKfyqSQGQKlHALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQNIAELSHSELIQ 94
Cdd:COG1127 4 PMIEVRNLTK---SFGDR-VVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 95 TRQRIGMIFQHFNLMSAKTVWENVALPLKV-SNYNKADIDQRVNEVLALVGLADKSNYYPSQLSGGQKQRVGIARALVHH 173
Cdd:COG1127 80 LRRRIGMLFQGGALFDSLTVFENVAFPLREhTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALD 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1194606020 174 PEILLCDEATSALDPESTATILALLKKINQELGLTIVLITHEMQVIREICDQVVVIDQGEIVEAG 238
Cdd:COG1127 160 PEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEG 224
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
17-236 |
2.10e-91 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 273.07 E-value: 2.10e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 17 IKIRGLNKFYQSQGQKLHALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQNIAELSHSELIQTR 96
Cdd:COG1136 5 LELRNLTKSYGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELARLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 97 -QRIGMIFQHFNLMSAKTVWENVALPLKVSNYNKADIDQRVNEVLALVGLADKSNYYPSQLSGGQKQRVGIARALVHHPE 175
Cdd:COG1136 85 rRHIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNRPK 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1194606020 176 ILLCDEATSALDPESTATILALLKKINQELGLTIVLITHEMQVIrEICDQVVVIDQGEIVE 236
Cdd:COG1136 165 LILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELA-ARADRVIRLRDGRIVS 224
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
15-256 |
2.27e-90 |
|
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: 280.25 E-value: 2.27e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 15 PHIKIRGLNKFYQSQGQK-LHALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQNIAELSHSELI 93
Cdd:COG1123 259 PLLEVRNLSKRYPVRGKGgVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLR 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 94 QTRQRIGMIFQH----FNlmSAKTVWENVALPLKVSN-YNKADIDQRVNEVLALVGL-ADKSNYYPSQLSGGQKQRVGIA 167
Cdd:COG1123 339 ELRRRVQMVFQDpyssLN--PRMTVGDIIAEPLRLHGlLSRAERRERVAELLERVGLpPDLADRYPHELSGGQRQRVAIA 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 168 RALVHHPEILLCDEATSALDPESTATILALLKKINQELGLTIVLITHEMQVIREICDQVVVIDQGEIVEAGQVWSVFSRP 247
Cdd:COG1123 417 RALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVFANP 496
|
....*....
gi 1194606020 248 EQQITQELL 256
Cdd:COG1123 497 QHPYTRALL 505
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
17-239 |
1.65e-86 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 260.37 E-value: 1.65e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 17 IKIRGLNKFYqsqGQKLHALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQNIAELSHSELIQTR 96
Cdd:COG2884 2 IRFENVSKRY---PGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 97 QRIGMIFQHFNLMSAKTVWENVALPLKVSNYNKADIDQRVNEVLALVGLADKSNYYPSQLSGGQKQRVGIARALVHHPEI 176
Cdd:COG2884 79 RRIGVVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPEL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1194606020 177 LLCDEATSALDPESTATILALLKKINQeLGLTIVLITHEMQVIREICDQVVVIDQGEIVEAGQ 239
Cdd:COG2884 159 LLADEPTGNLDPETSWEIMELLEEINR-RGTTVLIATHDLELVDRMPKRVLELEDGRLVRDEA 220
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
17-234 |
9.88e-85 |
|
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: 255.88 E-value: 9.88e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 17 IKIRGLNKFYQSQGQKLHALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQNIAELSHSELIQTR 96
Cdd:cd03255 1 IELKNLSKTYGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 97 -QRIGMIFQHFNLMSAKTVWENVALPLKVSNYNKADIDQRVNEVLALVGLADKSNYYPSQLSGGQKQRVGIARALVHHPE 175
Cdd:cd03255 81 rRHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1194606020 176 ILLCDEATSALDPESTATILALLKKINQELGLTIVLITHEMQVIrEICDQVVVIDQGEI 234
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELA-EYADRIIELRDGKI 218
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
17-253 |
1.55e-82 |
|
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: 250.88 E-value: 1.55e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 17 IKIRGLNKFYQSQgqklHALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQNIAELSHSELIQTR 96
Cdd:cd03261 1 IELRGLTKSFGGR----TVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 97 QRIGMIFQHFNLMSAKTVWENVALPLKV-SNYNKADIDQRVNEVLALVGLADKSNYYPSQLSGGQKQRVGIARALVHHPE 175
Cdd:cd03261 77 RRMGMLFQSGALFDSLTVFENVAFPLREhTRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPE 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1194606020 176 ILLCDEATSALDPESTATILALLKKINQELGLTIVLITHEMQVIREICDQVVVIDQGEIVEAGQVWSVFSRPEQQITQ 253
Cdd:cd03261 157 LLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRASDDPLVRQ 234
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
17-234 |
2.06e-82 |
|
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: 249.75 E-value: 2.06e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 17 IKIRGLNKFYQsqgqKLHALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQNIaELSHSELIQTR 96
Cdd:cd03262 1 IEIKNLHKSFG----DFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKL-TDDKKNINELR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 97 QRIGMIFQHFNLMSAKTVWENVAL-PLKVSNYNKADIDQRVNEVLALVGLADKSNYYPSQLSGGQKQRVGIARALVHHPE 175
Cdd:cd03262 76 QKVGMVFQQFNLFPHLTVLENITLaPIKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPK 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1194606020 176 ILLCDEATSALDPESTATILALLKKINQElGLTIVLITHEMQVIREICDQVVVIDQGEI 234
Cdd:cd03262 156 VMLFDEPTSALDPELVGEVLDVMKDLAEE-GMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
17-257 |
5.07e-79 |
|
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: 242.40 E-value: 5.07e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 17 IKIRGLNKFYQSQGQKLHALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQniaELSHSELIQTR 96
Cdd:COG1124 2 LEVRNLSVSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGR---PVTRRRRKAFR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 97 QRIGMIFQHFnlMSA----KTVWENVALPLKVsnYNKADIDQRVNEVLALVGL-ADKSNYYPSQLSGGQKQRVGIARALV 171
Cdd:COG1124 79 RRVQMVFQDP--YASlhprHTVDRILAEPLRI--HGLPDREERIAELLEQVGLpPSFLDRYPHQLSGGQRQRVAIARALI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 172 HHPEILLCDEATSALDPESTATILALLKKINQELGLTIVLITHEMQVIREICDQVVVIDQGEIVEAGQVWSVFSRPEQQI 251
Cdd:COG1124 155 LEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAGPKHPY 234
|
....*.
gi 1194606020 252 TQELLN 257
Cdd:COG1124 235 TRELLA 240
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
15-257 |
8.29e-79 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 241.50 E-value: 8.29e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 15 PHIKIRGLNKFYQSQgqkLHALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQNIAELSHSELIQ 94
Cdd:COG3638 1 PMLELRNLSKRYPGG---TPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 95 TRQRIGMIFQHFNLMSAKTVWENV---ALP----LK--VSNYNKADIdQRVNEVLALVGLADKSNYYPSQLSGGQKQRVG 165
Cdd:COG3638 78 LRRRIGMIFQQFNLVPRLSVLTNVlagRLGrtstWRslLGLFPPEDR-ERALEALERVGLADKAYQRADQLSGGQQQRVA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 166 IARALVHHPEILLCDEATSALDPESTATILALLKKINQELGLTIVLITHEMQVIREICDQVVVIDQGEIveagqvwsVFS 245
Cdd:COG3638 157 IARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRV--------VFD 228
|
250
....*....|..
gi 1194606020 246 RPEQQITQELLN 257
Cdd:COG3638 229 GPPAELTDAVLR 240
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
15-236 |
1.07e-76 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 236.52 E-value: 1.07e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 15 PHIKIRGLNKFYQSQGQKLHALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQNIAELSHseliq 94
Cdd:COG1116 6 PALELRGVSKRFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGP----- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 95 trqRIGMIFQHFNLMSAKTVWENVALPLKVSNYNKADIDQRVNEVLALVGLADKSNYYPSQLSGGQKQRVGIARALVHHP 174
Cdd:COG1116 81 ---DRGVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDP 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1194606020 175 EILLCDEATSALDPESTATILALLKKINQELGLTIVLITHEmqvIRE---ICDQVVVIDQ--GEIVE 236
Cdd:COG1116 158 EVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHD---VDEavfLADRVVVLSArpGRIVE 221
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
17-247 |
3.51e-76 |
|
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: 237.26 E-value: 3.51e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 17 IKIRGLNKFYQSQGQKLHALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVN---TGSIHIHQQNIAELSHSELI 93
Cdd:COG0444 2 LEVRNLKVYFPTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPgitSGEILFDGEDLLKLSEKELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 94 QTR-QRIGMIFQhfNLMSA----KTVWENVALPLKVSN-YNKADIDQRVNEVLALVGLADKSNY---YPSQLSGGQKQRV 164
Cdd:COG0444 82 KIRgREIQMIFQ--DPMTSlnpvMTVGDQIAEPLRIHGgLSKAEARERAIELLERVGLPDPERRldrYPHELSGGMRQRV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 165 GIARALVHHPEILLCDEATSALDPESTATILALLKKINQELGLTIVLITHEMQVIREICDQVVVIDQGEIVEAGQVWSVF 244
Cdd:COG0444 160 MIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGPVEELF 239
|
...
gi 1194606020 245 SRP 247
Cdd:COG0444 240 ENP 242
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
17-238 |
2.13e-75 |
|
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: 232.40 E-value: 2.13e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 17 IKIRGLNKFYQSQGQKLHALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQNIAELSHSELIQTR 96
Cdd:cd03257 2 LEVKNLSVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 97 QRIGMIFQhfNLMSA----KTVWENVALPLKV--SNYNKADIDQRVNEVLALVGLADK-SNYYPSQLSGGQKQRVGIARA 169
Cdd:cd03257 82 KEIQMVFQ--DPMSSlnprMTIGEQIAEPLRIhgKLSKKEARKEAVLLLLVGVGLPEEvLNRYPHELSGGQRQRVAIARA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1194606020 170 LVHHPEILLCDEATSALDPESTATILALLKKINQELGLTIVLITHEMQVIREICDQVVVIDQGEIVEAG 238
Cdd:cd03257 160 LALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
17-248 |
2.57e-75 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 232.22 E-value: 2.57e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 17 IKIRGLNKFYQSQGQklhALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQNIAELSHSELiqtR 96
Cdd:COG1122 1 IELENLSFSYPGGTP---ALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLREL---R 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 97 QRIGMIFQH-FNLMSAKTVWENVALPLKVSNYNKADIDQRVNEVLALVGLADKSNYYPSQLSGGQKQRVGIARALVHHPE 175
Cdd:COG1122 75 RKVGLVFQNpDDQLFAPTVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPE 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1194606020 176 ILLCDEATSALDPESTATILALLKKINQElGLTIVLITHEMQVIREICDQVVVIDQGEIVEAGQVWSVFSRPE 248
Cdd:COG1122 155 VLVLDEPTAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDYE 226
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
17-257 |
3.43e-73 |
|
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: 227.07 E-value: 3.43e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 17 IKIRGLNKFYqsqGQKLHALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQNIAELSHSELIQTR 96
Cdd:cd03256 1 IEVENLSKTY---PNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 97 QRIGMIFQHFNLMSAKTVWENV---ALPLK------VSNYNKADIdQRVNEVLALVGLADKSNYYPSQLSGGQKQRVGIA 167
Cdd:cd03256 78 RQIGMIFQQFNLIERLSVLENVlsgRLGRRstwrslFGLFPKEEK-QRALAALERVGLLDKAYQRADQLSGGQQQRVAIA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 168 RALVHHPEILLCDEATSALDPESTATILALLKKINQELGLTIVLITHEMQVIREICDQVVVIDQGEIveagqvwsVFSRP 247
Cdd:cd03256 157 RALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRI--------VFDGP 228
|
250
....*....|
gi 1194606020 248 EQQITQELLN 257
Cdd:cd03256 229 PAELTDEVLD 238
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
17-238 |
6.89e-73 |
|
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: 225.48 E-value: 6.89e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 17 IKIRGLNKFYQSQgqklHALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQNIAELShseliqTR 96
Cdd:cd03259 1 LELKGLSKTYGSV----RALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVP------PE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 97 QR-IGMIFQHFNLMSAKTVWENVALPLKVSNYNKADIDQRVNEVLALVGLADKSNYYPSQLSGGQKQRVGIARALVHHPE 175
Cdd:cd03259 71 RRnIGMVFQDYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPS 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1194606020 176 ILLCDEATSALDPESTATILALLKKINQELGLTIVLITHEMQVIREICDQVVVIDQGEIVEAG 238
Cdd:cd03259 151 LLLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
15-247 |
1.11e-72 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 229.60 E-value: 1.11e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 15 PHIKIRGLNKFYQSQgqklHALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQNIAELShseliq 94
Cdd:COG3842 4 PALELENVSKRYGDV----TALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLP------ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 95 TRQR-IGMIFQHFNLMSAKTVWENVALPLKVSNYNKADIDQRVNEVLALVGLADKSNYYPSQLSGGQKQRVGIARALVHH 173
Cdd:COG3842 74 PEKRnVGMVFQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPE 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1194606020 174 PEILLCDEATSALDPESTATILALLKKINQELGLTIVLITHEMQvirE---ICDQVVVIDQGEIVEAGQVWSVFSRP 247
Cdd:COG3842 154 PRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQE---EalaLADRIAVMNDGRIEQVGTPEEIYERP 227
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
17-238 |
5.27e-70 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 218.78 E-value: 5.27e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 17 IKIRGLNKFYQSQgqklHALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQNIAElshsELIQTR 96
Cdd:COG1131 1 IEVRGLTKRYGDK----TALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVAR----DPAEVR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 97 QRIGMIFQHFNLMSAKTVWENVALPLKVSNYNKADIDQRVNEVLALVGLADKSNYYPSQLSGGQKQRVGIARALVHHPEI 176
Cdd:COG1131 73 RRIGYVPQEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPEL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1194606020 177 LLCDEATSALDPESTATILALLKKINQElGLTIVLITHEMQVIREICDQVVVIDQGEIVEAG 238
Cdd:COG1131 153 LILDEPTSGLDPEARRELWELLRELAAE-GKTVLLSTHYLEEAERLCDRVAIIDKGRIVADG 213
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
17-257 |
9.71e-70 |
|
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: 218.32 E-value: 9.71e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 17 IKIRGLNKFYQSQGQklhALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQNIAELSHSELIQTR 96
Cdd:TIGR02315 2 LEVENLSKVYPNGKQ---ALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKLRKLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 97 QRIGMIFQHFNLMSAKTVWENV---------ALPLKVSNYNKADIdQRVNEVLALVGLADKSNYYPSQLSGGQKQRVGIA 167
Cdd:TIGR02315 79 RRIGMIFQHYNLIERLTVLENVlhgrlgykpTWRSLLGRFSEEDK-ERALSALERVGLADKAYQRADQLSGGQQQRVAIA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 168 RALVHHPEILLCDEATSALDPESTATILALLKKINQELGLTIVLITHEMQVIREICDQVVVIDQGEIveagqvwsVFSRP 247
Cdd:TIGR02315 158 RALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEI--------VFDGA 229
|
250
....*....|
gi 1194606020 248 EQQITQELLN 257
Cdd:TIGR02315 230 PSELDDEVLR 239
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
15-254 |
1.99e-69 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 217.98 E-value: 1.99e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 15 PHIKIRGLNKFYqsqGQKlHALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVN-----TGSIHIHQQNIAElSH 89
Cdd:COG1117 10 PKIEVRNLNVYY---GDK-QALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDLIpgarvEGEILLDGEDIYD-PD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 90 SELIQTRQRIGMIFQHFNLMsAKTVWENVALPLKVSNY-NKADIDQRVNEVLALVGL----ADKSNYYPSQLSGGQKQRV 164
Cdd:COG1117 85 VDVVELRRRVGMVFQKPNPF-PKSIYDNVAYGLRLHGIkSKSELDEIVEESLRKAALwdevKDRLKKSALGLSGGQQQRL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 165 GIARALVHHPEILLCDEATSALDPESTATILALLKKINQElgLTIVLITHEMQVIREICDQVVVIDQGEIVEAGQVWSVF 244
Cdd:COG1117 164 CIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKD--YTIVIVTHNMQQAARVSDYTAFFYLGELVEFGPTEQIF 241
|
250
....*....|
gi 1194606020 245 SRPEQQITQE 254
Cdd:COG1117 242 TNPKDKRTED 251
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
17-243 |
3.31e-69 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 216.28 E-value: 3.31e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 17 IKIRGLNKFYqsqGQKlHALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVN-----TGSIHIHQQNIAELShSE 91
Cdd:cd03260 1 IELRDLNVYY---GDK-HALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIpgapdEGEVLLDGKDIYDLD-VD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 92 LIQTRQRIGMIFQHFNLMSaKTVWENVALPLKVSNY-NKADIDQRVNEVLALVGLAD--KSNYYPSQLSGGQKQRVGIAR 168
Cdd:cd03260 76 VLELRRRVGMVFQKPNPFP-GSIYDNVAYGLRLHGIkLKEELDERVEEALRKAALWDevKDRLHALGLSGGQQQRLCLAR 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1194606020 169 ALVHHPEILLCDEATSALDPESTATILALLKKINQElgLTIVLITHEMQVIREICDQVVVIDQGEIVEAGQVWSV 243
Cdd:cd03260 155 ALANEPEVLLLDEPTSALDPISTAKIEELIAELKKE--YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
18-233 |
6.90e-69 |
|
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: 215.02 E-value: 6.90e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 18 KIRGLNKFYQSQGQKlhALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQNIAELSHSELiqtRQ 97
Cdd:cd03225 1 ELKNLSFSYPDGARP--ALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKEL---RR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 98 RIGMIFQHFNLM-SAKTVWENVALPLKVSNYNKADIDQRVNEVLALVGLADKSNYYPSQLSGGQKQRVGIARALVHHPEI 176
Cdd:cd03225 76 KVGLVFQNPDDQfFGPTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDI 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1194606020 177 LLCDEATSALDPESTATILALLKKINQElGLTIVLITHEMQVIREICDQVVVIDQGE 233
Cdd:cd03225 156 LLLDEPTAGLDPAGRRELLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
17-236 |
5.14e-67 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 210.41 E-value: 5.14e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 17 IKIRGLNKFYQSQGQKLHALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQNIAELSHseliqtr 96
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGP------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 97 qRIGMIFQHFNLMSAKTVWENVALPLKVSNYNKADIDQRVNEVLALVGLADKSNYYPSQLSGGQKQRVGIARALVHHPEI 176
Cdd:cd03293 74 -DRGYVFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDV 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1194606020 177 LLCDEATSALDPESTATILALLKKINQELGLTIVLITHEmqvIRE---ICDQVVVIDQ--GEIVE 236
Cdd:cd03293 153 LLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHD---IDEavfLADRVVVLSArpGRIVA 214
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
15-249 |
1.92e-66 |
|
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: 218.23 E-value: 1.92e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 15 PHIKIRGLNKFYQsqGQKLHALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVN---TGSIHIHQQNIAELSHSE 91
Cdd:COG1123 3 PLLEVRDLSVRYP--GGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 92 LiqtRQRIGMIFQhfNLMSA---KTVWENVALPLKVSNYNKADIDQRVNEVLALVGLADKSNYYPSQLSGGQKQRVGIAR 168
Cdd:COG1123 81 R---GRRIGMVFQ--DPMTQlnpVTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 169 ALVHHPEILLCDEATSALDPESTATILALLKKINQELGLTIVLITHEMQVIREICDQVVVIDQGEIVEAGQVWSVFSRPE 248
Cdd:COG1123 156 ALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAPQ 235
|
.
gi 1194606020 249 Q 249
Cdd:COG1123 236 A 236
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
17-233 |
5.17e-66 |
|
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: 206.27 E-value: 5.17e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 17 IKIRGLNKFYqsqGQKlHALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQNIAELSHSELIQtR 96
Cdd:cd03229 1 LELKNVSKRY---GQK-TVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPPL-R 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 97 QRIGMIFQHFNLMSAKTVWENVALPLkvsnynkadidqrvnevlalvgladksnyypsqlSGGQKQRVGIARALVHHPEI 176
Cdd:cd03229 76 RRIGMVFQDFALFPHLTVLENIALGL----------------------------------SGGQQQRVALARALAMDPDV 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1194606020 177 LLCDEATSALDPESTATILALLKKINQELGLTIVLITHEMQVIREICDQVVVIDQGE 233
Cdd:cd03229 122 LLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
15-239 |
8.59e-66 |
|
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: 207.67 E-value: 8.59e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 15 PHIKIRGLNKFYQSQGQKLHALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQNIAELSHSELIQ 94
Cdd:COG4181 7 PIIELRGLTKTVGTGAGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDARAR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 95 TR-QRIGMIFQHFNLMSAKTVWENVALPLKVSNynKADIDQRVNEVLALVGLADKSNYYPSQLSGGQKQRVGIARALVHH 173
Cdd:COG4181 87 LRaRHVGFVFQSFQLLPTLTALENVMLPLELAG--RRDARARARALLERVGLGHRLDHYPAQLSGGEQQRVALARAFATE 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1194606020 174 PEILLCDEATSALDPESTATILALLKKINQELGLTIVLITHEMQVIREiCDQVVVIDQGEIVEAGQ 239
Cdd:COG4181 165 PAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAAR-CDRVLRLRAGRLVEDTA 229
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
17-247 |
7.64e-65 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 209.16 E-value: 7.64e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 17 IKIRGLNKFYQSQgqklHALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQNIAELShseliqTR 96
Cdd:COG3839 4 LELENVSKSYGGV----EALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLP------PK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 97 QR-IGMIFQHFNLMSAKTVWENVALPLKVSNYNKADIDQRVNEVLALVGLADKSNYYPSQLSGGQKQRVGIARALVHHPE 175
Cdd:COG3839 74 DRnIAMVFQSYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPK 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1194606020 176 ILLCDEATSALDPESTATILALLKKINQELGLTIVLITHEmQVirE---ICDQVVVIDQGEIVEAGQVWSVFSRP 247
Cdd:COG3839 154 VFLLDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHD-QV--EamtLADRIAVMNDGRIQQVGTPEELYDRP 225
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
6-214 |
2.81e-64 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 208.80 E-value: 2.81e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 6 FGSQVDFSLPHIKiRGLNKF--YQSQGQKLhALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQN 83
Cdd:COG4175 13 FGKRPERALKLLD-QGKSKDeiLEKTGQTV-GVNDASFDVEEGEIFVIMGLSGSGKSTLVRCLNRLIEPTAGEVLIDGED 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 84 IAELSHSELIQTRQ-RIGMIFQHFNLMSAKTVWENVALPLKVSNYNKADIDQRVNEVLALVGLADKSNYYPSQLSGGQKQ 162
Cdd:COG4175 91 ITKLSKKELRELRRkKMSMVFQHFALLPHRTVLENVAFGLEIQGVPKAERRERAREALELVGLAGWEDSYPDELSGGMQQ 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 163 RVGIARALVHHPEILLCDEATSALDP--------EstatilaLLkKINQELGLTIVLITH 214
Cdd:COG4175 171 RVGLARALATDPDILLMDEAFSALDPlirremqdE-------LL-ELQAKLKKTIVFITH 222
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
17-248 |
3.44e-64 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 204.09 E-value: 3.44e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 17 IKIRGLNKFYQSQgqklHALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQNI---AELSHSELI 93
Cdd:COG4161 3 IQLKNINCFYGSH----QALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFdfsQKPSEKAIR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 94 QTRQRIGMIFQHFNLMSAKTVWEN-VALPLKVSNYNKADIDQRVNEVLALVGLADKSNYYPSQLSGGQKQRVGIARALVH 172
Cdd:COG4161 79 LLRQKVGMVFQQYNLWPHLTVMENlIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMM 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1194606020 173 HPEILLCDEATSALDPESTATILALLKKInQELGLTIVLITHEMQVIREICDQVVVIDQGEIVEAGQVwSVFSRPE 248
Cdd:COG4161 159 EPQVLLFDEPTAALDPEITAQVVEIIREL-SQTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQGDA-SHFTQPQ 232
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
15-256 |
1.68e-63 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 204.97 E-value: 1.68e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 15 PHIKIRGLNKFY-------QSQGQKLHALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQNIAEL 87
Cdd:COG4608 6 PLLEVRDLKKHFpvrgglfGRTVGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 88 SHSELIQTRQRIGMIFQhfNLMSA----KTVWENVALPLKVSN-YNKADIDQRVNEVLALVGL-ADKSNYYPSQLSGGQK 161
Cdd:COG4608 86 SGRELRPLRRRMQMVFQ--DPYASlnprMTVGDIIAEPLRIHGlASKAERRERVAELLELVGLrPEHADRYPHEFSGGQR 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 162 QRVGIARALVHHPEILLCDEATSALDPESTATILALLKKINQELGLTIVLITHEMQVIREICDQVVVIDQGEIVEAGQVW 241
Cdd:COG4608 164 QRIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDELGLTYLFISHDLSVVRHISDRVAVMYLGKIVEIAPRD 243
|
250
....*....|....*
gi 1194606020 242 SVFSRPEQQITQELL 256
Cdd:COG4608 244 ELYARPLHPYTQALL 258
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
17-248 |
3.12e-63 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 205.00 E-value: 3.12e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 17 IKIRGLNKFYQSqgqkLHALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQNIAelSHselIQTR 96
Cdd:COG1118 3 IEVRNISKRFGS----FTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLF--TN---LPPR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 97 QR-IGMIFQHFNLMSAKTVWENVALPLKVSNYNKADIDQRVNEVLALVGLADKSNYYPSQLSGGQKQRVGIARALVHHPE 175
Cdd:COG1118 74 ERrVGFVFQHYALFPHMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPE 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1194606020 176 ILLCDEATSALDPESTATILALLKKINQELGLTIVLITHEMQVIREICDQVVVIDQGEIVEAGQVWSVFSRPE 248
Cdd:COG1118 154 VLLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDRPA 226
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
15-247 |
6.53e-63 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 201.18 E-value: 6.53e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 15 PHIKIRGLNKFYQSqgqkLHALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQNIA-------EL 87
Cdd:COG4598 7 PALEVRDLHKSFGD----LEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIRlkpdrdgEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 88 ---SHSELIQTRQRIGMIFQHFNLMSAKTVWENVAL-PLKVSNYNKADIDQRVNEVLALVGLADKSNYYPSQLSGGQKQR 163
Cdd:COG4598 83 vpaDRRQLQRIRTRLGMVFQSFNLWSHMTVLENVIEaPVHVLGRPKAEAIERAEALLAKVGLADKRDAYPAHLSGGQQQR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 164 VGIARALVHHPEILLCDEATSALDPESTATILALLKKINQElGLTIVLITHEMQVIREICDQVVVIDQGEIVEAGQVWSV 243
Cdd:COG4598 163 AAIARALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEE-GRTMLVVTHEMGFARDVSSHVVFLHQGRIEEQGPPAEV 241
|
....
gi 1194606020 244 FSRP 247
Cdd:COG4598 242 FGNP 245
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
17-238 |
6.85e-63 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 201.72 E-value: 6.85e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 17 IKIRGLNKFYQSQGQK--------------------LHALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGS 76
Cdd:cd03294 1 IKIKGLYKIFGKNPQKafkllakgkskeeilkktgqTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 77 IHIHQQNIAELSHSELIQTR-QRIGMIFQHFNLMSAKTVWENVALPLKVSNYNKADIDQRVNEVLALVGLADKSNYYPSQ 155
Cdd:cd03294 81 VLIDGQDIAAMSRKELRELRrKKISMVFQSFALLPHRTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 156 LSGGQKQRVGIARALVHHPEILLCDEATSALDPESTATILALLKKINQELGLTIVLITHEMQVIREICDQVVVIDQGEIV 235
Cdd:cd03294 161 LSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLV 240
|
...
gi 1194606020 236 EAG 238
Cdd:cd03294 241 QVG 243
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
9-256 |
7.19e-63 |
|
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: 209.16 E-value: 7.19e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 9 QVDFSLPhikiRGLnkfYQSQGQKLHALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQvNTGSIHIHQQNIAELS 88
Cdd:COG4172 282 KVWFPIK----RGL---FRRTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIP-SEGEIRFDGQDLDGLS 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 89 HSELIQTRQRIGMIFQH-FNLMSAK-TVWENVALPLKVSN--YNKADIDQRVNEVLALVGL-ADKSNYYPSQLSGGQKQR 163
Cdd:COG4172 354 RRALRPLRRRMQVVFQDpFGSLSPRmTVGQIIAEGLRVHGpgLSAAERRARVAEALEEVGLdPAARHRYPHEFSGGQRQR 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 164 VGIARALVHHPEILLCDEATSALDPESTATILALLKKINQELGLTIVLITHEMQVIREICDQVVVIDQGEIVEAGQVWSV 243
Cdd:COG4172 434 IAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREHGLAYLFISHDLAVVRALAHRVMVMKDGKVVEQGPTEQV 513
|
250
....*....|...
gi 1194606020 244 FSRPEQQITQELL 256
Cdd:COG4172 514 FDAPQHPYTRALL 526
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
17-248 |
1.05e-62 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 200.24 E-value: 1.05e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 17 IKIRGLNKFYQSQgqklHALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQNI---AELSHSELI 93
Cdd:PRK11124 3 IQLNGINCFYGAH----QALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFdfsKTPSDKAIR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 94 QTRQRIGMIFQHFNLMSAKTVWEN-VALPLKVSNYNKADIDQRVNEVLALVGLADKSNYYPSQLSGGQKQRVGIARALVH 172
Cdd:PRK11124 79 ELRRNVGMVFQQYNLWPHLTVQQNlIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMM 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1194606020 173 HPEILLCDEATSALDPESTATILALLKKInQELGLTIVLITHEMQVIREICDQVVVIDQGEIVEAGQVwSVFSRPE 248
Cdd:PRK11124 159 EPQVLLFDEPTAALDPEITAQIVSIIREL-AETGITQVIVTHEVEVARKTASRVVYMENGHIVEQGDA-SCFTQPQ 232
|
|
| ectoine_ehuA |
TIGR03005 |
ectoine/hydroxyectoine ABC transporter, ATP-binding protein; Members of this family are the ... |
33-256 |
3.80e-62 |
|
ectoine/hydroxyectoine ABC transporter, ATP-binding protein; Members of this family are the ATP-binding protein of a conserved four gene ABC transporter operon found next to ectoine unilization operons and ectoine biosynthesis operons. Ectoine is a compatible solute that protects enzymes from high osmolarity. It is released by some species in response to hypoosmotic shock, and it is taken up by a number of bacteria as a compatible solute or for consumption. This family shows strong sequence similiarity to a number of amino acid ABC transporter ATP-binding proteins.
Pssm-ID: 132050 [Multi-domain] Cd Length: 252 Bit Score: 199.29 E-value: 3.80e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 33 LHALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHI------HQQN----IAELSHSELIQTRQRIGMI 102
Cdd:TIGR03005 13 LTVLDGLNFSVAAGEKVALIGPSGSGKSTILRILMTLEPIDEGQIQVegeqlyHMPGrngpLVPADEKHLRQMRNKIGMV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 103 FQHFNLMSAKTVWENVAL-PLKVSNYNKADIDQRVNEVLALVGLADKSNYYPSQLSGGQKQRVGIARALVHHPEILLCDE 181
Cdd:TIGR03005 93 FQSFNLFPHKTVLDNVTEaPVLVLGMARAEAEKRAMELLDMVGLADKADHMPAQLSGGQQQRVAIARALAMRPKVMLFDE 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1194606020 182 ATSALDPESTATILALLKKINQELGLTIVLITHEMQVIREICDQVVVIDQGEIVEAGQVWSVFSRPEQQITQELL 256
Cdd:TIGR03005 173 VTSALDPELVGEVLNVIRRLASEHDLTMLLVTHEMGFAREFADRVCFFDKGRIVEQGKPDEIFRQPKEERTREFL 247
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
17-281 |
1.21e-61 |
|
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: 198.83 E-value: 1.21e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 17 IKIRGLNKFYQSQG--QKlHALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQNIAELSHSELIQ 94
Cdd:TIGR04521 1 IKLKNVSYIYQPGTpfEK-KALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKLKD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 95 TRQRIGMIFQH-----FnlmsAKTVWENVALPLKVSNYNKADIDQRVNEVLALVGL----ADKSnyyPSQLSGGQKQRVG 165
Cdd:TIGR04521 80 LRKKVGLVFQFpehqlF----EETVYKDIAFGPKNLGLSEEEAEERVKEALELVGLdeeyLERS---PFELSGGQMRRVA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 166 IARALVHHPEILLCDEATSALDPESTATILALLKKINQELGLTIVLITHEMQVIREICDQVVVIDQGEIVEAGQVWSVFS 245
Cdd:TIGR04521 153 IAGVLAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVFS 232
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1194606020 246 RPEQ---------QITQELLNLEQITLPFKINPLPDEDSTHIIVK 281
Cdd:TIGR04521 233 DVDElekigldvpEITELARKLKEKGLPVPKDPLTVEEAADEILK 277
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
17-248 |
2.44e-61 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 196.30 E-value: 2.44e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 17 IKIRGLNKFYQSQgqklHALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQNIAELshseLIQTR 96
Cdd:cd03300 1 IELENVSKFYGGF----VALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNL----PPHKR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 97 QrIGMIFQHFNLMSAKTVWENVALPLKVSNYNKADIDQRVNEVLALVGLADKSNYYPSQLSGGQKQRVGIARALVHHPEI 176
Cdd:cd03300 73 P-VNTVFQNYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKV 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1194606020 177 LLCDEATSALDPESTATILALLKKINQELGLTIVLITHEMQVIREICDQVVVIDQGEIVEAGQVWSVFSRPE 248
Cdd:cd03300 152 LLLDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPA 223
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
36-256 |
3.03e-61 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 196.47 E-value: 3.03e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 36 LKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQNIAElSHSELIQTRQRIGMIFQHFNLMSAKTVW 115
Cdd:PRK09493 17 LHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVND-PKVDERLIRQEAGMVFQQFYLFPHLTAL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 116 ENVAL-PLKVSNYNKADIDQRVNEVLALVGLADKSNYYPSQLSGGQKQRVGIARALVHHPEILLCDEATSALDPESTATI 194
Cdd:PRK09493 96 ENVMFgPLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTSALDPELRHEV 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1194606020 195 LALLKKINQElGLTIVLITHEMQVIREICDQVVVIDQGEIVEAGQVWSVFSRPEQQITQELL 256
Cdd:PRK09493 176 LKVMQDLAEE-GMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPPSQRLQEFL 236
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
17-257 |
7.16e-61 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 195.74 E-value: 7.16e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 17 IKIRGLNKfyQSQGQKLhaLKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQNI---AELSHSE-L 92
Cdd:PRK11264 4 IEVKNLVK--KFHGQTV--LHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIdtaRSLSQQKgL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 93 I-QTRQRIGMIFQHFNLMSAKTVWENVAL-PLKVSNYNKADIDQRVNEVLALVGLADKSNYYPSQLSGGQKQRVGIARAL 170
Cdd:PRK11264 80 IrQLRQHVGFVFQNFNLFPHRTVLENIIEgPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 171 VHHPEILLCDEATSALDPESTATILALLKKINQElGLTIVLITHEMQVIREICDQVVVIDQGEIVEAGQVWSVFSRPEQQ 250
Cdd:PRK11264 160 AMRPEVILFDEPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADPQQP 238
|
....*..
gi 1194606020 251 ITQELLN 257
Cdd:PRK11264 239 RTRQFLE 245
|
|
| heterocyst_DevA |
TIGR02982 |
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly ... |
17-235 |
7.89e-60 |
|
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: 192.16 E-value: 7.89e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 17 IKIRGLNKFYQSQGQKLHALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQNIAELSHSELIQTR 96
Cdd:TIGR02982 2 ISIRNLNHYYGHGSLRKQVLFDINLEINPGEIVILTGPSGSGKTTLLTLIGGLRSVQEGSLKVLGQELHGASKKQLVQLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 97 QRIGMIFQHFNLMSAKTVWENVALPLKVS-NYNKADIDQRVNEVLALVGLADKSNYYPSQLSGGQKQRVGIARALVHHPE 175
Cdd:TIGR02982 82 RRIGYIFQAHNLLGFLTARQNVQMALELQpNLSYQEARERARAMLEAVGLGDHLNYYPHNLSGGQKQRVAIARALVHHPK 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 176 ILLCDEATSALDPESTATILALLKKINQELGLTIVLITHEMQvIREICDQVVVIDQGEIV 235
Cdd:TIGR02982 162 LVLADEPTAALDSKSGRDVVELMQKLAKEQGCTILMVTHDNR-ILDVADRILQMEDGKLL 220
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
17-247 |
9.13e-60 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 192.52 E-value: 9.13e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 17 IKIRGLNKFYQSqGQKlhALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQNIAELSHSELiqtR 96
Cdd:cd03295 1 IEFENVTKRYGG-GKK--AVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVEL---R 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 97 QRIGMIFQHFNLMSAKTVWENVALPLKVSNYNKADIDQRVNEVLALVGLADKS--NYYPSQLSGGQKQRVGIARALVHHP 174
Cdd:cd03295 75 RKIGYVIQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLDPAEfaDRYPHELSGGQQQRVGVARALAADP 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1194606020 175 EILLCDEATSALDPESTATILALLKKINQELGLTIVLITHEMQVIREICDQVVVIDQGEIVEAGQVWSVFSRP 247
Cdd:cd03295 155 PLLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSP 227
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
17-268 |
1.05e-59 |
|
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: 193.42 E-value: 1.05e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 17 IKIRGLNKFYQsqGQKLHALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIhqQNIAELSHSELIQTR 96
Cdd:TIGR04520 1 IEVENVSFSYP--ESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTV--DGLDTLDEENLWEIR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 97 QRIGMIFQH-FNLMSAKTVWENVALPLKVSNYNKADIDQRVNEVLALVGLADKSNYYPSQLSGGQKQRVGIARALVHHPE 175
Cdd:TIGR04520 77 KKVGMVFQNpDNQFVGATVEDDVAFGLENLGVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLAMRPD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 176 ILLCDEATSALDPESTATILALLKKINQELGLTIVLITHEMQVIREiCDQVVVIDQGEIVEAGQVWSVFSRPEQ------ 249
Cdd:TIGR04520 157 IIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEAVL-ADRVIVMNKGKIVAEGTPREIFSQVELlkeigl 235
|
250 260
....*....|....*....|....
gi 1194606020 250 ---QITQ--ELLNLEQITLPFKIN 268
Cdd:TIGR04520 236 dvpFITElaKALKKRGIPLPPDIL 259
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
17-257 |
1.80e-58 |
|
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: 197.60 E-value: 1.80e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 17 IKIRGLNKFYQSQGQKLHALKEINLDIPQGKILGIIGKSGAGKS----SLLRTLNGLEQVNTGSIHIHQQNIAELSHSEL 92
Cdd:COG4172 7 LSVEDLSVAFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSEREL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 93 IQTR-QRIGMIFQhfNLMSA----KTVWENVALPLKV-SNYNKADIDQRVNEVLALVGLAD---KSNYYPSQLSGGQKQR 163
Cdd:COG4172 87 RRIRgNRIAMIFQ--EPMTSlnplHTIGKQIAEVLRLhRGLSGAAARARALELLERVGIPDperRLDAYPHQLSGGQRQR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 164 VGIARALVHHPEILLCDEATSALDPESTATILALLKKINQELGLTIVLITHEMQVIREICDQVVVIDQGEIVEAGQVWSV 243
Cdd:COG4172 165 VMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFADRVAVMRQGEIVEQGPTAEL 244
|
250
....*....|....
gi 1194606020 244 FSRPEQQITQELLN 257
Cdd:COG4172 245 FAAPQHPYTRKLLA 258
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
35-234 |
8.32e-58 |
|
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: 186.84 E-value: 8.32e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 35 ALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQNIAELSHSELIQTRQRIGMIFQHFNLMSAKTV 114
Cdd:cd03292 16 ALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYLRRKIGVVFQDFRLLPDRNV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 115 WENVALPLKVSNYNKADIDQRVNEVLALVGLADKSNYYPSQLSGGQKQRVGIARALVHHPEILLCDEATSALDPESTATI 194
Cdd:cd03292 96 YENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTTWEI 175
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1194606020 195 LALLKKINQElGLTIVLITHEMQVIREICDQVVVIDQGEI 234
Cdd:cd03292 176 MNLLKKINKA-GTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
17-256 |
1.42e-57 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 186.50 E-value: 1.42e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 17 IKIRGLNKFYQsqgqklHALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQNIAELSHSeliqtr 96
Cdd:COG3840 2 LRLDDLTYRYG------DFPLRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPA------ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 97 QR-IGMIFQHFNLMSAKTVWENVALPLKVS-NYNKADIdQRVNEVLALVGLADKSNYYPSQLSGGQKQRVGIARALVHHP 174
Cdd:COG3840 70 ERpVSMLFQENNLFPHLTVAQNIGLGLRPGlKLTAEQR-AQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 175 EILLCDEATSALDPESTATILALLKKINQELGLTIVLITHEMQVIREICDQVVVIDQGEIVEAGQVWSVFSRPEQQITQE 254
Cdd:COG3840 149 PILLLDEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPPALAA 228
|
..
gi 1194606020 255 LL 256
Cdd:COG3840 229 YL 230
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
17-256 |
4.34e-57 |
|
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: 186.02 E-value: 4.34e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 17 IKIRGLNKFYQSQgqklHALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQNIAELSHSELiqtR 96
Cdd:COG1120 2 LEAENLSVGYGGR----PVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRREL---A 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 97 QRIGMIFQHFNLMSAKTVWENVAL---PLK--VSNYNKADiDQRVNEVLALVGLADKSNYYPSQLSGGQKQRVGIARALV 171
Cdd:COG1120 75 RRIAYVPQEPPAPFGLTVRELVALgryPHLglFGRPSAED-REAVEEALERTGLEHLADRPVDELSGGERQRVLIARALA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 172 HHPEILLCDEATSALDPESTATILALLKKINQELGLTIVLITHEMQVIREICDQVVVIDQGEIVEAGqvwsvfsRPEQQI 251
Cdd:COG1120 154 QEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQG-------PPEEVL 226
|
....*
gi 1194606020 252 TQELL 256
Cdd:COG1120 227 TPELL 231
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
17-257 |
1.46e-56 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 185.04 E-value: 1.46e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 17 IKIRGLNKFYQSQG-----QKLHALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQniaELSHSE 91
Cdd:COG4167 5 LEVRNLSKTFKYRTglfrrQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGH---KLEYGD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 92 lIQTR-QRIGMIFQHFN--LMSAKTVWENVALPLKV-SNYNKADIDQRVNEVLALVGL-ADKSNYYPSQLSGGQKQRVGI 166
Cdd:COG4167 82 -YKYRcKHIRMIFQDPNtsLNPRLNIGQILEEPLRLnTDLTAEEREERIFATLRLVGLlPEHANFYPHMLSSGQKQRVAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 167 ARALVHHPEILLCDEATSALDPESTATILALLKKINQELGLTIVLITHEMQVIREICDQVVVIDQGEIVEAGQVWSVFSR 246
Cdd:COG4167 161 ARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKHISDKVLVMHQGEVVEYGKTAEVFAN 240
|
250
....*....|.
gi 1194606020 247 PEQQITQELLN 257
Cdd:COG4167 241 PQHEVTKRLIE 251
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
17-247 |
8.43e-56 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 182.54 E-value: 8.43e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 17 IKIRGLNKFYQSqgqkLHALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQNIAELShselIQTR 96
Cdd:cd03296 3 IEVRNVSKRFGD----FVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVP----VQER 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 97 QrIGMIFQHFNLMSAKTVWENVALPLKV----SNYNKADIDQRVNEVLALVGLADKSNYYPSQLSGGQKQRVGIARALVH 172
Cdd:cd03296 75 N-VGFVFQHYALFRHMTVFDNVAFGLRVkprsERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1194606020 173 HPEILLCDEATSALDPESTATILALLKKINQELGLTIVLITHEMQVIREICDQVVVIDQGEIVEAGQVWSVFSRP 247
Cdd:cd03296 154 EPKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHP 228
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
17-245 |
8.88e-56 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 182.60 E-value: 8.88e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 17 IKIRGLNKFYQSQgqklHALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQNIAelshseliQTR 96
Cdd:COG1121 7 IELENLTVSYGGR----PVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPR--------RAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 97 QRIGMIFQHFNLMSAK--TVWENVALPLK-----VSNYNKADiDQRVNEVLALVGLADKSNYYPSQLSGGQKQRVGIARA 169
Cdd:COG1121 75 RRIGYVPQRAEVDWDFpiTVRDVVLMGRYgrrglFRRPSRAD-REAVDEALERVGLEDLADRPIGELSGGQQQRVLLARA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1194606020 170 LVHHPEILLCDEATSALDPESTATILALLKKINQElGLTIVLITHEMQVIREICDQVVVIDQGeIVEAGQVWSVFS 245
Cdd:COG1121 154 LAQDPDLLLLDEPFAGVDAATEEALYELLRELRRE-GKTILVVTHDLGAVREYFDRVLLLNRG-LVAHGPPEEVLT 227
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
17-256 |
2.33e-55 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 184.90 E-value: 2.33e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 17 IKIRGLNKFYQsqgqKLHALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQNIAELSHSEliqtr 96
Cdd:PRK10851 3 IEIANIKKSFG----RTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARD----- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 97 QRIGMIFQHFNLMSAKTVWENVALPLKV----SNYNKADIDQRVNEVLALVGLADKSNYYPSQLSGGQKQRVGIARALVH 172
Cdd:PRK10851 74 RKVGFVFQHYALFRHMTVFDNIAFGLTVlprrERPNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 173 HPEILLCDEATSALDPESTATILALLKKINQELGLTIVLITHEMQVIREICDQVVVIDQGEIVEAG---QVWSVfsrPEQ 249
Cdd:PRK10851 154 EPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGtpdQVWRE---PAT 230
|
....*..
gi 1194606020 250 QITQELL 256
Cdd:PRK10851 231 RFVLEFM 237
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
17-240 |
1.29e-54 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 179.28 E-value: 1.29e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 17 IKIRGLNKFYQsqgqKLHALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQNiaelSHSELIQTR 96
Cdd:COG4555 2 IEVENLSKKYG----KVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGED----VRKEPREAR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 97 QRIGMIFQHFNLMSAKTVWENVALPLKVSNYNKADIDQRVNEVLALVGLADKSNYYPSQLSGGQKQRVGIARALVHHPEI 176
Cdd:COG4555 74 RQIGVLPDERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKV 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1194606020 177 LLCDEATSALDPESTATILALLKKINQElGLTIVLITHEMQVIREICDQVVVIDQGEIVEAGQV 240
Cdd:COG4555 154 LLLDEPTNGLDVMARRLLREILRALKKE-GKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSL 216
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
17-238 |
3.55e-54 |
|
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: 177.45 E-value: 3.55e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 17 IKIRGLNKFYQSQgqklHALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQNIAELSHSEliqtr 96
Cdd:cd03301 1 VELENVTKRFGNV----TALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKD----- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 97 QRIGMIFQHFNLMSAKTVWENVALPLKVSNYNKADIDQRVNEVLALVGLADKSNYYPSQLSGGQKQRVGIARALVHHPEI 176
Cdd:cd03301 72 RDIAMVFQNYALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKV 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1194606020 177 LLCDEATSALDPESTATILALLKKINQELGLTIVLITHEMQVIREICDQVVVIDQGEIVEAG 238
Cdd:cd03301 152 FLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
15-238 |
4.61e-54 |
|
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: 178.31 E-value: 4.61e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 15 PHIKIRGLNKFYqsqGqKLHALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQNIAELSHSELiq 94
Cdd:COG0411 3 PLLEVRGLTKRF---G-GLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRI-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 95 TRQRIGMIFQHFNLMSAKTVWENVA---------------LPLKVSNYNKADIDQRVNEVLALVGLADKSNYYPSQLSGG 159
Cdd:COG0411 77 ARLGIARTFQNPRLFPELTVLENVLvaaharlgrgllaalLRLPRARREEREARERAEELLERVGLADRADEPAGNLSYG 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1194606020 160 QKQRVGIARALVHHPEILLCDEATSALDPESTATILALLKKINQELGLTIVLITHEMQVIREICDQVVVIDQGEIVEAG 238
Cdd:COG0411 157 QQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFGRVIAEG 235
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
17-234 |
5.88e-54 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 175.28 E-value: 5.88e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 17 IKIRGLNKFYQSQgqklHALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQNIAElshsELIQTR 96
Cdd:cd03230 1 IEVRNLSKRYGKK----TALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK----EPEEVK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 97 QRIGMIFQHFNLMSAKTVWENValplkvsnynkadidqrvnevlalvgladksnyypsQLSGGQKQRVGIARALVHHPEI 176
Cdd:cd03230 73 RRIGYLPEEPSLYENLTVRENL------------------------------------KLSGGMKQRLALAQALLHDPEL 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1194606020 177 LLCDEATSALDPESTATILALLKKINQElGLTIVLITHEMQVIREICDQVVVIDQGEI 234
Cdd:cd03230 117 LILDEPTSGLDPESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
15-238 |
1.19e-53 |
|
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: 187.73 E-value: 1.19e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 15 PHIKIRGLNKFYQSQGQKlhALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQNIAELSHSELiq 94
Cdd:COG2274 472 GDIELENVSFRYPGDSPP--VLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASL-- 547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 95 tRQRIGMIFQHFNLMSAkTVWENVALplkvsnyNKADI-DQRVNEVLALVGLADKSNYYP-----------SQLSGGQKQ 162
Cdd:COG2274 548 -RRQIGVVLQDVFLFSG-TIRENITL-------GDPDAtDEEIIEAARLAGLHDFIEALPmgydtvvgeggSNLSGGQRQ 618
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1194606020 163 RVGIARALVHHPEILLCDEATSALDPESTATILALLKKINQelGLTIVLITHEMQVIReICDQVVVIDQGEIVEAG 238
Cdd:COG2274 619 RLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLK--GRTVIIIAHRLSTIR-LADRIIVLDKGRIVEDG 691
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
17-234 |
3.18e-53 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 174.62 E-value: 3.18e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 17 IKIRGLNkfYQSQGQKLhaLKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQNIAELSHSELiqtR 96
Cdd:COG4619 1 LELEGLS--FRVGGKPI--LSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEW---R 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 97 QRIGMIFQHFNLMsAKTVWENVALPLKVSNynKADIDQRVNEVLALVGLADKSNYYP-SQLSGGQKQRVGIARALVHHPE 175
Cdd:COG4619 74 RQVAYVPQEPALW-GGTVRDNLPFPFQLRE--RKFDRERALELLERLGLPPDILDKPvERLSGGERQRLALIRALLLQPD 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1194606020 176 ILLCDEATSALDPESTATILALLKKINQELGLTIVLITHEMQVIREICDQVVVIDQGEI 234
Cdd:COG4619 151 VLLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
17-233 |
5.00e-52 |
|
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: 170.26 E-value: 5.00e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 17 IKIRGLNKFYQSQGQKlhALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQNIAELSHSELiqtR 96
Cdd:cd03228 1 IEFKNVSFSYPGRPKP--VLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESL---R 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 97 QRIGMIFQHFNLMSAkTVWENValplkvsnynkadidqrvnevlalvgladksnyypsqLSGGQKQRVGIARALVHHPEI 176
Cdd:cd03228 76 KNIAYVPQDPFLFSG-TIRENI-------------------------------------LSGGQRQRIAIARALLRDPPI 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1194606020 177 LLCDEATSALDPESTATILALLKKINQelGLTIVLITHEMQVIReICDQVVVIDQGE 233
Cdd:cd03228 118 LILDEATSALDPETEALILEALRALAK--GKTVIVIAHRLSTIR-DADRIIVLDDGR 171
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
36-257 |
1.55e-51 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 172.08 E-value: 1.55e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 36 LKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQNIAELSHS----------ELIQTRQRIGMIFQH 105
Cdd:PRK10619 21 LKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKdgqlkvadknQLRLLRTRLTMVFQH 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 106 FNLMSAKTVWENV-ALPLKVSNYNKADIDQRVNEVLALVGLADKSN-YYPSQLSGGQKQRVGIARALVHHPEILLCDEAT 183
Cdd:PRK10619 101 FNLWSHMTVLENVmEAPIQVLGLSKQEARERAVKYLAKVGIDERAQgKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPT 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1194606020 184 SALDPESTATILALLKKINQElGLTIVLITHEMQVIREICDQVVVIDQGEIVEAGQVWSVFSRPEQQITQELLN 257
Cdd:PRK10619 181 SALDPELVGEVLRIMQQLAEE-GKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGNPQSPRLQQFLK 253
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
16-274 |
2.20e-50 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 171.04 E-value: 2.20e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 16 HIKIRGLNKFYQSQGQKLHALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQNIAELSHSELIQT 95
Cdd:PRK15079 17 HFDIKDGKQWFWQPPKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRAV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 96 RQRIGMIFQH--FNLMSAKTVWENVALPLKV--SNYNKADIDQRVNEVLALVGL-ADKSNYYPSQLSGGQKQRVGIARAL 170
Cdd:PRK15079 97 RSDIQMIFQDplASLNPRMTIGEIIAEPLRTyhPKLSRQEVKDRVKAMMLKVGLlPNLINRYPHEFSGGQCQRIGIARAL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 171 VHHPEILLCDEATSALDPESTATILALLKKINQELGLTIVLITHEMQVIREICDQVVVIDQGEIVEAGQVWSVFSRPEQQ 250
Cdd:PRK15079 177 ILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNPLHP 256
|
250 260
....*....|....*....|....
gi 1194606020 251 ITQELLNLEqitlpfkinPLPDED 274
Cdd:PRK15079 257 YTKALMSAV---------PIPDPD 271
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
35-238 |
2.56e-50 |
|
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: 167.55 E-value: 2.56e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 35 ALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQNIAelshSELIQTRQRIGMIFQHFNLMSAKTV 114
Cdd:cd03265 15 AVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVV----REPREVRRRIGIVFQDLSVDDELTG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 115 WENVALPLKVSNYNKADIDQRVNEVLALVGLADKSNYYPSQLSGGQKQRVGIARALVHHPEILLCDEATSALDPESTATI 194
Cdd:cd03265 91 WENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRAHV 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1194606020 195 LALLKKINQELGLTIVLITHEMQVIREICDQVVVIDQGEIVEAG 238
Cdd:cd03265 171 WEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEG 214
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
17-235 |
3.37e-50 |
|
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: 167.61 E-value: 3.37e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 17 IKIRGLNKFYqsqGqKLHALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQNIAELSHSELIqtR 96
Cdd:cd03219 1 LEVRGLTKRF---G-GLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIA--R 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 97 QRIGMIFQHFNLMSAKTVWENVALPLKVSN----------YNKADIDQRVNEVLALVGLADKSNYYPSQLSGGQKQRVGI 166
Cdd:cd03219 75 LGIGRTFQIPRLFPELTVLENVMVAAQARTgsglllararREEREARERAEELLERVGLADLADRPAGELSYGQQRRLEI 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1194606020 167 ARALVHHPEILLCDEATSALDPESTATILALLKKINQElGLTIVLITHEMQVIREICDQVVVIDQGEIV 235
Cdd:cd03219 155 ARALATDPKLLLLDEPAAGLNPEETEELAELIRELRER-GITVLLVEHDMDVVMSLADRVTVLDQGRVI 222
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
17-261 |
1.29e-48 |
|
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: 163.66 E-value: 1.29e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 17 IKIRGLNKFYqsqgqKLHALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQNIAELShseliQTR 96
Cdd:cd03299 1 LKVENLSKDW-----KEFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLP-----PEK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 97 QRIGMIFQHFNLMSAKTVWENVALPLKVSNYNKADIDQRVNEVLALVGLADKSNYYPSQLSGGQKQRVGIARALVHHPEI 176
Cdd:cd03299 71 RDISYVPQNYALFPHMTVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 177 LLCDEATSALDPESTATILALLKKINQELGLTIVLITHEMQVIREICDQVVVIDQGEIVEAGQVWSVFSRPEQQITQELL 256
Cdd:cd03299 151 LLLDEPFSALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPKNEFVAEFL 230
|
....*
gi 1194606020 257 NLEQI 261
Cdd:cd03299 231 GFNNI 235
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
17-256 |
2.18e-48 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 163.86 E-value: 2.18e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 17 IKIRGLNKFYQSQgqklHALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNT-----GSIHIHQQNIAElSHSE 91
Cdd:PRK14267 5 IETVNLRVYYGSN----HVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNEearveGEVRLFGRNIYS-PDVD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 92 LIQTRQRIGMIFQHFNLMSAKTVWENVALPLKVSNY--NKADIDQRVNEVLALVGL----ADKSNYYPSQLSGGQKQRVG 165
Cdd:PRK14267 80 PIEVRREVGMVFQYPNPFPHLTIYDNVAIGVKLNGLvkSKKELDERVEWALKKAALwdevKDRLNDYPSNLSGGQRQRLV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 166 IARALVHHPEILLCDEATSALDPESTATILALLKKINQElgLTIVLITHEMQVIREICDQVVVIDQGEIVEAGQVWSVFS 245
Cdd:PRK14267 160 IARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKE--YTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFE 237
|
250
....*....|.
gi 1194606020 246 RPEQQITQELL 256
Cdd:PRK14267 238 NPEHELTEKYV 248
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
34-232 |
3.12e-48 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 161.93 E-value: 3.12e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 34 HALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQNIAelshseliQTRQRIGMIFQHFNLMSAK- 112
Cdd:cd03235 13 PVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLE--------KERKRIGYVPQRRSIDRDFp 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 113 -TVWENVALPL-----KVSNYNKADiDQRVNEVLALVGLADKSNYYPSQLSGGQKQRVGIARALVHHPEILLCDEATSAL 186
Cdd:cd03235 85 iSVRDVVLMGLyghkgLFRRLSKAD-KAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAGV 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1194606020 187 DPESTATILALLKKINQElGLTIVLITHEMQVIREICDQVVVIDQG 232
Cdd:cd03235 164 DPKTQEDIYELLRELRRE-GMTILVVTHDLGLVLEYFDRVLLLNRT 208
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
15-238 |
5.82e-48 |
|
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: 170.33 E-value: 5.82e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 15 PHIKIRGLNKFYQSQGQKlhALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQNIAELSHSELiq 94
Cdd:COG4987 332 PSLELEDVSFRYPGAGRP--VLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDL-- 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 95 tRQRIGMIFQHFNLMSAkTVWEN--VALPlkvsnynKADiDQRVNEVLALVGLADKSNYYP-----------SQLSGGQK 161
Cdd:COG4987 408 -RRRIAVVPQRPHLFDT-TLRENlrLARP-------DAT-DEELWAALERVGLGDWLAALPdgldtwlgeggRRLSGGER 477
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1194606020 162 QRVGIARALVHHPEILLCDEATSALDPESTATILALLKKINQelGLTIVLITHEMQVIrEICDQVVVIDQGEIVEAG 238
Cdd:COG4987 478 RRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALA--GRTVLLITHRLAGL-ERMDRILVLEDGRIVEQG 551
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
35-238 |
9.32e-48 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 169.96 E-value: 9.32e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 35 ALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQNIAELSHSELiqtRQRIGMIFQHFNLMSAkTV 114
Cdd:COG1132 355 VLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESL---RRQIGVVPQDTFLFSG-TI 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 115 WENVAlplkvsnYNKADI-DQRVNEVLALVGLADKSNYYP-----------SQLSGGQKQRVGIARALVHHPEILLCDEA 182
Cdd:COG1132 431 RENIR-------YGRPDAtDEEVEEAAKAAQAHEFIEALPdgydtvvgergVNLSGGQRQRIAIARALLKDPPILILDEA 503
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1194606020 183 TSALDPESTATILALLKKINQelGLTIVLITHEMQVIREiCDQVVVIDQGEIVEAG 238
Cdd:COG1132 504 TSALDTETEALIQEALERLMK--GRTTIVIAHRLSTIRN-ADRILVLDDGRIVEQG 556
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
36-184 |
1.27e-47 |
|
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: 158.19 E-value: 1.27e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 36 LKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQniaELSHSELIQTRQRIGMIFQHFNLMSAKTVW 115
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQ---DLTDDERKSLRKEIGYVFQDPQLFPRLTVR 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1194606020 116 ENVALPLKVSNYNKADIDQRVNEVLALVGLADKSN----YYPSQLSGGQKQRVGIARALVHHPEILLCDEATS 184
Cdd:pfam00005 78 ENLRLGLLLKGLSKREKDARAEEALEKLGLGDLADrpvgERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
17-238 |
1.65e-47 |
|
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: 160.05 E-value: 1.65e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 17 IKIRGLNKFYQSQgqklHALKEINLDIPQGkILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQNIAElSHSELiqtR 96
Cdd:cd03264 1 LQLENLTKRYGKK----RALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLK-QPQKL---R 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 97 QRIGMIFQHFNLMSAKTVWENVALPLKVSNYNKADIDQRVNEVLALVGLADKSNYYPSQLSGGQKQRVGIARALVHHPEI 176
Cdd:cd03264 72 RRIGYLPQEFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSI 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1194606020 177 LLCDEATSALDPESTATILALLKKINQElgLTIVLITHEMQVIREICDQVVVIDQGEIVEAG 238
Cdd:cd03264 152 LIVDEPTAGLDPEERIRFRNLLSELGED--RIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
20-256 |
2.61e-47 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 163.21 E-value: 2.61e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 20 RGLNKFYQ-SQG-----QKLHALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQNIAELSHSELI 93
Cdd:PRK11308 9 IDLKKHYPvKRGlfkpeRLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAQK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 94 QTRQRIGMIFQ--HFNLMSAKTVWENVALPLKV-SNYNKADIDQRVNEVLALVGL-ADKSNYYPSQLSGGQKQRVGIARA 169
Cdd:PRK11308 89 LLRQKIQIVFQnpYGSLNPRKKVGQILEEPLLInTSLSAAERREKALAMMAKVGLrPEHYDRYPHMFSGGQRQRIAIARA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 170 LVHHPEILLCDEATSALDPESTATILALLKKINQELGLTIVLITHEMQVIREICDQVVVIDQGEIVEAGQVWSVFSRPEQ 249
Cdd:PRK11308 169 LMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFNNPRH 248
|
....*..
gi 1194606020 250 QITQELL 256
Cdd:PRK11308 249 PYTQALL 255
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
34-237 |
6.33e-47 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 158.88 E-value: 6.33e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 34 HALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQNIAELSHSELIQTRQRIGMIFQHFNLMSAKT 113
Cdd:PRK10908 16 QALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPFLRRQIGMIFQDHHLLMDRT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 114 VWENVALPLKVSNYNKADIDQRVNEVLALVGLADKSNYYPSQLSGGQKQRVGIARALVHHPEILLCDEATSALDPESTAT 193
Cdd:PRK10908 96 VYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSEG 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1194606020 194 ILALLKKINQeLGLTIVLITHEMQVIREICDQVVVIDQGEIVEA 237
Cdd:PRK10908 176 ILRLFEEFNR-VGVTVLMATHDIGLISRRSYRMLTLSDGHLHGG 218
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
18-238 |
6.99e-47 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 157.21 E-value: 6.99e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 18 KIRGLNKFYQSQgqklHALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQNIAELSHSELiqtRQ 97
Cdd:cd03214 1 EVENLSVGYGGR----TVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKEL---AR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 98 RIGMIFQhfnlmsaktvwenvalplkvsnynkadidqrvneVLALVGLADKSNYYPSQLSGGQKQRVGIARALVHHPEIL 177
Cdd:cd03214 74 KIAYVPQ----------------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPIL 119
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1194606020 178 LCDEATSALDPESTATILALLKKINQELGLTIVLITHEMQVIREICDQVVVIDQGEIVEAG 238
Cdd:cd03214 120 LLDEPTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
20-258 |
8.62e-47 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 166.42 E-value: 8.62e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 20 RGLnkFYQSQGQKlHALKEINLDIPQGKILGIIGKSGAGKSS----LLRTLNgleqvNTGSIHIHQQNIAELSHSELIQT 95
Cdd:PRK15134 289 KGI--LKRTVDHN-VVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLIN-----SQGEIWFDGQPLHNLNRRQLLPV 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 96 RQRIGMIFQHFN--LMSAKTVWENVALPLKV--SNYNKADIDQRVNEVLALVGLADKSNY-YPSQLSGGQKQRVGIARAL 170
Cdd:PRK15134 361 RHRIQVVFQDPNssLNPRLNVLQIIEEGLRVhqPTLSAAQREQQVIAVMEEVGLDPETRHrYPAEFSGGQRQRIAIARAL 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 171 VHHPEILLCDEATSALDPESTATILALLKKINQELGLTIVLITHEMQVIREICDQVVVIDQGEIVEAGQVWSVFSRPEQQ 250
Cdd:PRK15134 441 ILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERVFAAPQQE 520
|
....*...
gi 1194606020 251 ITQELLNL 258
Cdd:PRK15134 521 YTRQLLAL 528
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
17-254 |
2.19e-46 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 158.54 E-value: 2.19e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 17 IKIRGLN-KFYQSQgqklhALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGL-----EQVNTGSIHIHQQNIAELSHS 90
Cdd:PRK14247 4 IEIRDLKvSFGQVE-----VLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQDIFKMDVI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 91 ELiqtRQRIGMIFQHFNLMSAKTVWENVALPLKVSNY--NKADIDQRVNEVLALVGL----ADKSNYYPSQLSGGQKQRV 164
Cdd:PRK14247 79 EL---RRRVQMVFQIPNPIPNLSIFENVALGLKLNRLvkSKKELQERVRWALEKAQLwdevKDRLDAPAGKLSGGQQQRL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 165 GIARALVHHPEILLCDEATSALDPESTATILALLKKINQElgLTIVLITHEMQVIREICDQVVVIDQGEIVEAGQVWSVF 244
Cdd:PRK14247 156 CIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKD--MTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVF 233
|
250
....*....|
gi 1194606020 245 SRPEQQITQE 254
Cdd:PRK14247 234 TNPRHELTEK 243
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
15-238 |
2.28e-46 |
|
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: 165.70 E-value: 2.28e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 15 PHIKIRGLNKFYQSQGQklhALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQNIAELSHSELiq 94
Cdd:COG4988 335 PSIELEDVSFSYPGGRP---ALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASW-- 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 95 tRQRIGMIFQHFNLMSAkTVWENVALplkvsnYNKADIDQRVNEVLALVGLADKSNYYP-----------SQLSGGQKQR 163
Cdd:COG4988 410 -RRQIAWVPQNPYLFAG-TIRENLRL------GRPDASDEELEAALEAAGLDEFVAALPdgldtplgeggRGLSGGQAQR 481
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1194606020 164 VGIARALVHHPEILLCDEATSALDPESTATILALLKKINQelGLTIVLITHEMQVIREiCDQVVVIDQGEIVEAG 238
Cdd:COG4988 482 LALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAK--GRTVILITHRLALLAQ-ADRILVLDDGRIVEQG 553
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
17-235 |
2.29e-46 |
|
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: 157.28 E-value: 2.29e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 17 IKIRGLNKFYqSQGQKlHALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQNIaelsHSELIQTR 96
Cdd:cd03263 1 LQIRNLTKTY-KKGTK-PAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSI----RTDRKAAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 97 QRIGMIFQHFNLMSAKTVWENVALPLKVSNYNKADIDQRVNEVLALVGLADKSNYYPSQLSGGQKQRVGIARALVHHPEI 176
Cdd:cd03263 75 QSLGYCPQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSV 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1194606020 177 LLCDEATSALDPESTATILALLKKINQelGLTIVLITHEMQVIREICDQVVVIDQGEIV 235
Cdd:cd03263 155 LLLDEPTSGLDPASRRAIWDLILEVRK--GRSIILTTHSMDEAEALCDRIAIMSDGKLR 211
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
35-238 |
5.08e-46 |
|
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin resistance ABC transporter, ATP binding subunit in bacteria and archaea. This model is restricted in its scope to preferentially recognize the ATP binding subunit associated with effux of the drug, daunorubicin. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. In eukaryotes proteins of similar function include p-gyco proteins, multidrug resistance protein etc. [Transport and binding proteins, Other]
Pssm-ID: 130256 [Multi-domain] Cd Length: 302 Bit Score: 159.09 E-value: 5.08e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 35 ALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQNIAelshSELIQTRQRIGMIFQHFNLMSAKTV 114
Cdd:TIGR01188 8 AVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVV----REPRKVRRSIGIVPQYASVDEDLTG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 115 WENVALPLKVSNYNKADIDQRVNEVLALVGLADKSNYYPSQLSGGQKQRVGIARALVHHPEILLCDEATSALDPESTATI 194
Cdd:TIGR01188 84 RENLEMMGRLYGLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPRTRRAI 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1194606020 195 LALLKKINqELGLTIVLITHEMQVIREICDQVVVIDQGEIVEAG 238
Cdd:TIGR01188 164 WDYIRALK-EEGVTILLTTHYMEEADKLCDRIAIIDHGRIIAEG 206
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
19-234 |
8.33e-46 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 157.15 E-value: 8.33e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 19 IRGLNKFYqsqGQKlHALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIhihqqniaeLSHSE-LIQTRQ 97
Cdd:PRK11247 15 LNAVSKRY---GER-TVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL---------LAGTApLAEARE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 98 RIGMIFQHFNLMSAKTVWENVALPLKvsnynkADIDQRVNEVLALVGLADKSNYYPSQLSGGQKQRVGIARALVHHPEIL 177
Cdd:PRK11247 82 DTRLMFQDARLLPWKKVIDNVGLGLK------GQWRDAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1194606020 178 LCDEATSALDPESTATILALLKKINQELGLTIVLITHEMQVIREICDQVVVIDQGEI 234
Cdd:PRK11247 156 LLDEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
15-238 |
1.57e-45 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 159.73 E-value: 1.57e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 15 PHIKIRGLNKFYQSQgqklHALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQNIAELShselIQ 94
Cdd:PRK09452 13 PLVELRGISKSFDGK----EVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVP----AE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 95 TRQrIGMIFQHFNLMSAKTVWENVALPLKVSNYNKADIDQRVNEVLALVGLADKSNYYPSQLSGGQKQRVGIARALVHHP 174
Cdd:PRK09452 85 NRH-VNTVFQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1194606020 175 EILLCDEATSALDPESTATILALLKKINQELGLTIVLITHEMQVIREICDQVVVIDQGEIVEAG 238
Cdd:PRK09452 164 KVLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDG 227
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
18-233 |
3.14e-45 |
|
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: 152.40 E-value: 3.14e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 18 KIRGLNKFYQSQgqklHALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQNIAELSHSELiqtRQ 97
Cdd:cd00267 1 EIENLSFRYGGR----TALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEEL---RR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 98 RIGMIFQhfnlmsaktvwenvalplkvsnynkadidqrvnevlalvgladksnyypsqLSGGQKQRVGIARALVHHPEIL 177
Cdd:cd00267 74 RIGYVPQ---------------------------------------------------LSGGQRQRVALARALLLNPDLL 102
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1194606020 178 LCDEATSALDPESTATILALLKKINQElGLTIVLITHEMQVIREICDQVVVIDQGE 233
Cdd:cd00267 103 LLDEPTSGLDPASRERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
38-248 |
5.13e-45 |
|
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: 157.96 E-value: 5.13e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 38 EINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHI-------HQQNIAELSHseliqtRQRIGMIFQHFNLMS 110
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLggevlqdSARGIFLPPH------RRRIGYVFQEARLFP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 111 AKTVWENVALPLKVSNYNKADIDqrVNEVLALVGLADKSNYYPSQLSGGQKQRVGIARALVHHPEILLCDEATSALDPES 190
Cdd:COG4148 91 HLSVRGNLLYGRKRAPRAERRIS--FDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLAR 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1194606020 191 TATILALLKKINQELGLTIVLITHEMQVIREICDQVVVIDQGEIVEAGQVWSVFSRPE 248
Cdd:COG4148 169 KAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRPD 226
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
17-236 |
6.79e-45 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 154.84 E-value: 6.79e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 17 IKIRGLNKFYQSQG-----QKLHALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQNIAELSHSE 91
Cdd:PRK10419 4 LNVSGLSHHYAHGGlsgkhQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 92 LIQTRQRIGMIFQhfNLMSA----KTVWENVALPLK-VSNYNKADIDQRVNEVLALVGLADK-SNYYPSQLSGGQKQRVG 165
Cdd:PRK10419 84 RKAFRRDIQMVFQ--DSISAvnprKTVREIIREPLRhLLSLDKAERLARASEMLRAVDLDDSvLDKRPPQLSGGQLQRVC 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1194606020 166 IARALVHHPEILLCDEATSALDPESTATILALLKKINQELGLTIVLITHEMQVIREICDQVVVIDQGEIVE 236
Cdd:PRK10419 162 LARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVE 232
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
15-214 |
1.03e-44 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 154.25 E-value: 1.03e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 15 PHIKIRGLNKFYQSQGQKLHALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQNI----AElshs 90
Cdd:COG4525 2 SMLTVRHVSVRYPGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVtgpgAD---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 91 eliqtrqRiGMIFQHFNLMSAKTVWENVALPLKVSNYNKADIDQRVNEVLALVGLADKSNYYPSQLSGGQKQRVGIARAL 170
Cdd:COG4525 78 -------R-GVVFQKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARAL 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1194606020 171 VHHPEILLCDEATSALDPESTATILALLKKINQELGLTIVLITH 214
Cdd:COG4525 150 AADPRFLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITH 193
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
13-230 |
1.15e-44 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 153.43 E-value: 1.15e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 13 SLPHIKIRGLNKFYQSQGQKLHALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQNIAELSHSEL 92
Cdd:PRK11629 2 NKILLQCDNLCKRYQEGSVQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 93 IQTRQR-IGMIFQHFNLMSAKTVWENVALPLKVSNYNKADIDQRVNEVLALVGLADKSNYYPSQLSGGQKQRVGIARALV 171
Cdd:PRK11629 82 AELRNQkLGFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALV 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1194606020 172 HHPEILLCDEATSALDPESTATILALLKKINQELGLTIVLITHEMQVIREICDQVVVID 230
Cdd:PRK11629 162 NNPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQLEMRD 220
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
18-265 |
1.36e-44 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 154.40 E-value: 1.36e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 18 KIRGLNKFYQSQGQKLHALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQniaELSHSELIQTRQ 97
Cdd:PRK13635 5 IIRVEHISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGM---VLSEETVWDVRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 98 RIGMIFQH-FNLMSAKTVWENVALPLKVSNYNKADIDQRVNEVLALVGLADKSNYYPSQLSGGQKQRVGIARALVHHPEI 176
Cdd:PRK13635 82 QVGMVFQNpDNQFVGATVQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 177 LLCDEATSALDPESTATILALLKKINQELGLTIVLITHEmqvIREI--CDQVVVIDQGEIVEAGQVWSVFSRPEQqitqe 254
Cdd:PRK13635 162 IILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHD---LDEAaqADRVIVMNKGEILEEGTPEEIFKSGHM----- 233
|
250
....*....|...
gi 1194606020 255 llnLEQITL--PF 265
Cdd:PRK13635 234 ---LQEIGLdvPF 243
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
17-235 |
8.37e-44 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 159.89 E-value: 8.37e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 17 IKIRGLNKFYQSQGQKLHALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQNIAELSHSELIQ-T 95
Cdd:PRK10535 5 LELKDIRRSYPSGEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQlR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 96 RQRIGMIFQHFNLMSAKTVWENVALPLKVSNYNKADIDQRVNEVLALVGLADKSNYYPSQLSGGQKQRVGIARALVHHPE 175
Cdd:PRK10535 85 REHFGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQ 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 176 ILLCDEATSALDPESTATILALLKKINQElGLTIVLITHEMQVIREiCDQVVVIDQGEIV 235
Cdd:PRK10535 165 VILADEPTGALDSHSGEEVMAILHQLRDR-GHTVIIVTHDPQVAAQ-AERVIEIRDGEIV 222
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
17-238 |
1.05e-43 |
|
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: 150.28 E-value: 1.05e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 17 IKIRGLNKFYqsqGqKLHALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQNIAELSHSELIqtR 96
Cdd:cd03224 1 LEVENLNAGY---G-KSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERA--R 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 97 QRIGMIFQHFNLMSAKTVWENVALPLKVSnyNKADIDQRVNEVLALV-GLADKSNYYPSQLSGGQKQRVGIARALVHHPE 175
Cdd:cd03224 75 AGIGYVPEGRRIFPELTVEENLLLGAYAR--RRAKRKARLERVYELFpRLKERRKQLAGTLSGGEQQMLAIARALMSRPK 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1194606020 176 ILLCDEATSALDPESTATILALLKKINQElGLTIVLITHEMQVIREICDQVVVIDQGEIVEAG 238
Cdd:cd03224 153 LLLLDEPSEGLAPKIVEEIFEAIRELRDE-GVTILLVEQNARFALEIADRAYVLERGRVVLEG 214
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
41-238 |
1.87e-43 |
|
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: 149.57 E-value: 1.87e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 41 LDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQNIAELSHSEliqtrQRIGMIFQHFNLMSAKTVWENVAL 120
Cdd:cd03298 19 LTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPAD-----RPVSMLFQENNLFAHLTVEQNVGL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 121 PLKVSNYNKADIDQRVNEVLALVGLADKSNYYPSQLSGGQKQRVGIARALVHHPEILLCDEATSALDPESTATILALLKK 200
Cdd:cd03298 94 GLSPGLKLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLD 173
|
170 180 190
....*....|....*....|....*....|....*...
gi 1194606020 201 INQELGLTIVLITHEMQVIREICDQVVVIDQGEIVEAG 238
Cdd:cd03298 174 LHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
17-263 |
4.48e-43 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 150.97 E-value: 4.48e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 17 IKIRGLNKFYQsQGQKLH--ALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQNIAELSHSeLIQ 94
Cdd:PRK13637 3 IKIENLTHIYM-EGTPFEkkALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVK-LSD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 95 TRQRIGMIFQH--FNLMSaKTVWENVALPLKVSNYNKADIDQRVNEVLALVGL-----ADKSnyyPSQLSGGQKQRVGIA 167
Cdd:PRK13637 81 IRKKVGLVFQYpeYQLFE-ETIEKDIAFGPINLGLSEEEIENRVKRAMNIVGLdyedyKDKS---PFELSGGQKRRVAIA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 168 RALVHHPEILLCDEATSALDPESTATILALLKKINQELGLTIVLITHEMQVIREICDQVVVIDQGEIVEAGQVWSVFsrp 247
Cdd:PRK13637 157 GVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVF--- 233
|
250
....*....|....*.
gi 1194606020 248 eqqitQELLNLEQITL 263
Cdd:PRK13637 234 -----KEVETLESIGL 244
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
26-278 |
1.61e-42 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 148.75 E-value: 1.61e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 26 YQSQGQKLHALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQNIAELSHSELiqtRQRIGMIFQH 105
Cdd:PRK13648 15 FQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKL---RKHIGIVFQN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 106 -FNLMSAKTVWENVALPLKVSNYNKADIDQRVNEVLALVGLADKSNYYPSQLSGGQKQRVGIARALVHHPEILLCDEATS 184
Cdd:PRK13648 92 pDNQFVGSIVKYDVAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATS 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 185 ALDPESTATILALLKKINQELGLTIVLITHEMQVIREiCDQVVVIDQGEIVEAGQVWSVFSRpEQQITQELLNLeqiTLP 264
Cdd:PRK13648 172 MLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIFDH-AEELTRIGLDL---PFP 246
|
250
....*....|....
gi 1194606020 265 FKINPLPDEDSTHI 278
Cdd:PRK13648 247 IKINQMLGHQTSFL 260
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
15-256 |
2.05e-42 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 151.53 E-value: 2.05e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 15 PHIKIRGLNKFYQSQgqklHALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQniaELSHselIQ 94
Cdd:PRK11607 18 PLLEIRNLTKSFDGQ----HAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGV---DLSH---VP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 95 TRQR-IGMIFQHFNLMSAKTVWENVALPLKVSNYNKADIDQRVNEVLALVGLADKSNYYPSQLSGGQKQRVGIARALVHH 173
Cdd:PRK11607 88 PYQRpINMMFQSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKR 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 174 PEILLCDEATSALDPESTATILALLKKINQELGLTIVLITHEMQVIREICDQVVVIDQGEIVEAGQVWSVFSRPEQQITQ 253
Cdd:PRK11607 168 PKLLLLDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSA 247
|
...
gi 1194606020 254 ELL 256
Cdd:PRK11607 248 EFI 250
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
35-289 |
2.16e-42 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 149.01 E-value: 2.16e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 35 ALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQNI-AELSHSELIQTRQRIGMIFQhF--NLMSA 111
Cdd:PRK13634 22 ALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVItAGKKNKKLKPLRKKVGIVFQ-FpeHQLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 112 KTVWENVAL-PLK--VSnynKADIDQRVNEVLALVGLA----DKSnyyPSQLSGGQKQRVGIARALVHHPEILLCDEATS 184
Cdd:PRK13634 101 ETVEKDICFgPMNfgVS---EEDAKQKAREMIELVGLPeellARS---PFELSGGQMRRVAIAGVLAMEPEVLVLDEPTA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 185 ALDPESTATILALLKKINQELGLTIVLITHEMQVIREICDQVVVIDQGEIVEAGQVWSVFSRPEqQITQELLNL------ 258
Cdd:PRK13634 175 GLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADPD-ELEAIGLDLpetvkf 253
|
250 260 270
....*....|....*....|....*....|....*.
gi 1194606020 259 -----EQITLPFKINPLPDEDSTHIIVKLKYEAEAH 289
Cdd:PRK13634 254 kraleEKFGISFPKPCLTLEELAHEVVQLLRKGGHE 289
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
35-284 |
2.88e-42 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 148.30 E-value: 2.88e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 35 ALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQNIaELSHSELIQTRQRIGMIFQHF-NLMSAKT 113
Cdd:PRK13639 17 ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPI-KYDKKSLLEVRKTVGIVFQNPdDQLFAPT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 114 VWENVAL-PLKVSnYNKADIDQRVNEVLALVGLADKSNYYPSQLSGGQKQRVGIARALVHHPEILLCDEATSALDPESTA 192
Cdd:PRK13639 96 VEEDVAFgPLNLG-LSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGAS 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 193 TILALLKKINQElGLTIVLITHEMQVIREICDQVVVIDQGEIVEAGQVWSVFSRPEqQITQELLNLEQITLPFKInpLPD 272
Cdd:PRK13639 175 QIMKLLYDLNKE-GITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDIE-TIRKANLRLPRVAHLIEI--LNK 250
|
250
....*....|..
gi 1194606020 273 EDstHIIVKLKY 284
Cdd:PRK13639 251 ED--NLPIKMGY 260
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
17-254 |
7.52e-42 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 146.85 E-value: 7.52e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 17 IKIRGLNKFYqsqGQKLhALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQV-----NTGSIHIHQQNIAElSHSE 91
Cdd:PRK14243 11 LRTENLNVYY---GSFL-AVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLipgfrVEGKVTFHGKNLYA-PDVD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 92 LIQTRQRIGMIFQHFNLMSaKTVWENVALPLKVSNYnKADIDQRVNEVLALVGL----ADKSNYYPSQLSGGQKQRVGIA 167
Cdd:PRK14243 86 PVEVRRRIGMVFQKPNPFP-KSIYDNIAYGARINGY-KGDMDELVERSLRQAALwdevKDKLKQSGLSLSGGQQQRLCIA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 168 RALVHHPEILLCDEATSALDPESTATILALLKKINQElgLTIVLITHEMQVIREICDQVVVID---------QGEIVEAG 238
Cdd:PRK14243 164 RAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQ--YTIIIVTHNMQQAARVSDMTAFFNveltegggrYGYLVEFD 241
|
250
....*....|....*.
gi 1194606020 239 QVWSVFSRPEQQITQE 254
Cdd:PRK14243 242 RTEKIFNSPQQQATRD 257
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
17-248 |
7.86e-42 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 147.30 E-value: 7.86e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 17 IKIRGLNKFYqSQGQklHALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQNIaELSHSELIQTR 96
Cdd:PRK13636 6 LKVEELNYNY-SDGT--HALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPI-DYSRKGLMKLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 97 QRIGMIFQH--FNLMSAkTVWENVALPLKVSNYNKADIDQRVNEVLALVGLADKSNYYPSQLSGGQKQRVGIARALVHHP 174
Cdd:PRK13636 82 ESVGMVFQDpdNQLFSA-SVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEP 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1194606020 175 EILLCDEATSALDPESTATILALLKKINQELGLTIVLITHEMQVIREICDQVVVIDQGEIVEAGQVWSVFSRPE 248
Cdd:PRK13636 161 KVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFAEKE 234
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
17-258 |
1.09e-41 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 146.80 E-value: 1.09e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 17 IKIRGLnKFYQSQGQKLHALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQniaELSHSELIQTR 96
Cdd:PRK13650 5 IEVKNL-TFKYKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGD---LLTEENVWDIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 97 QRIGMIFQH-FNLMSAKTVWENVALPLKVSNYNKADIDQRVNEVLALVGLADKSNYYPSQLSGGQKQRVGIARALVHHPE 175
Cdd:PRK13650 81 HKIGMVFQNpDNQFVGATVEDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 176 ILLCDEATSALDPESTATILALLKKINQELGLTIVLITHEMQVIrEICDQVVVIDQGEIVEAGQVWSVFSRPEqqitqEL 255
Cdd:PRK13650 161 IIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEV-ALSDRVLVMKNGQVESTSTPRELFSRGN-----DL 234
|
...
gi 1194606020 256 LNL 258
Cdd:PRK13650 235 LQL 237
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
17-238 |
1.68e-41 |
|
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: 144.43 E-value: 1.68e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 17 IKIRGLNKFYQSQGQKLHALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQNIaelsHSELIQTR 96
Cdd:cd03266 2 ITADALTKRFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDV----VKEPAEAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 97 QRIGMIFQHFNLMSAKTVWENVALPLKVSNYNKADIDQRVNEVLALVGLADKSNYYPSQLSGGQKQRVGIARALVHHPEI 176
Cdd:cd03266 78 RRLGFVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPV 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1194606020 177 LLCDEATSALDPESTATILALLKKInQELGLTIVLITHEMQVIREICDQVVVIDQGEIVEAG 238
Cdd:cd03266 158 LLLDEPTTGLDVMATRALREFIRQL-RALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
38-238 |
2.01e-41 |
|
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: 144.36 E-value: 2.01e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 38 EINLDIPQGkILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQNIAELSHSELIQTRQR-IGMIFQHFNLMSAKTVWE 116
Cdd:cd03297 16 KIDFDLNEE-VTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRKKINLPPQQRkIGLVFQQYALFPHLNVRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 117 NVALPLKVSNYNKadIDQRVNEVLALVGLADKSNYYPSQLSGGQKQRVGIARALVHHPEILLCDEATSALDPESTATILA 196
Cdd:cd03297 95 NLAFGLKRKRNRE--DRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLP 172
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1194606020 197 LLKKINQELGLTIVLITHEMQVIREICDQVVVIDQGEIVEAG 238
Cdd:cd03297 173 ELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
15-235 |
3.31e-41 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 150.95 E-value: 3.31e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 15 PHIKIRGLNKFYQSqgqkLHALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQNIAELSHSELIq 94
Cdd:COG3845 4 PALELRGITKRFGG----VVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRDAI- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 95 tRQRIGMIFQHFNLMSAKTVWENVAL---PLKVSNYNKADIDQRVNEVLALVGLADKSNYYPSQLSGGQKQRVGIARALV 171
Cdd:COG3845 79 -ALGIGMVHQHFMLVPNLTVAENIVLglePTKGGRLDRKAARARIRELSERYGLDVDPDAKVEDLSVGEQQRVEILKALY 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1194606020 172 HHPEILLCDEATSALDPESTATILALLKKINQElGLTIVLITHEMQVIREICDQVVVIDQGEIV 235
Cdd:COG3845 158 RGARILILDEPTAVLTPQEADELFEILRRLAAE-GKSIIFITHKLREVMAIADRVTVLRRGKVV 220
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
39-247 |
4.29e-41 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 147.17 E-value: 4.29e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 39 INLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQNIAELShselIQTRQrIGMIFQHFNLMSAKTVWENV 118
Cdd:PRK11432 25 LNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRS----IQQRD-ICMVFQSYALFPHMSLGENV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 119 ALPLKVSNYNKADIDQRVNEVLALVGLADKSNYYPSQLSGGQKQRVGIARALVHHPEILLCDEATSALDPESTATILALL 198
Cdd:PRK11432 100 GYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSMREKI 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1194606020 199 KKINQELGLTIVLITHEMQVIREICDQVVVIDQGEIVEAGQVWSVFSRP 247
Cdd:PRK11432 180 RELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQP 228
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
17-238 |
6.14e-41 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 142.74 E-value: 6.14e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 17 IKIRGLNKFYQSQgqklHALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQNIaelshSELIQTR 96
Cdd:cd03268 1 LKTNDLTKTYGKK----RVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSY-----QKNIEAL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 97 QRIGMIFQHFNLMSAKTVWENVALPLKVSNYNKadidQRVNEVLALVGLADKSNYYPSQLSGGQKQRVGIARALVHHPEI 176
Cdd:cd03268 72 RRIGALIEAPGFYPNLTARENLRLLARLLGIRK----KRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1194606020 177 LLCDEATSALDPESTATILALLKKINQElGLTIVLITHEMQVIREICDQVVVIDQGEIVEAG 238
Cdd:cd03268 148 LILDEPTNGLDPDGIKELRELILSLRDQ-GITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
19-248 |
3.13e-40 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 143.30 E-value: 3.13e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 19 IRGLNKFYQ----SQGQKLHALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQNIAELSHseLIQ 94
Cdd:PRK13633 5 IKCKNVSYKyesnEESTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEEN--LWD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 95 TRQRIGMIFQH-FNLMSAKTVWENVALPLKVSNYNKADIDQRVNEVLALVGLADKSNYYPSQLSGGQKQRVGIARALVHH 173
Cdd:PRK13633 83 IRNKAGMVFQNpDNQIVATIVEEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMR 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1194606020 174 PEILLCDEATSALDPESTATILALLKKINQELGLTIVLITHEMQVIREiCDQVVVIDQGEIVEAGQVWSVFSRPE 248
Cdd:PRK13633 163 PECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIFKEVE 236
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
36-250 |
9.81e-40 |
|
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: 140.29 E-value: 9.81e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 36 LKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQNIAELSHSELIqtrqrigmIFQHFNLMSAKTVW 115
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRMV--------VFQNYSLLPWLTVR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 116 ENVALPLKVSNYNKADIDQR--VNEVLALVGLADKSNYYPSQLSGGQKQRVGIARALVHHPEILLCDEATSALDPESTAT 193
Cdd:TIGR01184 73 ENIALAVDRVLPDLSKSERRaiVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGN 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1194606020 194 ILALLKKINQELGLTIVLITHEMQVIREICDQVVVIDQGEIVEAGQVWSV-FSRPEQQ 250
Cdd:TIGR01184 153 LQEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAANIGQILEVpFPRPRDR 210
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
37-239 |
1.51e-39 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 143.63 E-value: 1.51e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 37 KEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQNIAELSHSEliqtrQRIGMIFQHFNLMSAKTVWE 116
Cdd:PRK11000 20 KDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAE-----RGVGMVFQSYALYPHLSVAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 117 NVALPLKVSNYNKADIDQRVNEVLALVGLADKSNYYPSQLSGGQKQRVGIARALVHHPEILLCDEATSALDPESTATILA 196
Cdd:PRK11000 95 NMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRVQMRI 174
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1194606020 197 LLKKINQELGLTIVLITHEMQVIREICDQVVVIDQGEIVEAGQ 239
Cdd:PRK11000 175 EISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGK 217
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
15-254 |
2.37e-39 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 139.91 E-value: 2.37e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 15 PHIKIRGLNKFYQsqgqKLHALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVN-----TGSIHIHQQNIAElSH 89
Cdd:PRK14239 4 PILQVSDLSVYYN----KKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLNpevtiTGSIVYNGHNIYS-PR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 90 SELIQTRQRIGMIFQHFNLMSAkTVWENVALPLKVSN-YNKADIDQRVNEVLALVGLAD--KSNYYPSQ--LSGGQKQRV 164
Cdd:PRK14239 79 TDTVDLRKEIGMVFQQPNPFPM-SIYENVVYGLRLKGiKDKQVLDEAVEKSLKGASIWDevKDRLHDSAlgLSGGQQQRV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 165 GIARALVHHPEILLCDEATSALDPESTATILALLKKINQElgLTIVLITHEMQVIREICDQVVVIDQGEIVEAGQVWSVF 244
Cdd:PRK14239 158 CIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDD--YTMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQMF 235
|
250
....*....|
gi 1194606020 245 SRPEQQITQE 254
Cdd:PRK14239 236 MNPKHKETED 245
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
17-232 |
3.52e-39 |
|
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: 138.72 E-value: 3.52e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 17 IKIRGLNK---FYQSQGQKLHALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQ----NIAELSH 89
Cdd:COG4778 5 LEVENLSKtftLHLQGGKRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDggwvDLAQASP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 90 SELIQTRQR-IGMIFQHFNLM---SAKTVwenVALPLKVSNYNKADIDQRVNEVLALVGLADKS-NYYPSQLSGGQKQRV 164
Cdd:COG4778 85 REILALRRRtIGYVSQFLRVIprvSALDV---VAEPLLERGVDREEARARARELLARLNLPERLwDLPPATFSGGEQQRV 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1194606020 165 GIARALVHHPEILLCDEATSALDPESTATILALLKKINQElGLTIVLITHEMQVIREICDQVVVIDQG 232
Cdd:COG4778 162 NIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKAR-GTAIIGIFHDEEVREAVADRVVDVTPF 228
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
17-238 |
5.22e-39 |
|
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: 138.51 E-value: 5.22e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 17 IKIRGLNKFYqsqGQKLHALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQNIAELSHSELiqtR 96
Cdd:cd03254 3 IEFENVNFSY---DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSL---R 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 97 QRIGMIFQHFNLMSAkTVWENVALplkvsNYNKADiDQRVNEVLALVGLADKSNYYP-----------SQLSGGQKQRVG 165
Cdd:cd03254 77 SMIGVVLQDTFLFSG-TIMENIRL-----GRPNAT-DEEVIEAAKEAGAHDFIMKLPngydtvlgengGNLSQGERQLLA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1194606020 166 IARALVHHPEILLCDEATSALDPESTATILALLKKINQelGLTIVLITHEMQVIREiCDQVVVIDQGEIVEAG 238
Cdd:cd03254 150 IARAMLRDPKILILDEATSNIDTETEKLIQEALEKLMK--GRTSIIIAHRLSTIKN-ADKILVLDDGKIIEEG 219
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
17-266 |
2.19e-38 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 137.97 E-value: 2.19e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 17 IKIRGLNkFyqSQGQKLhALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQNIAELSHSELIQTR 96
Cdd:PRK11831 8 VDMRGVS-F--TRGNRC-IFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTVR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 97 QRIGMIFQHFNLMSAKTVWENVALPLKV-SNYNKADIDQRVNEVLALVGLADKSNYYPSQLSGGQKQRVGIARALVHHPE 175
Cdd:PRK11831 84 KRMSMLFQSGALFTDMNVFDNVAYPLREhTQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPD 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 176 ILLCDEATSALDPESTATILALLKKINQELGLTIVLITHEMQVIREICDQVVVIDQGEIVEAGQVWSVFSRPEQQITQEL 255
Cdd:PRK11831 164 LIMFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQANPDPRVRQFL 243
|
250
....*....|.
gi 1194606020 256 LNLEQITLPFK 266
Cdd:PRK11831 244 DGIADGPVPFR 254
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
15-238 |
2.36e-38 |
|
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: 136.65 E-value: 2.36e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 15 PHIKIRGLNKFYqsqGqKLHALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQNIAELSHSELIq 94
Cdd:COG0410 2 PMLEVENLHAGY---G-GIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIA- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 95 tRQRIGM------IFQHFnlmsakTVWENVALPLKVSNyNKADIDQRVNEVLAL--VgLADKSNYYPSQLSGGQKQRVGI 166
Cdd:COG0410 77 -RLGIGYvpegrrIFPSL------TVEENLLLGAYARR-DRAEVRADLERVYELfpR-LKERRRQRAGTLSGGEQQMLAI 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1194606020 167 ARALVHHPEILLCDEATSALDPESTATILALLKKINQElGLTIVLITHEMQVIREICDQVVVIDQGEIVEAG 238
Cdd:COG0410 148 GRALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNRE-GVTILLVEQNARFALEIADRAYVLERGRIVLEG 218
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
9-238 |
3.15e-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: 136.18 E-value: 3.15e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 9 QVDFSLPhikirglnkfyqsqGQKLHALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQNIAELS 88
Cdd:cd03245 7 NVSFSYP--------------NQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLD 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 89 HSELiqtRQRIGMIFQHFNLMSAkTVWENVALPLKVSNynkadiDQRVNEVLALVGLADKSNYYP-----------SQLS 157
Cdd:cd03245 73 PADL---RRNIGYVPQDVTLFYG-TLRDNITLGAPLAD------DERILRAAELAGVTDFVNKHPngldlqigergRGLS 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 158 GGQKQRVGIARALVHHPEILLCDEATSALDPESTATilaLLKKINQEL-GLTIVLITHEMQVIrEICDQVVVIDQGEIVE 236
Cdd:cd03245 143 GGQRQAVALARALLNDPPILLLDEPTSAMDMNSEER---LKERLRQLLgDKTLIIITHRPSLL-DLVDRIIVMDSGRIVA 218
|
..
gi 1194606020 237 AG 238
Cdd:cd03245 219 DG 220
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
17-238 |
6.44e-38 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 136.79 E-value: 6.44e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 17 IKIRGLNKFYQSQGqklHALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQNIAELSHSELiqtR 96
Cdd:PRK13647 5 IEVEDLHFRYKDGT---KALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWV---R 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 97 QRIGMIFQH-FNLMSAKTVWENVALPLKVSNYNKADIDQRVNEVLALVGLADKSNYYPSQLSGGQKQRVGIARALVHHPE 175
Cdd:PRK13647 79 SKVGLVFQDpDDQVFSSTVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPD 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1194606020 176 ILLCDEATSALDPESTATILALLKKINQElGLTIVLITHEMQVIREICDQVVVIDQGEIVEAG 238
Cdd:PRK13647 159 VIVLDEPMAYLDPRGQETLMEILDRLHNQ-GKTVIVATHDVDLAAEWADQVIVLKEGRVLAEG 220
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
28-235 |
7.45e-38 |
|
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: 134.69 E-value: 7.45e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 28 SQGQKLHALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQNIAElshseliQTRQR-IGMIFQH- 105
Cdd:cd03226 8 SYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKA-------KERRKsIGYVMQDv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 106 -FNLMSaKTVWENVALPLKvsnyNKADIDQRVNEVLALVGLADKSNYYPSQLSGGQKQRVGIARALVHHPEILLCDEATS 184
Cdd:cd03226 81 dYQLFT-DSVREELLLGLK----ELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTS 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1194606020 185 ALDPESTATILALLKKInQELGLTIVLITHEMQVIREICDQVVVIDQGEIV 235
Cdd:cd03226 156 GLDYKNMERVGELIREL-AAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
17-257 |
9.99e-38 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 136.07 E-value: 9.99e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 17 IKIRGLNKFYQSQG-----QKLHALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQniaELSHSE 91
Cdd:PRK15112 5 LEVRNLSKTFRYRTgwfrrQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDH---PLHFGD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 92 LIQTRQRIGMIFQ--HFNLMSAKTVWENVALPLKV-SNYNKADIDQRVNEVLALVGL-ADKSNYYPSQLSGGQKQRVGIA 167
Cdd:PRK15112 82 YSYRSQRIRMIFQdpSTSLNPRQRISQILDFPLRLnTDLEPEQREKQIIETLRQVGLlPDHASYYPHMLAPGQKQRLGLA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 168 RALVHHPEILLCDEATSALDPESTATILALLKKINQELGLTIVLITHEMQVIREICDQVVVIDQGEIVEAGQVWSVFSRP 247
Cdd:PRK15112 162 RALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVLASP 241
|
250
....*....|
gi 1194606020 248 EQQITQELLN 257
Cdd:PRK15112 242 LHELTKRLIA 251
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
15-238 |
1.28e-37 |
|
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: 134.54 E-value: 1.28e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 15 PHIKIRGLNKFYQSQGQKlhALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQNIAELSHSELiq 94
Cdd:cd03244 1 GDIEFKNVSLRYRPNLPP--VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDL-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 95 tRQRIGMIFQHFNLMSAkTVWENVAlPLKVSNynkadiDQRVNEVLALVGLADKSNYYP-----------SQLSGGQKQR 163
Cdd:cd03244 77 -RSRISIIPQDPVLFSG-TIRSNLD-PFGEYS------DEELWQALERVGLKEFVESLPggldtvveeggENLSVGQRQL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1194606020 164 VGIARALVHHPEILLCDEATSALDPESTATILALLKkiNQELGLTIVLITHEMQVIREiCDQVVVIDQGEIVEAG 238
Cdd:cd03244 148 LCLARALLRKSKILVLDEATASVDPETDALIQKTIR--EAFKDCTVLTIAHRLDTIID-SDRILVLDKGRVVEFD 219
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
36-256 |
2.11e-37 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 134.90 E-value: 2.11e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 36 LKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQNIAELSHSELIQTRqriGMIFQHFNLMSAKTVW 115
Cdd:PRK13548 18 LDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRR---AVLPQHSSLSFPFTVE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 116 ENVALPLKVSNYNKADIDQRVNEVLALVGLAD-KSNYYPsQLSGGQKQRVGIARALV------HHPEILLCDEATSALDP 188
Cdd:PRK13548 95 EVVAMGRAPHGLSRAEDDALVAAALAQVDLAHlAGRDYP-QLSGGEQQRVQLARVLAqlwepdGPPRWLLLDEPTSALDL 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1194606020 189 ESTATILALLKKINQELGLTIVLITHEMQVIREICDQVVVIDQGEIVEAGqvwsvfsRPEQQITQELL 256
Cdd:PRK13548 174 AHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADG-------TPAEVLTPETL 234
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
34-247 |
2.53e-37 |
|
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: 137.55 E-value: 2.53e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 34 HALKeINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQNIAelSHSELIQT---RQRIGMIFQHFNLMS 110
Cdd:TIGR02142 12 FSLD-ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLF--DSRKGIFLppeKRRIGYVFQEARLFP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 111 AKTVWENValplkVSNYNKADIDQRV---NEVLALVGLADKSNYYPSQLSGGQKQRVGIARALVHHPEILLCDEATSALD 187
Cdd:TIGR02142 89 HLSVRGNL-----RYGMKRARPSERRisfERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALD 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 188 PESTATILALLKKINQELGLTIVLITHEMQVIREICDQVVVIDQGEIVEAGQVWSVFSRP 247
Cdd:TIGR02142 164 DPRKYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASP 223
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
17-235 |
2.60e-37 |
|
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: 131.78 E-value: 2.60e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 17 IKIRGLNKFYQSQgqklHALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQNIAELSHSELIqtR 96
Cdd:cd03216 1 LELRGITKRFGGV----KALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDAR--R 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 97 QRIGMIFQhfnlmsaktvwenvalplkvsnynkadidqrvnevlalvgladksnyypsqLSGGQKQRVGIARALVHHPEI 176
Cdd:cd03216 75 AGIAMVYQ---------------------------------------------------LSVGERQMVEIARALARNARL 103
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1194606020 177 LLCDEATSALDPESTATILALLKKInQELGLTIVLITHEMQVIREICDQVVVIDQGEIV 235
Cdd:cd03216 104 LILDEPTAALTPAEVERLFKVIRRL-RAQGVAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
17-256 |
2.62e-37 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 134.86 E-value: 2.62e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 17 IKIRGLNkfYQSQGQKLhaLKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQNIAELSHSELIQTR 96
Cdd:COG4559 2 LEAENLS--VRLGGRTL--LDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 97 qriGMIFQHFNLMSAKTVWENVALPLKVSNYNKADIDQRVNEVLALVGLADKSN-YYPsQLSGGQKQRVGIARAL--VHH 173
Cdd:COG4559 78 ---AVLPQHSSLAFPFTVEEVVALGRAPHGSSAAQDRQIVREALALVGLAHLAGrSYQ-TLSGGEQQRVQLARVLaqLWE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 174 PE-----ILLCDEATSALDPESTATILALLKKINQElGLTIVLITHEMQVIREICDQVVVIDQGEIVEAGqvwsvfsRPE 248
Cdd:COG4559 154 PVdggprWLFLDEPTSALDLAHQHAVLRLARQLARR-GGGVVAVLHDLNLAAQYADRILLLHQGRLVAQG-------TPE 225
|
....*...
gi 1194606020 249 QQITQELL 256
Cdd:COG4559 226 EVLTDELL 233
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
36-254 |
3.17e-37 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 134.79 E-value: 3.17e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 36 LKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQNI---AELSHSELIQTRQRIGMIFQHFNLMSAK 112
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLyfgKDIFQIDAIKLRKEVGMVFQQPNPFPHL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 113 TVWENVALPLKVSNY-NKADIDQRVNEVLALVGL----ADKSNYYPSQLSGGQKQRVGIARALVHHPEILLCDEATSALD 187
Cdd:PRK14246 106 SIYDNIAYPLKSHGIkEKREIKKIVEECLRKVGLwkevYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSMID 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1194606020 188 PESTATILALLKKINQElgLTIVLITHEMQVIREICDQVVVIDQGEIVEAGQVWSVFSRPEQQITQE 254
Cdd:PRK14246 186 IVNSQAIEKLITELKNE--IAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNELTEK 250
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
17-248 |
3.31e-37 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 136.90 E-value: 3.31e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 17 IKIRGLNKFYQSqgqKLHALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQNIAELSHSEliqtr 96
Cdd:PRK11650 4 LKLQAVRKSYDG---KTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPAD----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 97 qR-IGMIFQHFNLMSAKTVWENVALPLKVSNYNKADIDQRVNEVLALVGLADKSNYYPSQLSGGQKQRVGIARALVHHPE 175
Cdd:PRK11650 76 -RdIAMVFQNYALYPHMSVRENMAYGLKIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1194606020 176 ILLCDEATSALDPESTATILALLKKINQELGLTIVLITHEmQVirE---ICDQVVVIDQGEIVEAGQVWSVFSRPE 248
Cdd:PRK11650 155 VFLFDEPLSNLDAKLRVQMRLEIQRLHRRLKTTSLYVTHD-QV--EamtLADRVVVMNGGVAEQIGTPVEVYEKPA 227
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
36-238 |
3.80e-37 |
|
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: 133.89 E-value: 3.80e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 36 LKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQNIAELSHSELiqtRQRIGMIFQH---FNlmsaK 112
Cdd:cd03253 17 LKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSL---RRAIGVVPQDtvlFN----D 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 113 TVWENVAlplkvsnYNKADI-DQRVNEVLALVGLADKSNYYPSQ-----------LSGGQKQRVGIARALVHHPEILLCD 180
Cdd:cd03253 90 TIGYNIR-------YGRPDAtDEEVIEAAKAAQIHDKIMRFPDGydtivgerglkLSGGEKQRVAIARAILKNPPILLLD 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1194606020 181 EATSALDPESTATILALLKKINQelGLTIVLITHEMQVIREiCDQVVVIDQGEIVEAG 238
Cdd:cd03253 163 EATSALDTHTEREIQAALRDVSK--GRTTIVIAHRLSTIVN-ADKIIVLKDGRIVERG 217
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
35-250 |
6.49e-37 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 134.34 E-value: 6.49e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 35 ALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIhqQNIAELSHSELIQTRQRIGMIFQHFNL-MSAKT 113
Cdd:PRK13644 17 ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLV--SGIDTGDFSKLQGIRKLVGIVFQNPETqFVGRT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 114 VWENVALPLKVSNYNKADIDQRVNEVLALVGLADKSNYYPSQLSGGQKQRVGIARALVHHPEILLCDEATSALDPESTAT 193
Cdd:PRK13644 95 VEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGIA 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1194606020 194 ILALLKKINQElGLTIVLITHEMQVIrEICDQVVVIDQGEIVEAGQVWSVFSRPEQQ 250
Cdd:PRK13644 175 VLERIKKLHEK-GKTIVYITHNLEEL-HDADRIIVMDRGKIVLEGEPENVLSDVSLQ 229
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
17-271 |
8.36e-37 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 134.16 E-value: 8.36e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 17 IKIRGLNKFYQSQgqkLHALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQNIAELSHSELiqtR 96
Cdd:PRK13652 4 IETRDLCYSYSGS---KEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREV---R 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 97 QRIGMIFQHFN-LMSAKTVWENVALPLKVSNYNKADIDQRVNEVLALVGLADKSNYYPSQLSGGQKQRVGIARALVHHPE 175
Cdd:PRK13652 78 KFVGLVFQNPDdQIFSPTVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 176 ILLCDEATSALDPESTATILALLKKINQELGLTIVLITHEMQVIREICDQVVVIDQGEIVEAGQVWSVFSRPeqqitqEL 255
Cdd:PRK13652 158 VLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP------DL 231
|
250
....*....|....*.
gi 1194606020 256 LNLEQITLPfkinPLP 271
Cdd:PRK13652 232 LARVHLDLP----SLP 243
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
35-247 |
1.08e-36 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 136.70 E-value: 1.08e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 35 ALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQNIAELSHSELIQTR-QRIGMIFQHFNLMSAKT 113
Cdd:PRK10070 43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVRrKKIAMVFQSFALMPHMT 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 114 VWENVALPLKVSNYNKADIDQRVNEVLALVGLADKSNYYPSQLSGGQKQRVGIARALVHHPEILLCDEATSALDPESTAT 193
Cdd:PRK10070 123 VLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTE 202
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1194606020 194 ILALLKKINQELGLTIVLITHEMQVIREICDQVVVIDQGEIVEAGQVWSVFSRP 247
Cdd:PRK10070 203 MQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNP 256
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
17-274 |
1.65e-36 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 133.19 E-value: 1.65e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 17 IKIRGLNKFYQSQgqKLHALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQniaELSHSELIQTR 96
Cdd:PRK13632 8 IKVENVSFSYPNS--ENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGI---TISKENLKEIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 97 QRIGMIFQH-FNLMSAKTVWENVALPLKVSNYNKADIDQRVNEVLALVGLADKSNYYPSQLSGGQKQRVGIARALVHHPE 175
Cdd:PRK13632 83 KKIGIIFQNpDNQFIGATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 176 ILLCDEATSALDPESTATILALLKKINQELGLTIVLITHEM-QVIreICDQVVVIDQGEIVEAGQVWSVFSrpeqqiTQE 254
Cdd:PRK13632 163 IIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMdEAI--LADKVIVFSEGKLIAQGKPKEILN------NKE 234
|
250 260
....*....|....*....|....*....
gi 1194606020 255 LLNLEQITLPF---------KINPLPDED 274
Cdd:PRK13632 235 ILEKAKIDSPFiyklskklkGIDPTYNEE 263
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
35-263 |
2.75e-36 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 132.56 E-value: 2.75e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 35 ALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQNIAELSHSELI-QTRQRIGMIFQhF--NLMSA 111
Cdd:PRK13649 22 ALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNKDIkQIRKKVGLVFQ-FpeSQLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 112 KTVWENVALPLKVSNYNKADIDQRVNEVLALVGLADK-SNYYPSQLSGGQKQRVGIARALVHHPEILLCDEATSALDPES 190
Cdd:PRK13649 101 ETVLKDVAFGPQNFGVSQEEAEALAREKLALVGISESlFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKG 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1194606020 191 TATILALLKKINQElGLTIVLITHEMQVIREICDQVVVIDQGEIVEAGQVWSVFsrpeqqitQELLNLEQITL 263
Cdd:PRK13649 181 RKELMTLFKKLHQS-GMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIF--------QDVDFLEEKQL 244
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
35-268 |
2.95e-36 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 132.62 E-value: 2.95e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 35 ALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGL--------EQVNTGSIHIHQQNIAELshseliqtRQRIGMIFQH- 105
Cdd:PRK13640 22 ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLllpddnpnSKITVDGITLTAKTVWDI--------REKVGIVFQNp 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 106 FNLMSAKTVWENVALPLKVSNYNKADIDQRVNEVLALVGLADKSNYYPSQLSGGQKQRVGIARALVHHPEILLCDEATSA 185
Cdd:PRK13640 94 DNQFVGATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSM 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 186 LDPESTATILALLKKINQELGLTIVLITHEMQVIrEICDQVVVIDQGEIVEAGQVWSVFSRPE--QQITQEL-------- 255
Cdd:PRK13640 174 LDPAGKEQILKLIRKLKKKNNLTVISITHDIDEA-NMADQVLVLDDGKLLAQGSPVEIFSKVEmlKEIGLDIpfvyklkn 252
|
250
....*....|....
gi 1194606020 256 -LNLEQITLPFKIN 268
Cdd:PRK13640 253 kLKEKGISVPQEIN 266
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
17-300 |
3.61e-36 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 132.93 E-value: 3.61e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 17 IKIRGLNKFYQSQgqklHALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQNIAElshseliQTR 96
Cdd:COG4152 2 LELKGLTKRFGDK----TAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDP-------EDR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 97 QRIG-----------MifqhfnlmsakTVWENVALPLKVSNYNKADIDQRVNEVLALVGLADKSNYYPSQLSGGQKQRVG 165
Cdd:COG4152 71 RRIGylpeerglypkM-----------KVGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQ 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 166 IARALVHHPEILLCDEATSALDPESTATILALLKKINQElGLTIVLITHEMQVIREICDQVVVIDQGEIVEAGQVWSV-- 243
Cdd:COG4152 140 LIAALLHDPELLILDEPFSGLDPVNVELLKDVIRELAAK-GTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEIrr 218
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1194606020 244 -FSRPEQQIT-----QELLNLEQITlpfkinpLPDEDSTHIIVKLKYEAEAHQVpdIQELLAR 300
Cdd:COG4152 219 qFGRNTLRLEadgdaGWLRALPGVT-------VVEEDGDGAELKLEDGADAQEL--LRALLAR 272
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
35-238 |
5.39e-36 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 138.17 E-value: 5.39e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 35 ALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQNIAELSHSELiqtRQRIGMIFQHFNLMSAkTV 114
Cdd:TIGR03797 468 ILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAGLDVQAV---RRQLGVVLQNGRLMSG-SI 543
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 115 WENVA----LPLKvsnynkadidqRVNEVLALVGLADKSNYYP-----------SQLSGGQKQRVGIARALVHHPEILLC 179
Cdd:TIGR03797 544 FENIAggapLTLD-----------EAWEAARMAGLAEDIRAMPmgmhtviseggGTLSGGQRQRLLIARALVRKPRILLF 612
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1194606020 180 DEATSALDPESTATILALLKKINqelgLTIVLITHEMQVIREiCDQVVVIDQGEIVEAG 238
Cdd:TIGR03797 613 DEATSALDNRTQAIVSESLERLK----VTRIVIAHRLSTIRN-ADRIYVLDAGRVVQQG 666
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
36-215 |
8.62e-36 |
|
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: 129.14 E-value: 8.62e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 36 LKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQNIaelsHSELIQTRQRIGMIFQHFNLMSAKTVW 115
Cdd:COG4133 18 FSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPI----RDAREDYRRRLAYLGHADGLKPELTVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 116 ENVALPLKVsnYNKADIDQRVNEVLALVGLADKSNYYPSQLSGGQKQRVGIARALVHHPEILLCDEATSALDPESTATIL 195
Cdd:COG4133 94 ENLRFWAAL--YGLRADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGVALLA 171
|
170 180
....*....|....*....|..
gi 1194606020 196 ALlkkINQEL--GLTIVLITHE 215
Cdd:COG4133 172 EL---IAAHLarGGAVLLTTHQ 190
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
35-238 |
9.29e-36 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 130.04 E-value: 9.29e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 35 ALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQNIAELSHSELiqtRQRIGMIFQHFNLMSAkTV 114
Cdd:cd03251 17 VLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASL---RRQIGLVSQDVFLFND-TV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 115 WENVAlplkvsnYNKADIDQ-RVNEVLALVGLADKSNYYP-----------SQLSGGQKQRVGIARALVHHPEILLCDEA 182
Cdd:cd03251 93 AENIA-------YGRPGATReEVEEAARAANAHEFIMELPegydtvigergVKLSGGQRQRIAIARALLKDPPILILDEA 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1194606020 183 TSALDPESTATILALLKKINQelGLTIVLITHEMQVIREIcDQVVVIDQGEIVEAG 238
Cdd:cd03251 166 TSALDTESERLVQAALERLMK--NRTTFVIAHRLSTIENA-DRIVVLEDGKIVERG 218
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
34-264 |
2.45e-35 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 134.76 E-value: 2.45e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 34 HALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQNIAELSHSELIqtRQRIGMIFQHFNLMSAKT 113
Cdd:COG1129 18 KALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDAQ--AAGIAIIHQELNLVPNLS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 114 VWENVAL---PLKVSNYNKADIDQRVNEVLALVGLA-DksnyyP----SQLSGGQKQRVGIARALVHHPEILLCDEATSA 185
Cdd:COG1129 96 VAENIFLgrePRRGGLIDWRAMRRRARELLARLGLDiD-----PdtpvGDLSVAQQQLVEIARALSRDARVLILDEPTAS 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 186 LDPESTATILALLKKInQELGLTIVLITHEMQVIREICDQVVV--------------IDQGEIVEA--G-QVWSVFSRPE 248
Cdd:COG1129 171 LTEREVERLFRIIRRL-KAQGVAIIYISHRLDEVFEIADRVTVlrdgrlvgtgpvaeLTEDELVRLmvGrELEDLFPKRA 249
|
250
....*....|....*.
gi 1194606020 249 QQITQELLNLEQITLP 264
Cdd:COG1129 250 AAPGEVVLEVEGLSVG 265
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
17-238 |
2.59e-35 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 129.75 E-value: 2.59e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 17 IKIRGLNKFYQsQGQKLHAlkeINLDIPQGKILGIIGKSGAGKSSLLRTLNGLeqvntgsihIHQQNIAElSHSELI--- 93
Cdd:PRK09984 5 IRVEKLAKTFN-QHQALHA---VDLNIHHGEMVALLGPSGSGKSTLLRHLSGL---------ITGDKSAG-SHIELLgrt 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 94 ------------QTRQRIGMIFQHFNLMSAKTVWENVAL------PL--KVSNYNKADIDQRVNEVLALVGLADKSNYYP 153
Cdd:PRK09984 71 vqregrlardirKSRANTGYIFQQFNLVNRLSVLENVLIgalgstPFwrTCFSWFTREQKQRALQALTRVGMVHFAHQRV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 154 SQLSGGQKQRVGIARALVHHPEILLCDEATSALDPESTATILALLKKINQELGLTIVLITHEMQVIREICDQVVVIDQGE 233
Cdd:PRK09984 151 STLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGH 230
|
....*
gi 1194606020 234 IVEAG 238
Cdd:PRK09984 231 VFYDG 235
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
31-256 |
2.86e-35 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 135.75 E-value: 2.86e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 31 QKLHALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQNIAELSHSELIQTRQRIGMIFQ--HFNL 108
Cdd:PRK10261 335 REVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQALRRDIQFIFQdpYASL 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 109 MSAKTVWENVALPLKVSNYNKADIDQ-RVNEVLALVGLADKSNY-YPSQLSGGQKQRVGIARALVHHPEILLCDEATSAL 186
Cdd:PRK10261 415 DPRQTVGDSIMEPLRVHGLLPGKAAAaRVAWLLERVGLLPEHAWrYPHEFSGGQRQRICIARALALNPKVIIADEAVSAL 494
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 187 DPESTATILALLKKINQELGLTIVLITHEMQVIREICDQVVVIDQGEIVEAGQVWSVFSRPEQQITQELL 256
Cdd:PRK10261 495 DVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENPQHPYTRKLM 564
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
17-238 |
3.05e-35 |
|
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: 127.78 E-value: 3.05e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 17 IKIRGLNKFYqsqGQKlHALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIhqqniaeLSHSELIQTR 96
Cdd:cd03269 1 LEVENVTKRF---GRV-TALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLF-------DGKPLDIAAR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 97 QRIGMIFQHFNLMSAKTVWENVALPLKVSNYNKADIDQRVNEVLALVGLADKSNYYPSQLSGGQKQRVGIARALVHHPEI 176
Cdd:cd03269 70 NRIGYLPEERGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPEL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1194606020 177 LLCDEATSALDPESTatilALLKKINQEL---GLTIVLITHEMQVIREICDQVVVIDQGEIVEAG 238
Cdd:cd03269 150 LILDEPFSGLDPVNV----ELLKDVIRELaraGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
13-281 |
3.30e-35 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 134.83 E-value: 3.30e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 13 SLPHIKIRGLNKFYQSQGQKLHALKEINLDIPQGKILGIIGKSGAGKS----SLLRTLNGLEQVNT-GSIHIHQQNIAEL 87
Cdd:PRK15134 2 TQPLLAIENLSVAFRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSvtalSILRLLPSPPVVYPsGDIRFHGESLLHA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 88 SHSELIQTR-QRIGMIFQHfnlmsaktvwENVAL-PLKvsnynkaDIDQRVNEVLAL-------------------VGL- 145
Cdd:PRK15134 82 SEQTLRGVRgNKIAMIFQE----------PMVSLnPLH-------TLEKQLYEVLSLhrgmrreaargeilncldrVGIr 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 146 --ADKSNYYPSQLSGGQKQRVGIARALVHHPEILLCDEATSALDPESTATILALLKKINQELGLTIVLITHEMQVIREIC 223
Cdd:PRK15134 145 qaAKRLTDYPHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLA 224
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1194606020 224 DQVVVIDQGEIVEAGQVWSVFSRPEQQITQELLNLEQITLPFkinPLPDEDSTHIIVK 281
Cdd:PRK15134 225 DRVAVMQNGRCVEQNRAATLFSAPTHPYTQKLLNSEPSGDPV---PLPEPASPLLDVE 279
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
40-257 |
3.64e-35 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 128.55 E-value: 3.64e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 40 NLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQNiaelsHSELIQTRQRIGMIFQHFNLMSAKTVWENVA 119
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQD-----HTTTPPSRRPVSMLFQENNLFSHLTVAQNIG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 120 L---P-LKVSNYNKadidQRVNEVLALVGLADKSNYYPSQLSGGQKQRVGIARALVHHPEILLCDEATSALDPESTATIL 195
Cdd:PRK10771 94 LglnPgLKLNAAQR----EKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEML 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1194606020 196 ALLKKINQELGLTIVLITHEMQVIREICDQVVVIDQGEIVEAGQvwsvfsrpeqqiTQELLN 257
Cdd:PRK10771 170 TLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGP------------TDELLS 219
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
36-238 |
8.99e-35 |
|
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: 134.18 E-value: 8.99e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 36 LKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQNIAELSHSELiqtRQRIGMIFQH---FNlmsaK 112
Cdd:COG5265 374 LKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASL---RAAIGIVPQDtvlFN----D 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 113 TVWENVAlplkvsnYNKADIDQRvnEVLALVGLADKSNY-------YPSQ-------LSGGQKQRVGIARALVHHPEILL 178
Cdd:COG5265 447 TIAYNIA-------YGRPDASEE--EVEAAARAAQIHDFieslpdgYDTRvgerglkLSGGEKQRVAIARTLLKNPPILI 517
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 179 CDEATSALDPESTATILALLKKINQelGLTIVLITHEMQVIREiCDQVVVIDQGEIVEAG 238
Cdd:COG5265 518 FDEATSALDSRTERAIQAALREVAR--GRTTLVIAHRLSTIVD-ADEILVLEAGRIVERG 574
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
35-257 |
2.25e-34 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 129.07 E-value: 2.25e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 35 ALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVN---TGSIHIHQQNIAELSHSELIQTR-QRIGMIFQHfnlms 110
Cdd:PRK09473 31 AVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANgriGGSATFNGREILNLPEKELNKLRaEQISMIFQD----- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 111 aktvwenvalPLKVSN-YNKadIDQRVNEVLALVGLADKS----------------------NYYPSQLSGGQKQRVGIA 167
Cdd:PRK09473 106 ----------PMTSLNpYMR--VGEQLMEVLMLHKGMSKAeafeesvrmldavkmpearkrmKMYPHEFSGGMRQRVMIA 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 168 RALVHHPEILLCDEATSALDPESTATILALLKKINQELGLTIVLITHEMQVIREICDQVVVIDQGEIVEAGQVWSVFSRP 247
Cdd:PRK09473 174 MALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARDVFYQP 253
|
250
....*....|
gi 1194606020 248 EQQITQELLN 257
Cdd:PRK09473 254 SHPYSIGLLN 263
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
35-238 |
2.44e-34 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 126.45 E-value: 2.44e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 35 ALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQNIAELSHSELiqtRQRIGMIFQHfNLMSAKTV 114
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWL---RRQVGVVLQE-NVLFNRSI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 115 WENVALPlkvsnyNKADIDQRVNEVLALVGLADKSNYYP-----------SQLSGGQKQRVGIARALVHHPEILLCDEAT 183
Cdd:cd03252 93 RDNIALA------DPGMSMERVIEAAKLAGAHDFISELPegydtivgeqgAGLSGGQRQRIAIARALIHNPRILIFDEAT 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1194606020 184 SALDPESTATILALLKKINQelGLTIVLITHEMQVIREiCDQVVVIDQGEIVEAG 238
Cdd:cd03252 167 SALDYESEHAIMRNMHDICA--GRTVIIIAHRLSTVKN-ADRIIVMEKGRIVEQG 218
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
19-301 |
3.53e-34 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 132.67 E-value: 3.53e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 19 IRGLNKFYQSQGQKLHALKEINLDIPQGKILGIIGKSGAGKS----SLLRTLNGL-EQVNTGSIHIHQQN-----IAELS 88
Cdd:PRK10261 15 VENLNIAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSvtalALMRLLEQAgGLVQCDKMLLRRRSrqvieLSEQS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 89 HSELIQTR-QRIGMIFQH--FNLMSAKTVWENVALPLKV-SNYNKADIDQRVNEVLALVGLADKS---NYYPSQLSGGQK 161
Cdd:PRK10261 95 AAQMRHVRgADMAMIFQEpmTSLNPVFTVGEQIAESIRLhQGASREEAMVEAKRMLDQVRIPEAQtilSRYPHQLSGGMR 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 162 QRVGIARALVHHPEILLCDEATSALDPESTATILALLKKINQELGLTIVLITHEMQVIREICDQVVVIDQGEIVEAGQVW 241
Cdd:PRK10261 175 QRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVE 254
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1194606020 242 SVFSRPEQQITQELL-------NLEQITLP--FKINPLPDEDSTHIIVKLKYEAEAHQVPDIQELLARF 301
Cdd:PRK10261 255 QIFHAPQHPYTRALLaavpqlgAMKGLDYPrrFPLISLEHPAKQEPPIEQDTVVDGEPILQVRNLVTRF 323
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
10-238 |
3.95e-34 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 125.96 E-value: 3.95e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 10 VDFSLPHIKIRGL----NKFYQSQGQKLHALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHqQNIA 85
Cdd:COG1134 12 KSYRLYHEPSRSLkellLRRRRTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVN-GRVS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 86 ---ELS---HSELiqtrqrigmifqhfnlmsakTVWENVALPLKVSNYNKADIDQRVNEVLALVGLADK-----SNYyps 154
Cdd:COG1134 91 allELGagfHPEL--------------------TGRENIYLNGRLLGLSRKEIDEKFDEIVEFAELGDFidqpvKTY--- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 155 qlSGGQKQRVGIARALVHHPEILLCDEATSALDPE----STATILALLKKinqelGLTIVLITHEMQVIREICDQVVVID 230
Cdd:COG1134 148 --SSGMRARLAFAVATAVDPDILLVDEVLAVGDAAfqkkCLARIRELRES-----GRTVIFVSHSMGAVRRLCDRAIWLE 220
|
....*...
gi 1194606020 231 QGEIVEAG 238
Cdd:COG1134 221 KGRLVMDG 228
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
4-239 |
6.29e-34 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 131.49 E-value: 6.29e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 4 VSFGSQVDFSLPHIKIRGLNKFYQSQGQKLHALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQN 83
Cdd:PRK11160 324 VTFPTTSTAAADQVSLTLNNVSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQP 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 84 IAELSHSELiqtRQRIGMIFQHFNLMSAkTVWENVALPLKVSNynkadiDQRVNEVLALVGLADKSNYYPS--------- 154
Cdd:PRK11160 404 IADYSEAAL---RQAISVVSQRVHLFSA-TLRDNLLLAAPNAS------DEALIEVLQQVGLEKLLEDDKGlnawlgegg 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 155 -QLSGGQKQRVGIARALVHHPEILLCDEATSALDPESTATILALLKKINQelGLTIVLITHEMQVIrEICDQVVVIDQGE 233
Cdd:PRK11160 474 rQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQ--NKTVLMITHRLTGL-EQFDRICVMDNGQ 550
|
....*.
gi 1194606020 234 IVEAGQ 239
Cdd:PRK11160 551 IIEQGT 556
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
17-218 |
8.64e-34 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 124.51 E-value: 8.64e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 17 IKIRGLNKFYQSQGQKLHALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQNIAELSHSELIQTR 96
Cdd:PRK10584 7 VEVHHLKKSVGQGEHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKLR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 97 -QRIGMIFQHFNLMSAKTVWENVALPLKVSNYNKADIDQRVNEVLALVGLADKSNYYPSQLSGGQKQRVGIARALVHHPE 175
Cdd:PRK10584 87 aKHVGFVFQSFMLIPTLNALENVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPD 166
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1194606020 176 ILLCDEATSALDPESTATILALLKKINQELGLTIVLITHEMQV 218
Cdd:PRK10584 167 VLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQL 209
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
24-303 |
1.33e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 126.50 E-value: 1.33e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 24 KFYQSQGQKLHALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSI---------HIHQQNIAELSHSELIQ 94
Cdd:PRK13631 30 VFDEKQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIqvgdiyigdKKNNHELITNPYSKKIK 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 95 T----RQRIGMIFQHFNLMSAKTVWEN------VALPLKvsnynKADIDQRVNEVLALVGLadKSNYY---PSQLSGGQK 161
Cdd:PRK13631 110 NfkelRRRVSMVFQFPEYQLFKDTIEKdimfgpVALGVK-----KSEAKKLAKFYLNKMGL--DDSYLersPFGLSGGQK 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 162 QRVGIARALVHHPEILLCDEATSALDPESTATILALLKKINQElGLTIVLITHEMQVIREICDQVVVIDQGEIVEAGQVW 241
Cdd:PRK13631 183 RRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKAN-NKTVFVITHTMEHVLEVADEVIVMDKGKILKTGTPY 261
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1194606020 242 SVFsrpeqqITQELLNLEQITLPFKINPLPDEDSTHIIVKLKYEAEAHQVPDIQELLARFKA 303
Cdd:PRK13631 262 EIF------TDQHIINSTSIQVPRVIQVINDLIKKDPKYKKLYQKQPRTIEQLADAINEFIK 317
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
14-254 |
1.74e-33 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 124.76 E-value: 1.74e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 14 LPHIKIRGLNKFYQSQgqklHALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNT-----GSIHIHQQNIAElS 88
Cdd:PRK14258 5 IPAIKVNNLSFYYDTQ----KILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNIYE-R 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 89 HSELIQTRQRIGMIFQHFNLMSAkTVWENVALPLKVSNYN-KADIDQRVNEVLALVGLAD--KSNYYPS--QLSGGQKQR 163
Cdd:PRK14258 80 RVNLNRLRRQVSMVHPKPNLFPM-SVYDNVAYGVKIVGWRpKLEIDDIVESALKDADLWDeiKHKIHKSalDLSGGQQQR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 164 VGIARALVHHPEILLCDEATSALDPESTATILALLKKINQELGLTIVLITHEMQVIREICDQVVVIDQ-----GEIVEAG 238
Cdd:PRK14258 159 LCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGnenriGQLVEFG 238
|
250
....*....|....*.
gi 1194606020 239 QVWSVFSRPEQQITQE 254
Cdd:PRK14258 239 LTKKIFNSPHDSRTRE 254
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
36-238 |
2.47e-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: 123.80 E-value: 2.47e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 36 LKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQNIAELSHSELiqtRQRIGMIFQHFNLMSAkTVW 115
Cdd:cd03249 19 LKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWL---RSQIGLVSQEPVLFDG-TIA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 116 ENVAlplkvsnYNKAD-IDQRVNEVLALVGLADKSNYYP-----------SQLSGGQKQRVGIARALVHHPEILLCDEAT 183
Cdd:cd03249 95 ENIR-------YGKPDaTDEEVEEAAKKANIHDFIMSLPdgydtlvgergSQLSGGQKQRIAIARALLRNPKILLLDEAT 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1194606020 184 SALDPESTATILALLKKInqELGLTIVLITHEMQVIREiCDQVVVIDQGEIVEAG 238
Cdd:cd03249 168 SALDAESEKLVQEALDRA--MKGRTTIVIAHRLSTIRN-ADLIAVLQNGQVVEQG 219
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
18-239 |
4.46e-33 |
|
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: 122.63 E-value: 4.46e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 18 KIRGLNKFYqsqGQKlHALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQNIAELSHSEliqtRQ 97
Cdd:TIGR03410 2 EVSNLNVYY---GQS-HILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHE----RA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 98 RIG--------MIFQHFnlmsakTVWENVALPLKVSNYNKADIDQRVNEVLALvgLADKSNYYPSQLSGGQKQRVGIARA 169
Cdd:TIGR03410 74 RAGiayvpqgrEIFPRL------TVEENLLTGLAALPRRSRKIPDEIYELFPV--LKEMLGRRGGDLSGGQQQQLAIARA 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 170 LVHHPEILLCDEATSALDPESTATILALLKKINQELGLTIVLITHEMQVIREICDQVVVIDQGEIVEAGQ 239
Cdd:TIGR03410 146 LVTRPKLLLLDEPTEGIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRVVASGA 215
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
36-256 |
6.13e-33 |
|
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: 122.89 E-value: 6.13e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 36 LKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLE-QVNTGSIHI-----HQQNIAELshseliqtRQRIGMI--FQHFN 107
Cdd:COG1119 19 LDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLpPTYGNDVRLfgerrGGEDVWEL--------RKRIGLVspALQLR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 108 LMSAKTVWENVA--------LPLKVSnynkADIDQRVNEVLALVGLADKSNYYPSQLSGGQKQRVGIARALVHHPEILLC 179
Cdd:COG1119 91 FPRDETVLDVVLsgffdsigLYREPT----DEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIARALVKDPELLIL 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1194606020 180 DEATSALDPESTATILALLKKINQELGLTIVLITHEMQVIREICDQVVVIDQGEIVEAGQVwsvfsrpEQQITQELL 256
Cdd:COG1119 167 DEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRVVAAGPK-------EEVLTSENL 236
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
35-256 |
8.96e-33 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 124.47 E-value: 8.96e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 35 ALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGL----EQVNTGSIHIHQQNIAELSHSEliqTRQRIG----MIFQH- 105
Cdd:PRK11022 22 AVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLidypGRVMAEKLEFNGQDLQRISEKE---RRNLVGaevaMIFQDp 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 106 -FNLMSAKTVWENVALPLKV-SNYNKADIDQRVNEVLALVGLADKS---NYYPSQLSGGQKQRVGIARALVHHPEILLCD 180
Cdd:PRK11022 99 mTSLNPCYTVGFQIMEAIKVhQGGNKKTRRQRAIDLLNQVGIPDPAsrlDVYPHQLSGGMSQRVMIAMAIACRPKLLIAD 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1194606020 181 EATSALDPESTATILALLKKINQELGLTIVLITHEMQVIREICDQVVVIDQGEIVEAGQVWSVFSRPEQQITQELL 256
Cdd:PRK11022 179 EPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDIFRAPRHPYTQALL 254
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
33-244 |
1.03e-32 |
|
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: 127.61 E-value: 1.03e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 33 LHALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQV--NTGSIHIH------------QQNIAE------------ 86
Cdd:TIGR03269 13 KEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQYepTSGRIIYHvalcekcgyverPSKVGEpcpvcggtlepe 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 87 ------LSHSELIQTRQRIGMIFQH-FNLMSAKTVWENVALPLKVSNYNKADIDQRVNEVLALVGLADKSNYYPSQLSGG 159
Cdd:TIGR03269 93 evdfwnLSDKLRRRIRKRIAIMLQRtFALYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEMVQLSHRITHIARDLSGG 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 160 QKQRVGIARALVHHPEILLCDEATSALDPESTATILALLKKINQELGLTIVLITHEMQVIREICDQVVVIDQGEIVEAG- 238
Cdd:TIGR03269 173 EKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDLSDKAIWLENGEIKEEGt 252
|
....*...
gi 1194606020 239 --QVWSVF 244
Cdd:TIGR03269 253 pdEVVAVF 260
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
35-217 |
1.41e-32 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 122.12 E-value: 1.41e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 35 ALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQNIAELSHSEliqtrqriGMIFQHFNLMSAKTV 114
Cdd:PRK11248 16 ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAER--------GVVFQNEGLLPWRNV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 115 WENVALPLKVSNYNKADIDQRVNEVLALVGLADKSNYYPSQLSGGQKQRVGIARALVHHPEILLCDEATSALDPESTATI 194
Cdd:PRK11248 88 QDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQM 167
|
170 180
....*....|....*....|...
gi 1194606020 195 LALLKKINQELGLTIVLITHEMQ 217
Cdd:PRK11248 168 QTLLLKLWQETGKQVLLITHDIE 190
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
31-248 |
1.64e-32 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 122.42 E-value: 1.64e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 31 QKLHALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIhIHQQNIAELSHSELIQTRQRIGMIFQHFNLMS 110
Cdd:PRK13638 12 QDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAV-LWQGKPLDYSKRGLLALRQQVATVFQDPEQQI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 111 AKT-VWENVALPLKVSNYNKADIDQRVNEVLALVGlADKSNYYPSQ-LSGGQKQRVGIARALVHHPEILLCDEATSALDP 188
Cdd:PRK13638 91 FYTdIDSDIAFSLRNLGVPEAEITRRVDEALTLVD-AQHFRHQPIQcLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDP 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 189 ESTATILALLKKINQElGLTIVLITHEMQVIREICDQVVVIDQGEIVEAGQVWSVFSRPE 248
Cdd:PRK13638 170 AGRTQMIAIIRRIVAQ-GNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVFACTE 228
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
35-229 |
1.99e-32 |
|
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: 127.02 E-value: 1.99e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 35 ALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQNIAELSHSELiqtRQRIGMIFQHfNLMSAKTV 114
Cdd:TIGR02857 337 ALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSW---RDQIAWVPQH-PFLFAGTI 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 115 WENVALplkvsnYNKADIDQRVNEVLALVGLADKSNYYP-----------SQLSGGQKQRVGIARALVHHPEILLCDEAT 183
Cdd:TIGR02857 413 AENIRL------ARPDASDAEIREALERAGLDEFVAALPqgldtpigeggAGLSGGQAQRLALARAFLRDAPLLLLDEPT 486
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1194606020 184 SALDPESTATILALLKKINQelGLTIVLITHEMQVIREiCDQVVVI 229
Cdd:TIGR02857 487 AHLDAETEAEVLEALRALAQ--GRTVLLVTHRLALAAL-ADRIVVL 529
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
35-287 |
2.28e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 122.58 E-value: 2.28e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 35 ALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQNIAELSHSELIQT-RQRIGMIFQH-FNLMSAK 112
Cdd:PRK13646 22 AIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDKYIRPvRKRIGMVFQFpESQLFED 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 113 TVWENVALPLKVSNYNKADIDQRVNEVLALVGLA-DKSNYYPSQLSGGQKQRVGIARALVHHPEILLCDEATSALDPEST 191
Cdd:PRK13646 102 TVEREIIFGPKNFKMNLDEVKNYAHRLLMDLGFSrDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSK 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 192 ATILALLKKINQELGLTIVLITHEMQVIREICDQVVVIDQGEIVEAGQVWSVFSRPEQqitqellnLEQITLpfkinPLP 271
Cdd:PRK13646 182 RQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFKDKKK--------LADWHI-----GLP 248
|
250
....*....|....*.
gi 1194606020 272 DedsthiIVKLKYEAE 287
Cdd:PRK13646 249 E------IVQLQYDFE 258
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
17-255 |
1.07e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 120.61 E-value: 1.07e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 17 IKIRGLNKFYQSQGQ-KLHALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQNIAELS-HSELIQ 94
Cdd:PRK13643 2 IKFEKVNYTYQPNSPfASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSkQKEIKP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 95 TRQRIGMIFQH-FNLMSAKTVWENVALPLKVSNYNKADIDQRVNEVLALVGLA----DKSnyyPSQLSGGQKQRVGIARA 169
Cdd:PRK13643 82 VRKKVGVVFQFpESQLFEETVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLAdefwEKS---PFELSGGQMRRVAIAGI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 170 LVHHPEILLCDEATSALDPESTATILALLKKINQElGLTIVLITHEMQVIREICDQVVVIDQGEIVEAGQVWSVFSRPEQ 249
Cdd:PRK13643 159 LAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQS-GQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQEVDF 237
|
....*.
gi 1194606020 250 QITQEL 255
Cdd:PRK13643 238 LKAHEL 243
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
36-234 |
1.76e-31 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 116.93 E-value: 1.76e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 36 LKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQNIAELSHSELiqtRQRIGMIFQHFNLMSAkTVW 115
Cdd:cd03246 18 LRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNEL---GDHVGYLPQDDELFSG-SIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 116 ENValplkvsnynkadidqrvnevlalvgladksnyypsqLSGGQKQRVGIARALVHHPEILLCDEATSALDPESTATIL 195
Cdd:cd03246 94 ENI-------------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALN 136
|
170 180 190
....*....|....*....|....*....|....*....
gi 1194606020 196 ALLKKInQELGLTIVLITHEMQVIrEICDQVVVIDQGEI 234
Cdd:cd03246 137 QAIAAL-KAAGATRIVIAHRPETL-ASADRILVLEDGRV 173
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
32-264 |
2.40e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 119.73 E-value: 2.40e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 32 KLHALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQNI-AELSH-SELIQTRQRIGMIFQ--HFN 107
Cdd:PRK13645 23 EFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIpANLKKiKEVKRLRKEIGLVFQfpEYQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 108 LMSaKTVWENVAL-PLKVSNyNKADIDQRVNEVLALVGLA-DKSNYYPSQLSGGQKQRVGIARALVHHPEILLCDEATSA 185
Cdd:PRK13645 103 LFQ-ETIEKDIAFgPVNLGE-NKQEAYKKVPELLKLVQLPeDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGG 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1194606020 186 LDPESTATILALLKKINQELGLTIVLITHEMQVIREICDQVVVIDQGEIVEAGQVWSVFSrpeqqiTQELLNLEQITLP 264
Cdd:PRK13645 181 LDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFS------NQELLTKIEIDPP 253
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
15-255 |
2.65e-31 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 118.88 E-value: 2.65e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 15 PHIKIRGLNKFYQSqgqkLHALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQ-----NIAELSH 89
Cdd:PRK11701 5 PLLSVRGLTKLYGP----RKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRdgqlrDLYALSE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 90 SEL-IQTRQRIGMIFQHF--NLMSAKTVWENVALPL-KVSNYNKADIDQRVNEVLALVGL-ADKSNYYPSQLSGGQKQRV 164
Cdd:PRK11701 81 AERrRLLRTEWGFVHQHPrdGLRMQVSAGGNIGERLmAVGARHYGDIRATAGDWLERVEIdAARIDDLPTTFSGGMQQRL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 165 GIARALVHHPEILLCDEATSALDPESTATILALLKKINQELGLTIVLITHEMQVIREICDQVVVIDQGEIVEAGQVWSVF 244
Cdd:PRK11701 161 QIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVVESGLTDQVL 240
|
250
....*....|.
gi 1194606020 245 SRPEQQITQEL 255
Cdd:PRK11701 241 DDPQHPYTQLL 251
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
17-238 |
4.17e-31 |
|
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: 123.67 E-value: 4.17e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 17 IKIRGLNKFYQSQGQKlhALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQNIAELSHSELiqtR 96
Cdd:TIGR02203 331 VEFRNVTFRYPGRDRP--ALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASL---R 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 97 QRIGMIFQHFNLMSaKTVWENVAlplkvsnYNKAD--IDQRVNEVLALVGLADKSNYYP-----------SQLSGGQKQR 163
Cdd:TIGR02203 406 RQVALVSQDVVLFN-DTIANNIA-------YGRTEqaDRAEIERALAAAYAQDFVDKLPlgldtpigengVLLSGGQRQR 477
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1194606020 164 VGIARALVHHPEILLCDEATSALDPESTATILALLKKINQelGLTIVLITHEMQVIrEICDQVVVIDQGEIVEAG 238
Cdd:TIGR02203 478 LAIARALLKDAPILILDEATSALDNESERLVQAALERLMQ--GRTTLVIAHRLSTI-EKADRIVVMDDGRIVERG 549
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
17-245 |
5.83e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 119.04 E-value: 5.83e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 17 IKIRGLNKFYQSQ-GQKLHALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHI--------HQQNIAEL 87
Cdd:PRK13651 3 IKVKNIVKIFNKKlPTELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWifkdeknkKKTKEKEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 88 SHSELI-------------QTRQRIGMIFQ--HFNLMSAkTVWENVALPLKVSNYNKADIDQRVNEVLALVGLA----DK 148
Cdd:PRK13651 83 VLEKLViqktrfkkikkikEIRRRVGVVFQfaEYQLFEQ-TIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLDesylQR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 149 SnyyPSQLSGGQKQRVGIARALVHHPEILLCDEATSALDPESTATILALLKKINQElGLTIVLITHEMQVIREICDQVVV 228
Cdd:PRK13651 162 S---PFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQ-GKTIILVTHDLDNVLEWTKRTIF 237
|
250
....*....|....*..
gi 1194606020 229 IDQGEIVEAGQVWSVFS 245
Cdd:PRK13651 238 FKDGKIIKDGDTYDILS 254
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
25-299 |
8.75e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 117.89 E-value: 8.75e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 25 FYQSQGQKLHALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQniaELSHSELIQTRQRIGMIFQ 104
Cdd:PRK13642 12 FKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGE---LLTAENVWNLRRKIGMVFQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 105 H-FNLMSAKTVWENVALPLKVSNYNKADIDQRVNEVLALVGLADKSNYYPSQLSGGQKQRVGIARALVHHPEILLCDEAT 183
Cdd:PRK13642 89 NpDNQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDEST 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 184 SALDPESTATILALLKKINQELGLTIVLITHEMQVIREiCDQVVVIDQGEIVEAGQVWSVFSRPEQQITQELlnleqiTL 263
Cdd:PRK13642 169 SMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELFATSEDMVEIGL------DV 241
|
250 260 270
....*....|....*....|....*....|....*.
gi 1194606020 264 PFKINPLPDEDSTHIIVKLKYEAEAHQVpdiqELLA 299
Cdd:PRK13642 242 PFSSNLMKDLRKNGFDLPEKYLSEDELV----ELLA 273
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
10-238 |
1.02e-30 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 116.48 E-value: 1.02e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 10 VDFSLPHIKIRGL----NKFYQSQGQKLHALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQNIA 85
Cdd:cd03220 8 KSYPTYKGGSSSLkklgILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 86 ELShseliqtrqrIGMIFQhfnlmSAKTVWENVALPLKVSNYNKADIDQRVNEVLALVGLADKSNYYPSQLSGGQKQRVG 165
Cdd:cd03220 88 LLG----------LGGGFN-----PELTGRENIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1194606020 166 IARALVHHPEILLCDEATSALDPE----STATILALLKKinqelGLTIVLITHEMQVIREICDQVVVIDQGEIVEAG 238
Cdd:cd03220 153 FAIATALEPDILLIDEVLAVGDAAfqekCQRRLRELLKQ-----GKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
35-235 |
1.02e-30 |
|
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: 116.66 E-value: 1.02e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 35 ALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIhqqnIAELSHSELIQTRQRIGMIF-QHFNLMSAKT 113
Cdd:cd03267 36 ALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRV----AGLVPWKRRKKFLRRIGVVFgQKTQLWWDLP 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 114 VWENVALPLKVSNYNKADIDQRVNEVLALVGLADKSNYYPSQLSGGQKQRVGIARALVHHPEILLCDEATSALDPESTAT 193
Cdd:cd03267 112 VIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQEN 191
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1194606020 194 ILALLKKINQELGLTIVLITHEMQVIREICDQVVVIDQGEIV 235
Cdd:cd03267 192 IRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLL 233
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
17-248 |
3.05e-30 |
|
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: 3.05e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 17 IKIRGLNKFYQsqgqKLHALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQNIAELShselIQTR 96
Cdd:cd03218 1 LRAENLSKRYG----KRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLP----MHKR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 97 QRIGMIF--QHFNLMSAKTVWENVALPLKVSNYNKADIDQRVNEVLALVGLADKSNYYPSQLSGGQKQRVGIARALVHHP 174
Cdd:cd03218 73 ARLGIGYlpQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNP 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1194606020 175 EILLCDEATSALDPESTATILALLKKINQE-LGltiVLIT-HEMQVIREICDQVVVIDQGEIVEAGQVWSVFSRPE 248
Cdd:cd03218 153 KFLLLDEPFAGVDPIAVQDIQKIIKILKDRgIG---VLITdHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANEL 225
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
16-238 |
3.23e-30 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 121.28 E-value: 3.23e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 16 HIKIRGLNKFYQsqGQKLHALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQNIAELSHSELiqt 95
Cdd:PRK11176 341 DIEFRNVTFTYP--GKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASL--- 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 96 RQRIGMIFQHFNLMSaKTVWENVALPLKvSNYNKADIDQRVNEVLAL-------VGLADKSNYYPSQLSGGQKQRVGIAR 168
Cdd:PRK11176 416 RNQVALVSQNVHLFN-DTIANNIAYART-EQYSREQIEEAARMAYAMdfinkmdNGLDTVIGENGVLLSGGQRQRIAIAR 493
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 169 ALVHHPEILLCDEATSALDPESTATILALLKKINQElgLTIVLITHEMQVIrEICDQVVVIDQGEIVEAG 238
Cdd:PRK11176 494 ALLRDSPILILDEATSALDTESERAIQAALDELQKN--RTSLVIAHRLSTI-EKADEILVVEDGEIVERG 560
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
25-253 |
3.77e-30 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 118.05 E-value: 3.77e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 25 FYQSQGQklHALkEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQNiaeLSHSE----LIQTRQRIG 100
Cdd:PRK11144 6 FKQQLGD--LCL-TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRV---LFDAEkgicLPPEKRRIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 101 MIFQHFNLMSAKTVWENvaLPLKVSNYNKADIDQrvneVLALVGLADKSNYYPSQLSGGQKQRVGIARALVHHPEILLCD 180
Cdd:PRK11144 80 YVFQDARLFPHYKVRGN--LRYGMAKSMVAQFDK----IVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMD 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1194606020 181 EATSALDPESTATILALLKKINQELGLTIVLITHEMQVIREICDQVVVIDQGEIVEAG---QVW--SVFsRPEQQITQ 253
Cdd:PRK11144 154 EPLASLDLPRKRELLPYLERLAREINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGpleEVWasSAM-RPWLPKEE 230
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
17-235 |
3.84e-30 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 115.95 E-value: 3.84e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 17 IKIRGLNK-FYQSQGQKLHALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQNIAELShseliqT 95
Cdd:COG1101 2 LELKNLSKtFNPGTVNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLP------E 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 96 RQR---IGMIFQhfNLM----SAKTVWENVALPLK----------VSNYNKADIDQRVnEVLALvGLADKSNYYPSQLSG 158
Cdd:COG1101 76 YKRakyIGRVFQ--DPMmgtaPSMTIEENLALAYRrgkrrglrrgLTKKRRELFRELL-ATLGL-GLENRLDTKVGLLSG 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1194606020 159 GQKQRVGIARALVHHPEILLCDEATSALDPESTATILALLKKINQELGLTIVLITHEMQVIREICDQVVVIDQGEIV 235
Cdd:COG1101 152 GQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNMEQALDYGNRLIMMHEGRII 228
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
17-248 |
5.23e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 116.08 E-value: 5.23e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 17 IKIRGLNKFYqSQGQKLHA--LKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQNI-AELSHSELI 93
Cdd:PRK13641 3 IKFENVDYIY-SPGTPMEKkgLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHItPETGNKNLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 94 QTRQRIGMIFQhF--NLMSAKTVWENVALPLKVSNYNKADIDQRVNEVLALVGLADK-SNYYPSQLSGGQKQRVGIARAL 170
Cdd:PRK13641 82 KLRKKVSLVFQ-FpeAQLFENTVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLSEDlISKSPFELSGGQMRRVAIAGVM 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1194606020 171 VHHPEILLCDEATSALDPESTATILALLKKInQELGLTIVLITHEMQVIREICDQVVVIDQGEIVEAGQVWSVFSRPE 248
Cdd:PRK13641 161 AYEPEILCLDEPAAGLDPEGRKEMMQLFKDY-QKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDKE 237
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
13-255 |
5.93e-30 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 116.44 E-value: 5.93e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 13 SLPHIKIRGLNKFYqsqGQKLhALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQNIAELSHsel 92
Cdd:PRK13537 4 SVAPIDFRNVEKRY---GDKL-VVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRAR--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 93 iQTRQRIGMIFQHFNLMSAKTVWENVALPLKVSNYNKADIDQRVNEVLALVGLADKSNYYPSQLSGGQKQRVGIARALVH 172
Cdd:PRK13537 77 -HARQRVGVVPQFDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVN 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 173 HPEILLCDEATSALDPESTATILALLKKINQElGLTIVLITHEMQVIREICDQVVVIDQGEIVEAGqvwsvfsRPEQQIT 252
Cdd:PRK13537 156 DPDVLVLDEPTTGLDPQARHLMWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVIEEGRKIAEG-------APHALIE 227
|
...
gi 1194606020 253 QEL 255
Cdd:PRK13537 228 SEI 230
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
19-257 |
7.04e-30 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 116.93 E-value: 7.04e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 19 IRGLNKFYQSQGQKLHALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLE----QVNTGSIHIHQQNIAELSHSELIQ 94
Cdd:COG4170 6 IRNLTIEIDTPQGRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITkdnwHVTADRFRWNGIDLLKLSPRERRK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 95 -TRQRIGMIFQHFN--LMSAKTVWENV--ALP---LKVSNYNKA-DIDQRVNEVLALVGLADKS---NYYPSQLSGGQKQ 162
Cdd:COG4170 86 iIGREIAMIFQEPSscLDPSAKIGDQLieAIPswtFKGKWWQRFkWRKKRAIELLHRVGIKDHKdimNSYPHELTEGECQ 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 163 RVGIARALVHHPEILLCDEATSALDPESTATILALLKKINQELGLTIVLITHEMQVIREICDQVVVIDQGEIVEAGQVWS 242
Cdd:COG4170 166 KVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYCGQTVESGPTEQ 245
|
250
....*....|....*
gi 1194606020 243 VFSRPEQQITQELLN 257
Cdd:COG4170 246 ILKSPHHPYTKALLR 260
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
15-245 |
1.01e-29 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 119.14 E-value: 1.01e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 15 PHIKIRGLNKFYQSQGQKL-HALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQ----NIAELSH 89
Cdd:TIGR03269 278 PIIKVRNVSKRYISVDRGVvKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRVGdewvDMTKPGP 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 90 SELIQTRQRIGMIFQHFNLMSAKTVWENVA------LPLKVSNYnKADIdqrvneVLALVGLADKS-----NYYPSQLSG 158
Cdd:TIGR03269 358 DGRGRAKRYIGILHQEYDLYPHRTVLDNLTeaigleLPDELARM-KAVI------TLKMVGFDEEKaeeilDKYPDELSE 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 159 GQKQRVGIARALVHHPEILLCDEATSALDPESTATILALLKKINQELGLTIVLITHEMQVIREICDQVVVIDQGEIVEAG 238
Cdd:TIGR03269 431 GERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIG 510
|
....*..
gi 1194606020 239 QVWSVFS 245
Cdd:TIGR03269 511 DPEEIVE 517
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
39-256 |
1.74e-29 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 114.03 E-value: 1.74e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 39 INLDIPQGKILGIIGKSGAGKS----SLLRTL-NGLEQVNtGSIHIHQQNIAelshseLIQTRQR-IGMIFQH----FN- 107
Cdd:PRK10418 22 VSLTLQRGRVLALVGGSGSGKSltcaAALGILpAGVRQTA-GRVLLDGKPVA------PCALRGRkIATIMQNprsaFNp 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 108 --LMSAKTVWENVALplkvsnyNKADIDQRVNEVLALVGLADKS---NYYPSQLSGGQKQRVGIARALVHHPEILLCDEA 182
Cdd:PRK10418 95 lhTMHTHARETCLAL-------GKPADDATLTAALEAVGLENAArvlKLYPFEMSGGMLQRMMIALALLCEAPFIIADEP 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1194606020 183 TSALDPESTATILALLKKINQELGLTIVLITHEMQVIREICDQVVVIDQGEIVEAGQVWSVFSRPEQQITQELL 256
Cdd:PRK10418 168 TTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPKHAVTRSLV 241
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
17-235 |
2.24e-29 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 115.18 E-value: 2.24e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 17 IKIRGLNKFYQSQGQK-----------------LHALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHI 79
Cdd:COG4586 2 IEVENLSKTYRVYEKEpglkgalkglfrreyreVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 80 -----HQQNIAELshseliqtrQRIGMIF-QhfnlmsaKT--VWEnvaLPLKVS-NYNKA--DID-----QRVNEVLALV 143
Cdd:COG4586 82 lgyvpFKRRKEFA---------RRIGVVFgQ-------RSqlWWD---LPAIDSfRLLKAiyRIPdaeykKRLDELVELL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 144 GLADKSNYYPSQLSGGQKQRVGIARALVHHPEILLCDEATSALDPESTATILALLKKINQELGLTIVLITHEMQVIREIC 223
Cdd:COG4586 143 DLGELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEALC 222
|
250
....*....|..
gi 1194606020 224 DQVVVIDQGEIV 235
Cdd:COG4586 223 DRVIVIDHGRII 234
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
17-238 |
4.48e-29 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 112.43 E-value: 4.48e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 17 IKIRGLNKFYQsqgqKLHALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQNIAELShselIQTR 96
Cdd:COG1137 4 LEAENLVKSYG----KRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLP----MHKR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 97 QRIGM--------IFQhfNLmsakTVWENVALPLKVSNYNKADIDQRVNEVLALVGLADKSNYYPSQLSGGQKQRVGIAR 168
Cdd:COG1137 76 ARLGIgylpqeasIFR--KL----TVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIAR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1194606020 169 ALVHHPEILLCDEATSALDPESTA---TILALLKKINqeLGltiVLIT-HemQViRE---ICDQVVVIDQGEIVEAG 238
Cdd:COG1137 150 ALATNPKFILLDEPFAGVDPIAVAdiqKIIRHLKERG--IG---VLITdH--NV-REtlgICDRAYIISEGKVLAEG 218
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
15-243 |
5.28e-29 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 117.19 E-value: 5.28e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 15 PHIKIRGLNKFYQSqgqkLHALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQNIAELSHSelIQ 94
Cdd:PRK09700 4 PYISMAGIGKSFGP----VHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHK--LA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 95 TRQRIGMIFQHFNLMSAKTVWENV---ALPLK------VSNYNKadIDQRVNEVLALVGLADKSNYYPSQLSGGQKQRVG 165
Cdd:PRK09700 78 AQLGIGIIYQELSVIDELTVLENLyigRHLTKkvcgvnIIDWRE--MRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLE 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1194606020 166 IARALVHHPEILLCDEATSALDPESTATILALLKKINQElGLTIVLITHEMQVIREICDQVVVIDQGEIVEAGQVWSV 243
Cdd:PRK09700 156 IAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKE-GTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDV 232
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
36-238 |
2.65e-28 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 115.97 E-value: 2.65e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 36 LKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQNIAELSHSELiqtRQRIGMIFQHFNLMSaKTVW 115
Cdd:TIGR00958 497 LKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYL---HRQVALVGQEPVLFS-GSVR 572
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 116 ENVALPLKvsNYNKADIDQRVNEVLALVGLADKSNYYP-------SQLSGGQKQRVGIARALVHHPEILLCDEATSALDP 188
Cdd:TIGR00958 573 ENIAYGLT--DTPDEEIMAAAKAANAHDFIMEFPNGYDtevgekgSQLSGGQKQRIAIARALVRKPRVLILDEATSALDA 650
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1194606020 189 ESTATILALLKKinqeLGLTIVLITHEMQVIREiCDQVVVIDQGEIVEAG 238
Cdd:TIGR00958 651 ECEQLLQESRSR----ASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMG 695
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
13-250 |
2.70e-28 |
|
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: 115.62 E-value: 2.70e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 13 SLP----HIKIRGLnkFYQSQGQKLHALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSI-----HIHQQN 83
Cdd:COG4618 323 PLPrpkgRLSVENL--TVVPPGSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVrldgaDLSQWD 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 84 IAELShseliqtrQRIGMIFQHFNLMSAkTVWENVALplkvsnYNKADiDQRVNEVLALVGLADKSNYYP---------- 153
Cdd:COG4618 401 REELG--------RHIGYLPQDVELFDG-TIAENIAR------FGDAD-PEKVVAAAKLAGVHEMILRLPdgydtrigeg 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 154 -SQLSGGQKQRVGIARALVHHPEILLCDEATSALDPESTAtilALLKKINQ--ELGLTIVLITHEMQVIReICDQVVVID 230
Cdd:COG4618 465 gARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEA---ALAAAIRAlkARGATVVVITHRPSLLA-AVDKLLVLR 540
|
250 260
....*....|....*....|...
gi 1194606020 231 QGEIVEAG---QVWSVFSRPEQQ 250
Cdd:COG4618 541 DGRVQAFGprdEVLARLARPAAA 563
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
17-234 |
3.22e-28 |
|
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: 109.80 E-value: 3.22e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 17 IKIRGLNKFYQSQgqklHALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQniaELSHSELiqtr 96
Cdd:TIGR03740 1 LETKNLSKRFGKQ----TAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGH---PWTRKDL---- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 97 QRIGMIFQHFNLMSAKTVWENvalpLKVSNYNKADIDQRVNEVLALVGLADKSNYYPSQLSGGQKQRVGIARALVHHPEI 176
Cdd:TIGR03740 70 HKIGSLIESPPLYENLTAREN----LKVHTTLLGLPDSRIDEVLNIVDLTNTGKKKAKQFSLGMKQRLGIAIALLNHPKL 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1194606020 177 LLCDEATSALDPESTATILALLKKINQElGLTIVLITHEMQVIREICDQVVVIDQGEI 234
Cdd:TIGR03740 146 LILDEPTNGLDPIGIQELRELIRSFPEQ-GITVILSSHILSEVQQLADHIGIISEGVL 202
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
36-257 |
6.88e-28 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 109.72 E-value: 6.88e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 36 LKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQNIAELSHSELiqtRQRIGMIFQHFNLMSAKTVW 115
Cdd:PRK11231 18 LNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQL---ARRLALLPQHHLTPEGITVR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 116 ENVA------LPL--KVSNYNKADIDQRVNEvLALVGLADKSnyyPSQLSGGQKQRVGIARALVHHPEILLCDEATSALD 187
Cdd:PRK11231 95 ELVAygrspwLSLwgRLSAEDNARVNQAMEQ-TRINHLADRR---LTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLD 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 188 PESTATILALLKKINQElGLTIVLITHEMQVIREICDQVVVIDQGEIVEAGQvwsvfsrPEQQITQELLN 257
Cdd:PRK11231 171 INHQVELMRLMRELNTQ-GKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGT-------PEEVMTPGLLR 232
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
35-234 |
7.29e-28 |
|
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: 107.52 E-value: 7.29e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 35 ALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQNIAELSHSELIqtRQRIGMI---FQHFNLMSA 111
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAI--RAGIAYVpedRKREGLVLD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 112 KTVWENVALPlkvsnynkadidqrvnevlalvgladksnyypSQLSGGQKQRVGIARALVHHPEILLCDEATSALDPEST 191
Cdd:cd03215 93 LSVAENIALS--------------------------------SLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAK 140
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1194606020 192 ATILALLKKINQElGLTIVLITHEMQVIREICDQVVVIDQGEI 234
Cdd:cd03215 141 AEIYRLIRELADA-GKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
33-232 |
2.50e-27 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 108.15 E-value: 2.50e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 33 LHALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQNIAELShSELIQtrqRIGMI--FQHFNLMS 110
Cdd:PRK11300 18 LLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLP-GHQIA---RMGVVrtFQHVRLFR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 111 AKTVWEN--VA---------LP--LKVSNYNKADID--QRVNEVLALVGLADKSNYYPSQLSGGQKQRVGIARALVHHPE 175
Cdd:PRK11300 94 EMTVIENllVAqhqqlktglFSglLKTPAFRRAESEalDRAATWLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPE 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1194606020 176 ILLCDEATSALDPESTATILALLKKINQELGLTIVLITHEMQVIREICDQVVVIDQG 232
Cdd:PRK11300 174 ILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQG 230
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
36-271 |
1.50e-26 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 106.41 E-value: 1.50e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 36 LKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQNIAELSHSELIQtrqRIGMIFQHFNLMSAKTVW 115
Cdd:PRK10575 27 LHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFAR---KVAYLPQQLPAAEGMTVR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 116 ENVAL---PLK--VSNYNKADiDQRVNEVLALVGLADKSNYYPSQLSGGQKQRVGIARALVHHPEILLCDEATSALDPES 190
Cdd:PRK10575 104 ELVAIgryPWHgaLGRFGAAD-REKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAH 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 191 TATILALLKKINQELGLTIVLITHEMQVIREICDQVVVIDQGEIVEAGQvwsvfsrPEQQITQELlnLEQI-TLPFKINP 269
Cdd:PRK10575 183 QVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGT-------PAELMRGET--LEQIyGIPMGILP 253
|
..
gi 1194606020 270 LP 271
Cdd:PRK10575 254 HP 255
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
15-214 |
2.82e-26 |
|
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: 109.37 E-value: 2.82e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 15 PHIKIRGLNKFYQSQGQklhALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQNIAELSHSELiq 94
Cdd:TIGR02868 333 PTLELRDLSAGYPGAPP---VLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEV-- 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 95 tRQRIGMIFQHFNLMSAkTVWENVALplkvsnyNKADI-DQRVNEVLALVGLADKSNYYP-----------SQLSGGQKQ 162
Cdd:TIGR02868 408 -RRRVSVCAQDAHLFDT-TVRENLRL-------ARPDAtDEELWAALERVGLADWLRALPdgldtvlgeggARLSGGERQ 478
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1194606020 163 RVGIARALVHHPEILLCDEATSALDPESTATILALLKKINQelGLTIVLITH 214
Cdd:TIGR02868 479 RLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALS--GRTVVLITH 528
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
36-238 |
4.28e-26 |
|
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: 103.01 E-value: 4.28e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 36 LKEINLDIPQGKILGIIGKSGAGKSSLLRTLNG-LEQVNT-GSIHIHQQNiaelshSELIQTRQRIGMIFQHFNLMSAKT 113
Cdd:cd03213 25 LKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGrRTGLGVsGEVLINGRP------LDKRSFRKIIGYVPQDDILHPTLT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 114 VWENVALPLKVSnynkadidqrvnevlalvgladksnyypsQLSGGQKQRVGIARALVHHPEILLCDEATSALDPESTAT 193
Cdd:cd03213 99 VRETLMFAAKLR-----------------------------GLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQ 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1194606020 194 ILALLKKINQElGLTIVLITHE-MQVIREICDQVVVIDQGEIVEAG 238
Cdd:cd03213 150 VMSLLRRLADT-GRTIICSIHQpSSEIFELFDKLLLLSQGRVIYFG 194
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
29-238 |
4.54e-26 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 109.16 E-value: 4.54e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 29 QGQKLhaLKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVnTGSIHIhqqNIAELSHSELIQTRQRIGMIFQHFNL 108
Cdd:PRK11174 361 DGKTL--AGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPY-QGSLKI---NGIELRELDPESWRKHLSWVGQNPQL 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 109 MSAkTVWENVALplkvsnyNKADI-DQRVNEVLALVGLADKSNYYP-----------SQLSGGQKQRVGIARALVHHPEI 176
Cdd:PRK11174 435 PHG-TLRDNVLL-------GNPDAsDEQLQQALENAWVSEFLPLLPqgldtpigdqaAGLSVGQAQRLALARALLQPCQL 506
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1194606020 177 LLCDEATSALDPESTATILALLKKINQelGLTIVLITHEMQVIREiCDQVVVIDQGEIVEAG 238
Cdd:PRK11174 507 LLLDEPTASLDAHSEQLVMQALNAASR--RQTTLMVTHQLEDLAQ-WDQIWVMQDGQIVQQG 565
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
17-238 |
4.67e-26 |
|
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: 103.26 E-value: 4.67e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 17 IKIRGLNKFYQSQGQKlhALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQNIaelSHSELIQTR 96
Cdd:cd03369 7 IEVENLSVRYAPDLPP--VLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDI---STIPLEDLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 97 QRIGMIFQHFNLMSAkTVWENValplkvSNYNKADiDQRVNEVLALVGLAdksnyypSQLSGGQKQRVGIARALVHHPEI 176
Cdd:cd03369 82 SSLTIIPQDPTLFSG-TIRSNL------DPFDEYS-DEEIYGALRVSEGG-------LNLSQGQRQLLCLARALLKRPRV 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1194606020 177 LLCDEATSALDPESTATIlalLKKINQEL-GLTIVLITHEMQVIREiCDQVVVIDQGEIVEAG 238
Cdd:cd03369 147 LVLDEATASIDYATDALI---QKTIREEFtNSTILTIAHRLRTIID-YDKILVMDAGEVKEYD 205
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
15-237 |
5.04e-26 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 103.88 E-value: 5.04e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 15 PHIKIRGLNKFYQSQ-------------------GQKLHALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLE--QVN 73
Cdd:COG2401 6 PFFVLMRVTKVYSSVldlservaivleafgvelrVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 74 TGSIHIHQQNIAElshseliqtrqrigmifqhfnlmsAKTVWENVALplkvsnynKADIDQRVnEVLALVGLADKSNYY- 152
Cdd:COG2401 86 AGCVDVPDNQFGR------------------------EASLIDAIGR--------KGDFKDAV-ELLNAVGLSDAVLWLr 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 153 -PSQLSGGQKQRVGIARALVHHPEILLCDEATSALDPEsTATILAL-LKKINQELGLTIVLITHEMQVIREIC-DQVVVI 229
Cdd:COG2401 133 rFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQ-TAKRVARnLQKLARRAGITLVVATHHYDVIDDLQpDLLIFV 211
|
....*...
gi 1194606020 230 DQGEIVEA 237
Cdd:COG2401 212 GYGGVPEE 219
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
15-214 |
1.25e-25 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 107.59 E-value: 1.25e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 15 PHIKIRGLNkFYQSQGQKLhaLKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQ-QNIAELShseli 93
Cdd:COG4178 361 GALALEDLT-LRTPDGRPL--LEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARPAgARVLFLP----- 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 94 qtrQR----IGmifqhfNLMSAktvwenVALPLKVSNYNkadiDQRVNEVLALVGLA------DKSNYYPSQLSGGQKQR 163
Cdd:COG4178 433 ---QRpylpLG------TLREA------LLYPATAEAFS----DAELREALEAVGLGhlaerlDEEADWDQVLSLGEQQR 493
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1194606020 164 VGIARALVHHPEILLCDEATSALDPESTATILALLKkinQEL-GLTIVLITH 214
Cdd:COG4178 494 LAFARLLLHKPDWLFLDEATSALDEENEAALYQLLR---EELpGTTVISVGH 542
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
17-233 |
1.32e-25 |
|
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: 102.16 E-value: 1.32e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 17 IKIRGLNKFYQSQGQKLH-ALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQqniaelshseliqt 95
Cdd:cd03250 1 ISVEDASFTWDSGEQETSfTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG-------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 96 rqRIGMIFQHFNLMSAkTVWENV--ALPLKVSNYNKA--------DIDQRVNEVLALVGlaDKSnyypSQLSGGQKQRVG 165
Cdd:cd03250 67 --SIAYVSQEPWIQNG-TIRENIlfGKPFDEERYEKVikacalepDLEILPDGDLTEIG--EKG----INLSGGQKQRIS 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1194606020 166 IARALVHHPEILLCDEATSALDPEsTAT------ILALLKKinqelGLTIVLITHEMQVIREiCDQVVVIDQGE 233
Cdd:cd03250 138 LARAVYSDADIYLLDDPLSAVDAH-VGRhifencILGLLLN-----NKTRILVTHQLQLLPH-ADQIVVLDNGR 204
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
17-238 |
1.96e-25 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 104.91 E-value: 1.96e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 17 IKIRGLNKFYqsqGQKLhALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIhqqnIAELSHSELIQTR 96
Cdd:PRK13536 42 IDLAGVSKSY---GDKA-VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITV----LGVPVPARARLAR 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 97 QRIGMIFQHFNLMSAKTVWENVALPLKVSNYNKADIDQRVNEVLALVGLADKSNYYPSQLSGGQKQRVGIARALVHHPEI 176
Cdd:PRK13536 114 ARIGVVPQFDNLDLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQL 193
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1194606020 177 LLCDEATSALDPESTATILALLKKInQELGLTIVLITHEMQVIREICDQVVVIDQG-EIVEAG 238
Cdd:PRK13536 194 LILDEPTTGLDPHARHLIWERLRSL-LARGKTILLTTHFMEEAERLCDRLCVLEAGrKIAEGR 255
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
36-252 |
2.66e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 103.25 E-value: 2.66e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 36 LKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGL-EQVN----TGSIHIHQQNIaeLSHSELIQTRQRIGMIFQHFNLMS 110
Cdd:PRK14271 37 LDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMnDKVSgyrySGDVLLGGRSI--FNYRDVLEFRRRVGMLFQRPNPFP 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 111 AkTVWENV-----ALPLKVSNYNKADIDQRVNEVLALVGLADKSNYYPSQLSGGQKQRVGIARALVHHPEILLCDEATSA 185
Cdd:PRK14271 115 M-SIMDNVlagvrAHKLVPRKEFRGVAQARLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSA 193
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1194606020 186 LDPESTATILALLKKINQElgLTIVLITHEMQVIREICDQVVVIDQGEIVEAGQVWSVFSRPEQQIT 252
Cdd:PRK14271 194 LDPTTTEKIEEFIRSLADR--LTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKHAET 258
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
36-276 |
1.10e-24 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 103.77 E-value: 1.10e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 36 LKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQNIAELSHSELiqtRQRIGMIFQHFNL---MSAK 112
Cdd:PRK09536 19 LDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAA---SRRVASVPQDTSLsfeFDVR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 113 TVWENVALPlKVSNYNKADIDQR--VNEVLALVGLADKSNYYPSQLSGGQKQRVGIARALVHHPEILLCDEATSALDPES 190
Cdd:PRK09536 96 QVVEMGRTP-HRSRFDTWTETDRaaVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASLDINH 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 191 TATILALLKKINQElGLTIVLITHEMQVIREICDQVVVIDQGEIVEAGqvwsvfsRPEQQITQELL----------NLEQ 260
Cdd:PRK09536 175 QVRTLELVRRLVDD-GKTAVAAIHDLDLAARYCDELVLLADGRVRAAG-------PPADVLTADTLraafdartavGTDP 246
|
250
....*....|....*.
gi 1194606020 261 ITLPFKINPLPDEDST 276
Cdd:PRK09536 247 ATGAPTVTPLPDPDRT 262
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
17-214 |
1.10e-24 |
|
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: 98.38 E-value: 1.10e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 17 IKIRGLnKFYQSQGQKLhaLKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQNiaelshseliqtr 96
Cdd:cd03223 1 IELENL-SLATPDGRVL--LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEGE------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 97 qriGMIF--QHfNLMSAKTVWENVALPLKvsnynkadidqrvnevlalvgladksnyypSQLSGGQKQRVGIARALVHHP 174
Cdd:cd03223 65 ---DLLFlpQR-PYLPLGTLREQLIYPWD------------------------------DVLSGGEQQRLAFARLLLHKP 110
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1194606020 175 EILLCDEATSALDPESTATILALLKkinqELGLTIVLITH 214
Cdd:cd03223 111 KFVFLDEATSALDEESEDRLYQLLK----ELGITVISVGH 146
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
37-261 |
1.23e-24 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 101.22 E-value: 1.23e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 37 KEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQNIAELSHSELIQtrqRIGMIFQHFNLMSAKTVWE 116
Cdd:PRK10253 24 ENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVAR---RIGLLAQNATTPGDITVQE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 117 NVA------LPLkVSNYNKADIDQrVNEVLALVGLADKSNYYPSQLSGGQKQRVGIARALVHHPEILLCDEATSALDPES 190
Cdd:PRK10253 101 LVArgryphQPL-FTRWRKEDEEA-VTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISH 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1194606020 191 TATILALLKKINQELGLTIVLITHEMQVIREICDQVVVIDQGEIVEAGQvwsvfsrPEQQITQELlnLEQI 261
Cdd:PRK10253 179 QIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGA-------PKEIVTAEL--IERI 240
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
14-256 |
1.33e-24 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 102.19 E-value: 1.33e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 14 LPHIKIRGLNKFYQSQGQKLHALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQ----VNTGSIHIHQQNIAELSH 89
Cdd:PRK15093 1 MPLLDIRNLTIEFKTSDGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKdnwrVTADRMRFDDIDLLRLSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 90 SEliqTRQRIG----MIFQH------------FNLMSAKTVWENVALPLKVSNYNKadidQRVNEVLALVGLADKSNY-- 151
Cdd:PRK15093 81 RE---RRKLVGhnvsMIFQEpqscldpservgRQLMQNIPGWTYKGRWWQRFGWRK----RRAIELLHRVGIKDHKDAmr 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 152 -YPSQLSGGQKQRVGIARALVHHPEILLCDEATSALDPESTATILALLKKINQELGLTIVLITHEMQVIREICDQVVVID 230
Cdd:PRK15093 154 sFPYELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLY 233
|
250 260
....*....|....*....|....*.
gi 1194606020 231 QGEIVEAGQVWSVFSRPEQQITQELL 256
Cdd:PRK15093 234 CGQTVETAPSKELVTTPHHPYTQALI 259
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
36-239 |
2.35e-24 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 104.03 E-value: 2.35e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 36 LKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQNIAELSHSELiqtRQRIGMIFQHFNLMsAKTVW 115
Cdd:PRK10790 357 LQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVL---RQGVAMVQQDPVVL-ADTFL 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 116 ENVALPLKVSnynkadiDQRVNEVLALVGLADKSNYYP-----------SQLSGGQKQRVGIARALVHHPEILLCDEATS 184
Cdd:PRK10790 433 ANVTLGRDIS-------EEQVWQALETVQLAELARSLPdglytplgeqgNNLSVGQKQLLALARVLVQTPQILILDEATA 505
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1194606020 185 ALDPESTATILALLKKINQElgLTIVLITHEMQVIREiCDQVVVIDQGEIVEAGQ 239
Cdd:PRK10790 506 NIDSGTEQAIQQALAAVREH--TTLVVIAHRLSTIVE-ADTILVLHRGQAVEQGT 557
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
17-238 |
2.79e-24 |
|
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: 97.77 E-value: 2.79e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 17 IKIRGLNKFYQSQGQklHALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQNIAELSHseliQTR 96
Cdd:cd03247 1 LSINNVSFSYPEQEQ--QVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEK----ALS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 97 QRIGMIFQHFNLMSAkTVWENVALplkvsnynkadidqrvnevlalvgladksnyypsQLSGGQKQRVGIARALVHHPEI 176
Cdd:cd03247 75 SLISVLNQRPYLFDT-TLRNNLGR----------------------------------RFSGGERQRLALARILLQDAPI 119
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1194606020 177 LLCDEATSALDPESTATILALLKKINQElgLTIVLITHEMQVIrEICDQVVVIDQGEIVEAG 238
Cdd:cd03247 120 VLLDEPTVGLDPITERQLLSLIFEVLKD--KTLIWITHHLTGI-EHMDKILFLENGKIIMQG 178
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
35-238 |
7.55e-24 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 102.73 E-value: 7.55e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 35 ALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQNIAELSHSELiqtRQRIGMIFQHFNLMsAKTV 114
Cdd:PRK13657 350 GVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASL---RRNIAVVFQDAGLF-NRSI 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 115 WENVALplkvsnyNKAD-IDQRVNEVL----ALVGLADKSNYYP-------SQLSGGQKQRVGIARALVHHPEILLCDEA 182
Cdd:PRK13657 426 EDNIRV-------GRPDaTDEEMRAAAeraqAHDFIERKPDGYDtvvgergRQLSGGERQRLAIARALLKDPPILILDEA 498
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1194606020 183 TSALDPESTATILALLKKINQelGLTIVLITHEMQVIREiCDQVVVIDQGEIVEAG 238
Cdd:PRK13657 499 TSALDVETEAKVKAALDELMK--GRTTFIIAHRLSTVRN-ADRILVFDNGRVVESG 551
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
36-234 |
9.13e-24 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 102.07 E-value: 9.13e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 36 LKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQniaelshseliqtrQRIGMIFQHFNLMSAKTVW 115
Cdd:COG0488 14 LDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKG--------------LRIGYLPQEPPLDDDLTVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 116 ENVALPLK-----VSNYNKA---------------------------DIDQRVNEVLALVGLADKSNYYP-SQLSGGQKQ 162
Cdd:COG0488 80 DTVLDGDAelralEAELEELeaklaepdedlerlaelqeefealggwEAEARAEEILSGLGFPEEDLDRPvSELSGGWRR 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1194606020 163 RVGIARALVHHPEILLCDEATSALDPESTATILALLKKINqelGlTIVLITHEMQVIREICDQVVVIDQGEI 234
Cdd:COG0488 160 RVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYP---G-TVLVVSHDRYFLDRVATRILELDRGKL 227
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
29-238 |
7.93e-23 |
|
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: 95.03 E-value: 7.93e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 29 QGQKLHALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQ---VNTGSIHIHQQniaELSHSeliQTRQRIGMIFQH 105
Cdd:cd03234 16 WNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEgggTTSGQILFNGQ---PRKPD---QFQKCVAYVRQD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 106 FNLMSAKTVWENV--ALPLKVSNYNKADIDQRVNEVLALVGLADKS--NYYPSQLSGGQKQRVGIARALVHHPEILLCDE 181
Cdd:cd03234 90 DILLPGLTVRETLtyTAILRLPRKSSDAIRKKRVEDVLLRDLALTRigGNLVKGISGGERRRVSIAVQLLWDPKVLILDE 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1194606020 182 ATSALDPESTATILALLKKINQELGLTIVLITHEMQVIREICDQVVVIDQGEIVEAG 238
Cdd:cd03234 170 PTSGLDSFTALNLVSTLSQLARRNRIVILTIHQPRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
36-234 |
3.98e-22 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 93.30 E-value: 3.98e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 36 LKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQNIAELSHSELiqtRQRIGMIFQHFNLmSAKTVW 115
Cdd:cd03248 30 LQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYL---HSKVSLVGQEPVL-FARSLQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 116 ENVALPLK-VSNYNKADIDQRVNEVLALVGLADksNYYP------SQLSGGQKQRVGIARALVHHPEILLCDEATSALDP 188
Cdd:cd03248 106 DNIAYGLQsCSFECVKEAAQKAHAHSFISELAS--GYDTevgekgSQLSGGQKQRVAIARALIRNPQVLILDEATSALDA 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1194606020 189 ESTATILALLKKINQElgLTIVLITHEMQVIrEICDQVVVIDQGEI 234
Cdd:cd03248 184 ESEQQVQQALYDWPER--RTVLVIAHRLSTV-ERADQILVLDGGRI 226
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
35-236 |
2.04e-21 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 94.98 E-value: 2.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 35 ALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQNIAELSHSELIQtrQRIGMIFQHFNLMSAKTV 114
Cdd:PRK11288 19 ALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAALA--AGVAIIYQELHLVPEMTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 115 WENV---ALPLKVSNYNKADIDQRVNEVLALVGLADKSNYYPSQLSGGQKQRVGIARALVHHPEILLCDEATSALDPEST 191
Cdd:PRK11288 97 AENLylgQLPHKGGIVNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAFDEPTSSLSAREI 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1194606020 192 ATILALLKKINQElGLTIVLITHEMQVIREICDQVVVIDQGEIVE 236
Cdd:PRK11288 177 EQLFRVIRELRAE-GRVILYVSHRMEEIFALCDAITVFKDGRYVA 220
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
35-233 |
2.43e-21 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 95.00 E-value: 2.43e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 35 ALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNT--GSIHI-----HQQNIAElshSEliqtRQRIGMIFQHFN 107
Cdd:PRK13549 20 ALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGTyeGEIIFegeelQASNIRD---TE----RAGIAIIHQELA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 108 LMSAKTVWENVAL-----PLKVSNYNKadIDQRVNEVLALVGLADKSNYYPSQLSGGQKQRVGIARALVHHPEILLCDEA 182
Cdd:PRK13549 93 LVKELSVLENIFLgneitPGGIMDYDA--MYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQARLLILDEP 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1194606020 183 TSALDPESTATILALLKKINQElGLTIVLITHEMQVIREICDQVVVIDQGE 233
Cdd:PRK13549 171 TASLTESETAVLLDIIRDLKAH-GIACIYISHKLNEVKAISDTICVIRDGR 220
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
14-238 |
3.49e-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: 95.47 E-value: 3.49e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 14 LPHIKIRGLNKFYQSQGQKlhALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQNIaelsHSELI 93
Cdd:TIGR01257 926 VPGVCVKNLVKIFEPSGRP--AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI----ETNLD 999
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 94 QTRQRIGMIFQHFNLMSAKTVWENVALPLKVSNYNKADIDQRVNEVLALVGLADKSNYYPSQLSGGQKQRVGIARALVHH 173
Cdd:TIGR01257 1000 AVRQSLGMCPQHNILFHHLTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGD 1079
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1194606020 174 PEILLCDEATSALDPESTATILALLKKINQelGLTIVLITHEMQVIREICDQVVVIDQGEIVEAG 238
Cdd:TIGR01257 1080 AKVVVLDEPTSGVDPYSRRSIWDLLLKYRS--GRTIIMSTHHMDEADLLGDRIAIISQGRLYCSG 1142
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
36-238 |
3.58e-21 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 91.11 E-value: 3.58e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 36 LKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQNIAELSHSEliQTRQRIGMIFQHFNLMSAKTVW 115
Cdd:PRK10895 19 VEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHA--RARRGIGYLPQEASIFRRLSVY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 116 ENVALPLKV-SNYNKADIDQRVNEVLALVGLADKSNYYPSQLSGGQKQRVGIARALVHHPEILLCDEATSALDPESTATI 194
Cdd:PRK10895 97 DNLMAVLQIrDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPISVIDI 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1194606020 195 lallKKINQEL---GLTIVLITHEMQVIREICDQVVVIDQGEIVEAG 238
Cdd:PRK10895 177 ----KRIIEHLrdsGLGVLITDHNVRETLAVCERAYIVSQGHLIAHG 219
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
35-245 |
5.24e-21 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 91.10 E-value: 5.24e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 35 ALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQNIAELSHSELIQTRQRIGMIFQHFNLMSAKTV 114
Cdd:PRK15056 22 ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNLVAYVPQSEEVDWSFPVLVEDVV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 115 WENVALPLKVSNYNKADIDQRVNEVLALVGLADKSNYYPSQLSGGQKQRVGIARALVHHPEILLCDEATSALDPESTATI 194
Cdd:PRK15056 102 MMGRYGHMGWLRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARI 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1194606020 195 LALLKKINQElGLTIVLITHEMQVIREICDQVVVIdQGEIVEAGQVWSVFS 245
Cdd:PRK15056 182 ISLLRELRDE-GKTMLVSTHNLGSVTEFCDYTVMV-KGTVLASGPTETTFT 230
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
39-256 |
5.27e-21 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 90.67 E-value: 5.27e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 39 INLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQvNTGSIHIHQQNIAELSHSELiqTRQRiGMIFQHFNLMSAKTVWENV 118
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKSTLLARMAGLLP-GQGEILLNGRPLSDWSAAEL--ARHR-AYLSQQQSPPFAMPVFQYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 119 ALPLKvSNYNKADIDQRVNEVLALVGLADKSNYYPSQLSGGQKQRVGIARALVH-HPEI------LLCDEATSALDPEST 191
Cdd:COG4138 91 ALHQP-AGASSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLQvWPTInpegqlLLLDEPMNSLDVAQQ 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1194606020 192 ATILALLKKINQeLGLTIVLITHEMQVIREICDQVVVIDQGEIVEAGqvwsvfsRPEQQITQELL 256
Cdd:COG4138 170 AALDRLLRELCQ-QGITVVMSSHDLNHTLRHADRVWLLKQGKLVASG-------ETAEVMTPENL 226
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
34-254 |
5.57e-21 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 93.93 E-value: 5.57e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 34 HALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQNIAELSHSELIqtRQRIGMI---FQHFNLMS 110
Cdd:COG1129 266 GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDAI--RAGIAYVpedRKGEGLVL 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 111 AKTVWENVALPL--KVSNY---NKADIDQRVNEVLALVGLADKSNYYP-SQLSGGQKQRVGIARALVHHPEILLCDEATS 184
Cdd:COG1129 344 DLSIRENITLASldRLSRGgllDRRRERALAEEYIKRLRIKTPSPEQPvGNLSGGNQQKVVLAKWLATDPKVLILDEPTR 423
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 185 ALDPESTATILALLKKINQElGLTIVLITHEMQVIREICDQVVVIDQGEIVEagqvwsVFSRPEqqITQE 254
Cdd:COG1129 424 GIDVGAKAEIYRLIRELAAE-GKAVIVISSELPELLGLSDRILVMREGRIVG------ELDREE--ATEE 484
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
15-238 |
7.67e-21 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 93.58 E-value: 7.67e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 15 PHIKIRGLNKFYQSqgqkLHALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQNIAELSHSELIQ 94
Cdd:PRK15439 10 PLLCARSISKQYSG----VEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 95 TrqRIGMIFQHFNLMSAKTVWENVALPLKvsnyNKADIDQRVNEVLALVGLADKSNYYPSQLSGGQKQRVGIARALVHHP 174
Cdd:PRK15439 86 L--GIYLVPQEPLLFPNLSVKENILFGLP----KRQASMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDS 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1194606020 175 EILLCDEATSALDPESTATILALLKKInQELGLTIVLITHEMQVIREICDQVVVIDQGEIVEAG 238
Cdd:PRK15439 160 RILILDEPTASLTPAETERLFSRIREL-LAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSG 222
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
32-235 |
1.22e-20 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 89.55 E-value: 1.22e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 32 KLHALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQNIAELSHSELIqtRQRIGMIFQHFNLMSA 111
Cdd:PRK11614 17 KIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIM--REAVAIVPEGRRVFSR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 112 KTVWENVALPLKVSnyNKADIDQRVNEVLALVG-LADKSNYYPSQLSGGQKQRVGIARALVHHPEILLCDEATSALDPES 190
Cdd:PRK11614 95 MTVEENLAMGGFFA--ERDQFQERIKWVYELFPrLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPII 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1194606020 191 TATILALLKKINQElGLTIVLITHEMQVIREICDQVVVIDQGEIV 235
Cdd:PRK11614 173 IQQIFDTIEQLREQ-GMTIFLVEQNANQALKLADRGYVLENGHVV 216
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
35-238 |
1.33e-20 |
|
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: 93.27 E-value: 1.33e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 35 ALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQNIAELSHSELiqtRQRIGMIFQHfNLMSAKTV 114
Cdd:TIGR01193 489 ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTL---RQFINYLPQE-PYIFSGSI 564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 115 WENVALPLKvSNYNKADIDQ--RVNEVLALV-----GLADKSNYYPSQLSGGQKQRVGIARALVHHPEILLCDEATSALD 187
Cdd:TIGR01193 565 LENLLLGAK-ENVSQDEIWAacEIAEIKDDIenmplGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLD 643
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1194606020 188 PESTATILALLKKINQElglTIVLITHEMQVIREIcDQVVVIDQGEIVEAG 238
Cdd:TIGR01193 644 TITEKKIVNNLLNLQDK---TIIFVAHRLSVAKQS-DKIIVLDHGKIIEQG 690
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
35-233 |
2.72e-20 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 91.60 E-value: 2.72e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 35 ALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQNIAELS--HSEliqtRQRIGMIFQHFNLMSAK 112
Cdd:PRK10762 19 ALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGpkSSQ----EAGIGIIHQELNLIPQL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 113 TVWENVALPLKVSN----------YNKADidqrvnEVLALVGLADKSNYYPSQLSGGQKQRVGIARALVHHPEILLCDEA 182
Cdd:PRK10762 95 TIAENIFLGREFVNrfgridwkkmYAEAD------KLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEP 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1194606020 183 TSALDPESTAtilALLKKIN--QELGLTIVLITHEMQVIREICDQVVVIDQGE 233
Cdd:PRK10762 169 TDALTDTETE---SLFRVIRelKSQGRGIVYISHRLKEIFEICDDVTVFRDGQ 218
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
17-236 |
4.19e-20 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 91.28 E-value: 4.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 17 IKIRGLNKFYQsqGQKLhaLKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHqqniaelshseliqTR 96
Cdd:COG0488 316 LELEGLSKSYG--DKTL--LDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLG--------------ET 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 97 QRIGMIFQHF-NLMSAKTVWENvalplkVSNYNKADIDQRVNEVLALVGLA-DKSNYYPSQLSGGQKQRVGIARALVHHP 174
Cdd:COG0488 378 VKIGYFDQHQeELDPDKTVLDE------LRDGAPGGTEQEVRGYLGRFLFSgDDAFKPVGVLSGGEKARLALAKLLLSPP 451
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1194606020 175 EILLCDEATSALDPEStatiLALLkkinqELGL-----TIVLITHEMQVIREICDQVVVIDQGEIVE 236
Cdd:COG0488 452 NVLLLDEPTNHLDIET----LEAL-----EEALddfpgTVLLVSHDRYFLDRVATRILEFEDGGVRE 509
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
36-220 |
5.70e-20 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 86.85 E-value: 5.70e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 36 LKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQNIAELSHSELIQTrqrIGmifqHFNLM-SAKTV 114
Cdd:PRK13539 18 FSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACHY---LG----HRNAMkPALTV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 115 WENVALPLKVSNYNKADIDqrvnEVLALVGLAD----KSNYypsqLSGGQKQRVGIARALVHHPEILLCDEATSALDPES 190
Cdd:PRK13539 91 AENLEFWAAFLGGEELDIA----AALEAVGLAPlahlPFGY----LSAGQKRRVALARLLVSNRPIWILDEPTAALDAAA 162
|
170 180 190
....*....|....*....|....*....|....*.
gi 1194606020 191 TATILALLkKINQELGLTIVLITH------EMQVIR 220
Cdd:PRK13539 163 VALFAELI-RAHLAQGGIVIAATHiplglpGARELD 197
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
17-233 |
9.56e-20 |
|
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: 84.42 E-value: 9.56e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 17 IKIRGLNKFYQsqGQKLhaLKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQqniaelshseliqtR 96
Cdd:cd03221 1 IELENLSKTYG--GKLL--LKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGS--------------T 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 97 QRIGmifqhfnlmsaktvwenvalplkvsnynkadidqrvnevlalvgladksnYYPsQLSGGQKQRVGIARALVHHPEI 176
Cdd:cd03221 63 VKIG--------------------------------------------------YFE-QLSGGEKMRLALAKLLLENPNL 91
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1194606020 177 LLCDEATSALDPESTATILALLKKINQelglTIVLITHEMQVIREICDQVVVIDQGE 233
Cdd:cd03221 92 LLLDEPTNHLDLESIEALEEALKEYPG----TVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
35-235 |
1.37e-19 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 89.88 E-value: 1.37e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 35 ALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQNiAELSHSELIQT-RQRIGMIFQHFNLMSAKT 113
Cdd:TIGR02633 16 ALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTWDGEIYWSG-SPLKASNIRDTeRAGIVIIHQELTLVPELS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 114 VWENV------ALPLKVSNYNKadIDQRVNEVLALVGLADKSNYYP-SQLSGGQKQRVGIARALVHHPEILLCDEATSAL 186
Cdd:TIGR02633 95 VAENIflgneiTLPGGRMAYNA--MYLRAKNLLRELQLDADNVTRPvGDYGGGQQQLVEIAKALNKQARLLILDEPSSSL 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1194606020 187 DPESTATILALLKKINQElGLTIVLITHEMQVIREICDQVVVIDQGEIV 235
Cdd:TIGR02633 173 TEKETEILLDIIRDLKAH-GVACVYISHKLNEVKAVCDTICVIRDGQHV 220
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
39-214 |
1.82e-19 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 85.10 E-value: 1.82e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 39 INLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQNIAELSHSeliqtRQRIGMIFQHFN-LMSAKTVWEN 117
Cdd:TIGR01189 19 LSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDE-----PHENILYLGHLPgLKPELSALEN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 118 valpLKVSNYNKADIDQRVNEVLALVGLADKSNYYPSQLSGGQKQRVGIARALVHHPEILLCDEATSALDPESTATILAL 197
Cdd:TIGR01189 94 ----LHFWAAIHGGAQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVALLAGL 169
|
170
....*....|....*..
gi 1194606020 198 LKKINQELGLTIvLITH 214
Cdd:TIGR01189 170 LRAHLARGGIVL-LTTH 185
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
39-216 |
2.10e-19 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 89.80 E-value: 2.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 39 INLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSihihqqniAELSHSEL----IQTRQRIGMIFQHFNLMSAKTV 114
Cdd:NF033858 285 VSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGE--------AWLFGQPVdagdIATRRRVGYMSQAFSLYGELTV 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 115 WENVALPLKVSNYNKADIDQRVNEVLALVGLADKSNYYPSQLSGGQKQRVGIARALVHHPEILLCDEATSALDPestati 194
Cdd:NF033858 357 RQNLELHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDP------ 430
|
170 180
....*....|....*....|....*...
gi 1194606020 195 LA------LLKKINQELGLTIVLITHEM 216
Cdd:NF033858 431 VArdmfwrLLIELSREDGVTIFISTHFM 458
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
35-239 |
7.47e-19 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 87.85 E-value: 7.47e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 35 ALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQNIAELSHSELiqtRQRIGMIFQHFNLMSaKTV 114
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSW---RSRLAVVSQTPFLFS-DTV 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 115 WENVALplkvsnyNKADIDQ-RVNEVLALVGLADKSNYYPS-----------QLSGGQKQRVGIARALVHHPEILLCDEA 182
Cdd:PRK10789 406 ANNIAL-------GRPDATQqEIEHVARLASVHDDILRLPQgydtevgergvMLSGGQKQRISIARALLLNAEILILDDA 478
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1194606020 183 TSALDPESTATILALLKKINQelGLTIVLITHEMQVIREiCDQVVVIDQGEIVEAGQ 239
Cdd:PRK10789 479 LSAVDGRTEHQILHNLRQWGE--GRTVIISAHRLSALTE-ASEILVMQHGHIAQRGN 532
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
32-273 |
9.31e-19 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 87.87 E-value: 9.31e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 32 KLHALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQNIAELSHSELIQTR-----QRIGMifqhf 106
Cdd:NF033858 13 KTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMADARHRRAVCPRiaympQGLGK----- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 107 NLMSAKTVWENVALPLKVSNYNKADIDQRVNEVLALVGLADKSNYYPSQLSGGQKQRVGIARALVHHPEILLCDEATSAL 186
Cdd:NF033858 88 NLYPTLSVFENLDFFGRLFGQDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCALIHDPDLLILDEPTTGV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 187 DPESTATILALLKKINQEL-GLTIVLITHEMQVIrEICDQVVVIDQGEIVEAGQvwsvfsrpeqqiTQELL------NLE 259
Cdd:NF033858 168 DPLSRRQFWELIDRIRAERpGMSVLVATAYMEEA-ERFDWLVAMDAGRVLATGT------------PAELLartgadTLE 234
|
250
....*....|....*.
gi 1194606020 260 Q--ITLpfkinpLPDE 273
Cdd:NF033858 235 AafIAL------LPEE 244
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
20-240 |
2.19e-18 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 86.25 E-value: 2.19e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 20 RGLNKFYQSQGQKlHALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNT---GSIHIHQQNIaelshsELIQTR 96
Cdd:TIGR00955 26 RLRGCFCRERPRK-HLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGVkgsGSVLLNGMPI------DAKEMR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 97 QRIGMIFQHFNLMSAKTVWEN------VALPLKVSNYNKAdidQRVNEVLALVGLADKSNY---YPSQ---LSGGQKQRV 164
Cdd:TIGR00955 99 AISAYVQQDDLFIPTLTVREHlmfqahLRMPRRVTKKEKR---ERVDEVLQALGLRKCANTrigVPGRvkgLSGGERKRL 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1194606020 165 GIARALVHHPEILLCDEATSALDPESTATILALLKKINQElGLTIVLITHE-MQVIREICDQVVVIDQGEIVEAGQV 240
Cdd:TIGR00955 176 AFASELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGLAQK-GKTIICTIHQpSSELFELFDKIILMAEGRVAYLGSP 251
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
39-267 |
2.72e-18 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 83.06 E-value: 2.72e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 39 INLDIPQGKILGIIGKSGAGKSSLLRTLNGLeQVNTGSIHIHQQNIAELSHSELIQTRqriGMIFQHFNLMSAKTVWENV 118
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGL-LPGSGSIQFAGQPLEAWSAAELARHR---AYLSQQQTPPFAMPVFQYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 119 ALPLKVSNyNKADIDQRVNEVLALVGLADKSNYYPSQLSGGQKQRVGIARALVH-HPEI------LLCDEATSALDPEST 191
Cdd:PRK03695 91 TLHQPDKT-RTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVLQvWPDInpagqlLLLDEPMNSLDVAQQ 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1194606020 192 ATILALLKKINQeLGLTIVLITHEMQVIREICDQVVVIDQGEIVEAGqvwsvfsRPEQQITQEllNLEQI-TLPFKI 267
Cdd:PRK03695 170 AALDRLLSELCQ-QGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASG-------RRDEVLTPE--NLAQVfGVNFRR 236
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
33-235 |
2.79e-18 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 85.85 E-value: 2.79e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 33 LHALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQNIAELSHSELIQT--------RQRIGMIfq 104
Cdd:COG3845 271 VPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLgvayipedRLGRGLV-- 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 105 hfnlmSAKTVWENVALplkvSNYNKAD------IDQRVNEVLA--LV--------GLADKSnyypSQLSGGQKQRVGIAR 168
Cdd:COG3845 349 -----PDMSVAENLIL----GRYRRPPfsrggfLDRKAIRAFAeeLIeefdvrtpGPDTPA----RSLSGGNQQKVILAR 415
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1194606020 169 ALVHHPEILLCDEATSALDPESTATILALLKKINQElGLTIVLITHEMQVIREICDQVVVIDQGEIV 235
Cdd:COG3845 416 ELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDA-GAAVLLISEDLDEILALSDRIAVMYEGRIV 481
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
22-231 |
4.21e-18 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 82.47 E-value: 4.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 22 LNKFYQSQGQKlHALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIhIHQQNIaelshseliqtrqRIGM 101
Cdd:PRK09544 7 LENVSVSFGQR-RVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI-KRNGKL-------------RIGY 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 102 IFQHFNLmsaktvweNVALPLKVSNY-------NKADIdqrvNEVLALVGLADKSNYYPSQLSGGQKQRVGIARALVHHP 174
Cdd:PRK09544 72 VPQKLYL--------DTTLPLTVNRFlrlrpgtKKEDI----LPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRP 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1194606020 175 EILLCDEATSALDPESTATILALLKKINQELGLTIVLITHEMQVIREICDQVVVIDQ 231
Cdd:PRK09544 140 QLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCLNH 196
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
26-217 |
5.56e-18 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 81.61 E-value: 5.56e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 26 YQSQGQKLHALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQNIAELSHSEL-IQTRQRIGMIFQ 104
Cdd:cd03290 7 YFSWGSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATrSRNRYSVAYAAQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 105 HFNLMSAkTVWENVALPlkvSNYNKadidQRVNEVLALVGLADKSNYYPS-----------QLSGGQKQRVGIARALVHH 173
Cdd:cd03290 87 KPWLLNA-TVEENITFG---SPFNK----QRYKAVTDACSLQPDIDLLPFgdqteigergiNLSGGQRQRICVARALYQN 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1194606020 174 PEILLCDEATSALDPE-STATILALLKKINQELGLTIVLITHEMQ 217
Cdd:cd03290 159 TNIVFLDDPFSALDIHlSDHLMQEGILKFLQDDKRTLVLVTHKLQ 203
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
26-227 |
6.08e-18 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 81.68 E-value: 6.08e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 26 YQSQGQKLhaLKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQNIAELSHSeliQTRQRIGMIFQH 105
Cdd:PRK10247 15 YLAGDAKI--LNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPE---IYRQQVSYCAQT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 106 FNLMsAKTVWENVALPLKVSNynKADIDQRVNEVLALVGLADKSNYYP-SQLSGGQKQRVGIARALVHHPEILLCDEATS 184
Cdd:PRK10247 90 PTLF-GDTVYDNLIFPWQIRN--QQPDPAIFLDDLERFALPDTILTKNiAELSGGEKQRISLIRNLQFMPKVLLLDEITS 166
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1194606020 185 ALDPESTATILALLKKINQELGLTIVLITHEMQVIREiCDQVV 227
Cdd:PRK10247 167 ALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDEINH-ADKVI 208
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
36-238 |
9.81e-18 |
|
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: 85.00 E-value: 9.81e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 36 LKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQNIAELSHSELiqtRQRIGMIFQHFNLMSAkTVW 115
Cdd:TIGR00957 1302 LRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDL---RFKITIIPQDPVLFSG-SLR 1377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 116 ENVAlPLkvSNYNKADIDQRVnEVLALVG----LADKSNYYPSQ----LSGGQKQRVGIARALVHHPEILLCDEATSALD 187
Cdd:TIGR00957 1378 MNLD-PF--SQYSDEEVWWAL-ELAHLKTfvsaLPDKLDHECAEggenLSVGQRQLVCLARALLRKTKILVLDEATAAVD 1453
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1194606020 188 PESTATILALLKkiNQELGLTIVLITHEMQVIREICdQVVVIDQGEIVEAG 238
Cdd:TIGR00957 1454 LETDNLIQSTIR--TQFEDCTVLTIAHRLNTIMDYT-RVIVLDKGEVAEFG 1501
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
33-254 |
7.95e-17 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 82.09 E-value: 7.95e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 33 LHALK-EINldiPQGKiLGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQNIAELSHSELiqtRQRIGMIFQHFNLMSA 111
Cdd:PLN03130 1255 LHGLSfEIS---PSEK-VGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDL---RKVLGIIPQAPVLFSG 1327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 112 kTVWENVAlPLkvSNYNKADIdqrvNEVLALVGLADKSNYYPSQL-----------SGGQKQRVGIARALVHHPEILLCD 180
Cdd:PLN03130 1328 -TVRFNLD-PF--NEHNDADL----WESLERAHLKDVIRRNSLGLdaevseagenfSVGQRQLLSLARALLRRSKILVLD 1399
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1194606020 181 EATSALDPESTATIlalLKKINQEL-GLTIVLITHEMQVIREiCDQVVVIDQGEIVEagqvwsvFSRPEQQITQE 254
Cdd:PLN03130 1400 EATAAVDVRTDALI---QKTIREEFkSCTMLIIAHRLNTIID-CDRILVLDAGRVVE-------FDTPENLLSNE 1463
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
45-222 |
1.05e-16 |
|
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: 77.53 E-value: 1.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 45 QGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQNIAElSHSELIQTRQRIGmifqHFNLMSAK-TVWENVALplk 123
Cdd:cd03231 25 AGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDF-QRDSIARGLLYLG----HAPGIKTTlSVLENLRF--- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 124 vsnYNKADIDQRVNEVLALVGLADKSNYYPSQLSGGQKQRVGIARALVHHPEILLCDEATSALDPESTATILALLKKiNQ 203
Cdd:cd03231 97 ---WHADHSDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEAMAG-HC 172
|
170 180
....*....|....*....|....
gi 1194606020 204 ELGLTIVLITH-----EMQVIREI 222
Cdd:cd03231 173 ARGGMVVLTTHqdlglSEAGAREL 196
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
38-219 |
1.40e-16 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 77.15 E-value: 1.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 38 EINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQNIAELS---HSELIQtrqrIGmifqHFN-LMSAKT 113
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRdeyHQDLLY----LG----HQPgIKTELT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 114 VWENVALPLKVSNYNKADidqRVNEVLALVGLADKSNYYPSQLSGGQKQRVGIARALVHHPEILLCDEATSALDPESTAT 193
Cdd:PRK13538 91 ALENLRFYQRLHGPGDDE---ALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGVAR 167
|
170 180
....*....|....*....|....*..
gi 1194606020 194 ILALLKKiNQELGLTIVLITH-EMQVI 219
Cdd:PRK13538 168 LEALLAQ-HAEQGGMVILTTHqDLPVA 193
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
35-235 |
1.82e-16 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 80.16 E-value: 1.82e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 35 ALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQNIAELSHSELIQtrQRIGMIFQHFNLMSAKTV 114
Cdd:PRK10982 13 ALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEALE--NGISMVHQELNLVLQRSV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 115 WENVAL---PLKVSNYNKADIDQRVNEVLALVGLADKSNYYPSQLSGGQKQRVGIARALVHHPEILLCDEATSALDPEST 191
Cdd:PRK10982 91 MDNMWLgryPTKGMFVDQDKMYRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLTEKEV 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1194606020 192 ATILALLKKInQELGLTIVLITHEMQVIREICDQVVVIDQGEIV 235
Cdd:PRK10982 171 NHLFTIIRKL-KERGCGIVYISHKMEEIFQLCDEITILRDGQWI 213
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
36-238 |
2.26e-16 |
|
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: 76.41 E-value: 2.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 36 LKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLE--QVNTGSIHIHQQNIAELSHSEliqtRQR--IGMIFQHfnlmsa 111
Cdd:cd03217 16 LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKGEDITDLPPEE----RARlgIFLAFQY------ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 112 ktvwenvalPLKVSNYNKADIDQRVNEvlalvgladksnyypsQLSGGQKQRVGIARALVHHPEILLCDEATSALDPEST 191
Cdd:cd03217 86 ---------PPEIPGVKNADFLRYVNE----------------GFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDAL 140
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1194606020 192 ATILALLKKINQElGLTIVLITHEMQVIREI-CDQVVVIDQGEIVEAG 238
Cdd:cd03217 141 RLVAEVINKLREE-GKSVLIITHYQRLLDYIkPDRVHVLYDGRIVKSG 187
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
17-215 |
2.37e-16 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 79.98 E-value: 2.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 17 IKIRGLNKFYqsqGQKLhALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQniAELSHSEliQTR 96
Cdd:TIGR03719 323 IEAENLTKAF---GDKL-LIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGET--VKLAYVD--QSR 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 97 QrigmifqhfNLMSAKTVWENVALPLKVSNYNKADIDQRvnevlALVGL-----ADKSNYYpSQLSGGQKQRVGIARALV 171
Cdd:TIGR03719 395 D---------ALDPNKTVWEEISGGLDIIKLGKREIPSR-----AYVGRfnfkgSDQQKKV-GQLSGGERNRVHLAKTLK 459
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1194606020 172 HHPEILLCDEATSALDPEstaTILALLKKInQELGLTIVLITHE 215
Cdd:TIGR03719 460 SGGNVLLLDEPTNDLDVE---TLRALEEAL-LNFAGCAVVISHD 499
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
37-234 |
9.64e-16 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 78.17 E-value: 9.64e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 37 KEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQNIAELShselIQTRQRIGMIF------QHFNLMS 110
Cdd:PRK15439 280 RNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALS----TAQRLARGLVYlpedrqSSGLYLD 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 111 AKTVWENVALplkvsNYNKADIDQRVNEVLALV-----GLADKSNYyPSQ----LSGGQKQRVGIARALVHHPEILLCDE 181
Cdd:PRK15439 356 APLAWNVCAL-----THNRRGFWIKPARENAVLeryrrALNIKFNH-AEQaartLSGGNQQKVLIAKCLEASPQLLIVDE 429
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1194606020 182 ATSALDPESTATILALLKKINQElGLTIVLITHEMQVIREICDQVVVIDQGEI 234
Cdd:PRK15439 430 PTRGVDVSARNDIYQLIRSIAAQ-NVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
19-233 |
1.11e-15 |
|
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: 78.05 E-value: 1.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 19 IRGLNKFYqsqGQKLHALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIhQQNIaelshseliqtrqR 98
Cdd:TIGR03719 7 MNRVSKVV---PPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARP-QPGI-------------K 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 99 IGMIFQHFNLMSAKTVWENVALPL-----KVSNYNK---------ADIDQ------RVNEVLALVGL----------ADK 148
Cdd:TIGR03719 70 VGYLPQEPQLDPTKTVRENVEEGVaeikdALDRFNEisakyaepdADFDKlaaeqaELQEIIDAADAwdldsqleiaMDA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 149 SNYYP-----SQLSGGQKQRVGIARALVHHPEILLCDEATSALDPESTatilALLKKINQELGLTIVLITHEMQVIREIC 223
Cdd:TIGR03719 150 LRCPPwdadvTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESV----AWLERHLQEYPGTVVAVTHDRYFLDNVA 225
|
250
....*....|
gi 1194606020 224 DQVVVIDQGE 233
Cdd:TIGR03719 226 GWILELDRGR 235
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
49-254 |
2.48e-15 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 77.71 E-value: 2.48e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 49 LGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQNIAELSHSELiqtRQRIGMIFQHFNLMSAkTVWENVAlPLkvSNYN 128
Cdd:PLN03232 1265 VGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDL---RRVLSIIPQSPVLFSG-TVRFNID-PF--SEHN 1337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 129 KADIdqrvNEVLALVGLADKSNYYPSQL-----------SGGQKQRVGIARALVHHPEILLCDEATSALDPESTATIlal 197
Cdd:PLN03232 1338 DADL----WEALERAHIKDVIDRNPFGLdaevseggenfSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLI--- 1410
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1194606020 198 LKKINQEL-GLTIVLITHEMQVIREiCDQVVVIDQGEIVEagqvwsvFSRPEQQITQE 254
Cdd:PLN03232 1411 QRTIREEFkSCTMLVIAHRLNTIID-CDKILVLSSGQVLE-------YDSPQELLSRD 1460
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
35-236 |
2.51e-15 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 76.75 E-value: 2.51e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 35 ALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNT--GSIHIHQQ--NIAELSHSEliqtRQRIGMIFQHFNLMS 110
Cdd:NF040905 16 ALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGSyeGEILFDGEvcRFKDIRDSE----ALGIVIIHQELALIP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 111 AKTVWENVAL---PLK--VSNYNKAdiDQRVNEVLALVGLADKSNYYPSQLSGGQKQRVGIARALVHHPEILLCDEATSA 185
Cdd:NF040905 92 YLSIAENIFLgneRAKrgVIDWNET--NRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLILDEPTAA 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1194606020 186 LDPESTATILALLKKINQElGLTIVLITHEMQVIREICDQVVVIDQGEIVE 236
Cdd:NF040905 170 LNEEDSAALLDLLLELKAQ-GITSIIISHKLNEIRRVADSITVLRDGRTIE 219
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
37-236 |
4.43e-15 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 75.98 E-value: 4.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 37 KEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQNIAelSHSELIQTRQRIGMI---------FQHFN 107
Cdd:PRK09700 280 RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDIS--PRSPLDAVKKGMAYItesrrdngfFPNFS 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 108 LMsaktvwENVALP--LKVSNY----------NKADIDQRVNEVLALVGLADKSNYypSQLSGGQKQRVGIARALVHHPE 175
Cdd:PRK09700 358 IA------QNMAISrsLKDGGYkgamglfhevDEQRTAENQRELLALKCHSVNQNI--TELSGGNQQKVLISKWLCCCPE 429
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1194606020 176 ILLCDEATSALDPESTATILALLKKINQElGLTIVLITHEMQVIREICDQVVVIDQGEIVE 236
Cdd:PRK09700 430 VIIFDEPTRGIDVGAKAEIYKVMRQLADD-GKVILMVSSELPEIITVCDRIAVFCEGRLTQ 489
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
20-214 |
6.74e-15 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 75.54 E-value: 6.74e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 20 RGLNKFYqsqGQKLHALKEINLD-IPQGKIlGIIGKSGAGKSSLLRTLNGLEQVNTGSIhIHQQNIaelshseliqtrqR 98
Cdd:PRK11819 10 NRVSKVV---PPKKQILKDISLSfFPGAKI-GVLGLNGAGKSTLLRIMAGVDKEFEGEA-RPAPGI-------------K 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 99 IGMIFQHFNLMSAKTVWENVALPLKvsnyNKADIDQRVNEVLALvgLADKSNYY-------------------------- 152
Cdd:PRK11819 72 VGYLPQEPQLDPEKTVRENVEEGVA----EVKAALDRFNEIYAA--YAEPDADFdalaaeqgelqeiidaadawdldsql 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1194606020 153 ---------P------SQLSGGQKQRVGIARALVHHPEILLCDEATSALDPESTatilALLKKINQELGLTIVLITH 214
Cdd:PRK11819 146 eiamdalrcPpwdakvTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESV----AWLEQFLHDYPGTVVAVTH 218
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
14-238 |
9.79e-15 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 75.54 E-value: 9.79e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 14 LPHIKIRGLNKFYQSQGQKlHALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNG-LEQVNTGSIHIhQQNIAELSHSEL 92
Cdd:PLN03130 612 LPAISIKNGYFSWDSKAER-PTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGeLPPRSDASVVI-RGTVAYVPQVSW 689
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 93 IqtrqrigmifqhFNlmsaKTVWENV--ALPLKVSNYNKAdID----QRVNEVLA---LVGLADKSnyypSQLSGGQKQR 163
Cdd:PLN03130 690 I------------FN----ATVRDNIlfGSPFDPERYERA-IDvtalQHDLDLLPggdLTEIGERG----VNISGGQKQR 748
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1194606020 164 VGIARALVHHPEILLCDEATSALDPESTATILAllKKINQEL-GLTIVLITHEMQVIREIcDQVVVIDQGEIVEAG 238
Cdd:PLN03130 749 VSMARAVYSNSDVYIFDDPLSALDAHVGRQVFD--KCIKDELrGKTRVLVTNQLHFLSQV-DRIILVHEGMIKEEG 821
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
51-235 |
2.16e-14 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 74.22 E-value: 2.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 51 IIGKSGAGKSSLLRTLNGLEQVNTGSIHIH--------QQN------------IAE-LSH-SELIQTRQRIGMIFQHfnL 108
Cdd:PRK11147 34 LVGRNGAGKSTLMKILNGEVLLDDGRIIYEqdlivarlQQDpprnvegtvydfVAEgIEEqAEYLKRYHDISHLVET--D 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 109 MSAKTVWENVALPLKVSNYNKADIDQRVNEVLALVGL-ADKSnyyPSQLSGGQKQRVGIARALVHHPEILLCDEATSALD 187
Cdd:PRK11147 112 PSEKNLNELAKLQEQLDHHNLWQLENRINEVLAQLGLdPDAA---LSSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLD 188
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1194606020 188 PESTATILALLKkinqELGLTIVLITHEMQVIREICDQVVVIDQGEIV 235
Cdd:PRK11147 189 IETIEWLEGFLK----TFQGSIIFISHDRSFIRNMATRIVDLDRGKLV 232
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
13-220 |
4.83e-14 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 73.52 E-value: 4.83e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 13 SLPHIK-IRGLN-KFYQSQGQKLHALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQNiaELSHS 90
Cdd:PTZ00265 376 KLKDIKkIQFKNvRFHYDTRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDSH--NLKDI 453
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 91 ELIQTRQRIGMIFQ-----------------------------------------------------HFNLMSaKTVWEN 117
Cdd:PTZ00265 454 NLKWWRSKIGVVSQdpllfsnsiknnikyslyslkdlealsnyynedgndsqenknkrnscrakcagDLNDMS-NTTDSN 532
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 118 VALPLKvSNYNKADIDQRVN---EVLA---LVGLADK------SNyyPSQLSGGQKQRVGIARALVHHPEILLCDEATSA 185
Cdd:PTZ00265 533 ELIEMR-KNYQTIKDSEVVDvskKVLIhdfVSALPDKyetlvgSN--ASKLSGGQKQRISIARAIIRNPKILILDEATSS 609
|
250 260 270
....*....|....*....|....*....|....*
gi 1194606020 186 LDPESTATILALLKKINQELGLTIVLITHEMQVIR 220
Cdd:PTZ00265 610 LDNKSEYLVQKTINNLKGNENRITIIIAHRLSTIR 644
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
21-238 |
5.87e-14 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 73.27 E-value: 5.87e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 21 GLNKFYQSQGQKLhaLKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIhihqqnIAELShseliqtrqrIG 100
Cdd:PTZ00243 663 KTDDFFELEPKVL--LRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV------WAERS----------IA 724
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 101 MIFQHFNLMSAkTVWENValpLKVSNYNKADIDQ--RVNEVLALV-----GLADKSNYYPSQLSGGQKQRVGIARALVHH 173
Cdd:PTZ00243 725 YVPQQAWIMNA-TVRGNI---LFFDEEDAARLADavRVSQLEADLaqlggGLETEIGEKGVNLSGGQKARVSLARAVYAN 800
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1194606020 174 PEILLCDEATSALDPEstatilaLLKKINQEL------GLTIVLITHEMQVIrEICDQVVVIDQGEIVEAG 238
Cdd:PTZ00243 801 RDVYLLDDPLSALDAH-------VGERVVEECflgalaGKTRVLATHQVHVV-PRADYVVALGDGRVEFSG 863
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
36-256 |
6.19e-14 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 72.73 E-value: 6.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 36 LKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQNIAELSHSELI--------QTRQRIGMIFQhfn 107
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDGLangivyisEDRKRDGLVLG--- 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 108 lMSAKtvwENVALP-LKVSNYNKADIDQRvNEVLALVGLADKSNY-YPSQ------LSGGQKQRVGIARALVHHPEILLC 179
Cdd:PRK10762 345 -MSVK---ENMSLTaLRYFSRAGGSLKHA-DEQQAVSDFIRLFNIkTPSMeqaiglLSGGNQQKVAIARGLMTRPKVLIL 419
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1194606020 180 DEATSALDPESTATILALLKKINQElGLTIVLITHEMQVIREICDQVVVIDQGEIveAGQvwsvFSRpeQQITQELL 256
Cdd:PRK10762 420 DEPTRGVDVGAKKEIYQLINQFKAE-GLSIILVSSEMPEVLGMSDRILVMHEGRI--SGE----FTR--EQATQEKL 487
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
30-214 |
1.20e-13 |
|
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: 72.09 E-value: 1.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 30 GQKLhaLKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIhqqniaelshseliQTRQRIGMIFQHfNLM 109
Cdd:TIGR00954 464 GDVL--IESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTK--------------PAKGKLFYVPQR-PYM 526
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 110 SAKTVWENVALPLKVSNYNKADI-DQRVNEVLALVGLA---------DKSNYYPSQLSGGQKQRVGIARALVHHPEILLC 179
Cdd:TIGR00954 527 TLGTLRDQIIYPDSSEDMKRRGLsDKDLEQILDNVQLThilereggwSAVQDWMDVLSGGEKQRIAMARLFYHKPQFAIL 606
|
170 180 190
....*....|....*....|....*....|....*
gi 1194606020 180 DEATSALDPESTATILALLKkinqELGLTIVLITH 214
Cdd:TIGR00954 607 DECTSAVSVDVEGYMYRLCR----EFGITLFSVSH 637
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
152-237 |
1.22e-13 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 72.37 E-value: 1.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 152 YPSQLSGGQKQRVGIARALVHHPEILLCDEATSALDPESTATILALLKKINQELGLTIVLITHEMQVIREiCDQVVVIDQ 231
Cdd:PTZ00265 1355 YGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASIKR-SDKIVVFNN 1433
|
90
....*....|
gi 1194606020 232 ----GEIVEA 237
Cdd:PTZ00265 1434 pdrtGSFVQA 1443
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
3-232 |
2.41e-13 |
|
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: 71.58 E-value: 2.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 3 MVSFGSQVDFslphIKIRGLNKFYQsqGQKLHALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQ 82
Cdd:TIGR01257 1928 IISGGNKTDI----LRLNELTKVYS--GTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGK 2001
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 83 NIAelshSELIQTRQRIGMIFQHFNLMSAKTVWENVALPLKVSNYNKADIDQRVNEVLALVGLADKSNYYPSQLSGGQKQ 162
Cdd:TIGR01257 2002 SIL----TNISDVHQNMGYCPQFDAIDDLLTGREHLYLYARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKR 2077
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 163 RVGIARALVHHPEILLCDEATSALDPESTATILALLKKINQElGLTIVLITHEMQVIREICDQVVVIDQG 232
Cdd:TIGR01257 2078 KLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKG 2146
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
7-197 |
2.83e-13 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 70.53 E-value: 2.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 7 GSQVdfslphIKIRGLNKFYqsqGQKLhALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQniAE 86
Cdd:PRK11819 321 GDKV------IEAENLSKSF---GDRL-LIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGET--VK 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 87 LSHSEliQTRQrigmifqhfNLMSAKTVWENVALPLKVSNYNKADIDQRvnevlALVGL-----ADKSNYYpSQLSGGQK 161
Cdd:PRK11819 389 LAYVD--QSRD---------ALDPNKTVWEEISGGLDIIKVGNREIPSR-----AYVGRfnfkgGDQQKKV-GVLSGGER 451
|
170 180 190
....*....|....*....|....*....|....*.
gi 1194606020 162 QRVGIARALVHHPEILLCDEATSALDPEstaTILAL 197
Cdd:PRK11819 452 NRLHLAKTLKQGGNVLLLDEPTNDLDVE---TLRAL 484
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
11-236 |
3.80e-13 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 70.39 E-value: 3.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 11 DFSLPH-------IKIRGLNKFYQSQGqklHALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQN 83
Cdd:PRK10522 310 EFPRPQafpdwqtLELRNVTFAYQDNG---FSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKP 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 84 IAELSHSELiqtRQRIGMIFQHFNLMSAKTVWENVALPlkvsnynkadiDQRVNEVLALVGLADK--------SNyypSQ 155
Cdd:PRK10522 387 VTAEQPEDY---RKLFSAVFTDFHLFDQLLGPEGKPAN-----------PALVEKWLERLKMAHKleledgriSN---LK 449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 156 LSGGQKQRVGIARALVHHPEILLCDEATSALDPESTATILALLKKINQELGLTIVLITHEMQVIrEICDQVVVIDQGEIV 235
Cdd:PRK10522 450 LSKGQKKRLALLLALAEERDILLLDEWAADQDPHFRREFYQVLLPLLQEMGKTIFAISHDDHYF-IHADRLLEMRNGQLS 528
|
.
gi 1194606020 236 E 236
Cdd:PRK10522 529 E 529
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
25-243 |
6.53e-13 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 69.53 E-value: 6.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 25 FYQSQGQKLHALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIhqqniaelshseliqtRQRIGMIFQ 104
Cdd:PRK13545 29 FRSKDGEYHYALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDI----------------KGSAALIAI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 105 HFNLMSAKTVWENVALPLKVSNYNKADIDQRVNEVLALVGLADKSNYYPSQLSGGQKQRVGIARALVHHPEILLCDEATS 184
Cdd:PRK13545 93 SSGLNGQLTGIENIELKGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALS 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1194606020 185 ALDPESTATIlalLKKINQ--ELGLTIVLITHEMQVIREICDQVVVIDQGEIVEAGQVWSV 243
Cdd:PRK13545 173 VGDQTFTKKC---LDKMNEfkEQGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEV 230
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
36-277 |
9.77e-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: 69.59 E-value: 9.77e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 36 LKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIhQQNIAELSHSELIQTrqrigmifqhfnlmsaKTVW 115
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHM-KGSVAYVPQQAWIQN----------------DSLR 716
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 116 ENVAL--PLKVSNYnkadidQRVNEVLALvgLADKSnYYPS-----------QLSGGQKQRVGIARALVHHPEILLCDEA 182
Cdd:TIGR00957 717 ENILFgkALNEKYY------QQVLEACAL--LPDLE-ILPSgdrteigekgvNLSGGQKQRVSLARAVYSNADIYLFDDP 787
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 183 TSALDPESTATIL-------ALLKkinqelGLTIVLITHEMQVIREIcDQVVVIDQGEIVEAGQVwsvfsrpeqqitQEL 255
Cdd:TIGR00957 788 LSAVDAHVGKHIFehvigpeGVLK------NKTRILVTHGISYLPQV-DVIIVMSGGKISEMGSY------------QEL 848
|
250 260
....*....|....*....|..
gi 1194606020 256 LNLEQITLPFKINPLPDEDSTH 277
Cdd:TIGR00957 849 LQRDGAFAEFLRTYAPDEQQGH 870
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
36-238 |
1.55e-12 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 69.04 E-value: 1.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 36 LKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQNIAELSHSELiqtRQRIGMIFQH---------- 105
Cdd:PTZ00243 1326 LRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLREL---RRQFSMIPQDpvlfdgtvrq 1402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 106 ----FNLMSAKTVW---ENVALPLKVSNYNKAdIDQRVnevlalvgLADKSNYypsqlSGGQKQRVGIARALVHHPE-IL 177
Cdd:PTZ00243 1403 nvdpFLEASSAEVWaalELVGLRERVASESEG-IDSRV--------LEGGSNY-----SVGQRQLMCMARALLKKGSgFI 1468
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1194606020 178 LCDEATSALDPestatilALLKKINQEL-----GLTIVLITHEMQVIREiCDQVVVIDQGEIVEAG 238
Cdd:PTZ00243 1469 LMDEATANIDP-------ALDRQIQATVmsafsAYTVITIAHRLHTVAQ-YDKIIVMDHGAVAEMG 1526
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
17-246 |
1.65e-12 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 66.86 E-value: 1.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 17 IKIRGLNKFYQSQGQKLhaLKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQNIAELSHSELiqtR 96
Cdd:cd03288 20 IKIHDLCVRYENNLKPV--LKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTL---R 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 97 QRIGMIFQHFNLMSAkTVWENVALPLKVSN---YNKADIDQRVNEVLALVGLADKSNYYPSQ-LSGGQKQRVGIARALVH 172
Cdd:cd03288 95 SRLSIILQDPILFSG-SIRFNLDPECKCTDdrlWEALEIAQLKNMVKSLPGGLDAVVTEGGEnFSVGQRQLFCLARAFVR 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1194606020 173 HPEILLCDEATSALDpesTATILALLKKINQELG-LTIVLITHEMQVIREiCDQVVVIDQGEIVEAGQVWSVFSR 246
Cdd:cd03288 174 KSSILIMDEATASID---MATENILQKVVMTAFAdRTVVTIAHRVSTILD-ADLVLVLSRGILVECDTPENLLAQ 244
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
17-240 |
2.25e-12 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 67.45 E-value: 2.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 17 IKIRGLNKFYQsqgqKLHALKEINLDIPQGKILGIIGKSGAG--KSSLLRTLNGLEQ-----------VNTGSIH--IHQ 81
Cdd:NF000106 14 VEVRGLVKHFG----EVKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*GPDAgrrpwrf*twcANRRALRrtIG* 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 82 QNIAELSHSELIQTRQRIGMIFQHFNLmsaktvwenvalplkvsnyNKADIDQRVNEVLALVGLADKSNYYPSQLSGGQK 161
Cdd:NF000106 90 HRPVR*GRRESFSGRENLYMIGR*LDL-------------------SRKDARARADELLERFSLTEAAGRAAAKYSGGMR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1194606020 162 QRVGIARALVHHPEILLCDEATSALDPESTATILALLKKINQElGLTIVLITHEMQVIREICDQVVVIDQGEIVEAGQV 240
Cdd:NF000106 151 RRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRD-GATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKV 228
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
15-238 |
2.36e-12 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 68.46 E-value: 2.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 15 PHIKIRGLNKFYQSQGQKlHALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGleqvntgsihihqqniaELSHSEL-- 92
Cdd:PLN03232 613 PAISIKNGYFSWDSKTSK-PTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLG-----------------ELSHAETss 674
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 93 IQTRQRIGMIFQHFNLMSAkTVWENValpLKVSNYNKadidQRVNEVLALVGLADKSNYYPSQ-----------LSGGQK 161
Cdd:PLN03232 675 VVIRGSVAYVPQVSWIFNA-TVRENI---LFGSDFES----ERYWRAIDVTALQHDLDLLPGRdlteigergvnISGGQK 746
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1194606020 162 QRVGIARALVHHPEILLCDEATSALDPESTATILAllKKINQEL-GLTIVLITHEMQVIREIcDQVVVIDQGEIVEAG 238
Cdd:PLN03232 747 QRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFD--SCMKDELkGKTRVLVTNQLHFLPLM-DRIILVSEGMIKEEG 821
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
28-281 |
5.87e-12 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 66.58 E-value: 5.87e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 28 SQGQ-KLHALKEINLD---IPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQNIAELShseLIQTRQRIGMIF 103
Cdd:PRK10938 7 SQGTfRLSDTKTLQLPsltLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLS---FEQLQKLVSDEW 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 104 QHFN--LMSA------KTVWENVAlplkvsnyNKADIDQRVNEVLALVGLADKSNYYPSQLSGGQKQRVGIARALVHHPE 175
Cdd:PRK10938 84 QRNNtdMLSPgeddtgRTTAEIIQ--------DEVKDPARCEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 176 ILLCDEATSALDPESTATILALLKKINQElGLTIVLITHEMQVIREICDQVVVIDQGEIVEAGqvwsvfsrPEQQITQEL 255
Cdd:PRK10938 156 LLILDEPFDGLDVASRQQLAELLASLHQS-GITLVLVLNRFDEIPDFVQFAGVLADCTLAETG--------EREEILQQA 226
|
250 260 270
....*....|....*....|....*....|....*...
gi 1194606020 256 L--------NLEQITLP----FKINPLPDEDSTHIIVK 281
Cdd:PRK10938 227 LvaqlahseQLEGVQLPepdePSARHALPANEPRIVLN 264
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
31-240 |
6.69e-12 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 64.66 E-value: 6.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 31 QKLHA-------LKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLE--QVNTGSIHIHQQNIAELSHSEliqtRQRIGm 101
Cdd:CHL00131 11 KNLHAsvneneiLKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPayKILEGDILFKGESILDLEPEE----RAHLG- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 102 IFQHFNLmsaktvweNVALPlKVSN--------------YNKADID-----QRVNEVLALVGLADK--SNYYPSQLSGGQ 160
Cdd:CHL00131 86 IFLAFQY--------PIEIP-GVSNadflrlaynskrkfQGLPELDpleflEIINEKLKLVGMDPSflSRNVNEGFSGGE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 161 KQRVGIARALVHHPEILLCDEATSALDPESTATIlalLKKINQELGLT--IVLITHEMQVIREIC-DQVVVIDQGEIVEA 237
Cdd:CHL00131 157 KKRNEILQMALLDSELAILDETDSGLDIDALKII---AEGINKLMTSEnsIILITHYQRLLDYIKpDYVHVMQNGKIIKT 233
|
...
gi 1194606020 238 GQV 240
Cdd:CHL00131 234 GDA 236
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
22-215 |
6.77e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 63.82 E-value: 6.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 22 LNKFYQSQgqklHALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQNIAElshsELIQTRQRIGM 101
Cdd:PRK13540 7 LDFDYHDQ----PLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKK----DLCTYQKQLCF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 102 IFQHFNLMSAKTVWENVALPLKVSNYNkadidQRVNEVLALVGLADKSNYYPSQLSGGQKQRVGIARALVHHPEILLCDE 181
Cdd:PRK13540 79 VGHRSGINPYLTLRENCLYDIHFSPGA-----VGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDE 153
|
170 180 190
....*....|....*....|....*....|....
gi 1194606020 182 ATSALDPESTATILALLKKiNQELGLTIVLITHE 215
Cdd:PRK13540 154 PLVALDELSLLTIITKIQE-HRAKGGAVLLTSHQ 186
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
16-230 |
3.74e-11 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 64.55 E-value: 3.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 16 HIKIRGLNKFYQSQGQKLhaLKEINLDIPQGKILGIIGKSGAGKSSLLRTLngLEQVNT-GSIHIHQQNIAELShseLIQ 94
Cdd:TIGR01271 1217 QMDVQGLTAKYTEAGRAV--LQDLSFSVEGGQRVGLLGRTGSGKSTLLSAL--LRLLSTeGEIQIDGVSWNSVT---LQT 1289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 95 TRQRIGMIFQHFNLMSAkTVWENVALPLKVSnynkadiDQRVNEVLALVGLADKSNYYPSQL-----------SGGQKQR 163
Cdd:TIGR01271 1290 WRKAFGVIPQKVFIFSG-TFRKNLDPYEQWS-------DEEIWKVAEEVGLKSVIEQFPDKLdfvlvdggyvlSNGHKQL 1361
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1194606020 164 VGIARALVHHPEILLCDEATSALDPESTATILALLKKINQElgLTIVLITHEMQVIREiCDQVVVID 230
Cdd:TIGR01271 1362 MCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSN--CTVILSEHRVEALLE-CQQFLVIE 1425
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
36-235 |
4.02e-11 |
|
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: 61.51 E-value: 4.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 36 LKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGL----EQVNtGSIH---IHQQNIAELSHSELIqtrqrigMIFQHFNL 108
Cdd:cd03233 23 LKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRtegnVSVE-GDIHyngIPYKEFAEKYPGEII-------YVSEEDVH 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 109 MSAKTVWENVALPLKVsnynkadidqrvnevlalvgladKSNYYPSQLSGGQKQRVGIARALVHHPEILLCDEATSALDP 188
Cdd:cd03233 95 FPTLTVRETLDFALRC-----------------------KGNEFVRGISGGERKRVSIAEALVSRASVLCWDNSTRGLDS 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1194606020 189 ESTATILALLKKINQELGLT-IVLITHEMQVIREICDQVVVIDQGEIV 235
Cdd:cd03233 152 STALEILKCIRTMADVLKTTtFVSLYQASDEIYDLFDKVLVLYEGRQI 199
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
38-234 |
4.06e-11 |
|
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: 64.08 E-value: 4.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 38 EINLDIPQGKILGIIGKSGAGKSSLLRTLNGL-EQVNTGSIHIHQQNIAELSHSELIqtRQRIGMI---FQHFNLMSAKT 113
Cdd:TIGR02633 278 DVSFSLRRGEILGVAGLVGAGRTELVQALFGAyPGKFEGNVFINGKPVDIRNPAQAI--RAGIAMVpedRKRHGIVPILG 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 114 VWENVALPL-----KVSNYNKADIDQRVNEVLALVGLADKSNYYP-SQLSGGQKQRVGIARALVHHPEILLCDEATSALD 187
Cdd:TIGR02633 356 VGKNITLSVlksfcFKMRIDAAAELQIIGSAIQRLKVKTASPFLPiGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVD 435
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1194606020 188 PESTATILALLKKINQElGLTIVLITHEMQVIREICDQVVVIDQGEI 234
Cdd:TIGR02633 436 VGAKYEIYKLINQLAQE-GVAIIVVSSELAEVLGLSDRVLVIGEGKL 481
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
17-234 |
4.09e-11 |
|
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: 62.95 E-value: 4.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 17 IKIRGLNKFYQSQGQKLhaLKEINLDIPQGKILGIIGKSGAGKSSLLRTLngLEQVNT-GSIHIHQQNIAELShseLIQT 95
Cdd:cd03289 3 MTVKDLTAKYTEGGNAV--LENISFSISPGQRVGLLGRTGSGKSTLLSAF--LRLLNTeGDIQIDGVSWNSVP---LQKW 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 96 RQRIGMIFQHFNLMSAktvwenvALPLKVSNYNKADiDQRVNEVLALVGLADKSNYYPSQL-----------SGGQKQRV 164
Cdd:cd03289 76 RKAFGVIPQKVFIFSG-------TFRKNLDPYGKWS-DEEIWKVAEEVGLKSVIEQFPGQLdfvlvdggcvlSHGHKQLM 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 165 GIARALVHHPEILLCDEATSALDPESTATILALLKKINQelGLTIVLITHEMQVIREiCDQVVVIDQGEI 234
Cdd:cd03289 148 CLARSVLSKAKILLLDEPSAHLDPITYQVIRKTLKQAFA--DCTVILSEHRIEAMLE-CQRFLVIEENKV 214
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
35-239 |
1.36e-10 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 62.44 E-value: 1.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 35 ALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQNIAELSHSELIQ------TRQR-----IGMIF 103
Cdd:PRK10982 263 SIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANEAINhgfalvTEERrstgiYAYLD 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 104 QHFNLMSAKTVWENVALPLKVSNYNKADIdQRVNEVLALVGLADKSNYypSQLSGGQKQRVGIARALVHHPEILLCDEAT 183
Cdd:PRK10982 343 IGFNSLISNIRNYKNKVGLLDNSRMKSDT-QWVIDSMRVKTPGHRTQI--GSLSGGNQQKVIIGRWLLTQPEILMLDEPT 419
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1194606020 184 SALDPESTATILALLKKINQElGLTIVLITHEMQVIREICDQVVVIDQGE---IVEAGQ 239
Cdd:PRK10982 420 RGIDVGAKFEIYQLIAELAKK-DKGIIIISSEMPELLGITDRILVMSNGLvagIVDTKT 477
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
39-189 |
2.68e-10 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 59.48 E-value: 2.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 39 INLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHqqniaelSHSELIQTRQRIGMIFQHFNLMSAK-TVWEN 117
Cdd:PRK13543 30 LDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQID-------GKTATRGDRSRFMAYLGHLPGLKADlSTLEN 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1194606020 118 VALPLKVSNYNKadiDQRVNEVLALVGLADKSNYYPSQLSGGQKQRVGIARALVHHPEILLCDEATSALDPE 189
Cdd:PRK13543 103 LHFLCGLHGRRA---KQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLE 171
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
32-247 |
2.86e-10 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 61.79 E-value: 2.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 32 KLHALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVN--TGSIHI-----HQQNIAELS--------HSELIQTR 96
Cdd:PLN03140 892 RLQLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTGGyiEGDIRIsgfpkKQETFARISgyceqndiHSPQVTVR 971
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 97 QriGMIFQHFnlmsaktvwenVALPLKVSNYNKADIDQRVNEVLALVGLADKSNYYP--SQLSGGQKQRVGIARALVHHP 174
Cdd:PLN03140 972 E--SLIYSAF-----------LRLPKEVSKEEKMMFVDEVMELVELDNLKDAIVGLPgvTGLSTEQRKRLTIAVELVANP 1038
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1194606020 175 EILLCDEATSALDPESTATILALLKKiNQELGLTIVLITHEMQV-IREICDQVVVIDQGeiveaGQVwsVFSRP 247
Cdd:PLN03140 1039 SIIFMDEPTSGLDARAAAIVMRTVRN-TVDTGRTVVCTIHQPSIdIFEAFDELLLMKRG-----GQV--IYSGP 1104
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
36-248 |
3.14e-10 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 60.23 E-value: 3.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 36 LKEINLDIPQGKILGIIGKSGAGKSSLLRTLNG--LEQVN------TGSIHIHQQNIAELSHSELIQTRQRIGMIFQHFN 107
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGdlTGGGAprgarvTGDVTLNGEPLAAIDAPRLARLRAVLPQAAQPAF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 108 LMSAKtvwENVALPLKVSNYNKADIDQRVNEV----LALVGLADKSNYYPSQLSGGQKQRVGIARALVH---------HP 174
Cdd:PRK13547 97 AFSAR---EIVLLGRYPHARRAGALTHRDGEIawqaLALAGATALVGRDVTTLSGGELARVQFARVLAQlwpphdaaqPP 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1194606020 175 EILLCDEATSALDPESTATILALLKKINQELGLTIVLITHEMQVIREICDQVVVIDQGEIVEAGQVWSVFsRPE 248
Cdd:PRK13547 174 RYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPADVL-TPA 246
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
29-249 |
5.01e-10 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 59.44 E-value: 5.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 29 QGQKLHALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQniaelshseliqtrqrIGMIFQHFNL 108
Cdd:PRK13546 33 KNKTFFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGE----------------VSVIAISAGL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 109 MSAKTVWENVALPLKVSNYNKADIDQRVNEVLALVGLADKSNYYPSQLSGGQKQRVGIARALVHHPEILLCDEATSALDP 188
Cdd:PRK13546 97 SGQLTGIENIEFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQ 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1194606020 189 ESTATILALLKKInQELGLTIVLITHEMQVIREICDQVVVIDQGEIVEAGQVWSVFSRPEQ 249
Cdd:PRK13546 177 TFAQKCLDKIYEF-KEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDVLPKYEA 236
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
45-234 |
5.45e-10 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 60.33 E-value: 5.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 45 QGKILGIIGKSGAGKSSLLRTLNGLEQ-VNTGSIHIHQQNIAELSHSELIqtRQRIGMIFQ---HFNLMSAKTVWENVAL 120
Cdd:PRK13549 287 RGEILGIAGLVGAGRTELVQCLFGAYPgRWEGEIFIDGKPVKIRNPQQAI--AQGIAMVPEdrkRDGIVPVMGVGKNITL 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 121 PL-----KVSNYNKADIDQRVNEVLALVGLADKSNYYP-SQLSGGQKQRVGIARALVHHPEILLCDEATSALDPESTATI 194
Cdd:PRK13549 365 AAldrftGGSRIDDAAELKTILESIQRLKVKTASPELAiARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEI 444
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1194606020 195 LALLKKINQElGLTIVLITHEMQVIREICDQVVVIDQGEI 234
Cdd:PRK13549 445 YKLINQLVQQ-GVAIIVISSELPEVLGLSDRVLVMHEGKL 483
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
20-215 |
9.11e-10 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 60.51 E-value: 9.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 20 RGLNKFYQSQGQKLHALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNglEQVNTGSIhihQQNIAELSHSELIQTRQR- 98
Cdd:TIGR00956 763 RNLTYEVKIKKEKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLA--ERVTTGVI---TGGDRLVNGRPLDSSFQRs 837
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 99 IGMIFQHFNLMSAKTVWENVA------LPLKVSNYNKADIDQRVNEVL-------ALVGLADksnyypSQLSGGQKQRVG 165
Cdd:TIGR00956 838 IGYVQQQDLHLPTSTVRESLRfsaylrQPKSVSKSEKMEYVEEVIKLLemesyadAVVGVPG------EGLNVEQRKRLT 911
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1194606020 166 IARALVHHPEILL-CDEATSALDPESTATILALLKKINQElGLTIVLITHE 215
Cdd:TIGR00956 912 IGVELVAKPKLLLfLDEPTSGLDSQTAWSICKLMRKLADH-GQAILCTIHQ 961
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
25-236 |
9.38e-10 |
|
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: 59.81 E-value: 9.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 25 FYQSQGQKLHALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIH-----IHQQNIAELshseliqtRQRI 99
Cdd:COG4615 337 YPGEDGDEGFTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILldgqpVTADNREAY--------RQLF 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 100 GMIFQHFNLMSaktvwenvalplKVSNYNKADIDQRVNEVLALVGLADK--------SNyypSQLSGGQKQRVGIARALV 171
Cdd:COG4615 409 SAVFSDFHLFD------------RLLGLDGEADPARARELLERLELDHKvsvedgrfST---TDLSQGQRKRLALLVALL 473
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1194606020 172 HHPEILLCDEATSALDPESTA----TILALLKKinqeLGLTIVLITHEMQVIrEICDQVVVIDQGEIVE 236
Cdd:COG4615 474 EDRPILVFDEWAADQDPEFRRvfytELLPELKA----RGKTVIAISHDDRYF-DLADRVLKMDYGKLVE 537
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
36-233 |
1.84e-09 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 57.94 E-value: 1.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 36 LKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGleqvntgsihihqqniaELSHSE-LIQTRQRIGMIFQhFNLMSAKTV 114
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILG-----------------ELEPSEgKIKHSGRISFSSQ-FSWIMPGTI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 115 WENVALPLKVSNYNKADIDQRVNEVLALVGLADKSNYYPSQ----LSGGQKQRVGIARALVHHPEILLCDEATSALDPES 190
Cdd:cd03291 115 KENIIFGVSYDEYRYKSVVKACQLEEDITKFPEKDNTVLGEggitLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFT 194
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1194606020 191 TATIL--ALLKKINQElglTIVLITHEMQVIReICDQVVVIDQGE 233
Cdd:cd03291 195 EKEIFesCVCKLMANK---TRILVTSKMEHLK-KADKILILHEGS 235
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
42-230 |
1.97e-09 |
|
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: 57.42 E-value: 1.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 42 DIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQNIA----ELSHSELIQTRQrigMIFQHFNLMSAKTVWEN 117
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSykpqYIKADYEGTVRD---LLSSITKDFYTHPYFKT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 118 -VALPLKVSNYnkadIDQRVNEvlalvgladksnyypsqLSGGQKQRVGIARALVHHPEILLCDEATSALDPESTATILA 196
Cdd:cd03237 98 eIAKPLQIEQI----LDREVPE-----------------LSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASK 156
|
170 180 190
....*....|....*....|....*....|....
gi 1194606020 197 LLKKINQELGLTIVLITHEMQVIREICDQVVVID 230
Cdd:cd03237 157 VIRRFAENNEKTAFVVEHDIIMIDYLADRLIVFE 190
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
4-238 |
4.03e-09 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 58.20 E-value: 4.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 4 VSFGSQVDFSLPHIKIRGLNKFYQS-QGQKLHALKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGleqvNTGSIHIHQQ 82
Cdd:TIGR00956 44 SDYQPTFPNALLKILTRGFRKLKKFrDTKTFDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIAS----NTDGFHIGVE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 83 N-IAELSHS-ELIQTRQRIGMIFQ-----HFNLMSAKTVWENVALPLKVSN-YNKADIDQRVNEV----LALVGLADKSN 150
Cdd:TIGR00956 120 GvITYDGITpEEIKKHYRGDVVYNaetdvHFPHLTVGETLDFAARCKTPQNrPDGVSREEYAKHIadvyMATYGLSHTRN 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 151 Y-----YPSQLSGGQKQRVGIARALVHHPEILLCDEATSALDPESTATILALLKKINQELGLT-IVLITHEMQVIREICD 224
Cdd:TIGR00956 200 TkvgndFVRGVSGGERKRVSIAEASLGGAKIQCWDNATRGLDSATALEFIRALKTSANILDTTpLVAIYQCSQDAYELFD 279
|
250
....*....|....
gi 1194606020 225 QVVVIDQGEIVEAG 238
Cdd:TIGR00956 280 KVIVLYEGYQIYFG 293
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
29-240 |
4.40e-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: 56.11 E-value: 4.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 29 QGQKLHALKEINLDIPQGKILGIIGKSGAGKSSL-------------LRTL-----NGLEQVN-------TG---SIHIH 80
Cdd:cd03270 4 RGAREHNLKNVDVDIPRNKLVVITGVSGSGKSSLafdtiyaegqrryVESLsayarQFLGQMDkpdvdsiEGlspAIAID 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 81 QQNIAELSHSeliqTRQRIGMIFQHFNLMsaktvwenvalplkvsnYNKADIDQRVNeVLALVGLADKSNYYPSQ-LSGG 159
Cdd:cd03270 84 QKTTSRNPRS----TVGTVTEIYDYLRLL-----------------FARVGIRERLG-FLVDVGLGYLTLSRSAPtLSGG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 160 QKQRVGIAR----ALVHHPEILlcDEATSALDPESTATILALLKKInQELGLTIVLITHEMQVIREiCDQVVVIDQGEIV 235
Cdd:cd03270 142 EAQRIRLATqigsGLTGVLYVL--DEPSIGLHPRDNDRLIETLKRL-RDLGNTVLVVEHDEDTIRA-ADHVIDIGPGAGV 217
|
....*
gi 1194606020 236 EAGQV 240
Cdd:cd03270 218 HGGEI 222
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
51-190 |
4.53e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 55.65 E-value: 4.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 51 IIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQNIAELShseliqtRQRIGMIFQHFNLMSAKTVWENVALPLKVsnYNKA 130
Cdd:PRK13541 31 IKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIA-------KPYCTYIGHNLGLKLEMTVFENLKFWSEI--YNSA 101
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 131 DIDQRVNEVLALVGLADKSNYypsQLSGGQKQRVGIARALVHHPEILLCDEATSALDPES 190
Cdd:PRK13541 102 ETLYAAIHYFKLHDLLDEKCY---SLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKEN 158
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
43-233 |
6.14e-09 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 57.51 E-value: 6.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 43 IPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSihihqqniaelshseliqtrqrigmifqhfnlmsaktvwenVALPL 122
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGE-----------------------------------------VDPEL 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 123 KVS---NYNKADIDQRVNEVLALVGLADKSNYYPSQ-----------------LSGGQKQRVGIARALVHHPEILLCDEA 182
Cdd:PRK13409 401 KISykpQYIKPDYDGTVEDLLRSITDDLGSSYYKSEiikplqlerlldknvkdLSGGELQRVAIAACLSRDADLYLLDEP 480
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1194606020 183 TSALDPESTATILALLKKINQELGLTIVLITHEMQVIREICDQVVVIDqGE 233
Cdd:PRK13409 481 SAHLDVEQRLAVAKAIRRIAEEREATALVVDHDIYMIDYISDRLMVFE-GE 530
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
45-221 |
1.24e-08 |
|
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: 53.53 E-value: 1.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 45 QGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIhqqniaelshseliqtrqrigmifqhfnlmsaktvwenvalpLKV 124
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIY------------------------------------------IDG 38
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 125 SNYNKADIDQRVNEVLALVGLadksnyypsQLSGGQKQRVGIARALVHHPEILLCDEATSALDPESTATILAL-----LK 199
Cdd:smart00382 39 EDILEEVLDQLLLIIVGGKKA---------SGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLeelrlLL 109
|
170 180
....*....|....*....|..
gi 1194606020 200 KINQELGLTIVLITHEMQVIRE 221
Cdd:smart00382 110 LLKSEKNLTVILTTNDEKDLGP 131
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
26-221 |
1.45e-08 |
|
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: 53.87 E-value: 1.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 26 YQSQGQKLHALKEINLDIPQGKILGIIGKSGAGKSSLLrtlngleqvntgsihihQQNIAELSHSELIQTRQRigmiFQH 105
Cdd:cd03238 1 LTVSGANVHNLQNLDVSIPLNVLVVVTGVSGSGKSTLV-----------------NEGLYASGKARLISFLPK----FSR 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 106 FNLMSaktvwenvalplkvsnynkadIDQRVNevLALVGLadksNYYP-----SQLSGGQKQRVGIARALVHHPE--ILL 178
Cdd:cd03238 60 NKLIF---------------------IDQLQF--LIDVGL----GYLTlgqklSTLSGGELQRVKLASELFSEPPgtLFI 112
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1194606020 179 CDEATSALDPESTATILALLKKINQeLGLTIVLITHEMQVIRE 221
Cdd:cd03238 113 LDEPSTGLHQQDINQLLEVIKGLID-LGNTVILIEHNLDVLSS 154
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
29-240 |
1.95e-08 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 55.69 E-value: 1.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 29 QGQKLHAlkEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQQNIAELSHSELIQT--------RQRIG 100
Cdd:PRK11288 264 KGPGLRE--PISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRDAIRAgimlcpedRKAEG 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 101 MIFQHfnlmsakTVWENVALPLKvSNYNKAD--IDQRVNEVLALVGLADKSNYYPS------QLSGGQKQRVGIARALVH 172
Cdd:PRK11288 342 IIPVH-------SVADNINISAR-RHHLRAGclINNRWEAENADRFIRSLNIKTPSreqlimNLSGGNQQKAILGRWLSE 413
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1194606020 173 HPEILLCDEATSALDPESTATILALLKKINQElGLTIVLITHEMQVIREICDQVVVIDQGEIveAGQV 240
Cdd:PRK11288 414 DMKVILLDEPTRGIDVGAKHEIYNVIYELAAQ-GVAVLFVSSDLPEVLGVADRIVVMREGRI--AGEL 478
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
40-229 |
3.09e-08 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 55.18 E-value: 3.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 40 NLDIPQ-GKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHihqqniAELSHSELIQtRQRIGMIFQHFNLMSAKTVweNV 118
Cdd:COG1245 92 GLPVPKkGKVTGILGPNGIGKSTALKILSGELKPNLGDYD------EEPSWDEVLK-RFRGTELQDYFKKLANGEI--KV 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 119 AL-PLKVSNYNKA----------DIDQR--VNEVLALVGLADKSNYYPSQLSGGQKQRVGIARALVHHPEILLCDEATSA 185
Cdd:COG1245 163 AHkPQYVDLIPKVfkgtvrelleKVDERgkLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSY 242
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1194606020 186 LDPESTATILALLKKINQElGLTIVLITHEMQVIREICDQVVVI 229
Cdd:COG1245 243 LDIYQRLNVARLIRELAEE-GKYVLVVEHDLAILDYLADYVHIL 285
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
21-229 |
4.96e-08 |
|
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: 53.52 E-value: 4.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 21 GLNKFyqsqgqKLHALKeinldIPQ-GKILGIIGKSGAGKSSLLRTLNGLEQVNTGSihiHQQN------IAELSHSELI 93
Cdd:cd03236 11 GPNSF------KLHRLP-----VPReGQVLGLVGPNGIGKSTALKILAGKLKPNLGK---FDDPpdwdeiLDEFRGSELQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 94 Q--TRQRIGMIF-----QHFNLMSaKTVWENVALPL-KVSNYNKADIdqrVNEVLALVGLADKSnyyPSQLSGGQKQRVG 165
Cdd:cd03236 77 NyfTKLLEGDVKvivkpQYVDLIP-KAVKGKVGELLkKKDERGKLDE---LVDQLELRHVLDRN---IDQLSGGELQRVA 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1194606020 166 IARALVHHPEILLCDEATSALDPESTATILALLKKINQElGLTIVLITHEMQVIREICDQVVVI 229
Cdd:cd03236 150 IAAALARDADFYFFDEPSSYLDIKQRLNAARLIRELAED-DNYVLVVEHDLAVLDYLSDYIHCL 212
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
42-233 |
7.51e-08 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 54.02 E-value: 7.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 42 DIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHihqqniaelshseliqtrqrigmifqhfnlmsaktvwenvaLP 121
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVD-----------------------------------------ED 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 122 LKVS---NYNKADIDQRVNEVLALVgLADK--SNYYPSQ-----------------LSGGQKQRVGIARALVHHPEILLC 179
Cdd:COG1245 401 LKISykpQYISPDYDGTVEEFLRSA-NTDDfgSSYYKTEiikplgleklldknvkdLSGGELQRVAIAACLSRDADLYLL 479
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1194606020 180 DEATSALDPESTATILALLKKINQELGLTIVLITHEMQVIREICDQVVVIDqGE 233
Cdd:COG1245 480 DEPSAHLDVEQRLAVAKAIRRFAENRGKTAMVVDHDIYLIDYISDRLMVFE-GE 532
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
36-232 |
1.26e-07 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 53.76 E-value: 1.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 36 LKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGleqvntgsihihqqniaELSHSE-LIQTRQRIGMIFQHFNLMSAkTV 114
Cdd:TIGR01271 442 LKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMG-----------------ELEPSEgKIKHSGRISFSPQTSWIMPG-TI 503
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 115 WENVALPLKVSNYNKADIDQ--RVNEVLALVGLADKSNYYPS--QLSGGQKQRVGIARALVHHPEILLCDEATSALDPES 190
Cdd:TIGR01271 504 KDNIIFGLSYDEYRYTSVIKacQLEEDIALFPEKDKTVLGEGgiTLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVT 583
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1194606020 191 TATIL--ALLKKINQElglTIVLITHEMQVIREiCDQVVVIDQG 232
Cdd:TIGR01271 584 EKEIFesCLCKLMSNK---TRILVTSKLEHLKK-ADKILLLHEG 623
|
|
| NIL |
smart00930 |
This domain is found at the C-terminus of ABC transporter proteins involved in D-methionine ... |
276-351 |
4.43e-07 |
|
This domain is found at the C-terminus of ABC transporter proteins involved in D-methionine transport as well as a number of ferredoxin-like proteins; This domain is likely to act as a substrate binding domain. The domain has been named after a conserved sequence in some members of the family.
Pssm-ID: 197998 [Multi-domain] Cd Length: 76 Bit Score: 46.73 E-value: 4.43e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1194606020 276 THIIVKLKYEAEAHQVPDIQELLARFKAPVNLYQSQVDTIQGHIIGSLLVGIPNVEIDLSSIQQDALTAIAQFEVL 351
Cdd:smart00930 1 DGRLVRLTFTGESADEPLISQLAREFGVDVNILHGNIERIQGGPFGSLVVELTGDEEDIEAALAYLREQGVEVEVL 76
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
36-256 |
6.92e-07 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 50.94 E-value: 6.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 36 LKEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLE--QVNTGSIHIHQQNIAELSHSELIQT--------RQRIGMifqh 105
Cdd:NF040905 276 VDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFGRSygRNISGTVFKDGKEVDVSTVSDAIDAglayvtedRKGYGL---- 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 106 fNLMsaKTVWENVALP----------------LKVSNYNKADIDQRVNEVLALVGladksnyypsQLSGGQKQRVGIARA 169
Cdd:NF040905 352 -NLI--DDIKRNITLAnlgkvsrrgvideneeIKVAEEYRKKMNIKTPSVFQKVG----------NLSGGNQQKVVLSKW 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 170 LVHHPEILLCDEATSALDPESTATILALlkkINQ--ELGLTIVLITHEMQVIREICDQVVVIDQGEIVeaGQVwsvfsrP 247
Cdd:NF040905 419 LFTDPDVLILDEPTRGIDVGAKYEIYTI---INElaAEGKGVIVISSELPELLGMCDRIYVMNEGRIT--GEL------P 487
|
....*....
gi 1194606020 248 EQQITQELL 256
Cdd:NF040905 488 REEASQERI 496
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
29-232 |
6.95e-07 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 49.92 E-value: 6.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 29 QGQKLHALKEINLDIPQGKILGIIGKSGAGKSSL--------LRTLNGLEQVNTGS-------------IHIHQQNIAEL 87
Cdd:cd03271 4 KGARENNLKNIDVDIPLGVLTCVTGVSGSGKSSLindtlypaLARRLHLKKEQPGNhdrieglehidkvIVIDQSPIGRT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 88 SHS---------ELIQ------------TRQRIGMIFQHFNL-----MS---AKTVWENVAlplKVSNYNKADIDqrvne 138
Cdd:cd03271 84 PRSnpatytgvfDEIRelfcevckgkryNRETLEVRYKGKSIadvldMTveeALEFFENIP---KIARKLQTLCD----- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 139 vlalVGLadksNYYP-----SQLSGGQKQRVGIARALVH---HPEILLCDEATSALDPESTATILALLKKInQELGLTIV 210
Cdd:cd03271 156 ----VGL----GYIKlgqpaTTLSGGEAQRIKLAKELSKrstGKTLYILDEPTTGLHFHDVKKLLEVLQRL-VDKGNTVV 226
|
250 260
....*....|....*....|..
gi 1194606020 211 LITHEMQVIReICDQvvVIDQG 232
Cdd:cd03271 227 VIEHNLDVIK-CADW--IIDLG 245
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
43-303 |
1.16e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 50.17 E-value: 1.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 43 IPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHIHQ--------QNIAELSHSEL---IQTRQRIGMIFQHFNLMSA 111
Cdd:PRK10636 24 INPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGnwqlawvnQETPALPQPALeyvIDGDREYRQLEAQLHDANE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 112 KTVWENVA-LPLKVSNYNKADIDQRVNEVLALVGLADKSNYYP-SQLSGGQKQRVGIARALVHHPEILLCDEATSALDPE 189
Cdd:PRK10636 104 RNDGHAIAtIHGKLDAIDAWTIRSRAASLLHGLGFSNEQLERPvSDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLDLD 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 190 STATILALLKKINQelglTIVLITHEMQVIREICDQVVVIDQGEIVEAGQVWSVFSRpeQQITQelLNLEQITlpfkinp 269
Cdd:PRK10636 184 AVIWLEKWLKSYQG----TLILISHDRDFLDPIVDKIIHIEQQSLFEYTGNYSSFEV--QRATR--LAQQQAM------- 248
|
250 260 270
....*....|....*....|....*....|....
gi 1194606020 270 lpdedsthiivklkYEAEAHQVPDIQELLARFKA 303
Cdd:PRK10636 249 --------------YESQQERVAHLQSYIDRFRA 268
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
50-234 |
1.51e-06 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 49.89 E-value: 1.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 50 GIIGKSGAGKSSLLRTLNG-LEQVNtGSIHIH-QQNIAELS------------------HSEL---IQTRQRI------- 99
Cdd:PRK15064 31 GLIGANGCGKSTFMKILGGdLEPSA-GNVSLDpNERLGKLRqdqfafeeftvldtvimgHTELwevKQERDRIyalpems 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 100 ---GMifqhfnlmsaktvweNVA-LPLKVSNYNKADIDQRVNEVLALVGLADKSNYYP-SQLSGGQKQRVGIARALVHHP 174
Cdd:PRK15064 110 eedGM---------------KVAdLEVKFAEMDGYTAEARAGELLLGVGIPEEQHYGLmSEVAPGWKLRVLLAQALFSNP 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 175 EILLCDEATSALDpesTATILALLKKINQElGLTIVLITHEMQVIREICDQVVVIDQGEI 234
Cdd:PRK15064 175 DILLLDEPTNNLD---INTIRWLEDVLNER-NSTMIIISHDRHFLNSVCTHMADLDYGEL 230
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
40-229 |
2.33e-06 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 49.42 E-value: 2.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 40 NLDIPQ-GKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHihqqniAELSHSELIQtRQRIGMIFQHFNLMSAKTVweNV 118
Cdd:PRK13409 92 GLPIPKeGKVTGILGPNGIGKTTAVKILSGELIPNLGDYE------EEPSWDEVLK-RFRGTELQNYFKKLYNGEI--KV 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 119 A--------LPlKVSNYNKADI----DQR-----VNEVLALVGLADKSnyyPSQLSGGQKQRVGIARALVHHPEILLCDE 181
Cdd:PRK13409 163 VhkpqyvdlIP-KVFKGKVRELlkkvDERgkldeVVERLGLENILDRD---ISELSGGELQRVAIAAALLRDADFYFFDE 238
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1194606020 182 ATSALDPESTATILALLKKINQelGLTIVLITHEMQVIREICDQVVVI 229
Cdd:PRK13409 239 PTSYLDIRQRLNVARLIRELAE--GKYVLVVEHDLAVLDYLADNVHIA 284
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
34-227 |
1.31e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 47.13 E-value: 1.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 34 HALKEINLDIPQGKILGIIGKSGAGKSSLLR-TL-----NGLEQVNTGSIHIHQQNIAELSH------------------ 89
Cdd:PRK00635 609 HNLKDLTISLPLGRLTVVTGVSGSGKSSLINdTLvpaveEFIEQGFCSNLSIQWGAISRLVHitrdlpgrsqrsipltyi 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 90 ------SELI--QTR-QRIGMIFQHFNL------------MSAKTVWEN----------------VALPLKVSNYNKADI 132
Cdd:PRK00635 689 kafddlRELFaeQPRsKRLGLTKSHFSFntplgacaecqgLGSITTTDNrtsipcpsclgkrflpQVLEVRYKGKNIADI 768
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 133 DQRV---------------NEVLALVGLAdkSNYYP-----SQLSGGQKQRVGIARAL---VHHPEILLCDEATSALDPE 189
Cdd:PRK00635 769 LEMTayeaekffldepsihEKIHALCSLG--LDYLPlgrplSSLSGGEIQRLKLAYELlapSKKPTLYVLDEPTTGLHTH 846
|
250 260 270
....*....|....*....|....*....|....*...
gi 1194606020 190 STATILALLKKINQElGLTIVLITHEMQVIReICDQVV 227
Cdd:PRK00635 847 DIKALIYVLQSLTHQ-GHTVVIIEHNMHVVK-VADYVL 882
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
42-248 |
1.33e-05 |
|
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: 45.26 E-value: 1.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 42 DIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTgsihihqqniaelshseliqtrqrigmifqhfnlmsaktvwENVALP 121
Cdd:cd03222 21 VVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNG-----------------------------------------DNDEWD 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 122 LKVSNYNKADIDqrvnevlalvgladksnyypsqLSGGQKQRVGIARALVHHPEILLCDEATSALDPESTATILALLKKI 201
Cdd:cd03222 60 GITPVYKPQYID----------------------LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRL 117
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1194606020 202 NQELGLTIVLITHEMQVIREICDQVVVIdQGEiveaGQVWSVFSRPE 248
Cdd:cd03222 118 SEEGKKTALVVEHDLAVLDYLSDRIHVF-EGE----PGVYGIASQPK 159
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
29-190 |
2.59e-05 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 46.04 E-value: 2.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 29 QGQKLH--AL---------------KEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIHihqqniaelsHSE 91
Cdd:PRK15064 311 QDKKLHrnALevenltkgfdngplfKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVK----------WSE 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 92 liqtRQRIGMIFQHfnlmSAKTVWENVALPLKVSNYNKA-DIDQRVNEVLA-LVGLADKSNYYPSQLSGGQKQRVGIARA 169
Cdd:PRK15064 381 ----NANIGYYAQD----HAYDFENDLTLFDWMSQWRQEgDDEQAVRGTLGrLLFSQDDIKKSVKVLSGGEKGRMLFGKL 452
|
170 180
....*....|....*....|.
gi 1194606020 170 LVHHPEILLCDEATSALDPES 190
Cdd:PRK15064 453 MMQKPNVLVMDEPTNHMDMES 473
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
134-188 |
2.81e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 45.78 E-value: 2.81e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1194606020 134 QRVNEVLALVGLADKSNYYPSQ-LSGGQKQRVGIARALVHHPEILLCDEATSALDP 188
Cdd:PRK10938 379 KLAQQWLDILGIDKRTADAPFHsLSWGQQRLALIVRALVKHPTLLILDEPLQGLDP 434
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
29-62 |
2.97e-05 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 46.16 E-value: 2.97e-05
10 20 30
....*....|....*....|....*....|....
gi 1194606020 29 QGQKLHALKEINLDIPQGKILGIIGKSGAGKSSL 62
Cdd:TIGR00630 5 RGAREHNLKNIDVEIPRDKLVVITGLSGSGKSSL 38
|
|
| NIL |
pfam09383 |
NIL domain; This domain is found at the C-terminus of ABC transporter proteins involved in ... |
279-328 |
3.33e-05 |
|
NIL domain; This domain is found at the C-terminus of ABC transporter proteins involved in D-methionine transport as well as a number of ferredoxin-like proteins. This domain is likely to act as a substrate binding domain. The domain has been named after a conserved sequence in some members of the family.
Pssm-ID: 462781 [Multi-domain] Cd Length: 73 Bit Score: 41.67 E-value: 3.33e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1194606020 279 IVKLKYEAEAHQVPDIQELLARFKAPVNLYQSQVDTIQGHIIGSLLVGIP 328
Cdd:pfam09383 2 LVRLTFPGESADEPVISRLAREFGVDVNILYGNIEEIQGTPFGSLILELP 51
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
37-234 |
3.62e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 45.62 E-value: 3.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 37 KEINLDIPQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSIhihqqniaelshseLIQTRQRIGMIFQH----FNLMSAK 112
Cdd:PLN03073 526 KNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTV--------------FRSAKVRMAVFSQHhvdgLDLSSNP 591
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 113 TVWENVALPlkvsnynkADIDQRVNEVLALVG----LADKSNYypsQLSGGQKQRVGIARALVHHPEILLCDEATSALDP 188
Cdd:PLN03073 592 LLYMMRCFP--------GVPEQKLRAHLGSFGvtgnLALQPMY---TLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDL 660
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1194606020 189 ESTATILallkkinQELGL---TIVLITHEMQVIREICDQVVVIDQGEI 234
Cdd:PLN03073 661 DAVEALI-------QGLVLfqgGVLMVSHDEHLISGSVDELWVVSEGKV 702
|
|
| SbcC_Walker_B |
pfam13558 |
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from ... |
154-200 |
4.08e-05 |
|
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from eukaryotes and the prokaryotic homolog SbcCD complex subunit C. RAD50-ATPase forms a complex with Mre11-nuclease that detects and processes diverse and obstructed DNA ends. This domain is separated of the Walker A domain by a long coiled-coil domain and forms the nucleotide-binding domain (NBD) when the coiled coils fold back on themselves and bring together Walker A and B domains. Two RAD50-NBDs forms heterotetramers with a Mre11 nuclease dimer that assemble as catalytic head module that binds and cleaves DNA in an ATP-dependent reaction. Through secondary structural analysis, it has been suggested that there is a wide structural conservation in the Rad50/SMC protein family as seen in structural similarities between RAD50's hook and ABC-ATPase MukB's elbow region.
Pssm-ID: 463921 [Multi-domain] Cd Length: 90 Bit Score: 41.84 E-value: 4.08e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 154 SQLSGGQKQ-------------RVGIARALVHHPEILLCDEATSALDPESTATILALLKK 200
Cdd:pfam13558 31 GGLSGGEKQllaylplaaalaaQYGSAEGRPPAPRLVFLDEAFAKLDEENIRTALELLRA 90
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
16-62 |
4.21e-05 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 45.40 E-value: 4.21e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1194606020 16 HIKIRGLnkfyqsqgqKLHALKEINLDIPQGKILGIIGKSGAGKSSL 62
Cdd:COG0178 5 KIRIRGA---------REHNLKNIDVDIPRNKLVVITGLSGSGKSSL 42
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
13-63 |
9.32e-05 |
|
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: 44.23 E-value: 9.32e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1194606020 13 SLPHIKIRGLNKFYQSQGQKLHALKEINLDIPQGKILGIIGKSGAGKSSLL 63
Cdd:TIGR00630 601 EVPAERRPGNGKFLTLKGARENNLKNITVSIPLGLFTCITGVSGSGKSTLI 651
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
16-62 |
1.06e-04 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 44.29 E-value: 1.06e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1194606020 16 HIKIRGlnkfyqsqgQKLHALKEINLDIPQGKILGIIGKSGAGKSSL 62
Cdd:PRK00349 5 KIIIRG---------AREHNLKNIDLDIPRDKLVVFTGLSGSGKSSL 42
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
46-187 |
2.41e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 42.92 E-value: 2.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 46 GKILGIIGKSGAGKSSLLR-----TLNGLEQvNTGSIHIHQQNIAELS---HSELIQTRQRIGMIFQHFNLMSAKTVWEN 117
Cdd:PLN03073 203 GRHYGLVGRNGTGKTTFLRymamhAIDGIPK-NCQILHVEQEVVGDDTtalQCVLNTDIERTQLLEEEAQLVAQQRELEF 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 118 VALPLKVSNYNKADID-----QRVNEVLA-----------------LVGL---ADKSNYYPSQLSGGQKQRVGIARALVH 172
Cdd:PLN03073 282 ETETGKGKGANKDGVDkdavsQRLEEIYKrlelidaytaearaasiLAGLsftPEMQVKATKTFSGGWRMRIALARALFI 361
|
170
....*....|....*
gi 1194606020 173 HPEILLCDEATSALD 187
Cdd:PLN03073 362 EPDLLLLDEPTNHLD 376
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
16-233 |
2.58e-04 |
|
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: 41.87 E-value: 2.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 16 HIKIRGLNKFYQSQgqklhalkEINL-DIPQGKILGIIGKSGAGKSSLL---------RTLNGLEQVNTGSIHIHQQNIA 85
Cdd:cd03279 5 KLELKNFGPFREEQ--------VIDFtGLDNNGLFLICGPTGAGKSTILdaityalygKTPRYGRQENLRSVFAPGEDTA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194606020 86 ELSHSelIQTRQRIGMIFQHFNLmsaktvwenvalplkvsnynkaDIDQRVNEVLALVGLADKSNYYP-SQLSGGQKQRV 164
Cdd:cd03279 77 EVSFT--FQLGGKKYRVERSRGL----------------------DYDQFTRIVLLPQGEFDRFLARPvSTLSGGETFLA 132
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1194606020 165 GIARAL-----VHHP-----EILLCDEATSALDPESTATILALLKKINQElGLTIVLITHeMQVIREICDQVVVIDQGE 233
Cdd:cd03279 133 SLSLALalsevLQNRggarlEALFIDEGFGTLDPEALEAVATALELIRTE-NRMVGVISH-VEELKERIPQRLEVIKTP 209
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
29-77 |
3.75e-04 |
|
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; YjeQ (YloQ in Bacillus subtilis) is a ribosomal small subunit-dependent GTPase; hence also known as RsgA. YjeQ is a late-stage ribosomal biogenesis factor involved in the 30S subunit maturation, and it represents a protein family whose members are broadly conserved in bacteria and have been shown to be essential to the growth of E. coli and B. subtilis. Proteins of the YjeQ family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. All YjeQ family proteins display a unique domain architecture, which includes an N-terminal OB-fold RNA-binding domain, the central permuted GTPase domain, and a zinc knuckle-like C-terminal cysteine domain.
Pssm-ID: 206747 [Multi-domain] Cd Length: 211 Bit Score: 41.23 E-value: 3.75e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1194606020 29 QGQKLHALKEInLdipQGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSI 77
Cdd:cd01854 72 TGEGLDELREL-L---KGKTSVLVGQSGVGKSTLLNALLPELVLATGEI 116
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
156-220 |
1.35e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 40.77 E-value: 1.35e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1194606020 156 LSGGQKQRVGIARAL---VHHPEILLCDEATSALDPESTATILALLKKInQELGLTIVLITHEMQVIR 220
Cdd:TIGR00630 830 LSGGEAQRIKLAKELskrSTGRTLYILDEPTTGLHFDDIKKLLEVLQRL-VDKGNTVVVIEHNLDVIK 896
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
155-219 |
1.39e-03 |
|
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: 38.88 E-value: 1.39e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1194606020 155 QLSGGQKQRVGIARALVHH---PEILLC-DEATSALDPESTATILALLKKINQELGLTIVlITHEMQVI 219
Cdd:cd03227 77 QLSGGEKELSALALILALAslkPRPLYIlDEIDRGLDPRDGQALAEAILEHLVKGAQVIV-ITHLPELA 144
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| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
15-63 |
2.51e-03 |
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excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 39.67 E-value: 2.51e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1194606020 15 PHIKIRGLNKFYQSQGQKLHALKEINLDIPQGKILGIIGKSGAGKSSLL 63
Cdd:PRK00349 604 PKERRKGNGKFLKLKGARENNLKNVDVEIPLGKFTCVTGVSGSGKSTLI 652
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| RsgA_GTPase |
pfam03193 |
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ... |
45-77 |
6.19e-03 |
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RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are broadly conserved in bacteria and are indispensable for growth. The GTPase domain of RsgA is very similar to several P-loop GTPases, but differs in having a circular permutation of the GTPase structure described by a G4-G1-G3 pattern.
Pssm-ID: 427191 [Multi-domain] Cd Length: 174 Bit Score: 37.14 E-value: 6.19e-03
10 20 30
....*....|....*....|....*....|...
gi 1194606020 45 QGKILGIIGKSGAGKSSLLRTLNGLEQVNTGSI 77
Cdd:pfam03193 105 KGKTTVLAGQSGVGKSTLLNALLPELDLRTGEI 137
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