|
Name |
Accession |
Description |
Interval |
E-value |
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
8-249 |
2.43e-122 |
|
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: 348.51 E-value: 2.43e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 8 PAEAVIEVRGLCNRFGPQSVHENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQNLPSLAEHERSLI 87
Cdd:COG1127 1 MSEPMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 88 ERRFGVLFQKGALFSSLTVTENVALPLIEHAGLSRADAEHLAAVKLALAGLPlSAADKYPASLSGGMIKraalaralalD 167
Cdd:COG1127 81 RRRIGMLFQGGALFDSLTVFENVAFPLREHTDLSEAEIRELVLEKLELVGLP-GAADKMPSELSGGMRKrvalaralalD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 168 PDILFLDEPTAGLDPIGAAAFDQLILTLRDALGLSVFLVTHDLDTLYTITDRVAVLAQKKVLVADAIDQVAETDDTWIHE 247
Cdd:COG1127 160 PEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLASDDPWVRQ 239
|
..
gi 1316494952 248 YF 249
Cdd:COG1127 240 FL 241
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
13-248 |
6.02e-105 |
|
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: 304.04 E-value: 6.02e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 13 IEVRGLCNRFGPQSVHENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQNLPSLAEHERSLIERRFG 92
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLRRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 93 VLFQKGALFSSLTVTENVALPLIEHAGLSRADAEHLAAVKLALAGLPlSAADKYPASLSGGMIKRAALARALALDPDILF 172
Cdd:cd03261 81 MLFQSGALFDSLTVFENVAFPLREHTRLSEEEIREIVLEKLEAVGLR-GAEDLYPAELSGGMKKRVALARALALDPELLL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1316494952 173 LDEPTAGLDPIGAAAFDQLILTLRDALGLSVFLVTHDLDTLYTITDRVAVLAQKKVLVADAIDQVAETDDTWIHEY 248
Cdd:cd03261 160 YDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRASDDPLVRQF 235
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
3-237 |
1.31e-53 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 181.25 E-value: 1.31e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 3 RSTRPPAEAVIEVRGLCNRF---GPQSVH--ENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQNLP 77
Cdd:COG1123 251 APAAAAAEPLLEVRNLSKRYpvrGKGGVRavDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLT 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 78 SLAEHERSLIERRFGVLFQ--KGALFSSLTVTENVALPLIEHAGLSRADAEHLAAVKLALAGLPLSAADKYPASLSGGMI 155
Cdd:COG1123 331 KLSRRSLRELRRRVQMVFQdpYSSLNPRMTVGDIIAEPLRLHGLLSRAERRERVAELLERVGLPPDLADRYPHELSGGQR 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 156 KRAALARALALDPDILFLDEPTAGLDPIGAAAFDQLILTLRDALGLSVFLVTHDLDTLYTITDRVAVLAQKKVLVADAID 235
Cdd:COG1123 411 QRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTE 490
|
..
gi 1316494952 236 QV 237
Cdd:COG1123 491 EV 492
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
12-223 |
1.46e-53 |
|
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: 173.08 E-value: 1.46e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 12 VIEVRGL----CNRFGPQSVHENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQNLPSLAEHERSLI 87
Cdd:cd03257 1 LLEVKNLsvsfPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 88 ERRFGVLFQK--GALFSSLTVTENVALPLIEHAGLSRADAEhLAAVKLALAGLPLSA--ADKYPASLSGGMIKRAALARA 163
Cdd:cd03257 81 RKEIQMVFQDpmSSLNPRMTIGEQIAEPLRIHGKLSKKEAR-KEAVLLLLVGVGLPEevLNRYPHELSGGQRQRVAIARA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 164 LALDPDILFLDEPTAGLDPIGAAAFDQLILTLRDALGLSVFLVTHDLDTLYTITDRVAVL 223
Cdd:cd03257 160 LALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVM 219
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
13-239 |
1.22e-52 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 171.01 E-value: 1.22e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 13 IEVRGLCNRFGPQSVHENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQNLPSLAEHERslieRRFG 92
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVR----RRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 93 VLFQKGALFSSLTVTENVALplieHA---GLSRADAEHLAAVKLALAGLPlSAADKYPASLSGGMIKRAALARALALDPD 169
Cdd:COG1131 77 YVPQEPALYPDLTVRENLRF----FArlyGLPRKEARERIDELLELFGLT-DAADRKVGTLSGGMKQRLGLALALLHDPE 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 170 ILFLDEPTAGLDPIGAAAFDQLILTLRDAlGLSVFLVTHDLDTLYTITDRVAVLAQKKVLVADAIDQVAE 239
Cdd:COG1131 152 LLILDEPTSGLDPEARRELWELLRELAAE-GKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKA 220
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
12-228 |
5.22e-52 |
|
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: 169.30 E-value: 5.22e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 12 VIEVRGLCNRFG--PQSVH--ENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQNLPSLAEHERSLI 87
Cdd:cd03258 1 MIELKNVSKVFGdtGGKVTalKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 88 ERRFGVLFQKGALFSSLTVTENVALPLiEHAGLSRADAEHLAAVKLALAGLPlSAADKYPASLSGGMIKRAALARALALD 167
Cdd:cd03258 81 RRRIGMIFQHFNLLSSRTVFENVALPL-EIAGVPKAEIEERVLELLELVGLE-DKADAYPAQLSGGQKQRVGIARALANN 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1316494952 168 PDILFLDEPTAGLDPIGAAAFDQLILTLRDALGLSVFLVTHDLDTLYTITDRVAVLAQKKV 228
Cdd:cd03258 159 PKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEV 219
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
13-223 |
2.16e-49 |
|
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: 162.26 E-value: 2.16e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 13 IEVRGLCNRFG----PQSVHENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQNLPSLAeherslie 88
Cdd:cd03293 1 LEVRNVSKTYGggggAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPG-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 89 RRFGVLFQKGALFSSLTVTENVALPLiEHAGLSRADAEHLAAVKLALAGLpLSAADKYPASLSGGMIKRAALARALALDP 168
Cdd:cd03293 73 PDRGYVFQQDALLPWLTVLDNVALGL-ELQGVPKAEARERAEELLELVGL-SGFENAYPHQLSGGMRQRVALARALAVDP 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1316494952 169 DILFLDEPTAGLDPIGAAAFDQLILTLRDALGLSVFLVTHDLDTLYTITDRVAVL 223
Cdd:cd03293 151 DVLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVL 205
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
13-228 |
6.85e-48 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 161.78 E-value: 6.85e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 13 IEVRGLCNRF--GPQSVH--ENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQNLPSLAEHERSLIE 88
Cdd:COG1135 2 IELENLSKTFptKGGPVTalDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRAAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 89 RRFGVLFQKGALFSSLTVTENVALPLiEHAGLSRADAEHLAAVKLALAGLPlSAADKYPASLSGG------------Mik 156
Cdd:COG1135 82 RKIGMIFQHFNLLSSRTVAENVALPL-EIAGVPKAEIRKRVAELLELVGLS-DKADAYPSQLSGGqkqrvgiaralaN-- 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1316494952 157 raalaralalDPDILFLDEPTAGLDPIGAAAFDQLILTLRDALGLSVFLVTHDLDTLYTITDRVAVLAQKKV 228
Cdd:COG1135 158 ----------NPKVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRICDRVAVLENGRI 219
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
7-224 |
1.69e-47 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 158.71 E-value: 1.69e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 7 PPAEAVIEVRGLCNRF----GPQSVHENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQNLPSLAeh 82
Cdd:COG1116 2 SAAAPALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPG-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 83 erslieRRFGVLFQKGALFSSLTVTENVALPLiEHAGLSRADAEHLAAVKLALAGLpLSAADKYPASLSGGM-------- 154
Cdd:COG1116 80 ------PDRGVVFQEPALLPWLTVLDNVALGL-ELRGVPKAERRERARELLELVGL-AGFEDAYPHQLSGGMrqrvaiar 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1316494952 155 --IkraalaralaLDPDILFLDEPTAGLDPIGAAAFDQLILTLRDALGLSVFLVTHDLD-TLYtITDRVAVLA 224
Cdd:COG1116 152 alA----------NDPEVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDeAVF-LADRVVVLS 213
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
10-220 |
1.21e-46 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 155.20 E-value: 1.21e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 10 EAVIEVRGLCNRF--GPQSVH--ENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQNLPSLAEHERS 85
Cdd:COG1136 2 SPLLELRNLTKSYgtGEGEVTalRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 86 LIERR-FGVLFQKGALFSSLTVTENVALPLIeHAGLSRADAEHLAAVKLALAGLPlSAADKYPASLSGG----------M 154
Cdd:COG1136 82 RLRRRhIGFVFQFFNLLPELTALENVALPLL-LAGVSRKERRERARELLERVGLG-DRLDHRPSQLSGGqqqrvaiaraL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1316494952 155 IKraalaralalDPDILFLDEPTAGLDPIGAAAFDQLILTLRDALGLSVFLVTHDLDtLYTITDRV 220
Cdd:COG1136 160 VN----------RPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPE-LAARADRV 214
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
13-229 |
1.97e-46 |
|
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: 154.21 E-value: 1.97e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 13 IEVRGLCNRFGPQSVHENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQNLPSLAEHERslierRFG 92
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPERR-----NIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 93 VLFQKGALFSSLTVTENVALPLiEHAGLSRADAEhlAAVKLALAGLPLSA-ADKYPASLSGGMIKRAALARALALDPDIL 171
Cdd:cd03259 76 MVFQDYALFPHLTVAENIAFGL-KLRGVPKAEIR--ARVRELLELVGLEGlLNRYPHELSGGQQQRVALARALAREPSLL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1316494952 172 FLDEPTAGLDPIGAAAFDQLILTLRDALGLSVFLVTHDLDTLYTITDRVAVLAQKKVL 229
Cdd:cd03259 153 LLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIV 210
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
14-227 |
3.61e-46 |
|
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: 153.78 E-value: 3.61e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 14 EVRGLCNRFGPQSVH--ENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQNLPSLAEHERSlieRRF 91
Cdd:cd03225 1 ELKNLSFSYPDGARPalDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELR---RKV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 92 GVLFQKGAL-FSSLTVTENVALPLiEHAGLSRADAEhlAAVKLALAGLPLSA-ADKYPASLSGGMIKRAALARALALDPD 169
Cdd:cd03225 78 GLVFQNPDDqFFGPTVEEEVAFGL-ENLGLPEEEIE--ERVEEALELVGLEGlRDRSPFTLSGGQKQRVAIAGVLAMDPD 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1316494952 170 ILFLDEPTAGLDPIGAAAFDQLILTLRDAlGLSVFLVTHDLDTLYTITDRVAVLAQKK 227
Cdd:cd03225 155 ILLLDEPTAGLDPAGRRELLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
13-225 |
6.29e-46 |
|
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: 151.96 E-value: 6.29e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 13 IEVRGLCNRFGPQSVHENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQNLPSLaEHERSLIERRFG 92
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDL-EDELPPLRRRIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 93 VLFQKGALFSSLTVTENVALPLiehaglsradaehlaavklalaglplsaadkypaslSGGMIKRAALARALALDPDILF 172
Cdd:cd03229 80 MVFQDFALFPHLTVLENIALGL------------------------------------SGGQQQRVALARALAMDPDVLL 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1316494952 173 LDEPTAGLDPIGAAAFDQLILTLRDALGLSVFLVTHDLDTLYTITDRVAVLAQ 225
Cdd:cd03229 124 LDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRD 176
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
13-228 |
1.01e-45 |
|
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: 151.01 E-value: 1.01e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 13 IEVRGLCNRFGPQSVHENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQNLPSlaehERSLIERRFG 92
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK----EPEEVKRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 93 VLFQKGALFSSLTVTENValpliehaglsradaehlaavklalaglplsaadkypaSLSGGMIKRAALARALALDPDILF 172
Cdd:cd03230 77 YLPEEPSLYENLTVRENL--------------------------------------KLSGGMKQRLALAQALLHDPELLI 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1316494952 173 LDEPTAGLDPIGAAAFDQLILTLRDAlGLSVFLVTHDLDTLYTITDRVAVLAQKKV 228
Cdd:cd03230 119 LDEPTSGLDPESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
13-228 |
1.35e-45 |
|
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: 152.26 E-value: 1.35e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 13 IEVRGLCNRFGPQSVH----ENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQNLPSLAEHERSLIE 88
Cdd:cd03255 1 IELKNLSKTYGGGGEKvqalKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 89 RR-FGVLFQKGALFSSLTVTENVALPLIeHAGLSRADAEHLAAVKLALAGLPlSAADKYPASLSGGMIKRAALARALALD 167
Cdd:cd03255 81 RRhIGFVFQSFNLLPDLTALENVELPLL-LAGVPKKERRERAEELLERVGLG-DRLNHYPSELSGGQQQRVAIARALAND 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1316494952 168 PDILFLDEPTAGLDPIGAAAFDQLILTLRDALGLSVFLVTHDLDtLYTITDRVAVLAQKKV 228
Cdd:cd03255 159 PKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPE-LAEYADRIIELRDGKI 218
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
9-251 |
2.62e-45 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 153.38 E-value: 2.62e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 9 AEAVIEVRGLCNRFGPQSVHENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQNLPSLAEHERSLIE 88
Cdd:PRK11831 4 VANLVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTVR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 89 RRFGVLFQKGALFSSLTVTENVALPLIEHAGLSRADAEHLAAVKLALAGLPlSAADKYPASLSGGMIKRAALARALALDP 168
Cdd:PRK11831 84 KRMSMLFQSGALFTDMNVFDNVAYPLREHTQLPAPLLHSTVMMKLEAVGLR-GAAKLMPSELSGGMARRAALARAIALEP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 169 DILFLDEPTAGLDPIGAAAFDQLILTLRDALGLSVFLVTHDLDTLYTITDRVAVLAQKKVLVADAIDQVAETDDTWIHEY 248
Cdd:PRK11831 163 DLIMFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQANPDPRVRQF 242
|
...
gi 1316494952 249 FHG 251
Cdd:PRK11831 243 LDG 245
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
10-237 |
2.58e-44 |
|
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: 156.60 E-value: 2.58e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 10 EAVIEVRGLCNRFGPQSVH--ENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPS---EGSVRVFGQNLPSLAEHER 84
Cdd:COG1123 2 TPLLEVRDLSVRYPGGDVPavDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 85 SlieRRFGVLFQK-GALFSSLTVTENVALPLiEHAGLSRADAEHLAAVKLALAGLPlSAADKYPASLSGGMIKRAALARA 163
Cdd:COG1123 82 G---RRIGMVFQDpMTQLNPVTVGDQIAEAL-ENLGLSRAEARARVLELLEAVGLE-RRLDRYPHQLSGGQRQRVAIAMA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1316494952 164 LALDPDILFLDEPTAGLDPIGAAAFDQLILTLRDALGLSVFLVTHDLDTLYTITDRVAVLAQKKVLVADAIDQV 237
Cdd:COG1123 157 LALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEI 230
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
12-237 |
4.42e-44 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 148.99 E-value: 4.42e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 12 VIEVRGLCNRFGPQSVHENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQNLpSLAEHERSLIERRF 91
Cdd:COG1126 1 MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDL-TDSKKDINKLRRKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 92 GVLFQKGALFSSLTVTENVALPLIEHAGLSRADAEHLAAVKLALAGLpLSAADKYPASLSGG------------Mikraa 159
Cdd:COG1126 80 GMVFQQFNLFPHLTVLENVTLAPIKVKKMSKAEAEERAMELLERVGL-ADKADAYPAQLSGGqqqrvaiaralaM----- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 160 laralalDPDILFLDEPTAGLDPigaaafdQLI---L-TLRD--ALGLSVFLVTHDLDTLYTITDRVAVLAQKKVLVADA 233
Cdd:COG1126 154 -------EPKVMLFDEPTSALDP-------ELVgevLdVMRDlaKEGMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGP 219
|
....
gi 1316494952 234 IDQV 237
Cdd:COG1126 220 PEEF 223
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
9-229 |
5.52e-43 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 149.48 E-value: 5.52e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 9 AEAVIEVRGLCNRFGPQSVHENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQNLPSLAEHersliE 88
Cdd:COG3842 2 AMPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPE-----K 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 89 RRFGVLFQKGALFSSLTVTENVALPLiEHAGLSRADAEHLAAVKLALAGLPlSAADKYPASLSGG----------MIKra 158
Cdd:COG3842 77 RNVGMVFQDYALFPHLTVAENVAFGL-RMRGVPKAEIRARVAELLELVGLE-GLADRYPHQLSGGqqqrvalaraLAP-- 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1316494952 159 alaralalDPDILFLDEPTAGLDPIGAAAFDQLILTLRDALGLSVFLVTHDLDTLYTITDRVAVLAQKKVL 229
Cdd:COG3842 153 --------EPRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIE 215
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
13-237 |
6.60e-43 |
|
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: 145.94 E-value: 6.60e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 13 IEVRGLCNRFGPQS-VHENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQNLpslAEHERSLIERRF 91
Cdd:COG1122 1 IELENLSFSYPGGTpALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDI---TKKNLRELRRKV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 92 GVLFQKGA--LFSSlTVTENVALPLiEHAGLSRADAEhlAAVKLALAGLPLSA-ADKYPASLSGG------------Mik 156
Cdd:COG1122 78 GLVFQNPDdqLFAP-TVEEDVAFGP-ENLGLPREEIR--ERVEEALELVGLEHlADRPPHELSGGqkqrvaiagvlaM-- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 157 raalaralalDPDILFLDEPTAGLDPIGAAAFDQLILTLRDAlGLSVFLVTHDLDTLYTITDRVAVLAQKKVLVADAIDQ 236
Cdd:COG1122 152 ----------EPEVLVLDEPTAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPRE 220
|
.
gi 1316494952 237 V 237
Cdd:COG1122 221 V 221
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
13-225 |
1.81e-42 |
|
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: 144.21 E-value: 1.81e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 13 IEVRGLCNRFGPQSVHENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQNLPSlAEHERSLIERRFG 92
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTD-DKKNINELRQKVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 93 VLFQKGALFSSLTVTENVALPLIEHAGLSRADAEHLAAVKLALAGLpLSAADKYPASLSGGMIKRAALARALALDPDILF 172
Cdd:cd03262 80 MVFQQFNLFPHLTVLENITLAPIKVKGMSKAEAEERALELLEKVGL-ADKADAYPAQLSGGQQQRVAIARALAMNPKVML 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1316494952 173 LDEPTAGLDPigaaafdQLILTLRDAL------GLSVFLVTHDLDTLYTITDRVAVLAQ 225
Cdd:cd03262 159 FDEPTSALDP-------ELVGEVLDVMkdlaeeGMTMVVVTHEMGFAREVADRVIFMDD 210
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
12-223 |
2.90e-42 |
|
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: 146.74 E-value: 2.90e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 12 VIEVRGLCNRF--GPQSVH--ENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQP---SEGSVRVFGQNLPSLAEHE- 83
Cdd:COG0444 1 LLEVRNLKVYFptRRGVVKavDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKEl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 84 RSLIERRFGVLFQkgALFSSL----TVTENVALPLIEHAGLSRADAEHLAAVKLALAGLPLSA--ADKYPASLSGGM--- 154
Cdd:COG0444 81 RKIRGREIQMIFQ--DPMTSLnpvmTVGDQIAEPLRIHGGLSKAEARERAIELLERVGLPDPErrLDRYPHELSGGMrqr 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1316494952 155 -------IkraalaralaLDPDILFLDEPTAGLDPIGAAAFDQLILTLRDALGLSVFLVTHDLDTLYTITDRVAVL 223
Cdd:COG0444 159 vmiaralA----------LEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVM 224
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
30-229 |
1.06e-40 |
|
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: 141.24 E-value: 1.06e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 30 NLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQNLPSLAEHE-RSLIERRFGVLFQKGALFSSLTVTE 108
Cdd:cd03294 42 DVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKElRELRRKKISMVFQSFALLPHRTVLE 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 109 NVALPLiEHAGLSRADAEHLAAVKLALAGLpLSAADKYPASLSGGMIKRAALARALALDPDILFLDEPTAGLDPIGAAAF 188
Cdd:cd03294 122 NVAFGL-EVQGVPRAEREERAAEALELVGL-EGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREM 199
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1316494952 189 DQLILTLRDALGLSVFLVTHDLDTLYTITDRVAVLAQKKVL 229
Cdd:cd03294 200 QDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLV 240
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
13-223 |
1.68e-40 |
|
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: 139.62 E-value: 1.68e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 13 IEVRGLCNRFGPQSVHENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLR-----QPSEGSVRVFGQNLPSLAEhERSLI 87
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNdlipgAPDEGEVLLDGKDIYDLDV-DVLEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 88 ERRFGVLFQKGALFSsLTVTENVALPLIEHAGLSRADAEHLAAVKLALAGLPLSAADKYPA-SLSGGMIKRAALARALAL 166
Cdd:cd03260 80 RRRVGMVFQKPNPFP-GSIYDNVAYGLRLHGIKLKEELDERVEEALRKAALWDEVKDRLHAlGLSGGQQQRLCLARALAN 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1316494952 167 DPDILFLDEPTAGLDPIGAAAFDQLILTLRDAlgLSVFLVTHDLDTLYTITDRVAVL 223
Cdd:cd03260 159 EPEVLLLDEPTSALDPISTAKIEELIAELKKE--YTIVIVTHNMQQAARVADRTAFL 213
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
9-237 |
1.95e-40 |
|
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: 140.17 E-value: 1.95e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 9 AEAVIEVRGLCNRFGpqSVH--ENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQNLPSLAEHERSl 86
Cdd:COG0411 1 SDPLLEVRGLTKRFG--GLVavDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIA- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 87 ierRFGVL--FQKGALFSSLTVTENVALPLIEHAGLS------------RADAEHLAAVK--LALAGLpLSAADKYPASL 150
Cdd:COG0411 78 ---RLGIArtFQNPRLFPELTVLENVLVAAHARLGRGllaallrlprarREEREARERAEelLERVGL-ADRADEPAGNL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 151 SGGMIKRAALARALALDPDILFLDEPTAGLDPIGAAAFDQLILTLRDALGLSVFLVTHDLDTLYTITDRVAVLAQKKVLV 230
Cdd:COG0411 154 SYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFGRVIA 233
|
....*..
gi 1316494952 231 ADAIDQV 237
Cdd:COG0411 234 EGTPAEV 240
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
13-238 |
1.11e-38 |
|
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: 134.87 E-value: 1.11e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 13 IEVRGLCNRFGPQSVHENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQNLPSLAEHERSlierRFG 92
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIA----RLG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 93 VL--FQKGALFSSLTVTENVALPLIEHAGLS-------RADAEHLAAVKLALAGLPLSA-ADKYPASLSGGMIKRAALAR 162
Cdd:cd03219 77 IGrtFQIPRLFPELTVLENVMVAAQARTGSGlllararREEREARERAEELLERVGLADlADRPAGELSYGQQRRLEIAR 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1316494952 163 ALALDPDILFLDEPTAGLDPIGAAAFDQLILTLRDAlGLSVFLVTHDLDTLYTITDRVAVLAQKKVLVADAIDQVA 238
Cdd:cd03219 157 ALATDPKLLLLDEPAAGLNPEETEELAELIRELRER-GITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVR 231
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
13-237 |
8.28e-38 |
|
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: 133.19 E-value: 8.28e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 13 IEVRGLCNRF-GPQSVHENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQNLPSLAEHErslIERRF 91
Cdd:cd03295 1 IEFENVTKRYgGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVE---LRRKI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 92 GVLFQKGALFSSLTVTENVAL-PLIEhaGLSRADAEHLAAVKLALAGL-PLSAADKYPASLSGGMIKRAALARALALDPD 169
Cdd:cd03295 78 GYVIQQIGLFPHMTVEENIALvPKLL--KWPKEKIRERADELLALVGLdPAEFADRYPHELSGGQQQRVGVARALAADPP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1316494952 170 ILFLDEPTAGLDPIGAAAFDQLILTLRDALGLSVFLVTHDLDTLYTITDRVAVLAQKKVLVADAIDQV 237
Cdd:cd03295 156 LLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEI 223
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
8-228 |
9.13e-38 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 132.91 E-value: 9.13e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 8 PAEAVIEVRGLCNRFGPQSVHENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQNLpslaEHERSLI 87
Cdd:COG1121 2 MMMPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPP----RRARRRI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 88 errfGVLFQKGALFSS--LTVTENVALPLIEHAGL-SRADAEHLAAVKLALA--GLpLSAADKYPASLSGG--------- 153
Cdd:COG1121 78 ----GYVPQRAEVDWDfpITVRDVVLMGRYGRRGLfRRPSRADREAVDEALErvGL-EDLADRPIGELSGGqqqrvllar 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1316494952 154 -MIKraalaralalDPDILFLDEPTAGLDPIGAAAFDQLILTLRDAlGLSVFLVTHDLDTLYTITDRVAVLAQKKV 228
Cdd:COG1121 153 aLAQ----------DPDLLLLDEPFAGVDAATEEALYELLRELRRE-GKTILVVTHDLGAVREYFDRVLLLNRGLV 217
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
13-225 |
1.55e-37 |
|
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: 132.62 E-value: 1.55e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 13 IEVRGLCNRFGPQSVH----ENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQNLPSLAEHERSlie 88
Cdd:COG1124 2 LEVRNLSVSYGQGGRRvpvlKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFR--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 89 RRFGVLFQ--KGALFSSLTVTENVALPLIEHaGLSRADAEhlAAVKLALAGLPLSAADKYPASLSGG----------MIk 156
Cdd:COG1124 79 RRVQMVFQdpYASLHPRHTVDRILAEPLRIH-GLPDREER--IAELLEQVGLPPSFLDRYPHQLSGGqrqrvaiaraLI- 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1316494952 157 raalaralaLDPDILFLDEPTAGLDPIGAAAFDQLILTLRDALGLSVFLVTHDLDTLYTITDRVAVLAQ 225
Cdd:COG1124 155 ---------LEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQN 214
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
30-228 |
1.56e-37 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 131.71 E-value: 1.56e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 30 NLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQNLPSLAEHERSLIERRFGVLFQKGALFSSLTVTEN 109
Cdd:COG2884 20 DVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYLRRRIGVVFQDFRLLPDRTVYEN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 110 VALPLiEHAGLSRADAEHLAAVKLALAGLpLSAADKYPASLSGG----------MIKraalaralalDPDILFLDEPTAG 179
Cdd:COG2884 100 VALPL-RVTGKSRKEIRRRVREVLDLVGL-SDKAKALPHELSGGeqqrvaiaraLVN----------RPELLLADEPTGN 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1316494952 180 LDPIGAAAFDQLILTLRdALGLSVFLVTHDLDTLYTITDRVAVLAQKKV 228
Cdd:COG2884 168 LDPETSWEIMELLEEIN-RRGTTVLIATHDLELVDRMPKRVLELEDGRL 215
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
12-228 |
3.04e-37 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 134.16 E-value: 3.04e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 12 VIEVRGLCNRF--GPQSVH--ENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQNLPSLAEHERSLI 87
Cdd:PRK11153 1 MIELKNISKVFpqGGRTIHalNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 88 ERRFGVLFQKGALFSSLTVTENVALPLiEHAGLSRADAEHLAAVKLALAGlpLSA-ADKYPASLSGGMIKRAALARALAL 166
Cdd:PRK11153 81 RRQIGMIFQHFNLLSSRTVFDNVALPL-ELAGTPKAEIKARVTELLELVG--LSDkADRYPAQLSGGQKQRVAIARALAS 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1316494952 167 DPDILFLDEPTAGLDPigaaAFDQLILTL-----RDaLGLSVFLVTHDLDTLYTITDRVAVLAQKKV 228
Cdd:PRK11153 158 NPKVLLCDEATSALDP----ATTRSILELlkdinRE-LGLTIVLITHEMDVVKRICDRVAVIDAGRL 219
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
7-210 |
8.26e-37 |
|
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: 130.25 E-value: 8.26e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 7 PPAEAVIEVRGLCNRF----GPQSVHENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQNLPSLAEH 82
Cdd:COG4181 3 SSSAPIIELRGLTKTVgtgaGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDED 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 83 ERSLIERR-FGVLFQKGALFSSLTVTENVALPLiEHAGlsRADAEHLAAVKLALAGLPlSAADKYPASLSGG-----MIk 156
Cdd:COG4181 83 ARARLRARhVGFVFQSFQLLPTLTALENVMLPL-ELAG--RRDARARARALLERVGLG-HRLDHYPAQLSGGeqqrvAL- 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1316494952 157 raalARALALDPDILFLDEPTAGLDPIGAAAFDQLILTLRDALGLSVFLVTHDL 210
Cdd:COG4181 158 ----ARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDP 207
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
12-237 |
1.16e-36 |
|
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: 130.16 E-value: 1.16e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 12 VIEVRGLCNRFGPQSVHENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQNLPSLAEHERSlieRRF 91
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELA---RRI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 92 GVLFQKGALFSSLTVTENVALPLIEHAG-LSRADAEHLAAVKLALAGLPLSA-ADKYPASLSGG-----MIkraalaral 164
Cdd:COG1120 78 AYVPQEPPAPFGLTVRELVALGRYPHLGlFGRPSAEDREAVEEALERTGLEHlADRPVDELSGGerqrvLIara-----l 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1316494952 165 alDPDILFLDEPTAGLDPIGAAAFDQLILTLRDALGLSVFLVTHDLDTLYTITDRVAVLAQKKVLVADAIDQV 237
Cdd:COG1120 153 aqEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEV 225
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
13-228 |
1.66e-36 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 128.78 E-value: 1.66e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 13 IEVRGLCNRFGPQSVHENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQNLPSLAEHErslIERRFG 92
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPE---WRRQVA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 93 VLFQKGALFSSlTVTENVALPL-IEHAGLSRADAEHLaavkLALAGLPLSAADKYPASLSGG---------MIkraalar 162
Cdd:COG4619 78 YVPQEPALWGG-TVRDNLPFPFqLRERKFDRERALEL----LERLGLPPDILDKPVERLSGGerqrlalirAL------- 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1316494952 163 alALDPDILFLDEPTAGLDPIGAAAFDQLILTLRDALGLSVFLVTHDLDTLYTITDRVAVLAQKKV 228
Cdd:COG4619 146 --LLQPDVLLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
13-228 |
2.30e-36 |
|
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ATP-binding protein is found in a number of genomes in operon-like contexts strongly suggesting a substrate specificity for 2-aminoethylphosphonate (2-AEP). The characterized PhnSTUV system is absent in the genomes in which this system is found. These genomes encode systems for the catabolism of 2-AEP, making the need for a 2-AEP-specific transporter likely. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274496 [Multi-domain] Cd Length: 353 Bit Score: 132.08 E-value: 2.30e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 13 IEVRGLCNRFGPQSVHENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQ---NLPSLAeherslieR 89
Cdd:TIGR03265 5 LSIDNIRKRFGAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRditRLPPQK--------R 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 90 RFGVLFQKGALFSSLTVTENVALPLiEHAGLSRADAEHLAAVKLALAGLPlSAADKYPASLSGGMIKRAALARALALDPD 169
Cdd:TIGR03265 77 DYGIVFQSYALFPNLTVADNIAYGL-KNRGMGRAEVAERVAELLDLVGLP-GSERKYPGQLSGGQQQRVALARALATSPG 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1316494952 170 ILFLDEPTAGLDPIGAAAFDQLILTLRDALGLSVFLVTHDLDTLYTITDRVAVLAQKKV 228
Cdd:TIGR03265 155 LLLLDEPLSALDARVREHLRTEIRQLQRRLGVTTIMVTHDQEEALSMADRIVVMNHGVI 213
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
13-228 |
3.85e-36 |
|
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: 128.51 E-value: 3.85e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 13 IEVRGLCNRFGPQSVHENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQNLPSLAEHersliERRFG 92
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPH-----KRPVN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 93 VLFQKGALFSSLTVTENVALPLiEHAGLSRADAEHLAAVKLALAGLpLSAADKYPASLSGGMIKRAALARALALDPDILF 172
Cdd:cd03300 76 TVFQNYALFPHLTVFENIAFGL-RLKKLPKAEIKERVAEALDLVQL-EGYANRKPSQLSGGQQQRVAIARALVNEPKVLL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1316494952 173 LDEPTAGLDPigaaafdQL-------ILTLRDALGLSVFLVTHDLDTLYTITDRVAVLAQKKV 228
Cdd:cd03300 154 LDEPLGALDL-------KLrkdmqleLKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKI 209
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
12-223 |
8.91e-36 |
|
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ABC transporter family (pfam00005). LolD is involved in localization of lipoproteins in some bacteria. It works with a transmembrane protein LolC, which in some species is a paralogous pair LolC and LolE. Depending on whether the residue immediately following the new, modified N-terminal Cys residue, the nascent lipoprotein may be carried further by LolA and LolB to the outer membrane, or remain at the inner membrane. The top scoring proteins excluded by this model include homologs from the archaeal genus Methanosarcina. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 131266 [Multi-domain] Cd Length: 221 Bit Score: 127.08 E-value: 8.91e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 12 VIEVRGLCNRFGPQS----VHENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQNLPSLAEHERS-L 86
Cdd:TIGR02211 1 LLKCENLGKRYQEGKldtrVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSSNERAkL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 87 IERRFGVLFQKGALFSSLTVTENVALPLIEhAGLSRADAEHLAAVKLALAGLPlSAADKYPASLSGGMIKRAALARALAL 166
Cdd:TIGR02211 81 RNKKLGFIYQFHHLLPDFTALENVAMPLLI-GKKSVKEAKERAYEMLEKVGLE-HRINHRPSELSGGERQRVAIARALVN 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1316494952 167 DPDILFLDEPTAGLDPIGAAAFDQLILTLRDALGLSVFLVTHDLdTLYTITDRVAVL 223
Cdd:TIGR02211 159 QPSLVLADEPTGNLDNNNAKIIFDLMLELNRELNTSFLVVTHDL-ELAKKLDRVLEM 214
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
29-229 |
1.59e-35 |
|
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: 127.95 E-value: 1.59e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 29 ENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQNLPSLAEHERSLIERRFGVLFQ--KGALFSsLTV 106
Cdd:TIGR04521 22 DDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKLKDLRKKVGLVFQfpEHQLFE-ETV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 107 TENVAL-PLieHAGLSRADAEHLAAVKLALAGLPLSAADKYPASLSGGMIKRAALARALALDPDILFLDEPTAGLDPIGA 185
Cdd:TIGR04521 101 YKDIAFgPK--NLGLSEEEAEERVKEALELVGLDEEYLERSPFELSGGQMRRVAIAGVLAMEPEVLILDEPTAGLDPKGR 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1316494952 186 AAFDQLILTLRDALGLSVFLVTHDLDTLYTITDRVAVLAQKKVL 229
Cdd:TIGR04521 179 KEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIV 222
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
13-229 |
2.27e-35 |
|
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: 126.08 E-value: 2.27e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 13 IEVRGLCNRFGPQSVH--ENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQNLPSlaehERSLIERR 90
Cdd:cd03263 1 LQIRNLTKTYKKGTKPavDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT----DRKAARQS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 91 FGVLFQKGALFSSLTVTENVALplieHA---GLSRADAEHLAAVKLALAGLpLSAADKYPASLSGGMIKRAALARALALD 167
Cdd:cd03263 77 LGYCPQFDALFDELTVREHLRF----YArlkGLPKSEIKEEVELLLRVLGL-TDKANKRARTLSGGMKRKLSLAIALIGG 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1316494952 168 PDILFLDEPTAGLDPIGAAAFDQLILTLRDalGLSVFLVTHDLDTLYTITDRVAVLAQKKVL 229
Cdd:cd03263 152 PSVLLLDEPTSGLDPASRRAIWDLILEVRK--GRSIILTTHSMDEAEALCDRIAIMSDGKLR 211
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
13-242 |
2.96e-35 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 129.11 E-value: 2.96e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 13 IEVRGLCNRFGPQSVHENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQNLPSlaehERSLIERRFG 92
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFT----NLPPRERRVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 93 VLFQKGALFSSLTVTENVALPLiEHAGLSRADA-----EHLAAVKLAlaGLplsaADKYPASLSGG---------MIkra 158
Cdd:COG1118 79 FVFQHYALFPHMTVAENIAFGL-RVRPPSKAEIrarveELLELVQLE--GL----ADRYPSQLSGGqrqrvalarAL--- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 159 alaralALDPDILFLDEPTAGLDpigAAAFDQLILTLR---DALGLSVFLVTHDLDTLYTITDRVAVLAQKKvlvadaID 235
Cdd:COG1118 149 ------AVEPEVLLLDEPFGALD---AKVRKELRRWLRrlhDELGGTTVFVTHDQEEALELADRVVVMNQGR------IE 213
|
....*..
gi 1316494952 236 QVAETDD 242
Cdd:COG1118 214 QVGTPDE 220
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
14-228 |
7.48e-35 |
|
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: 124.57 E-value: 7.48e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 14 EVRGLCNRFGPQSVHENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQNlpslAEHERSLIerrfGV 93
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKP----LEKERKRI----GY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 94 LFQKGALFSS--LTVTENVALPLIEHAGL-SRADAEHLAAVKLALAGLPLSA-ADKYPASLSGGMIKRAALARALALDPD 169
Cdd:cd03235 73 VPQRRSIDRDfpISVRDVVLMGLYGHKGLfRRLSKADKAKVDEALERVGLSElADRQIGELSGGQQQRVLLARALVQDPD 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1316494952 170 ILFLDEPTAGLDPIGAAAFDQLILTLRDaLGLSVFLVTHDLDTLYTITDRVAVLAQKKV 228
Cdd:cd03235 153 LLLLDEPFAGVDPKTQEDIYELLRELRR-EGMTILVVTHDLGLVLEYFDRVLLLNRTVV 210
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
12-210 |
1.87e-34 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 124.43 E-value: 1.87e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 12 VIEVRGLCNRFGPQSVHENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQNLPSLAEHERsLIERRF 91
Cdd:PRK09493 1 MIEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDER-LIRQEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 92 GVLFQKGALFSSLTVTENVALPLIEHAGLSRADAEHLAAVKLALAGLPlSAADKYPASLSGGMIKRAALARALALDPDIL 171
Cdd:PRK09493 80 GMVFQQFYLFPHLTALENVMFGPLRVRGASKEEAEKQARELLAKVGLA-ERAHHYPSELSGGQQQRVAIARALAVKPKLM 158
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1316494952 172 FLDEPTAGLDPigaaAFDQLILTLRDAL---GLSVFLVTHDL 210
Cdd:PRK09493 159 LFDEPTSALDP----ELRHEVLKVMQDLaeeGMTMVIVTHEI 196
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
13-236 |
3.15e-34 |
|
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: 123.25 E-value: 3.15e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 13 IEVRGLCNRFGPQSVHENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQNLPSlaehERSLIERRFG 92
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR----EPREVRRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 93 VLFQKGALFSSLTVTENVALplieHA---GLSRADAEHLAAVKLALAGLpLSAADKYPASLSGGMIKRAALARALALDPD 169
Cdd:cd03265 77 IVFQDLSVDDELTGWENLYI----HArlyGVPGAERRERIDELLDFVGL-LEAADRLVKTYSGGMRRRLEIARSLVHRPE 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1316494952 170 ILFLDEPTAGLDPIGAAAFDQLILTLRDALGLSVFLVTHDLDTLYTITDRVAVLAQKKVLVADAIDQ 236
Cdd:cd03265 152 VLFLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEE 218
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
12-239 |
3.98e-34 |
|
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: 123.43 E-value: 3.98e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 12 VIEVRGLCNRFGPQSVHENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQNlpslAEHERSLIERRF 91
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGED----VRKEPREARRQI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 92 GVLFQKGALFSSLTVTENVALpLIEHAGLSRADAEHLAAVKLALAGLPlSAADKYPASLSGGMIKRAALARALALDPDIL 171
Cdd:COG4555 77 GVLPDERGLYDRLTVRENIRY-FAELYGLFDEELKKRIEELIELLGLE-EFLDRRVGELSTGMKKKVALARALVHDPKVL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1316494952 172 FLDEPTAGLDPIGAAAFDQLILTLRDaLGLSVFLVTHDLDTLYTITDRVAVLAQKKVLVADAIDQVAE 239
Cdd:COG4555 155 LLDEPTNGLDVMARRLLREILRALKK-EGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELRE 221
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
31-234 |
8.23e-34 |
|
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: 124.04 E-value: 8.23e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 31 LDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQNLPSLAEHERslieRRFGVLFQKGALFSSLTVTENV 110
Cdd:TIGR01188 12 VNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVVREPRKVR----RSIGIVPQYASVDEDLTGRENL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 111 ALplieHA---GLSRADAEHLAAVKLALAGLpLSAADKYPASLSGGMIKRAALARALALDPDILFLDEPTAGLDPIGAAA 187
Cdd:TIGR01188 88 EM----MGrlyGLPKDEAEERAEELLELFEL-GEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPRTRRA 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1316494952 188 FDQLILTLRDAlGLSVFLVTHDLDTLYTITDRVAVLAQKKVLVADAI 234
Cdd:TIGR01188 163 IWDYIRALKEE-GVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTP 208
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
13-246 |
1.33e-33 |
|
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: 122.06 E-value: 1.33e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 13 IEVRGLCNRFGPQSVHENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQNLPSlaeheRSLIERRFG 92
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATD-----VPVQERNVG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 93 VLFQKGALFSSLTVTENVALPLIEHAGLSRADAEHLAA-VKLALAGLPLSA-ADKYPASLSGGMIKRAALARALALDPDI 170
Cdd:cd03296 78 FVFQHYALFRHMTVFDNVAFGLRVKPRSERPPEAEIRAkVHELLKLVQLDWlADRYPAQLSGGQRQRVALARALAVEPKV 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1316494952 171 LFLDEPTAGLDpigAAAFDQLILTLR---DALGLSVFLVTHDLDTLYTITDRVAVLAQKKvlvadaIDQVAETDDTWIH 246
Cdd:cd03296 158 LLLDEPFGALD---AKVRKELRRWLRrlhDELHVTTVFVTHDQEEALEVADRVVVMNKGR------IEQVGTPDEVYDH 227
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
13-229 |
9.87e-33 |
|
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: 118.86 E-value: 9.87e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 13 IEVRGLCNRFGPQSVHENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQNLPSLAEherslIERRFG 92
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIE-----ALRRIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 93 VLFQKGALFSSLTVTENVALPLIEHaGLSRADAEHLaavkLALAGLPlSAADKYPASLSGGMIKRAALARALALDPDILF 172
Cdd:cd03268 76 ALIEAPGFYPNLTARENLRLLARLL-GIRKKRIDEV----LDVVGLK-DSAKKKVKGFSLGMKQRLGIALALLGNPDLLI 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1316494952 173 LDEPTAGLDPIGAAAFDQLILTLRDAlGLSVFLVTHDLDTLYTITDRVAVLAQKKVL 229
Cdd:cd03268 150 LDEPTNGLDPDGIKELRELILSLRDQ-GITVLISSHLLSEIQKVADRIGIINKGKLI 205
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
10-223 |
1.01e-32 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 122.90 E-value: 1.01e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 10 EAVIEVRGLCNRFGPQS-------------------------VHeNLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQP 64
Cdd:COG4175 1 MPKIEVRNLYKIFGKRPeralklldqgkskdeilektgqtvgVN-DASFDVEEGEIFVIMGLSGSGKSTLVRCLNRLIEP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 65 SEGSVRVFGQNLPSLAEHErsLIE---RRFGVLFQKGALFSSLTVTENVALPLiEHAGLSRADAEHLAAVKLALAGLpLS 141
Cdd:COG4175 80 TAGEVLIDGEDITKLSKKE--LRElrrKKMSMVFQHFALLPHRTVLENVAFGL-EIQGVPKAERRERAREALELVGL-AG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 142 AADKYPASLSGGMikraalaralaLDPDILFLDEPTAGLDPigaaafdqLI--------LTLRDALGLSVFLVTHDLDTL 213
Cdd:COG4175 156 WEDSYPDELSGGMqqrvglaralaTDPDILLMDEAFSALDP--------LIrremqdelLELQAKLKKTIVFITHDLDEA 227
|
250
....*....|
gi 1316494952 214 YTITDRVAVL 223
Cdd:COG4175 228 LRLGDRIAIM 237
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
30-223 |
1.87e-32 |
|
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Functionally, this transport system is involved in osmoregulation. Under conditions of stress, the organism recruits these transport system to accumulate glycine betaine and other solutes which offer osmo-protection. It has been demonstrated that glycine betaine uptake is accompanied by symport with sodium ions. The locus has been named variously as proU or opuA. A gene library from L.lactis functionally complements an E.coli proU mutant. The comlementing locus is similar to a opuA locus in B.sutlis. This clarifies the differences in nomenclature. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 130254 [Multi-domain] Cd Length: 363 Bit Score: 121.88 E-value: 1.87e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 30 NLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQNLPSLAEHE-RSLIERRFGVLFQKGALFSSLTVTE 108
Cdd:TIGR01186 11 DADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEPTAGQIFIDGENIMKQSPVElREVRRKKIGMVFQQFALFPHMTILQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 109 NVALPLiEHAGLSRADAEHLAAVKLALAGLPlSAADKYPASLSGGMIKRAALARALALDPDILFLDEPTAGLDPIGAAAF 188
Cdd:TIGR01186 91 NTSLGP-ELLGWPEQERKEKALELLKLVGLE-EYEHRYPDELSGGMQQRVGLARALAAEPDILLMDEAFSALDPLIRDSM 168
|
170 180 190
....*....|....*....|....*....|....*
gi 1316494952 189 DQLILTLRDALGLSVFLVTHDLDTLYTITDRVAVL 223
Cdd:TIGR01186 169 QDELKKLQATLQKTIVFITHDLDEAIRIGDRIVIM 203
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
11-213 |
2.34e-32 |
|
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: 117.58 E-value: 2.34e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 11 AVIEVRGLCNRFGPQSVHENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQNLPSLAEHERslieRR 90
Cdd:COG4133 1 MMLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYR----RR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 91 FGVLFQKGALFSSLTVTENVALpLIEHAGLSRADAEHLAAvkLALAGLPlSAADKYPASLSGGMIKRAALARALALDPDI 170
Cdd:COG4133 77 LAYLGHADGLKPELTVRENLRF-WAALYGLRADREAIDEA--LEAVGLA-GLADLPVRQLSAGQKRRVALARLLLSPAPL 152
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1316494952 171 LFLDEPTAGLDPIGAAAFDQLILTLRDAlGLSVFLVTHDLDTL 213
Cdd:COG4133 153 WLLDEPFTALDAAGVALLAELIAAHLAR-GGAVLLTTHQPLEL 194
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
13-244 |
3.15e-32 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 120.96 E-value: 3.15e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 13 IEVRGLCNRFGPQSVHENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQNLPSLaeHERsliERRFG 92
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRL--HAR---DRKVG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 93 VLFQKGALFSSLTVTENVALPLiehAGLSRADAEHLAAVKLALAGL----PLS-AADKYPASLSGGMIKRAALARALALD 167
Cdd:PRK10851 78 FVFQHYALFRHMTVFDNIAFGL---TVLPRRERPNAAAIKAKVTQLlemvQLAhLADRYPAQLSGGQKQRVALARALAVE 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1316494952 168 PDILFLDEPTAGLDPIGAAAFDQLILTLRDALGL-SVFlVTHDLDTLYTITDRVAVLAQKKvlvadaIDQVAETDDTW 244
Cdd:PRK10851 155 PQILLLDEPFGALDAQVRKELRRWLRQLHEELKFtSVF-VTHDQEEAMEVADRVVVMSQGN------IEQAGTPDQVW 225
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
9-228 |
4.30e-32 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 118.53 E-value: 4.30e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 9 AEAVIEVRGLCNRFGPQSVHENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQN----------LPS 78
Cdd:PRK10619 2 SENKLNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTinlvrdkdgqLKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 79 LAEHERSLIERRFGVLFQKGALFSSLTVTENVALPLIEHAGLSRADAEHLAAVKLALAGLPLSAADKYPASLSGGMIKRA 158
Cdd:PRK10619 82 ADKNQLRLLRTRLTMVFQHFNLWSHMTVLENVMEAPIQVLGLSKQEARERAVKYLAKVGIDERAQGKYPVHLSGGQQQRV 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 159 ALARALALDPDILFLDEPTAGLDPIGAAAFDQLILTLRDAlGLSVFLVTHDLDTLYTITDRVAVLAQKKV 228
Cdd:PRK10619 162 SIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEE-GKTMVVVTHEMGFARHVSSHVIFLHQGKI 230
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
11-223 |
1.33e-31 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 117.60 E-value: 1.33e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 11 AVIEVRGLCNRF---------GPQSVHENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQNLPSLAE 81
Cdd:TIGR02769 1 SLLEVRDVTHTYrtgglfgakQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 82 HERSLIERRFGVLFQK--GALFSSLTVTENVALPLIEHAGLSRADAEHLAAVKLALAGLPLSAADKYPASLSGGMIKRAA 159
Cdd:TIGR02769 81 KQRRAFRRDVQLVFQDspSAVNPRMTVRQIIGEPLRHLTSLDESEQKARIAELLDMVGLRSEDADKLPRQLSGGQLQRIN 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1316494952 160 LARALALDPDILFLDEPTAGLDPIGAAAFDQLILTLRDALGLSVFLVTHDLDTLYTITDRVAVL 223
Cdd:TIGR02769 161 IARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVM 224
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
9-237 |
1.90e-31 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 116.63 E-value: 1.90e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 9 AEAVIEVRGLCNRFGPQSVHENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQNLPSLAEHERSlie 88
Cdd:PRK11300 2 SQPLLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIA--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 89 rRFGVL--FQKGALFSSLTVTENvaLPLIEH--------AGL------SRADAEHL--AAVKLALAGLpLSAADKYPASL 150
Cdd:PRK11300 79 -RMGVVrtFQHVRLFREMTVIEN--LLVAQHqqlktglfSGLlktpafRRAESEALdrAATWLERVGL-LEHANRQAGNL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 151 SGGMIKRAALARALALDPDILFLDEPTAGLDPIGAAAFDQLILTLRDALGLSVFLVTHDLDTLYTITDRVAVLAQKKVLV 230
Cdd:PRK11300 155 AYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLA 234
|
....*..
gi 1316494952 231 ADAIDQV 237
Cdd:PRK11300 235 NGTPEEI 241
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
29-178 |
1.93e-31 |
|
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: 113.51 E-value: 1.93e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 29 ENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQNLPSLaehERSLIERRFGVLFQKGALFSSLTVTE 108
Cdd:pfam00005 2 KNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDD---ERKSLRKEIGYVFQDPQLFPRLTVRE 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1316494952 109 NVALPLIEHAGLSRADAEHLAAV--KLALAGLPLSAADKYPASLSGGMIKRAALARALALDPDILFLDEPTA 178
Cdd:pfam00005 79 NLRLGLLLKGLSKREKDARAEEAleKLGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
11-229 |
4.00e-31 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 118.25 E-value: 4.00e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 11 AVIEVRGLCNRFGPQSVHENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQNLPSLAEHersliERR 90
Cdd:COG3839 2 ASLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPK-----DRN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 91 FGVLFQKGALFSSLTVTENVALPLiEHAGLSRADAEhlAAVKLALAGLPLSA-ADKYPASLSGG----------MIKraa 159
Cdd:COG3839 77 IAMVFQSYALYPHMTVYENIAFPL-KLRKVPKAEID--RRVREAAELLGLEDlLDRKPKQLSGGqrqrvalgraLVR--- 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1316494952 160 laralalDPDILFLDEPTAGLDpigAAAFDQLILTLRD---ALGLSVFLVTHDLDTLYTITDRVAVLAQKKVL 229
Cdd:COG3839 151 -------EPKVFLLDEPLSNLD---AKLRVEMRAEIKRlhrRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQ 213
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
11-211 |
4.73e-31 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 115.73 E-value: 4.73e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 11 AVIEVRGLCNRFG----PQSVHENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQNL--PSlaeher 84
Cdd:COG4525 2 SMLTVRHVSVRYPgggqPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVtgPG------ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 85 slIERrfGVLFQKGALFSSLTVTENVALPLiEHAGLSRADAEHLAAVKLALAGLPlSAADKYPASLSGGMIKRAALARAL 164
Cdd:COG4525 76 --ADR--GVVFQKDALLPWLNVLDNVAFGL-RLRGVPKAERRARAEELLALVGLA-DFARRRIWQLSGGMRQRVGIARAL 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1316494952 165 ALDPDILFLDEPTAGLDPIGAAAFDQLILTLRDALGLSVFLVTHDLD 211
Cdd:COG4525 150 AADPRFLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHSVE 196
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
13-236 |
1.40e-30 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 113.70 E-value: 1.40e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 13 IEVRGLCNRFGPQSVHenLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQNLPSLAEHERSlierrFG 92
Cdd:COG3840 2 LRLDDLTYRYGDFPLR--FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAERP-----VS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 93 VLFQKGALFSSLTVTENVALPLieHAGLSRADAEHL----AAVKLALAGLplsaADKYPASLSGG----------MIKra 158
Cdd:COG3840 75 MLFQENNLFPHLTVAQNIGLGL--RPGLKLTAEQRAqveqALERVGLAGL----LDRLPGQLSGGqrqrvalarcLVR-- 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1316494952 159 alaralalDPDILFLDEPTAGLDPIGAAAFDQLILTLRDALGLSVFLVTHDLDTLYTITDRVAVLAQKKVLVADAIDQ 236
Cdd:COG3840 147 --------KRPILLLDEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAA 216
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
7-237 |
1.81e-30 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 114.25 E-value: 1.81e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 7 PPAEAVIEVRGLCNRFGPQSVHENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQ-----NLPSLAE 81
Cdd:PRK11701 1 MMDQPLLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRdgqlrDLYALSE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 82 HERSLIER-RFGVLFQKGA--LFSSLTVTENVALPLI----EHAGLSRADAEH-LAAVKLALAGLplsaaDKYPASLSGG 153
Cdd:PRK11701 81 AERRRLLRtEWGFVHQHPRdgLRMQVSAGGNIGERLMavgaRHYGDIRATAGDwLERVEIDAARI-----DDLPTTFSGG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 154 MIKRAALARALALDPDILFLDEPTAGLDPIGAAAFDQLILTLRDALGLSVFLVTHDLDTLYTITDRVAVLAQKKVLVADA 233
Cdd:PRK11701 156 MQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVVESGL 235
|
....
gi 1316494952 234 IDQV 237
Cdd:PRK11701 236 TDQV 239
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
13-229 |
1.87e-30 |
|
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: 114.45 E-value: 1.87e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 13 IEVRGLCNRFGPQSVH--ENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQNlpSLAEHERSLIERR 90
Cdd:TIGR04520 1 IEVENVSFSYPESEKPalKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLD--TLDEENLWEIRKK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 91 FGVLFQK------GAlfsslTVTENVALPLiEHAGLSRADAEHLAAVKLALAGLpLSAADKYPASLSGG----------- 153
Cdd:TIGR04520 79 VGMVFQNpdnqfvGA-----TVEDDVAFGL-ENLGVPREEMRKRVDEALKLVGM-EDFRDREPHLLSGGqkqrvaiagvl 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1316494952 154 -MikraalaralalDPDILFLDEPTAGLDPIGAAAFDQLILTLRDALGLSVFLVTHDLDTLyTITDRVAVLAQKKVL 229
Cdd:TIGR04520 152 aM------------RPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEA-VLADRVIVMNKGKIV 215
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
13-228 |
2.08e-30 |
|
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: 112.73 E-value: 2.08e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 13 IEVRGLCNRFGPQSVHENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQNLPSLAEHERSLierrfG 92
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDRDI-----A 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 93 VLFQKGALFSSLTVTENVALPLiEHAGLSRADAE---HLAAVKLALAGLplsaADKYPASLSGGMIKRAALARALALDPD 169
Cdd:cd03301 76 MVFQNYALYPHMTVYDNIAFGL-KLRKVPKDEIDervREVAELLQIEHL----LDRKPKQLSGGQRQRVALGRAIVREPK 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1316494952 170 ILFLDEPTAGLDPIGAAAFDQLILTLRDALGLSVFLVTHDLDTLYTITDRVAVLAQKKV 228
Cdd:cd03301 151 VFLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQI 209
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
14-231 |
2.79e-30 |
|
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: 111.37 E-value: 2.79e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 14 EVRGLCNRFGPQSVHENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQNLPSLAEHERSlieRRFGV 93
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELA---RKIAY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 94 LFQkgalfssltvtenvalpliehaGLSRADAEHLaavklalaglplsaADKYPASLSGG-----MIkraalARALALDP 168
Cdd:cd03214 78 VPQ----------------------ALELLGLAHL--------------ADRPFNELSGGerqrvLL-----ARALAQEP 116
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1316494952 169 DILFLDEPTAGLDPIGAAAFDQLILTLRDALGLSVFLVTHDLDTLYTITDRVAVLAQKKVLVA 231
Cdd:cd03214 117 PILLLDEPTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQ 179
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
2-223 |
3.58e-30 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 117.82 E-value: 3.58e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 2 NRSTRPPAEAVIEVRGLC--NRFGPQSVHeNLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQNLPSL 79
Cdd:COG3845 247 EKAPAEPGEVVLEVENLSvrDDRGVPALK-DVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGL 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 80 AEHERslieRRFGVLF-----QKGALFSSLTVTENVALPLIEHAGLSR----------ADAEHLAA---VKLALAGLPLS 141
Cdd:COG3845 326 SPRER----RRLGVAYipedrLGRGLVPDMSVAENLILGRYRRPPFSRggfldrkairAFAEELIEefdVRTPGPDTPAR 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 142 aadkypaSLSGG----------MikraalaralALDPDILFLDEPTAGLDpIGAAAF-DQLILTLRDAlGLSVFLVTHDL 210
Cdd:COG3845 402 -------SLSGGnqqkvilareL----------SRDPKLLIAAQPTRGLD-VGAIEFiHQRLLELRDA-GAAVLLISEDL 462
|
250
....*....|...
gi 1316494952 211 DTLYTITDRVAVL 223
Cdd:COG3845 463 DEILALSDRIAVM 475
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
30-247 |
7.21e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 113.68 E-value: 7.21e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 30 NLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQNLPSLAEH-ERSLIERRFGVLFQ--KGALFSSlTV 106
Cdd:PRK13643 24 DIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQkEIKPVRKKVGVVFQfpESQLFEE-TV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 107 TENVAL-PliEHAGLSRADAEHLAAVKLALAGLPLSAADKYPASLSGGMIKRAALARALALDPDILFLDEPTAGLDPIGA 185
Cdd:PRK13643 103 LKDVAFgP--QNFGIPKEKAEKIAAEKLEMVGLADEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKAR 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1316494952 186 AAFDQLILTLRDAlGLSVFLVTHDLDTLYTITDRVAVLAQKKVL-VADAIDQVAETDDTWIHE 247
Cdd:PRK13643 181 IEMMQLFESIHQS-GQTVVLVTHLMDDVADYADYVYLLEKGHIIsCGTPSDVFQEVDFLKAHE 242
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
13-239 |
7.49e-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: 111.87 E-value: 7.49e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 13 IEVRGLCNRFGPQSVHENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQNLPSLAEHERSlierRFG 92
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRA----RLG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 93 V--LFQKGALFSSLTVTENVALPLiEHAGLSRADAEHLAAVKLALAGLpLSAADKYPASLSGGMIKRAALARALALDPDI 170
Cdd:cd03218 77 IgyLPQEASIFRKLTVEENILAVL-EIRGLSKKEREEKLEELLEEFHI-THLRKSKASSLSGGERRRVEIARALATNPKF 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1316494952 171 LFLDEPTAGLDPIGAAAFDQLILTLRDaLGLSVFLVTHDLDTLYTITDRVAVLAQKKVLVADAIDQVAE 239
Cdd:cd03218 155 LLLDEPFAGVDPIAVQDIQKIIKILKD-RGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAA 222
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
11-228 |
9.68e-30 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 112.07 E-value: 9.68e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 11 AVIEVRGLCNRF-GPQSVHENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQNLPSLAEHERSLIER 89
Cdd:COG3638 1 PMLELRNLSKRYpGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRRLRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 90 RFGVLFQKGALFSSLTVTENVALPLIEHAGLSRA-----DAEHLAAVKLALA--GLpLSAADKYPASLSGG--------- 153
Cdd:COG3638 81 RIGMIFQQFNLVPRLSVLTNVLAGRLGRTSTWRSllglfPPEDRERALEALErvGL-ADKAYQRADQLSGGqqqrvaiar 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1316494952 154 --MikraalaralaLDPDILFLDEPTAGLDPIGAAAFDQLILTLRDALGLSVFLVTHDLDTLYTITDRVAVLAQKKV 228
Cdd:COG3638 160 alV-----------QEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRV 225
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
7-222 |
1.19e-29 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 113.67 E-value: 1.19e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 7 PPAEAVIEVRGLCNRF---------GPQSVH--ENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQN 75
Cdd:COG4608 2 AMAEPLLEVRDLKKHFpvrgglfgrTVGVVKavDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 76 LPSLAEHERSLIERRFGVLFQKGalFSSL----TVTENVALPLIEHAGLSRADAEHLAAVKLALAGLPLSAADKYPASLS 151
Cdd:COG4608 82 ITGLSGRELRPLRRRMQMVFQDP--YASLnprmTVGDIIAEPLRIHGLASKAERRERVAELLELVGLRPEHADRYPHEFS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 152 GG----------MIkraalaralaLDPDILFLDEPTAGLD-PIGAaafdQ---LILTLRDALGLSVFLVTHDLDTLYTIT 217
Cdd:COG4608 160 GGqrqrigiaraLA----------LNPKLIVCDEPVSALDvSIQA----QvlnLLEDLQDELGLTYLFISHDLSVVRHIS 225
|
....*
gi 1316494952 218 DRVAV 222
Cdd:COG4608 226 DRVAV 230
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
11-237 |
2.17e-29 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 111.40 E-value: 2.17e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 11 AVIEVRGLCNRFGPQSVHENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQNLPSLAEHERSlieRR 90
Cdd:PRK13548 1 AMLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELA---RR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 91 FGVLFQKGALFSSLTVTENVALPLIEHAGLSRADAEHLAAVkLALAGLPLSAADKYPAsLSGG------MIKRAALARAL 164
Cdd:PRK13548 78 RAVLPQHSSLSFPFTVEEVVAMGRAPHGLSRAEDDALVAAA-LAQVDLAHLAGRDYPQ-LSGGeqqrvqLARVLAQLWEP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1316494952 165 ALDPDILFLDEPTAGLDPigaaAFDQLILTLRDAL----GLSVFLVTHDLD--TLYtiTDRVAVLAQKKVLVADAIDQV 237
Cdd:PRK13548 156 DGPPRWLLLDEPTSALDL----AHQHHVLRLARQLaherGLAVIVVLHDLNlaARY--ADRIVLLHQGRLVADGTPAEV 228
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
29-255 |
2.69e-29 |
|
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: 110.63 E-value: 2.69e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 29 ENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQNLpslaehERSLIERRfgVLFQKGALFSSLTVTE 108
Cdd:TIGR01184 2 KGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQI------TEPGPDRM--VVFQNYSLLPWLTVRE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 109 NVALPLIE-HAGLSRADAEHLAAVKLALAGLPlSAADKYPASLSGGMIKRAALARALALDPDILFLDEPTAGLDPIGAAA 187
Cdd:TIGR01184 74 NIALAVDRvLPDLSKSERRAIVEEHIALVGLT-EAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGN 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1316494952 188 FDQLILTLRDALGLSVFLVTHDLDTLYTITDRVAVLAQKKvlvADAIDQVAETDdtwiheyFHGPRGR 255
Cdd:TIGR01184 153 LQEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNGP---AANIGQILEVP-------FPRPRDR 210
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
14-228 |
2.84e-29 |
|
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: 109.65 E-value: 2.84e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 14 EVRGLCNRFGPQ-SVHENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQNLPSlaeHERSlieRRFG 92
Cdd:cd03226 1 RIENISFSYKKGtEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKA---KERR---KSIG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 93 VLFQ--KGALFSSlTVTENVALPLiEHAGLSRADAEHLAAvKLALAGLplsaADKYPASLSGGMIKRAALARALALDPDI 170
Cdd:cd03226 75 YVMQdvDYQLFTD-SVREELLLGL-KELDAGNEQAETVLK-DLDLYAL----KERHPLSLSGGQKQRLAIAAALLSGKDL 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1316494952 171 LFLDEPTAGLDPIGAAAFDQLILTLRDAlGLSVFLVTHDLDTLYTITDRVAVLAQKKV 228
Cdd:cd03226 148 LIFDEPTSGLDYKNMERVGELIRELAAQ-GKAVIVITHDYEFLAKVCDRVLLLANGAI 204
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
14-227 |
3.89e-29 |
|
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: 107.72 E-value: 3.89e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 14 EVRGLCNRFGPQSVHENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQNLPSLAEHERsliERRFGV 93
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEEL---RRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 94 LFQkgalfssltvtenvalpliehaglsradaehlaavklalaglplsaadkypasLSGGMIKRAALARALALDPDILFL 173
Cdd:cd00267 78 VPQ-----------------------------------------------------LSGGQRQRVALARALLLNPDLLLL 104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1316494952 174 DEPTAGLDPIGAAAFDQLILTLRDAlGLSVFLVTHDLDTLYTITDRVAVLAQKK 227
Cdd:cd00267 105 DEPTSGLDPASRERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
30-229 |
5.38e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 110.99 E-value: 5.38e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 30 NLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQNLPSLAEH-ERSLIERRFGVLFQ--KGALFSSlTV 106
Cdd:PRK13649 25 DVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNkDIKQIRKKVGLVFQfpESQLFEE-TV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 107 TENVAL-PliEHAGLSRADAEHLAAVKLALAGLPLSAADKYPASLSGGMIKRAALARALALDPDILFLDEPTAGLDPIGA 185
Cdd:PRK13649 104 LKDVAFgP--QNFGVSQEEAEALAREKLALVGISESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGR 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1316494952 186 AAFDQLILTLRDAlGLSVFLVTHDLDTLYTITDRVAVLAQKKVL 229
Cdd:PRK13649 182 KELMTLFKKLHQS-GMTIVLVTHLMDDVANYADFVYVLEKGKLV 224
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
6-246 |
5.58e-29 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 113.01 E-value: 5.58e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 6 RPPAEA------VIEVRGLCNRFGPQSVHENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQNLPSL 79
Cdd:PRK11607 7 RPQAKTrkaltpLLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 80 AEHERSLierrfGVLFQKGALFSSLTVTENVALPLiEHAGLSRADAEHLAAVKLALAGLPLSAADKyPASLSGGMIKRAA 159
Cdd:PRK11607 87 PPYQRPI-----NMMFQSYALFPHMTVEQNIAFGL-KQDKLPKAEIASRVNEMLGLVHMQEFAKRK-PHQLSGGQRQRVA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 160 LARALALDPDILFLDEPTAGLDpigAAAFDQLILTLRDAL---GLSVFLVTHDLDTLYTITDRVAVLAQKKVLvadaidQ 236
Cdd:PRK11607 160 LARSLAKRPKLLLLDEPMGALD---KKLRDRMQLEVVDILervGVTCVMVTHDQEEAMTMAGRIAIMNRGKFV------Q 230
|
250
....*....|
gi 1316494952 237 VAETDDTWIH 246
Cdd:PRK11607 231 IGEPEEIYEH 240
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
13-239 |
1.10e-28 |
|
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: 108.68 E-value: 1.10e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 13 IEVRGLCNRFGPQSVHENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQNLPSLAEHERSlierRFG 92
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERA----RAG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 93 VLF--QKGALFSSLTVTENVALpliehAGLSRADAEHLAAVKLALAGLP-LSAADKYPA-SLSGG-----------Mikr 157
Cdd:cd03224 77 IGYvpEGRRIFPELTVEENLLL-----GAYARRRAKRKARLERVYELFPrLKERRKQLAgTLSGGeqqmlaiaralM--- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 158 aalaralaLDPDILFLDEPTAGLDPIGAAAFDQLILTLRDaLGLSVFLVTHDLDTLYTITDRVAVLAQKKVLVADAIDQV 237
Cdd:cd03224 149 --------SRPKLLLLDEPSEGLAPKIVEEIFEAIRELRD-EGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAEL 219
|
..
gi 1316494952 238 AE 239
Cdd:cd03224 220 LA 221
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
3-228 |
1.54e-28 |
|
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: 113.24 E-value: 1.54e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 3 RSTRPPAEAVIEVRGLCNRF-------GPQSVH----ENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLrQPSEGSVRV 71
Cdd:COG4172 266 RPVPPDAPPLLEARDLKVWFpikrglfRRTVGHvkavDGVSLTLRRGETLGLVGESGSGKSTLGLALLRL-IPSEGEIRF 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 72 FGQNLPSLAEHERSLIERRFGVLFQKGalFSSL----TVTENVALPLIEHA-GLSRADAEHLAAVKLALAGLPLSAADKY 146
Cdd:COG4172 345 DGQDLDGLSRRALRPLRRRMQVVFQDP--FGSLsprmTVGQIIAEGLRVHGpGLSAAERRARVAEALEEVGLDPAARHRY 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 147 PASLSGG----------MikraalaralALDPDILFLDEPTAGLDPIGAAAFDQLILTLRDALGLSVFLVTHDLDTLYTI 216
Cdd:COG4172 423 PHEFSGGqrqriaiaraL----------ILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREHGLAYLFISHDLAVVRAL 492
|
250
....*....|..
gi 1316494952 217 TDRVAVLAQKKV 228
Cdd:COG4172 493 AHRVMVMKDGKV 504
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
8-228 |
2.03e-28 |
|
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: 113.24 E-value: 2.03e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 8 PAEAVIEVRGLCNRFG----PQSVHENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGL-----RQPSeGSVRVFGQNLPS 78
Cdd:COG4172 2 MSMPLLSVEDLSVAFGqgggTVEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLlpdpaAHPS-GSILFDGQDLLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 79 LAEHE-RSLIERRFGVLFQKGalFSSL----TVTENVALPLIEHAGLSRADAEHLAAVKLALAGLPLSA--ADKYPASLS 151
Cdd:COG4172 81 LSERElRRIRGNRIAMIFQEP--MTSLnplhTIGKQIAEVLRLHRGLSGAAARARALELLERVGIPDPErrLDAYPHQLS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 152 GG-----MIkraalARALALDPDILFLDEPTAGLDPIGAAAFDQLILTLRDALGLSVFLVTHDLDTLYTITDRVAVLAQK 226
Cdd:COG4172 159 GGqrqrvMI-----AMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFADRVAVMRQG 233
|
..
gi 1316494952 227 KV 228
Cdd:COG4172 234 EI 235
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
9-229 |
2.04e-28 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 109.33 E-value: 2.04e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 9 AEAVIEVRGLCNRFGPQSVH--ENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQnlpSLAEHERSL 86
Cdd:PRK13635 2 KEEIIRVEHISFRYPDAATYalKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGM---VLSEETVWD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 87 IERRFGVLFQK-GALFSSLTVTENVALPLiEHAGLSRAdaEHLAAVKLALAGLPLSA-ADKYPASLSGGMIKRAALARAL 164
Cdd:PRK13635 79 VRRQVGMVFQNpDNQFVGATVQDDVAFGL-ENIGVPRE--EMVERVDQALRQVGMEDfLNREPHRLSGGQKQRVAIAGVL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1316494952 165 ALDPDILFLDEPTAGLDPIGAAAFDQLILTLRDALGLSVFLVTHDLDTLYTiTDRVAVLAQKKVL 229
Cdd:PRK13635 156 ALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEIL 219
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
13-237 |
2.20e-28 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 108.66 E-value: 2.20e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 13 IEVRGLCNRFGPQSVHENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQNLPSLAEHERSlieRRFG 92
Cdd:COG4559 2 LEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELA---RRRA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 93 VLFQKGALFSSLTVTENVALPLIEHAGLSRADAEHLAAVkLALAGLPLSAADKYPaSLSGG------------MIkraal 160
Cdd:COG4559 79 VLPQHSSLAFPFTVEEVVALGRAPHGSSAAQDRQIVREA-LALVGLAHLAGRSYQ-TLSGGeqqrvqlarvlaQL----- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 161 ARALALDPDILFLDEPTAGLDPigaaAFDQLILTL-RD--ALGLSVFLVTHDLD--TLYtiTDRVAVLAQKKVLVADAID 235
Cdd:COG4559 152 WEPVDGGPRWLFLDEPTSALDL----AHQHAVLRLaRQlaRRGGGVVAVLHDLNlaAQY--ADRILLLHQGRLVAQGTPE 225
|
..
gi 1316494952 236 QV 237
Cdd:COG4559 226 EV 227
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
2-228 |
3.14e-28 |
|
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: 113.01 E-value: 3.14e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 2 NRSTRPPAEAVIEVRGLCNRFGPQS--VHENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQNLpsl 79
Cdd:COG2274 463 SKLSLPRLKGDIELENVSFRYPGDSppVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDL--- 539
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 80 AEHERSLIERRFGVLFQKGALFSSlTVTENVALpliehaGLSRADAEHLAAVkLALAGLpLSAADKYP-----------A 148
Cdd:COG2274 540 RQIDPASLRRQIGVVLQDVFLFSG-TIRENITL------GDPDATDEEIIEA-ARLAGL-HDFIEALPmgydtvvgeggS 610
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 149 SLSGG----------MIKraalaralalDPDILFLDEPTAGLDPIGAAAFDQLILTLRDalGLSVFLVTHDLDTLyTITD 218
Cdd:COG2274 611 NLSGGqrqrlaiaraLLR----------NPRILILDEATSALDAETEAIILENLRRLLK--GRTVIIIAHRLSTI-RLAD 677
|
250
....*....|
gi 1316494952 219 RVAVLAQKKV 228
Cdd:COG2274 678 RIIVLDKGRI 687
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
9-228 |
3.32e-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: 106.36 E-value: 3.32e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 9 AEAVIEVRGLCNRfgpqSVHENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQNLPSLAEHERslie 88
Cdd:cd03215 1 GEPVLEVRGLSVK----GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDA---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 89 RRFGVLF-----QKGALFSSLTVTENVALPLIehaglsradaehlaavklalaglplsaadkypasLSGGMIKRAALARA 163
Cdd:cd03215 73 IRAGIAYvpedrKREGLVLDLSVAENIALSSL----------------------------------LSGGNQQKVVLARW 118
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1316494952 164 LALDPDILFLDEPTAGLDpIGAAAF-DQLILTLRDAlGLSVFLVTHDLDTLYTITDRVAVLAQKKV 228
Cdd:cd03215 119 LARDPRVLILDEPTRGVD-VGAKAEiYRLIRELADA-GKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
13-231 |
3.60e-28 |
|
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: 106.98 E-value: 3.60e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 13 IEVRGLCNRFGPQSVHENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQNLPSLAEHerslierRFG 92
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARN-------RIG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 93 VLFQKGALFSSLTVTEnVALPLIEHAGLSRADAehLAAVKLALAGLPLSA-ADKYPASLSGGMIKRAALARALALDPDIL 171
Cdd:cd03269 74 YLPEERGLYPKMKVID-QLVYLAQLKGLKKEEA--RRRIDEWLERLELSEyANKRVEELSKGNQQKVQFIAAVIHDPELL 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 172 FLDEPTAGLDPIGAAAFDQLILTLRDAlGLSVFLVTHDLDTLYTITDRVAVLAQKKVLVA 231
Cdd:cd03269 151 ILDEPFSGLDPVNVELLKDVIRELARA-GKTVILSTHQMELVEELCDRVLLLNKGRAVLY 209
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
9-223 |
4.51e-28 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 112.04 E-value: 4.51e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 9 AEAVIEVRGLCNRFGpqSVH--ENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQNL----PSLAeh 82
Cdd:COG3845 2 MPPALELRGITKRFG--GVVanDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVrirsPRDA-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 83 erslIERRFGVLFQKGALFSSLTVTENVALPLiEHAGLSRADAEHLAAVKLALA---GLPLSaADKYPASLSGGM----- 154
Cdd:COG3845 78 ----IALGIGMVHQHFMLVPNLTVAENIVLGL-EPTKGGRLDRKAARARIRELSeryGLDVD-PDAKVEDLSVGEqqrve 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1316494952 155 -IKraalarALALDPDILFLDEPTAGLDPIGAaafDQLILTLRD--ALGLSVFLVTHDLDTLYTITDRVAVL 223
Cdd:COG3845 152 iLK------ALYRGARILILDEPTAVLTPQEA---DELFEILRRlaAEGKSIIFITHKLREVMAIADRVTVL 214
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
21-228 |
7.97e-28 |
|
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: 106.04 E-value: 7.97e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 21 RFGPQSVHenLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQNLPSLAEHERSLierrfGVLFQKGAL 100
Cdd:cd03298 9 SYGEQPMH--FDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRPV-----SMLFQENNL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 101 FSSLTVTENVALPLIEHAGLSRADAEhlaAVKLALAGLPLSAADK-YPASLSGGMIKRAALARALALDPDILFLDEPTAG 179
Cdd:cd03298 82 FAHLTVEQNVGLGLSPGLKLTAEDRQ---AIEVALARVGLAGLEKrLPGELSGGERQRVALARVLVRDKPVLLLDEPFAA 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1316494952 180 LDPIGAAAFDQLILTLRDALGLSVFLVTHDLDTLYTITDRVAVLAQKKV 228
Cdd:cd03298 159 LDPALRAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRI 207
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
13-227 |
9.19e-28 |
|
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: 104.77 E-value: 9.19e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 13 IEVRGLCNRFGPQSVH--ENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQNLPSLAEHERSlieRR 90
Cdd:cd03228 1 IEFKNVSFSYPGRPKPvlKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLR---KN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 91 FGVLFQKGALFSSlTVTENValpliehaglsradaehlaavklalaglplsaadkypasLSGG----------MIKraal 160
Cdd:cd03228 78 IAYVPQDPFLFSG-TIRENI---------------------------------------LSGGqrqriaiaraLLR---- 113
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1316494952 161 aralalDPDILFLDEPTAGLDPIGAAAFDQLILTLRDalGLSVFLVTHDLDTLyTITDRVAVLAQKK 227
Cdd:cd03228 114 ------DPPILILDEATSALDPETEALILEALRALAK--GKTVIVIAHRLSTI-RDADRIIVLDDGR 171
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
13-239 |
1.11e-27 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 106.85 E-value: 1.11e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 13 IEVRGLCNRFGPQSVHENLDLDLYKGEILAVVGGSGSGKSVLLRS---IIGLRQPS--EGSVRVFGQNLPSlAEHERSLI 87
Cdd:PRK14267 5 IETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTfnrLLELNEEArvEGEVRLFGRNIYS-PDVDPIEV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 88 ERRFGVLFQKGALFSSLTVTENVALPLiEHAGLSRADAEHLAAVKLAL--AGLPLSAADK---YPASLSGGMIKRAALAR 162
Cdd:PRK14267 84 RREVGMVFQYPNPFPHLTIYDNVAIGV-KLNGLVKSKKELDERVEWALkkAALWDEVKDRlndYPSNLSGGQRQRLVIAR 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1316494952 163 ALALDPDILFLDEPTAGLDPIGAAAFDQLILTLRDAlgLSVFLVTHDLDTLYTITDRVAVLAQKKVLVADAIDQVAE 239
Cdd:PRK14267 163 ALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKE--YTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFE 237
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
13-228 |
1.18e-27 |
|
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: 106.27 E-value: 1.18e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 13 IEVRGLCNRFGPQSVhENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQNLPSLaeherSLIERRFG 92
Cdd:cd03299 1 LKVENLSKDWKEFKL-KNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNL-----PPEKRDIS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 93 VLFQKGALFSSLTVTENVALPLIeHAGLSRADAE---HLAAVKLALAGLplsaADKYPASLSGGMIKRAALARALALDPD 169
Cdd:cd03299 75 YVPQNYALFPHMTVYKNIAYGLK-KRKVDKKEIErkvLEIAEMLGIDHL----LNRKPETLSGGEQQRVAIARALVVNPK 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1316494952 170 ILFLDEPTAGLDPIGAAAFDQLILTLRDALGLSVFLVTHDLDTLYTITDRVAVLAQKKV 228
Cdd:cd03299 150 ILLLDEPFSALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKL 208
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-223 |
1.41e-27 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 106.66 E-value: 1.41e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 1 MNrSTRPPAEAVIEVRGLCNRFGPQSVHENLDLDLYKGEILAVVGGSGSGKSVLLRS-------IIGLRqpSEGSVRVFG 73
Cdd:COG1117 1 MT-APASTLEPKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRClnrmndlIPGAR--VEGEILLDG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 74 QNL--PSLaeherSLIE--RRFGVLFQKGALFSsLTVTENVALPLIEHAGLSRADAEHLaaVKLAL--AGLP------Ls 141
Cdd:COG1117 78 EDIydPDV-----DVVElrRRVGMVFQKPNPFP-KSIYDNVAYGLRLHGIKSKSELDEI--VEESLrkAALWdevkdrL- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 142 aaDKYPASLSGG------------MikraalaralalDPDILFLDEPTAGLDPIGAAAFDQLILTLRDAlgLSVFLVTHD 209
Cdd:COG1117 149 --KKSALGLSGGqqqrlciaralaV------------EPEVLLMDEPTSALDPISTAKIEELILELKKD--YTIVIVTHN 212
|
250
....*....|....
gi 1316494952 210 LDTLYTITDRVAVL 223
Cdd:COG1117 213 MQQAARVSDYTAFF 226
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
13-228 |
1.77e-27 |
|
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: 105.18 E-value: 1.77e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 13 IEVRGLCNRFGPQSVH-ENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQNLPSLAEHERSLIERRF 91
Cdd:cd03292 1 IEFINVTKTYPNGTAAlDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYLRRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 92 GVLFQKGALFSSLTVTENVALPLiEHAGLSRADAEHLAAVKLALAGLPlSAADKYPASLSGGMIKRAALARALALDPDIL 171
Cdd:cd03292 81 GVVFQDFRLLPDRNVYENVAFAL-EVTGVPPREIRKRVPAALELVGLS-HKHRALPAELSGGEQQRVAIARAIVNSPTIL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1316494952 172 FLDEPTAGLDPIGAAAFDQLILTLRDAlGLSVFLVTHDLDTLYTITDRVAVLAQKKV 228
Cdd:cd03292 159 IADEPTGNLDPDTTWEIMNLLKKINKA-GTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
12-248 |
1.84e-27 |
|
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: 105.84 E-value: 1.84e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 12 VIEVRGLCNRF--GPQSVHeNLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQNLPSLAEHERSLIER 89
Cdd:TIGR02315 1 MLEVENLSKVYpnGKQALK-NINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKLRKLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 90 RFGVLFQKGALFSSLTVTENVALP-LIEHAGL-------SRAD-AEHLAAV-KLALAGLPLSAADKypasLSGGMIKRAA 159
Cdd:TIGR02315 80 RIGMIFQHYNLIERLTVLENVLHGrLGYKPTWrsllgrfSEEDkERALSALeRVGLADKAYQRADQ----LSGGQQQRVA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 160 LARALALDPDILFLDEPTAGLDPIGAAAFDQLILTLRDALGLSVFLVTHDLDTLYTITDRVAVLAQKKVLVADAIDQVae 239
Cdd:TIGR02315 156 IARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSEL-- 233
|
....*....
gi 1316494952 240 TDDTWIHEY 248
Cdd:TIGR02315 234 DDEVLRHIY 242
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
30-223 |
2.33e-27 |
|
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: 105.07 E-value: 2.33e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 30 NLDLDLyKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQnlpSLAEHERSLI----ERRFGVLFQKGALFSSLT 105
Cdd:cd03297 16 KIDFDL-NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGT---VLFDSRKKINlppqQRKIGLVFQQYALFPHLN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 106 VTENVALPLIEHAGLSRADAEHLAAVKLALAGLplsaADKYPASLSGGMIKRAALARALALDPDILFLDEPTAGLDpigA 185
Cdd:cd03297 92 VRENLAFGLKRKRNREDRISVDELLDLLGLDHL----LNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALD---R 164
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1316494952 186 AAFDQLILTLRD---ALGLSVFLVTHDLDTLYTITDRVAVL 223
Cdd:cd03297 165 ALRLQLLPELKQikkNLNIPVIFVTHDLSEAEYLADRIVVM 205
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
29-249 |
3.16e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 106.45 E-value: 3.16e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 29 ENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQNL-PSLAEHERSLIERRFGVLFQkgalFSSLTVT 107
Cdd:PRK13641 24 DNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHItPETGNKNLKKLRKKVSLVFQ----FPEAQLF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 108 ENVALPLIEHA----GLSRADAEHLAAVKLALAGLPLSAADKYPASLSGGMIKRAALARALALDPDILFLDEPTAGLDPI 183
Cdd:PRK13641 100 ENTVLKDVEFGpknfGFSEDEAKEKALKWLKKVGLSEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPE 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1316494952 184 GAAAFDQLILTLRDAlGLSVFLVTHDLDTLYTITDRVAVLAQKKVLVADAIDQVAeTDDTWIHEYF 249
Cdd:PRK13641 180 GRKEMMQLFKDYQKA-GHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIF-SDKEWLKKHY 243
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
38-229 |
4.38e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 106.26 E-value: 4.38e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 38 GEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVfGQNLPSLAEHERSL--IERRFGVLFQ--KGALFSSlTVTENVAL- 112
Cdd:PRK13634 33 GSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTI-GERVITAGKKNKKLkpLRKKVGIVFQfpEHQLFEE-TVEKDICFg 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 113 PLieHAGLSRADAEHLAAVKLALAGLPLSAADKYPASLSGGMIKRAALARALALDPDILFLDEPTAGLDPIGAAAFDQLI 192
Cdd:PRK13634 111 PM--NFGVSEEDAKQKAREMIELVGLPEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMF 188
|
170 180 190
....*....|....*....|....*....|....*..
gi 1316494952 193 LTLRDALGLSVFLVTHDLDTLYTITDRVAVLAQKKVL 229
Cdd:PRK13634 189 YKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVF 225
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
7-223 |
6.21e-27 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 106.04 E-value: 6.21e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 7 PPAEAVIEVRGLCNRFGPQSVHENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQNLPSLAEHERsl 86
Cdd:PRK13537 2 PMSVAPIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHAR-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 87 ieRRFGVLFQKGALFSSLTVTENVaLPLIEHAGLSRADAEHLAAVKLALAGLPlSAADKYPASLSGGMIKRAALARALAL 166
Cdd:PRK13537 80 --QRVGVVPQFDNLDPDFTVRENL-LVFGRYFGLSAAAARALVPPLLEFAKLE-NKADAKVGELSGGMKRRLTLARALVN 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1316494952 167 DPDILFLDEPTAGLDPigaAAFDQLILTLRDAL--GLSVFLVTHDLDTLYTITDRVAVL 223
Cdd:PRK13537 156 DPDVLVLDEPTTGLDP---QARHLMWERLRSLLarGKTILLTTHFMEEAERLCDRLCVI 211
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
17-260 |
7.78e-27 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 104.77 E-value: 7.78e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 17 GLCNRFGPQSVHENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQNLPSLAEHERSLIERRFGVLFQ 96
Cdd:PRK10419 17 GLSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQRKAFRRDIQMVFQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 97 K--GALFSSLTVTENVALPLIEHAGLSRADAEHLAAVKLALAGLPLSAADKYPASLSGGMIKRAALARALALDPDILFLD 174
Cdd:PRK10419 97 DsiSAVNPRKTVREIIREPLRHLLSLDKAERLARASEMLRAVDLDDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILD 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 175 EPTAGLDPIGAAAFDQLILTLRDALGLSVFLVTHDLDTLYTITDRVAVLAQkkvlvadaiDQVAETDDTWIHEYFHGPRG 254
Cdd:PRK10419 177 EAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDN---------GQIVETQPVGDKLTFSSPAG 247
|
....*.
gi 1316494952 255 RAAYQA 260
Cdd:PRK10419 248 RVLQNA 253
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
13-229 |
1.31e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 105.17 E-value: 1.31e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 13 IEVRGLCNRFGPQSVHE-----NLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVF---GQNLPSLAEHER 84
Cdd:PRK13651 3 IKVKNIVKIFNKKLPTElkaldNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIfkdEKNKKKTKEKEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 85 SLIE------------------RRFGVLFQ--KGALFSSlTVTENVALPLIEHaGLSRADAEHLAAVKLALAGLPLSAAD 144
Cdd:PRK13651 83 VLEKlviqktrfkkikkikeirRRVGVVFQfaEYQLFEQ-TIEKDIIFGPVSM-GVSKEEAKKRAAKYIELVGLDESYLQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 145 KYPASLSGGMIKRAALARALALDPDILFLDEPTAGLDPIGAaafdQLILTLRDAL---GLSVFLVTHDLDTLYTITDRVA 221
Cdd:PRK13651 161 RSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGV----KEILEIFDNLnkqGKTIILVTHDLDNVLEWTKRTI 236
|
....*...
gi 1316494952 222 VLAQKKVL 229
Cdd:PRK13651 237 FFKDGKII 244
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
7-182 |
2.79e-26 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 103.34 E-value: 2.79e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 7 PPAEAVIEVRGLCNRFGPQSVHENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQNLP-------SL 79
Cdd:COG4598 3 DTAPPALEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIRlkpdrdgEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 80 AEHERSLIER---RFGVLFQKGALFSSLTVTENVALPLIEHAGLSRADAEHLAAVKLALAGLPlSAADKYPASLSGGMIK 156
Cdd:COG4598 83 VPADRRQLQRirtRLGMVFQSFNLWSHMTVLENVIEAPVHVLGRPKAEAIERAEALLAKVGLA-DKRDAYPAHLSGGQQQ 161
|
170 180
....*....|....*....|....*.
gi 1316494952 157 RAALARALALDPDILFLDEPTAGLDP 182
Cdd:COG4598 162 RAAIARALAMEPEVMLFDEPTSALDP 187
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
10-237 |
7.40e-26 |
|
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated complex. This protein (PhnK) and the adjacent-encoded PhnL resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this complex rather than part of a transporter per se. [Central intermediary metabolism, Phosphorus compounds]
Pssm-ID: 188208 [Multi-domain] Cd Length: 253 Bit Score: 101.83 E-value: 7.40e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 10 EAVIEVRGLCNRFGPQSVHENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQN-----LPSLAEHER 84
Cdd:TIGR02323 1 KPLLQVSGLSKSYGGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMRSgaeleLYQLSEAER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 85 SLIER-RFGVLFQ--KGALFSSLTVTENVALPLI----EHAGLSRADAEHLaavkLALAGLPLSAADKYPASLSGGMIKR 157
Cdd:TIGR02323 81 RRLMRtEWGFVHQnpRDGLRMRVSAGANIGERLMaigaRHYGNIRATAQDW----LEEVEIDPTRIDDLPRAFSGGMQQR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 158 AALARALALDPDILFLDEPTAGLDPIGAAAFDQLILTLRDALGLSVFLVTHDLDTLYTITDRVAVLAQKKVLVADAIDQV 237
Cdd:TIGR02323 157 LQIARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRVVESGLTDQV 236
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
3-236 |
8.77e-26 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 105.49 E-value: 8.77e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 3 RSTRPPAEAVIEVRGLCNRfgpqSVHENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQNLPSLAEH 82
Cdd:COG1129 247 KRAAAPGEVVLEVEGLSVG----GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPR 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 83 ERslIERRFGVL----FQKGaLFSSLTVTENVALPLIEHAG----LSRADAEHLAA-------VKLALAGLPLSaadkyp 147
Cdd:COG1129 323 DA--IRAGIAYVpedrKGEG-LVLDLSIRENITLASLDRLSrgglLDRRRERALAEeyikrlrIKTPSPEQPVG------ 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 148 aSLSGG----------MIkraalaralaLDPDILFLDEPTAGLDpIGA-AAFDQLILTLRDAlGLSVFLVTHDLDTLYTI 216
Cdd:COG1129 394 -NLSGGnqqkvvlakwLA----------TDPKVLILDEPTRGID-VGAkAEIYRLIRELAAE-GKAVIVISSELPELLGL 460
|
250 260
....*....|....*....|...
gi 1316494952 217 TDRVAVLAQKKV---LVADAIDQ 236
Cdd:COG1129 461 SDRILVMREGRIvgeLDREEATE 483
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
15-228 |
8.84e-26 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 101.68 E-value: 8.84e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 15 VRGLCNRFGPQSVHENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQNLPSLAEHERslierrfgVL 94
Cdd:PRK11247 15 LNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEAREDTR--------LM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 95 FQKGALFSSLTVTENVALPLiehAGLSRADA-EHLAAVKLAlaglplSAADKYPASLSGGMIKRAALARALALDPDILFL 173
Cdd:PRK11247 87 FQDARLLPWKKVIDNVGLGL---KGQWRDAAlQALAAVGLA------DRANEWPAALSGGQKQRVALARALIHRPGLLLL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1316494952 174 DEPTAGLDPIGAAAFDQLILTLRDALGLSVFLVTHDLDTLYTITDRVAVLAQKKV 228
Cdd:PRK11247 158 DEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
9-223 |
9.03e-26 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 105.49 E-value: 9.03e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 9 AEAVIEVRGLCNRFGPQSVHENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQ--NLPSLAEHERSL 86
Cdd:COG1129 1 AEPLLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEpvRFRSPRDAQAAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 87 IerrfGVLFQKGALFSSLTVTENVALP-LIEHAGL-SRADAEHLAAVKLALAGLPLSAADKYpASLSGG---MI---Kra 158
Cdd:COG1129 81 I----AIIHQELNLVPNLSVAENIFLGrEPRRGGLiDWRAMRRRARELLARLGLDIDPDTPV-GDLSVAqqqLVeiaR-- 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1316494952 159 alarALALDPDILFLDEPTAGLDPIGAAAFDQLILTLRDAlGLSVFLVTHDLDTLYTITDRVAVL 223
Cdd:COG1129 154 ----ALSRDARVLILDEPTASLTEREVERLFRIIRRLKAQ-GVAIIYISHRLDEVFEIADRVTVL 213
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
10-229 |
1.17e-25 |
|
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: 105.27 E-value: 1.17e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 10 EAVIEVRGLCNRF-----GPQSVHENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRV-FGQ---NLPSLA 80
Cdd:TIGR03269 277 EPIIKVRNVSKRYisvdrGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrVGDewvDMTKPG 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 81 EHERSLIERRFGVLFQKGALFSSLTVTENvalpLIEHAGLSRAD--AEHLAAVKLALAGLPLSAA----DKYPASLSGGM 154
Cdd:TIGR03269 357 PDGRGRAKRYIGILHQEYDLYPHRTVLDN----LTEAIGLELPDelARMKAVITLKMVGFDEEKAeeilDKYPDELSEGE 432
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1316494952 155 IKRAALARALALDPDILFLDEPTAGLDPIGAAAFDQLILTLRDALGLSVFLVTHDLDTLYTITDRVAVLAQKKVL 229
Cdd:TIGR03269 433 RHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIV 507
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
13-229 |
1.62e-25 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 100.86 E-value: 1.62e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 13 IEVRGLCNRFGPQSVHENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQ--NLPS-LAEHERSLIER 89
Cdd:COG4161 3 IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHqfDFSQkPSEKAIRLLRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 90 RFGVLFQKGALFSSLTVTENvalpLIEH----AGLSRADAEHlAAVKLaLAGLPLS-AADKYPASLSGGMIKRAALARAL 164
Cdd:COG4161 83 KVGMVFQQYNLWPHLTVMEN----LIEApckvLGLSKEQARE-KAMKL-LARLRLTdKADRFPLHLSGGQQQRVAIARAL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1316494952 165 ALDPDILFLDEPTAGLDPIGAAAFDQLILTLRDAlGLSVFLVTHDLDTLYTITDRVAVLAQKKVL 229
Cdd:COG4161 157 MMEPQVLLFDEPTAALDPEITAQVVEIIRELSQT-GITQVIVTHEVEFARKVASQVVYMEKGRII 220
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
1-231 |
1.87e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 102.24 E-value: 1.87e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 1 MNRSTRPP----AEAVIEVRGLCNRFGPQSVHE-----NLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRV 71
Cdd:PRK13631 6 MKKKLKVPnplsDDIILRVKNLYCVFDEKQENElvalnNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 72 --------FGQNLPSLAEHERSL-----IERRFGVLFQ--KGALFSSlTVTENVALPLIEhAGLSRADAEHLAAVKLALA 136
Cdd:PRK13631 86 gdiyigdkKNNHELITNPYSKKIknfkeLRRRVSMVFQfpEYQLFKD-TIEKDIMFGPVA-LGVKKSEAKKLAKFYLNKM 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 137 GLPLSAADKYPASLSGGMIKRAALARALALDPDILFLDEPTAGLDPIGAAAFDQLILTLRdALGLSVFLVTHDLDTLYTI 216
Cdd:PRK13631 164 GLDDSYLERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAK-ANNKTVFVITHTMEHVLEV 242
|
250
....*....|....*
gi 1316494952 217 TDRVAVLAQKKVLVA 231
Cdd:PRK13631 243 ADEVIVMDKGKILKT 257
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
30-229 |
2.27e-25 |
|
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. NikD and NikE are homologous. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131817 [Multi-domain] Cd Length: 230 Bit Score: 100.14 E-value: 2.27e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 30 NLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQP----SEGSVRVFGQNLPSLaeherSLIERRFGVLFQ--KGALFSS 103
Cdd:TIGR02770 4 DLNLSLKRGEVLALVGESGSGKSLTCLAILGLLPPgltqTSGEILLDGRPLLPL-----SIRGRHIATIMQnpRTAFNPL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 104 LTVTENVALPLIEHAGLSrADAEHLAAVKLALAGLPLSAA--DKYPASLSGGMIKRAALARALALDPDILFLDEPTAGLD 181
Cdd:TIGR02770 79 FTMGNHAIETLRSLGKLS-KQARALILEALEAVGLPDPEEvlKKYPFQLSGGMLQRVMIALALLLEPPFLIADEPTTDLD 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1316494952 182 PIGAAAFDQLILTLRDALGLSVFLVTHDLDTLYTITDRVAVLAQKKVL 229
Cdd:TIGR02770 158 VVNQARVLKLLRELRQLFGTGILLITHDLGVVARIADEVAVMDDGRIV 205
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
12-239 |
2.57e-25 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 100.04 E-value: 2.57e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 12 VIEVRGLCNRFGPQSVHENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQNLPSLAEHERSlierRF 91
Cdd:TIGR04406 1 TLVAENLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHLPMHERA----RL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 92 GV--LFQKGALFSSLTVTENVALPLIEHAGLSRADAEHLAaVKLaLAGLPLS-AADKYPASLSGGMIKRAALARALALDP 168
Cdd:TIGR04406 77 GIgyLPQEASIFRKLTVEENIMAVLEIRKDLDRAEREERL-EAL-LEEFQIShLRDNKAMSLSGGERRRVEIARALATNP 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1316494952 169 DILFLDEPTAGLDPIGAAAFDQLILTLRDAlGLSVFLVTHDLDTLYTITDRVAVLAQKKVLVADAIDQVAE 239
Cdd:TIGR04406 155 KFILLDEPFAGVDPIAVGDIKKIIKHLKER-GIGVLITDHNVRETLDICDRAYIISDGKVLAEGTPAEIVA 224
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1-223 |
4.44e-25 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 102.33 E-value: 4.44e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 1 MNRSTRPPaeaVIEVRGLCNRFGPQSVHENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQNLPSL- 79
Cdd:PRK09452 6 KQPSSLSP---LVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVp 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 80 AEHerslieRRFGVLFQKGALFSSLTVTENVALPL----IEHAGLSRADAEHLAAVKLAlaglplSAADKYPASLSGGMI 155
Cdd:PRK09452 83 AEN------RHVNTVFQSYALFPHMTVFENVAFGLrmqkTPAAEITPRVMEALRMVQLE------EFAQRKPHQLSGGQQ 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1316494952 156 KRAALARALALDPDILFLDEPTAGLDPIGAAAFDQLILTLRDALGLSVFLVTHDLDTLYTITDRVAVL 223
Cdd:PRK09452 151 QRVAIARAVVNKPKVLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVM 218
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
13-240 |
5.33e-25 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 99.77 E-value: 5.33e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 13 IEVRGLCNRFGPQSVHENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQNL--PSlaeherslIERr 90
Cdd:PRK11248 2 LQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVegPG--------AER- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 91 fGVLFQKGALFSSLTVTENVALPLiEHAGLSRADAEHLAAVKLALAGLPlSAADKYPASLSGGMIKRAALARALALDPDI 170
Cdd:PRK11248 73 -GVVFQNEGLLPWRNVQDNVAFGL-QLAGVEKMQRLEIAHQMLKKVGLE-GAEKRYIWQLSGGQRQRVGIARALAANPQL 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1316494952 171 LFLDEPTAGLDPIGAAAFDQLILTLRDALGLSVFLVTHDLDTlytitdrvAV-LAQKKVLVADAIDQVAET 240
Cdd:PRK11248 150 LLLDEPFGALDAFTREQMQTLLLKLWQETGKQVLLITHDIEE--------AVfMATELVLLSPGPGRVVER 212
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
30-229 |
5.72e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 100.15 E-value: 5.72e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 30 NLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQnlpSLAEHERSLIERR--FGVLFQK--GALFSSlT 105
Cdd:PRK13639 20 GINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGE---PIKYDKKSLLEVRktVGIVFQNpdDQLFAP-T 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 106 VTENVAL-PLieHAGLSRADAEHlaAVKLALAGLPLSA-ADKYPASLSGGMIKRAALARALALDPDILFLDEPTAGLDPI 183
Cdd:PRK13639 96 VEEDVAFgPL--NLGLSKEEVEK--RVKEALKAVGMEGfENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPM 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1316494952 184 GAAAFDQLILTLRDAlGLSVFLVTHDLDTLYTITDRVAVLAQKKVL 229
Cdd:PRK13639 172 GASQIMKLLYDLNKE-GITIIISTHDVDLVPVYADKVYVMSDGKII 216
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
11-182 |
6.83e-25 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 99.44 E-value: 6.83e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 11 AVIEVRGLCNRFGPQSVHENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQNLPSLA--EHERSLIE 88
Cdd:PRK11264 2 SAIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTARslSQQKGLIR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 89 R---RFGVLFQKGALFSSLTVTENVALPLIEHAGLSRADAEHLAAVKLALAGLPlSAADKYPASLSGGMIKRAALARALA 165
Cdd:PRK11264 82 QlrqHVGFVFQNFNLFPHRTVLENIIEGPVIVKGEPKEEATARARELLAKVGLA-GKETSYPRRLSGGQQQRVAIARALA 160
|
170
....*....|....*..
gi 1316494952 166 LDPDILFLDEPTAGLDP 182
Cdd:PRK11264 161 MRPEVILFDEPTSALDP 177
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
13-228 |
7.08e-25 |
|
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: 97.29 E-value: 7.08e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 13 IEVRGLCNRFG--PQSVHENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQNLPSLAeheRSLIERR 90
Cdd:cd03246 1 LEVENVSFRYPgaEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWD---PNELGDH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 91 FGVLFQKGALFSSlTVTENValpliehaglsradaehlaavklalaglplsaadkypasLSGGMIKRAALARALALDPDI 170
Cdd:cd03246 78 VGYLPQDDELFSG-SIAENI---------------------------------------LSGGQRQRLGLARALYGNPRI 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1316494952 171 LFLDEPTAGLDPIGAAAFDQLILTLRdALGLSVFLVTHDLDTLyTITDRVAVLAQKKV 228
Cdd:cd03246 118 LVLDEPNSHLDVEGERALNQAIAALK-AAGATRIVIAHRPETL-ASADRILVLEDGRV 173
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
13-247 |
7.23e-25 |
|
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: 99.18 E-value: 7.23e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 13 IEVRGLCNRFgPQSVH--ENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQNLPSLAEHERSLIERR 90
Cdd:cd03256 1 IEVENLSKTY-PNGKKalKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLRRQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 91 FGVLFQKGALFSSLTVTENVALPLIEHAGLSRA------DAEHLAAVK-LALAGLpLSAADKYPASLSGGMIKRAALARA 163
Cdd:cd03256 80 IGMIFQQFNLIERLSVLENVLSGRLGRRSTWRSlfglfpKEEKQRALAaLERVGL-LDKAYQRADQLSGGQQQRVAIARA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 164 LALDPDILFLDEPTAGLDPIGAAAFDQLILTLRDALGLSVFLVTHDLDTLYTITDRVAVLAQKKVlVADAIdqVAETDDT 243
Cdd:cd03256 159 LMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRI-VFDGP--PAELTDE 235
|
....
gi 1316494952 244 WIHE 247
Cdd:cd03256 236 VLDE 239
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
8-209 |
8.38e-25 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 98.70 E-value: 8.38e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 8 PAEAVIEVRGLCNRFGpQSVHE-----NLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQNLPSLAEH 82
Cdd:PRK10584 2 PAENIVEVHHLKKSVG-QGEHElsiltGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 83 ERS-LIERRFGVLFQKGALFSSLTVTENVALPLI---EHAGLSRADAEHLaavkLALAGLPlSAADKYPASLSGGMIKRA 158
Cdd:PRK10584 81 ARAkLRAKHVGFVFQSFMLIPTLNALENVELPALlrgESSRQSRNGAKAL----LEQLGLG-KRLDHLPAQLSGGEQQRV 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1316494952 159 ALARALALDPDILFLDEPTAGLDPIGAAAFDQLILTLRDALGLSVFLVTHD 209
Cdd:PRK10584 156 ALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHD 206
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
4-241 |
1.07e-24 |
|
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: 102.54 E-value: 1.07e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 4 STRPPAEAVIEVRGLCNRF--GPQSVHENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQNLPSLAE 81
Cdd:COG4987 325 PAPAPGGPSLELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDE 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 82 HERSlieRRFGVLFQKGALFSSlTVTENVALpliehaGLSRADAEHLAAVkLALAGLpLSAADKYP-----------ASL 150
Cdd:COG4987 405 DDLR---RRIAVVPQRPHLFDT-TLRENLRL------ARPDATDEELWAA-LERVGL-GDWLAALPdgldtwlgeggRRL 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 151 SGGMIKRAALARALALDPDILFLDEPTAGLDPIGAaafDQLILTLRDAL-GLSVFLVTHDLDTLyTITDRVAVLAQKKVL 229
Cdd:COG4987 473 SGGERRRLALARALLRDAPILLLDEPTEGLDAATE---QALLADLLEALaGRTVLLITHRLAGL-ERMDRILVLEDGRIV 548
|
250
....*....|..
gi 1316494952 230 VADAIDQVAETD 241
Cdd:COG4987 549 EQGTHEELLAQN 560
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
12-237 |
1.13e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 99.54 E-value: 1.13e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 12 VIEVRGLCNRFgPQSVH--ENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGsvRVFGQNLPsLAEHERSLIER 89
Cdd:PRK13636 5 ILKVEELNYNY-SDGTHalKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSG--RILFDGKP-IDYSRKGLMKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 90 R--FGVLFQK--GALFSSLTVTE------NVALP------LIEHAgLSRADAEHLAavklalaglplsaaDKYPASLSGG 153
Cdd:PRK13636 81 ResVGMVFQDpdNQLFSASVYQDvsfgavNLKLPedevrkRVDNA-LKRTGIEHLK--------------DKPTHCLSFG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 154 MIKRAALARALALDPDILFLDEPTAGLDPIGAAAFDQLILTLRDALGLSVFLVTHDLDTLYTITDRVAVLAQKKVLVADA 233
Cdd:PRK13636 146 QKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGN 225
|
....
gi 1316494952 234 IDQV 237
Cdd:PRK13636 226 PKEV 229
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
10-228 |
1.21e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 99.42 E-value: 1.21e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 10 EAVIEVRGLCNRFGPQSVHENLD---LDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQnlpSLAEHERSL 86
Cdd:PRK13650 2 SNIIEVKNLTFKYKEDQEKYTLNdvsFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGD---LLTEENVWD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 87 IERRFGVLFQK-GALFSSLTVTENVALPLiEHAGLSRADAEHLAAVKLALAGLpLSAADKYPASLSGGMIKRAALARALA 165
Cdd:PRK13650 79 IRHKIGMVFQNpDNQFVGATVEDDVAFGL-ENKGIPHEEMKERVNEALELVGM-QDFKEREPARLSGGQKQRVAIAGAVA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1316494952 166 LDPDILFLDEPTAGLDPIGAAAFDQLILTLRDALGLSVFLVTHDLDTLyTITDRVAVLAQKKV 228
Cdd:PRK13650 157 MRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEV-ALSDRVLVMKNGQV 218
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
31-246 |
1.29e-24 |
|
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: 100.57 E-value: 1.29e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 31 LDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQNLPSLAEHERSLIE-RRFGVLFQKGALFSSLTVTEN 109
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKGIFLPPEkRRIGYVFQEARLFPHLSVRGN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 110 VALpliehaGLSRADAEHLAAVK---LALAGL-PLsaADKYPASLSGGMIKRAALARALALDPDILFLDEPTAGLDPIGA 185
Cdd:TIGR02142 96 LRY------GMKRARPSERRISFervIELLGIgHL--LGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRK 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1316494952 186 AAFDQLILTLRDALGLSVFLVTHDLDTLYTITDRVAVLAQKKVLVADAIDQVAETDD-TWIH 246
Cdd:TIGR02142 168 YEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPDlPWLA 229
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
12-237 |
1.61e-24 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 99.41 E-value: 1.61e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 12 VIEVRGLCNRFGPQSVHENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQnlpSLAEHERslieRRF 91
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGE---PLDPEDR----RRI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 92 GVLFQKGALFSSLTVTENvalpLIEHA---GLSRADAEHLAAVKLALAGLPLSAADKYpASLSGGMIKRAALARALALDP 168
Cdd:COG4152 74 GYLPEERGLYPKMKVGEQ----LVYLArlkGLSKAEAKRRADEWLERLGLGDRANKKV-EELSKGNQQKVQLIAALLHDP 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1316494952 169 DILFLDEPTAGLDPIGAAAFDQLILTLRDAlGLSVFLVTHDLDTLYTITDRVAVLAQKKVLVADAIDQV 237
Cdd:COG4152 149 ELLILDEPFSGLDPVNVELLKDVIRELAAK-GTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEI 216
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
10-242 |
2.17e-24 |
|
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: 97.75 E-value: 2.17e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 10 EAVIEVRGLCNRFGPQSVHENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQNLPSLAEHERSlier 89
Cdd:COG0410 1 MPMLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIA---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 90 RFGVLF--QKGALFSSLTVTENVALPLIeHAGLSRADAEHLAAV-----KLA-----LAGlplsaadkypaSLSGG---- 153
Cdd:COG0410 77 RLGIGYvpEGRRIFPSLTVEENLLLGAY-ARRDRAEVRADLERVyelfpRLKerrrqRAG-----------TLSGGeqqm 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 154 -------MikraalaralaLDPDILFLDEPTAGLDPIGAAAFDQLILTLRDAlGLSVFLVTHDLDTLYTITDRVAVLAQK 226
Cdd:COG0410 145 laigralM-----------SRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNRE-GVTILLVEQNARFALEIADRAYVLERG 212
|
250
....*....|....*.
gi 1316494952 227 KVLVADAIDQVAETDD 242
Cdd:COG0410 213 RIVLEGTAAELLADPE 228
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
32-223 |
3.81e-24 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 99.01 E-value: 3.81e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 32 DLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQNLPSLAEHERSLIERRFGVLFQK--GALFSSLTVTEN 109
Cdd:PRK15079 41 TLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRAVRSDIQMIFQDplASLNPRMTIGEI 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 110 VALPL-IEHAGLSRADAEHLAAVKLALAGLPLSAADKYPASLSGGMIKRAALARALALDPDILFLDEPTAGLDPIGAAAF 188
Cdd:PRK15079 121 IAEPLrTYHPKLSRQEVKDRVKAMMLKVGLLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQV 200
|
170 180 190
....*....|....*....|....*....|....*
gi 1316494952 189 DQLILTLRDALGLSVFLVTHDLDTLYTITDRVAVL 223
Cdd:PRK15079 201 VNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVM 235
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
14-211 |
4.05e-24 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 96.40 E-value: 4.05e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 14 EVRGLCNRFGPQSVHENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQP---SEGSVRVFGQNLPSLAEHERslierR 90
Cdd:COG4136 3 SLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLTALPAEQR-----R 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 91 FGVLFQKGALFSSLTVTENV--ALPliehAGLSRADAEHLAAVKLALAGLPlSAADKYPASLSGGMIKRAALARALALDP 168
Cdd:COG4136 78 IGILFQDDLLFPHLSVGENLafALP----PTIGRAQRRARVEQALEEAGLA-GFADRDPATLSGGQRARVALLRALLAEP 152
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1316494952 169 DILFLDEPTAGLDPIGAAAFDQLILTLRDALGLSVFLVTHDLD 211
Cdd:COG4136 153 RALLLDEPFSKLDAALRAQFREFVFEQIRQRGIPALLVTHDEE 195
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
13-229 |
4.09e-24 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 99.02 E-value: 4.09e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 13 IEVRGLCNRFGPQSVHENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQNLPslaehERSLIERRFG 92
Cdd:PRK11432 7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVT-----HRSIQQRDIC 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 93 VLFQKGALFSSLTVTENVALPLiehAGLSRADAEHLAAVKLALAGLPLSA-ADKYPASLSGGMIKRAALARALALDPDIL 171
Cdd:PRK11432 82 MVFQSYALFPHMSLGENVGYGL---KMLGVPKEERKQRVKEALELVDLAGfEDRYVDQISGGQQQRVALARALILKPKVL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1316494952 172 FLDEPTAGLDPIGAAAFDQLILTLRDALGLSVFLVTHDLDTLYTITDRVAVLAQKKVL 229
Cdd:PRK11432 159 LFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIM 216
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-228 |
9.77e-24 |
|
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: 99.83 E-value: 9.77e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 2 NRSTRPPAEAVIEVRGLCNRFGP-QSVHENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQNLPSLA 80
Cdd:COG4988 326 TAPLPAAGPPSIELEDVSFSYPGgRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLD 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 81 EHERSlieRRFGVLFQKGALFSSlTVTENVALpliehaGLSRADAEHLAAVkLALAGLpLSAADKYP-----------AS 149
Cdd:COG4988 406 PASWR---RQIAWVPQNPYLFAG-TIRENLRL------GRPDASDEELEAA-LEAAGL-DEFVAALPdgldtplgeggRG 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 150 LSGG----------MIKraalaralalDPDILFLDEPTAGLDPIGAAAFDQLILTLrdALGLSVFLVTHDLDTLyTITDR 219
Cdd:COG4988 474 LSGGqaqrlalaraLLR----------DAPLLLLDEPTAHLDAETEAEILQALRRL--AKGRTVILITHRLALL-AQADR 540
|
....*....
gi 1316494952 220 VAVLAQKKV 228
Cdd:COG4988 541 ILVLDDGRI 549
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
13-229 |
1.18e-23 |
|
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: 94.95 E-value: 1.18e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 13 IEVRGLCNRFGPQSVHENLDLDLYKGeILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQNLPSlaehERSLIERRFG 92
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLK----QPQKLRRRIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 93 VLFQKGALFSSLTVTENVALPLIEHaGLSRADAEHLAAVKLALAGLpLSAADKYPASLSGGMIKRAALARALALDPDILF 172
Cdd:cd03264 76 YLPQEFGVYPNFTVREFLDYIAWLK-GIPSKEVKARVDEVLELVNL-GDRAKKKIGSLSGGMRRRVGIAQALVGDPSILI 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1316494952 173 LDEPTAGLDPIGAAAFDQLILTLrdALGLSVFLVTHDLDTLYTITDRVAVLAQKKVL 229
Cdd:cd03264 154 VDEPTAGLDPEERIRFRNLLSEL--GEDRIVILSTHIVEDVESLCNQVAVLNKGKLV 208
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
13-210 |
1.29e-23 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 96.31 E-value: 1.29e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 13 IEVRGLCNRFGPQSVHE-----NLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQNLPSLAEHERSli 87
Cdd:COG1101 2 LELKNLSKTFNPGTVNEkraldGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRA-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 88 eRRFGVLFQ---KGAlFSSLTVTENVALPLI--EHAGLSRA-DAEHLAAVKLALAGLPLSAADKYPA---SLSGG----- 153
Cdd:COG1101 80 -KYIGRVFQdpmMGT-APSMTIEENLALAYRrgKRRGLRRGlTKKRRELFRELLATLGLGLENRLDTkvgLLSGGqrqal 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1316494952 154 ---MikraalarALALDPDILFLDEPTAGLDPIGAAafdqLILTLRDAL----GLSVFLVTHDL 210
Cdd:COG1101 158 sllM--------ATLTKPKLLLLDEHTAALDPKTAA----LVLELTEKIveenNLTTLMVTHNM 209
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
13-237 |
1.32e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 96.66 E-value: 1.32e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 13 IEVRGLCNRFGPQSVHE-----NLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQNLpslAEHERSL- 86
Cdd:PRK13637 3 IKIENLTHIYMEGTPFEkkaldNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDI---TDKKVKLs 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 87 -IERRFGVLFQ--KGALFSSlTVTENVALPLIeHAGLSRADAEHLAAVKLALAGLPLSA-ADKYPASLSGGMIKRAALAR 162
Cdd:PRK13637 80 dIRKKVGLVFQypEYQLFEE-TIEKDIAFGPI-NLGLSEEEIENRVKRAMNIVGLDYEDyKDKSPFELSGGQKRRVAIAG 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1316494952 163 ALALDPDILFLDEPTAGLDPIGAAAFDQLILTLRDALGLSVFLVTHDLDTLYTITDRVAVLAQKKVLVADAIDQV 237
Cdd:PRK13637 158 VVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREV 232
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
18-210 |
1.41e-23 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 95.27 E-value: 1.41e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 18 LCNRFGPQSVH----ENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQNLPSLAEHERS-LIERRFG 92
Cdd:PRK11629 11 LCKRYQEGSVQtdvlHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAeLRNQKLG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 93 VLFQKGALFSSLTVTENVALPLIEhAGLSRADAEHLAAVKLALAGLPLSAADKyPASLSGGMIKRAALARALALDPDILF 172
Cdd:PRK11629 91 FIYQFHHLLPDFTALENVAMPLLI-GKKKPAEINSRALEMLAAVGLEHRANHR-PSELSGGERQRVAIARALVNNPRLVL 168
|
170 180 190
....*....|....*....|....*....|....*...
gi 1316494952 173 LDEPTAGLDPIGAAAFDQLILTLRDALGLSVFLVTHDL 210
Cdd:PRK11629 169 ADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDL 206
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
22-225 |
1.75e-23 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 94.94 E-value: 1.75e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 22 FGPQSVHENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQNLPSLAEHERSLIERRFGVLFQKGALF 101
Cdd:PRK10908 12 LGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPFLRRQIGMIFQDHHLL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 102 SSLTVTENVALPLIEhAGLSRADAEHLAAVKLALAGLpLSAADKYPASLSGGMIKRAALARALALDPDILFLDEPTAGLD 181
Cdd:PRK10908 92 MDRTVYDNVAIPLII-AGASGDDIRRRVSAALDKVGL-LDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLD 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1316494952 182 pigaAAFDQLILTLRDA---LGLSVFLVTHDLDTLYTITDRVAVLAQ 225
Cdd:PRK10908 170 ----DALSEGILRLFEEfnrVGVTVLMATHDIGLISRRSYRMLTLSD 212
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
32-237 |
2.24e-23 |
|
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: 97.09 E-value: 2.24e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 32 DLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQ---------NLPSlaehERslieRRFGVLFQKGALFS 102
Cdd:COG4148 19 DFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEvlqdsargiFLPP----HR----RRIGYVFQEARLFP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 103 SLTVTENVA-----LPliehAGLSRADAEHLAAVkLALAGLplsaADKYPASLSGG-----------MIkraalaralal 166
Cdd:COG4148 91 HLSVRGNLLygrkrAP----RAERRISFDEVVEL-LGIGHL----LDRRPATLSGGerqrvaigralLS----------- 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1316494952 167 DPDILFLDEPTAGLDpigaAAFDQLIL----TLRDALGLSVFLVTHDLDTLYTITDRVAVLAQKKVLVADAIDQV 237
Cdd:COG4148 151 SPRLLLMDEPLAALD----LARKAEILpyleRLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEV 221
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
4-241 |
3.94e-23 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 97.81 E-value: 3.94e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 4 STRPPaeaVIEVRGLCNRFGPQSVHENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQNL----PSL 79
Cdd:PRK15439 6 TTAPP---LLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCarltPAK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 80 AEherslierRFGVLF--QKGALFSSLTVTENVALPLIEHAGLSRADAEHLAA----VKLALAGLPLSAADKYPASLSGG 153
Cdd:PRK15439 83 AH--------QLGIYLvpQEPLLFPNLSVKENILFGLPKRQASMQKMKQLLAAlgcqLDLDSSAGSLEVADRQIVEILRG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 154 MIKraalaralalDPDILFLDEPTAGLDPIGAAAFDQLILTLRDaLGLSVFLVTHDLDTLYTITDRVAVLAQKKVLVADA 233
Cdd:PRK15439 155 LMR----------DSRILILDEPTASLTPAETERLFSRIRELLA-QGVGIVFISHKLPEIRQLADRISVMRDGTIALSGK 223
|
....*...
gi 1316494952 234 IDQVAETD 241
Cdd:PRK15439 224 TADLSTDD 231
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
29-251 |
4.51e-23 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 97.03 E-value: 4.51e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 29 ENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQNLPSLAEHE-RSLIERRFGVLFQKGALFSSLTVT 107
Cdd:PRK10070 45 KDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAElREVRRKKIAMVFQSFALMPHMTVL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 108 ENVALPLiEHAGLSRADAEHLAAVKLALAGLPlSAADKYPASLSGGMIKRAALARALALDPDILFLDEPTAGLDPIGAAA 187
Cdd:PRK10070 125 DNTAFGM-ELAGINAEERREKALDALRQVGLE-NYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTE 202
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1316494952 188 FDQLILTLRDALGLSVFLVTHDLDTLYTITDRVAVLAQKKVLVADAIDQVAETD-DTWIHEYFHG 251
Cdd:PRK10070 203 MQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPaNDYVRTFFRG 267
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
13-229 |
5.32e-23 |
|
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: 93.59 E-value: 5.32e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 13 IEVRGLCNRFGPQSVH----ENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQNlpslAEHERSLIE 88
Cdd:cd03266 2 ITADALTKRFRDVKKTvqavDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFD----VVKEPAEAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 89 RRFGVLFQKGALFSSLTVTENVALPLIEHaGLSRADAEhlAAVKLALAGLPLSA-ADKYPASLSGGMIKRAALARALALD 167
Cdd:cd03266 78 RRLGFVSDSTGLYDRLTARENLEYFAGLY-GLKGDELT--ARLEELADRLGMEElLDRRVGGFSTGMRQKVAIARALVHD 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1316494952 168 PDILFLDEPTAGLDPIGAAAFDQLILTLRDAlGLSVFLVTHDLDTLYTITDRVAVLAQKKVL 229
Cdd:cd03266 155 PPVLLLDEPTTGLDVMATRALREFIRQLRAL-GKCILFSTHIMQEVERLCDRVVVLHRGRVV 215
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
10-239 |
8.04e-23 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 93.56 E-value: 8.04e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 10 EAVIEVRGLCNRFGPQSVHENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQNLPSLAEHERSlier 89
Cdd:COG1137 1 MMTLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMHKRA---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 90 RFGV--LFQKGALFSSLTVTENVALPLiEHAGLSRADAEHLAAVKLA---LAGLplsaADKYPASLSGG----------M 154
Cdd:COG1137 77 RLGIgyLPQEASIFRKLTVEDNILAVL-ELRKLSKKEREERLEELLEefgITHL----RKSKAYSLSGGerrrveiaraL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 155 IkraalaralaLDPDILFLDEPTAGLDPIGAAAFDQLILTLRDAlGLSVfLVT-HDL-DTLyTITDRVAVLAQKKVLVAD 232
Cdd:COG1137 152 A----------TNPKFILLDEPFAGVDPIAVADIQKIIRHLKER-GIGV-LITdHNVrETL-GICDRAYIISEGKVLAEG 218
|
....*..
gi 1316494952 233 AIDQVAE 239
Cdd:COG1137 219 TPEEILN 225
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
31-211 |
1.42e-22 |
|
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 130234 [Multi-domain] Cd Length: 190 Bit Score: 91.72 E-value: 1.42e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 31 LDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQnlpSLAEHERSLIERR--FGVLFQ--KGALFSSlTV 106
Cdd:TIGR01166 11 LNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGE---PLDYSRKGLLERRqrVGLVFQdpDDQLFAA-DV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 107 TENVALPLIeHAGLSRADAEhlAAVKLALAGLPLSA-ADKYPASLSGGMIKRAALARALALDPDILFLDEPTAGLDPIGA 185
Cdd:TIGR01166 87 DQDVAFGPL-NLGLSEAEVE--RRVREALTAVGASGlRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAGLDPAGR 163
|
170 180
....*....|....*....|....*.
gi 1316494952 186 AAFDQLILTLRDAlGLSVFLVTHDLD 211
Cdd:TIGR01166 164 EQMLAILRRLRAE-GMTVVISTHDVD 188
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
13-223 |
4.16e-22 |
|
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: 89.80 E-value: 4.16e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 13 IEVRGLCNRFGPQSVHENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQ--NLPSLAEHERSLIerr 90
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKevSFASPRDARRAGI--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 91 fGVLFQkgalfssltvtenvalpliehagLSRADAEHLAAVKlALAGlplsaadkypaslsggmikraalaralalDPDI 170
Cdd:cd03216 78 -AMVYQ-----------------------LSVGERQMVEIAR-ALAR-----------------------------NARL 103
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1316494952 171 LFLDEPTAGLDPIGAAAFDQLILTLRDAlGLSVFLVTHDLDTLYTITDRVAVL 223
Cdd:cd03216 104 LILDEPTAALTPAEVERLFKVIRRLRAQ-GVAVIFISHRLDEVFEIADRVTVL 155
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-223 |
4.19e-22 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 93.36 E-value: 4.19e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 1 MNRSTRPPAEAVIEVRGLCNRFGPQSVHENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQNLPSLA 80
Cdd:PRK13536 30 KASIPGSMSTVAIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 81 EHERslieRRFGVLFQKGALFSSLTVTENVaLPLIEHAGLSRADAEHLAAVKLALAGLPlSAADKYPASLSGGMIKRAAL 160
Cdd:PRK13536 110 RLAR----ARIGVVPQFDNLDLEFTVRENL-LVFGRYFGMSTREIEAVIPSLLEFARLE-SKADARVSDLSGGMKRRLTL 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1316494952 161 ARALALDPDILFLDEPTAGLDPIGAaafdQLILT-LRD--ALGLSVFLVTHDLDTLYTITDRVAVL 223
Cdd:PRK13536 184 ARALINDPQLLILDEPTTGLDPHAR----HLIWErLRSllARGKTILLTTHFMEEAERLCDRLCVL 245
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1-237 |
4.70e-22 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 95.31 E-value: 4.70e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 1 MNRSTRPPAEAVIEVRGLCNRF----GPQSVHENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSV------- 69
Cdd:PRK10261 1 MPHSDELDARDVLAVENLNIAFmqeqQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVqcdkmll 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 70 RVFGQNLPSLAEHERSLIERRFG----VLFQK--GALFSSLTVTENVALPLIEHAGLSRADAEHLAAVKLALAGLPLSAA 143
Cdd:PRK10261 81 RRRSRQVIELSEQSAAQMRHVRGadmaMIFQEpmTSLNPVFTVGEQIAESIRLHQGASREEAMVEAKRMLDQVRIPEAQT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 144 --DKYPASLSGGMIKRAALARALALDPDILFLDEPTAGLDPIGAAAFDQLILTLRDALGLSVFLVTHDLDTLYTITDRVA 221
Cdd:PRK10261 161 ilSRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVL 240
|
250
....*....|....*.
gi 1316494952 222 VLAQKKVLVADAIDQV 237
Cdd:PRK10261 241 VMYQGEAVETGSVEQI 256
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
10-220 |
7.53e-22 |
|
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: 90.57 E-value: 7.53e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 10 EAVIEVRGLCNRF------GPQ-SVHENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRV---FGQ-NLPS 78
Cdd:COG4778 2 TTLLEVENLSKTFtlhlqgGKRlPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrhdGGWvDLAQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 79 LAEHErsLIE-RRFG---------VLFQKGALfssltvtENVALPLIEhAGLSRADAEHLAAVKLALAGLPLSAADKYPA 148
Cdd:COG4778 82 ASPRE--ILAlRRRTigyvsqflrVIPRVSAL-------DVVAEPLLE-RGVDREEARARARELLARLNLPERLWDLPPA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 149 SLSGG----------MIKraalaralalDPDILFLDEPTAGLDPIGAAAFDQLILTLRDAlGLSVFLVTHDLDTLYTITD 218
Cdd:COG4778 152 TFSGGeqqrvniargFIA----------DPPLLLLDEPTASLDAANRAVVVELIEEAKAR-GTAIIGIFHDEEVREAVAD 220
|
..
gi 1316494952 219 RV 220
Cdd:COG4778 221 RV 222
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
13-236 |
9.53e-22 |
|
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: 90.15 E-value: 9.53e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 13 IEVRGLCNRFGPQSVHENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQnlpslaEHERSLIeRRFG 92
Cdd:TIGR03740 1 LETKNLSKRFGKQTAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGH------PWTRKDL-HKIG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 93 VLFQKGALFSSLTVTENVAL-PLIEHAGLSRADaEHLAAVKLALAGlplsaadKYPAS-LSGGMIKRAALARALALDPDI 170
Cdd:TIGR03740 74 SLIESPPLYENLTARENLKVhTTLLGLPDSRID-EVLNIVDLTNTG-------KKKAKqFSLGMKQRLGIAIALLNHPKL 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1316494952 171 LFLDEPTAGLDPIGAAAFDQLILTLRDAlGLSVFLVTHDLDTLYTITDRVAVLAQKKVLVADAIDQ 236
Cdd:TIGR03740 146 LILDEPTNGLDPIGIQELRELIRSFPEQ-GITVILSSHILSEVQQLADHIGIISEGVLGYQGKINK 210
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
29-229 |
1.15e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 91.61 E-value: 1.15e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 29 ENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQNLPSLAEH--ERSLIERRFGVLFQ--KGALFSSl 104
Cdd:PRK13645 28 NNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPANLKKikEVKRLRKEIGLVFQfpEYQLFQE- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 105 TVTENVALPLIeHAGLSRADAEHLAAVKLALAGLPLSAADKYPASLSGGMIKRAALARALALDPDILFLDEPTAGLDPIG 184
Cdd:PRK13645 107 TIEKDIAFGPV-NLGENKQEAYKKVPELLKLVQLPEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKG 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1316494952 185 AAAFDQLILTLRDALGLSVFLVTHDLDTLYTITDRVAVLAQKKVL 229
Cdd:PRK13645 186 EEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVI 230
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
21-220 |
1.42e-21 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 88.83 E-value: 1.42e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 21 RFGPQSVHENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGqnlpslaehersliERRFGVLFQKGAL 100
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG--------------GARVAYVPQRSEV 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 101 FSSL--TVTENVALPLIEHAGLSRA-DAEHLAAVKLALAGLPLSAADKYP-ASLSGGMIKRAALARALALDPDILFLDEP 176
Cdd:NF040873 67 PDSLplTVRDLVAMGRWARRGLWRRlTRDDRAAVDDALERVGLADLAGRQlGELSGGQRQRALLAQGLAQEADLLLLDEP 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1316494952 177 TAGLDPIGAAAFDQLILTLRDAlGLSVFLVTHDLDTLYTITDRV 220
Cdd:NF040873 147 TTGLDAESRERIIALLAEEHAR-GATVVVVTHDLELVRRADPCV 189
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
10-228 |
2.04e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 90.44 E-value: 2.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 10 EAVIEVRGLCNRFGPQS--VHENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQNLPSlaeHERSLI 87
Cdd:PRK13632 5 SVMIKVENVSFSYPNSEnnALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISK---ENLKEI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 88 ERRFGVLFQK-GALFSSLTVTENVALPLiEHAGLSRADA----EHLAAVklalAGLpLSAADKYPASLSGGMIKRAALAR 162
Cdd:PRK13632 82 RKKIGIIFQNpDNQFIGATVEDDIAFGL-ENKKVPPKKMkdiiDDLAKK----VGM-EDYLDKEPQNLSGGQKQRVAIAS 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1316494952 163 ALALDPDILFLDEPTAGLDPIGAAAFDQLILTLRDALGLSVFLVTHDLDTLyTITDRVAVLAQKKV 228
Cdd:PRK13632 156 VLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEA-ILADKVIVFSEGKL 220
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
11-223 |
3.30e-21 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 91.24 E-value: 3.30e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 11 AVIEVRGLCNRFGPQSVHENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQNLPSLAEHERSLierr 90
Cdd:PRK11000 2 ASVTLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAERGV---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 91 fGVLFQKGALFSSLTVTENVALPLiEHAGLSRADA----EHLAAVkLALAGLplsaADKYPASLSGGMIKRAALARALAL 166
Cdd:PRK11000 78 -GMVFQSYALYPHLSVAENMSFGL-KLAGAKKEEInqrvNQVAEV-LQLAHL----LDRKPKALSGGQRQRVAIGRTLVA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 167 DPDILFLDEPTAGLDpigAAAFDQL---ILTLRDALGLSVFLVTHDLDTLYTITDRVAVL 223
Cdd:PRK11000 151 EPSVFLLDEPLSNLD---AALRVQMrieISRLHKRLGRTMIYVTHDQVEAMTLADKIVVL 207
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
11-237 |
5.54e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 88.82 E-value: 5.54e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 11 AVIEVRGLCNRFGPQSVHENLDLDLYKGEILAVVGGSGSGKSVLLR---SIIGLRQPS--EGSVRVFGQNLPSLaehERS 85
Cdd:PRK14247 2 NKIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRvfnRLIELYPEArvSGEVYLDGQDIFKM---DVI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 86 LIERRFGVLFQKGALFSSLTVTENVALPLiEHAGLSRADAEHLAAVKLALAGLPL-----SAADKYPASLSGGMIKRAAL 160
Cdd:PRK14247 79 ELRRRVQMVFQIPNPIPNLSIFENVALGL-KLNRLVKSKKELQERVRWALEKAQLwdevkDRLDAPAGKLSGGQQQRLCI 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1316494952 161 ARALALDPDILFLDEPTAGLDPIGAAAFDQLILTLRDAlgLSVFLVTHDLDTLYTITDRVAVLAQKKVLVADAIDQV 237
Cdd:PRK14247 158 ARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKD--MTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREV 232
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
4-210 |
6.23e-21 |
|
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: 91.65 E-value: 6.23e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 4 STRPPAEAVIEVRGLCNRFGPQS-VHENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQNLPSLAEH 82
Cdd:TIGR02868 326 GAVGLGKPTLELRDLSAGYPGAPpVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQD 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 83 ErslIERRFGVLFQKGALFSSlTVTENVALPLIEHAGLSRADAehLAAVKLA--LAGLPLSAADKY---PASLSGGMIKR 157
Cdd:TIGR02868 406 E---VRRRVSVCAQDAHLFDT-TVRENLRLARPDATDEELWAA--LERVGLAdwLRALPDGLDTVLgegGARLSGGERQR 479
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1316494952 158 AALARALALDPDILFLDEPTAGLDPIGAaafDQLILTLRDAL-GLSVFLVTHDL 210
Cdd:TIGR02868 480 LALARALLADAPILLLDEPTEHLDAETA---DELLEDLLAALsGRTVVLITHHL 530
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
16-223 |
6.41e-21 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 90.02 E-value: 6.41e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 16 RGLcnrFGPQSVHENLD---LDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQNLPSLAEHERSLIERRFG 92
Cdd:PRK11308 19 RGL---FKPERLVKALDgvsFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAQKLLRQKIQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 93 VLFQKGalFSSL----TVTENVALPLIEHAGLSRADAEHLAAVKLALAGLPLSAADKYPASLSGGMIKRAALARALALDP 168
Cdd:PRK11308 96 IVFQNP--YGSLnprkKVGQILEEPLLINTSLSAAERREKALAMMAKVGLRPEHYDRYPHMFSGGQRQRIAIARALMLDP 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1316494952 169 DILFLDEPTAGLDPIGAAAFDQLILTLRDALGLSVFLVTHDLDTLYTITDRVAVL 223
Cdd:PRK11308 174 DVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVM 228
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
12-242 |
6.61e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 89.09 E-value: 6.61e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 12 VIEVRGLCNRF-GPQSVHENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQNLPSLAEHErslIERR 90
Cdd:PRK13652 3 LIETRDLCYSYsGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIRE---VRKF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 91 FGVLFQK--GALFSSlTVTENVALPLIeHAGLSRADAEHLAAVKLALAGLPlSAADKYPASLSGGMIKRAALARALALDP 168
Cdd:PRK13652 80 VGLVFQNpdDQIFSP-TVEQDIAFGPI-NLGLDEETVAHRVSSALHMLGLE-ELRDRVPHHLSGGEKKRVAIAGVIAMEP 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1316494952 169 DILFLDEPTAGLDPIGAAAFDQLILTLRDALGLSVFLVTHDLDTLYTITDRVAVLAQKKVLVADAIDQVAETDD 242
Cdd:PRK13652 157 QVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQPD 230
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
12-245 |
8.72e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 89.00 E-value: 8.72e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 12 VIEVRGLCNRFGPQSVHENLD---LDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQNLPslAEHERSLiE 88
Cdd:PRK13642 4 ILEVENLVFKYEKESDVNQLNgvsFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLT--AENVWNL-R 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 89 RRFGVLFQK-GALFSSLTVTENVALPLiEHAGLSRADA-----EHLAAVKLalaglpLSAADKYPASLSGGMIKRAALAR 162
Cdd:PRK13642 81 RKIGMVFQNpDNQFVGATVEDDVAFGM-ENQGIPREEMikrvdEALLAVNM------LDFKTREPARLSGGQKQRVAVAG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 163 ALALDPDILFLDEPTAGLDPIGAAAFDQLILTLRDALGLSVFLVTHDLDTLYTiTDRVAVLAQKKVLVADAIDQVAETDD 242
Cdd:PRK13642 154 IIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELFATSE 232
|
...
gi 1316494952 243 TWI 245
Cdd:PRK13642 233 DMV 235
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
13-229 |
1.05e-20 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 87.76 E-value: 1.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 13 IEVRGLCNRFGPQSVHENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQNL---PSLAEHERSLIER 89
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFdfsKTPSDKAIRELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 90 RFGVLFQKGALFSSLTVTENvalpLIEH----AGLSRADAeHLAAVKLaLAGLPLSA-ADKYPASLSGGMIKRAALARAL 164
Cdd:PRK11124 83 NVGMVFQQYNLWPHLTVQQN----LIEApcrvLGLSKDQA-LARAEKL-LERLRLKPyADRFPLHLSGGQQQRVAIARAL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1316494952 165 ALDPDILFLDEPTAGLDPIGAAAFDQLILTLRDAlGLSVFLVTHDLDTLYTITDRVAVLAQKKVL 229
Cdd:PRK11124 157 MMEPQVLLFDEPTAALDPEITAQIVSIIRELAET-GITQVIVTHEVEVARKTASRVVYMENGHIV 220
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
12-229 |
1.86e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 87.87 E-value: 1.86e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 12 VIEVRGL--CNRFGPQSVhENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQNLPSLAEHErslIER 89
Cdd:PRK13647 4 IIEVEDLhfRYKDGTKAL-KGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKW---VRS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 90 RFGVLFQK--GALFSSlTVTENVAL-PLieHAGLSRADAEHLAAVKLALAGLpLSAADKYPASLSGGMIKRAALARALAL 166
Cdd:PRK13647 80 KVGLVFQDpdDQVFSS-TVWDDVAFgPV--NMGLDKDEVERRVEEALKAVRM-WDFRDKPPYHLSYGQKKRVAIAGVLAM 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1316494952 167 DPDILFLDEPTAGLDPIGAAAFDQlILTLRDALGLSVFLVTHDLDTLYTITDRVAVLAQKKVL 229
Cdd:PRK13647 156 DPDVIVLDEPMAYLDPRGQETLME-ILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVL 217
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
27-209 |
2.05e-20 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 90.17 E-value: 2.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 27 VHENLDLDLYKGEILAVVGGSGSGKSVLLrSIIG-LRQPSEGSVRVFGQNLPSLAEHERSLIERR-FGVLFQKGALFSSL 104
Cdd:PRK10535 23 VLKGISLDIYAGEMVAIVGASGSGKSTLM-NILGcLDKPTSGTYRVAGQDVATLDADALAQLRREhFGFIFQRYHLLSHL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 105 TVTENVALPLIeHAGLSRADAEHLAAVKLALAGLPlSAADKYPASLSGGMIKRAALARALALDPDILFLDEPTAGLDPIG 184
Cdd:PRK10535 102 TAAQNVEVPAV-YAGLERKQRLLRAQELLQRLGLE-DRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDSHS 179
|
170 180
....*....|....*....|....*
gi 1316494952 185 AAAFDQLILTLRDAlGLSVFLVTHD 209
Cdd:PRK10535 180 GEEVMAILHQLRDR-GHTVIIVTHD 203
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
32-228 |
2.14e-20 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 86.94 E-value: 2.14e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 32 DLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQNlpslaeHERSLIERR-FGVLFQKGALFSSLTVTENV 110
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQD------HTTTPPSRRpVSMLFQENNLFSHLTVAQNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 111 ALPLieHAGLsRADAEHLAAVKLALAGLPLSAA-DKYPASLSGGMIKRAALARALALDPDILFLDEPTAGLDPigaaAFD 189
Cdd:PRK10771 93 GLGL--NPGL-KLNAAQREKLHAIARQMGIEDLlARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDP----ALR 165
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1316494952 190 QLILTLRDAL----GLSVFLVTHDLDTLYTITDRVAVLAQKKV 228
Cdd:PRK10771 166 QEMLTLVSQVcqerQLTLLMVSHSLEDAARIAPRSLVVADGRI 208
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
13-221 |
2.71e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 87.40 E-value: 2.71e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 13 IEVRGLCNRFGPQSVHENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPS-----EGSVRVFGQNLpslaeHERSL- 86
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELEsevrvEGRVEFFNQNI-----YERRVn 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 87 ---IERRFGVLFQKGALFSsLTVTENVAL--------PLIEHAGLSRA---DAEHLAAVKLALaglplsaaDKYPASLSG 152
Cdd:PRK14258 83 lnrLRRQVSMVHPKPNLFP-MSVYDNVAYgvkivgwrPKLEIDDIVESalkDADLWDEIKHKI--------HKSALDLSG 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1316494952 153 GMIKRAALARALALDPDILFLDEPTAGLDPIGAAAFDQLILTLRDALGLSVFLVTHDLDTLYTITDRVA 221
Cdd:PRK14258 154 GQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTA 222
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
8-223 |
4.23e-20 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 89.53 E-value: 4.23e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 8 PAEAVIEVRGLCNRFGPQS---------VH--ENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQNL 76
Cdd:PRK10261 309 DGEPILQVRNLVTRFPLRSgllnrvtreVHavEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRI 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 77 PSLAEHERSLIERRFGVLFQK--GALFSSLTVTENVALPLIEHAGLSRADAEHLAAVKLALAGLPLSAADKYPASLSGGM 154
Cdd:PRK10261 389 DTLSPGKLQALRRDIQFIFQDpyASLDPRQTVGDSIMEPLRVHGLLPGKAAAARVAWLLERVGLLPEHAWRYPHEFSGGQ 468
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1316494952 155 IKRAALARALALDPDILFLDEPTAGLDPIGAAAFDQLILTLRDALGLSVFLVTHDLDTLYTITDRVAVL 223
Cdd:PRK10261 469 RQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVM 537
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
10-221 |
6.77e-20 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 85.98 E-value: 6.77e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 10 EAVIEVRGLCNRFGPQSVHENLDLDLYKGEILAVVGGSGSGKSVLLRSI--IGLRQPS---EGSVRVFGQNLPSlAEHER 84
Cdd:PRK14239 3 EPILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDLNPEvtiTGSIVYNGHNIYS-PRTDT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 85 SLIERRFGVLFQKGALFSsLTVTENVALPLiEHAGLSraDAEHL-AAVKLALAGLPL--SAADKYPAS---LSGGMIKRA 158
Cdd:PRK14239 82 VDLRKEIGMVFQQPNPFP-MSIYENVVYGL-RLKGIK--DKQVLdEAVEKSLKGASIwdEVKDRLHDSalgLSGGQQQRV 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1316494952 159 ALARALALDPDILFLDEPTAGLDPIGAAAFDQLILTLRDAlgLSVFLVTHDLDTLYTITDRVA 221
Cdd:PRK14239 158 CIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDD--YTMLLVTRSMQQASRISDRTG 218
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
13-223 |
8.48e-20 |
|
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: 88.50 E-value: 8.48e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 13 IEVRGLCNRF-GPQSVHENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQnlpSLAEHERSLIERRF 91
Cdd:TIGR02857 322 LEFSGVSVAYpGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGV---PLADADADSWRDQI 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 92 GVLFQKGALFSSlTVTENVALPLIEHAGLSRADAEHLAAVKLALAGLPL---SAADKYPASLSGGMIKRAALARALALDP 168
Cdd:TIGR02857 399 AWVPQHPFLFAG-TIAENIRLARPDASDAEIREALERAGLDEFVAALPQgldTPIGEGGAGLSGGQAQRLALARAFLRDA 477
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1316494952 169 DILFLDEPTAGLDPIGAAAFDQLILTLRDalGLSVFLVTHDLDTLYTItDRVAVL 223
Cdd:TIGR02857 478 PLLLLDEPTAHLDAETEAEVLEALRALAQ--GRTVLLVTHRLALAALA-DRIVVL 529
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
12-257 |
1.43e-19 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 85.14 E-value: 1.43e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 12 VIEVRGLCNRFGPQSVHeNLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQP----SEGSVRVFGQNLpslaeHERSLI 87
Cdd:PRK10418 4 QIELRNIALQAAQPLVH-GVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGRVLLDGKPV-----APCALR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 88 ERRFGVLFQKG-ALFSSLTVTENVALPLIEHAGLSRADAEHLAAvkLALAGL--PLSAADKYPASLSGGMIKRAALARAL 164
Cdd:PRK10418 78 GRKIATIMQNPrSAFNPLHTMHTHARETCLALGKPADDATLTAA--LEAVGLenAARVLKLYPFEMSGGMLQRMMIALAL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 165 ALDPDILFLDEPTAGLDPIGAAAFDQLILTLRDALGLSVFLVTHDLDTLYTITDRVAVLAQKKVLvadaidqvaETDDtw 244
Cdd:PRK10418 156 LCEAPFIIADEPTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIV---------EQGD-- 224
|
250
....*....|...
gi 1316494952 245 IHEYFHGPRGRAA 257
Cdd:PRK10418 225 VETLFNAPKHAVT 237
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
29-223 |
2.40e-19 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 87.14 E-value: 2.40e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 29 ENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQNLPSLAEHE-RslieRRFGVLFQKGALFsSLTVT 107
Cdd:COG1132 357 KDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESlR----RQIGVVPQDTFLF-SGTIR 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 108 ENVALpliehaGLSRA-DAEHLAAVKLALA-----GLPlsaaDKYP-------ASLSGG----------MIKraalaral 164
Cdd:COG1132 432 ENIRY------GRPDAtDEEVEEAAKAAQAhefieALP----DGYDtvvgergVNLSGGqrqriaiaraLLK-------- 493
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1316494952 165 alDPDILFLDEPTAGLDPIGAAAfdqliltLRDAL-----GLSVFLVTHDLDTLyTITDRVAVL 223
Cdd:COG1132 494 --DPPILILDEATSALDTETEAL-------IQEALerlmkGRTTIVIAHRLSTI-RNADRILVL 547
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
30-229 |
3.16e-19 |
|
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: 83.92 E-value: 3.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 30 NLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGqNLPSlaeHERSLIERRFGVLF-QKGALFSSLTVTE 108
Cdd:cd03267 39 GISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAG-LVPW---KRRKKFLRRIGVVFgQKTQLWWDLPVID 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 109 NVALplieHAGLSRADAEHLAAVKLALAG-LPLSAADKYPA-SLSGGMIKRAALARALALDPDILFLDEPTAGLDPIGAA 186
Cdd:cd03267 115 SFYL----LAAIYDLPPARFKKRLDELSElLDLEELLDTPVrQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQE 190
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1316494952 187 AFDQLILTLRDALGLSVFLVTHDLDTLYTITDRVAVLAQKKVL 229
Cdd:cd03267 191 NIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLL 233
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
13-232 |
4.73e-19 |
|
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: 83.02 E-value: 4.73e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 13 IEVRGLCNRFGPQSVH--ENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQNLPSLaehERSLIERR 90
Cdd:cd03245 3 IEFRNVSFSYPNQEIPalDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQL---DPADLRRN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 91 FGVLFQKGALFSSlTVTENVALpliehAGLSRADAEHLAAVKLAlaGLpLSAADKYP-----------ASLSGGMIKRAA 159
Cdd:cd03245 80 IGYVPQDVTLFYG-TLRDNITL-----GAPLADDERILRAAELA--GV-TDFVNKHPngldlqigergRGLSGGQRQAVA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1316494952 160 LARALALDPDILFLDEPTAGLDPIGAAAF-DQLILTLRDAlglSVFLVTHDLDTLyTITDRVAVLAQKKvLVAD 232
Cdd:cd03245 151 LARALLNDPPILLLDEPTSAMDMNSEERLkERLRQLLGDK---TLIIITHRPSLL-DLVDRIIVMDSGR-IVAD 219
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
22-225 |
7.16e-19 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 83.24 E-value: 7.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 22 FGPQSVHENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVrvfgqnlpslaEHERSLierRFGVLFQKGALF 101
Cdd:PRK09544 14 FGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI-----------KRNGKL---RIGYVPQKLYLD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 102 SSLTVTenVALPLIEHAGLSRADAehLAAVKLALAGLPLSAADKypaSLSGGMIKRAALARALALDPDILFLDEPTAGLD 181
Cdd:PRK09544 80 TTLPLT--VNRFLRLRPGTKKEDI--LPALKRVQAGHLIDAPMQ---KLSGGETQRVLLARALLNRPQLLVLDEPTQGVD 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1316494952 182 PIGAAAFDQLILTLRDALGLSVFLVTHDLDTLYTITDRVAVLAQ 225
Cdd:PRK09544 153 VNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCLNH 196
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
15-228 |
9.90e-19 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 85.84 E-value: 9.90e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 15 VRGLCNRFGP--QSVHENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQNLpslaEHERSLIERRFG 92
Cdd:TIGR01257 931 VKNLVKIFEPsgRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI----ETNLDAVRQSLG 1006
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 93 VLFQKGALFSSLTVTENVaLPLIEHAGLSRADAEHLAAVKLALAGLPlSAADKYPASLSGGMIKRAALARALALDPDILF 172
Cdd:TIGR01257 1007 MCPQHNILFHHLTVAEHI-LFYAQLKGRSWEEAQLEMEAMLEDTGLH-HKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVV 1084
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1316494952 173 LDEPTAGLDPIGAAAFDQLILTLRDalGLSVFLVTHDLDTLYTITDRVAVLAQKKV 228
Cdd:TIGR01257 1085 LDEPTSGVDPYSRRSIWDLLLKYRS--GRTIIMSTHHMDEADLLGDRIAIISQGRL 1138
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
25-225 |
2.61e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 82.13 E-value: 2.61e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 25 QSVHeNLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQNLPSLAE--HERSlIERRFGVLFQ--KGAL 100
Cdd:PRK13646 21 QAIH-DVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKdkYIRP-VRKRIGMVFQfpESQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 101 FSSLTVTE------NVALPLIEhaglSRADAEHLaavkLALAGLPLSAADKYPASLSGGMIKRAALARALALDPDILFLD 174
Cdd:PRK13646 99 FEDTVEREiifgpkNFKMNLDE----VKNYAHRL----LMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLD 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1316494952 175 EPTAGLDPIGAAAFDQLILTLRDALGLSVFLVTHDLDTLYTITDRVAVLAQ 225
Cdd:PRK13646 171 EPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKE 221
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
13-241 |
3.15e-18 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 83.35 E-value: 3.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 13 IEVRGLCNRFGPQSVHENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQNLPSLAEHERSlieRRFG 92
Cdd:PRK09536 4 IDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAAS---RRVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 93 VLFQKGALFSSLTVTENVALPLIEHAG-LSRADAEHLAAVKLALAGLPLSA-ADKYPASLSGGMIKRAALARALALDPDI 170
Cdd:PRK09536 81 SVPQDTSLSFEFDVRQVVEMGRTPHRSrFDTWTETDRAAVERAMERTGVAQfADRPVTSLSGGERQRVLLARALAQATPV 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1316494952 171 LFLDEPTAGLDPIGAAAFDQLILTLRDAlGLSVFLVTHDLDTLYTITDRVAVLAQKKVLVADAIDQVAETD 241
Cdd:PRK09536 161 LLLDEPTASLDINHQVRTLELVRRLVDD-GKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVLTAD 230
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
30-224 |
6.64e-18 |
|
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: 80.01 E-value: 6.64e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 30 NLDLDLYKGEILAVVGGSGSGKSVLLRSIIGlRQPS----EGSVRVFGQnlpslaEHERSLIERRFGVLFQKGALFSSLT 105
Cdd:cd03234 25 DVSLHVESGQVMAILGSSGSGKTTLLDAISG-RVEGggttSGQILFNGQ------PRKPDQFQKCVAYVRQDDILLPGLT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 106 VTE------NVALPLIEHAGLSRADAEHLAAVKLALAglplSAADKYPASLSGGMIKRAALARALALDPDILFLDEPTAG 179
Cdd:cd03234 98 VREtltytaILRLPRKSSDAIRKKRVEDVLLRDLALT----RIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSG 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1316494952 180 LDPIGAaafDQLILTLRD-ALGLSVFLVT-H----DldtLYTITDRVAVLA 224
Cdd:cd03234 174 LDSFTA---LNLVSTLSQlARRNRIVILTiHqprsD---LFRLFDRILLLS 218
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
9-223 |
6.70e-18 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 81.69 E-value: 6.70e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 9 AEAVIEVRGLCNRFGPQ-----SVHEnLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPS---EGSVRVFGQNLPSLA 80
Cdd:PRK09473 9 ADALLDVKDLRVTFSTPdgdvtAVND-LNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANgriGGSATFNGREILNLP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 81 EHERSLIE-RRFGVLFQK--GALFSSLTVTENVALPLIEHAGLSRADA-----EHLAAVKLALAGLPLSAadkYPASLSG 152
Cdd:PRK09473 88 EKELNKLRaEQISMIFQDpmTSLNPYMRVGEQLMEVLMLHKGMSKAEAfeesvRMLDAVKMPEARKRMKM---YPHEFSG 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1316494952 153 GMIKRAALARALALDPDILFLDEPTAGLDPIGAAAFDQLILTLRDALGLSVFLVTHDLDTLYTITDRVAVL 223
Cdd:PRK09473 165 GMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVM 235
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
10-237 |
6.83e-18 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 80.80 E-value: 6.83e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 10 EAVIEVRG--LCNRFGPQSVHENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQNLPSLAEHErslI 87
Cdd:PRK10253 3 ESVARLRGeqLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKE---V 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 88 ERRFGVLFQKGALFSSLTVTENVALPLIEHAGL-SRADAEHLAAVKLALAGLPLSA-ADKYPASLSGGMIKRAALARALA 165
Cdd:PRK10253 80 ARRIGLLAQNATTPGDITVQELVARGRYPHQPLfTRWRKEDEEAVTKAMQATGITHlADQSVDTLSGGQRQRAWIAMVLA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 166 LDPDILFLDEPTAGLDPIGAAAFDQLILTLRDALGLSVFLVTHDLD-----TLYTITDR----VAVLAQKKVLVADAIDQ 236
Cdd:PRK10253 160 QETAIMLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNqacryASHLIALRegkiVAQGAPKEIVTAELIER 239
|
.
gi 1316494952 237 V 237
Cdd:PRK10253 240 I 240
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
30-225 |
7.85e-18 |
|
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: 82.49 E-value: 7.85e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 30 NLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQNLpslAEHERSLIERRFGVLFQKGALFSSlTVTEN 109
Cdd:COG4618 350 GVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADL---SQWDREELGRHIGYLPQDVELFDG-TIAEN 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 110 VAlpliehaGLSRADAEH-LAAVKLA-----LAGLPlsaaDKY-------PASLSGGMIKRAALARALALDPDILFLDEP 176
Cdd:COG4618 426 IA-------RFGDADPEKvVAAAKLAgvhemILRLP----DGYdtrigegGARLSGGQRQRIGLARALYGDPRLVVLDEP 494
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1316494952 177 TAGLDPIGAAAFDQLILTLRDAlGLSVFLVTHDLDTLyTITDRVAVLAQ 225
Cdd:COG4618 495 NSNLDDEGEAALAAAIRALKAR-GATVVVITHRPSLL-AAVDKLLVLRD 541
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
9-223 |
9.12e-18 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 82.52 E-value: 9.12e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 9 AEAVIEVRGLCNRFGPQSVHENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQNLPSLaEHERSlIE 88
Cdd:PRK09700 2 ATPYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKL-DHKLA-AQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 89 RRFGVLFQKGALFSSLTVTENV---ALPLIEHAGLSRADAEHL---AAVKLALAGLPLSaADKYPASLSGGMIKRAALAR 162
Cdd:PRK09700 80 LGIGIIYQELSVIDELTVLENLyigRHLTKKVCGVNIIDWREMrvrAAMMLLRVGLKVD-LDEKVANLSISHKQMLEIAK 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1316494952 163 ALALDPDILFLDEPTAGLDpigAAAFDQLILTLRD--ALGLSVFLVTHDLDTLYTITDRVAVL 223
Cdd:PRK09700 159 TLMLDAKVIIMDEPTSSLT---NKEVDYLFLIMNQlrKEGTAIVYISHKLAEIRRICDRYTVM 218
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
13-210 |
1.02e-17 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 80.13 E-value: 1.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 13 IEVRGLCNRFGPQSVHENLDLDLYKGEILAVVGGSGSGKSVLLrSIIG-LRQPSEGSVRVFGQNLPSLAEHERSlieRRF 91
Cdd:COG4604 2 IEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLL-SMISrLLPPDSGEVLVDGLDVATTPSRELA---KRL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 92 GVLFQKGALFSSLTVTENVAL---PlieHAG--LSRADAEHlaaVKLALAGLPLSA-ADKYPASLSGG--------MIkr 157
Cdd:COG4604 78 AILRQENHINSRLTVRELVAFgrfP---YSKgrLTAEDREI---IDEAIAYLDLEDlADRYLDELSGGqrqrafiaMV-- 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1316494952 158 aalaraLALDPDILFLDEPTAGLDPIGAAAFDQLILTLRDALGLSVFLVTHDL 210
Cdd:COG4604 150 ------LAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDI 196
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
24-232 |
1.21e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 80.23 E-value: 1.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 24 PQSVHENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQP---SEGSVRVFGQNLPSLAEHErslIERRFGVLFQK-GA 99
Cdd:PRK13640 19 KKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPddnPNSKITVDGITLTAKTVWD---IREKVGIVFQNpDN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 100 LFSSLTVTENVALPLiEHAGLSRADAEHLAAVKLALAGLpLSAADKYPASLSGGMIKRAALARALALDPDILFLDEPTAG 179
Cdd:PRK13640 96 QFVGATVGDDVAFGL-ENRAVPRPEMIKIVRDVLADVGM-LDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSM 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1316494952 180 LDPIGAAAFDQLILTLRDALGLSVFLVTHDLDTLyTITDRVAVLAQKKVLVAD 232
Cdd:PRK13640 174 LDPAGKEQILKLIRKLKKKNNLTVISITHDIDEA-NMADQVLVLDDGKLLAQG 225
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
29-230 |
1.33e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 80.03 E-value: 1.33e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 29 ENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQNL--PSLAEHERSLIerrfGVLFQKGAL-FSSLT 105
Cdd:PRK13644 19 ENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTgdFSKLQGIRKLV----GIVFQNPETqFVGRT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 106 VT-------ENVALPLIEHAGLsradaehlaaVKLALAGLPLsaaDKY----PASLSGGMIKRAALARALALDPDILFLD 174
Cdd:PRK13644 95 VEedlafgpENLCLPPIEIRKR----------VDRALAEIGL---EKYrhrsPKTLSGGQGQCVALAGILTMEPECLIFD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1316494952 175 EPTAGLDPIGAAAFDQLILTLRDAlGLSVFLVTHDLDTLYtITDRVAVLAQKKVLV 230
Cdd:PRK13644 162 EVTSMLDPDSGIAVLERIKKLHEK-GKTIVYITHNLEELH-DADRIIVMDRGKIVL 215
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
16-228 |
2.13e-17 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 81.29 E-value: 2.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 16 RGLCNR-FGPQSVHENLDLDLYKGEILAVVGGSGSGKSV----LLRSIiglrqPSEGSVRVFGQNLPSLAEHERSLIERR 90
Cdd:PRK15134 289 KGILKRtVDHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLI-----NSQGEIWFDGQPLHNLNRRQLLPVRHR 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 91 FGVLFQ--KGALFSSLTVTENVALPL-IEHAGLSRADAEhlAAVKLALAGLPLSAADK--YPASLSGGMIKRAALARALA 165
Cdd:PRK15134 364 IQVVFQdpNSSLNPRLNVLQIIEEGLrVHQPTLSAAQRE--QQVIAVMEEVGLDPETRhrYPAEFSGGQRQRIAIARALI 441
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1316494952 166 LDPDILFLDEPTAGLDPIGAAAFDQLILTLRDALGLSVFLVTHDLDTLYTITDRVAVLAQKKV 228
Cdd:PRK15134 442 LKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEV 504
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
37-253 |
4.18e-17 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 79.40 E-value: 4.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 37 KGEILAVVGGSGSGKSVLLRSIIGL----RQPSEGSVRVFGQNLPSLAEHE-RSLIERRFGVLFQKG--ALFSSLTVTEN 109
Cdd:PRK11022 32 QGEVVGIVGESGSGKSVSSLAIMGLidypGRVMAEKLEFNGQDLQRISEKErRNLVGAEVAMIFQDPmtSLNPCYTVGFQ 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 110 VALPLIEHAGLSRADAEHLAAVKLALAGLP--LSAADKYPASLSGGMIKRAALARALALDPDILFLDEPTAGLDPIGAAA 187
Cdd:PRK11022 112 IMEAIKVHQGGNKKTRRQRAIDLLNQVGIPdpASRLDVYPHQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQ 191
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1316494952 188 FDQLILTLRDALGLSVFLVTHDLDTLYTITDRVAVLAQkkvlvadaiDQVAETDDTwiHEYFHGPR 253
Cdd:PRK11022 192 IIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYA---------GQVVETGKA--HDIFRAPR 246
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
10-237 |
4.49e-17 |
|
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: 78.20 E-value: 4.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 10 EAVIEVRGLCNRFGPQSVHENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEG-SVRVFGQNLP--SLAEhersl 86
Cdd:COG1119 1 DPLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRGgeDVWE----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 87 IERRFGVLfqKGALFSSLTVTENValpliEHAGLS----------RADAEHLAAVKLALAGLPLSA-ADKYPASLSGG-- 153
Cdd:COG1119 76 LRKRIGLV--SPALQLRFPRDETV-----LDVVLSgffdsiglyrEPTDEQRERARELLELLGLAHlADRPFGTLSQGeq 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 154 --------MIKraalaralalDPDILFLDEPTAGLDPIGAAAFDQLILTLRDALGLSVFLVTHDLDTLYTITDRVAVLAQ 225
Cdd:COG1119 149 rrvliaraLVK----------DPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKD 218
|
250
....*....|..
gi 1316494952 226 KKVLVADAIDQV 237
Cdd:COG1119 219 GRVVAAGPKEEV 230
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
22-237 |
9.00e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 77.83 E-value: 9.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 22 FGPQSVHENLDLDLYKGEILAVVGGSGSGKSVLLRS-------IIGLRQpsEGSVRVFGQNLPSLaeheRSLIE--RRFG 92
Cdd:PRK14271 31 FAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTlnrmndkVSGYRY--SGDVLLGGRSIFNY----RDVLEfrRRVG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 93 VLFQKGALFSsLTVTENVALPLIEHAGLSRADAEHLAAVKLALAGLPLSAADKY---PASLSGGMIKRAALARALALDPD 169
Cdd:PRK14271 105 MLFQRPNPFP-MSIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLWDAVKDRLsdsPFRLSGGQQQLLCLARTLAVNPE 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1316494952 170 ILFLDEPTAGLDPIGAAAFDQLILTLRDAlgLSVFLVTHDLDTLYTITDRVAVLAQKKVLVADAIDQV 237
Cdd:PRK14271 184 VLLLDEPTSALDPTTTEKIEEFIRSLADR--LTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQL 249
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
13-228 |
9.15e-17 |
|
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: 77.14 E-value: 9.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 13 IEVRGLCNRFGPQS--VHENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQNLpslAEHERSLIERR 90
Cdd:cd03252 1 ITFEHVRFRYKPDGpvILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDL---ALADPAWLRRQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 91 FGVLFQKGALFSSlTVTENVALpliEHAGLSRADAEhlAAVKLALA-----GLPL---SAADKYPASLSGGMIKRAALAR 162
Cdd:cd03252 78 VGVVLQENVLFNR-SIRDNIAL---ADPGMSMERVI--EAAKLAGAhdfisELPEgydTIVGEQGAGLSGGQRQRIAIAR 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1316494952 163 ALALDPDILFLDEPTAGLDPIGAAAFDQlilTLRDAL-GLSVFLVTHDLDTLYTiTDRVAVLAQKKV 228
Cdd:cd03252 152 ALIHNPRILIFDEATSALDYESEHAIMR---NMHDICaGRTVIIIAHRLSTVKN-ADRIIVMEKGRI 214
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
17-237 |
1.05e-16 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 77.74 E-value: 1.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 17 GLCNRFGPQSVHENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQnlpSLAEHERSLIERRFGV--L 94
Cdd:PRK13638 6 DLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGK---PLDYSKRGLLALRQQVatV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 95 FQ--KGALFSSlTVTENVALPLiehAGLSRADAEHLAAVKLALAGLPLSAADKYPAS-LSGGMIKRAALARALALDPDIL 171
Cdd:PRK13638 83 FQdpEQQIFYT-DIDSDIAFSL---RNLGVPEAEITRRVDEALTLVDAQHFRHQPIQcLSHGQKKRVAIAGALVLQARYL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1316494952 172 FLDEPTAGLDPIGAAafdQLILTLRD--ALGLSVFLVTHDLDTLYTITDRVAVLAQKKVLVADAIDQV 237
Cdd:PRK13638 159 LLDEPTAGLDPAGRT---QMIAIIRRivAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEV 223
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
37-228 |
1.21e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 77.48 E-value: 1.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 37 KGEILAVVGGSGSGKSVLLRSIIGLRQPSEGsvRVFGQNLPsLAEHERSLIERRFGVLFQKGA-LFSSLTVTENVALPLI 115
Cdd:PRK13648 34 KGQWTSIVGHNGSGKSTIAKLMIGIEKVKSG--EIFYNNQA-ITDDNFEKLRKHIGIVFQNPDnQFVGSIVKYDVAFGLE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 116 EHA----GLSRADAEHLAAVKLalaglpLSAADKYPASLSGGMIKRAALARALALDPDILFLDEPTAGLDPIGAAAFDQL 191
Cdd:PRK13648 111 NHAvpydEMHRRVSEALKQVDM------LERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLDL 184
|
170 180 190
....*....|....*....|....*....|....*..
gi 1316494952 192 ILTLRDALGLSVFLVTHDLDTLYTiTDRVAVLAQKKV 228
Cdd:PRK13648 185 VRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTV 220
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
22-237 |
1.46e-16 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 76.98 E-value: 1.46e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 22 FGPQSVHENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQNLPSLAEHERSlieRRFGVLFQKGALF 101
Cdd:PRK11231 12 YGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLA---RRLALLPQHHLTP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 102 SSLTVTENVAL---PLIEHAG-LSRADAEHlaaVKLALAGLPLSA-ADKYPASLSGGMIKRAALARALALDPDILFLDEP 176
Cdd:PRK11231 89 EGITVRELVAYgrsPWLSLWGrLSAEDNAR---VNQAMEQTRINHlADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEP 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1316494952 177 TAGLDPIGAAAFDQLILTLRDAlGLSVFLVTHDLDTLYTITDRVAVLAQKKVLVADAIDQV 237
Cdd:PRK11231 166 TTYLDINHQVELMRLMRELNTQ-GKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEV 225
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
30-239 |
1.60e-16 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 76.66 E-value: 1.60e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 30 NLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGqnlpSLAeherSLIErrFGVLFQkgalfSSLTVTEN 109
Cdd:COG1134 44 DVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNG----RVS----ALLE--LGAGFH-----PELTGREN 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 110 V---ALPLiehaGLSRAD-AEHLAAVkLALAGL------PLSaadkypaSLSGGM-----------IkraalaralalDP 168
Cdd:COG1134 109 IylnGRLL----GLSRKEiDEKFDEI-VEFAELgdfidqPVK-------TYSSGMrarlafavataV-----------DP 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1316494952 169 DILFLDEPTAgldpIGAAAF----DQLILTLRDAlGLSVFLVTHDLDTLYTITDRVAVLAQKKVLVADAIDQVAE 239
Cdd:COG1134 166 DILLVDEVLA----VGDAAFqkkcLARIRELRES-GRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPEEVIA 235
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
9-223 |
1.82e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 76.62 E-value: 1.82e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 9 AEAVIEVRGLCNRFGPQSVHENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQNL---PSLAEHERS 85
Cdd:PRK14246 7 AEDVFNISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLyfgKDIFQIDAI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 86 LIERRFGVLFQKGALFSSLTVTENVALPLIEHAGLSRADAEHLAAVKLALAGLPLSAADKY--PAS-LSGGMIKRAALAR 162
Cdd:PRK14246 87 KLRKEVGMVFQQPNPFPHLSIYDNIAYPLKSHGIKEKREIKKIVEECLRKVGLWKEVYDRLnsPASqLSGGQQQRLTIAR 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1316494952 163 ALALDPDILFLDEPTAGLDPIGAAAFDQLILTLRDAlgLSVFLVTHDLDTLYTITDRVAVL 223
Cdd:PRK14246 167 ALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNE--IAIVIVSHNPQQVARVADYVAFL 225
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
3-208 |
2.07e-16 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 78.63 E-value: 2.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 3 RSTRPPAEAVIEVRGLCNRFGPQSVHENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQnlpSLAEH 82
Cdd:NF033858 257 RPADDDDEPAIEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQ---PVDAG 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 83 ERSlIERRFGVLFQKGALFSSLTVTENVALplieHA---GLSRADAEhlAAVKLALAGLPLSA-ADKYPASLSGG----- 153
Cdd:NF033858 334 DIA-TRRRVGYMSQAFSLYGELTVRQNLEL----HArlfHLPAAEIA--ARVAEMLERFDLADvADALPDSLPLGirqrl 406
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1316494952 154 -----MIKraalaralalDPDILFLDEPTAGLDPIGAAAFDQLILTL--RDalGLSVFLVTH 208
Cdd:NF033858 407 slavaVIH----------KPELLILDEPTSGVDPVARDMFWRLLIELsrED--GVTIFISTH 456
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
11-237 |
3.11e-16 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 75.70 E-value: 3.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 11 AVIEVRGLCNRFGPQSVHENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQNLPSLAEHERSLieRR 90
Cdd:PRK10895 2 ATLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARAR--RG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 91 FGVLFQKGALFSSLTVTENVALPLIEHAGLS---RADAEHLAAVKLALAGLplsaADKYPASLSGGMIKRAALARALALD 167
Cdd:PRK10895 80 IGYLPQEASIFRRLSVYDNLMAVLQIRDDLSaeqREDRANELMEEFHIEHL----RDSMGQSLSGGERRRVEIARALAAN 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 168 PDILFLDEPTAGLDPIGAAAFDQLILTLRDAlGLSVFLVTHDLDTLYTITDRVAVLAQKKVLVADAIDQV 237
Cdd:PRK10895 156 PKFILLDEPFAGVDPISVIDIKRIIEHLRDS-GLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEI 224
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
29-229 |
3.35e-16 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 76.66 E-value: 3.35e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 29 ENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQNlPSlaEHERSLIeRRFGVLF-QKGALFSSLTVT 107
Cdd:COG4586 39 DDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYV-PF--KRRKEFA-RRIGVVFgQRSQLWWDLPAI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 108 ENVALplieHA---GLSRADA----EHLAAVkLALAGL---P---LSAADKYPASLSGGMIKraalaralalDPDILFLD 174
Cdd:COG4586 115 DSFRL----LKaiyRIPDAEYkkrlDELVEL-LDLGELldtPvrqLSLGQRMRCELAAALLH----------RPKILFLD 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1316494952 175 EPTAGLDPIGAAAFDQLILTLRDALGLSVFLVTHDLDTLYTITDRVAVLAQKKVL 229
Cdd:COG4586 180 EPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEALCDRVIVIDHGRII 234
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
16-232 |
5.41e-16 |
|
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: 74.88 E-value: 5.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 16 RGLCNRFGPQSVHENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQnlpslaehERSLIErrFGVLF 95
Cdd:cd03220 26 LGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGR--------VSSLLG--LGGGF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 96 QKgalfsSLTVTENVALPLIEHaGLSRADAEHLAAVKLALAGL------PLSaadkypaSLSGGMIKRAALARALALDPD 169
Cdd:cd03220 96 NP-----ELTGRENIYLNGRLL-GLSRKEIDEKIDEIIEFSELgdfidlPVK-------TYSSGMKARLAFAIATALEPD 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1316494952 170 ILFLDEPTAgldpIGAAAF----DQLILTLRDAlGLSVFLVTHDLDTLYTITDRVAVLAQKKVLVAD 232
Cdd:cd03220 163 ILLIDEVLA----VGDAAFqekcQRRLRELLKQ-GKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
13-226 |
5.55e-16 |
|
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: 77.15 E-value: 5.55e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 13 IEVRGLCNRFGPQSVHENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQ--PSEGSV----------------RVFGQ 74
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQyePTSGRIiyhvalcekcgyverpSKVGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 75 NLP--------------SLAEHERSLIERRFGVLFQKG-ALFSSLTVTENV--ALPLIEHAG---LSRAdAEHLAAVKLA 134
Cdd:TIGR03269 81 PCPvcggtlepeevdfwNLSDKLRRRIRKRIAIMLQRTfALYGDDTVLDNVleALEEIGYEGkeaVGRA-VDLIEMVQLS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 135 LAGLPLsAADkypasLSGGMIKRAALARALALDPDILFLDEPTAGLDPIGAAAFDQLILTLRDALGLSVFLVTHDLDTLY 214
Cdd:TIGR03269 160 HRITHI-ARD-----LSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIE 233
|
250
....*....|..
gi 1316494952 215 TITDRvAVLAQK 226
Cdd:TIGR03269 234 DLSDK-AIWLEN 244
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
4-256 |
1.04e-15 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 74.82 E-value: 1.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 4 STRPPAEAVIEVRGLCNRFGPQSVHENLDLDLYKGEILAVVGGSGSGKSVLLRS-------IIGLRqpSEGSVRVFGQNL 76
Cdd:PRK14243 2 STLNGTETVLRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCfnrlndlIPGFR--VEGKVTFHGKNL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 77 PSlAEHERSLIERRFGVLFQKGALFSSlTVTENVAL-PLIEhaGLsRADAEHLAAVKLALAGLPLSAADKYPAS---LSG 152
Cdd:PRK14243 80 YA-PDVDPVEVRRRIGMVFQKPNPFPK-SIYDNIAYgARIN--GY-KGDMDELVERSLRQAALWDEVKDKLKQSglsLSG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 153 GMIKRAALARALALDPDILFLDEPTAGLDPIGAAAFDQLILTLRDAlgLSVFLVTHDLDTLYTITDRVAVLAQKKVLVAD 232
Cdd:PRK14243 155 GQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQ--YTIIIVTHNMQQAARVSDMTAFFNVELTEGGG 232
|
250 260
....*....|....*....|....
gi 1316494952 233 AIDQVAETDDTWIheYFHGPRGRA 256
Cdd:PRK14243 233 RYGYLVEFDRTEK--IFNSPQQQA 254
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
10-229 |
1.53e-15 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 74.28 E-value: 1.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 10 EAVIEVRGLCNRFGPQSVHENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGL---RQPSEGSVRVFGQNLPSLAEHERSL 86
Cdd:PRK09984 2 QTIIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgDKSAGSHIELLGRTVQREGRLARDI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 87 IERR--FGVLFQKGALFSSLTVTENValpLIEHAG-----------LSRADAEHlAAVKLALAGLPLSAADKYpASLSGG 153
Cdd:PRK09984 82 RKSRanTGYIFQQFNLVNRLSVLENV---LIGALGstpfwrtcfswFTREQKQR-ALQALTRVGMVHFAHQRV-STLSGG 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1316494952 154 MIKRAALARALALDPDILFLDEPTAGLDPIGAAAfdqLILTLRD---ALGLSVFLVTHDLDTLYTITDRVAVLAQKKVL 229
Cdd:PRK09984 157 QQQRVAIARALMQQAKVILADEPIASLDPESARI---VMDTLRDinqNDGITVVVTLHQVDYALRYCERIVALRQGHVF 232
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
20-237 |
3.61e-15 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 73.04 E-value: 3.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 20 NRFGPqsvhenLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLrQPSEGSVRVFGQNLPSLAEHErsLIERRFGVLFQKGA 99
Cdd:PRK03695 10 TRLGP------LSAEVRAGEILHLVGPNGAGKSTLLARMAGL-LPGSGSIQFAGQPLEAWSAAE--LARHRAYLSQQQTP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 100 LFssltvtenvALPLIEHAGLSRADAEHLAAVKLALAGLP--LSAADKYPAS---LSGG-MIKRAALARALALDPDI--- 170
Cdd:PRK03695 81 PF---------AMPVFQYLTLHQPDKTRTEAVASALNEVAeaLGLDDKLGRSvnqLSGGeWQRVRLAAVVLQVWPDInpa 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 171 ---LFLDEPTAGLDPIGAAAFDQLILTLRdALGLSVFLVTHDLDTLYTITDRVAVLAQKKVLVADAIDQV 237
Cdd:PRK03695 152 gqlLLLDEPMNSLDVAQQAALDRLLSELC-QQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEV 220
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
12-208 |
4.45e-15 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 71.83 E-value: 4.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 12 VIEVRGLCNRFGPQSVHENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQN--LPSLAEherslier 89
Cdd:PRK13539 2 MLEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDidDPDVAE-------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 90 RFGVLFQKGALFSSLTVTENVALPLIEHAGLSRADAEHLAAVKLA-LAGLP---LSAADKYPASLSGGMIKRAAlarala 165
Cdd:PRK13539 74 ACHYLGHRNAMKPALTVAENLEFWAAFLGGEELDIAAALEAVGLApLAHLPfgyLSAGQKRRVALARLLVSNRP------ 147
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1316494952 166 ldpdILFLDEPTAGLDPIGAAAFDQLILTLRDALGLsVFLVTH 208
Cdd:PRK13539 148 ----IWILDEPTAALDAAAVALFAELIRAHLAQGGI-VIAATH 185
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
13-228 |
5.99e-15 |
|
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: 70.80 E-value: 5.99e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 13 IEVRGLCNRFGPQSVH--ENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQNLPSLAEHERSLIerr 90
Cdd:cd03247 1 LSINNVSFSYPEQEQQvlKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSLI--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 91 fGVLFQKGALFSSlTVTENVALPLiehAGLSRAdaehlaavKLALAGLPLSaadkypaslsggmikraalaralalDPDI 170
Cdd:cd03247 78 -SVLNQRPYLFDT-TLRNNLGRRF---SGGERQ--------RLALARILLQ-------------------------DAPI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1316494952 171 LFLDEPTAGLDPIGAaafDQLILTLRDAL-GLSVFLVTHDLDTLYTItDRVAVLAQKKV 228
Cdd:cd03247 120 VLLDEPTVGLDPITE---RQLLSLIFEVLkDKTLIWITHHLTGIEHM-DKILFLENGKI 174
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
25-223 |
6.79e-15 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 73.97 E-value: 6.79e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 25 QSVHENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRqPS------EGSVRVFGQNLPSLAEHE-RSLIERRFGVLFQK 97
Cdd:PRK15134 22 RTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLL-PSppvvypSGDIRFHGESLLHASEQTlRGVRGNKIAMIFQE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 98 GalFSSLTVTENVALPLIE----HAGLSR--ADAEHLAAvkLALAGLPLSA---ADkYPASLSGGMIKRAALARALALDP 168
Cdd:PRK15134 101 P--MVSLNPLHTLEKQLYEvlslHRGMRReaARGEILNC--LDRVGIRQAAkrlTD-YPHQLSGGERQRVMIAMALLTRP 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1316494952 169 DILFLDEPTAGLDPIGAAAFDQLILTLRDALGLSVFLVTHDLDTLYTITDRVAVL 223
Cdd:PRK15134 176 ELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVM 230
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
38-229 |
6.93e-15 |
|
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: 71.04 E-value: 6.93e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 38 GEILAVVGGSGSGKSVLLRSIIGLRQPS--EGSVRVFGQNLPslaeheRSLIERRFGVLFQKGALFSSLTVTENVALpli 115
Cdd:cd03213 35 GELTAIMGPSGAGKSTLLNALAGRRTGLgvSGEVLINGRPLD------KRSFRKIIGYVPQDDILHPTLTVRETLMF--- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 116 eHAGLSradaehlaavklalaglplsaadkypaSLSGGMIKRAALARALALDPDILFLDEPTAGLDPIGAAafdQLILTL 195
Cdd:cd03213 106 -AAKLR---------------------------GLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSAL---QVMSLL 154
|
170 180 190
....*....|....*....|....*....|....*..
gi 1316494952 196 RD--ALGLSVFLVTHDL-DTLYTITDRVAVLAQKKVL 229
Cdd:cd03213 155 RRlaDTGRTIICSIHQPsSEIFELFDKLLLLSQGRVI 191
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
13-229 |
7.08e-15 |
|
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: 71.88 E-value: 7.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 13 IEVRGLCNRFGP-QSVHENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQNLPSLAEHerSLiERRF 91
Cdd:cd03253 1 IEFENVTFAYDPgRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLD--SL-RRAI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 92 GVLFQKGALFSSlTVTENvalplIEHAGLSRADAEHLAAVKLA-LAGLPLSAADKYPA-------SLSGGMIKRAALARA 163
Cdd:cd03253 78 GVVPQDTVLFND-TIGYN-----IRYGRPDATDEEVIEAAKAAqIHDKIMRFPDGYDTivgerglKLSGGEKQRVAIARA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1316494952 164 LALDPDILFLDEPTAGLDPIGaaafDQLIL-TLRDAL-GLSVFLVTHDLDTLYTiTDRVAVLAQKKVL 229
Cdd:cd03253 152 ILKNPPILLLDEATSALDTHT----EREIQaALRDVSkGRTTIVIAHRLSTIVN-ADKIIVLKDGRIV 214
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
25-246 |
1.06e-14 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 73.60 E-value: 1.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 25 QSVHENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQNLPslaEHERSLIERRFGVLFQKGALFSSl 104
Cdd:TIGR00958 494 VPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLV---QYDHHYLHRQVALVGQEPVLFSG- 569
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 105 TVTENVALpliehaGLSRA-DAEHLAAVKLALA-----GLPL---SAADKYPASLSGGMIKRAALARALALDPDILFLDE 175
Cdd:TIGR00958 570 SVRENIAY------GLTDTpDEEIMAAAKAANAhdfimEFPNgydTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDE 643
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1316494952 176 PTAGLDpigaAAFDQLILTLRDALGLSVFLVTHDLDTLYTiTDRVAVLAQKKVLVADAIDQVAETDDTWIH 246
Cdd:TIGR00958 644 ATSALD----AECEQLLQESRSRASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQLMEDQGCYKH 709
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
30-237 |
1.20e-14 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 72.60 E-value: 1.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 30 NLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQ---------NLPSlaehERslieRRFGVLFQKGAL 100
Cdd:PRK11144 16 TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRvlfdaekgiCLPP----EK----RRIGYVFQDARL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 101 FSSLTVTENValplieHAGLSRADAEHLAAVkLALAGL-PLsaADKYPASLSGGMIKRAALARALALDPDILFLDEPTAG 179
Cdd:PRK11144 88 FPHYKVRGNL------RYGMAKSMVAQFDKI-VALLGIePL--LDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLAS 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1316494952 180 LD-PIGAAAFDQLiLTLRDALGLSVFLVTHDLDTLYTITDRVAVLAQKKVLVADAIDQV 237
Cdd:PRK11144 159 LDlPRKRELLPYL-ERLAREINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEV 216
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
13-229 |
1.51e-14 |
|
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: 70.60 E-value: 1.51e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 13 IEVRGLCNRFGPQS--VHENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQNLPSLAEHErslIERR 90
Cdd:cd03244 3 IEFKNVSLRYRPNLppVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHD---LRSR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 91 FGVLFQKGALFSSlTVTENVAlPLIEHAGLSRADAEHLAAVKLALAGLP-------------LSAADKYPASLSGGMIKr 157
Cdd:cd03244 80 ISIIPQDPVLFSG-TIRSNLD-PFGEYSDEELWQALERVGLKEFVESLPggldtvveeggenLSVGQRQLLCLARALLR- 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1316494952 158 aalaralalDPDILFLDEPTAGLDPIGaaafDQLIL-TLRDAL-GLSVFLVTHDLDTLYTiTDRVAVLAQKKVL 229
Cdd:cd03244 157 ---------KSKILVLDEATASVDPET----DALIQkTIREAFkDCTVLTIAHRLDTIID-SDRILVLDKGRVV 216
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
13-208 |
1.60e-14 |
|
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: 70.08 E-value: 1.60e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 13 IEVRGLCNRFGPQSVHENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQNLPSLAEHErsliERRFG 92
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEP----HENIL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 93 VLFQKGALFSSLTVTENVALPLIEHAGLSRADAEHLAAVKLAlaglplSAADKYPASLSGGMIKRAALARALALDPDILF 172
Cdd:TIGR01189 77 YLGHLPGLKPELSALENLHFWAAIHGGAQRTIEDALAAVGLT------GFEDLPAAQLSAGQQRRLALARLWLSRRPLWI 150
|
170 180 190
....*....|....*....|....*....|....*.
gi 1316494952 173 LDEPTAGLDPIGAAAFDQlILTLRDALGLSVFLVTH 208
Cdd:TIGR01189 151 LDEPTTALDKAGVALLAG-LLRAHLARGGIVLLTTH 185
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
29-228 |
1.84e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 71.27 E-value: 1.84e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 29 ENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVfgQNLPSLAEHERSLIERRFGVLFQK--GALFSSLtV 106
Cdd:PRK13633 27 DDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYV--DGLDTSDEENLWDIRNKAGMVFQNpdNQIVATI-V 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 107 TENVAL-PliEHAGLsrADAEHLAAVKLALAGLPLSAADKY-PASLSGGMIKRAALARALALDPDILFLDEPTAGLDPIG 184
Cdd:PRK13633 104 EEDVAFgP--ENLGI--PPEEIRERVDESLKKVGMYEYRRHaPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSG 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1316494952 185 AAAFDQLILTLRDALGLSVFLVTHDLDTLYTiTDRVAVLAQKKV 228
Cdd:PRK13633 180 RREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKV 222
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
12-228 |
2.41e-14 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 72.40 E-value: 2.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 12 VIEVRGLCNRFGPQSVHENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVfGQNLpslaeherslierRF 91
Cdd:COG0488 315 VLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETV-------------KI 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 92 GVLFQKGALF-SSLTVTENVAlpliehAGLSRADAEHLAAVkLALAGLPLSAADKYPASLSGG----------MIKraal 160
Cdd:COG0488 381 GYFDQHQEELdPDKTVLDELR------DGAPGGTEQEVRGY-LGRFLFSGDDAFKPVGVLSGGekarlalaklLLS---- 449
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1316494952 161 aralalDPDILFLDEPTAGLDpigaaafdqlILTLR---DAL----GlSVFLVTHDLDTLYTITDRVAVLAQKKV 228
Cdd:COG0488 450 ------PPNVLLLDEPTNHLD----------IETLEaleEALddfpG-TVLLVSHDRYFLDRVATRILEFEDGGV 507
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
30-229 |
9.44e-14 |
|
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: 68.41 E-value: 9.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 30 NLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQNLPSLaehERSLIERRFGVLFQKGALFSSlTVTEN 109
Cdd:cd03254 21 DINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDI---SRKSLRSMIGVVLQDTFLFSG-TIMEN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 110 VALpliehAGLSRADAEHLAAVKLALAG-----LP-------------LSAADKYPASLSGGMIKraalaralalDPDIL 171
Cdd:cd03254 97 IRL-----GRPNATDEEVIEAAKEAGAHdfimkLPngydtvlgenggnLSQGERQLLAIARAMLR----------DPKIL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1316494952 172 FLDEPTAGLDPIGAAAFDQLILTLRDalGLSVFLVTHDLDTLYTiTDRVAVLAQKKVL 229
Cdd:cd03254 162 ILDEATSNIDTETEKLIQEALEKLMK--GRTSIIIAHRLSTIKN-ADKILVLDDGKII 216
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
8-228 |
5.15e-13 |
|
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: 66.28 E-value: 5.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 8 PAEAVIEVRGLCNRFGPQ--SVHENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQNLPSLAEHErs 85
Cdd:cd03369 2 PEHGEIEVENLSVRYAPDlpPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLED-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 86 lIERRFGVLFQKGALFSSlTVTENVAlPLIEHaglsrADAEHLAAVKLALAGLPLSAADKYPASLSGGMIKRaalarala 165
Cdd:cd03369 80 -LRSSLTIIPQDPTLFSG-TIRSNLD-PFDEY-----SDEEIYGALRVSEGGLNLSQGQRQLLCLARALLKR-------- 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1316494952 166 ldPDILFLDEPTAGLDPIGAAAFDQLILTLRDalGLSVFLVTHDLDTLYTItDRVAVLAQKKV 228
Cdd:cd03369 144 --PRVLVLDEATASIDYATDALIQKTIREEFT--NSTILTIAHRLRTIIDY-DKILVMDAGEV 201
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
12-203 |
6.53e-13 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 68.23 E-value: 6.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 12 VIEVRGLCNRFGPQSVHENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQNLPSlaEHERSLIERRF 91
Cdd:NF033858 1 VARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMAD--ARHRRAVCPRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 92 GVLFQ--KGALFSSLTVTENVALplieHA---GLSRADAEHLAAVKLALAGLpLSAADKyPAS-LSGGM----------I 155
Cdd:NF033858 79 AYMPQglGKNLYPTLSVFENLDF----FGrlfGQDAAERRRRIDELLRATGL-APFADR-PAGkLSGGMkqklglccalI 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1316494952 156 KraalaralalDPDILFLDEPTAGLDPIGAAAFDQLILTLRDAL-GLSV 203
Cdd:NF033858 153 H----------DPDLLILDEPTTGVDPLSRRQFWELIDRIRAERpGMSV 191
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
4-228 |
7.61e-13 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 67.93 E-value: 7.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 4 STRPPAEAVIEVRGLCNRF--GPQSVHENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQNLPSLAE 81
Cdd:PRK11160 330 STAAADQVSLTLNNVSFTYpdQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSE 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 82 HE-RSLIerrfGVLFQKGALFSSlTVTENVALpliehaGLSRADAEHLAAV--KLALAGLpLSAADKYPA-------SLS 151
Cdd:PRK11160 410 AAlRQAI----SVVSQRVHLFSA-TLRDNLLL------AAPNASDEALIEVlqQVGLEKL-LEDDKGLNAwlgeggrQLS 477
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1316494952 152 GGMIKRAALARALALDPDILFLDEPTAGLDpigaAAFDQLILTL--RDALGLSVFLVTHDLdTLYTITDRVAVLAQKKV 228
Cdd:PRK11160 478 GGEQRRLGIARALLHDAPLLLLDEPTEGLD----AETERQILELlaEHAQNKTVLMITHRL-TGLEQFDRICVMDNGQI 551
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
9-211 |
8.55e-13 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 65.89 E-value: 8.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 9 AEAVIEVRGLCNRFGPQSVHENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQNLPSLA-EHERsli 87
Cdd:PRK10247 4 NSPLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKpEIYR--- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 88 eRRFGVLFQKGALFSSlTVTENVALP-LIEHaglSRADAEHLAAvKLALAGLPLSAADKYPASLSGGMIKRAALARALAL 166
Cdd:PRK10247 81 -QQVSYCAQTPTLFGD-TVYDNLIFPwQIRN---QQPDPAIFLD-DLERFALPDTILTKNIAELSGGEKQRISLIRNLQF 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1316494952 167 DPDILFLDEPTAGLDPIGAAAFDQLILTLRDALGLSVFLVTHDLD 211
Cdd:PRK10247 155 MPKVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKD 199
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
13-229 |
8.96e-13 |
|
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: 66.10 E-value: 8.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 13 IEVRGLCNRFGP--QSVHENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQNlpsLAEHERSLIERR 90
Cdd:cd03251 1 VEFKNVTFRYPGdgPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHD---VRDYTLASLRRQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 91 FGVLFQKGALFSSlTVTENVALpliehaGLSRA-DAEHLAAVKLALA-----GLPlsaaDKYPA-------SLSGGMIKR 157
Cdd:cd03251 78 IGLVSQDVFLFND-TVAENIAY------GRPGAtREEVEEAARAANAhefimELP----EGYDTvigergvKLSGGQRQR 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1316494952 158 AALARALALDPDILFLDEPTAGLDPIG----AAAFDQLiltlrdALGLSVFLVTHDLDTLYTItDRVAVLAQKKVL 229
Cdd:cd03251 147 IAIARALLKDPPILILDEATSALDTESerlvQAALERL------MKNRTTFVIAHRLSTIENA-DRIVVLEDGKIV 215
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
27-229 |
1.46e-12 |
|
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: 65.25 E-value: 1.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 27 VHENLDLDLYKGEILAVVGGSGSGKSvllrSIIGLRQ----PSEGSVRVFGQNLPSLA-EHERSLIerrfGVLFQKGALF 101
Cdd:cd03249 18 ILKGLSLTIPPGKTVALVGSSGCGKS----TVVSLLErfydPTSGEILLDGVDIRDLNlRWLRSQI----GLVSQEPVLF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 102 SSlTVTENVALpliehaGLSRADAEHL-AAVKLALA-----GLPlsaaDKYP-------ASLSGG----------MIKra 158
Cdd:cd03249 90 DG-TIAENIRY------GKPDATDEEVeEAAKKANIhdfimSLP----DGYDtlvgergSQLSGGqkqriaiaraLLR-- 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1316494952 159 alaralalDPDILFLDEPTAGLDP----IGAAAFDQLIltlrdaLGLSVFLVTHdldTLYTI--TDRVAVLAQKKVL 229
Cdd:cd03249 157 --------NPKILLLDEATSALDAesekLVQEALDRAM------KGRTTIVIAH---RLSTIrnADLIAVLQNGQVV 216
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
3-238 |
1.51e-12 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 66.92 E-value: 1.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 3 RSTRPPAEAVIEVRGLCNRFGPQSVHEN-LDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQNLPSLAE 81
Cdd:PRK10522 313 RPQAFPDWQTLELRNVTFAYQDNGFSVGpINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQP 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 82 HE-RSLierrFGVLFQKGALFSSLTVTEN-VALPLIEHAGLSRADAEHlaavKLALAGLPLSAADkypasLSGGMIKRAA 159
Cdd:PRK10522 393 EDyRKL----FSAVFTDFHLFDQLLGPEGkPANPALVEKWLERLKMAH----KLELEDGRISNLK-----LSKGQKKRLA 459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 160 LARALALDPDILFLDEPTAGLDPIGAAAFDQLILTLRDALGLSVFLVTHDlDTLYTITDRVAVLAQKKV--LVADAIDQV 237
Cdd:PRK10522 460 LLLALAEERDILLLDEWAADQDPHFRREFYQVLLPLLQEMGKTIFAISHD-DHYFIHADRLLEMRNGQLseLTGEERDAA 538
|
.
gi 1316494952 238 A 238
Cdd:PRK10522 539 S 539
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
35-228 |
1.52e-12 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 66.99 E-value: 1.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 35 LYKGEILAVVGGSGSGKSVLLrSIIGLRQPS----EGSVRVFGQNLpslaehERSLIERRFGVLFQKGALFSSLTVTENv 110
Cdd:TIGR00955 48 AKPGELLAVMGSSGAGKTTLM-NALAFRSPKgvkgSGSVLLNGMPI------DAKEMRAISAYVQQDDLFIPTLTVREH- 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 111 alpLIEHAGL----SRADAEHLAAVKLALAGLPL-SAAD------KYPASLSGGMIKRAALARALALDPDILFLDEPTAG 179
Cdd:TIGR00955 120 ---LMFQAHLrmprRVTKKEKRERVDEVLQALGLrKCANtrigvpGRVKGLSGGERKRLAFASELLTDPPLLFCDEPTSG 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1316494952 180 LDPIGAAafdQLILTLRDAL--GLSVFLVTHD-LDTLYTITDRVAVLAQKKV 228
Cdd:TIGR00955 197 LDSFMAY---SVVQVLKGLAqkGKTIICTIHQpSSELFELFDKIILMAEGRV 245
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
13-208 |
1.78e-12 |
|
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: 64.44 E-value: 1.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 13 IEVRGLCNRFGPQSVHENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQNLpslaEHERSLIERRFG 92
Cdd:cd03231 1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPL----DFQRDSIARGLL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 93 VLFQKGALFSSLTVTENVALPLIEHAGlsradaehlAAVKLALAGLPLSAADKYP-ASLSGGMIKRAALARALALDPDIL 171
Cdd:cd03231 77 YLGHAPGIKTTLSVLENLRFWHADHSD---------EQVEEALARVGLNGFEDRPvAQLSAGQQRRVALARLLLSGRPLW 147
|
170 180 190
....*....|....*....|....*....|....*..
gi 1316494952 172 FLDEPTAGLDPIGAAAFDQLiLTLRDALGLSVFLVTH 208
Cdd:cd03231 148 ILDEPTTALDKAGVARFAEA-MAGHCARGGMVVLTTH 183
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
30-257 |
2.04e-12 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 66.61 E-value: 2.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 30 NLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQNLPSLAEHER------SLIERRfgvlfQKGALFSS 103
Cdd:PRK15439 281 NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRlarglvYLPEDR-----QSSGLYLD 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 104 LTVTENVA------LPLIEHAGLSRADAEHLAAvklALaGLPLSAADKYPASLSGGMIKRAALARALALDPDILFLDEPT 177
Cdd:PRK15439 356 APLAWNVCalthnrRGFWIKPARENAVLERYRR---AL-NIKFNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPT 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 178 AGLDPIGAAAFDQLILTLRdALGLSVFLVTHDLDTLYTITDRVAVLAQKKV---LVADAIDQvaetdDTWIHEYFHGPRG 254
Cdd:PRK15439 432 RGVDVSARNDIYQLIRSIA-AQNVAVLFISSDLEEIEQMADRVLVMHQGEIsgaLTGAAINV-----DTIMRLAFGEHQA 505
|
...
gi 1316494952 255 RAA 257
Cdd:PRK15439 506 QEA 508
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
25-232 |
2.43e-12 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 64.90 E-value: 2.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 25 QSVHeNLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQNLpslAEHERSLIERRFGVLFQKGA-LFSS 103
Cdd:PRK11614 19 QALH-EVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDI---TDWQTAKIMREAVAIVPEGRrVFSR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 104 LTVTENVALpliehAGLSRADAEHLAAVKLALAGLP--LSAADKYPASLSGGMIKRAALARALALDPDILFLDEPTAGLD 181
Cdd:PRK11614 95 MTVEENLAM-----GGFFAERDQFQERIKWVYELFPrlHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLA 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1316494952 182 PIGAAAFDQLILTLRDAlGLSVFLVTHDLDTLYTITDRVAVLAQKKVLVAD 232
Cdd:PRK11614 170 PIIIQQIFDTIEQLREQ-GMTIFLVEQNANQALKLADRGYVLENGHVVLED 219
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
3-223 |
2.49e-12 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 66.18 E-value: 2.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 3 RSTRPPAEAVIEVRGLCnrfGPqSVHeNLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQNLpslaeH 82
Cdd:PRK10762 248 RLDKAPGEVRLKVDNLS---GP-GVN-DVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEV-----V 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 83 ERSLIER-RFGVLF----QKG-ALFSSLTVTENVALPLIEH----AGLSRADAEHLAAVK-LALAGLPLSAADKYPASLS 151
Cdd:PRK10762 318 TRSPQDGlANGIVYisedRKRdGLVLGMSVKENMSLTALRYfsraGGSLKHADEQQAVSDfIRLFNIKTPSMEQAIGLLS 397
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1316494952 152 GGMIKRAALARALALDPDILFLDEPTAGLDpIGAAA-FDQLILTLRdALGLSVFLVTHDLDTLYTITDRVAVL 223
Cdd:PRK10762 398 GGNQQKVAIARGLMTRPKVLILDEPTRGVD-VGAKKeIYQLINQFK-AEGLSIILVSSEMPEVLGMSDRILVM 468
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
29-229 |
9.88e-12 |
|
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: 62.54 E-value: 9.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 29 ENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLR--QPSEGSVRVFGQNLPSLAEHERSLieRRFGVLFQKGALFSSLTV 106
Cdd:cd03217 17 KGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKGEDITDLPPEERAR--LGIFLAFQYPPEIPGVKN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 107 tenvalpliehaglsradAEHLAAVKlalaglplsaadkypASLSGGMIKRAALARALALDPDILFLDEPTAGLDPIGAA 186
Cdd:cd03217 95 ------------------ADFLRYVN---------------EGFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALR 141
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1316494952 187 AFDQLILTLRDAlGLSVFLVTHDLDTL-YTITDRVAVLAQKKVL 229
Cdd:cd03217 142 LVAEVINKLREE-GKSVLIITHYQRLLdYIKPDRVHVLYDGRIV 184
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-239 |
1.58e-11 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 64.04 E-value: 1.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 1 MNRSTRPPA-EAVIEVRGLCNRFGPQSvhENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQNLPSL 79
Cdd:PRK09700 253 MKENVSNLAhETVFEVRNVTSRDRKKV--RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPR 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 80 AEhersLIERRFGVLF-----QKGALFSSLTVTENVAL-PLIEHAGLSRA-------DAEHLAAVKLALAGLPLSAADKY 146
Cdd:PRK09700 331 SP----LDAVKKGMAYitesrRDNGFFPNFSIAQNMAIsRSLKDGGYKGAmglfhevDEQRTAENQRELLALKCHSVNQN 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 147 PASLSGGMIKRAALARALALDPDILFLDEPTAGLDpIGAAA-FDQLILTLRDAlGLSVFLVTHDLDTLYTITDRVAVLAQ 225
Cdd:PRK09700 407 ITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGID-VGAKAeIYKVMRQLADD-GKVILMVSSELPEIITVCDRIAVFCE 484
|
250
....*....|....*
gi 1316494952 226 KKVL-VADAIDQVAE 239
Cdd:PRK09700 485 GRLTqILTNRDDMSE 499
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
9-237 |
3.84e-11 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 62.45 E-value: 3.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 9 AEAVIEVRGLCNRFGPQSVHENLDLDLYKGEILAVVG--GSGSGKSVLLRSIIGlrqPSEGSvRVFgqNLPSLAEHERSL 86
Cdd:NF000106 10 ARNAVEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGp*GAA**RGALPAHV*G---PDAGR-RPW--RF*TWCANRRAL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 87 iERRFGVLFQ-KGALFSSLTVTENVALpLIEHAGLSRADAEHLAAVKLALAGLPlSAADKYPASLSGGMIKRAALARALA 165
Cdd:NF000106 84 -RRTIG*HRPvR*GRRESFSGRENLYM-IGR*LDLSRKDARARADELLERFSLT-EAAGRAAAKYSGGMRRRLDLAASMI 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1316494952 166 LDPDILFLDEPTAGLDP-IGAAAFDQLILTLRDalGLSVFLVTHDLDTLYTITDRVAVLAQKKVLVADAIDQV 237
Cdd:NF000106 161 GRPAVLYLDEPTTGLDPrTRNEVWDEVRSMVRD--GATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDEL 231
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
23-223 |
4.71e-11 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 61.85 E-value: 4.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 23 GPQSVHENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPS----EGSVRVFGQNLPSLAEHER-SLIERRFGVLFQK 97
Cdd:COG4170 18 GRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDNwhvtADRFRWNGIDLLKLSPRERrKIIGREIAMIFQE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 98 GAlfSSLTVTENV------ALPLIEHAG--LSRADAEHLAAVKLaL--AGLPLSAA--DKYPASLSGGMIKRAALARALA 165
Cdd:COG4170 98 PS--SCLDPSAKIgdqlieAIPSWTFKGkwWQRFKWRKKRAIEL-LhrVGIKDHKDimNSYPHELTEGECQKVMIAMAIA 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1316494952 166 LDPDILFLDEPTAGLDPIGAAAFDQLILTLRDALGLSVFLVTHDLDTLYTITDRVAVL 223
Cdd:COG4170 175 NQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVL 232
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
12-223 |
4.80e-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: 62.53 E-value: 4.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 12 VIEVRGLCNRFGPQSVHENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQNLPSLAEHERSLIERRF 91
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTWDGEIYWSGSPLKASNIRDTERAGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 92 GVLFQKGALFSSLTVTENVAL-PLIEHAGLSRADAEHLAAVKLALAGLPLSAA-DKYPAS-LSGGMIKRAALARALALDP 168
Cdd:TIGR02633 81 VIIHQELTLVPELSVAENIFLgNEITLPGGRMAYNAMYLRAKNLLRELQLDADnVTRPVGdYGGGQQQLVEIAKALNKQA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1316494952 169 DILFLDEPTAGLDpigAAAFDQLILTLRD--ALGLSVFLVTHDLDTLYTITDRVAVL 223
Cdd:TIGR02633 161 RLLILDEPSSSLT---EKETEILLDIIRDlkAHGVACVYISHKLNEVKAVCDTICVI 214
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
29-236 |
5.52e-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: 62.15 E-value: 5.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 29 ENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPS-EGSVRVFGQ--NLPSLAEHERSLI----ERRfgvlfQKGALF 101
Cdd:TIGR02633 277 DDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKpvDIRNPAQAIRAGIamvpEDR-----KRHGIV 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 102 SSLTVTENVALPLIE-HAGLSRADAE-HLAAVKLALAGLPLSAA--DKYPASLSGGMIKRAALARALALDPDILFLDEPT 177
Cdd:TIGR02633 352 PILGVGKNITLSVLKsFCFKMRIDAAaELQIIGSAIQRLKVKTAspFLPIGRLSGGNQQKAVLAKMLLTNPRVLILDEPT 431
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1316494952 178 AGLDpIGAAAFDQLILTLRDALGLSVFLVTHDLDTLYTITDRVAVLAQKKV---LVADAIDQ 236
Cdd:TIGR02633 432 RGVD-VGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGKLkgdFVNHALTQ 492
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
10-229 |
5.64e-11 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 61.34 E-value: 5.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 10 EAVIEVRGLCNR-------FGPQSVH--ENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQNLPSLA 80
Cdd:PRK15112 2 ETLLEVRNLSKTfryrtgwFRRQTVEavKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 81 EHERSlieRRFGVLFQKGAlfSSLTVTENVA----LPLIEHAGLSRADAEHLAAVKLALAGLPLSAADKYPASLSGGMIK 156
Cdd:PRK15112 82 YSYRS---QRIRMIFQDPS--TSLNPRQRISqildFPLRLNTDLEPEQREKQIIETLRQVGLLPDHASYYPHMLAPGQKQ 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1316494952 157 RAALARALALDPDILFLDEPTAGLDPIGAAAFDQLILTLRDALGLSVFLVTHDLDTLYTITDRVAVLAQKKVL 229
Cdd:PRK15112 157 RLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVV 229
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
7-71 |
5.71e-11 |
|
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: 62.26 E-value: 5.71e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1316494952 7 PPAE----AVIEVRGLCNRFGPQSVHENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRV 71
Cdd:TIGR03719 313 PPGPrlgdKVIEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI 381
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
5-228 |
6.17e-11 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 62.05 E-value: 6.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 5 TRPPAEAVIEVRGLCNRFGPqSVhENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQNLPSLAEHER 84
Cdd:PRK10982 243 ENKPGEVILEVRNLTSLRQP-SI-RDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANEA 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 85 -----SLI--ERRfgvlfqKGALFSSLTVTENVALPLIE----HAGLsRADAEHLAAVKLALAGLPLsaadKYPA----- 148
Cdd:PRK10982 321 inhgfALVteERR------STGIYAYLDIGFNSLISNIRnyknKVGL-LDNSRMKSDTQWVIDSMRV----KTPGhrtqi 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 149 -SLSGGMIKRAALARALALDPDILFLDEPTAGLDpIGaAAFD--QLILTLRDAlGLSVFLVTHDLDTLYTITDRVAVLAQ 225
Cdd:PRK10982 390 gSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGID-VG-AKFEiyQLIAELAKK-DKGIIIISSEMPELLGITDRILVMSN 466
|
...
gi 1316494952 226 KKV 228
Cdd:PRK10982 467 GLV 469
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
15-228 |
9.33e-11 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 61.62 E-value: 9.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 15 VRGLCNRFGPQSVHENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVfGQNLpslaeherslierRFGVL 94
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSI-PKGL-------------RIGYL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 95 FQKGALFSSLTVTENVA------------LPLIEHA-GLSRADAEHLAAVKLALA------------------GLPLSAA 143
Cdd:COG0488 67 PQEPPLDDDLTVLDTVLdgdaelraleaeLEELEAKlAEPDEDLERLAELQEEFEalggweaearaeeilsglGFPEEDL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 144 DKYPASLSGGMIKRAALARALALDPDILFLDEPTAGLDpIGAaafdqlILTLRDAL----GlSVFLVTHDLDTLYTITDR 219
Cdd:COG0488 147 DRPVSELSGGWRRRVALARALLSEPDLLLLDEPTNHLD-LES------IEWLEEFLknypG-TVLVVSHDRYFLDRVATR 218
|
....*....
gi 1316494952 220 VAVLAQKKV 228
Cdd:COG0488 219 ILELDRGKL 227
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
31-211 |
1.65e-10 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 59.80 E-value: 1.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 31 LDLDLYKGEILAVVGGSGSGKSVLLRsIIGLRQ-PSEGSVRVFGQnlpSLAEHERSLIERRFGVLFQKGALFSSLTVTEN 109
Cdd:PRK10575 30 LSLTFPAGKVTGLIGHNGSGKSTLLK-MLGRHQpPSEGEILLDAQ---PLESWSSKAFARKVAYLPQQLPAAEGMTVREL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 110 VAL---PLieHAGLSRADAEHLAAVK--LALAGL-PLsaADKYPASLSGGMIKRAALARALALDPDILFLDEPTAGLDPI 183
Cdd:PRK10575 106 VAIgryPW--HGALGRFGAADREKVEeaISLVGLkPL--AHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIA 181
|
170 180
....*....|....*....|....*...
gi 1316494952 184 GAAAFDQLILTLRDALGLSVFLVTHDLD 211
Cdd:PRK10575 182 HQVDVLALVHRLSQERGLTVIAVLHDIN 209
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
38-229 |
3.31e-10 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 60.28 E-value: 3.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 38 GEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQNLPSLAEherslIERRFGVLFQKGALFSSLTVTENVALPLIEH 117
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAGRIQGNNFTGTILANNRKPTKQ-----ILKRTGFVTQDDILYPHLTVRETLVFCSLLR 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 118 AGLSRADAEHLAAVKLALAGLPLSA------ADKYPASLSGGMIKRAALARALALDPDILFLDEPTAGLDpigAAAFDQL 191
Cdd:PLN03211 169 LPKSLTKQEKILVAESVISELGLTKcentiiGNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLD---ATAAYRL 245
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1316494952 192 ILTLRDAL--GLSVFLVTHDLDT-LYTITDRVAVLAQKKVL 229
Cdd:PLN03211 246 VLTLGSLAqkGKTIVTSMHQPSSrVYQMFDSVLVLSEGRCL 286
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
9-241 |
3.36e-10 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 59.94 E-value: 3.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 9 AEAVIEVRGLCNRFGPQSVHENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLrQPS---EGSVRVFGQNL--PSLAEHE 83
Cdd:PRK13549 2 MEYLLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGV-YPHgtyEGEIIFEGEELqaSNIRDTE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 84 RSLIerrfGVLFQKGALFSSLTVTENVAL-PLIEHAGLSRADAEHLAAVKLaLAGLPLSAADKYPAS-LSGGMIKRAALA 161
Cdd:PRK13549 81 RAGI----AIIHQELALVKELSVLENIFLgNEITPGGIMDYDAMYLRAQKL-LAQLKLDINPATPVGnLGLGQQQLVEIA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 162 RALALDPDILFLDEPTAGLDpigAAAFDQLILTLRD--ALGLSVFLVTHDLDTLYTITDRVAVLAQKKVLVADAIDQVAE 239
Cdd:PRK13549 156 KALNKQARLLILDEPTASLT---ESETAVLLDIIRDlkAHGIACIYISHKLNEVKAISDTICVIRDGRHIGTRPAAGMTE 232
|
..
gi 1316494952 240 TD 241
Cdd:PRK13549 233 DD 234
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
30-228 |
5.07e-10 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 58.15 E-value: 5.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 30 NLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLR--QPSEGSVRVFGQNLPSLAEHERSlierRFGVL--FQKGALFSSLT 105
Cdd:COG0396 18 GVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPkyEVTSGSILLDGEDILELSPDERA----RAGIFlaFQYPVEIPGVS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 106 VTE--NVALPLIEHAGLSRADAEHLAAVKLALAGLPLSAADKY-PASLSGGMIKRAALARALALDPDILFLDEPTAGLDp 182
Cdd:COG0396 94 VSNflRTALNARRGEELSAREFLKLLKEKMKELGLDEDFLDRYvNEGFSGGEKKRNEILQMLLLEPKLAILDETDSGLD- 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1316494952 183 igAAAFDQL---ILTLRDAlGLSVFLVTHD---LDtlYTITDRVAVLAQKKV 228
Cdd:COG0396 173 --IDALRIVaegVNKLRSP-DRGILIITHYqriLD--YIKPDFVHVLVDGRI 219
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
13-227 |
6.12e-10 |
|
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: 56.30 E-value: 6.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 13 IEVRGLCNRFGPQSVHENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVfGQNLpslaeherslierRFG 92
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTW-GSTV-------------KIG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 93 VLFQkgalfssltvtenvalpliehagLSraDAEHlaaVKLALAGLPLSaadkypaslsggmikraalaralalDPDILF 172
Cdd:cd03221 67 YFEQ-----------------------LS--GGEK---MRLALAKLLLE-------------------------NPNLLL 93
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1316494952 173 LDEPTAGLDPIGAAAFDQLILTLRDAlglsVFLVTHDLDTLYTITDRVAVLAQKK 227
Cdd:cd03221 94 LDEPTNHLDLESIEALEEALKEYPGT----VILVSHDRYFLDQVATKIIELEDGK 144
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
3-236 |
7.08e-10 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 58.79 E-value: 7.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 3 RSTRPPAEAVIEVRGLCNrFGPQSVH----ENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQ-PSEGSVRVFGQnlP 77
Cdd:PRK13549 250 REPHTIGEVILEVRNLTA-WDPVNPHikrvDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPgRWEGEIFIDGK--P 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 78 SLAEHERSLIE----------RRFGVLFQKGalfssltVTENVALP-LIEHAGLSRADAEH-LAAVKLALAGLPLSAADk 145
Cdd:PRK13549 327 VKIRNPQQAIAqgiamvpedrKRDGIVPVMG-------VGKNITLAaLDRFTGGSRIDDAAeLKTILESIQRLKVKTAS- 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 146 yP----ASLSGGMIKRAALARALALDPDILFLDEPTAGLDpIGAAAfdqLILTLRDAL---GLSVFLVTHDLDTLYTITD 218
Cdd:PRK13549 399 -PelaiARLSGGNQQKAVLAKCLLLNPKILILDEPTRGID-VGAKY---EIYKLINQLvqqGVAIIVISSELPEVLGLSD 473
|
250 260
....*....|....*....|.
gi 1316494952 219 RVAVLAQKKV---LVADAIDQ 236
Cdd:PRK13549 474 RVLVMHEGKLkgdLINHNLTQ 494
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
5-229 |
8.66e-10 |
|
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: 58.57 E-value: 8.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 5 TRPP--AEAVIEVRGLCNRFGPQSVH--ENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQnlpSLA 80
Cdd:TIGR02203 321 TRAIerARGDVEFRNVTFRYPGRDRPalDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGH---DLA 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 81 EHERSLIERRFGVLFQKGALFSSlTVTENVALPLIEHAGlsraDAEHLAAVKLALAglpLSAADKYP-----------AS 149
Cdd:TIGR02203 398 DYTLASLRRQVALVSQDVVLFND-TIANNIAYGRTEQAD----RAEIERALAAAYA---QDFVDKLPlgldtpigengVL 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 150 LSGGMIKRAALARALALDPDILFLDEPTAGLDPIG----AAAFDQLIltlrdaLGLSVFLVTHDLDTLYTiTDRVAVLAQ 225
Cdd:TIGR02203 470 LSGGQRQRLAIARALLKDAPILILDEATSALDNESerlvQAALERLM------QGRTTLVIAHRLSTIEK-ADRIVVMDD 542
|
....
gi 1316494952 226 KKVL 229
Cdd:TIGR02203 543 GRIV 546
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
30-223 |
1.09e-09 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 58.38 E-value: 1.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 30 NLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQnlPSLAEHERSLIERRFGVLFQKGALFSSLTVTEN 109
Cdd:PRK11288 22 DISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQ--EMRFASTTAALAAGVAIIYQELHLVPEMTVAEN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 110 VALPLIEHAG--LSRADAEHLAAVKLALAGLPLSAADKYpASLSGGMIKRAALARALALDPDILFLDEPTAGLDpigAAA 187
Cdd:PRK11288 100 LYLGQLPHKGgiVNRRLLNYEAREQLEHLGVDIDPDTPL-KYLSIGQRQMVEIAKALARNARVIAFDEPTSSLS---ARE 175
|
170 180 190
....*....|....*....|....*....|....*....
gi 1316494952 188 FDQL---ILTLRDAlGLSVFLVTHDLDTLYTITDRVAVL 223
Cdd:PRK11288 176 IEQLfrvIRELRAE-GRVILYVSHRMEEIFALCDAITVF 213
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
7-211 |
2.03e-09 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 56.12 E-value: 2.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 7 PPAEAVIEVRGLCNRFGPQSVHENLDLDLYKGEILAVVGGSGSGKSVLLRSIIG--LRQPSEGSVRVFGQNLPSlaehER 84
Cdd:COG2401 25 ERVAIVLEAFGVELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGalKGTPVAGCVDVPDNQFGR----EA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 85 SLIErrfgvlfqkgALFSSLTVTENVALpliehaglsradaehLAAVKLALAGLPLsaadKYPASLSGGMIKRAALARAL 164
Cdd:COG2401 101 SLID----------AIGRKGDFKDAVEL---------------LNAVGLSDAVLWL----RRFKELSTGQKFRFRLALLL 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1316494952 165 ALDPDILFLDEPTAGLDPIGAAAFDQLILTLRDALGLSVFLVTHDLD 211
Cdd:COG2401 152 AERPKLLVIDEFCSHLDRQTAKRVARNLQKLARRAGITLVVATHHYD 198
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
30-228 |
2.35e-09 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 57.55 E-value: 2.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 30 NLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLrQPSEGSVRVFGQNLPSLaehERSLIERRFGVLFQKGALFSSlTVTEN 109
Cdd:PRK11174 368 PLNFTLPAGQRIALVGPSGAGKTSLLNALLGF-LPYQGSLKINGIELREL---DPESWRKHLSWVGQNPQLPHG-TLRDN 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 110 VALpliehaGLSRADAEHL-AAVKLA-----LAGLPL---SAADKYPASLSGGMIKRAALARALALDPDILFLDEPTAGL 180
Cdd:PRK11174 443 VLL------GNPDASDEQLqQALENAwvsefLPLLPQgldTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASL 516
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1316494952 181 DpigaAAFDQLIL-TLRDA-LGLSVFLVTHDLDTLYTItDRVAVLAQKKV 228
Cdd:PRK11174 517 D----AHSEQLVMqALNAAsRRQTTLMVTHQLEDLAQW-DQIWVMQDGQI 561
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
13-74 |
4.24e-09 |
|
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: 56.73 E-value: 4.24e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1316494952 13 IEVRGLCNRF-----------GPqsvhenLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQ 74
Cdd:COG4615 328 LELRGVTYRYpgedgdegftlGP------IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQ 394
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
7-71 |
4.50e-09 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 56.67 E-value: 4.50e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1316494952 7 PPAE----AVIEVRGLCNRFGPQSVHENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRV 71
Cdd:PRK11819 315 PPGPrlgdKVIEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI 383
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
12-223 |
4.77e-09 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 55.96 E-value: 4.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 12 VIEVRGLCNRF----GPQSVHENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLrqpSEGSVRVFGQ-------NLPSLA 80
Cdd:PRK15093 3 LLDIRNLTIEFktsdGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGV---TKDNWRVTADrmrfddiDLLRLS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 81 EHER-SLIERRFGVLFQKGAlfSSLTVTENVALPLIE------HAG--LSRADAEHLAAVKLA-LAGL--PLSAADKYPA 148
Cdd:PRK15093 80 PRERrKLVGHNVSMIFQEPQ--SCLDPSERVGRQLMQnipgwtYKGrwWQRFGWRKRRAIELLhRVGIkdHKDAMRSFPY 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1316494952 149 SLSGGMIKRAALARALALDPDILFLDEPTAGLDPIGAAAFDQLILTLRDALGLSVFLVTHDLDTLYTITDRVAVL 223
Cdd:PRK15093 158 ELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVL 232
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
37-208 |
4.98e-09 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 54.56 E-value: 4.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 37 KGEILAVVGGSGSGKSVLL-----RSIIGLRqpsEGSVRVFGQNLPSLaeherslIERRFGVLFQKGALFSSLTVTEnva 111
Cdd:cd03232 32 PGTLTALMGESGAGKTTLLdvlagRKTAGVI---TGEILINGRPLDKN-------FQRSTGYVEQQDVHSPNLTVRE--- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 112 lPLIEHA---GLSRADAEHLA-AVKLAlaglplsaadkypaslsggmikraalaralaLDPDILFLDEPTAGLDPIGAAA 187
Cdd:cd03232 99 -ALRFSAllrGLSVEQRKRLTiGVELA-------------------------------AKPSILFLDEPTSGLDSQAAYN 146
|
170 180
....*....|....*....|.
gi 1316494952 188 FDQLILTLRDAlGLSVFLVTH 208
Cdd:cd03232 147 IVRFLKKLADS-GQAILCTIH 166
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
27-228 |
5.81e-09 |
|
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: 54.78 E-value: 5.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 27 VHENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQNLPslaEHERSLIERRFGVLFQKGALFSSlTV 106
Cdd:cd03248 29 VLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPIS---QYEHKYLHSKVSLVGQEPVLFAR-SL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 107 TENVALPLIEHAGLSRADAEHLAAVKLALAGLPL---SAADKYPASLSGGMIKRAALARALALDPDILFLDEPTAGLDPI 183
Cdd:cd03248 105 QDNIAYGLQSCSFECVKEAAQKAHAHSFISELASgydTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAE 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1316494952 184 GAAAFDQLiltLRDAL-GLSVFLVTHDLDTLYTiTDRVAVLAQKKV 228
Cdd:cd03248 185 SEQQVQQA---LYDWPeRRTVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
29-229 |
6.01e-09 |
|
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: 56.29 E-value: 6.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 29 ENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQNLPSLAEHE-RSLIErrfgVLFQKGALFSSlTVT 107
Cdd:TIGR01193 491 SDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTlRQFIN----YLPQEPYIFSG-SIL 565
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 108 ENVALPLIEHAGLSRAD-AEHLAAVKLALAGLPL---SAADKYPASLSGGMIKRAALARALALDPDILFLDEPTAGLDPI 183
Cdd:TIGR01193 566 ENLLLGAKENVSQDEIWaACEIAEIKDDIENMPLgyqTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTI 645
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1316494952 184 GAAAFDQLILTLRDAlglSVFLVTHDLdTLYTITDRVAVLAQKKVL 229
Cdd:TIGR01193 646 TEKKIVNNLLNLQDK---TIIFVAHRL-SVAKQSDKIIVLDHGKII 687
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
23-223 |
8.38e-09 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 55.23 E-value: 8.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 23 GPQSVHENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQNLPSLAEHERSLierrfGVLFQKGALFS 102
Cdd:PRK11650 15 GKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPADRDI-----AMVFQNYALYP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 103 SLTVTENVALPLiEHAGLSRAD-----AEhlAAVKLALAGLplsaADKYPASLSGG----------MIKraalaralalD 167
Cdd:PRK11650 90 HMSVRENMAYGL-KIRGMPKAEieervAE--AARILELEPL----LDRKPRELSGGqrqrvamgraIVR----------E 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1316494952 168 PDILFLDEPTAGLDpigAAAFDQL---ILTLRDALGLSVFLVTHDLDTLYTITDRVAVL 223
Cdd:PRK11650 153 PAVFLFDEPLSNLD---AKLRVQMrleIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVM 208
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
30-229 |
1.12e-08 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 54.45 E-value: 1.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 30 NLDLDLYKGEILAVVGGSGSGKSVLLRSIIG-LRQP-SEGSVRVFGQ---NLPSLAEHERSLIERRFGVLFQKGALFSSL 104
Cdd:PRK13547 19 DLSLRIEPGRVTALLGRNGAGKSTLLKALAGdLTGGgAPRGARVTGDvtlNGEPLAAIDAPRLARLRAVLPQAAQPAFAF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 105 TVTENVALPLIEHA----GLSRADAEhLAAVKLALAGL-PLSAADKypASLSGG---------MIKRAALARALALDPDI 170
Cdd:PRK13547 99 SAREIVLLGRYPHArragALTHRDGE-IAWQALALAGAtALVGRDV--TTLSGGelarvqfarVLAQLWPPHDAAQPPRY 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1316494952 171 LFLDEPTAGLDpigAAAFDQLILTLRDA---LGLSVFLVTHDLDTLYTITDRVAVLAQKKVL 229
Cdd:PRK13547 176 LLLDEPTAALD---LAHQHRLLDTVRRLardWNLGVLAIVHDPNLAARHADRIAMLADGAIV 234
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
38-228 |
1.16e-08 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 55.35 E-value: 1.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 38 GEILAVVGGSGSGKSVLlrsiIGLRQ----PSEGSVRVFGQNLPSLAeheRSLIERRFGVLFQKGALFSSlTVTENVALp 113
Cdd:PRK13657 361 GQTVAIVGPTGAGKSTL----INLLQrvfdPQSGRILIDGTDIRTVT---RASLRRNIAVVFQDAGLFNR-SIEDNIRV- 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 114 liehaGLSRA-DAEHLAAVKLALA-GLPLSAADKYPA-------SLSGGMIKRAALARALALDPDILFLDEPTAGLDPIG 184
Cdd:PRK13657 432 -----GRPDAtDEEMRAAAERAQAhDFIERKPDGYDTvvgergrQLSGGERQRLAIARALLKDPPILILDEATSALDVET 506
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1316494952 185 AAAFDQLILTLRDalGLSVFLVTHDLDTLYTiTDRVAVLAQKKV 228
Cdd:PRK13657 507 EAKVKAALDELMK--GRTTFIIAHRLSTVRN-ADRILVFDNGRV 547
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
12-76 |
2.27e-08 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 52.88 E-value: 2.27e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1316494952 12 VIEVRGL-CNRfGPQSVHENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQNL 76
Cdd:PRK13538 1 MLEARNLaCER-DERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPI 65
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
29-208 |
2.55e-08 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 54.43 E-value: 2.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 29 ENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRvfgqnLPSLAEherslierrfgVLF--QK-----GALf 101
Cdd:COG4178 380 EDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIA-----RPAGAR-----------VLFlpQRpylplGTL- 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 102 ssltvTENVALPLIEHAglsrADAEHLAAVkLALAGLP-----LSAADKYPASLSGG-----------MIKraalarala 165
Cdd:COG4178 443 -----REALLYPATAEA----FSDAELREA-LEAVGLGhlaerLDEEADWDQVLSLGeqqrlafarllLHK--------- 503
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1316494952 166 ldPDILFLDEPTAGLDPIGAAAFDQLiltLRDAL-GLSVFLVTH 208
Cdd:COG4178 504 --PDWLFLDEATSALDEENEAALYQL---LREELpGTTVISVGH 542
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
38-224 |
3.92e-08 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 52.96 E-value: 3.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 38 GEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQnlPSLAEHERSLI---------ERRFGVLfqkgalfssltVTE 108
Cdd:PRK15056 33 GSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQ--PTRQALQKNLVayvpqseevDWSFPVL-----------VED 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 109 NVALPLIEHAG-LSRADAEHLAAVKLALAGLPLSA-ADKYPASLSGGMIKRAALARALALDPDILFLDEPTAGLDPIGAA 186
Cdd:PRK15056 100 VVMMGRYGHMGwLRRAKKRDRQIVTAALARVDMVEfRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEA 179
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1316494952 187 AFDQLILTLRDAlGLSVFLVTHDLDTL-----YTITDRVAVLA 224
Cdd:PRK15056 180 RIISLLRELRDE-GKTMLVSTHNLGSVtefcdYTVMVKGTVLA 221
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
9-209 |
6.02e-08 |
|
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: 53.02 E-value: 6.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 9 AEAVIEVRGLCNRFGPQ-SVHENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRvfgqnlPSLAehersli 87
Cdd:TIGR03719 1 AQYIYTMNRVSKVVPPKkEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEAR------PQPG------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 88 eRRFGVLFQKGALFSSLTVTENV--ALPLIEHAgLSR------------ADAEHLAA--------------------VKL 133
Cdd:TIGR03719 68 -IKVGYLPQEPQLDPTKTVRENVeeGVAEIKDA-LDRfneisakyaepdADFDKLAAeqaelqeiidaadawdldsqLEI 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1316494952 134 ALAGLPLSAADKYPASLSGGMIKRAALARALALDPDILFLDEPTAGLDpigAAAFDQLILTLRDALGlSVFLVTHD 209
Cdd:TIGR03719 146 AMDALRCPPWDADVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLD---AESVAWLERHLQEYPG-TVVAVTHD 217
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
26-229 |
1.78e-07 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 50.95 E-value: 1.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 26 SVHEN-----LDLDLYKGEILAVVGGSGSGKSVLLRSIIGLR--QPSEGSVRVFGQNLPSLAEHERSLiERRFgVLFQ-- 96
Cdd:PRK09580 10 SVEDKailrgLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLELSPEDRAG-EGIF-MAFQyp 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 97 ------KGALFssLTVTENVALPLIEHAGLSRADAEHLAAVKLALAGLPlsaADKYPASL----SGGMIKRAALARALAL 166
Cdd:PRK09580 88 veipgvSNQFF--LQTALNAVRSYRGQEPLDRFDFQDLMEEKIALLKMP---EDLLTRSVnvgfSGGEKKRNDILQMAVL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1316494952 167 DPDILFLDEPTAGLDPIGAAAFDQLILTLRDAlGLSVFLVTHDLDTL-YTITDRVAVLAQKKVL 229
Cdd:PRK09580 163 EPELCILDESDSGLDIDALKIVADGVNSLRDG-KRSFIIVTHYQRILdYIKPDYVHVLYQGRIV 225
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
38-225 |
3.66e-07 |
|
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: 51.17 E-value: 3.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 38 GEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQN-LPSLAEherslIERRFGVLFQKGALFSSLTVTENVALplie 116
Cdd:TIGR01257 1965 GECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSiLTNISD-----VHQNMGYCPQFDAIDDLLTGREHLYL---- 2035
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 117 HAGLSRADAEHLAAV-KLALAGLPLSA-ADKYPASLSGGMIKRAALARALALDPDILFLDEPTAGLDPIGAAAFDQLILT 194
Cdd:TIGR01257 2036 YARLRGVPAEEIEKVaNWSIQSLGLSLyADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVS 2115
|
170 180 190
....*....|....*....|....*....|..
gi 1316494952 195 -LRDalGLSVFLVTHDLDTLYTITDRVAVLAQ 225
Cdd:TIGR01257 2116 iIRE--GRAVVLTSHSMEECEALCTRLAIMVK 2145
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
30-181 |
5.66e-07 |
|
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: 50.20 E-value: 5.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 30 NLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQNLPSLAEHerSLieRR-FGVLFQKGALFSSlTVTE 108
Cdd:COG5265 376 GVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQA--SL--RAaIGIVPQDTVLFND-TIAY 450
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 109 NVALPlieHAGLSRADAEhlAAVKLA-----LAGLPlsaaDKYPAS-------LSGG----------MIKraalaralal 166
Cdd:COG5265 451 NIAYG---RPDASEEEVE--AAARAAqihdfIESLP----DGYDTRvgerglkLSGGekqrvaiartLLK---------- 511
|
170
....*....|....*
gi 1316494952 167 DPDILFLDEPTAGLD 181
Cdd:COG5265 512 NPPILIFDEATSALD 526
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
22-192 |
7.18e-07 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 48.69 E-value: 7.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 22 FGPqsvhenLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQnlpSLAEHERSlieRRFGVLFQKGALF 101
Cdd:PRK13543 27 FGP------LDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGK---TATRGDRS---RFMAYLGHLPGLK 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 102 SSLTVTENVALPliehAGLSRADAEHLAAVKLALAGLPlSAADKYPASLSGGMIKRAALARALALDPDILFLDEPTAGLD 181
Cdd:PRK13543 95 ADLSTLENLHFL----CGLHGRRAKQMPGSALAIVGLA-GYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLD 169
|
170
....*....|.
gi 1316494952 182 PIGAAAFDQLI 192
Cdd:PRK13543 170 LEGITLVNRMI 180
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
29-73 |
7.77e-07 |
|
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: 48.62 E-value: 7.77e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1316494952 29 ENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFG 73
Cdd:cd03250 22 KDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG 66
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
27-74 |
9.78e-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: 49.91 E-value: 9.78e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1316494952 27 VHENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQ 74
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR 488
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
3-252 |
1.23e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 49.59 E-value: 1.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 3 RSTRP----PAEAVIEVRGLCNRFGPQ--SVHENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQNL 76
Cdd:PLN03232 1221 ENNRPvsgwPSRGSIKFEDVHLRYRPGlpPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDV 1300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 77 pslAEHERSLIERRFGVLFQKGALFSSlTVTENVAlPLIEHAGLSRADAEHLAAVKLALAGLPL---SAADKYPASLSGG 153
Cdd:PLN03232 1301 ---AKFGLTDLRRVLSIIPQSPVLFSG-TVRFNID-PFSEHNDADLWEALERAHIKDVIDRNPFgldAEVSEGGENFSVG 1375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 154 MIKRAALARALALDPDILFLDEPTAGLDpigaAAFDQLIL-TLRDAL-GLSVFLVTHDLDTLYTiTDRVAVLAQKKVLVA 231
Cdd:PLN03232 1376 QRQLLSLARALLRRSKILVLDEATASVD----VRTDSLIQrTIREEFkSCTMLVIAHRLNTIID-CDKILVLSSGQVLEY 1450
|
250 260
....*....|....*....|...
gi 1316494952 232 DAIDQVAETDDTWIHEYFH--GP 252
Cdd:PLN03232 1451 DSPQELLSRDTSAFFRMVHstGP 1473
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
25-208 |
1.25e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 48.02 E-value: 1.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 25 QSVHENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQNLpslaEHERSLIERRFGVLFQKGALFSSL 104
Cdd:PRK13540 14 QPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSI----KKDLCTYQKQLCFVGHRSGINPYL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 105 TVTENVALPLieHAGLSRADAEHLAAVklalagLPLSAADKYPAS-LSGGMIKRAALARALALDPDILFLDEPTAGLDPI 183
Cdd:PRK13540 90 TLRENCLYDI--HFSPGAVGITELCRL------FSLEHLIDYPCGlLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDEL 161
|
170 180
....*....|....*....|....*
gi 1316494952 184 GAAAFDQLILTLRdALGLSVFLVTH 208
Cdd:PRK13540 162 SLLTIITKIQEHR-AKGGAVLLTSH 185
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
27-74 |
1.62e-06 |
|
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: 48.31 E-value: 1.62e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1316494952 27 VHENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQ 74
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR 99
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
5-233 |
1.81e-06 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 48.79 E-value: 1.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 5 TRPPA----EAVIEVRGLCNRFGP--QSVHENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQNLPS 78
Cdd:TIGR00957 1273 TAPPSgwppRGRVEFRNYCLRYREdlDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAK 1352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 79 LAEHErslIERRFGVLFQKGALFSSlTVTENVAlPLIEHAGLSRADAEHLAAVKLALAGLPlSAADKYPA----SLSGGM 154
Cdd:TIGR00957 1353 IGLHD---LRFKITIIPQDPVLFSG-SLRMNLD-PFSQYSDEEVWWALELAHLKTFVSALP-DKLDHECAeggeNLSVGQ 1426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 155 IKRAALARALALDPDILFLDEPTAGLDpigaAAFDQLI-LTLRDAL-GLSVFLVTHDLDTLYTITdRVAVLAQKKVLVAD 232
Cdd:TIGR00957 1427 RQLVCLARALLRKTKILVLDEATAAVD----LETDNLIqSTIRTQFeDCTVLTIAHRLNTIMDYT-RVIVLDKGEVAEFG 1501
|
.
gi 1316494952 233 A 233
Cdd:TIGR00957 1502 A 1502
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
6-225 |
2.34e-06 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 48.37 E-value: 2.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 6 RPPAEAVIEVRGLcnrFGPqSVHENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQNLPSlaeheRS 85
Cdd:PRK11288 251 RPLGEVRLRLDGL---KGP-GLREPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDI-----RS 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 86 LIER-RFGVLF-----QKGALFSSLTVTENVALPLIEH---AGL---SRADAEhLAAVKLALAGLPLSAADKYPASLSGG 153
Cdd:PRK11288 322 PRDAiRAGIMLcpedrKAEGIIPVHSVADNINISARRHhlrAGClinNRWEAE-NADRFIRSLNIKTPSREQLIMNLSGG 400
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1316494952 154 MIKRAALARALALDPDILFLDEPTAGLDpIGAAA-FDQLILTLRDAlGLSVFLVTHDLDTLYTITDRVAVLAQ 225
Cdd:PRK11288 401 NQQKAILGRWLSEDMKVILLDEPTRGID-VGAKHeIYNVIYELAAQ-GVAVLFVSSDLPEVLGVADRIVVMRE 471
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
30-213 |
2.75e-06 |
|
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: 46.94 E-value: 2.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 30 NLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRvFGQNLPSLAEHERSLIERRFGVLF--QKGALFSSlTVT 107
Cdd:cd03290 19 NINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVH-WSNKNESEPSFEATRSRNRYSVAYaaQKPWLLNA-TVE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 108 ENVALPliehaglSRADAEHLAAVKLALAGLP----LSAADKYP-----ASLSGGMIKRAALARALALDPDILFLDEPTA 178
Cdd:cd03290 97 ENITFG-------SPFNKQRYKAVTDACSLQPdidlLPFGDQTEigergINLSGGQRQRICVARALYQNTNIVFLDDPFS 169
|
170 180 190
....*....|....*....|....*....|....*.
gi 1316494952 179 GLD-PIGAAAFDQLILTLRDALGLSVFLVTHDLDTL 213
Cdd:cd03290 170 ALDiHLSDHLMQEGILKFLQDDKRTLVLVTHKLQYL 205
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
29-181 |
2.93e-06 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 48.09 E-value: 2.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 29 ENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQNLpslAEHERSLIERRFGVLFQKGALFSSlTVTE 108
Cdd:PRK11176 360 RNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDL---RDYTLASLRNQVALVSQNVHLFND-TIAN 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 109 NVALPLIEHagLSRADAEHlaAVKLALAglpLSAADKYP-----------ASLSGGMIKRAALARALALDPDILFLDEPT 177
Cdd:PRK11176 436 NIAYARTEQ--YSREQIEE--AARMAYA---MDFINKMDngldtvigengVLLSGGQRQRIAIARALLRDSPILILDEAT 508
|
....
gi 1316494952 178 AGLD 181
Cdd:PRK11176 509 SALD 512
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
13-70 |
5.37e-06 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 47.19 E-value: 5.37e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1316494952 13 IEVRGLCNRFGPQSVHENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVR 70
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVK 377
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
12-229 |
7.01e-06 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 46.17 E-value: 7.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 12 VIEVRGLCNRFGPQSVHENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGlrQPS----EGSVRVFGQNLPSLAEHERSli 87
Cdd:CHL00131 7 ILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG--HPAykilEGDILFKGESILDLEPEERA-- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 88 erRFGVL--FQkgalfssltvtenvaLPlIEHAGLSRADAEHLA-AVKLALAGLP--------------LSAADKYPASL 150
Cdd:CHL00131 83 --HLGIFlaFQ---------------YP-IEIPGVSNADFLRLAyNSKRKFQGLPeldplefleiinekLKLVGMDPSFL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 151 --------SGGMIKRAALARALALDPDILFLDEPTAGLDPIGAAAFDQLILTLRDAlGLSVFLVTHD---LDtlYTITDR 219
Cdd:CHL00131 145 srnvnegfSGGEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTS-ENSIILITHYqrlLD--YIKPDY 221
|
250
....*....|
gi 1316494952 220 VAVLAQKKVL 229
Cdd:CHL00131 222 VHVMQNGKII 231
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
33-223 |
1.10e-05 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 46.15 E-value: 1.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 33 LDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQNL----PslaeheRSLIERRFGVLFQKGALFSSLTVTE 108
Cdd:PRK10762 25 LNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVtfngP------KSSQEAGIGIIHQELNLIPQLTIAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 109 NVAL--PLIEHAGLSRADAEHLAAVKLaLAGLPLSAADKYPAS-LSGGMIKRAALARALALDPDILFLDEPTAGLDPIGA 185
Cdd:PRK10762 99 NIFLgrEFVNRFGRIDWKKMYAEADKL-LARLNLRFSSDKLVGeLSIGEQQMVEIAKVLSFESKVIIMDEPTDALTDTET 177
|
170 180 190
....*....|....*....|....*....|....*...
gi 1316494952 186 AAFDQLILTLRDAlGLSVFLVTHDLDTLYTITDRVAVL 223
Cdd:PRK10762 178 ESLFRVIRELKSQ-GRGIVYISHRLKEIFEICDDVTVF 214
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
24-181 |
1.21e-05 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 46.24 E-value: 1.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 24 PQSVH---ENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQNLPSLAEHE-RSlierRFGVLFQKGA 99
Cdd:PRK10789 324 PQTDHpalENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSwRS----RLAVVSQTPF 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 100 LFSSlTVTENVALpliEHAGLSRADAEH---LAAVKLALAGLP---LSAADKYPASLSGGMIKRAALARALALDPDILFL 173
Cdd:PRK10789 400 LFSD-TVANNIAL---GRPDATQQEIEHvarLASVHDDILRLPqgyDTEVGERGVMLSGGQKQRISIARALLLNAEILIL 475
|
....*...
gi 1316494952 174 DEPTAGLD 181
Cdd:PRK10789 476 DDALSAVD 483
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
13-237 |
1.30e-05 |
|
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: 45.62 E-value: 1.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 13 IEVRGLCNRF--GPQSVHENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQpSEGSVRVFGQNLPSLAEHErslIERR 90
Cdd:cd03289 3 MTVKDLTAKYteGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQK---WRKA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 91 FGVLFQKGALFSS-----------------LTVTENVALPLIEHAGLSRADaehlaaVKLALAGLPLSAADKYPASLSGG 153
Cdd:cd03289 79 FGVIPQKVFIFSGtfrknldpygkwsdeeiWKVAEEVGLKSVIEQFPGQLD------FVLVDGGCVLSHGHKQLMCLARS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 154 MIKRAAlaralaldpdILFLDEPTAGLDPIgaaAFDQLILTLRDAL-GLSVFLVTHDLDTLYTiTDRVAVLAQKKVLVAD 232
Cdd:cd03289 153 VLSKAK----------ILLLDEPSAHLDPI---TYQVIRKTLKQAFaDCTVILSEHRIEAMLE-CQRFLVIEENKVRQYD 218
|
....*
gi 1316494952 233 AIDQV 237
Cdd:cd03289 219 SIQKL 223
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
8-213 |
2.53e-05 |
|
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: 45.29 E-value: 2.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 8 PAEAVIEVRGLCNRF--GPQSVHENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQpSEGSVRVFGQNLPSLAEHErs 85
Cdd:TIGR01271 1213 PSGGQMDVQGLTAKYteAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVSWNSVTLQT-- 1289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 86 lIERRFGVLFQKGALFSSlTVTENvalpLIEHAGLSRADAEHLAAVklalAGLPlSAADKYPAS-----------LSGGM 154
Cdd:TIGR01271 1290 -WRKAFGVIPQKVFIFSG-TFRKN----LDPYEQWSDEEIWKVAEE----VGLK-SVIEQFPDKldfvlvdggyvLSNGH 1358
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 155 IKRAALARALALDPDILFLDEPTAGLDPIgaaAFDQLILTLRDALG-LSVFLVTHDLDTL 213
Cdd:TIGR01271 1359 KQLMCLARSILSKAKILLLDEPSAHLDPV---TLQIIRKTLKQSFSnCTVILSEHRVEAL 1415
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
38-225 |
2.57e-05 |
|
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: 44.18 E-value: 2.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 38 GEILAVVGGSGSGKSVLLRSIIGLRQPS---EGSVRvFGqNLPSLAEHERslierrfgvlFQKGALFSS--------LTV 106
Cdd:cd03233 33 GEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIH-YN-GIPYKEFAEK----------YPGEIIYVSeedvhfptLTV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 107 TEnvalpLIEHAGLSRADAehlaavklalaglplsaadkYPASLSGGMIKRAALARALALDPDILFLDEPTAGLDPIGAA 186
Cdd:cd03233 101 RE-----TLDFALRCKGNE--------------------FVRGISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTAL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1316494952 187 AFDQLILTLRDALGLSVFL-VTHDLDTLYTITDRVAVLAQ 225
Cdd:cd03233 156 EILKCIRTMADVLKTTTFVsLYQASDEIYDLFDKVLVLYE 195
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
24-228 |
4.51e-05 |
|
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: 44.55 E-value: 4.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 24 PQSVHeNLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGqnlpSLAeherslierrfgvLFQKGALFSS 103
Cdd:TIGR00957 651 PPTLN-GITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKG----SVA-------------YVPQQAWIQN 712
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 104 LTVTENValpLIEHAglsrADAEHLAAVKLALAGLP----LSAADKYP-----ASLSGGMIKRAALARALALDPDILFLD 174
Cdd:TIGR00957 713 DSLRENI---LFGKA----LNEKYYQQVLEACALLPdleiLPSGDRTEigekgVNLSGGQKQRVSLARAVYSNADIYLFD 785
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1316494952 175 EPTAGLDP-IGAAAFDQLILTLRDALGLSVFLVTHDLDTLYTiTDRVAVLAQKKV 228
Cdd:TIGR00957 786 DPLSAVDAhVGKHIFEHVIGPEGVLKNKTRILVTHGISYLPQ-VDVIIVMSGGKI 839
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
34-222 |
5.59e-05 |
|
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: 43.55 E-value: 5.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 34 DLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQNL---PSLAEHERSLIERRFGVLFQKGALFSSLTVTEnV 110
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVsykPQYIKADYEGTVRDLLSSITKDFYTHPYFKTE-I 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 111 ALPL-IEhaglsradaehlaavklalaglplSAADKYPASLSGGMIKRAALARALALDPDILFLDEPTAGLDP----IGA 185
Cdd:cd03237 100 AKPLqIE------------------------QILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVeqrlMAS 155
|
170 180 190
....*....|....*....|....*....|....*..
gi 1316494952 186 AAFDQLILTLRDalglSVFLVTHDLDTLYTITDRVAV 222
Cdd:cd03237 156 KVIRRFAENNEK----TAFVVEHDIIMIDYLADRLIV 188
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
29-211 |
7.46e-05 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 43.57 E-value: 7.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 29 ENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVfgqnLPSLaeherslierRFGVLFQKGALFSSLTVTE 108
Cdd:PRK11819 24 KDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARP----APGI----------KVGYLPQEPQLDPEKTVRE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 109 NV---------------------ALP------LIEHAG-----LSRADAEHL-AAVKLALAGLPLSAADKYPASLSGGMI 155
Cdd:PRK11819 90 NVeegvaevkaaldrfneiyaayAEPdadfdaLAAEQGelqeiIDAADAWDLdSQLEIAMDALRCPPWDAKVTKLSGGER 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1316494952 156 KRAALARALALDPDILFLDEPTAGLDpigAAAFDQLILTLRDALGlSVFLVTHD---LD 211
Cdd:PRK11819 170 RRVALCRLLLEKPDMLLLDEPTNHLD---AESVAWLEQFLHDYPG-TVVAVTHDryfLD 224
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
37-213 |
1.10e-04 |
|
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: 41.59 E-value: 1.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 37 KGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFgqnlpslaeherslierrfgvlfqkgalfssltvtenvalplie 116
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYI-------------------------------------------- 36
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 117 haglsraDAEHLAAVKLALAGLPLSAADKYpaSLSGGMIKRAALARALALDPDILFLDEPTAGLDP-----IGAAAFDQL 191
Cdd:smart00382 37 -------DGEDILEEVLDQLLLIIVGGKKA--SGSGELRLRLALALARKLKPDVLILDEITSLLDAeqealLLLLEELRL 107
|
170 180
....*....|....*....|..
gi 1316494952 192 ILTLRDALGLSVFLVTHDLDTL 213
Cdd:smart00382 108 LLLLKSEKNLTVILTTNDEKDL 129
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
5-213 |
1.11e-04 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 43.17 E-value: 1.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 5 TRPPAEAVIEVRGLCNRFGP-QSVHENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQNLPSLAehE 83
Cdd:PRK10790 333 DRPLQSGRIDIDNVSFAYRDdNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLS--H 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 84 RSLierRFGV-LFQK------GALFSSLTVTENV-------ALPLIEHAGLSRADAEHLAAvKLALAGLPLSAADKYPAS 149
Cdd:PRK10790 411 SVL---RQGVaMVQQdpvvlaDTFLANVTLGRDIseeqvwqALETVQLAELARSLPDGLYT-PLGEQGNNLSVGQKQLLA 486
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1316494952 150 LSGGMIKRaalaralaldPDILFLDEPTAGLDPIGAAAFDQLILTLRDALGLSVflVTHDLDTL 213
Cdd:PRK10790 487 LARVLVQT----------PQILILDEATANIDSGTEQAIQQALAAVREHTTLVV--IAHRLSTI 538
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
30-248 |
1.35e-04 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 42.96 E-value: 1.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 30 NLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQnlpslaeheRSLIERRFGvlfqkgaLFSSLTVTEN 109
Cdd:PRK13545 42 NISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGS---------AALIAISSG-------LNGQLTGIEN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 110 VALPLIeHAGLSRADAEHLA--AVKLALAGLPLSAADKypaSLSGGMIKRAALARALALDPDILFLDEPTAgldpIGAAA 187
Cdd:PRK13545 106 IELKGL-MMGLTKEKIKEIIpeIIEFADIGKFIYQPVK---TYSSGMKSRLGFAISVHINPDILVIDEALS----VGDQT 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1316494952 188 FDQLILTLRDAL---GLSVFLVTHDLDTLYTITDRVAVLAQKKVLVADAIDQVAETDDTWIHEY 248
Cdd:PRK13545 178 FTKKCLDKMNEFkeqGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEVVDHYDEFLKKY 241
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
32-224 |
1.84e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 42.31 E-value: 1.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 32 DLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGS--------VRVFGQNLPSLAEHErslIERRFGVLFQKGALFSS 103
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGErqsqfshiTRLSFEQLQKLVSDE---WQRNNTDMLSPGEDDTG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 104 LTVTEnvalpLIEHAGLSRADAEHLAAvKLALAGLpLSAADKYpasLSGGMIKRAALARALALDPDILFLDEPTAGLDPI 183
Cdd:PRK10938 100 RTTAE-----IIQDEVKDPARCEQLAQ-QFGITAL-LDRRFKY---LSTGETRKTLLCQALMSEPDLLILDEPFDGLDVA 169
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1316494952 184 GAAAFDQLILTLRDAlGLSVFLVTHDLDTLYTITDRVAVLA 224
Cdd:PRK10938 170 SRQQLAELLASLHQS-GITLVLVLNRFDEIPDFVQFAGVLA 209
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
30-211 |
2.36e-04 |
|
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: 40.81 E-value: 2.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 30 NLDLDLYKGEILAVVGGSGSGKSVLLRSII---GLRQPSEGSVRVFGQNLPSLAEHerslIERRFGVLfqkgalfssltv 106
Cdd:cd03227 13 PNDVTFGEGSLTIITGPNGSGKSTILDAIGlalGGAQSATRRRSGVKAGCIVAAVS----AELIFTRL------------ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 107 tenvalpliehaGLSRADAEhLAAVKLALAGlplsaADKYPASLsggmikraalaralaldpdiLFLDEPTAGLDPIGAA 186
Cdd:cd03227 77 ------------QLSGGEKE-LSALALILAL-----ASLKPRPL--------------------YILDEIDRGLDPRDGQ 118
|
170 180
....*....|....*....|....*
gi 1316494952 187 AFDQLILTLRDaLGLSVFLVTHDLD 211
Cdd:cd03227 119 ALAEAILEHLV-KGAQVIVITHLPE 142
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
30-208 |
8.29e-04 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 39.47 E-value: 8.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 30 NLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQNLPSLAEHERSLIERRFGvlfqkgaLFSSLTVTEN 109
Cdd:PRK13541 18 DLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKPYCTYIGHNLG-------LKLEMTVFEN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 110 valpLIEHAGLSRADAEHLAAVK-LALAGLplsaADKYPASLSGGMIKRAALARALALDPDILFLDEPTAGLDPIGAAAF 188
Cdd:PRK13541 91 ----LKFWSEIYNSAETLYAAIHyFKLHDL----LDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLL 162
|
170 180
....*....|....*....|
gi 1316494952 189 DQLILTLRDALGLsVFLVTH 208
Cdd:PRK13541 163 NNLIVMKANSGGI-VLLSSH 181
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
115-181 |
1.21e-03 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 39.93 E-value: 1.21e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1316494952 115 IEHAGLSRADAEhlaaVKLALAGLPLSAaDKYPASLSGGMIKRAALARALALDPDILFLDEPTAGLD 181
Cdd:PRK11147 127 LDHHNLWQLENR----INEVLAQLGLDP-DAALSSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLD 188
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
27-114 |
1.48e-03 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 40.01 E-value: 1.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 27 VHENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVfgQNLPSLAEHERSLIERRFGVLFQKGALFSSlTV 106
Cdd:PTZ00265 400 IYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIII--NDSHNLKDINLKWWRSKIGVVSQDPLLFSN-SI 476
|
....*...
gi 1316494952 107 TENVALPL 114
Cdd:PTZ00265 477 KNNIKYSL 484
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
3-225 |
1.52e-03 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 39.61 E-value: 1.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 3 RSTRPPAEAVIEVRGLCNRFGPQSVHENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLR-QPSEGSVRVFGQnlpslae 81
Cdd:PRK10938 251 RHALPANEPRIVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDHpQGYSNDLTLFGR------- 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 82 hERSLIERRFGVLFQKGALFSSL-------TVTENVALP-LIEHAGLSRA--DAEH-LAAVKLALAGLPLSAADKYPASL 150
Cdd:PRK10938 324 -RRGSGETIWDIKKHIGYVSSSLhldyrvsTSVRNVILSgFFDSIGIYQAvsDRQQkLAQQWLDILGIDKRTADAPFHSL 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 151 SGGMIKRAALARALALDPDILFLDEPTAGLDPIGAaafdQLILTLRDAL-GLS----VFLVTHDLDTLYTITDRVAVLAQ 225
Cdd:PRK10938 403 SWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNR----QLVRRFVDVLiSEGetqlLFVSHHAEDAPACITHRLEFVPD 478
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
29-210 |
2.00e-03 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 38.64 E-value: 2.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 29 ENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGqnlpslaehERSLIERRFGvlfqkgaLFSSLTVTE 108
Cdd:PRK13546 41 DDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG---------EVSVIAISAG-------LSGQLTGIE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 109 NVALPLIeHAGLSRADAEHLAA--VKLA-LAGLPLSAADKYpaslSGGMIKRAALARALALDPDILFLDEPTAgldpIGA 185
Cdd:PRK13546 105 NIEFKML-CMGFKRKEIKAMTPkiIEFSeLGEFIYQPVKKY----SSGMRAKLGFSINITVNPDILVIDEALS----VGD 175
|
170 180
....*....|....*....|....*....
gi 1316494952 186 AAFDQ----LILTLRDAlGLSVFLVTHDL 210
Cdd:PRK13546 176 QTFAQkcldKIYEFKEQ-NKTIFFVSHNL 203
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
38-225 |
2.02e-03 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 39.32 E-value: 2.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 38 GEILAVVGGSGSGKSVLLRSI----IGLRQPSEGSVRVFGqnlpsLAEHErslIERRF--GVLF--QKGALFSSLTVTEN 109
Cdd:TIGR00956 87 GELTVVLGRPGSGCSTLLKTIasntDGFHIGVEGVITYDG-----ITPEE---IKKHYrgDVVYnaETDVHFPHLTVGET 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 110 VAL------PLIEHAGLSRAD-AEHLAAVKLALAGLPLS----AADKYPASLSGGMIKRAALARALALDPDILFLDEPTA 178
Cdd:TIGR00956 159 LDFaarcktPQNRPDGVSREEyAKHIADVYMATYGLSHTrntkVGNDFVRGVSGGERKRVSIAEASLGGAKIQCWDNATR 238
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1316494952 179 GLDPIGAAAFDQLILTLRDALGLSVFLVTHDL-DTLYTITDRVAVLAQ 225
Cdd:TIGR00956 239 GLDSATALEFIRALKTSANILDTTPLVAIYQCsQDAYELFDKVIVLYE 286
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
30-225 |
2.35e-03 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 39.19 E-value: 2.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 30 NLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVfgqnlpslaeherslIERRFGVLFQKGALFSSlTVTEN 109
Cdd:PLN03232 635 DINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAETSSVV---------------IRGSVAYVPQVSWIFNA-TVREN 698
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 110 VAL-PLIEHAGLSRA-DAEHLAAVKLALAGLPLSAADKYPASLSGGMIKRAALARALALDPDILFLDEPTAGLDP-IGAA 186
Cdd:PLN03232 699 ILFgSDFESERYWRAiDVTALQHDLDLLPGRDLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAhVAHQ 778
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1316494952 187 AFDQLIltlRDAL-GLSVFLVTHDLDTLyTITDRVAVLAQ 225
Cdd:PLN03232 779 VFDSCM---KDELkGKTRVLVTNQLHFL-PLMDRIILVSE 814
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
149-223 |
2.95e-03 |
|
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: 37.55 E-value: 2.95e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1316494952 149 SLSGGMIKRAALARALALDPDILFLDEPTAGLDPIGAAAFDQLILTLRDALGLSVFLVTHDLDTLYTITDRVAVL 223
Cdd:cd03222 71 DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTALVVEHDLAVLDYLSDRIHVF 145
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
29-61 |
3.27e-03 |
|
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: 37.52 E-value: 3.27e-03
10 20 30
....*....|....*....|....*....|...
gi 1316494952 29 ENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGL 61
Cdd:cd03223 18 KDLSFEIKPGDRLLITGPSGTGKSSLFRALAGL 50
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
34-222 |
4.25e-03 |
|
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: 38.23 E-value: 4.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 34 DLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSV-----------RVFGQNLPSLAEHERSLIERRFGvlfqkgalfS 102
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVdedlkisykpqYISPDYDGTVEEFLRSANTDDFG---------S 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 103 SLTVTEnvalpLIEHAGLsradaEHLAavklalaglplsaaDKYPASLSGGMIKRAALARALALDPDILFLDEPTAGLD- 181
Cdd:COG1245 433 SYYKTE-----IIKPLGL-----EKLL--------------DKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDv 488
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1316494952 182 --PIGAAAFDQLILTLRDAlglSVFLVTHDLDTLYTITDRVAV 222
Cdd:COG1245 489 eqRLAVAKAIRRFAENRGK---TAMVVDHDIYLIDYISDRLMV 528
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
91-223 |
4.93e-03 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 38.09 E-value: 4.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 91 FGVLFQKGALFSsLTVTENVALPLiEHAglSRAD---AEHLAAVKLALAGLPL---SAADKYPASLSGGMIKRAALARAL 164
Cdd:PTZ00265 1298 FSIVSQEPMLFN-MSIYENIKFGK-EDA--TREDvkrACKFAAIDEFIESLPNkydTNVGPYGKSLSGGQKQRIAIARAL 1373
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1316494952 165 ALDPDILFLDEPTAGLDPIGAAAFDQLILTLRDALGLSVFLVTHDLDTLYTiTDRVAVL 223
Cdd:PTZ00265 1374 LREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASIKR-SDKIVVF 1431
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
4-229 |
5.00e-03 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 38.18 E-value: 5.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 4 STRPP----AEAVIEVRGLCNRFGPQ--SVHENLDLDLYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSVRVFGQNLP 77
Cdd:PLN03130 1225 NNRPPpgwpSSGSIKFEDVVLRYRPElpPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDIS 1304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 78 SLAEHErslIERRFGVLFQKGALFSSlTVTENVAlPLIEHA------GLSRAdaeHLAAV----------KLALAGLPLS 141
Cdd:PLN03130 1305 KFGLMD---LRKVLGIIPQAPVLFSG-TVRFNLD-PFNEHNdadlweSLERA---HLKDVirrnslgldaEVSEAGENFS 1376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 142 AADKYPASLSGGMIKRAalaralaldpDILFLDEPTAGLDpIGAAAFDQliLTLRDALGLSVFLV-THDLDTLYTiTDRV 220
Cdd:PLN03130 1377 VGQRQLLSLARALLRRS----------KILVLDEATAAVD-VRTDALIQ--KTIREEFKSCTMLIiAHRLNTIID-CDRI 1442
|
....*....
gi 1316494952 221 AVLAQKKVL 229
Cdd:PLN03130 1443 LVLDAGRVV 1451
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
35-69 |
8.00e-03 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 37.48 E-value: 8.00e-03
10 20 30
....*....|....*....|....*....|....*
gi 1316494952 35 LYKGEILAVVGGSGSGKSVLLRSIIGLRQPSEGSV 69
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEV 396
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
31-228 |
8.12e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 37.53 E-value: 8.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 31 LDLDlykgEILAVVGGSGSGKSVLLRSIIGLRQPSEGSV--------RVFGQNLPS---LAEHERSLIERRF-GVLFQK- 97
Cdd:PLN03073 532 IDLD----SRIAMVGPNGIGKSTILKLISGELQPSSGTVfrsakvrmAVFSQHHVDgldLSSNPLLYMMRCFpGVPEQKl 607
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316494952 98 GALFSSLTVTENVALPLIehaglsradaehlaavklalaglplsaadkypASLSGGMIKRAALARALALDPDILFLDEPT 177
Cdd:PLN03073 608 RAHLGSFGVTGNLALQPM--------------------------------YTLSGGQKSRVAFAKITFKKPHILLLDEPS 655
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1316494952 178 AGLDPIGAAAFDQLILTLRDAlglsVFLVTHDLDTLYTITDRVAVLAQKKV 228
Cdd:PLN03073 656 NHLDLDAVEALIQGLVLFQGG----VLMVSHDEHLISGSVDELWVVSEGKV 702
|
|
| |
