|
Name |
Accession |
Description |
Interval |
E-value |
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
2-239 |
5.69e-101 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 293.51 E-value: 5.69e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 2 RKSYGELDVLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGHDVAAAAGRVRESISLTGQFAAVDE 81
Cdd:COG1131 7 TKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRRIGYVPQEPALYP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 82 VLTGRENLVLVARLRHLPDPGA--VADDMLARFSLTDAGGRRAGEYSGGMRRRLDIAMSLVGDPPVIFLDEPTTGLDPQA 159
Cdd:COG1131 87 DLTVRENLRFFARLYGLPRKEAreRIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTSGLDPEA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 160 RAEVWRTVKQLADGGTTVLLTTQYLDEAEQLADRIAILHEGRIIQNGTLAELKRLlpsatveyvekqpTLEEVFLAVVGE 239
Cdd:COG1131 167 RRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKAR-------------LLEDVFLELTGE 233
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
3-227 |
9.10e-90 |
|
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: 267.33 E-value: 9.10e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 3 KSYGELDVLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGHDVAAAAGRVRESISLTGQFAAVDEV 82
Cdd:TIGR01188 1 KVYGDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVVREPRKVRRSIGIVPQYASVDED 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 83 LTGRENLVLVARLRHLPDPGA--VADDMLARFSLTDAGGRRAGEYSGGMRRRLDIAMSLVGDPPVIFLDEPTTGLDPQAR 160
Cdd:TIGR01188 81 LTGRENLEMMGRLYGLPKDEAeeRAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPRTR 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2794531883 161 AEVWRTVKQLADGGTTVLLTTQYLDEAEQLADRIAILHEGRIIQNGTLAELKRLLPSATVEYVEKQP 227
Cdd:TIGR01188 161 RAIWDYIRALKEEGVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPEELKRRLGKDTLESRPRDI 227
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
3-212 |
2.08e-86 |
|
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: 256.14 E-value: 2.08e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 3 KSYGELDVLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGHDVAAAAGRVRESISLTGQFAAVDEV 82
Cdd:cd03265 8 KKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREVRRRIGIVFQDLSVDDE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 83 LTGRENLVLVARLRHLpdPGAV----ADDMLARFSLTDAGGRRAGEYSGGMRRRLDIAMSLVGDPPVIFLDEPTTGLDPQ 158
Cdd:cd03265 88 LTGWENLYIHARLYGV--PGAErrerIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQ 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2794531883 159 ARAEVWRTVKQL-ADGGTTVLLTTQYLDEAEQLADRIAILHEGRIIQNGTLAELK 212
Cdd:cd03265 166 TRAHVWEYIEKLkEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEELK 220
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
2-212 |
9.16e-75 |
|
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: 226.23 E-value: 9.16e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 2 RKSYGELD--VLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGHDVAAAAGRVRESISLTGQFAAV 79
Cdd:cd03263 7 TKTYKKGTkpAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAARQSLGYCPQFDAL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 80 DEVLTGRENLVLVARLRHLP--DPGAVADDMLARFSLTDAGGRRAGEYSGGMRRRLDIAMSLVGDPPVIFLDEPTTGLDP 157
Cdd:cd03263 87 FDELTVREHLRFYARLKGLPksEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDP 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2794531883 158 QARAEVWRTVKQLAdGGTTVLLTTQYLDEAEQLADRIAILHEGRIIQNGTLAELK 212
Cdd:cd03263 167 ASRRAIWDLILEVR-KGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQELK 220
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
3-244 |
1.02e-70 |
|
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: 217.03 E-value: 1.02e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 3 KSYGELDVLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGHDVAAAAGRVRESISLTGQFAAVDEV 82
Cdd:COG4555 9 KKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQIGVLPDERGLYDR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 83 LTGRENLVLVARLRHLPD--PGAVADDMLARFSLTDAGGRRAGEYSGGMRRRLDIAMSLVGDPPVIFLDEPTTGLDPQAR 160
Cdd:COG4555 89 LTVRENIRYFAELYGLFDeeLKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTNGLDVMAR 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 161 AEVWRTVKQLADGGTTVLLTTQYLDEAEQLADRIAILHEGRIIQNGTLAELKRLlpsatveyvEKQPTLEEVFLAVVGET 240
Cdd:COG4555 169 RLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREE---------IGEENLEDAFVALIGSE 239
|
....
gi 2794531883 241 DGSA 244
Cdd:COG4555 240 EGEA 243
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
3-202 |
2.95e-70 |
|
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: 213.03 E-value: 2.95e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 3 KSYGELDVLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGHDVAAAAGRVRESISLTGQFAAVDEV 82
Cdd:cd03230 8 KRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKRRIGYLPEEPSLYEN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 83 LTGRENLvlvarlrhlpdpgavaddmlarfsltdaggrragEYSGGMRRRLDIAMSLVGDPPVIFLDEPTTGLDPQARAE 162
Cdd:cd03230 88 LTVRENL----------------------------------KLSGGMKQRLALAQALLHDPELLILDEPTSGLDPESRRE 133
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2794531883 163 VWRTVKQLADGGTTVLLTTQYLDEAEQLADRIAILHEGRI 202
Cdd:cd03230 134 FWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
3-206 |
4.60e-55 |
|
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: 175.87 E-value: 4.60e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 3 KSYGELDVLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGHDV---AAAAGRVRESISLTGQFAAv 79
Cdd:cd03268 8 KTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYqknIEALRRIGALIEAPGFYPN- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 80 devLTGRENLVLVARLRHLPDpgAVADDMLARFSLTDAGGRRAGEYSGGMRRRLDIAMSLVGDPPVIFLDEPTTGLDPQA 159
Cdd:cd03268 87 ---LTARENLRLLARLLGIRK--KRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPDG 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2794531883 160 RAEVWRTVKQLADGGTTVLLTTQYLDEAEQLADRIAILHEGRIIQNG 206
Cdd:cd03268 162 IKELRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
3-181 |
4.89e-53 |
|
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: 170.35 E-value: 4.89e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 3 KSYGELDVLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGHDVAAAAGRVRESISLTGQFAAVDEV 82
Cdd:COG4133 10 CRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRRLAYLGHADGLKPE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 83 LTGRENLVLVARLRHLPDPGAVADDMLARFSLTDAGGRRAGEYSGGMRRRLDIAMSLVGDPPVIFLDEPTTGLDPQARAE 162
Cdd:COG4133 90 LTVRENLRFWAALYGLRADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGVAL 169
|
170
....*....|....*....
gi 2794531883 163 VWRTVKQLADGGTTVLLTT 181
Cdd:COG4133 170 LAELIAAHLARGGAVLLTT 188
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
5-212 |
3.42e-50 |
|
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: 163.76 E-value: 3.42e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 5 YGELDVLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGHDVAAAA--GRVRESISLTGQFAAVDEV 82
Cdd:cd03224 10 YGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPphERARAGIGYVPEGRRIFPE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 83 LTGRENLVLVARLRHLPDPGAVADDMLARFS-LTDAGGRRAGEYSGGMRRRLDIAMSLVGDPPVIFLDEPTTGLDPQARA 161
Cdd:cd03224 90 LTVEENLLLGAYARRRAKRKARLERVYELFPrLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLAPKIVE 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2794531883 162 EVWRTVKQLADGGTTVLLTTQYLDEAEQLADRIAILHEGRIIQNGTLAELK 212
Cdd:cd03224 170 EIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELL 220
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
3-221 |
1.72e-49 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 166.06 E-value: 1.72e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 3 KSYGELDVLRGVDLGVAPGTIHALLGSNGAGKTTLVkILSTLVRADAGTASVQGHDVAAAAGRVRESISLTGQF-AAVDE 81
Cdd:NF000106 21 KHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RGA-LPAHV*GPDAGRRPWRF*TWCANRRALRRTIG*HRPVr*GRRE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 82 VLTGRENLVLVARLRHLP--DPGAVADDMLARFSLTDAGGRRAGEYSGGMRRRLDIAMSLVGDPPVIFLDEPTTGLDPQA 159
Cdd:NF000106 100 SFSGRENLYMIGR*LDLSrkDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRT 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2794531883 160 RAEVWRTVKQLADGGTTVLLTTQYLDEAEQLADRIAILHEGRIIQNGTLAELKRLLPSATVE 221
Cdd:NF000106 180 RNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDELKTKVGGRTLQ 241
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
2-221 |
2.36e-49 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 163.74 E-value: 2.36e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 2 RKSYGELDVLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGHDVAAAAGRV------------RES 69
Cdd:COG4152 8 TKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDRRRigylpeerglypKMK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 70 IsltgqfaavdevltgRENLVLVARLRHLPDPGAV--ADDMLARFSLTDAGGRRAGEYSGGMRRRLDIAMSLVGDPPVIF 147
Cdd:COG4152 88 V---------------GEQLVYLARLKGLSKAEAKrrADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLI 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2794531883 148 LDEPTTGLDPQARAEVWRTVKQLADGGTTVLLTTQYLDEAEQLADRIAILHEGRIIQNGTLAELKRLLPSATVE 221
Cdd:COG4152 153 LDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEIRRQFGRNTLR 226
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
3-206 |
3.49e-49 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 160.82 E-value: 3.49e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 3 KSYGELDVLRGVDLGVAPGtIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGHDVAAAAGRVRESISLTGQFAAVDEV 82
Cdd:cd03264 8 KRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRRIGYLPQEFGVYPN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 83 LTGRENLVLVARLRHLPDPG--AVADDMLARFSLTDAGGRRAGEYSGGMRRRLDIAMSLVGDPPVIFLDEPTTGLDPQAR 160
Cdd:cd03264 87 FTVREFLDYIAWLKGIPSKEvkARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDPEER 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2794531883 161 AEVWRTVKQLADgGTTVLLTTQYLDEAEQLADRIAILHEGRIIQNG 206
Cdd:cd03264 167 IRFRNLLSELGE-DRIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-211 |
7.09e-49 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 163.05 E-value: 7.09e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 1 MRKSYGELDVLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGHDVAAAAGRVRESISLTGQFAAVD 80
Cdd:PRK13537 13 VEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQRVGVVPQFDNLD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 81 EVLTGRENLVLVARLRHLPDPGAVAD-DMLARFS-LTDAGGRRAGEYSGGMRRRLDIAMSLVGDPPVIFLDEPTTGLDPQ 158
Cdd:PRK13537 93 PDFTVRENLLVFGRYFGLSAAAARALvPPLLEFAkLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQ 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2794531883 159 ARAEVWRTVKQLADGGTTVLLTTQYLDEAEQLADRIAILHEGRIIQNGTLAEL 211
Cdd:PRK13537 173 ARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHAL 225
|
|
| PQQ_ABC_ATP |
TIGR03864 |
ABC transporter, ATP-binding subunit, PQQ-dependent alcohol dehydrogenase system; Members of ... |
1-221 |
9.06e-49 |
|
ABC transporter, ATP-binding subunit, PQQ-dependent alcohol dehydrogenase system; Members of this protein family are the ATP-binding subunit of an ABC transporter system that is associated with PQQ biosynthesis and PQQ-dependent alcohol dehydrogenases. While this family shows homology to several efflux ABC transporter subunits, the presence of a periplasmic substrate-binding protein and association with systems for catabolism of alcohols suggests a role in import rather than detoxification. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 274822 [Multi-domain] Cd Length: 236 Bit Score: 160.54 E-value: 9.06e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 1 MRKSYGELDVLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGHDVAAAAGRVRESISLTGQFAAVD 80
Cdd:TIGR03864 7 LSFRYGARRALDDVSFTVRPGRFVALLGPNGAGKSTLFSLLTRLYVAQSGQISVAGHDLRRAPRAALARLGVVFQQPTLD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 81 EVLTGRENLVLVARLRHLPDPGAVA--DDMLARFSLTDAGGRRAGEYSGGMRRRLDIAMSLVGDPPVIFLDEPTTGLDPQ 158
Cdd:TIGR03864 87 LDLSVRQNLRYHAALHGLSRAEARAriAELLARLGLAERADDKVRELNGGHRRRVEIARALLHRPALLLLDEPTVGLDPA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2794531883 159 ARAEVWRTVKQLA-DGGTTVLLTTQYLDEAEQlADRIAILHEGRIIQNGTLAELKRLLPSATVE 221
Cdd:TIGR03864 167 SRAAITAHVRALArDQGLSVLWATHLVDEIEA-SDRLVVLHRGRVLADGAAAELRGATGGADLE 229
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
10-206 |
1.38e-48 |
|
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: 159.46 E-value: 1.38e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 10 VLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGHDVAAAAGRVRESISLTGQFAAVDEVLTGRENL 89
Cdd:cd03266 20 AVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARRRLGFVSDSTGLYDRLTARENL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 90 VLVARLRHLPDPGAVA--DDMLARFSLTDAGGRRAGEYSGGMRRRLDIAMSLVGDPPVIFLDEPTTGLDPQARAEVWRTV 167
Cdd:cd03266 100 EYFAGLYGLKGDELTArlEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRALREFI 179
|
170 180 190
....*....|....*....|....*....|....*....
gi 2794531883 168 KQLADGGTTVLLTTQYLDEAEQLADRIAILHEGRIIQNG 206
Cdd:cd03266 180 RQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
1-213 |
4.12e-48 |
|
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: 158.75 E-value: 4.12e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 1 MRKSYGELDVLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGHDVAA--AAGRVRESISLTGQFAA 78
Cdd:cd03219 6 LTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGlpPHEIARLGIGRTFQIPR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 79 VDEVLTGRENLVLVARLRHLPDPGAV------------ADDMLARFSLTDAGGRRAGEYSGGMRRRLDIAMSLVGDPPVI 146
Cdd:cd03219 86 LFPELTVLENVMVAAQARTGSGLLLArarreerearerAEELLERVGLADLADRPAGELSYGQQRRLEIARALATDPKLL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2794531883 147 FLDEPTTGLDPQARAEVWRTVKQLADGGTTVLLTTQYLDEAEQLADRIAILHEGRIIQNGTLAELKR 213
Cdd:cd03219 166 LLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRN 232
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
2-213 |
1.24e-47 |
|
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: 157.83 E-value: 1.24e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 2 RKSYGELDVLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGHDVAAAAG----RVRESISLTGQFA 77
Cdd:COG1127 12 TKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEkelyELRRRIGMLFQGG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 78 AVDEVLTGRENLVLvaRLR---HLPDPGA--VADDMLARFSLTDAGGRRAGEYSGGMRRRLDIAMSLVGDPPVIFLDEPT 152
Cdd:COG1127 92 ALFDSLTVFENVAF--PLRehtDLSEAEIreLVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDPEILLYDEPT 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2794531883 153 TGLDPQARAEVWRTVKQLADG-GTTVLLTTQYLDEAEQLADRIAILHEGRIIQNGTLAELKR 213
Cdd:COG1127 170 AGLDPITSAVIDELIRELRDElGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLA 231
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
4-211 |
1.27e-47 |
|
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: 157.45 E-value: 1.27e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 4 SYGELDVLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGHDVA--AAAGRVRESISLTGQ----FA 77
Cdd:COG0410 12 GYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITglPPHRIARLGIGYVPEgrriFP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 78 AvdevLTGRENLVLVARLRH-LPDPGAVADDMLARF-SLTDAGGRRAGEYSGGMRRRLDIAMSLVGDPPVIFLDEPTTGL 155
Cdd:COG0410 92 S----LTVEENLLLGAYARRdRAEVRADLERVYELFpRLKERRRQRAGTLSGGEQQMLAIGRALMSRPKLLLLDEPSLGL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2794531883 156 DPQARAEVWRTVKQLADGGTTVLLTTQYLDEAEQLADRIAILHEGRIIQNGTLAEL 211
Cdd:COG0410 168 APLIVEEIFEIIRRLNREGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAEL 223
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
6-211 |
1.68e-46 |
|
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: 154.41 E-value: 1.68e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 6 GELDVLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGHDVAAAAGR-VRESISLTGQ------FAA 78
Cdd:COG1122 12 GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLReLRRKVGLVFQnpddqlFAP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 79 V--DEVLTGRENLVL---VARLRhlpdpgavADDMLARFSLTDAGGRRAGEYSGGMRRRLDIAMSLVGDPPVIFLDEPTT 153
Cdd:COG1122 92 TveEDVAFGPENLGLpreEIRER--------VEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLVLDEPTA 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2794531883 154 GLDPQARAEVWRTVKQLADGGTTVLLTTQYLDEAEQLADRIAILHEGRIIQNGTLAEL 211
Cdd:COG1122 164 GLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREV 221
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
4-211 |
2.71e-46 |
|
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: 154.82 E-value: 2.71e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 4 SYGELDVLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGHDVAA-AAGRVRESISLTGQFAAVDEV 82
Cdd:COG1120 10 GYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASlSRRELARRIAYVPQEPPAPFG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 83 LTGREnLVLVARLRHLPDPG-------AVADDMLARFSLTDAGGRRAGEYSGGMRRRLDIAMSLVGDPPVIFLDEPTTGL 155
Cdd:COG1120 90 LTVRE-LVALGRYPHLGLFGrpsaedrEAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLLLDEPTSHL 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2794531883 156 DPQARAEVWRTVKQLA-DGGTTVLLTTQYLDEAEQLADRIAILHEGRIIQNGTLAEL 211
Cdd:COG1120 169 DLAHQLEVLELLRRLArERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEV 225
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
3-238 |
2.13e-45 |
|
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: 151.40 E-value: 2.13e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 3 KSYGELDVLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGHDVAAaagRVRESISLTGQFAAVDEV 82
Cdd:TIGR03740 8 KRFGKQTAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGHPWTR---KDLHKIGSLIESPPLYEN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 83 LTGRENLVLVARLRHLPDpgAVADDMLARFSLTDAGGRRAGEYSGGMRRRLDIAMSLVGDPPVIFLDEPTTGLDPQARAE 162
Cdd:TIGR03740 85 LTARENLKVHTTLLGLPD--SRIDEVLNIVDLTNTGKKKAKQFSLGMKQRLGIAIALLNHPKLLILDEPTNGLDPIGIQE 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2794531883 163 VWRTVKQLADGGTTVLLTTQYLDEAEQLADRIAILHEGRIIQNGTlaelkrllpsatveyVEKQPTLEEVFLAVVG 238
Cdd:TIGR03740 163 LRELIRSFPEQGITVILSSHILSEVQQLADHIGIISEGVLGYQGK---------------INKSENLEKLFVEVVK 223
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-206 |
2.81e-45 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 154.60 E-value: 2.81e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 1 MRKSYGELDVLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGHDVAAAAGRVRESISLTGQFAAVD 80
Cdd:PRK13536 47 VSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLARARIGVVPQFDNLD 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 81 EVLTGRENLVLVARL--RHLPDPGAVADDMLARFSLTDAGGRRAGEYSGGMRRRLDIAMSLVGDPPVIFLDEPTTGLDPQ 158
Cdd:PRK13536 127 LEFTVRENLLVFGRYfgMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPH 206
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2794531883 159 ARAEVWRTVKQLADGGTTVLLTTQYLDEAEQLADRIAILHEGRIIQNG 206
Cdd:PRK13536 207 ARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEG 254
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
2-213 |
3.97e-45 |
|
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: 151.12 E-value: 3.97e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 2 RKSYGELDVLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGHDVAAAAG----RVRESISLTGQFA 77
Cdd:cd03261 7 TKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEaelyRLRRRMGMLFQSG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 78 AVDEVLTGRENLVLvaRLR-H--LPDP--GAVADDMLARFSLTDAGGRRAGEYSGGMRRRLDIAMSLVGDPPVIFLDEPT 152
Cdd:cd03261 87 ALFDSLTVFENVAF--PLReHtrLSEEeiREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLYDEPT 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2794531883 153 TGLDPQARAEVWRTVKQLAD-GGTTVLLTTQYLDEAEQLADRIAILHEGRIIQNGTLAELKR 213
Cdd:cd03261 165 AGLDPIASGVIDDLIRSLKKeLGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRA 226
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
16-212 |
4.67e-45 |
|
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: 161.72 E-value: 4.67e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 16 LGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGHDVAAAAGRVRESISLTGQFAAVDEVLTGRENLVLVARL 95
Cdd:TIGR01257 1960 VGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISDVHQNMGYCPQFDAIDDLLTGREHLYLYARL 2039
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 96 RHLP--DPGAVADDMLARFSLTDAGGRRAGEYSGGMRRRLDIAMSLVGDPPVIFLDEPTTGLDPQARAEVWRTVKQLADG 173
Cdd:TIGR01257 2040 RGVPaeEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIRE 2119
|
170 180 190
....*....|....*....|....*....|....*....
gi 2794531883 174 GTTVLLTTQYLDEAEQLADRIAILHEGRIIQNGTLAELK 212
Cdd:TIGR01257 2120 GRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGTIQHLK 2158
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
2-206 |
1.14e-44 |
|
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: 149.21 E-value: 1.14e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 2 RKSYGELDVLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGHDVAAAAGRvRESISLTGQFAAVDE 81
Cdd:cd03259 7 SKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE-RRNIGMVFQDYALFP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 82 VLTGRENLVLVARLRHLPDP--GAVADDMLARFSLTDAGGRRAGEYSGGMRRRLDIAMSLVGDPPVIFLDEPTTGLDPQA 159
Cdd:cd03259 86 HLTVAENIAFGLKLRGVPKAeiRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSALDAKL 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2794531883 160 RAEVWRTVKQL-ADGGTTVLLTTQYLDEAEQLADRIAILHEGRIIQNG 206
Cdd:cd03259 166 REELREELKELqRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
2-213 |
4.29e-44 |
|
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: 149.03 E-value: 4.29e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 2 RKSYGELDVLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGHDVA--AAAGRVRESISLTGQFAAV 79
Cdd:COG0411 11 TKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITglPPHRIARLGIARTFQNPRL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 80 DEVLTGRENlVLVARLRHLPDPG------------------AVADDMLARFSLTDAGGRRAGEYSGGMRRRLDIAMSLVG 141
Cdd:COG0411 91 FPELTVLEN-VLVAAHARLGRGLlaallrlprarreerearERAEELLERVGLADRADEPAGNLSYGQQRRLEIARALAT 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2794531883 142 DPPVIFLDEPTTGLDPQARAEVWRTVKQLADG-GTTVLLTTQYLDEAEQLADRIAILHEGRIIQNGTLAELKR 213
Cdd:COG0411 170 EPKLLLLDEPAAGLNPEETEELAELIRRLRDErGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGTPAEVRA 242
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
4-202 |
1.92e-43 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 147.16 E-value: 1.92e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 4 SYGELDVLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGHDVAAAAGRVresisltG---QFAAVD 80
Cdd:COG1121 15 SYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARRRI-------GyvpQRAEVD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 81 EV--LTGREnLVLVARLRHLPDPG-------AVADDMLARFSLTDAGGRRAGEYSGGMRRRLDIAMSLVGDPPVIFLDEP 151
Cdd:COG1121 88 WDfpITVRD-VVLMGRYGRRGLFRrpsradrEAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDPDLLLLDEP 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2794531883 152 TTGLDPQARAEVWRTVKQLADGGTTVLLTTQYLDEAEQLADRIAILHEGRI 202
Cdd:COG1121 167 FAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLLNRGLV 217
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
2-201 |
2.29e-42 |
|
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: 141.61 E-value: 2.29e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 2 RKSYGELDVLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGHDVAAAAGR-VRESISLTGQFaavd 80
Cdd:cd00267 6 SFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEeLRRRIGYVPQL---- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 81 evltgrenlvlvarlrhlpdpgavaddmlarfsltdaggrrageySGGMRRRLDIAMSLVGDPPVIFLDEPTTGLDPQAR 160
Cdd:cd00267 82 ---------------------------------------------SGGQRQRVALARALLLNPDLLLLDEPTSGLDPASR 116
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2794531883 161 AEVWRTVKQLADGGTTVLLTTQYLDEAEQLADRIAILHEGR 201
Cdd:cd00267 117 ERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
10-201 |
8.55e-42 |
|
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: 141.84 E-value: 8.55e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 10 VLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGHDVAAA-AGRVRESISLTGQFAAV--------D 80
Cdd:cd03225 16 ALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLsLKELRRKVGLVFQNPDDqffgptveE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 81 EVLTGRENLvlvarlrHLPDP--GAVADDMLARFSLTDAGGRRAGEYSGGMRRRLDIAMSLVGDPPVIFLDEPTTGLDPQ 158
Cdd:cd03225 96 EVAFGLENL-------GLPEEeiEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDPA 168
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2794531883 159 ARAEVWRTVKQLADGGTTVLLTTQYLDEAEQLADRIAILHEGR 201
Cdd:cd03225 169 GRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
3-211 |
6.97e-41 |
|
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: 139.99 E-value: 6.97e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 3 KSYGELDVLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGHDVAAAA--GRVRESISLTGQFAAVD 80
Cdd:cd03218 8 KRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPmhKRARLGIGYLPQEASIF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 81 EVLTGRENLVLVARLRHLPDPGAV--ADDMLARFSLTDAGGRRAGEYSGGMRRRLDIAMSLVGDPPVIFLDEPTTGLDPQ 158
Cdd:cd03218 88 RKLTVEENILAVLEIRGLSKKEREekLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVDPI 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2794531883 159 ARAEVWRTVKQLADGGTTVLLTTQYLDEAEQLADRIAILHEGRIIQNGTLAEL 211
Cdd:cd03218 168 AVQDIQKIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEI 220
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
1-211 |
1.12e-39 |
|
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: 137.41 E-value: 1.12e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 1 MRKSYGELDVLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGHDVAAAA--GRVRESISLTGQFAA 78
Cdd:TIGR04406 7 LIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHLPmhERARLGIGYLPQEAS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 79 VDEVLTGRENLVLVARLRHLPDPGAV---ADDMLARFSLTDAGGRRAGEYSGGMRRRLDIAMSLVGDPPVIFLDEPTTGL 155
Cdd:TIGR04406 87 IFRKLTVEENIMAVLEIRKDLDRAEReerLEALLEEFQISHLRDNKAMSLSGGERRRVEIARALATNPKFILLDEPFAGV 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2794531883 156 DPQARAEVWRTVKQLADGGTTVLLTTQYLDEAEQLADRIAILHEGRIIQNGTLAEL 211
Cdd:TIGR04406 167 DPIAVGDIKKIIKHLKERGIGVLITDHNVRETLDICDRAYIISDGKVLAEGTPAEI 222
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
2-211 |
1.15e-39 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 137.08 E-value: 1.15e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 2 RKSYGELDVLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGHDVAAAA--GRVRESISLTGQFAAV 79
Cdd:COG1137 10 VKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPmhKRARLGIGYLPQEASI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 80 DEVLTGRENLVLVARLRHLPDPG--AVADDMLARFSLTDAGGRRAGEYSGGMRRRLDIAMSLVGDPPVIFLDEPTTGLDP 157
Cdd:COG1137 90 FRKLTVEDNILAVLELRKLSKKEreERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKFILLDEPFAGVDP 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2794531883 158 QARAEVWRTVKQLADGGTTVLLTTQYLDEAEQLADRIAILHEGRIIQNGTLAEL 211
Cdd:COG1137 170 IAVADIQKIIRHLKERGIGVLITDHNVRETLGICDRAYIISEGKVLAEGTPEEI 223
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
2-202 |
2.68e-39 |
|
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: 135.70 E-value: 2.68e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 2 RKSYGELD----VLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGHDVAAAAGR-----VRESISL 72
Cdd:cd03255 7 SKTYGGGGekvqALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKelaafRRRHIGF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 73 TGQFAAVDEVLTGRENLVLVARLRHLPDPGA--VADDMLARFSLTDAGGRRAGEYSGGMRRRLDIAMSLVGDPPVIFLDE 150
Cdd:cd03255 87 VFQSFNLLPDLTALENVELPLLLAGVPKKERreRAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPKIILADE 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2794531883 151 PTTGLDPQARAEVWRTVKQLADG-GTTVLLTTQYLDEAEqLADRIAILHEGRI 202
Cdd:cd03255 167 PTGNLDSETGKEVMELLRELNKEaGTTIVVVTHDPELAE-YADRIIELRDGKI 218
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
2-206 |
4.04e-39 |
|
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: 135.10 E-value: 4.04e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 2 RKSYGELDVLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGHDVAAAAGRvresisltgQFAAVDE 81
Cdd:cd03269 7 TKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARN---------RIGYLPE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 82 ------VLTGRENLVLVARLRHLP--DPGAVADDMLARFSLTDAGGRRAGEYSGGMRRRLDIAMSLVGDPPVIFLDEPTT 153
Cdd:cd03269 78 erglypKMKVIDQLVYLAQLKGLKkeEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFS 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2794531883 154 GLDPQARAEVWRTVKQLADGGTTVLLTTQYLDEAEQLADRIAILHEGRIIQNG 206
Cdd:cd03269 158 GLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
2-205 |
7.41e-39 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 134.79 E-value: 7.41e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 2 RKSYG----ELDVLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGHDVAAAAGRV-----RESISL 72
Cdd:COG1136 11 TKSYGtgegEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERElarlrRRHIGF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 73 TGQFAAVDEVLTGRENLVLVARLRHLPDPGAV--ADDMLARFSLTDAGGRRAGEYSGGMRRRLDIAMSLVGDPPVIFLDE 150
Cdd:COG1136 91 VFQFFNLLPELTALENVALPLLLAGVSRKERRerARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNRPKLILADE 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2794531883 151 PTTGLDPQARAEVWRTVKQLA-DGGTTVLLTTQYLDEAEQlADRIAILHEGRIIQN 205
Cdd:COG1136 171 PTGNLDSKTGEEVLELLRELNrELGTTIVMVTHDPELAAR-ADRVIRLRDGRIVSD 225
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
4-206 |
2.60e-38 |
|
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: 131.79 E-value: 2.60e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 4 SYGELDVLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGHDVAAAAGRVResisltgqfaavdevl 83
Cdd:cd03214 8 GYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKEL---------------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 84 tgrenlvlvARLRhlpdpgAVADDMLARFSLTDAGGRRAGEYSGGMRRRLDIAMSLVGDPPVIFLDEPTTGLDPQARAEV 163
Cdd:cd03214 72 ---------ARKI------AYVPQALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQIEL 136
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2794531883 164 WRTVKQLAD-GGTTVLLTTQYLDEAEQLADRIAILHEGRIIQNG 206
Cdd:cd03214 137 LELLRRLAReRGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
4-206 |
1.56e-37 |
|
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: 130.73 E-value: 1.56e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 4 SYGELDVLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGHDVAaaagRVRESISLTGQFAAVDEV- 82
Cdd:cd03235 8 SYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLE----KERKRIGYVPQRRSIDRDf 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 83 -LTGREnLVLVARLRHLPDPG-------AVADDMLARFSLTDAGGRRAGEYSGGMRRRLDIAMSLVGDPPVIFLDEPTTG 154
Cdd:cd03235 84 pISVRD-VVLMGLYGHKGLFRrlskadkAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAG 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2794531883 155 LDPQARAEVWRTVKQLADGGTTVLLTTQYLDEAEQLADRIAILhEGRIIQNG 206
Cdd:cd03235 163 VDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRVLLL-NRTVVASG 213
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
6-211 |
8.16e-37 |
|
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: 135.80 E-value: 8.16e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 6 GELDVLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGHDVAAAAGR----VRESISLTGQ--FAAV 79
Cdd:COG1123 276 GGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRslreLRRRVQMVFQdpYSSL 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 80 DEVLTGRENLVLVARLRHLPDPGAV---ADDMLARFSL-TDAGGRRAGEYSGGMRRRLDIAMSLVGDPPVIFLDEPTTGL 155
Cdd:COG1123 356 NPRMTVGDIIAEPLRLHGLLSRAERrerVAELLERVGLpPDLADRYPHELSGGQRQRVAIARALALEPKLLILDEPTSAL 435
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2794531883 156 DPQARAEVWRTVKQLAD-GGTTVLLTTQYLDEAEQLADRIAILHEGRIIQNGTLAEL 211
Cdd:COG1123 436 DVSVQAQILNLLRDLQReLGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEV 492
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1-203 |
9.45e-37 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 127.16 E-value: 9.45e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 1 MRKSYGELDVLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGHDVAAAagrvresisltgqfaavd 80
Cdd:cd03216 6 ITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFA------------------ 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 81 evltgrenlvlvarlrhlpdpgavaddmlarfSLTDAggRRAG-----EYSGGMRRRLDIAMSLVGDPPVIFLDEPTTGL 155
Cdd:cd03216 68 --------------------------------SPRDA--RRAGiamvyQLSVGERQMVEIARALARNARLLILDEPTAAL 113
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2794531883 156 DPQARAEVWRTVKQLADGGTTVLLTTQYLDEAEQLADRIAILHEGRII 203
Cdd:cd03216 114 TPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
2-206 |
1.84e-36 |
|
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: 128.99 E-value: 1.84e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 2 RKSYGELDVLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGHDVAAAAGRVRESISLT-GQFAAVD 80
Cdd:cd03267 28 KRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLRRIGVVfGQKTQLW 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 81 EVLTGRENLVLVARLRHLPDPGAVAD-----DMLARFSLTDAGGRRageYSGGMRRRLDIAMSLVGDPPVIFLDEPTTGL 155
Cdd:cd03267 108 WDLPVIDSFYLLAAIYDLPPARFKKRldelsELLDLEELLDTPVRQ---LSLGQRMRAEIAAALLHEPEILFLDEPTIGL 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2794531883 156 DPQARAEVWRTVKQL-ADGGTTVLLTTQYLDEAEQLADRIAILHEGRIIQNG 206
Cdd:cd03267 185 DVVAQENIRNFLKEYnRERGTTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
2-203 |
2.55e-36 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 129.05 E-value: 2.55e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 2 RKSY----GELDVLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGHDVAAAAGRvresISLTGQFA 77
Cdd:COG1116 14 SKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPD----RGVVFQEP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 78 AVDEVLTGRENLVLVARLRHLPDP--GAVADDMLARFSLTDAGGRRAGEYSGGMRRRLDIAMSLVGDPPVIFLDEPTTGL 155
Cdd:COG1116 90 ALLPWLTVLDNVALGLELRGVPKAerRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPEVLLMDEPFGAL 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2794531883 156 DPQARAEVWRTVKQL-ADGGTTVLLTTQYLDEAEQLADRIAILHE--GRII 203
Cdd:COG1116 170 DALTRERLQDELLRLwQETGKTVLFVTHDVDEAVFLADRVVVLSArpGRIV 220
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
6-211 |
4.37e-36 |
|
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: 133.49 E-value: 4.37e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 6 GELDVLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADA---GTASVQGHDVAAAAGRVR-ESISLTGQFAAVDE 81
Cdd:COG1123 17 GDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGrisGEVLLDGRDLLELSEALRgRRIGMVFQDPMTQL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 82 V-LTGRENLVLVARLRHLP--DPGAVADDMLARFSLTDAGGRRAGEYSGGMRRRLDIAMSLVGDPPVIFLDEPTTGLDPQ 158
Cdd:COG1123 97 NpVTVGDQIAEALENLGLSraEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPDLLIADEPTTALDVT 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2794531883 159 ARAEVWRTVKQL-ADGGTTVLLTTQYLDEAEQLADRIAILHEGRIIQNGTLAEL 211
Cdd:COG1123 177 TQAEILDLLRELqRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEI 230
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
14-251 |
6.84e-36 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 134.87 E-value: 6.84e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 14 VDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGHDVAAA--AGRVR-----ESISLTGQfaavdevLTGR 86
Cdd:NF033858 285 VSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDAGdiATRRRvgymsQAFSLYGE-------LTVR 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 87 ENLVLVARLRHLPD---PGAVADdMLARFSLTDAGGRRAGEYSGGMRRRLDIAMSLVGDPPVIFLDEPTTGLDPQARAEV 163
Cdd:NF033858 358 QNLELHARLFHLPAaeiAARVAE-MLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVARDMF 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 164 WRTVKQLA-DGGTTVLLTTQYLDEAEQlADRIAILHEGRIIQNGTLAELkrllpsatveyVEKQ--PTLEEVFLAVVGET 240
Cdd:NF033858 437 WRLLIELSrEDGVTIFISTHFMNEAER-CDRISLMHAGRVLASDTPAAL-----------VAARgaATLEEAFIAYLEEA 504
|
250
....*....|.
gi 2794531883 241 DGSASAGKEPS 251
Cdd:NF033858 505 AGAAAAPAAAA 515
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
2-213 |
1.49e-35 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 128.67 E-value: 1.49e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 2 RKSYGELDVLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGHDvaaaagRVRESISLTGQFAAV-- 79
Cdd:COG4586 29 RREYREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYV------PFKRRKEFARRIGVVfg 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 80 -------DevLTGRENLVLVARLRHLPDpgAVADDMLARFS----LTDAGGRRAGEYSGGMRRRLDIAMSLVGDPPVIFL 148
Cdd:COG4586 103 qrsqlwwD--LPAIDSFRLLKAIYRIPD--AEYKKRLDELVelldLGELLDTPVRQLSLGQRMRCELAAALLHRPKILFL 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2794531883 149 DEPTTGLDPQARAEVWRTVKQL-ADGGTTVLLTTQYLDEAEQLADRIAILHEGRIIQNGTLAELKR 213
Cdd:COG4586 179 DEPTIGLDVVSKEAIREFLKEYnRERGTTILLTSHDMDDIEALCDRVIVIDHGRIIYDGSLEELKE 244
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
2-213 |
1.51e-35 |
|
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: 126.84 E-value: 1.51e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 2 RKSYGELDVLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGHDVAAAAGRV-RESISLTGQ--FAA 78
Cdd:COG1124 12 GQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAfRRRVQMVFQdpYAS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 79 VDEVLTGRENLVLVARLRHLPDPGAVADDMLARFSLTDA-GGRRAGEYSGGMRRRLDIAMSLVGDPPVIFLDEPTTGLDP 157
Cdd:COG1124 92 LHPRHTVDRILAEPLRIHGLPDREERIAELLEQVGLPPSfLDRYPHQLSGGQRQRVAIARALILEPELLLLDEPTSALDV 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2794531883 158 QARAEVWRTVKQL-ADGGTTVLLTTQYLDEAEQLADRIAILHEGRIIQNGTLAELKR 213
Cdd:COG1124 172 SVQAEILNLLKDLrEERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLA 228
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
2-204 |
4.91e-35 |
|
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: 124.51 E-value: 4.91e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 2 RKSYG----ELDVLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGHDVAaaagRVRESISLTGQFA 77
Cdd:cd03293 7 SKTYGggggAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVT----GPGPDRGYVFQQD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 78 AVDEVLTGRENLVLVARLRHLPDPGA--VADDMLARFSLTDAGGRRAGEYSGGMRRRLDIAMSLVGDPPVIFLDEPTTGL 155
Cdd:cd03293 83 ALLPWLTVLDNVALGLELQGVPKAEAreRAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDEPFSAL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2794531883 156 DPQARAEVWR-TVKQLADGGTTVLLTTQYLDEAEQLADRIAIL--HEGRIIQ 204
Cdd:cd03293 163 DALTREQLQEeLLDIWRETGKTVLLVTHDIDEAVFLADRVVVLsaRPGRIVA 214
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-203 |
5.39e-35 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 130.53 E-value: 5.39e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 1 MRKSYGELDVLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGHDV-------AAAAGrvresISLT 73
Cdd:COG3845 11 ITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVrirsprdAIALG-----IGMV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 74 GQ-FAAVDeVLTGRENLVLVA--RLRHLPDPGAVADDMLA---RFSLT---DAggrRAGEYSGGMRRRLDIAMSLVGDPP 144
Cdd:COG3845 86 HQhFMLVP-NLTVAENIVLGLepTKGGRLDRKAARARIRElseRYGLDvdpDA---KVEDLSVGEQQRVEILKALYRGAR 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2794531883 145 VIFLDEPTTGLDPQARAEVWRTVKQLADGGTTVLLTTQYLDEAEQLADRIAILHEGRII 203
Cdd:COG3845 162 ILILDEPTAVLTPQEADELFEILRRLAAEGKSIIFITHKLREVMAIADRVTVLRRGKVV 220
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
11-153 |
6.54e-35 |
|
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: 121.99 E-value: 6.54e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 11 LRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGHDVAAAAGR-VRESISLTGQFAAVDEVLTGRENL 89
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKsLRKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 90 VLVARLRHLPDP--GAVADDMLARFSLTDAGGRRAG----EYSGGMRRRLDIAMSLVGDPPVIFLDEPTT 153
Cdd:pfam00005 81 RLGLLLKGLSKRekDARAEEALEKLGLGDLADRPVGerpgTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
3-201 |
1.82e-34 |
|
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: 121.91 E-value: 1.82e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 3 KSYGELDVLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGHDVAAAAGRV---RESISLTGQFAAV 79
Cdd:cd03229 8 KRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELpplRRRIGMVFQDFAL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 80 DEVLTGRENLVLVarlrhlpdpgavaddmlarfsltdaggrrageYSGGMRRRLDIAMSLVGDPPVIFLDEPTTGLDPQA 159
Cdd:cd03229 88 FPHLTVLENIALG--------------------------------LSGGQQQRVALARALAMDPDVLLLDEPTSALDPIT 135
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2794531883 160 RAEVWRTVKQLADG-GTTVLLTTQYLDEAEQLADRIAILHEGR 201
Cdd:cd03229 136 RREVRALLKSLQAQlGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
3-211 |
2.04e-34 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 128.98 E-value: 2.04e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 3 KSYGELDVLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGHDV-------AAAAGrvresISLTGQ 75
Cdd:COG1129 12 KSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVrfrsprdAQAAG-----IAIIHQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 76 -FAAVDEvLTGRENLVL--VARLRHLPDPGAV---ADDMLARFSLTDAGGRRAGEYSGGMRRRLDIAMSLVGDPPVIFLD 149
Cdd:COG1129 87 eLNLVPN-LSVAENIFLgrEPRRGGLIDWRAMrrrARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRDARVLILD 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2794531883 150 EPTTGLDPQARAEVWRTVKQLADGGTTVLLTTQYLDEAEQLADRIAILHEGRIIQNGTLAEL 211
Cdd:COG1129 166 EPTASLTEREVERLFRIIRRLKAQGVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVAEL 227
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
10-203 |
2.96e-34 |
|
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: 123.00 E-value: 2.96e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 10 VLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGHDVAAAAGRVRE----SISLTGQ--FAAVDEVL 83
Cdd:cd03257 20 ALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKirrkEIQMVFQdpMSSLNPRM 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 84 T------------------GRENLVLVARLRHLPDPGAVADdmlarfsltdaggRRAGEYSGGMRRRLDIAMSLVGDPPV 145
Cdd:cd03257 100 TigeqiaeplrihgklskkEARKEAVLLLLVGVGLPEEVLN-------------RYPHELSGGQRQRVAIARALALNPKL 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2794531883 146 IFLDEPTTGLDPQARAEVWRTVKQLADG-GTTVLLTTQYLDEAEQLADRIAILHEGRII 203
Cdd:cd03257 167 LIADEPTSALDVSVQAQILDLLKKLQEElGLTLLFITHDLGVVAKIADRVAVMYAGKIV 225
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
2-211 |
3.91e-34 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 123.24 E-value: 3.91e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 2 RKSY-GELDVLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGHDVAAAAGR-VRESISLTG----Q 75
Cdd:COG3638 9 SKRYpGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRaLRRLRRRIGmifqQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 76 FAAVDEvLTGRENlVLVARLRHLPDPGAV-----------ADDMLARFSLTDAGGRRAGEYSGGMRRRLDIAMSLVGDPP 144
Cdd:COG3638 89 FNLVPR-LSVLTN-VLAGRLGRTSTWRSLlglfppedrerALEALERVGLADKAYQRADQLSGGQQQRVAIARALVQEPK 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2794531883 145 VIFLDEPTTGLDPQARAEVWRTVKQLA-DGGTTVLLTTQYLDEAEQLADRIAILHEGRIIQNGTLAEL 211
Cdd:COG3638 167 LILADEPVASLDPKTARQVMDLLRRIArEDGITVVVNLHQVDLARRYADRIIGLRDGRVVFDGPPAEL 234
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
2-211 |
4.40e-34 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 122.80 E-value: 4.40e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 2 RKSYGELDVLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGHDVAAAAGRVRESISLTG---Q--- 75
Cdd:COG1126 8 HKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKKDINKLRRKVGmvfQqfn 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 76 -FAAvdevLTGRENLVLvA--RLRHLPDPGAV--ADDMLARFSLTDAGGRRAGEYSGGMRRRLDIAMSLVGDPPVIFLDE 150
Cdd:COG1126 88 lFPH----LTVLENVTL-ApiKVKKMSKAEAEerAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKVMLFDE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2794531883 151 PTTGLDPQARAEVWRTVKQLADGGTTVLLTTQYLDEAEQLADRIAILHEGRIIQNGTLAEL 211
Cdd:COG1126 163 PTSALDPELVGEVLDVMRDLAKEGMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEF 223
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
23-212 |
1.48e-33 |
|
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: 128.21 E-value: 1.48e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 23 IHALLGSNGAGKTTLVKILSTLVRADAGTASVQGHDVAAAAGRVRESISLTGQFAAVDEVLTGRENLVLVARL--RHLPD 100
Cdd:TIGR01257 958 ITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDAVRQSLGMCPQHNILFHHLTVAEHILFYAQLkgRSWEE 1037
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 101 PGAVADDMLARFSLTDAGGRRAGEYSGGMRRRLDIAMSLVGDPPVIFLDEPTTGLDPQARAEVWRTVKQLADgGTTVLLT 180
Cdd:TIGR01257 1038 AQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRS-GRTIIMS 1116
|
170 180 190
....*....|....*....|....*....|..
gi 2794531883 181 TQYLDEAEQLADRIAILHEGRIIQNGTLAELK 212
Cdd:TIGR01257 1117 THHMDEADLLGDRIAIISQGRLYCSGTPLFLK 1148
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
4-206 |
2.24e-33 |
|
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: 119.58 E-value: 2.24e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 4 SYGELDVLRGVDLGVAPGTIHALLGSNGAGKTTLVKILS--TLVRADAGTASVQGHDVAAAAgrVRESISLTGQFAAVDE 81
Cdd:cd03213 18 SKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAgrRTGLGVSGEVLINGRPLDKRS--FRKIIGYVPQDDILHP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 82 VLTGRENLVLVARLRHLpdpgavaddmlarfsltdaggrrageySGGMRRRLDIAMSLVGDPPVIFLDEPTTGLDPQARA 161
Cdd:cd03213 96 TLTVRETLMFAAKLRGL---------------------------SGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSAL 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2794531883 162 EVWRTVKQLADGGTTVLLTT-QYLDEAEQLADRIAILHEGRIIQNG 206
Cdd:cd03213 149 QVMSLLRRLADTGRTIICSIhQPSSEIFELFDKLLLLSQGRVIYFG 194
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
2-202 |
2.34e-33 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 119.92 E-value: 2.34e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 2 RKSYGELDVLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGHDVAAAAG-RVRESISLTGQ----F 76
Cdd:COG4619 7 SFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPpEWRRQVAYVPQepalW 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 77 AAvdevlTGRENLVLVARLRHLPDPGAVADDMLARFSLT-DAGGRRAGEYSGGMRRRLDIAMSLVGDPPVIFLDEPTTGL 155
Cdd:COG4619 87 GG-----TVRDNLPFPFQLRERKFDRERALELLERLGLPpDILDKPVERLSGGERQRLALIRALLLQPDVLLLDEPTSAL 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2794531883 156 DPQARAEVWRTVKQL-ADGGTTVLLTTQYLDEAEQLADRIAILHEGRI 202
Cdd:COG4619 162 DPENTRRVEELLREYlAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
2-211 |
3.24e-33 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 123.28 E-value: 3.24e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 2 RKSYGELDVLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGHDVAA-AAGRvREsISLtgqfaavd 80
Cdd:COG3842 12 SKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGlPPEK-RN-VGM-------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 81 eV---------LTGRENlvlVA---RLRHLP--DPGAVADDMLARFSLTDAGGRRAGEYSGGMRRRLDIAMSLVGDPPVI 146
Cdd:COG3842 82 -VfqdyalfphLTVAEN---VAfglRMRGVPkaEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2794531883 147 FLDEPTTGLDPQARAEVWRTVKQL-ADGGTTVLLTTQYLDEAEQLADRIAILHEGRIIQNGTLAEL 211
Cdd:COG3842 158 LLDEPLSALDAKLREEMREELRRLqRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEI 223
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
1-202 |
7.52e-33 |
|
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: 118.79 E-value: 7.52e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 1 MRKSYGELDVLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGHDV---AAAAGRVRESISLTGQFA 77
Cdd:cd03262 6 LHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLtddKKNINELRQKVGMVFQQF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 78 AVDEVLTGRENLVLVAR-LRHLPDPGAV--ADDMLARFSLTDAGGRRAGEYSGGMRRRLDIAMSLVGDPPVIFLDEPTTG 154
Cdd:cd03262 86 NLFPHLTVLENITLAPIkVKGMSKAEAEerALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFDEPTSA 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2794531883 155 LDPQARAEVWRTVKQLADGGTTVLLTTQYLDEAEQLADRIAILHEGRI 202
Cdd:cd03262 166 LDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
3-213 |
1.58e-32 |
|
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: 118.94 E-value: 1.58e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 3 KSYGELD-VLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGHDVAAAAG-RVRESISLTGQFAAVD 80
Cdd:cd03295 8 KRYGGGKkAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPvELRRKIGYVIQQIGLF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 81 EVLTGRENLVLVARLRHLPDPG--AVADDMLARFSLTDAG--GRRAGEYSGGMRRRLDIAMSLVGDPPVIFLDEPTTGLD 156
Cdd:cd03295 88 PHMTVEENIALVPKLLKWPKEKirERADELLALVGLDPAEfaDRYPHELSGGQQQRVGVARALAADPPLLLMDEPFGALD 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2794531883 157 PQARAEVWRTVKQL-ADGGTTVLLTTQYLDEAEQLADRIAILHEGRIIQNGTLAELKR 213
Cdd:cd03295 168 PITRDQLQEEFKRLqQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILR 225
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
3-211 |
5.62e-32 |
|
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: 117.28 E-value: 5.62e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 3 KSYGELD-VLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGHDVAAAAGR----VRESI------- 70
Cdd:cd03256 8 KTYPNGKkALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKalrqLRRQIgmifqqf 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 71 SLTGQFAAVDEVLTGRenLVLVARLRHLPDPGAVAD-----DMLARFSLTDAGGRRAGEYSGGMRRRLDIAMSLVGDPPV 145
Cdd:cd03256 88 NLIERLSVLENVLSGR--LGRRSTWRSLFGLFPKEEkqralAALERVGLLDKAYQRADQLSGGQQQRVAIARALMQQPKL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2794531883 146 IFLDEPTTGLDPQARAEVWRTVKQLADG-GTTVLLTTQYLDEAEQLADRIAILHEGRIIQNGTLAEL 211
Cdd:cd03256 166 ILADEPVASLDPASSRQVMDLLKRINREeGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAEL 232
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
2-211 |
1.00e-31 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 119.10 E-value: 1.00e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 2 RKSYGELDVLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGHDVAAAAgRVRES-ISLTGQFAAVD 80
Cdd:COG1118 9 SKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFTNL-PPRERrVGFVFQHYALF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 81 EVLTGRENlvlVA-RLRHLPDPGA----VADDMLARFSLTDAGGRRAGEYSGGMRRRLDIAMSLVGDPPVIFLDEPTTGL 155
Cdd:COG1118 88 PHMTVAEN---IAfGLRVRPPSKAeiraRVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLLLDEPFGAL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2794531883 156 DPQARAEVWRTVKQLAD--GGTTVLLTTQyLDEAEQLADRIAILHEGRIIQNGTLAEL 211
Cdd:COG1118 165 DAKVRKELRRWLRRLHDelGGTTVFVTHD-QEEALELADRVVVMNQGRIEQVGTPDEV 221
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1-211 |
2.22e-31 |
|
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: 115.51 E-value: 2.22e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 1 MRKSYGELDVLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGHDVAAAAGRVREsISLTGQFAAVD 80
Cdd:cd03296 8 VSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQERN-VGFVFQHYALF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 81 EVLTGRENLVLVARLRH---LPDPGAV---ADDMLARFSLTDAGGRRAGEYSGGMRRRLDIAMSLVGDPPVIFLDEPTTG 154
Cdd:cd03296 87 RHMTVFDNVAFGLRVKPrseRPPEAEIrakVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLDEPFGA 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2794531883 155 LDPQARAEVWRTVKQLAD--GGTTVLLTTQYlDEAEQLADRIAILHEGRIIQNGTLAEL 211
Cdd:cd03296 167 LDAKVRKELRRWLRRLHDelHVTTVFVTHDQ-EEALEVADRVVVMNKGRIEQVGTPDEV 224
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
6-211 |
1.69e-30 |
|
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: 113.06 E-value: 1.69e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 6 GELDVLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGHDVAAAAGR----VRESISLTGQFAAVDE 81
Cdd:cd03258 16 GKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKelrkARRRIGMIFQHFNLLS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 82 VLTGRENLVLVARLRHLPDP--GAVADDMLARFSLTDAGGRRAGEYSGGMRRRLDIAMSLVGDPPVIFLDEPTTGLDPQA 159
Cdd:cd03258 96 SRTVFENVALPLEIAGVPKAeiEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKVLLCDEATSALDPET 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2794531883 160 RAEVWRTVKQL-ADGGTTVLLTTQYLDEAEQLADRIAILHEGRIIQNGTLAEL 211
Cdd:cd03258 176 TQSILALLRDInRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEV 228
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
2-206 |
1.72e-30 |
|
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: 113.13 E-value: 1.72e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 2 RKSYGELDVLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADA---GTASVQGHDVAAAagRVRESISLTGQFAA 78
Cdd:cd03234 14 KNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGttsGQILFNGQPRKPD--QFQKCVAYVRQDDI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 79 VDEVLTGRENLVLVARLRhLPDPGA-------VADDMLARFSLTDAGGRRAGEYSGGMRRRLDIAMSLVGDPPVIFLDEP 151
Cdd:cd03234 92 LLPGLTVRETLTYTAILR-LPRKSSdairkkrVEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEP 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2794531883 152 TTGLDPQARAEVWRTVKQLADGGTTVLLTT-QYLDEAEQLADRIAILHEGRIIQNG 206
Cdd:cd03234 171 TSGLDSFTALNLVSTLSQLARRNRIVILTIhQPRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
4-211 |
1.77e-30 |
|
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: 113.64 E-value: 1.77e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 4 SYGELDVLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVR-ADAGTASVQGHDvaaaagRVRESI------------ 70
Cdd:COG1119 12 RRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPpTYGNDVRLFGER------RGGEDVwelrkriglvsp 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 71 SLTGQFAAVDEVLtgreNLVL------VARLRHlPDPG--AVADDMLARFSLTDAGGRRAGEYSGGMRRRLDIAMSLVGD 142
Cdd:COG1119 86 ALQLRFPRDETVL----DVVLsgffdsIGLYRE-PTDEqrERARELLELLGLAHLADRPFGTLSQGEQRRVLIARALVKD 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 143 PPVIFLDEPTTGLDPQARAEVWRTVKQLA-DGGTTVLLTTQYLDEAEQLADRIAILHEGRIIQNGTLAEL 211
Cdd:COG1119 161 PELLILDEPTAGLDLGARELLLALLDKLAaEGAPTLVLVTHHVEEIPPGITHVLLLKDGRVVAAGPKEEV 230
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
4-207 |
1.84e-30 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 113.57 E-value: 1.84e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 4 SYGELDVLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGHDVAAAAGRV-RESISLTGQFAAVDEV 82
Cdd:PRK11231 11 GYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQlARRLALLPQHHLTPEG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 83 LTGREnLVLVARLRHLPDPGAVADD-------MLARFSLTDAGGRRAGEYSGGMRRRLDIAMSLVGDPPVIFLDEPTTGL 155
Cdd:PRK11231 91 ITVRE-LVAYGRSPWLSLWGRLSAEdnarvnqAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYL 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2794531883 156 DPQARAEVWRTVKQLADGGTTVLLTTQYLDEAEQLADRIAILHEGRIIQNGT 207
Cdd:PRK11231 170 DINHQVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGT 221
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
15-218 |
2.80e-30 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 112.54 E-value: 2.80e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 15 DLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGHDVAAAAGRVReSISLTGQ----FAAvdevLTGREN-- 88
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAER-PVSMLFQennlFPH----LTVAQNig 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 89 LVLVARLRHLPDPGAVADDMLARFSLTDAGGRRAGEYSGGMRRRLDIAMSLVGDPPVIFLDEPTTGLDPQARAEVWRTVK 168
Cdd:COG3840 94 LGLRPGLKLTAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDPALRQEMLDLVD 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2794531883 169 QLADG-GTTVLLTTQYLDEAEQLADRIAILHEGRIIQNGTLAELKRLLPSA 218
Cdd:COG3840 174 ELCRErGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPP 224
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
2-211 |
2.83e-30 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 115.17 E-value: 2.83e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 2 RKSYGELDVLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGHDVAAAAGRVReSISLTGQFAAVDE 81
Cdd:COG3839 10 SKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKDR-NIAMVFQSYALYP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 82 VLTGRENLVLVARLRHLPDPGAVA--DDMLARFSLTDAGGRRAGEYSGGMRRRLDIAMSLVGDPPVIFLDEPTTGLDPQA 159
Cdd:COG3839 89 HMTVYENIAFPLKLRKVPKAEIDRrvREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFLLDEPLSNLDAKL 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2794531883 160 RAEVWRTVKQL-ADGGTTVLLTTQYLDEAEQLADRIAILHEGRIIQNGTLAEL 211
Cdd:COG3839 169 RVEMRAEIKRLhRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGTPEEL 221
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
11-213 |
2.99e-30 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 112.90 E-value: 2.99e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 11 LRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGHDVAA--AAGRVRESISLTGQFAAVDEVLTGREN 88
Cdd:COG4674 26 LNDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTRPDSGSVLFGGTDLTGldEHEIARLGIGRKFQKPTVFEELTVFEN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 89 LVLVAR--------LRHLPDPGAVA--DDMLARFSLTDAGGRRAGEYSGGMRRRLDIAMSLVGDPPVIFLDEPTTGLDPQ 158
Cdd:COG4674 106 LELALKgdrgvfasLFARLTAEERDriEEVLETIGLTDKADRLAGLLSHGQKQWLEIGMLLAQDPKLLLLDEPVAGMTDA 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2794531883 159 ARAEVWRTVKQLAdGGTTVLLTTQYLDEAEQLADRIAILHEGRIIQNGTLAELKR 213
Cdd:COG4674 186 ETERTAELLKSLA-GKHSVVVVEHDMEFVRQIARKVTVLHQGSVLAEGSLDEVQA 239
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
6-213 |
5.60e-30 |
|
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: 117.17 E-value: 5.60e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 6 GELDVLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGHDVAAAAGR-VRESISLTGQ----FAAvd 80
Cdd:COG4987 346 AGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDdLRRRIAVVPQrphlFDT-- 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 81 evlTGRENLvLVARlrhlpdPGAVADDM---LARFSLTD--------------AGGRRageYSGGMRRRLDIAMSLVGDP 143
Cdd:COG4987 424 ---TLRENL-RLAR------PDATDEELwaaLERVGLGDwlaalpdgldtwlgEGGRR---LSGGERRRLALARALLRDA 490
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 144 PVIFLDEPTTGLDPQARAEVWRTVKQLADGGTTVLLTTQyLDEAEQlADRIAILHEGRIIQNGTLAELKR 213
Cdd:COG4987 491 PILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHR-LAGLER-MDRILVLEDGRIVEQGTHEELLA 558
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
11-225 |
6.03e-30 |
|
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: 112.74 E-value: 6.03e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 11 LRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGHDVAA-AAGRVRE----SISLTGQFAAVDEVLTG 85
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAmSRKELRElrrkKISMVFQSFALLPHRTV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 86 RENLVLVARLRHLP--DPGAVADDMLARFSLTDAGGRRAGEYSGGMRRRLDIAMSLVGDPPVIFLDEPTTGLDPQARAEV 163
Cdd:cd03294 120 LENVAFGLEVQGVPraEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREM 199
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2794531883 164 WRTVKQL-ADGGTTVLLTTQYLDEAEQLADRIAILHEGRIIQNGTLAElkrLLPSATVEYVEK 225
Cdd:cd03294 200 QDELLRLqAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEE---ILTNPANDYVRE 259
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
4-210 |
9.37e-30 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 111.75 E-value: 9.37e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 4 SYGELDVLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGHDVAA------AAGR--VRESISLTGQ 75
Cdd:COG4559 10 RLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAwspwelARRRavLPQHSSLAFP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 76 FAAVDEVLTGREnlvlvARLRHLPDPGAVADDMLARFSLTDAGGRRAGEYSGGMRRRLDIAMSLV-------GDPPVIFL 148
Cdd:COG4559 90 FTVEEVVALGRA-----PHGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLAqlwepvdGGPRWLFL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2794531883 149 DEPTTGLDPQARAEVWRTVKQLADGGTTVL-------LTTQYldeaeqlADRIAILHEGRIIQNGTLAE 210
Cdd:COG4559 165 DEPTSALDLAHQHAVLRLARQLARRGGGVVavlhdlnLAAQY-------ADRILLLHQGRLVAQGTPEE 226
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
3-211 |
2.10e-29 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 110.94 E-value: 2.10e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 3 KSYGELDVLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGHDVAAAAGRVR-ESISLTGQFAAVDE 81
Cdd:COG4604 9 KRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELaKRLAILRQENHINS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 82 VLTGREnlvLVA-------RLRHLPDPGAVADDMLARFSLTDAGGRRAGEYSGGMRRRLDIAMSLVGDPPVIFLDEPTTG 154
Cdd:COG4604 89 RLTVRE---LVAfgrfpysKGRLTAEDREIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQDTDYVLLDEPLNN 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2794531883 155 LDPQARAEVWRTVKQLADG-GTTVLLTTQYLDEAEQLADRIAILHEGRIIQNGTLAEL 211
Cdd:COG4604 166 LDMKHSVQMMKLLRRLADElGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEI 223
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
4-203 |
2.52e-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: 109.27 E-value: 2.52e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 4 SYGEL-DVLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGHDvaAAAGRVRESISLTGQfaAVDEV 82
Cdd:cd03226 8 SYKKGtEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKP--IKAKERRKSIGYVMQ--DVDYQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 83 LTG---RENLVLvaRLRHLPDPGAVADDMLARFSLTDAGGRRAGEYSGGMRRRLDIAMSLVGDPPVIFLDEPTTGLDPQA 159
Cdd:cd03226 84 LFTdsvREELLL--GLKELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKN 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2794531883 160 RAEVWRTVKQLADGGTTVLLTTQYLDEAEQLADRIAILHEGRII 203
Cdd:cd03226 162 MERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
4-211 |
2.70e-29 |
|
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: 115.70 E-value: 2.70e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 4 SYGELD--VLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGHDVAA-AAGRVRESISLTGQfaavD 80
Cdd:COG2274 482 RYPGDSppVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQiDPASLRRQIGVVLQ----D 557
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 81 EVL---TGRENLVLVarlrhlpDPGAVADDMLArfSLTDAG----------------GRRAGEYSGGMRRRLDIAMSLVG 141
Cdd:COG2274 558 VFLfsgTIRENITLG-------DPDATDEEIIE--AARLAGlhdfiealpmgydtvvGEGGSNLSGGQRQRLAIARALLR 628
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 142 DPPVIFLDEPTTGLDPQARAEVWRTVKQLAdGGTTVLLTTQYLdEAEQLADRIAILHEGRIIQNGTLAEL 211
Cdd:COG2274 629 NPRILILDEATSALDAETEAIILENLRRLL-KGRTVIIIAHRL-STIRLADRIIVLDKGRIVEDGTHEEL 696
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
6-211 |
8.72e-29 |
|
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: 109.44 E-value: 8.72e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 6 GELDVLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGHDVAAAAGR--VRESISL-----TGQF-A 77
Cdd:TIGR04520 13 SEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLDEENLweIRKKVGMvfqnpDNQFvG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 78 AV--DEVLTGRENLVL-----VARLrhlpdpgavaDDMLARFSLTDAGGRRAGEYSGGMRRRLDIAMSLVGDPPVIFLDE 150
Cdd:TIGR04520 93 ATveDDVAFGLENLGVpreemRKRV----------DEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLAMRPDIIILDE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2794531883 151 PTTGLDPQARAEVWRTVKQL-ADGGTTVLLTTQYLDEAEQlADRIAILHEGRIIQNGTLAEL 211
Cdd:TIGR04520 163 ATSMLDPKGRKEVLETIRKLnKEEGITVISITHDMEEAVL-ADRVIVMNKGKIVAEGTPREI 223
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
17-211 |
1.85e-28 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 113.22 E-value: 1.85e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 17 GVA-PGTIHALLGSNGAGKTTLVKILSTLVRAD---AGTASVQGHDVAAAAGRVRESisltgqFAAVDEV----LTGREN 88
Cdd:TIGR00955 46 GVAkPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGMPIDAKEMRAISA------YVQQDDLfiptLTVREH 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 89 LVLVARLR---HLPDPGAVA--DDMLARFSLTDA-------GGRRAGeYSGGMRRRLDIAMSLVGDPPVIFLDEPTTGLD 156
Cdd:TIGR00955 120 LMFQAHLRmprRVTKKEKRErvDEVLQALGLRKCantrigvPGRVKG-LSGGERKRLAFASELLTDPPLLFCDEPTSGLD 198
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2794531883 157 PQARAEVWRTVKQLADGGTTVLLTT-QYLDEAEQLADRIAILHEGRIIQNGTLAEL 211
Cdd:TIGR00955 199 SFMAYSVVQVLKGLAQKGKTIICTIhQPSSELFELFDKIILMAEGRVAYLGSPDQA 254
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
10-201 |
1.94e-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: 105.93 E-value: 1.94e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 10 VLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGHDVAAAAGR-VRESISLTGQfaavDEVL---TG 85
Cdd:cd03228 17 VLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLEsLRKNIAYVPQ----DPFLfsgTI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 86 RENLVlvarlrhlpdpgavaddmlarfsltdaggrrageySGGMRRRLDIAMSLVGDPPVIFLDEPTTGLDPQARAEVWR 165
Cdd:cd03228 93 RENIL-----------------------------------SGGQRQRIAIARALLRDPPILILDEATSALDPETEALILE 137
|
170 180 190
....*....|....*....|....*....|....*.
gi 2794531883 166 TVKQLADgGTTVLLTTQYLDEAEQlADRIAILHEGR 201
Cdd:cd03228 138 ALRALAK-GKTVIVIAHRLSTIRD-ADRIIVLDDGR 171
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
10-210 |
2.70e-28 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 107.94 E-value: 2.70e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 10 VLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGHDVAAAAGR--------VRESISLTGQFAAVDE 81
Cdd:PRK13548 17 LLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAelarrravLPQHSSLSFPFTVEEV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 82 VLTGRenlvlvARLRHLPDPG-AVADDMLARFSLTDAGGRRAGEYSGGMRRRLDIAMSLV------GDPPVIFLDEPTTG 154
Cdd:PRK13548 97 VAMGR------APHGLSRAEDdALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAqlwepdGPPRWLLLDEPTSA 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2794531883 155 LDPQARAEVWRTVKQLA-DGGTTVLLTTQYLDEAEQLADRIAILHEGRIIQNGTLAE 210
Cdd:PRK13548 171 LDLAHQHHVLRLARQLAhERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAE 227
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
2-206 |
2.80e-28 |
|
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: 107.27 E-value: 2.80e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 2 RKSYGELDVLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLV-----RADAGTASVQGHDVAAAAGRV---RESISLT 73
Cdd:cd03260 7 NVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNdlipgAPDEGEVLLDGKDIYDLDVDVlelRRRVGMV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 74 GQFAAVDEvLTGRENLVLVARLRHLPDPGAVADDM---LARFSLTDAGGRR--AGEYSGGMRRRLDIAMSLVGDPPVIFL 148
Cdd:cd03260 87 FQKPNPFP-GSIYDNVAYGLRLHGIKLKEELDERVeeaLRKAALWDEVKDRlhALGLSGGQQQRLCLARALANEPEVLLL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2794531883 149 DEPTTGLDPQARAEVWRTVKQLADgGTTVLLTTQYLDEAEQLADRIAILHEGRIIQNG 206
Cdd:cd03260 166 DEPTSALDPISTAKIEELIAELKK-EYTIVIVTHNMQQAARVADRTAFLLNGRLVEFG 222
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
3-211 |
4.73e-28 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 107.10 E-value: 4.73e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 3 KSYGELDVLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGHDVAAA----------AGRVRESISL 72
Cdd:PRK09493 9 KHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPkvderlirqeAGMVFQQFYL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 73 TGQFAAVDEVLTGRenlvlvARLRHL--PDPGAVADDMLARFSLTDAGGRRAGEYSGGMRRRLDIAMSLVGDPPVIFLDE 150
Cdd:PRK09493 89 FPHLTALENVMFGP------LRVRGAskEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2794531883 151 PTTGLDPQARAEVWRTVKQLADGGTTVLLTTQYLDEAEQLADRIAILHEGRIIQNGTLAEL 211
Cdd:PRK09493 163 PTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVL 223
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
2-211 |
9.15e-28 |
|
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: 106.17 E-value: 9.15e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 2 RKSYGELDVLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGHDVAAAAGRVREsISLTGQFAAVDE 81
Cdd:cd03300 7 SKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKRP-VNTVFQNYALFP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 82 VLTGRENLVLVARLRHLP--DPGAVADDMLARFSLTDAGGRRAGEYSGGMRRRLDIAMSLVGDPPVIFLDEPTTGLDPQA 159
Cdd:cd03300 86 HLTVFENIAFGLRLKKLPkaEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALDLKL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2794531883 160 RAEVWRTVKQLADG-GTTVLLTTQYLDEAEQLADRIAILHEGRIIQNGTLAEL 211
Cdd:cd03300 166 RKDMQLELKRLQKElGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEI 218
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
6-211 |
1.18e-27 |
|
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: 107.83 E-value: 1.18e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 6 GELDVLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRA---DAGTASVQGHDVAAAAG------RVREsISLTGQ- 75
Cdd:COG0444 16 GVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEkelrkiRGRE-IQMIFQd 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 76 -FAAVDEVLTGRENLVLVARLrHLPDPGAVAD----DMLARFSLTDAGgRRAGEY----SGGMRRRLDIAMSLVGDPPVI 146
Cdd:COG0444 95 pMTSLNPVMTVGDQIAEPLRI-HGGLSKAEAReraiELLERVGLPDPE-RRLDRYphelSGGMRQRVMIARALALEPKLL 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2794531883 147 FLDEPTTGLDPQARAEVWRTVKQL-ADGGTTVLLTTQYLDEAEQLADRIAILHEGRIIQNGTLAEL 211
Cdd:COG0444 173 IADEPTTALDVTIQAQILNLLKDLqRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGPVEEL 238
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
3-209 |
2.82e-27 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 105.09 E-value: 2.82e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 3 KSYGELDVLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGH------DVAAAAGR-VRESISLTGQ 75
Cdd:COG4161 10 CFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHqfdfsqKPSEKAIRlLRQKVGMVFQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 76 FAAVDEVLTGRENLVLV-ARLRHLPDPGAV--ADDMLARFSLTDAGGRRAGEYSGGMRRRLDIAMSLVGDPPVIFLDEPT 152
Cdd:COG4161 90 QYNLWPHLTVMENLIEApCKVLGLSKEQARekAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPT 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2794531883 153 TGLDPQARAEVWRTVKQLADGGTTVLLTTQYLDEAEQLADRIAILHEGRIIQNGTLA 209
Cdd:COG4161 170 AALDPEITAQVVEIIRELSQTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQGDAS 226
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
3-203 |
4.12e-27 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 103.98 E-value: 4.12e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 3 KSY-GELDVLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGHDVAAAAGR----VRESISLTGQfa 77
Cdd:COG2884 9 KRYpGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRReipyLRRRIGVVFQ-- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 78 avD-EVLTGR---ENLVLVARLRHLPDP--GAVADDMLARFSLTDAGGRRAGEYSGGMRRRLDIAMSLVGDPPVIFLDEP 151
Cdd:COG2884 87 --DfRLLPDRtvyENVALPLRVTGKSRKeiRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLLADEP 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2794531883 152 TTGLDPQARAEVWRTVKQLADGGTTVLLTTQYLDEAEQLADRIAILHEGRII 203
Cdd:COG2884 165 TGNLDPETSWEIMELLEEINRRGTTVLIATHDLELVDRMPKRVLELEDGRLV 216
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
3-211 |
5.38e-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: 104.30 E-value: 5.38e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 3 KSYGELD-VLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGHDVAAAAGR----VRESISLTGQFA 77
Cdd:TIGR02315 9 KVYPNGKqALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKklrkLRRRIGMIFQHY 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 78 AVDEVLTGRENlVLVARL-----------RHLPDPGAVADDMLARFSLTDAGGRRAGEYSGGMRRRLDIAMSLVGDPPVI 146
Cdd:TIGR02315 89 NLIERLTVLEN-VLHGRLgykptwrsllgRFSEEDKERALSALERVGLADKAYQRADQLSGGQQQRVAIARALAQQPDLI 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2794531883 147 FLDEPTTGLDPQARAEVWRTVKQLA-DGGTTVLLTTQYLDEAEQLADRIAILHEGRIIQNGTLAEL 211
Cdd:TIGR02315 168 LADEPIASLDPKTSKQVMDYLKRINkEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSEL 233
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
3-206 |
5.56e-27 |
|
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: 103.49 E-value: 5.56e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 3 KSYGELDVLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGHDVAAAAGRVREsISLTGQFAAVDEV 82
Cdd:cd03301 8 KRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDRD-IAMVFQNYALYPH 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 83 LTGRENLVLVARLRHLPDPGAV-----ADDMLARFSLTDaggRRAGEYSGGMRRRLDIAMSLVGDPPVIFLDEPTTGLDP 157
Cdd:cd03301 87 MTVYDNIAFGLKLRKVPKDEIDervreVAELLQIEHLLD---RKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLDA 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2794531883 158 ----QARAEVWRTVKQLadgGTTVLLTTQYLDEAEQLADRIAILHEGRIIQNG 206
Cdd:cd03301 164 klrvQMRAELKRLQQRL---GTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
4-197 |
6.03e-27 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 102.70 E-value: 6.03e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 4 SYGELDVLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTasvqghdVAAAAGRvreSISLTGQFAAVDEVL 83
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGT-------VRRAGGA---RVAYVPQRSEVPDSL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 84 TGR-ENLVLVARLRHLP-------DPGAVADDMLARFSLTDAGGRRAGEYSGGMRRRLDIAMSLVGDPPVIFLDEPTTGL 155
Cdd:NF040873 71 PLTvRDLVAMGRWARRGlwrrltrDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGL 150
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2794531883 156 DPQARAEVWRTVKQLADGGTTVLLTTQYLDEAeQLADRIAIL 197
Cdd:NF040873 151 DAESRERIIALLAEEHARGATVVVVTHDLELV-RRADPCVLL 191
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
9-202 |
9.79e-27 |
|
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: 101.74 E-value: 9.79e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 9 DVLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGHDVAAaaGRVRESIsltgqfaavdevltgREN 88
Cdd:cd03215 14 GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTR--RSPRDAI---------------RAG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 89 LVLVA--RLRH-LPDPGAVADDMLARFSLtdaggrrageySGGMRRRLDIAMSLVGDPPVIFLDEPTTGLDPQARAEVWR 165
Cdd:cd03215 77 IAYVPedRKREgLVLDLSVAENIALSSLL-----------SGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYR 145
|
170 180 190
....*....|....*....|....*....|....*..
gi 2794531883 166 TVKQLADGGTTVLLTTQYLDEAEQLADRIAILHEGRI 202
Cdd:cd03215 146 LIRELADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
7-211 |
2.35e-26 |
|
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: 103.30 E-value: 2.35e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 7 ELDVLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGHDVAAAAG----RVRESISLTGQFAA---- 78
Cdd:TIGR04521 17 EKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKkklkDLRKKVGLVFQFPEhqlf 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 79 ----VDEVLTGRENLVL-----VARLRHLPDPGAVADDMLAR--FSLtdaggrrageySGGMRRRLDIAMSLVGDPPVIF 147
Cdd:TIGR04521 97 eetvYKDIAFGPKNLGLseeeaEERVKEALELVGLDEEYLERspFEL-----------SGGQMRRVAIAGVLAMEPEVLI 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2794531883 148 LDEPTTGLDPQARAEVWRTVKQLAD-GGTTVLLTTQYLDEAEQLADRIAILHEGRIIQNGTLAEL 211
Cdd:TIGR04521 166 LDEPTAGLDPKGRKEILDLFKRLHKeKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREV 230
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
10-211 |
7.92e-26 |
|
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: 105.23 E-value: 7.92e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 10 VLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGHDVAA-AAGRVRESISLTGQ----FAAvdevlT 84
Cdd:COG4988 352 ALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDlDPASWRRQIAWVPQnpylFAG-----T 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 85 GRENLVLVArlrhlpdPGAVADDM---LARFSLTD------AG-----GRRAGEYSGGMRRRLDIAMSLVGDPPVIFLDE 150
Cdd:COG4988 427 IRENLRLGR-------PDASDEELeaaLEAAGLDEfvaalpDGldtplGEGGRGLSGGQAQRLALARALLRDAPLLLLDE 499
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2794531883 151 PTTGLDPQARAEVWRTVKQLAdGGTTVLLTTQYLDEAEQlADRIAILHEGRIIQNGTLAEL 211
Cdd:COG4988 500 PTAHLDAETEAEILQALRRLA-KGRTVILITHRLALLAQ-ADRILVLDDGRIVEQGTHEEL 558
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
3-207 |
1.79e-25 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 100.09 E-value: 1.79e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 3 KSYGELDVLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGH------DVAAAAGR-VRESISLTGQ 75
Cdd:PRK11124 10 CFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNhfdfskTPSDKAIReLRRNVGMVFQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 76 FAAVDEVLTGRENLVLV-ARLRHLPDPGAV--ADDMLARFSLTDAGGRRAGEYSGGMRRRLDIAMSLVGDPPVIFLDEPT 152
Cdd:PRK11124 90 QYNLWPHLTVQQNLIEApCRVLGLSKDQALarAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPT 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2794531883 153 TGLDPQARAEVWRTVKQLADGGTTVLLTTQYLDEAEQLADRIAILHEGRIIQNGT 207
Cdd:PRK11124 170 AALDPEITAQIVSIIRELAETGITQVIVTHEVEVARKTASRVVYMENGHIVEQGD 224
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
1-211 |
2.59e-25 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 100.43 E-value: 2.59e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 1 MRKSYGELDVLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGHDVAAAAGR--------------V 66
Cdd:PRK10619 11 LHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKdgqlkvadknqlrlL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 67 RESISLTGQFAAVDEVLTGRENlVLVARLRHLPDPGAVADDMlARFSLTDAG--GRRAGEY----SGGMRRRLDIAMSLV 140
Cdd:PRK10619 91 RTRLTMVFQHFNLWSHMTVLEN-VMEAPIQVLGLSKQEARER-AVKYLAKVGidERAQGKYpvhlSGGQQQRVSIARALA 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2794531883 141 GDPPVIFLDEPTTGLDPQARAEVWRTVKQLADGGTTVLLTTQYLDEAEQLADRIAILHEGRIIQNGTLAEL 211
Cdd:PRK10619 169 MEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQL 239
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1-211 |
3.08e-25 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 99.58 E-value: 3.08e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 1 MRKSYGELDVLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGHDVAAAA--GRVRESISLTGQFAA 78
Cdd:PRK10895 9 LAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPlhARARRGIGYLPQEAS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 79 VDEVLTGRENLVLVARLRH---LPDPGAVADDMLARFSLTDAGGRRAGEYSGGMRRRLDIAMSLVGDPPVIFLDEPTTGL 155
Cdd:PRK10895 89 IFRRLSVYDNLMAVLQIRDdlsAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGV 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2794531883 156 DPQARAEVWRTVKQLADGGTTVLLTTQYLDEAEQLADRIAILHEGRIIQNGTLAEL 211
Cdd:PRK10895 169 DPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEI 224
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
11-214 |
3.22e-25 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 100.47 E-value: 3.22e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 11 LRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGHDVA-AAAGRVRESISLT-----GQF--AAV-DE 81
Cdd:PRK13635 23 LKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSeETVWDVRRQVGMVfqnpdNQFvgATVqDD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 82 VLTGRENlvlvarlRHLPDPGAV--ADDMLARFSLTDAGGRRAGEYSGGMRRRLDIAMSLVGDPPVIFLDEPTTGLDPQA 159
Cdd:PRK13635 103 VAFGLEN-------IGVPREEMVerVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRG 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2794531883 160 RAEVWRTVKQLAD-GGTTVLLTTQYLDEAEQlADRIAILHEGRIIQNGTLAELKRL 214
Cdd:PRK13635 176 RREVLETVRQLKEqKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEIFKS 230
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
18-206 |
3.27e-25 |
|
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: 98.91 E-value: 3.27e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 18 VAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGHDVAAAAGRV-----RESISLTGQFAAVDEVLTGRENLVLV 92
Cdd:cd03297 20 DLNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRKKInlppqQRKIGLVFQQYALFPHLNVRENLAFG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 93 ARlRHLPDPGAV-ADDMLARFSLTDAGGRRAGEYSGGMRRRLDIAMSLVGDPPVIFLDEPTTGLDPQARAEVWRTVKQL- 170
Cdd:cd03297 100 LK-RKRNREDRIsVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELKQIk 178
|
170 180 190
....*....|....*....|....*....|....*.
gi 2794531883 171 ADGGTTVLLTTQYLDEAEQLADRIAILHEGRIIQNG 206
Cdd:cd03297 179 KNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
2-206 |
4.27e-25 |
|
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: 98.33 E-value: 4.27e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 2 RKSYGELDVlrGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGHDVAAAAGRVReSISLTGQFAAVDE 81
Cdd:cd03298 7 RFSYGEQPM--HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADR-PVSMLFQENNLFA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 82 VLTGREN--LVLVARLRHLPDPGAVADDMLARFSLTDAGGRRAGEYSGGMRRRLDIAMSLVGDPPVIFLDEPTTGLDPQA 159
Cdd:cd03298 84 HLTVEQNvgLGLSPGLKLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPAL 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2794531883 160 RAEVWRTVKQL-ADGGTTVLLTTQYLDEAEQLADRIAILHEGRIIQNG 206
Cdd:cd03298 164 RAEMLDLVLDLhAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
2-210 |
8.10e-25 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 98.62 E-value: 8.10e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 2 RKSYGELDVLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQghdvaaaaGRVRESISLTGQFaavDE 81
Cdd:COG1134 33 RTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVN--------GRVSALLELGAGF---HP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 82 VLTGRENLVLVARLRHLP--DPGAVADDMLArFS-LTDAGGRRAGEYSGGMRRRLDIAMSLVGDPPVIFLDEPT-TGlDP 157
Cdd:COG1134 102 ELTGRENIYLNGRLLGLSrkEIDEKFDEIVE-FAeLGDFIDQPVKTYSSGMRARLAFAVATAVDPDILLVDEVLaVG-DA 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2794531883 158 --QARAEvwRTVKQLADGGTTVLLTTQYLDEAEQLADRIAILHEGRIIQNGTLAE 210
Cdd:COG1134 180 afQKKCL--ARIRELRESGRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPEE 232
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
6-190 |
8.92e-25 |
|
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: 97.43 E-value: 8.92e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 6 GELDVLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGHDVAAAAGRVRESISLTGQFAAVDEVLTG 85
Cdd:TIGR01189 11 GERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYLGHLPGLKPELSA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 86 RENLVLVARLrhLPDPGAVADDMLARFSLTDAGGRRAGEYSGGMRRRLDIAMSLVGDPPVIFLDEPTTGLDPQARAEVWR 165
Cdd:TIGR01189 91 LENLHFWAAI--HGGAQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVALLAG 168
|
170 180
....*....|....*....|....*...
gi 2794531883 166 TVKQ-LADGGTTVLLTTQYL--DEAEQL 190
Cdd:TIGR01189 169 LLRAhLARGGIVLLTTHQDLglVEAREL 196
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
5-211 |
8.93e-25 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 98.41 E-value: 8.93e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 5 YGELDVLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGHDVA--AAAGRVRESISLTGQFAAVDEV 82
Cdd:PRK11614 15 YGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITdwQTAKIMREAVAIVPEGRRVFSR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 83 LTGRENLVL---VARLRHLPDPGAVADDMLARfsLTDAGGRRAGEYSGGMRRRLDIAMSLVGDPPVIFLDEPTTGLDPQA 159
Cdd:PRK11614 95 MTVEENLAMggfFAERDQFQERIKWVYELFPR--LHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPII 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2794531883 160 RAEVWRTVKQLADGGTTVLLTTQYLDEAEQLADRIAILHEGRIIQNGTLAEL 211
Cdd:PRK11614 173 IQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHVVLEDTGDAL 224
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
2-206 |
1.01e-24 |
|
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: 97.60 E-value: 1.01e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 2 RKSYGELDVLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQghdvaaaaGRVRESISLTGQFaavDE 81
Cdd:cd03220 29 KGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVR--------GRVSSLLGLGGGF---NP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 82 VLTGRENLVLVARLRHL--PDPGAVADDMLArFS-LTDAGGRRAGEYSGGMRRRLDIAMSLVGDPPVIFLDEPTTGLDPQ 158
Cdd:cd03220 98 ELTGRENIYLNGRLLGLsrKEIDEKIDEIIE-FSeLGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAA 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2794531883 159 ARAEVWRTVKQLADGGTTVLLTTQYLDEAEQLADRIAILHEGRIIQNG 206
Cdd:cd03220 177 FQEKCQRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
4-211 |
3.00e-24 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 101.01 E-value: 3.00e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 4 SY-GELDVLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGHDVAA-AAGRVRESISLTGQ----FA 77
Cdd:COG1132 348 SYpGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDlTLESLRRQIGVVPQdtflFS 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 78 AvdevlTGRENLVL------------VARLrhlpdpgAVADDMLARFsltDAG-----GRRAGEYSGGMRRRLDIAMSLV 140
Cdd:COG1132 428 G-----TIRENIRYgrpdatdeeveeAAKA-------AQAHEFIEAL---PDGydtvvGERGVNLSGGQRQRIAIARALL 492
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2794531883 141 GDPPVIFLDEPTTGLDPQARAEVWRTVKQLADGGTTVL----LTTQyldeaeQLADRIAILHEGRIIQNGTLAEL 211
Cdd:COG1132 493 KDPPILILDEATSALDTETEALIQEALERLMKGRTTIViahrLSTI------RNADRILVLDDGRIVEQGTHEEL 561
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
1-211 |
4.19e-24 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 96.79 E-value: 4.19e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 1 MRKSYGELDVLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGHDVAAAAGRvresislTGQFAAVD 80
Cdd:COG4598 14 LHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIRLKPDR-------DGELVPAD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 81 E------------V---------LTGRENLVLV-ARLRHLPDPGAV--ADDMLARFSLTDAGGRRAGEYSGGMRRRLDIA 136
Cdd:COG4598 87 RrqlqrirtrlgmVfqsfnlwshMTVLENVIEApVHVLGRPKAEAIerAEALLAKVGLADKRDAYPAHLSGGQQQRAAIA 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2794531883 137 MSLVGDPPVIFLDEPTTGLDPQARAEVWRTVKQLADGGTTVLLTTQYLDEAEQLADRIAILHEGRIIQNGTLAEL 211
Cdd:COG4598 167 RALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEEGRTMLVVTHEMGFARDVSSHVVFLHQGRIEEQGPPAEV 241
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
1-210 |
5.10e-24 |
|
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: 96.25 E-value: 5.10e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 1 MRKSYGELdVLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGHDVAAAAGRVREsISLTGQFAAVD 80
Cdd:cd03299 6 LSKDWKEF-KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEKRD-ISYVPQNYALF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 81 EVLTGRENLVLVARLRHLPDP--GAVADDMLARFSLTDAGGRRAGEYSGGMRRRLDIAMSLVGDPPVIFLDEPTTGLDPQ 158
Cdd:cd03299 84 PHMTVYKNIAYGLKKRKVDKKeiERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVR 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2794531883 159 ARAEVWRTVKQLAD-GGTTVLLTTQYLDEAEQLADRIAILHEGRIIQNGTLAE 210
Cdd:cd03299 164 TKEKLREELKKIRKeFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEE 216
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
6-207 |
6.03e-24 |
|
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: 95.96 E-value: 6.03e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 6 GELDVLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGHDVAA------AAGRvRESISLTGQ-FAA 78
Cdd:COG4181 23 GELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFAldedarARLR-ARHVGFVFQsFQL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 79 VDEvLTGRENLVLVARLRHLPDPGAVADDMLARFSLtdagGRRAGEY----SGGMRRRLDIAMSLVGDPPVIFLDEPTTG 154
Cdd:COG4181 102 LPT-LTALENVMLPLELAGRRDARARARALLERVGL----GHRLDHYpaqlSGGEQQRVALARAFATEPAILFADEPTGN 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2794531883 155 LDPQARAEVWRTVKQL-ADGGTTVLLTTQyldeAEQLA---DRIAILHEGRIIQNGT 207
Cdd:COG4181 177 LDAATGEQIIDLLFELnRERGTTLVLVTH----DPALAarcDRVLRLRAGRLVEDTA 229
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
4-206 |
6.41e-24 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 94.30 E-value: 6.41e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 4 SYGELD--VLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGHDVAAAAGRVRESISLTGQ----FA 77
Cdd:cd03247 9 SYPEQEqqVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSLISVLNQrpylFD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 78 AvdevlTGRENLvlvarlrhlpdpgavaddmlarfsltdagGRRageYSGGMRRRLDIAMSLVGDPPVIFLDEPTTGLDP 157
Cdd:cd03247 89 T-----TLRNNL-----------------------------GRR---FSGGERQRLALARILLQDAPIVLLDEPTVGLDP 131
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2794531883 158 QARAEVWRTVKQLADgGTTVLLTTQYLDEAEQlADRIAILHEGRIIQNG 206
Cdd:cd03247 132 ITERQLLSLIFEVLK-DKTLIWITHHLTGIEH-MDKILFLENGKIIMQG 178
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
5-239 |
6.61e-24 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 100.20 E-value: 6.61e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 5 YGELDVLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGHDVAAAagRVRESIS------------- 71
Cdd:NF033858 11 YGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMADA--RHRRAVCpriaympqglgkn 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 72 --LTgqfaavdevLTGRENLVLVARL-------RHlpdpgAVADDMLARFSLTDAGGRRAGEYSGGMRRRLDIAMSLVGD 142
Cdd:NF033858 89 lyPT---------LSVFENLDFFGRLfgqdaaeRR-----RRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCALIHD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 143 PPVIFLDEPTTGLDPQARAEVWRTVKQL--ADGGTTVLLTTQYLDEAEQLaDRIAILHEGRIIQNGTLAELKRLLPSAtv 220
Cdd:NF033858 155 PDLLILDEPTTGVDPLSRRQFWELIDRIraERPGMSVLVATAYMEEAERF-DWLVAMDAGRVLATGTPAELLARTGAD-- 231
|
250
....*....|....*....
gi 2794531883 221 eyvekqpTLEEVFLAVVGE 239
Cdd:NF033858 232 -------TLEAAFIALLPE 243
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
6-181 |
7.75e-24 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 94.94 E-value: 7.75e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 6 GELDVLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGHDvaAAAGRVRESISLTGQFAAVDEVLTG 85
Cdd:PRK13539 13 GGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGD--IDDPDVAEACHYLGHRNAMKPALTV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 86 RENLVLVARLRHLPDPGAvaDDMLARFSLTDAGGRRAGEYSGGMRRRLDIAMSLVGDPPVIFLDEPTTGLDPQARAEVWR 165
Cdd:PRK13539 91 AENLEFWAAFLGGEELDI--AAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVALFAE 168
|
170
....*....|....*.
gi 2794531883 166 TVKQLADGGTTVLLTT 181
Cdd:PRK13539 169 LIRAHLAQGGIVIAAT 184
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
2-219 |
1.57e-23 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 97.07 E-value: 1.57e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 2 RKSY----GELDVLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGHDVAAAAGR----VRESISLT 73
Cdd:COG1135 8 SKTFptkgGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERelraARRKIGMI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 74 GQ-FAavdevL----TGRENlvlVAR-LRHLPDPGAV----ADDMLARFSLTDAGGRRAGEYSGGMRRRLDIAMSLVGDP 143
Cdd:COG1135 88 FQhFN-----LlssrTVAEN---VALpLEIAGVPKAEirkrVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 144 PVIFLDEPTTGLDPQARAEVWRTVKQL-ADGGTTVLLTTQYLDEAEQLADRIAILHEGRIIQNGTLAEL---------KR 213
Cdd:COG1135 160 KVLLCDEATSALDPETTRSILDLLKDInRELGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVLDVfanpqseltRR 239
|
....*.
gi 2794531883 214 LLPSAT 219
Cdd:COG1135 240 FLPTVL 245
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-211 |
1.91e-23 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 95.20 E-value: 1.91e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 1 MRKSYGELDVLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGHDVAAA----------------AG 64
Cdd:PRK11264 9 LVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTArslsqqkglirqlrqhVG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 65 RVRESISLTGQFAAVDEVLTGRenlVLVARLRHlPDPGAVADDMLARFSLT---DAGGRRageYSGGMRRRLDIAMSLVG 141
Cdd:PRK11264 89 FVFQNFNLFPHRTVLENIIEGP---VIVKGEPK-EEATARARELLAKVGLAgkeTSYPRR---LSGGQQQRVAIARALAM 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 142 DPPVIFLDEPTTGLDPQARAEVWRTVKQLADGGTTVLLTTQYLDEAEQLADRIAILHEGRIIQNGTLAEL 211
Cdd:PRK11264 162 RPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKAL 231
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
11-224 |
1.93e-23 |
|
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: 94.45 E-value: 1.93e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 11 LRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGHDVAAAaGRVRESISltgQFAAVDEVLTGRENLV 90
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEP-GPDRMVVF---QNYSLLPWLTVRENIA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 91 LV--ARLRHLPDPG--AVADDMLARFSLTDAGGRRAGEYSGGMRRRLDIAMSLVGDPPVIFLDEPTTGLDPQARAEVWRT 166
Cdd:TIGR01184 77 LAvdRVLPDLSKSErrAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2794531883 167 VKQLA-DGGTTVLLTTQYLDEAEQLADRIAILHEGRIIQNGTLAELKRLLPSATVEYVE 224
Cdd:TIGR01184 157 LMQIWeEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAANIGQILEVPFPRPRDRLEVVE 215
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1-205 |
2.85e-23 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 98.26 E-value: 2.85e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 1 MRKSY----GELDVLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGHDVA-----AAAGRVRESIS 71
Cdd:PRK10535 10 IRRSYpsgeEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVAtldadALAQLRREHFG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 72 LTGQFAAVDEVLTGRENLVLVARLRHLPDPG--AVADDMLARFSLTDAGGRRAGEYSGGMRRRLDIAMSLVGDPPVIFLD 149
Cdd:PRK10535 90 FIFQRYHLLSHLTAAQNVEVPAVYAGLERKQrlLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILAD 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2794531883 150 EPTTGLDPQARAEVWRTVKQLADGGTTVLLTTQYLDEAEQlADRIAILHEGRIIQN 205
Cdd:PRK10535 170 EPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHDPQVAAQ-AERVIEIRDGEIVRN 224
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
6-194 |
4.08e-23 |
|
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: 92.94 E-value: 4.08e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 6 GELDVLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGHDVAAAAGRVRESISLTGQFAAVDEVLTG 85
Cdd:cd03231 11 DGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTLSV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 86 RENLvlvaRLRHLPDPGAVADDMLARFSLTDAGGRRAGEYSGGMRRRLDIAMSLVGDPPVIFLDEPTTGLDPQARAEVWR 165
Cdd:cd03231 91 LENL----RFWHADHSDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAE 166
|
170 180 190
....*....|....*....|....*....|
gi 2794531883 166 TVKQLADGGTTVLLTT-QYLDEAEQLADRI 194
Cdd:cd03231 167 AMAGHCARGGMVVLTThQDLGLSEAGAREL 196
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-211 |
4.13e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 94.21 E-value: 4.13e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 1 MRKSYGELDVLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVR-----ADAGTASVQGHDV-AAAAGRVRESISLTG 74
Cdd:PRK14247 9 LKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElypeaRVSGEVYLDGQDIfKMDVIELRRRVQMVF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 75 QFAAVDEVLTGRENLVLVARLRHLPDPGAVADDMLaRFSLTDAG---------GRRAGEYSGGMRRRLDIAMSLVGDPPV 145
Cdd:PRK14247 89 QIPNPIPNLSIFENVALGLKLNRLVKSKKELQERV-RWALEKAQlwdevkdrlDAPAGKLSGGQQQRLCIARALAFQPEV 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2794531883 146 IFLDEPTTGLDPQARAEVWRTVKQLADgGTTVLLTTQYLDEAEQLADRIAILHEGRIIQNGTLAEL 211
Cdd:PRK14247 168 LLADEPTANLDPENTAKIESLFLELKK-DMTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREV 232
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1-212 |
5.07e-23 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 93.90 E-value: 5.07e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 1 MRksYGELDVLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGHDVAAAAGR--VRESISLTGQFAA 78
Cdd:PRK11300 13 MR--FGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHqiARMGVVRTFQHVR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 79 VDEVLTGRENLvLVARLRHL---------PDPG---AVADDM------LARFSLTDAGGRRAGEYSGGMRRRLDIAMSLV 140
Cdd:PRK11300 91 LFREMTVIENL-LVAQHQQLktglfsgllKTPAfrrAESEALdraatwLERVGLLEHANRQAGNLAYGQQRRLEIARCMV 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2794531883 141 GDPPVIFLDEPTTGLDPQARAEVWRTVKQLADG-GTTVLLTTQYLDEAEQLADRIAILHEGRIIQNGTLAELK 212
Cdd:PRK11300 170 TQPEILMLDEPAAGLNPKETKELDELIAELRNEhNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEIR 242
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
3-215 |
5.81e-23 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 97.16 E-value: 5.81e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 3 KSYGELDVLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGHD-------VAAAAGrvresISLTGQ 75
Cdd:PRK09700 13 KSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINynkldhkLAAQLG-----IGIIYQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 76 FAAVDEVLTGRENLvLVARLRHLPDPG----------AVADDMLARFSLTDAGGRRAGEYSGGMRRRLDIAMSLVGDPPV 145
Cdd:PRK09700 88 ELSVIDELTVLENL-YIGRHLTKKVCGvniidwremrVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKV 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2794531883 146 IFLDEPTTGLDPQARAEVWRTVKQLADGGTTVLLTTQYLDEAEQLADRIAILHEG-----RIIQNGTLAELKRLL 215
Cdd:PRK09700 167 IIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGssvcsGMVSDVSNDDIVRLM 241
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
3-213 |
6.93e-23 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 95.54 E-value: 6.93e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 3 KSYGELDVLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGHDVAAAAGRVREsISLTGQFAAVDEV 82
Cdd:PRK10851 10 KSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDRK-VGFVFQHYALFRH 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 83 LTGRENL-----VLVARLRhlPDPGAV---ADDMLARFSLTDAGGRRAGEYSGGMRRRLDIAMSLVGDPPVIFLDEPTTG 154
Cdd:PRK10851 89 MTVFDNIafgltVLPRRER--PNAAAIkakVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2794531883 155 LDPQARAEVWRTVKQLAD--GGTTVLLTTQYlDEAEQLADRIAILHEGRIIQNGTLAELKR 213
Cdd:PRK10851 167 LDAQVRKELRRWLRQLHEelKFTSVFVTHDQ-EEAMEVADRVVVMSQGNIEQAGTPDQVWR 226
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
10-204 |
7.06e-23 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 93.77 E-value: 7.06e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 10 VLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGHDVAA-AAGRvresiSLTGQFAAVDEVLTGREN 88
Cdd:COG4525 22 ALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGpGADR-----GVVFQKDALLPWLNVLDN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 89 LVLVARLRHLPDPG--AVADDMLARFSLTDAGGRRAGEYSGGMRRRLDIAMSLVGDPPVIFLDEPTTGLDPQARAEVWRT 166
Cdd:COG4525 97 VAFGLRLRGVPKAErrARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLLMDEPFGALDALTREQMQEL 176
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2794531883 167 VKQL-ADGGTTVLLTTQYLDEAEQLADRIAIL--HEGRIIQ 204
Cdd:COG4525 177 LLDVwQRTGKGVFLITHSVEEALFLATRLVVMspGPGRIVE 217
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
9-211 |
1.06e-22 |
|
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: 92.93 E-value: 1.06e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 9 DVLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGHDVAAAAgrvreSISLTGQFAAVDEvltgrEN 88
Cdd:cd03252 16 VILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALAD-----PAWLRRQVGVVLQ-----EN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 89 LVLVARLRH---LPDPGAVADDMLARFSLTDAG--------------GRRAGEYSGGMRRRLDIAMSLVGDPPVIFLDEP 151
Cdd:cd03252 86 VLFNRSIRDniaLADPGMSMERVIEAAKLAGAHdfiselpegydtivGEQGAGLSGGQRQRIAIARALIHNPRILIFDEA 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 152 TTGLDPQARAEVWRTVKQLADGGTTVLLTTQYldEAEQLADRIAILHEGRIIQNGTLAEL 211
Cdd:cd03252 166 TSALDYESEHAIMRNMHDICAGRTVIIIAHRL--STVKNADRIIVMEKGRIVEQGSHDEL 223
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
6-211 |
1.20e-22 |
|
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: 93.33 E-value: 1.20e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 6 GELDVLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGHDVA----AAAGRVRESISLTGQ--FAAV 79
Cdd:TIGR02769 22 QRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYqldrKQRRAFRRDVQLVFQdsPSAV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 80 DEVLTGREnlVLVARLRHLPDPGAVAD-----DMLARFSL-TDAGGRRAGEYSGGMRRRLDIAMSLVGDPPVIFLDEPTT 153
Cdd:TIGR02769 102 NPRMTVRQ--IIGEPLRHLTSLDESEQkariaELLDMVGLrSEDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVS 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2794531883 154 GLDPQARAEVWRTVKQL-ADGGTTVLLTTQYLDEAEQLADRIAILHEGRIIQNGTLAEL 211
Cdd:TIGR02769 180 NLDMVLQAVILELLRKLqQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIVEECDVAQL 238
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
14-211 |
2.00e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 93.26 E-value: 2.00e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 14 VDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGHDVAAAAGR-----VRESISLTGQF--------AAVD 80
Cdd:PRK13643 25 IDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQkeikpVRKKVGVVFQFpesqlfeeTVLK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 81 EVLTGRENLVLVARlrhlpDPGAVADDMLARFSLTDAGGRRAG-EYSGGMRRRLDIAMSLVGDPPVIFLDEPTTGLDPQA 159
Cdd:PRK13643 105 DVAFGPQNFGIPKE-----KAEKIAAEKLEMVGLADEFWEKSPfELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKA 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2794531883 160 RAEVWRTVKQLADGGTTVLLTTQYLDEAEQLADRIAILHEGRIIQNGTLAEL 211
Cdd:PRK13643 180 RIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDV 231
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
6-187 |
4.16e-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: 90.17 E-value: 4.16e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 6 GELDVLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGHDVAAAAG---RVRESISLTGQ------F 76
Cdd:TIGR01166 3 GGPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPLDYSRKgllERRQRVGLVFQdpddqlF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 77 AA-VDE-VLTGRENLVLV-ARLRhlpdpgAVADDMLARFSLTDAGGRRAGEYSGGMRRRLDIAMSLVGDPPVIFLDEPTT 153
Cdd:TIGR01166 83 AAdVDQdVAFGPLNLGLSeAEVE------RRVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTA 156
|
170 180 190
....*....|....*....|....*....|....
gi 2794531883 154 GLDPQARAEVWRTVKQLADGGTTVLLTTQYLDEA 187
Cdd:TIGR01166 157 GLDPAGREQMLAILRRLRAEGMTVVISTHDVDLA 190
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
9-213 |
4.34e-22 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 94.31 E-value: 4.34e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 9 DVLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGHDV-------AAAAG-------RVRESISLTg 74
Cdd:COG1129 266 GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVrirsprdAIRAGiayvpedRKGEGLVLD- 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 75 qfaavdevLTGRENLVLvARLRHLPDPG--------AVADDMLARFSL-TDAGGRRAGEYSGGMRRRLDIAMSLVGDPPV 145
Cdd:COG1129 345 --------LSIRENITL-ASLDRLSRGGlldrrrerALAEEYIKRLRIkTPSPEQPVGNLSGGNQQKVVLAKWLATDPKV 415
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2794531883 146 IFLDEPTTGLDPQARAEVWRTVKQLADGGTTVLLTTQYLDEAEQLADRIAILHEGRIIqngtlAELKR 213
Cdd:COG1129 416 LILDEPTRGIDVGAKAEIYRLIRELAAEGKAVIVISSELPELLGLSDRILVMREGRIV-----GELDR 478
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
6-180 |
4.94e-22 |
|
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: 90.00 E-value: 4.94e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 6 GELDVLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTlvRADAGTasVQGhDVAAAAGRVRESIS-LTG---QFAAVDE 81
Cdd:cd03232 18 GKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAG--RKTAGV--ITG-EILINGRPLDKNFQrSTGyveQQDVHSP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 82 VLTGRENLVLVARLRHLpdpgavaddmlarfSLTDaggrrageysggmRRRLDIAMSLVGDPPVIFLDEPTTGLDPQARA 161
Cdd:cd03232 93 NLTVREALRFSALLRGL--------------SVEQ-------------RKRLTIGVELAAKPSILFLDEPTSGLDSQAAY 145
|
170
....*....|....*....
gi 2794531883 162 EVWRTVKQLADGGTTVLLT 180
Cdd:cd03232 146 NIVRFLKKLADSGQAILCT 164
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
10-211 |
5.01e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 91.69 E-value: 5.01e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 10 VLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGHD---------VAAAAGRVRESISltGQFAA-- 78
Cdd:PRK13633 25 ALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDtsdeenlwdIRNKAGMVFQNPD--NQIVAti 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 79 VDE-VLTGRENLVLVA---RLRhlpdpgavADDMLARFSLTDAggRRAGEY--SGGMRRRLDIAMSLVGDPPVIFLDEPT 152
Cdd:PRK13633 103 VEEdVAFGPENLGIPPeeiRER--------VDESLKKVGMYEY--RRHAPHllSGGQKQRVAIAGILAMRPECIIFDEPT 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 153 TGLDPQARAEVWRTVKQLADG-GTTVLLTTQYLDEAEQlADRIAILHEGRIIQNGTLAEL 211
Cdd:PRK13633 173 AMLDPSGRREVVNTIKELNKKyGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEI 231
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
12-181 |
5.51e-22 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 89.86 E-value: 5.51e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 12 RGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGHDVAAAAGRVRESISLTGQFAAVDEVLTGRENLVL 91
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQDLLYLGHQPGIKTELTALENLRF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 92 VARLRHLPDPGAVAdDMLARFSLtdaGGRR---AGEYSGGMRRRLDIAMSLVGDPPVIFLDEPTTGLDPQARAEVWRTVK 168
Cdd:PRK13538 98 YQRLHGPGDDEALW-EALAQVGL---AGFEdvpVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGVARLEALLA 173
|
170
....*....|...
gi 2794531883 169 QLADGGTTVLLTT 181
Cdd:PRK13538 174 QHAEQGGMVILTT 186
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
2-211 |
1.41e-21 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 93.19 E-value: 1.41e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 2 RKSYGELDVLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGHDVAAA--AGRVRESISLTGQFAAV 79
Cdd:PRK15439 18 SKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLtpAKAHQLGIYLVPQEPLL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 80 DEVLTGRENLVLvaRLRHLPDPGAVADDMLARFSLTDAGGRRAGEYSGGMRRRLDIAMSLVGDPPVIFLDEPTTGLDPQA 159
Cdd:PRK15439 98 FPNLSVKENILF--GLPKRQASMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILILDEPTASLTPAE 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2794531883 160 RAEVWRTVKQLADGGTTVLLTTQYLDEAEQLADRIAILHEGRIIQNGTLAEL 211
Cdd:PRK15439 176 TERLFSRIRELLAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTADL 227
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
11-207 |
1.47e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 90.57 E-value: 1.47e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 11 LRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGHDVAAAA-----GRVRESISLTGQFA-------- 77
Cdd:PRK13649 23 LFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSknkdiKQIRKKVGLVFQFPesqlfeet 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 78 AVDEVLTGRENLvlvarlrhlpdpGAVADDM--LARFSLTDAG------GRRAGEYSGGMRRRLDIAMSLVGDPPVIFLD 149
Cdd:PRK13649 103 VLKDVAFGPQNF------------GVSQEEAeaLAREKLALVGiseslfEKNPFELSGGQMRRVAIAGILAMEPKILVLD 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2794531883 150 EPTTGLDPQARAEVWRTVKQLADGGTTVLLTTQYLDEAEQLADRIAILHEGRIIQNGT 207
Cdd:PRK13649 171 EPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGK 228
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
10-211 |
2.69e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 89.75 E-value: 2.69e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 10 VLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGHDV---AAAAGRVRESISLTGQ------FA-AV 79
Cdd:PRK13639 17 ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIkydKKSLLEVRKTVGIVFQnpddqlFApTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 80 DE-VLTGRENLVL----VARLrhlpdpgavADDMLARFSLTDAGGRRAGEYSGGMRRRLDIAMSLVGDPPVIFLDEPTTG 154
Cdd:PRK13639 97 EEdVAFGPLNLGLskeeVEKR---------VKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSG 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2794531883 155 LDPQARAEVWRTVKQLADGGTTVLLTTQYLDEAEQLADRIAILHEGRIIQNGTLAEL 211
Cdd:PRK13639 168 LDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEV 224
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
7-211 |
3.30e-21 |
|
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: 92.09 E-value: 3.30e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 7 ELDVLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGHDVAAAAGR-VRESISLTGQFAAV------ 79
Cdd:TIGR02203 344 DRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLAsLRRQVALVSQDVVLfndtia 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 80 DEVLTGRENLVLVARLRHlpdpgAVADDMLARF------SLTDAGGRRAGEYSGGMRRRLDIAMSLVGDPPVIFLDEPTT 153
Cdd:TIGR02203 424 NNIAYGRTEQADRAEIER-----ALAAAYAQDFvdklplGLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATS 498
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2794531883 154 GLDPQARAEVWRTVKQLADGGTTvLLTTQYLDEAEQlADRIAILHEGRIIQNGTLAEL 211
Cdd:TIGR02203 499 ALDNESERLVQAALERLMQGRTT-LVIAHRLSTIEK-ADRIVVMDDGRIVERGTHNEL 554
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
4-211 |
3.33e-21 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 91.44 E-value: 3.33e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 4 SYGELDVLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGHDVAAAAGR-VRESISLTGQFAAVDEV 82
Cdd:PRK09536 12 EFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARaASRRVASVPQDTSLSFE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 83 LTGREnLVLVARLRHL-------PDPGAVADDMLARFSLTDAGGRRAGEYSGGMRRRLDIAMSLVGDPPVIFLDEPTTGL 155
Cdd:PRK09536 92 FDVRQ-VVEMGRTPHRsrfdtwtETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASL 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2794531883 156 DPQARAEVWRTVKQLADGGTTVLLTTQYLDEAEQLADRIAILHEGRIIQNGTLAEL 211
Cdd:PRK09536 171 DINHQVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADV 226
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
10-214 |
4.36e-21 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 88.98 E-value: 4.36e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 10 VLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGHDVA----AAAGRVRESISLTGQ--FAAVDEVL 83
Cdd:PRK10419 27 VLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAklnrAQRKAFRRDIQMVFQdsISAVNPRK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 84 TGREnlVLVARLRHL-----PDPGAVADDMLARFSLTDA-GGRRAGEYSGGMRRRLDIAMSLVGDPPVIFLDEPTTGLDP 157
Cdd:PRK10419 107 TVRE--IIREPLRHLlsldkAERLARASEMLRAVDLDDSvLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDL 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2794531883 158 QARAEVWRTVKQL-ADGGTTVLLTTQYLDEAEQLADRIAILHEGRIIQNGTLAELKRL 214
Cdd:PRK10419 185 VLQAGVIRLLKKLqQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVETQPVGDKLTF 242
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
7-211 |
8.26e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 88.68 E-value: 8.26e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 7 ELDVLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGHDVAAAAG-----RVRESISLTGQFAAVD- 80
Cdd:PRK13646 19 EHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKdkyirPVRKRIGMVFQFPESQl 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 81 -------EVLTGRENLVLvarlrHLPDPGAVADDMLARFSLT-DAGGRRAGEYSGGMRRRLDIAMSLVGDPPVIFLDEPT 152
Cdd:PRK13646 99 fedtverEIIFGPKNFKM-----NLDEVKNYAHRLLMDLGFSrDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPT 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 153 TGLDPQARAEVWRTVKQLA-DGGTTVLLTTQYLDEAEQLADRIAILHEGRIIQNGTLAEL 211
Cdd:PRK13646 174 AGLDPQSKRQVMRLLKSLQtDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKEL 233
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
3-156 |
8.62e-21 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 90.89 E-value: 8.62e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 3 KSYGELDVLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGHdvaAAAGRVRESISLTGQFAAVDEV 82
Cdd:COG0488 6 KSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKG---LRIGYLPQEPPLDDDLTVLDTV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 83 LTGRENLV-LVARLRHLPDPGAVADDMLARFS-----LTDAGG----------------------RRAGEYSGGMRRRLD 134
Cdd:COG0488 83 LDGDAELRaLEAELEELEAKLAEPDEDLERLAelqeeFEALGGweaearaeeilsglgfpeedldRPVSELSGGWRRRVA 162
|
170 180
....*....|....*....|..
gi 2794531883 135 IAMSLVGDPPVIFLDEPTTGLD 156
Cdd:COG0488 163 LARALLSEPDLLLLDEPTNHLD 184
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
10-211 |
9.99e-21 |
|
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: 87.60 E-value: 9.99e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 10 VLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGHDVAAAAGR-VRESISLTGQfaavDEVL---TG 85
Cdd:cd03249 18 ILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRwLRSQIGLVSQ----EPVLfdgTI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 86 RENLVLVARLRHLPDPGAVADDMLARF---SLTDAG----GRRAGEYSGGMRRRLDIAMSLVGDPPVIFLDEPTTGLDPQ 158
Cdd:cd03249 94 AENIRYGKPDATDEEVEEAAKKANIHDfimSLPDGYdtlvGERGSQLSGGQKQRIAIARALLRNPKILLLDEATSALDAE 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2794531883 159 ARAEVWRTVKQLADGGTTV-----LLTTQYldeaeqlADRIAILHEGRIIQNGTLAEL 211
Cdd:cd03249 174 SEKLVQEALDRAMKGRTTIviahrLSTIRN-------ADLIAVLQNGQVVEQGTHDEL 224
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
10-220 |
1.24e-20 |
|
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: 90.19 E-value: 1.24e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 10 VLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGHDVAAA-------------------AGRVRESI 70
Cdd:COG4618 347 ILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWdreelgrhigylpqdvelfDGTIAENI 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 71 SltgQFAAVDevltgRENLVLVARLrhlpdpgAVADDMLARF-----SLTDAGGRRageYSGGMRRRLDIAMSLVGDPPV 145
Cdd:COG4618 427 A---RFGDAD-----PEKVVAAAKL-------AGVHEMILRLpdgydTRIGEGGAR---LSGGQRQRIGLARALYGDPRL 488
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2794531883 146 IFLDEPTTGLDPQARAEVWRTVKQLADGGTTVLLTTQYLdEAEQLADRIAILHEGRIIQNGTLAE-LKRLLPSATV 220
Cdd:COG4618 489 VVLDEPNSNLDDEGEAALAAAIRALKARGATVVVITHRP-SLLAAVDKLLVLRDGRVQAFGPRDEvLARLARPAAA 563
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
6-180 |
1.25e-20 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 90.55 E-value: 1.25e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 6 GELDVLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRA---DAGTASVQGHDVAAAAGRvreSISLTGQFAAVDEV 82
Cdd:TIGR00956 774 EKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVTTgviTGGDRLVNGRPLDSSFQR---SIGYVQQQDLHLPT 850
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 83 LTGRENLVLVARLRHlpdPGAVAD-----------DMLARFSLTDAGGRRAGEysgGM----RRRLDIAMSLVGDPP-VI 146
Cdd:TIGR00956 851 STVRESLRFSAYLRQ---PKSVSKsekmeyveeviKLLEMESYADAVVGVPGE---GLnveqRKRLTIGVELVAKPKlLL 924
|
170 180 190
....*....|....*....|....*....|....
gi 2794531883 147 FLDEPTTGLDPQARAEVWRTVKQLADGGTTVLLT 180
Cdd:TIGR00956 925 FLDEPTSGLDSQTAWSICKLMRKLADHGQAILCT 958
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
11-234 |
1.37e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 87.87 E-value: 1.37e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 11 LRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGHDVAAAAGR-VRESISLTGQ------FAAV--DE 81
Cdd:PRK13647 21 LKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKwVRSKVGLVFQdpddqvFSSTvwDD 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 82 VLTGRENLVLvarlrhlpDPGAV---ADDMLARFSLTDAGGRRAGEYSGGMRRRLDIAMSLVGDPPVIFLDEPTTGLDPQ 158
Cdd:PRK13647 101 VAFGPVNMGL--------DKDEVerrVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPR 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2794531883 159 ARAEVWRTVKQLADGGTTVLLTTQYLDEAEQLADRIAILHEGRIIQNGTLAEL--KRLLPSATVEYvekqPTLEEVFL 234
Cdd:PRK13647 173 GQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKSLLtdEDIVEQAGLRL----PLVAQIFE 246
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
10-211 |
1.65e-20 |
|
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: 86.90 E-value: 1.65e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 10 VLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGHDVAA-AAGRVRESISLTGQ------------- 75
Cdd:cd03251 17 VLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDyTLASLRRQIGLVSQdvflfndtvaeni 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 76 -FAAVDEvltGRENLVLVARLRHlpdpgavADDMLARFsltDAG-----GRRAGEYSGGMRRRLDIAMSLVGDPPVIFLD 149
Cdd:cd03251 97 aYGRPGA---TREEVEEAARAAN-------AHEFIMEL---PEGydtviGERGVKLSGGQRQRIAIARALLKDPPILILD 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2794531883 150 EPTTGLDPQARAEVWRTVKQLADGGTTvLLTTQYLDEAEQlADRIAILHEGRIIQNGTLAEL 211
Cdd:cd03251 164 EATSALDTESERLVQAALERLMKNRTT-FVIAHRLSTIEN-ADRIVVLEDGKIVERGTHEEL 223
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
3-212 |
1.72e-20 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 89.68 E-value: 1.72e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 3 KSYGELDVLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGHDVA---------AAAGRVRESISLT 73
Cdd:PRK10762 12 KAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTfngpkssqeAGIGIIHQELNLI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 74 GQFAAVDEVLTGRENLVLVARLRHlPDPGAVADDMLARFSLTDAGGRRAGEYSGGMRRRLDIAMSLVGDPPVIFLDEPTT 153
Cdd:PRK10762 92 PQLTIAENIFLGREFVNRFGRIDW-KKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTD 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2794531883 154 GLDPQARAEVWRTVKQLADGGTTVLLTTQYLDEAEQLADRIAILHEGRIIQNGTLAELK 212
Cdd:PRK10762 171 ALTDTETESLFRVIRELKSQGRGIVYISHRLKEIFEICDDVTVFRDGQFIAEREVADLT 229
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1-207 |
1.85e-20 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 87.38 E-value: 1.85e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 1 MRKSYGELDVLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTAS---VQGHDVAAA---AGRVRESISLTG 74
Cdd:PRK09984 10 LAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSAGShieLLGRTVQREgrlARDIRKSRANTG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 75 ----QFAAVDEvLTGRENlVLVARLRHLP-----------DPGAVADDMLARFSLTDAGGRRAGEYSGGMRRRLDIAMSL 139
Cdd:PRK09984 90 yifqQFNLVNR-LSVLEN-VLIGALGSTPfwrtcfswftrEQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAIARAL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2794531883 140 VGDPPVIFLDEPTTGLDPQARAEVWRTVKQL-ADGGTTVLLTTQYLDEAEQLADRIAILHEGRIIQNGT 207
Cdd:PRK09984 168 MQQAKVILADEPIASLDPESARIVMDTLRDInQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGS 236
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
6-214 |
1.96e-20 |
|
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: 85.66 E-value: 1.96e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 6 GELDVLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTL--VRADAGTASVQGHDVAAAA--GRVRESISLTGQFAAvdE 81
Cdd:cd03217 11 GGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLPpeERARLGIFLAFQYPP--E 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 82 VltgrenlvlvarlrhlpdPGAVADDMLaRFslTDAGgrrageYSGGMRRRLDIAMSLVGDPPVIFLDEPTTGLDPQARA 161
Cdd:cd03217 89 I------------------PGVKNADFL-RY--VNEG------FSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALR 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2794531883 162 EVWRTVKQLADGGTTVLLTTQYLDEAEQL-ADRIAILHEGRIIQNGTLAELKRL 214
Cdd:cd03217 142 LVAEVINKLREEGKSVLIITHYQRLLDYIkPDRVHVLYDGRIVKSGDKELALEI 195
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
13-211 |
1.99e-20 |
|
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: 86.65 E-value: 1.99e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 13 GVDLGVAPGTIHALLGSNGAGKTT----LVKILSTLVRADAGTASVQGHDVAAAAGRVRE-SISLTGQFAAVDEVLTGRE 87
Cdd:TIGR02770 4 DLNLSLKRGEVLALVGESGSGKSLtclaILGLLPPGLTQTSGEILLDGRPLLPLSIRGRHiATIMQNPRTAFNPLFTMGN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 88 NLVLVARLRHLP--DPGAVADDMLARFSLTDAG---GRRAGEYSGGMRRRLDIAMSLVGDPPVIFLDEPTTGLDPQARAE 162
Cdd:TIGR02770 84 HAIETLRSLGKLskQARALILEALEAVGLPDPEevlKKYPFQLSGGMLQRVMIALALLLEPPFLIADEPTTDLDVVNQAR 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2794531883 163 VWRTVKQL-ADGGTTVLLTTQYLDEAEQLADRIAILHEGRIIQNGTLAEL 211
Cdd:TIGR02770 164 VLKLLRELrQLFGTGILLITHDLGVVARIADEVAVMDDGRIVERGTVKEI 213
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
5-211 |
3.08e-20 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 86.98 E-value: 3.08e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 5 YGELDVLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGHDVAAAAgrvRESISLTGQFAAV----- 79
Cdd:PRK13638 11 YQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSK---RGLLALRQQVATVfqdpe 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 80 DEVLTGRENLVLVARLRHLpdpgAVADDMLAR-----FSLTDAGGRRAGE---YSGGMRRRLDIAMSLVGDPPVIFLDEP 151
Cdd:PRK13638 88 QQIFYTDIDSDIAFSLRNL----GVPEAEITRrvdeaLTLVDAQHFRHQPiqcLSHGQKKRVAIAGALVLQARYLLLDEP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 152 TTGLDPQARAEVWRTVKQLADGGTTVLLTTQYLDEAEQLADRIAILHEGRIIQNGTLAEL 211
Cdd:PRK13638 164 TAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEV 223
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
2-207 |
3.79e-20 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 88.08 E-value: 3.79e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 2 RKSYGELDVLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGHDVAAAAGRVREsISLTGQFAAVDE 81
Cdd:PRK09452 21 SKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAENRH-VNTVFQSYALFP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 82 VLTGRENLVLVARLRHLPDP--GAVADDMLARFSLTDAGGRRAGEYSGGMRRRLDIAMSLVGDPPVIFLDEPTTGLDPQA 159
Cdd:PRK09452 100 HMTVFENVAFGLRMQKTPAAeiTPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALDYKL 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2794531883 160 RAEVWRTVKQLADG-GTTVLLTTQYLDEAEQLADRIAILHEGRIIQNGT 207
Cdd:PRK09452 180 RKQMQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGT 228
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
6-211 |
5.50e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 86.40 E-value: 5.50e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 6 GELDVLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGHDVAAAAGR-VRESISLTGQ------FAA 78
Cdd:PRK13652 15 GSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIReVRKFVGLVFQnpddqiFSP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 79 VDE--VLTGRENLVLvarlrhlpDPGAVA---DDMLARFSLTDAGGRRAGEYSGGMRRRLDIAMSLVGDPPVIFLDEPTT 153
Cdd:PRK13652 95 TVEqdIAFGPINLGL--------DEETVAhrvSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTA 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2794531883 154 GLDPQARAEVWRTVKQLADG-GTTVLLTTQYLDEAEQLADRIAILHEGRIIQNGTLAEL 211
Cdd:PRK13652 167 GLDPQGVKELIDFLNDLPETyGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEI 225
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
11-192 |
6.42e-20 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 86.09 E-value: 6.42e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 11 LRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGHDVAAAagrVRES-ISLTGQFAAVD---EVLTgr 86
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQA---LQKNlVAYVPQSEEVDwsfPVLV-- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 87 ENLVLVARLRHL-------PDPGAVADDMLARFSLTDAGGRRAGEYSGGMRRRLDIAMSLVGDPPVIFLDEPTTGLDPQA 159
Cdd:PRK15056 98 EDVVMMGRYGHMgwlrrakKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKT 177
|
170 180 190
....*....|....*....|....*....|...
gi 2794531883 160 RAEVWRTVKQLADGGTTVLLTTQYLDEAEQLAD 192
Cdd:PRK15056 178 EARIISLLRELRDEGKTMLVSTHNLGSVTEFCD 210
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
6-211 |
7.82e-20 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 87.96 E-value: 7.82e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 6 GELDVLRGVDLGVAPGTIHALLGSNGAGKTTLvkiLSTLVRA---DAGTASVQGHDVAA-AAGRVRESISLTGQ----FA 77
Cdd:PRK11160 351 QPQPVLKGLSLQIKAGEKVALLGRTGCGKSTL---LQLLTRAwdpQQGEILLNGQPIADySEAALRQAISVVSQrvhlFS 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 78 AvdevlTGRENLVLVArlrhlPDpgavADD-----MLARFSLT---------DA----GGRragEYSGGMRRRLDIAMSL 139
Cdd:PRK11160 428 A-----TLRDNLLLAA-----PN----ASDealieVLQQVGLEklleddkglNAwlgeGGR---QLSGGEQRRLGIARAL 490
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2794531883 140 VGDPPVIFLDEPTTGLDPQARAEVWRTVKQLADgGTTVLLTTQYLDEAEQLaDRIAILHEGRIIQNGTLAEL 211
Cdd:PRK11160 491 LHDAPLLLLDEPTEGLDAETERQILELLAEHAQ-NKTVLMITHRLTGLEQF-DRICVMDNGQIIEQGTHQEL 560
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
6-197 |
1.15e-19 |
|
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: 87.34 E-value: 1.15e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 6 GELDVLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGHDVAAA-AGRVRESISLTGQFAAVDEVlT 84
Cdd:TIGR02857 333 GRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADAdADSWRDQIAWVPQHPFLFAG-T 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 85 GRENLVLVarlrhlpDPGAvADDMLARfSLTDAG----------------GRRAGEYSGGMRRRLDIAMSLVGDPPVIFL 148
Cdd:TIGR02857 412 IAENIRLA-------RPDA-SDAEIRE-ALERAGldefvaalpqgldtpiGEGGAGLSGGQAQRLALARAFLRDAPLLLL 482
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2794531883 149 DEPTTGLDPQARAEVWRTVKQLADGGTTVLLTTQylDEAEQLADRIAIL 197
Cdd:TIGR02857 483 DEPTAHLDAETEAEVLEALRALAQGRTVLLVTHR--LALAALADRIVVL 529
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
11-211 |
1.34e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 85.27 E-value: 1.34e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 11 LRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGHDVAAAAG-----RVRESISLTGQFAAVDEVltg 85
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGnknlkKLRKKVSLVFQFPEAQLF--- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 86 rENLVLvARLRHLPDPGAVADD--------MLARFSL-TDAGGRRAGEYSGGMRRRLDIAMSLVGDPPVIFLDEPTTGLD 156
Cdd:PRK13641 100 -ENTVL-KDVEFGPKNFGFSEDeakekalkWLKKVGLsEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLD 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2794531883 157 PQARAEVWRTVKQLADGGTTVLLTTQYLDEAEQLADRIAILHEGRIIQNGTLAEL 211
Cdd:PRK13641 178 PEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEI 232
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
7-206 |
1.47e-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: 83.79 E-value: 1.47e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 7 ELDVLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGHDVAAA-------------------AGRVR 67
Cdd:cd03245 16 EIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLdpadlrrnigyvpqdvtlfYGTLR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 68 ESISLTGQFAAVDEVLTGRENLVLVARLRHLPDpgavADDMLArfsltdagGRRAGEYSGGMRRRLDIAMSLVGDPPVIF 147
Cdd:cd03245 96 DNITLGAPLADDERILRAAELAGVTDFVNKHPN----GLDLQI--------GERGRGLSGGQRQAVALARALLNDPPILL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2794531883 148 LDEPTTGLDPQARAEVWRTVKQLADGGTTVLLT--TQYLDeaeqLADRIAILHEGRIIQNG 206
Cdd:cd03245 164 LDEPTSAMDMNSEERLKERLRQLLGDKTLIIIThrPSLLD----LVDRIIVMDSGRIVADG 220
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
3-211 |
1.66e-19 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 86.43 E-value: 1.66e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 3 KSYGELDVLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGHDVAAAAGRVReSISLTGQFAAVDEV 82
Cdd:PRK11607 27 KSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQR-PINMMFQSYALFPH 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 83 LTGRENLVLVARLRHLPDpGAVAD---DMLARFSLTDAGGRRAGEYSGGMRRRLDIAMSLVGDPPVIFLDEPTTGLDPQA 159
Cdd:PRK11607 106 MTVEQNIAFGLKQDKLPK-AEIASrvnEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKL 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2794531883 160 RAEV-WRTVKQLADGGTTVLLTTQYLDEAEQLADRIAILHEGRIIQNGTLAEL 211
Cdd:PRK11607 185 RDRMqLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEI 237
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-206 |
1.68e-19 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 84.59 E-value: 1.68e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 1 MRKSYGELDVLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQG-----HDVAAAAGRVRESISLTG- 74
Cdd:PRK11701 12 LTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMrdgqlRDLYALSEAERRRLLRTEw 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 75 ----QFAAvD----EVLTGR---ENLVLVARlRHLPDPGAVADDMLARFSLtdAGGR---RAGEYSGGMRRRLDIAMSLV 140
Cdd:PRK11701 92 gfvhQHPR-DglrmQVSAGGnigERLMAVGA-RHYGDIRATAGDWLERVEI--DAARiddLPTTFSGGMQQRLQIARNLV 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2794531883 141 GDPPVIFLDEPTTGLDPQARAEVWRTVKQL-ADGGTTVLLTTQYLDEAEQLADRIAILHEGRIIQNG 206
Cdd:PRK11701 168 THPRLVFMDEPTGGLDVSVQARLLDLLRGLvRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVVESG 234
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
3-210 |
2.05e-19 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 86.86 E-value: 2.05e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 3 KSYGELDVLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGHDVAAAagrvRESISLTGqFAAVDEV 82
Cdd:PLN03211 76 RQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNFTGTILANNRKPT----KQILKRTG-FVTQDDI 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 83 L----TGRENLVLVARLRhLP------DPGAVADDMLARFSLTDAGGRRAGE-----YSGGMRRRLDIAMSLVGDPPVIF 147
Cdd:PLN03211 151 LyphlTVRETLVFCSLLR-LPksltkqEKILVAESVISELGLTKCENTIIGNsfirgISGGERKRVSIAHEMLINPSLLI 229
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2794531883 148 LDEPTTGLDPQARAEVWRTVKQLADGGTTVLLTT-QYLDEAEQLADRIAILHEGRIIQNGTLAE 210
Cdd:PLN03211 230 LDEPTSGLDATAAYRLVLTLGSLAQKGKTIVTSMhQPSSRVYQMFDSVLVLSEGRCLFFGKGSD 293
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
2-206 |
2.25e-19 |
|
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: 83.08 E-value: 2.25e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 2 RKSYGELDVLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADA---GTASVQGHDVAAAAGRVRESISLTGQFAA 78
Cdd:cd03233 14 GKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVsveGDIHYNGIPYKEFAEKYPGEIIYVSEEDV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 79 VDEVLTGRENLVLVARLRhlpdpgavADDMLARFSltdaggrrageysGGMRRRLDIAMSLVGDPPVIFLDEPTTGLDPQ 158
Cdd:cd03233 94 HFPTLTVRETLDFALRCK--------GNEFVRGIS-------------GGERKRVSIAEALVSRASVLCWDNSTRGLDSS 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2794531883 159 ARAEVWRTVKQLAD--GGTTVLLTTQYLDEAEQLADRIAILHEGRIIQNG 206
Cdd:cd03233 153 TALEILKCIRTMADvlKTTTFVSLYQASDEIYDLFDKVLVLYEGRQIYYG 202
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
10-202 |
2.54e-19 |
|
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: 83.67 E-value: 2.54e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 10 VLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGHDVAAAAGR-VRESISLTGQfaavDEVLTGR-- 86
Cdd:cd03248 29 VLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKyLHSKVSLVGQ----EPVLFARsl 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 87 -ENL------VLVARLRHLPDpGAVADDMLARFSL---TDAGgRRAGEYSGGMRRRLDIAMSLVGDPPVIFLDEPTTGLD 156
Cdd:cd03248 105 qDNIayglqsCSFECVKEAAQ-KAHAHSFISELASgydTEVG-EKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALD 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2794531883 157 PQARAEVWRTVKQLADgGTTVLLTTQYLDEAEQlADRIAILHEGRI 202
Cdd:cd03248 183 AESEQQVQQALYDWPE-RRTVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
3-203 |
3.04e-19 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 86.23 E-value: 3.04e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 3 KSYGELDVLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGHDVAAAagRVRESISLtG-------- 74
Cdd:COG3845 266 RDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGL--SPRERRRL-Gvayipedr 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 75 -QFAAVDEvLTGRENLVLvARLRHLP-------DPGAV---ADDMLARFSL-TDAGGRRAGEYSGGMRRRLDIAMSLVGD 142
Cdd:COG3845 343 lGRGLVPD-MSVAENLIL-GRYRRPPfsrggflDRKAIrafAEELIEEFDVrTPGPDTPARSLSGGNQQKVILARELSRD 420
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2794531883 143 PPVIFLDEPTTGLDPQARAEVWRTVKQLADGGTTVLLTTQYLDEAEQLADRIAILHEGRII 203
Cdd:COG3845 421 PKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVLLISEDLDEILALSDRIAVMYEGRIV 481
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
2-213 |
3.59e-19 |
|
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: 85.16 E-value: 3.59e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 2 RKSYGE--LDVlrgvDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGHDVAAAAGRV-----RESISLTG 74
Cdd:TIGR02142 6 SKRLGDfsLDA----DFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKGIflppeKRRIGYVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 75 QFAAVDEVLTGRENLVLVARLRHLPDPGAVADDMLARFSLTDAGGRRAGEYSGGMRRRLDIAMSLVGDPPVIFLDEPTTG 154
Cdd:TIGR02142 82 QEARLFPHLSVRGNLRYGMKRARPSERRISFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 155 LDPQARAEVWRTVKQLADG-GTTVLLTTQYLDEAEQLADRIAILHEGRIIQNGTLAELKR 213
Cdd:TIGR02142 162 LDDPRKYEILPYLERLHAEfGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWA 221
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
15-211 |
3.64e-19 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 83.09 E-value: 3.64e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 15 DLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGHDVAAAAGRVReSISLTGQ----FAAvdevLTGREN-- 88
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSRR-PVSMLFQennlFSH----LTVAQNig 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 89 LVLVARLRHLPDPGAVADDMLARFSLTDAGGRRAGEYSGGMRRRLDIAMSLVGDPPVIFLDEPTTGLDPQARAEVWRTVK 168
Cdd:PRK10771 94 LGLNPGLKLNAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLVS 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2794531883 169 QL-ADGGTTVLLTTQYLDEAEQLADRIAILHEGRIIQNGTLAEL 211
Cdd:PRK10771 174 QVcQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDEL 217
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
4-211 |
5.24e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 83.50 E-value: 5.24e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 4 SYGELD--VLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGHDVAAAAGR-VRESISLT-----GQ 75
Cdd:PRK13632 16 SYPNSEnnALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKeIRKKIGIIfqnpdNQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 76 F--AAV-DEVLTGRENlvlvarlRHLP--DPGAVADDMLARFSLTDAGGRRAGEYSGGMRRRLDIAMSLVGDPPVIFLDE 150
Cdd:PRK13632 96 FigATVeDDIAFGLEN-------KKVPpkKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFDE 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2794531883 151 PTTGLDPQARAEVWRTVKQLADGGT-TVLLTTQYLDEAeQLADRIAILHEGRIIQNGTLAEL 211
Cdd:PRK13632 169 STSMLDPKGKREIKKIMVDLRKTRKkTLISITHDMDEA-ILADKVIVFSEGKLIAQGKPKEI 229
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
8-227 |
5.26e-19 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 86.05 E-value: 5.26e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 8 LDVLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTlvRADAGTasVQGHDVAAAAGRVRESISLTGQFAAVDEV----L 83
Cdd:PLN03140 893 LQLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAG--RKTGGY--IEGDIRISGFPKKQETFARISGYCEQNDIhspqV 968
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 84 TGRENLVLVARLRHlpdPGAVADDMLARF-----------SLTDAGGRRAG--EYSGGMRRRLDIAMSLVGDPPVIFLDE 150
Cdd:PLN03140 969 TVRESLIYSAFLRL---PKEVSKEEKMMFvdevmelveldNLKDAIVGLPGvtGLSTEQRKRLTIAVELVANPSIIFMDE 1045
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2794531883 151 PTTGLDPQARAEVWRTVKQLADGGTTVLLTTQY--LDEAEQLADRIAILHEGRIIQNGTLAELKRLLpsatVEYVEKQP 227
Cdd:PLN03140 1046 PTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQpsIDIFEAFDELLLMKRGGQVIYSGPLGRNSHKI----IEYFEAIP 1120
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
10-211 |
5.32e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 83.70 E-value: 5.32e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 10 VLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTAS---VQGHDVAA-AAGRVRESISLT-----GQF--AA 78
Cdd:PRK13640 22 ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPNSkitVDGITLTAkTVWDIREKVGIVfqnpdNQFvgAT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 79 V-DEVLTGRENlvlvarlRHLPDPG--AVADDMLARFSLTDAGGRRAGEYSGGMRRRLDIAMSLVGDPPVIFLDEPTTGL 155
Cdd:PRK13640 102 VgDDVAFGLEN-------RAVPRPEmiKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSML 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2794531883 156 DPQARAEVWRTVKQLA-DGGTTVLLTTQYLDEAEQlADRIAILHEGRIIQNGTLAEL 211
Cdd:PRK13640 175 DPAGKEQILKLIRKLKkKNNLTVISITHDIDEANM-ADQVLVLDDGKLLAQGSPVEI 230
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
11-202 |
7.27e-19 |
|
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: 82.07 E-value: 7.27e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 11 LRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGHDVAAAAGR----VRESISLTGQFAAVDEVLTGR 86
Cdd:cd03292 17 LDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRaipyLRRKIGVVFQDFRLLPDRNVY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 87 ENLVLVARLRHLPdPGAVAD---DMLARFSLTDAGGRRAGEYSGGMRRRLDIAMSLVGDPPVIFLDEPTTGLDPQARAEV 163
Cdd:cd03292 97 ENVAFALEVTGVP-PREIRKrvpAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTTWEI 175
|
170 180 190
....*....|....*....|....*....|....*....
gi 2794531883 164 WRTVKQLADGGTTVLLTTQYLDEAEQLADRIAILHEGRI 202
Cdd:cd03292 176 MNLLKKINKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
11-211 |
7.61e-19 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 84.70 E-value: 7.61e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 11 LRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGHDVAAAAGRV-----RESISLTGQFAAVDEVLTG 85
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAElrevrRKKIAMVFQSFALMPHMTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 86 RENLVLVARLRHLP--DPGAVADDMLARFSLTDAGGRRAGEYSGGMRRRLDIAMSLVGDPPVIFLDEPTTGLDPQARAEV 163
Cdd:PRK10070 124 LDNTAFGMELAGINaeERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEM 203
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2794531883 164 W-RTVKQLADGGTTVLLTTQYLDEAEQLADRIAILHEGRIIQNGTLAEL 211
Cdd:PRK10070 204 QdELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEI 252
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
7-211 |
9.00e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 83.15 E-value: 9.00e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 7 ELDVLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVqGHDVAAAAGR------VRESISLTGQFA--- 77
Cdd:PRK13634 19 ERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTI-GERVITAGKKnkklkpLRKKVGIVFQFPehq 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 78 -----AVDEVLTGRENL-VLVArlrhlpDPGAVADDMLARFSLT-DAGGRRAGEYSGGMRRRLDIAMSLVGDPPVIFLDE 150
Cdd:PRK13634 98 lfeetVEKDICFGPMNFgVSEE------DAKQKAREMIELVGLPeELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDE 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2794531883 151 PTTGLDPQARAEVWRTVKQL-ADGGTTVLLTTQYLDEAEQLADRIAILHEGRIIQNGTLAEL 211
Cdd:PRK13634 172 PTAGLDPKGRKEMMEMFYKLhKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREI 233
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1-236 |
9.77e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 83.17 E-value: 9.77e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 1 MRKSYGELDVLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGHDVA---AAAGRVRESISLTGQF- 76
Cdd:PRK13637 13 MEGTPFEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITdkkVKLSDIRKKVGLVFQYp 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 77 -------AAVDEVLTGRENLvlvarlrhlpdpGAVADDMLAR---------FSLTDAGGRRAGEYSGGMRRRLDIAMSLV 140
Cdd:PRK13637 93 eyqlfeeTIEKDIAFGPINL------------GLSEEEIENRvkramnivgLDYEDYKDKSPFELSGGQKRRVAIAGVVA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 141 GDPPVIFLDEPTTGLDPQARAEVWRTVKQLADG-GTTVLLTTQYLDEAEQLADRIAILHEGRIIQNGTLAELKRllpsaT 219
Cdd:PRK13637 161 MEPKILILDEPTAGLDPKGRDEILNKIKELHKEyNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVFK-----E 235
|
250
....*....|....*..
gi 2794531883 220 VEyvekqpTLEEVFLAV 236
Cdd:PRK13637 236 VE------TLESIGLAV 246
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
11-204 |
1.05e-18 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 84.58 E-value: 1.05e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 11 LRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGHDVAAAagRVRESIS-----LTGQFAAVDEvLTG 85
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFA--STTAALAagvaiIYQELHLVPE-MTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 86 RENLVlvarLRHLPDPGAVAD---------DMLARFSLTDAGGRRAGEYSGGMRRRLDIAMSLVGDPPVIFLDEPTTGLD 156
Cdd:PRK11288 97 AENLY----LGQLPHKGGIVNrrllnyearEQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAFDEPTSSLS 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2794531883 157 PQARAEVWRTVKQLADGGTTVLLTTQYLDEAEQLADRIAILHEGRIIQ 204
Cdd:PRK11288 173 AREIEQLFRVIRELRAEGRVILYVSHRMEEIFALCDAITVFKDGRYVA 220
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
10-180 |
1.05e-18 |
|
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: 84.72 E-value: 1.05e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 10 VLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGHDVAAAAG-RVRESISLTGQFAAVDEVlTGREN 88
Cdd:TIGR02868 350 VLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQdEVRRRVSVCAQDAHLFDT-TVREN 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 89 LvLVARlrhlPD-PGAVADDMLARFSLTD--------------AGGRRageYSGGMRRRLDIAMSLVGDPPVIFLDEPTT 153
Cdd:TIGR02868 429 L-RLAR----PDaTDEELWAALERVGLADwlralpdgldtvlgEGGAR---LSGGERQRLALARALLADAPILLLDEPTE 500
|
170 180
....*....|....*....|....*..
gi 2794531883 154 GLDPQARAEVWRTVKQLADGGTTVLLT 180
Cdd:TIGR02868 501 HLDAETADELLEDLLAALSGRTVVLIT 527
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
11-211 |
1.51e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 82.59 E-value: 1.51e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 11 LRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGHDVAAAAG---RVRESISLTGQ------FAA--V 79
Cdd:PRK13636 22 LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRKglmKLRESVGMVFQdpdnqlFSAsvY 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 80 DEVLTGRENLVLVARLRHlpdpgAVADDMLARFSLTDAGGRRAGEYSGGMRRRLDIAMSLVGDPPVIFLDEPTTGLDPQA 159
Cdd:PRK13636 102 QDVSFGAVNLKLPEDEVR-----KRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMG 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2794531883 160 RAEVWRTVKQLADG-GTTVLLTTQYLDEAEQLADRIAILHEGRIIQNGTLAEL 211
Cdd:PRK13636 177 VSEIMKLLVEMQKElGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEV 229
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
5-204 |
1.55e-18 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 82.05 E-value: 1.55e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 5 YGELDVLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGHDVA---AAAGRVRESISLTGQFAAVDE 81
Cdd:PRK11248 11 YGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEgpgAERGVVFQNEGLLPWRNVQDN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 82 VLTGREnLVLVARLRHLpdpgAVADDMLARFSLTDAGGRRAGEYSGGMRRRLDIAMSLVGDPPVIFLDEPTTGLDPQARA 161
Cdd:PRK11248 91 VAFGLQ-LAGVEKMQRL----EIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTRE 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2794531883 162 EVWRTVKQL-ADGGTTVLLTTQYLDEAEQLADRIAILH--EGRIIQ 204
Cdd:PRK11248 166 QMQTLLLKLwQETGKQVLLITHDIEEAVFMATELVLLSpgPGRVVE 211
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
11-225 |
2.27e-18 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 83.23 E-value: 2.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 11 LRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGHDVAAAAGRV-----RESISLTGQ-FAavdevL- 83
Cdd:COG4175 43 VNDASFDVEEGEIFVIMGLSGSGKSTLVRCLNRLIEPTAGEVLIDGEDITKLSKKElrelrRKKMSMVFQhFA-----Ll 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 84 ---TGRENlvlVA---RLRHLPDPG--AVADDMLARFSLTDAGGRRAGEYSGGMRRRLDIAMSLVGDPPVIFLDEPTTGL 155
Cdd:COG4175 118 phrTVLEN---VAfglEIQGVPKAErrERAREALELVGLAGWEDSYPDELSGGMQQRVGLARALATDPDILLMDEAFSAL 194
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2794531883 156 DPQARA----EVWRTVKQLadgGTTVLLTTQYLDEAEQLADRIAILHEGRIIQNGTLAELkrLLPSATvEYVEK 225
Cdd:COG4175 195 DPLIRRemqdELLELQAKL---KKTIVFITHDLDEALRLGDRIAIMKDGRIVQIGTPEEI--LTNPAN-DYVAD 262
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
12-211 |
2.66e-18 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 81.28 E-value: 2.66e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 12 RGVDLGVAPGTIHALLGSNGAGKT----TLVKILSTLVRADAGTASVQGHDVAAAAGRVReSISLTGQ--FAAVDEVLTG 85
Cdd:PRK10418 20 HGVSLTLQRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGRVLLDGKPVAPCALRGR-KIATIMQnpRSAFNPLHTM 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 86 RENLVLVARLRHLPDPGAVADDMLARFSLTDAG---GRRAGEYSGGMRRRLDIAMSLVGDPPVIFLDEPTTGLDPQARAE 162
Cdd:PRK10418 99 HTHARETCLALGKPADDATLTAALEAVGLENAArvlKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTTDLDVVAQAR 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2794531883 163 VWRTVKQL-ADGGTTVLLTTQYLDEAEQLADRIAILHEGRIIQNGTLAEL 211
Cdd:PRK10418 179 ILDLLESIvQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETL 228
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-206 |
3.42e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 81.04 E-value: 3.42e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 1 MRKSYGELDVLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADA-----GTASVQGHDVAAA---AGRVRESISL 72
Cdd:PRK14267 10 LRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNEearveGEVRLFGRNIYSPdvdPIEVRREVGM 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 73 TGQFAAVDEVLTGRENLVLVARLRHLPDPGAVADDM----LARFSLTDAGGRRAGEY----SGGMRRRLDIAMSLVGDPP 144
Cdd:PRK14267 90 VFQYPNPFPHLTIYDNVAIGVKLNGLVKSKKELDERvewaLKKAALWDEVKDRLNDYpsnlSGGQRQRLVIARALAMKPK 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2794531883 145 VIFLDEPTTGLDPQARAEVWRTVKQLADgGTTVLLTTQYLDEAEQLADRIAILHEGRIIQNG 206
Cdd:PRK14267 170 ILLMDEPTANIDPVGTAKIEELLFELKK-EYTIVLVTHSPAQAARVSDYVAFLYLGKLIEVG 230
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
14-211 |
3.45e-18 |
|
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: 82.46 E-value: 3.45e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 14 VDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGHDVAAAAGRV-----RESISLTGQFAAVDEVLTGREN 88
Cdd:COG4148 18 VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLQDSARGIflpphRRRIGYVFQEARLFPHLSVRGN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 89 LVLVARLRHLPDPGAVADDMLARFSLTDAGGRRAGEYSGGMRRRLDIAMSLVGDPPVIFLDEPTTGLDPQARAEVWRTVK 168
Cdd:COG4148 98 LLYGRKRAPRAERRISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAEILPYLE 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2794531883 169 QLAD-GGTTVLLTTQYLDEAEQLADRIAILHEGRIIQNGTLAEL 211
Cdd:COG4148 178 RLRDeLDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEV 221
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
10-211 |
5.08e-18 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 82.85 E-value: 5.08e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 10 VLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGHD------------VAAAA-------GRVRESI 70
Cdd:TIGR00958 496 VLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPlvqydhhylhrqVALVGqepvlfsGSVRENI 575
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 71 SLTGQFAAVDEVLTgrenlvlVARLrhlpdpgAVADDMLARFSLT--DAGGRRAGEYSGGMRRRLDIAMSLVGDPPVIFL 148
Cdd:TIGR00958 576 AYGLTDTPDEEIMA-------AAKA-------ANAHDFIMEFPNGydTEVGEKGSQLSGGQKQRIAIARALVRKPRVLIL 641
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2794531883 149 DEPTTGLDpqarAEVWRTVKQLAD-GGTTVLLTTQYLDEAEQlADRIAILHEGRIIQNGTLAEL 211
Cdd:TIGR00958 642 DEATSALD----AECEQLLQESRSrASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQL 700
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
7-211 |
5.78e-18 |
|
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: 79.97 E-value: 5.78e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 7 ELDVLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGHDVaaaagR------VRESISLTGQfaavD 80
Cdd:cd03253 13 GRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDI-----RevtldsLRRAIGVVPQ----D 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 81 EVL----------TGR-----ENLVLVARLRHLpdpgavaDDMLARFSltDAGGRRAGE----YSGGMRRRLDIAMSLVG 141
Cdd:cd03253 84 TVLfndtigynirYGRpdatdEEVIEAAKAAQI-------HDKIMRFP--DGYDTIVGErglkLSGGEKQRVAIARAILK 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2794531883 142 DPPVIFLDEPTTGLDPQARAEVWRTVKQLADGGTTVLLttqyldeAEQL-----ADRIAILHEGRIIQNGTLAEL 211
Cdd:cd03253 155 NPPILLLDEATSALDTHTEREIQAALRDVSKGRTTIVI-------AHRLstivnADKIIVLKDGRIVERGTHEEL 222
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
7-211 |
6.57e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 80.52 E-value: 6.57e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 7 ELDVLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGHDVAAA-AGRVRESISLT-----GQFAAV- 79
Cdd:PRK13642 19 DVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAEnVWNLRRKIGMVfqnpdNQFVGAt 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 80 --DEVLTGRENlvlvarlRHLPDPGAV--ADDMLARFSLTDAGGRRAGEYSGGMRRRLDIAMSLVGDPPVIFLDEPTTGL 155
Cdd:PRK13642 99 veDDVAFGMEN-------QGIPREEMIkrVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSML 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2794531883 156 DPQARAEVWRTVKQLADG-GTTVLLTTQYLDEAEQlADRIAILHEGRIIQNGTLAEL 211
Cdd:PRK13642 172 DPTGRQEIMRVIHEIKEKyQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSEL 227
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
11-207 |
6.59e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 80.42 E-value: 6.59e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 11 LRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGHDvAAAAGRVRESISLTG--------QFAA--VD 80
Cdd:PRK13644 18 LENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGID-TGDFSKLQGIRKLVGivfqnpetQFVGrtVE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 81 EVLT-GRENLVLVA-RLRHLpdpgavADDMLARFSLTDAGGRRAGEYSGGMRRRLDIAMSLVGDPPVIFLDEPTTGLDPQ 158
Cdd:PRK13644 97 EDLAfGPENLCLPPiEIRKR------VDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPD 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2794531883 159 ARAEVWRTVKQLADGGTTVLLTTQYLDEAeQLADRIAILHEGRIIQNGT 207
Cdd:PRK13644 171 SGIAVLERIKKLHEKGKTIVYITHNLEEL-HDADRIIVMDRGKIVLEGE 218
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
6-211 |
9.93e-18 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 79.34 E-value: 9.93e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 6 GELDVLRGVDLGVAPGTIHALLGSNGAGKTTLVKILS--TLVRADAGTASVQGHDVAAAA--GRVRESISLTGQ------ 75
Cdd:COG0396 11 EGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMghPKYEVTSGSILLDGEDILELSpdERARAGIFLAFQypveip 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 76 ------F--AAV----DEVLTGRENLVLV-ARLRHLpdpgAVADDMLARfSLtDAGgrrageYSGGMRRRLDIAMSLVGD 142
Cdd:COG0396 91 gvsvsnFlrTALnarrGEELSAREFLKLLkEKMKEL----GLDEDFLDR-YV-NEG------FSGGEKKRNEILQMLLLE 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2794531883 143 PPVIFLDEPTTGLDPQARAEVWRTVKQLADGGTTVLLTTQY---LDEAEqlADRIAILHEGRIIQNGTlAEL 211
Cdd:COG0396 159 PKLAILDETDSGLDIDALRIVAEGVNKLRSPDRGILIITHYqriLDYIK--PDFVHVLVDGRIVKSGG-KEL 227
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
3-221 |
1.01e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 80.66 E-value: 1.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 3 KSYGELDVLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQ----GHDVAAAAG-------------R 65
Cdd:PRK13631 34 KQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGdiyiGDKKNNHELitnpyskkiknfkE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 66 VRESISLTGQFAAVDEVLTGRENLVL---VARLRHLPDPGAVADDMLARFSLTDAGGRRAG-EYSGGMRRRLDIAMSLVG 141
Cdd:PRK13631 114 LRRRVSMVFQFPEYQLFKDTIEKDIMfgpVALGVKKSEAKKLAKFYLNKMGLDDSYLERSPfGLSGGQKRRVAIAGILAI 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 142 DPPVIFLDEPTTGLDPQARAEVWRTVKQLADGGTTVLLTTQYLDEAEQLADRIAILHEGRIIQNGTLAEL---KRLLPSA 218
Cdd:PRK13631 194 QPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTGTPYEIftdQHIINST 273
|
...
gi 2794531883 219 TVE 221
Cdd:PRK13631 274 SIQ 276
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
6-197 |
1.27e-17 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 78.99 E-value: 1.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 6 GELDVLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGHDVAA-AAGRVRESISLTGQFAAV--DEV 82
Cdd:PRK10247 18 GDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTlKPEIYRQQVSYCAQTPTLfgDTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 83 ltgRENLVLVARLRHL-PDPGAVADDmLARFSLTDAG-GRRAGEYSGGMRRRLDIAMSLVGDPPVIFLDEPTTGLDPQAR 160
Cdd:PRK10247 98 ---YDNLIFPWQIRNQqPDPAIFLDD-LERFALPDTIlTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDESNK 173
|
170 180 190
....*....|....*....|....*....|....*...
gi 2794531883 161 AEVWRTVKQLA-DGGTTVLLTTQYLDEAEQlADRIAIL 197
Cdd:PRK10247 174 HNVNEIIHRYVrEQNIAVLWVTHDKDEINH-ADKVITL 210
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
7-201 |
1.77e-17 |
|
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: 78.63 E-value: 1.77e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 7 ELDVLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASV--QGH--DVAAAAGRV-----RESISLTGQF- 76
Cdd:COG4778 23 RLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrhDGGwvDLAQASPREilalrRRTIGYVSQFl 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 77 ------AAVDevltgrenlvLVAR-LRHLPDPGAVADD----MLARFSL----------TdaggrrageYSGGMRRRLDI 135
Cdd:COG4778 103 rviprvSALD----------VVAEpLLERGVDREEARArareLLARLNLperlwdlppaT---------FSGGEQQRVNI 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2794531883 136 AMSLVGDPPVIFLDEPTTGLDPQARAEVWRTVKQLADGGTTVLLTTQYLDEAEQLADRIAILHEGR 201
Cdd:COG4778 164 ARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVREAVADRVVDVTPFS 229
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
10-211 |
1.79e-17 |
|
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: 78.42 E-value: 1.79e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 10 VLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGHDVAAA-------------------AGRVRESI 70
Cdd:cd03254 18 VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDIsrkslrsmigvvlqdtflfSGTIMENI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 71 SLTGQFAAVDEVLTGRENLVLVARLRHLPDpgavaddmlarfSLTDAGGRRAGEYSGGMRRRLDIAMSLVGDPPVIFLDE 150
Cdd:cd03254 98 RLGRPNATDEEVIEAAKEAGAHDFIMKLPN------------GYDTVLGENGGNLSQGERQLLAIARAMLRDPKILILDE 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2794531883 151 PTTGLDPQARAEVWRTVKQLADGGTTV-----LLTTQYldeaeqlADRIAILHEGRIIQNGTLAEL 211
Cdd:cd03254 166 ATSNIDTETEKLIQEALEKLMKGRTSIiiahrLSTIKN-------ADKILVLDDGKIIEEGTHDEL 224
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
5-225 |
1.89e-17 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 79.26 E-value: 1.89e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 5 YGELDVLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGHDVAAAAGR-VRESISLTGQFAAVDEVL 83
Cdd:PRK10253 17 YGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKeVARRIGLLAQNATTPGDI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 84 TGREnlvLVARLR--HLP--------DPGAVADDMLARfSLTDAGGRRAGEYSGGMRRRLDIAMSLVGDPPVIFLDEPTT 153
Cdd:PRK10253 97 TVQE---LVARGRypHQPlftrwrkeDEEAVTKAMQAT-GITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTT 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2794531883 154 GLDPQARAEVWRTVKQL-ADGGTTVLLTTQYLDEAEQLADRIAILHEGRIIQNGTLAELkrllpsATVEYVEK 225
Cdd:PRK10253 173 WLDISHQIDLLELLSELnREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEI------VTAELIER 239
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
1-206 |
2.63e-17 |
|
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: 78.72 E-value: 2.63e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 1 MRKSYGELDVLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTA-----SVQGHDVAAAAGRVRESISLT-- 73
Cdd:TIGR02323 9 LSKSYGGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTAtyimrSGAELELYQLSEAERRRLMRTew 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 74 ---------GQFAAVDEVLTGRENLVLVARlRHLPDPGAVADDMLARFSLtDAG--GRRAGEYSGGMRRRLDIAMSLVGD 142
Cdd:TIGR02323 89 gfvhqnprdGLRMRVSAGANIGERLMAIGA-RHYGNIRATAQDWLEEVEI-DPTriDDLPRAFSGGMQQRLQIARNLVTR 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2794531883 143 PPVIFLDEPTTGLDPQARAEVWRTVKQLA-DGGTTVLLTTQYLDEAEQLADRIAILHEGRIIQNG 206
Cdd:TIGR02323 167 PRLVFMDEPTGGLDVSVQARLLDLLRGLVrDLGLAVIIVTHDLGVARLLAQRLLVMQQGRVVESG 231
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
10-202 |
2.65e-17 |
|
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: 76.87 E-value: 2.65e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 10 VLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGHDVAAAA-GRVRESIsltGQFAAVDEVLtgren 88
Cdd:cd03246 17 VLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDpNELGDHV---GYLPQDDELF----- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 89 lvlvarlrhlpdPGAVADDMLarfsltdaggrrageySGGMRRRLDIAMSLVGDPPVIFLDEPTTGLDPQARAEVWRTVK 168
Cdd:cd03246 89 ------------SGSIAENIL----------------SGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQAIA 140
|
170 180 190
....*....|....*....|....*....|....
gi 2794531883 169 QLADGGTTVLLTTQYLdEAEQLADRIAILHEGRI 202
Cdd:cd03246 141 ALKAAGATRIVIAHRP-ETLASADRILVLEDGRV 173
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
10-221 |
3.09e-17 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 78.59 E-value: 3.09e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 10 VLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGHDV--------AAAAGRVRESiSLTGQFAAvde 81
Cdd:COG1101 21 ALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVtklpeykrAKYIGRVFQD-PMMGTAPS--- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 82 vLTGRENLVLvARLRHLPDP--GAVADDMLARF----SLTDAG-----GRRAGEYSGGMRRRLDIAMSLVGDPPVIFLDE 150
Cdd:COG1101 97 -MTIEENLAL-AYRRGKRRGlrRGLTKKRRELFrellATLGLGlenrlDTKVGLLSGGQRQALSLLMATLTKPKLLLLDE 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2794531883 151 PTTGLDPQARAEVWR-TVKQLADGGTTVLLTTQYLDEAEQLADRIAILHEGRIIQNGTLAELKRLlpsaTVE 221
Cdd:COG1101 175 HTAALDPKTAALVLElTEKIVEENNLTTLMVTHNMEQALDYGNRLIMMHEGRIILDVSGEEKKKL----TVE 242
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
2-211 |
3.55e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 78.90 E-value: 3.55e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 2 RKSYGELDVLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGHDVAAA------AGRVRESISLTGQ 75
Cdd:PRK13645 18 KKTPFEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPANlkkikeVKRLRKEIGLVFQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 76 FAAVDEVLTGRENLVLVARLRHLPDPGAV---ADDMLARFSLTDAGGRRAG-EYSGGMRRRLDIAMSLVGDPPVIFLDEP 151
Cdd:PRK13645 98 FPEYQLFQETIEKDIAFGPVNLGENKQEAykkVPELLKLVQLPEDYVKRSPfELSGGQKRRVALAGIIAMDGNTLVLDEP 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2794531883 152 TTGLDPQARAEVWRTVKQL-ADGGTTVLLTTQYLDEAEQLADRIAILHEGRIIQNGTLAEL 211
Cdd:PRK13645 178 TGGLDPKGEEDFINLFERLnKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEI 238
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
3-203 |
4.26e-17 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 80.11 E-value: 4.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 3 KSYGELDVLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVqGHDVAaaagrvresislTGQFAAVDEV 82
Cdd:COG0488 323 KSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETVK------------IGYFDQHQEE 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 83 LTGRENLVLVarLRHLPDPGAVAD--DMLARFSLT-DAGGRRAGEYSGGMRRRLDIAMSLVGDPPVIFLDEPTTGLDPQA 159
Cdd:COG0488 390 LDPDKTVLDE--LRDGAPGGTEQEvrGYLGRFLFSgDDAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIET 467
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2794531883 160 RAEVwrtVKQLADGGTTVLLTT--QYLDEAeqLADRIAILHEGRII 203
Cdd:COG0488 468 LEAL---EEALDDFPGTVLLVShdRYFLDR--VATRILEFEDGGVR 508
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
11-211 |
6.84e-17 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 79.62 E-value: 6.84e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 11 LRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGHDVAAAAGR-VRESISLTGQFAAV------DEVL 83
Cdd:PRK13657 351 VEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRAsLRRNIAVVFQDAGLfnrsieDNIR 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 84 TGREN-----LVLVARLrhlpdpgAVADDMLARFSL---TDAGgRRAGEYSGGMRRRLDIAMSLVGDPPVIFLDEPTTGL 155
Cdd:PRK13657 431 VGRPDatdeeMRAAAER-------AQAHDFIERKPDgydTVVG-ERGRQLSGGERQRLAIARALLKDPPILILDEATSAL 502
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2794531883 156 DPQARAEVWRTVKQLADGGTTVLLttqyldeAEQL-----ADRIAILHEGRIIQNGTLAEL 211
Cdd:PRK13657 503 DVETEAKVKAALDELMKGRTTFII-------AHRLstvrnADRILVFDNGRVVESGSFDEL 556
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
6-210 |
1.10e-16 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 77.92 E-value: 1.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 6 GELDVLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGHDVAA--AAG--RVRESISLTGQ-Faavd 80
Cdd:PRK11153 16 RTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTAlsEKElrKARRQIGMIFQhF---- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 81 EVLTGR---ENLVLVARLRHLP--DPGAVADDMLARFSLTDAGGRRAGEYSGGMRRRLDIAMSLVGDPPVIFLDEPTTGL 155
Cdd:PRK11153 92 NLLSSRtvfDNVALPLELAGTPkaEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPKVLLCDEATSAL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2794531883 156 DPQARAEVWRTVKQL-ADGGTTVLLTTQYLDEAEQLADRIAILHEGRIIQNGTLAE 210
Cdd:PRK11153 172 DPATTRSILELLKDInRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSE 227
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
6-211 |
1.43e-16 |
|
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: 78.57 E-value: 1.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 6 GELDVLRGVDLGVAPGTIHALLGSNGAGKT----TLVKILSTLVRADAGTASVQGHDVAAAAGRVRESI----------- 70
Cdd:COG4172 21 GTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERELRRIrgnriamifqe 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 71 ---SLT-----GQfaAVDEVL------TGREnlvlvARLRhlpdpgavADDMLARFSLTDAGgRRAGEY----SGGMRRR 132
Cdd:COG4172 101 pmtSLNplhtiGK--QIAEVLrlhrglSGAA-----ARAR--------ALELLERVGIPDPE-RRLDAYphqlSGGQRQR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 133 LDIAMSLVGDPPVIFLDEPTTGLDPQARAEVWRTVKQL-ADGGTTVLLTTQYLDEAEQLADRIAILHEGRIIQNGTLAEL 211
Cdd:COG4172 165 VMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLqRELGMALLLITHDLGVVRRFADRVAVMRQGEIVEQGPTAEL 244
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
124-225 |
7.04e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 75.51 E-value: 7.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 124 EYSGGMRRRLDIAMSLVGDPPVIFLDEPTTGLDPQARAEVWRTVKQLADGGTTVLLTTQYLDEAEQLADRIAILHEGRII 203
Cdd:PRK13651 165 ELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTKRTIFFKDGKII 244
|
90 100 110
....*....|....*....|....*....|.
gi 2794531883 204 QNG----TLAELK-----RLLPSATVEYVEK 225
Cdd:PRK13651 245 KDGdtydILSDNKflienNMEPPKLLNFVNK 275
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
11-211 |
7.17e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 75.15 E-value: 7.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 11 LRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGHDVAAA-AGRVRESISLT-----GQF--AAV-DE 81
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEEnVWDIRHKIGMVfqnpdNQFvgATVeDD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 82 VLTGRENlvlvarlrhlpdPGAVADDMLARFS-------LTDAGGRRAGEYSGGMRRRLDIAMSLVGDPPVIFLDEPTTG 154
Cdd:PRK13650 103 VAFGLEN------------KGIPHEEMKERVNealelvgMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSM 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2794531883 155 LDPQARAEVWRTVKQLADG-GTTVLLTTQYLDEAeQLADRIAILHEGRIIQNGTLAEL 211
Cdd:PRK13650 171 LDPEGRLELIKTIKGIRDDyQMTVISITHDLDEV-ALSDRVLVMKNGQVESTSTPREL 227
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
3-203 |
1.15e-15 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 75.74 E-value: 1.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 3 KSYGELDVLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVraDAGTAS----VQGHDVAAAAgrVRES----ISLTG 74
Cdd:PRK13549 13 KTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY--PHGTYEgeiiFEGEELQASN--IRDTeragIAIIH 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 75 QFAAVDEVLTGRENLVlvarLRHLPDPGAVADD---------MLARFSLTDAGGRRAGEYSGGMRRRLDIAMSLVGDPPV 145
Cdd:PRK13549 89 QELALVKELSVLENIF----LGNEITPGGIMDYdamylraqkLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQARL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2794531883 146 IFLDEPTTGLDPQARAEVWRTVKQLADGGTTVLLTTQYLDEAEQLADRIAILHEGRII 203
Cdd:PRK13549 165 LILDEPTASLTESETAVLLDIIRDLKAHGIACIYISHKLNEVKAISDTICVIRDGRHI 222
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
9-208 |
1.28e-15 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 73.70 E-value: 1.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 9 DVLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGHDV------AAAAGRVREsISLTGQFAAVDEV 82
Cdd:PRK11629 23 DVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMsklssaAKAELRNQK-LGFIYQFHHLLPD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 83 LTGRENLVLVARLRHLPDPGA--VADDMLARFSLTDAGGRRAGEYSGGMRRRLDIAMSLVGDPPVIFLDEPTTGLDPQAR 160
Cdd:PRK11629 102 FTALENVAMPLLIGKKKPAEInsRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNA 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2794531883 161 AEVWRTVKQL-ADGGTTVLLTTQYLDEAEQLaDRIAILHEGRIIQNGTL 208
Cdd:PRK11629 182 DSIFQLLGELnRLQGTAFLVVTHDLQLAKRM-SRQLEMRDGRLTAELSL 229
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
10-211 |
1.57e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 73.98 E-value: 1.57e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 10 VLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTL--------VRAD---AGTASVQGHDVAAAAGRVRESISLTGQF-- 76
Cdd:PRK14271 36 VLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMndkvsgyrYSGDvllGGRSIFNYRDVLEFRRRVGMLFQRPNPFpm 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 77 AAVDEVLTGRENLVLVARlrhlPDPGAVADDMLARFSLTDAGGRRAGE----YSGGMRRRLDIAMSLVGDPPVIFLDEPT 152
Cdd:PRK14271 116 SIMDNVLAGVRAHKLVPR----KEFRGVAQARLTEVGLWDAVKDRLSDspfrLSGGQQQLLCLARTLAVNPEVLLLDEPT 191
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2794531883 153 TGLDPQARAEVWRTVKQLADgGTTVLLTTQYLDEAEQLADRIAILHEGRIIQNGTLAEL 211
Cdd:PRK14271 192 SALDPTTTEKIEEFIRSLAD-RLTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQL 249
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
1-202 |
1.84e-15 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 73.56 E-value: 1.84e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 1 MRKSYGELDVLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTAsVQGhdvAAAAGRVRESISLTGQFA--- 77
Cdd:PRK11247 18 VSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL-LAG---TAPLAEAREDTRLMFQDArll 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 78 ----AVDEVLTGrenlvLVARLRhlpdpgAVADDMLARFSLTDaggrRAGEY----SGGMRRRLDIAMSLVGDPPVIFLD 149
Cdd:PRK11247 94 pwkkVIDNVGLG-----LKGQWR------DAALQALAAVGLAD----RANEWpaalSGGQKQRVALARALIHRPGLLLLD 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2794531883 150 EPTTGLDPQARAEVWRTVKQL-ADGGTTVLLTTQYLDEAEQLADRIAILHEGRI 202
Cdd:PRK11247 159 EPLGALDALTRIEMQDLIESLwQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
10-211 |
2.56e-15 |
|
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: 74.86 E-value: 2.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 10 VLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGHDVAAAAGR-VRESISLTGQfaavDEVL---TG 85
Cdd:COG5265 373 ILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQAsLRAAIGIVPQ----DTVLfndTI 448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 86 RENL------------VLVARLRHLpdpgavaDDMLArfSLTDAGGRRAGE----YSGGMRRRLDIAMSLVGDPPVIFLD 149
Cdd:COG5265 449 AYNIaygrpdaseeevEAAARAAQI-------HDFIE--SLPDGYDTRVGErglkLSGGEKQRVAIARTLLKNPPILIFD 519
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2794531883 150 EPTTGLDPQARAEVWRTVKQLADGGTTVLLttqyldeAEQL-----ADRIAILHEGRIIQNGTLAEL 211
Cdd:COG5265 520 EATSALDSRTERAIQAALREVARGRTTLVI-------AHRLstivdADEILVLEAGRIVERGTHAEL 579
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
3-202 |
3.31e-15 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 72.21 E-value: 3.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 3 KSY-GELDVLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGHDVAAAAGR----VRESISLTGQFA 77
Cdd:PRK10908 9 KAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNRevpfLRRQIGMIFQDH 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 78 AVDEVLTGRENLVLvarlrHLPDPGAVADDMLARFS-------LTDAGGRRAGEYSGGMRRRLDIAMSLVGDPPVIFLDE 150
Cdd:PRK10908 89 HLLMDRTVYDNVAI-----PLIIAGASGDDIRRRVSaaldkvgLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADE 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2794531883 151 PTTGLDPQARAEVWRTVKQLADGGTTVLLTTQYLDEAEQLADRIAILHEGRI 202
Cdd:PRK10908 164 PTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
5-211 |
7.87e-15 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 71.73 E-value: 7.87e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 5 YGELDVLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRAD-----AGTASVQGHDVAAAAG---RVRESISLTGQ- 75
Cdd:PRK14239 15 YNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLNpevtiTGSIVYNGHNIYSPRTdtvDLRKEIGMVFQq 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 76 ---FAavdevLTGRENLVLVARLRHLPDPG---AVADDMLARFSLTDAGGRR----AGEYSGGMRRRLDIAMSLVGDPPV 145
Cdd:PRK14239 95 pnpFP-----MSIYENVVYGLRLKGIKDKQvldEAVEKSLKGASIWDEVKDRlhdsALGLSGGQQQRVCIARVLATSPKI 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2794531883 146 IFLDEPTTGLDPQARAEVWRTVKQLADgGTTVLLTTQYLDEAEQLADRIAILHEGRIIQNGTLAEL 211
Cdd:PRK14239 170 ILLDEPTSALDPISAGKIEETLLGLKD-DYTMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQM 234
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
5-203 |
9.52e-15 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 71.61 E-value: 9.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 5 YGELDVLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTL------VRADaGTASVQGHDVAAAAG---RVRESISLTGQ 75
Cdd:COG1117 21 YGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMndlipgARVE-GEILLDGEDIYDPDVdvvELRRRVGMVFQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 76 ----FAavdevLTGRENLVLVARLRHLPDPGAVADdmLARFSLTDAG---------GRRAGEYSGGMRRRLDIAMSLVGD 142
Cdd:COG1117 100 kpnpFP-----KSIYDNVAYGLRLHGIKSKSELDE--IVEESLRKAAlwdevkdrlKKSALGLSGGQQQRLCIARALAVE 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2794531883 143 PPVIFLDEPTTGLDPQARAEVWRTVKQLADgGTTVLLTTQYLDEAEQLADRIAILHEGRII 203
Cdd:COG1117 173 PEVLLMDEPTSALDPISTAKIEELILELKK-DYTIVIVTHNMQQAARVSDYTAFFYLGELV 232
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
13-215 |
1.02e-14 |
|
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: 72.91 E-value: 1.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 13 GVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGHDV--------AAAAGRVRESISLTGQFAAVDEVLT 84
Cdd:TIGR03269 302 NVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRVGDEwvdmtkpgPDGRGRAKRYIGILHQEYDLYPHRT 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 85 GRENLVLVARLrHLPDPGAVaddMLARFSLTDAG----------GRRAGEYSGGMRRRLDIAMSLVGDPPVIFLDEPTTG 154
Cdd:TIGR03269 382 VLDNLTEAIGL-ELPDELAR---MKAVITLKMVGfdeekaeeilDKYPDELSEGERHRVALAQVLIKEPRIVILDEPTGT 457
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2794531883 155 LDPQARAEVWRTV-KQLADGGTTVLLTTQYLDEAEQLADRIAILHEGRIIQNGTLAELKRLL 215
Cdd:TIGR03269 458 MDPITKVDVTHSIlKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEEIVEEL 519
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
12-209 |
1.22e-14 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 72.78 E-value: 1.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 12 RGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGHDVAAAAGRVR---------ESISLTGQFaaVDEV 82
Cdd:PRK15439 280 RNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRlarglvylpEDRQSSGLY--LDAP 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 83 LTGRENLVLVARLRHLPDPG---AVADDMLA----RFSLTDAGGRRageYSGGMRRRLDIAMSLVGDPPVIFLDEPTTGL 155
Cdd:PRK15439 358 LAWNVCALTHNRRGFWIKPArenAVLERYRRalniKFNHAEQAART---LSGGNQQKVLIAKCLEASPQLLIVDEPTRGV 434
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2794531883 156 DPQARAEVWRTVKQLADGGTTVLLTTQYLDEAEQLADRIAILHEGRIiqNGTLA 209
Cdd:PRK15439 435 DVSARNDIYQLIRSIAAQNVAVLFISSDLEEIEQMADRVLVMHQGEI--SGALT 486
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
11-207 |
1.45e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 71.32 E-value: 1.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 11 LRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGHDVAAAAGR-VRESISLT---------GQFAAVD 80
Cdd:PRK13648 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEkLRKHIGIVfqnpdnqfvGSIVKYD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 81 eVLTGRENLVLVARLRHLPDPGAVAD-DMLARfsltdaGGRRAGEYSGGMRRRLDIAMSLVGDPPVIFLDEPTTGLDPQA 159
Cdd:PRK13648 105 -VAFGLENHAVPYDEMHRRVSEALKQvDMLER------ADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDA 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2794531883 160 RAEVWRTVKQL-ADGGTTVLLTTQYLDEAEQlADRIAILHEGRIIQNGT 207
Cdd:PRK13648 178 RQNLLDLVRKVkSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGT 225
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
123-204 |
2.01e-14 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 72.12 E-value: 2.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 123 GEYSGGMRRRLDIAMSLVGDPPVIFLDEPTTGLDPQARAEVWRTVKQLADGGTTVLLTTQYLDEAEQLADRIAILHEGRI 202
Cdd:PRK09700 408 TELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRL 487
|
..
gi 2794531883 203 IQ 204
Cdd:PRK09700 488 TQ 489
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
10-213 |
2.22e-14 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 70.59 E-value: 2.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 10 VLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGHDVAAAAGRV--RESISLTGQFAAVdEVLTGRE 87
Cdd:PRK10575 26 LLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAfaRKVAYLPQQLPAA-EGMTVRE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 88 nLVLVARLrhlPDPGAVA----------DDMLARFSLTDAGGRRAGEYSGGMRRRLDIAMSLVGDPPVIFLDEPTTGLDP 157
Cdd:PRK10575 105 -LVAIGRY---PWHGALGrfgaadrekvEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDI 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2794531883 158 QARAEVWRTVKQLA-DGGTTVLLTTQYLDEAEQLADRIAILHEGRIIQNGTLAELKR 213
Cdd:PRK10575 181 AHQVDVLALVHRLSqERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMR 237
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1-212 |
2.63e-14 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 70.56 E-value: 2.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 1 MRKSYGELDVLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGHDVAAAAGR----VRESISLTGQF 76
Cdd:PRK11831 13 VSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSrlytVRKRMSMLFQS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 77 AAVDEVLTGRENLVLVARLR-HLPDPGAVADDM--LARFSLTDAGGRRAGEYSGGMRRRLDIAMSLVGDPPVIFLDEPTT 153
Cdd:PRK11831 93 GALFTDMNVFDNVAYPLREHtQLPAPLLHSTVMmkLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFV 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 154 GLDPQARAEVWRTVKQLADG-GTTVLLTTQYLDEAEQLADRIAILHEGRIIQNGTLAELK 212
Cdd:PRK11831 173 GQDPITMGVLVKLISELNSAlGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQ 232
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
3-241 |
3.06e-14 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 71.68 E-value: 3.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 3 KSYGELDVLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGHDV-------AAAAG--RVRESISLT 73
Cdd:PRK10982 6 KSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIdfksskeALENGisMVHQELNLV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 74 GQFAAVDEVLTGRENL--VLVARLRHLPDPGAVADDMLARFSLTDaggrRAGEYSGGMRRRLDIAMSLVGDPPVIFLDEP 151
Cdd:PRK10982 86 LQRSVMDNMWLGRYPTkgMFVDQDKMYRDTKAIFDELDIDIDPRA----KVATLSVSQMQMIEIAKAFSYNAKIVIMDEP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 152 TTGLDPQARAEVWRTVKQLADGGTTVLLTTQYLDEAEQLADRIAILHEGRIIQNGTLAELK----------RLLpsaTVE 221
Cdd:PRK10982 162 TSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQWIATQPLAGLTmdkiiammvgRSL---TQR 238
|
250 260
....*....|....*....|
gi 2794531883 222 YVEKQPTLEEVFLAVVGETD 241
Cdd:PRK10982 239 FPDKENKPGEVILEVRNLTS 258
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
3-203 |
3.87e-14 |
|
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: 71.39 E-value: 3.87e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 3 KSYGELDVLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGHDVAAAAGRVRES----ISLTGQFAA 78
Cdd:TIGR02633 9 KTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTWDGEIYWSGSPLKASNIRDTeragIVIIHQELT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 79 VDEVLTGRENLVLVARLRHlpdPGAVADD---------MLARFSLTDAG-GRRAGEYSGGMRRRLDIAMSLVGDPPVIFL 148
Cdd:TIGR02633 89 LVPELSVAENIFLGNEITL---PGGRMAYnamylraknLLRELQLDADNvTRPVGDYGGGQQQLVEIAKALNKQARLLIL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2794531883 149 DEPTTGLDPQARAEVWRTVKQLADGGTTVLLTTQYLDEAEQLADRIAILHEGRII 203
Cdd:TIGR02633 166 DEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQHV 220
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
4-211 |
4.55e-14 |
|
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: 71.31 E-value: 4.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 4 SYGELD-VLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGHDVAA-AAGRVRESISLTGQ--FAAV 79
Cdd:TIGR01193 482 SYGYGSnILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDiDRHTLRQFINYLPQepYIFS 561
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 80 DEVLtgrENLVLVARlrhlpdPGAVADDMLARFSLTDAG--------------GRRAGEYSGGMRRRLDIAMSLVGDPPV 145
Cdd:TIGR01193 562 GSIL---ENLLLGAK------ENVSQDEIWAACEIAEIKddienmplgyqtelSEEGSSISGGQKQRIALARALLTDSKV 632
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2794531883 146 IFLDEPTTGLDPQARAEVWRTVKQLADggTTVLLTTQYLDEAEQlADRIAILHEGRIIQNGTLAEL 211
Cdd:TIGR01193 633 LILDESTSNLDTITEKKIVNNLLNLQD--KTIIFVAHRLSVAKQ-SDKIIVLDHGKIIEQGSHDEL 695
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
3-201 |
6.02e-14 |
|
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: 67.09 E-value: 6.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 3 KSYGELDVLRGVDLGVAPGTIHALLGSNGAGKTTLVKILstlvradagtasvqghdvaaaAGRVResisltgqfaavdev 82
Cdd:cd03221 8 KTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLI---------------------AGELE--------------- 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 83 ltgrenlvlvarlrhlPDPGAVADDMLARFSLTDaggrragEYSGGMRRRLDIAMSLVGDPPVIFLDEPTTGLDPQARAE 162
Cdd:cd03221 52 ----------------PDEGIVTWGSTVKIGYFE-------QLSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEA 108
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2794531883 163 VWRTVKQLADggtTVLLTT---QYLDeaeQLADRIAILHEGR 201
Cdd:cd03221 109 LEEALKEYPG---TVILVShdrYFLD---QVATKIIELEDGK 144
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
10-207 |
6.20e-14 |
|
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: 68.59 E-value: 6.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 10 VLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGHDVAAAA-GRVRESISLTGQfaavDEVL---TG 85
Cdd:cd03369 23 VLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPlEDLRSSLTIIPQ----DPTLfsgTI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 86 RENLvlvarlrhlpDPGAVADDMLARFSLTDAGGrrAGEYSGGMRRRLDIAMSLVGDPPVIFLDEPTTGLDPQARAEVWR 165
Cdd:cd03369 99 RSNL----------DPFDEYSDEEIYGALRVSEG--GLNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDALIQK 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2794531883 166 TVKQLADGGTTVLLttqyldeAEQLA-----DRIAILHEGRIIQNGT 207
Cdd:cd03369 167 TIREEFTNSTILTI-------AHRLRtiidyDKILVMDAGEVKEYDH 206
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
10-213 |
8.41e-14 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 69.09 E-value: 8.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 10 VLRGVDLGVAPGTIHALLGSNGAGKTTLVKILstlvrADAGTASVQGHDVaaaagRVRESISLTGQ-FAAVDEVLTGR-- 86
Cdd:PRK13547 16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLKAL-----AGDLTGGGAPRGA-----RVTGDVTLNGEpLAAIDAPRLARlr 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 87 ---------------ENLVLVARLRHLPDPGA-------VADDMLARFSLTDAGGRRAGEYSGGMRRRLDIAMSL----- 139
Cdd:PRK13547 86 avlpqaaqpafafsaREIVLLGRYPHARRAGAlthrdgeIAWQALALAGATALVGRDVTTLSGGELARVQFARVLaqlwp 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2794531883 140 ----VGDPPVIFLDEPTTGLDPQARAEVWRTVKQLA-DGGTTVLLTTQYLDEAEQLADRIAILHEGRIIQNGTLAELKR 213
Cdd:PRK13547 166 phdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLArDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPADVLT 244
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
14-202 |
9.81e-14 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 69.94 E-value: 9.81e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 14 VDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGHDVAAAAGR--VRESISLTGQ---FAAVDEVLTGREN 88
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRdaIRAGIMLCPEdrkAEGIIPVHSVADN 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 89 LVLVARLRHLP-----DPG---AVADDMLARFSLTDAGGRRA-GEYSGGMRRRLDIAMSLVGDPPVIFLDEPTTGLDPQA 159
Cdd:PRK11288 352 INISARRHHLRagcliNNRweaENADRFIRSLNIKTPSREQLiMNLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGA 431
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2794531883 160 RAEVWRTVKQLADGGTTVLLTTQYLDEAEQLADRIAILHEGRI 202
Cdd:PRK11288 432 KHEIYNVIYELAAQGVAVLFVSSDLPEVLGVADRIVVMREGRI 474
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
3-211 |
1.05e-13 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 69.67 E-value: 1.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 3 KSYGELDVLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQG---HDVAAA---AGRVRESISLTGQF 76
Cdd:PRK11000 11 KAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEkrmNDVPPAergVGMVFQSYALYPHL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 77 AAVDEV-----LTGRENLVLVARLRHlpdpgavADDMLARFSLTDaggRRAGEYSGGMRRRLDIAMSLVGDPPVIFLDEP 151
Cdd:PRK11000 91 SVAENMsfglkLAGAKKEEINQRVNQ-------VAEVLQLAHLLD---RKPKALSGGQRQRVAIGRTLVAEPSVFLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2794531883 152 TTGLDP----QARAEVWRTVKQLadgGTTVLLTTQYLDEAEQLADRIAILHEGRIIQNGTLAEL 211
Cdd:PRK11000 161 LSNLDAalrvQMRIEISRLHKRL---GRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLEL 221
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
3-213 |
1.22e-13 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 69.36 E-value: 1.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 3 KSYGELDVLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGHDVAAAAGRVREsISLTGQFAAVDEV 82
Cdd:PRK11432 14 KRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQRD-ICMVFQSYALFPH 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 83 LTGRENLVLVARLRHLPDPGAVA--DDMLARFSLTDAGGRRAGEYSGGMRRRLDIAMSLVGDPPVIFLDEPTTGLDPQAR 160
Cdd:PRK11432 93 MSLGENVGYGLKMLGVPKEERKQrvKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDANLR 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2794531883 161 AEVWRTVKQLADG-GTTVLLTTQYLDEAEQLADRIAILHEGRIIQNGTLAELKR 213
Cdd:PRK11432 173 RSMREKIRELQQQfNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYR 226
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
12-246 |
1.30e-13 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 69.65 E-value: 1.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 12 RGVDLGVApgtihallGSNGAGKTTLVKILSTLVRADAGTASVQGHDV-------AAAAGRVRESISLTGqfaavDEVLT 84
Cdd:PRK10762 277 KGEILGVS--------GLMGAGRTELMKVLYGALPRTSGYVTLDGHEVvtrspqdGLANGIVYISEDRKR-----DGLVL 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 85 G---RENLVLVA---------RLRHLPDPGAVaDDMLARFSL-TDAGGRRAGEYSGGMRRRLDIAMSLVGDPPVIFLDEP 151
Cdd:PRK10762 344 GmsvKENMSLTAlryfsraggSLKHADEQQAV-SDFIRLFNIkTPSMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEP 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 152 TTGLDPQARAEVWRTVKQLADGGTTVLLTTQYLDEAEQLADRIAILHEGRIiqngtlaelkrllpsaTVEYVEKQPTLEE 231
Cdd:PRK10762 423 TRGVDVGAKKEIYQLINQFKAEGLSIILVSSEMPEVLGMSDRILVMHEGRI----------------SGEFTREQATQEK 486
|
250
....*....|....*
gi 2794531883 232 VFLAVVGETDGSASA 246
Cdd:PRK10762 487 LMAAAVGKLNRVNQE 501
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
1-214 |
1.58e-13 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 67.89 E-value: 1.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 1 MRKSYGELDVLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTL--VRADAGTASVQGHDVAAAA--GRVRESISLTGQF 76
Cdd:PRK09580 7 LHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKDLLELSpeDRAGEGIFMAFQY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 77 A----AVDEVLTGRENLVLVARLRHLP--DPGAVADDMLARFSL----TDAGGRRAGE-YSGGMRRRLDIAMSLVGDPPV 145
Cdd:PRK09580 87 PveipGVSNQFFLQTALNAVRSYRGQEplDRFDFQDLMEEKIALlkmpEDLLTRSVNVgFSGGEKKRNDILQMAVLEPEL 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2794531883 146 IFLDEPTTGLDPQARAEVWRTVKQLADGGTTVLLTTQY---LDEAEqlADRIAILHEGRIIQNGTLAELKRL 214
Cdd:PRK09580 167 CILDESDSGLDIDALKIVADGVNSLRDGKRSFIIVTHYqriLDYIK--PDYVHVLYQGRIVKSGDFTLVKQL 236
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
11-211 |
2.29e-13 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 69.28 E-value: 2.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 11 LRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGHDVAA-AAGRVRESISLTGQ-------------- 75
Cdd:PRK11176 359 LRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDyTLASLRNQVALVSQnvhlfndtiannia 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 76 FAAVDEVltGRENLVLVARLRHlpdpgavADDMLARFS--LTDAGGRRAGEYSGGMRRRLDIAMSLVGDPPVIFLDEPTT 153
Cdd:PRK11176 439 YARTEQY--SREQIEEAARMAY-------AMDFINKMDngLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATS 509
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2794531883 154 GLDPQARAEVWRTVKQLADgGTTVLLTTQYLDEAEQlADRIAILHEGRIIQNGTLAEL 211
Cdd:PRK11176 510 ALDTESERAIQAALDELQK-NRTSLVIAHRLSTIEK-ADEILVVEDGEIVERGTHAEL 565
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
4-181 |
4.99e-13 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 66.03 E-value: 4.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 4 SYGELDVLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGHDvAAAAGRVREsISLTGQFAAVDEVL 83
Cdd:PRK13543 20 SRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKT-ATRGDRSRF-MAYLGHLPGLKADL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 84 TGRENLVLVARLrHLPDPGAVADDMLARFSLTDAGGRRAGEYSGGMRRRLDIAMSLVGDPPVIFLDEPTTGLDPQARAEV 163
Cdd:PRK13543 98 STLENLHFLCGL-HGRRAKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEGITLV 176
|
170
....*....|....*...
gi 2794531883 164 WRTVKQLADGGTTVLLTT 181
Cdd:PRK13543 177 NRMISAHLRGGGAALVTT 194
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
4-225 |
6.44e-13 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 66.20 E-value: 6.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 4 SYGELDVLRGVDLGVAPGTIHALLGSNGAGKTTLVKILstlvradAGTAS---------VQGHDV--AAAAGRVRESISL 72
Cdd:CHL00131 16 SVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVI-------AGHPAykilegdilFKGESIldLEPEERAHLGIFL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 73 TGQFAAvdEVlTGREN-----LVLVARLRHLPDPGAvadDMLARFSLTDAG-----------GRRAGE-YSGGMRRRLDI 135
Cdd:CHL00131 89 AFQYPI--EI-PGVSNadflrLAYNSKRKFQGLPEL---DPLEFLEIINEKlklvgmdpsflSRNVNEgFSGGEKKRNEI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 136 -AMSLVgDPPVIFLDEPTTGLDPQARAEVWRTVKQLADGGTTVLLTTQY---LDEAEqlADRIAILHEGRIIQNGTlAEL 211
Cdd:CHL00131 163 lQMALL-DSELAILDETDSGLDIDALKIIAEGINKLMTSENSIILITHYqrlLDYIK--PDYVHVMQNGKIIKTGD-AEL 238
|
250
....*....|....
gi 2794531883 212 KRLLPSATVEYVEK 225
Cdd:CHL00131 239 AKELEKKGYDWLKQ 252
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
7-193 |
6.92e-13 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 65.96 E-value: 6.92e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 7 ELDVLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGHDVAAAAGRVR-----ESISLTGQFAAVDE 81
Cdd:PRK10584 22 ELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARaklraKHVGFVFQSFMLIP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 82 VLTGRENLVLVARLRHLPDPGA--VADDMLARFSLTDAGGRRAGEYSGGMRRRLDIAMSLVGDPPVIFLDEPTTGLDPQA 159
Cdd:PRK10584 102 TLNALENVELPALLRGESSRQSrnGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQT 181
|
170 180 190
....*....|....*....|....*....|....*
gi 2794531883 160 RAEVWRTVKQL-ADGGTTVLLTTQyldeAEQLADR 193
Cdd:PRK10584 182 GDKIADLLFSLnREHGTTLILVTH----DLQLAAR 212
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
7-206 |
7.26e-13 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 67.83 E-value: 7.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 7 ELDVLRGVDLGVAPGTIHALLGSNGAGKTTLVKILST----LVRADAGTASVQGHDVAAAAGRVRESISLTGQFAAVDEV 82
Cdd:TIGR00956 73 TFDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASntdgFHIGVEGVITYDGITPEEIKKHYRGDVVYNAETDVHFPH 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 83 LTGRENLVLVARLRhlpDPG-------------AVADDMLARFSLTDAGGRRAGE-----YSGGMRRRLDIAMSLVGDPP 144
Cdd:TIGR00956 153 LTVGETLDFAARCK---TPQnrpdgvsreeyakHIADVYMATYGLSHTRNTKVGNdfvrgVSGGERKRVSIAEASLGGAK 229
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2794531883 145 VIFLDEPTTGLDPQARAEVWRTVKQLAD-GGTTVLLTT-QYLDEAEQLADRIAILHEGRIIQNG 206
Cdd:TIGR00956 230 IQCWDNATRGLDSATALEFIRALKTSANiLDTTPLVAIyQCSQDAYELFDKVIVLYEGYQIYFG 293
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-211 |
4.67e-12 |
|
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: 65.09 E-value: 4.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 1 MRKSYGELDVLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADaGTASVQGHDVAAAAGR----VRESISLTGQ- 75
Cdd:COG4172 292 FRRTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIPSE-GEIRFDGQDLDGLSRRalrpLRRRMQVVFQd 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 76 -FAA------VDEVLTgrENLVLvarlrHLPDPGAVADDMLARFSLTDAG------GRRAGEYSGGMRRRLDIAMSLVGD 142
Cdd:COG4172 371 pFGSlsprmtVGQIIA--EGLRV-----HGPGLSAAERRARVAEALEEVGldpaarHRYPHEFSGGQRQRIAIARALILE 443
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 143 PPVIFLDEPTTGLDPQARAEVWRTVKQL-ADGGTTVLLTTQYLDEAEQLADRIAILHEGRIIQNGTLAEL 211
Cdd:COG4172 444 PKLLVLDEPTSALDVSVQAQILDLLRDLqREHGLAYLFISHDLAVVRALAHRVMVMKDGKVVEQGPTEQV 513
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-223 |
9.63e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 63.13 E-value: 9.63e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 4 SYGELDVLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADaGTASVQG---------HDVAAAAGRVRESISLTG 74
Cdd:PRK14258 16 YYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELE-SEVRVEGrveffnqniYERRVNLNRLRRQVSMVH 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 75 Q------FAAVDEVLTGrenlVLVARLRHLPDPGAVADDMLARFSLTDAGGRR----AGEYSGGMRRRLDIAMSLVGDPP 144
Cdd:PRK14258 95 PkpnlfpMSVYDNVAYG----VKIVGWRPKLEIDDIVESALKDADLWDEIKHKihksALDLSGGQQQRLCIARALAVKPK 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 145 VIFLDEPTTGLDPQARAEVWRTVKQLA-DGGTTVLLTTQYLDEAEQLADRIAILH--EGRIIQNGTLAELKRLL----PS 217
Cdd:PRK14258 171 VLLMDEPCFGLDPIASMKVESLIQSLRlRSELTMVIVSHNLHQVSRLSDFTAFFKgnENRIGQLVEFGLTKKIFnsphDS 250
|
....*.
gi 2794531883 218 ATVEYV 223
Cdd:PRK14258 251 RTREYV 256
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
25-213 |
1.05e-11 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 64.10 E-value: 1.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 25 ALLGSNGAGKTTLVKILSTLVrADAGTASVQGHDVAA-AAGRVRESISLTGQ----FAAvdevlTGRENLVLV------A 93
Cdd:PRK11174 380 ALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRElDPESWRKHLSWVGQnpqlPHG-----TLRDNVLLGnpdasdE 453
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 94 RLRHLPDPgAVADDMLARFS--LTDAGGRRAGEYSGGMRRRLDIAMSLVGDPPVIFLDEPTTGLDPQARAEVWRTVKQLA 171
Cdd:PRK11174 454 QLQQALEN-AWVSEFLPLLPqgLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAAS 532
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2794531883 172 DGGTTVLLTTQyLDEAEQLaDRIAILHEGRIIQNGTLAELKR 213
Cdd:PRK11174 533 RRQTTLMVTHQ-LEDLAQW-DQIWVMQDGQIVQQGDYAELSQ 572
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
20-198 |
1.16e-11 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 64.04 E-value: 1.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 20 PGTIHALLGSNGAGKTTLVKILS-----------------TLVRADAGTAsVQGHDVAAAAGRVResISLTGQFaaVD-- 80
Cdd:COG1245 98 KGKVTGILGPNGIGKSTALKILSgelkpnlgdydeepswdEVLKRFRGTE-LQDYFKKLANGEIK--VAHKPQY--VDli 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 81 -EVLTGRenlvlVARLRHLPDPGAVADDMLARFSLTDAGGRRAGEYSGGMRRRLDIAMSLVGDPPVIFLDEPTTGLDPQA 159
Cdd:COG1245 173 pKVFKGT-----VRELLEKVDERGKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIYQ 247
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2794531883 160 RAEVWRTVKQLADGGTTVL-----LTTqyLDeaeQLADRIAILH 198
Cdd:COG1245 248 RLNVARLIRELAEEGKYVLvvehdLAI--LD---YLADYVHILY 286
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
13-211 |
1.45e-11 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 63.21 E-value: 1.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 13 GVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGHDVAAAAGR----VRESISLTGQ--FAAVDEVLTGR 86
Cdd:COG4608 36 GVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRelrpLRRRMQMVFQdpYASLNPRMTVG 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 87 ENLVLVARLRHLPDPGAVAD---DMLARFSL-TDAGGRRAGEYSGGMRRRLDIAMSLVGDPPVIFLDEPTTGLDPQARAE 162
Cdd:COG4608 116 DIIAEPLRIHGLASKAERRErvaELLELVGLrPEHADRYPHEFSGGQRQRIGIARALALNPKLIVCDEPVSALDVSIQAQ 195
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2794531883 163 VWRTVKQL-ADGGTTVLLTTQYLDEAEQLADRIAILHEGRIIQNGTLAEL 211
Cdd:COG4608 196 VLNLLEDLqDELGLTYLFISHDLSVVRHISDRVAVMYLGKIVEIAPRDEL 245
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
4-225 |
1.58e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 63.99 E-value: 1.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 4 SYGELDVLRGVDLGVAPGTIHALLGSNGAGKTTLVK-ILSTLVRADAGTASVQGhDVAAAA-------GRVRESISLTGQ 75
Cdd:PLN03130 626 SKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISaMLGELPPRSDASVVIRG-TVAYVPqvswifnATVRDNILFGSP 704
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 76 FAAVDevltgRENLVLVARLRHlpdpgavaD-DMLARFSLTDAGgRRAGEYSGGMRRRLDIAMSLVGDPPVIFLDEPTTG 154
Cdd:PLN03130 705 FDPER-----YERAIDVTALQH--------DlDLLPGGDLTEIG-ERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSA 770
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 155 LDPQARAEVWRT-VKQLADGGTTVLLTTQ--YLDEaeqlADRIAILHEGRIIQNGTLAEL-------KRLLPSA--TVEY 222
Cdd:PLN03130 771 LDAHVGRQVFDKcIKDELRGKTRVLVTNQlhFLSQ----VDRIILVHEGMIKEEGTYEELsnngplfQKLMENAgkMEEY 846
|
...
gi 2794531883 223 VEK 225
Cdd:PLN03130 847 VEE 849
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
10-211 |
1.59e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 62.37 E-value: 1.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 10 VLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGH------DV-AAAAGRVRESISLTGQFAAVDEV 82
Cdd:PRK14246 25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKvlyfgkDIfQIDAIKLRKEVGMVFQQPNPFPH 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 83 LTGRENLVLVARLRHLPDP---GAVADDMLARFSL----TDAGGRRAGEYSGGMRRRLDIAMSLVGDPPVIFLDEPTTGL 155
Cdd:PRK14246 105 LSIYDNIAYPLKSHGIKEKreiKKIVEECLRKVGLwkevYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSMI 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2794531883 156 DPQARAEVWRTVKQLADgGTTVLLTTQYLDEAEQLADRIAILHEGRIIQNGTLAEL 211
Cdd:PRK14246 185 DIVNSQAIEKLITELKN-EIAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEI 239
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
7-183 |
2.04e-11 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 61.51 E-value: 2.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 7 ELDVLRGVDLGVAPGTIHALLGSNGAGKTTLvkiLSTLVRADAGTASVQGHDVaaaagrvresisLTGQFAavdevltgr 86
Cdd:COG2401 42 ERYVLRDLNLEIEPGEIVLIVGASGSGKSTL---LRLLAGALKGTPVAGCVDV------------PDNQFG--------- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 87 ENLVLVARLRHLPDPGAVAdDMLARFSLTDAGG--RRAGEYSGGMRRRLDIAMSLVGDPPVIFLDEPTTGLDPQARAEVW 164
Cdd:COG2401 98 REASLIDAIGRKGDFKDAV-ELLNAVGLSDAVLwlRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVA 176
|
170 180
....*....|....*....|.
gi 2794531883 165 RTVKQLAD--GGTTVLLTTQY 183
Cdd:COG2401 177 RNLQKLARraGITLVVATHHY 197
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
11-213 |
2.09e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 63.46 E-value: 2.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 11 LRGVDLGVAPGTIHALLGSNGAGKTTLVK-ILSTLVRADAGTASVQGhDVAAAA-------GRVRESISLTGQFA----- 77
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISaMLGELSHAETSSVVIRG-SVAYVPqvswifnATVRENILFGSDFEseryw 711
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 78 -AVDevltgrenlvlVARLRHlpdpgavaD-DMLARFSLTDAGgRRAGEYSGGMRRRLDIAMSLVGDPPVIFLDEPTTGL 155
Cdd:PLN03232 712 rAID-----------VTALQH--------DlDLLPGRDLTEIG-ERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSAL 771
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2794531883 156 DPQARAEVWRT-VKQLADGGTTVLLTTQ--YLdeaeQLADRIAILHEGRIIQNGTLAELKR 213
Cdd:PLN03232 772 DAHVAHQVFDScMKDELKGKTRVLVTNQlhFL----PLMDRIILVSEGMIKEEGTFAELSK 828
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
123-202 |
2.36e-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: 62.92 E-value: 2.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 123 GEYSGGMRRRLDIAMSLVGDPPVIFLDEPTTGLDPQARAEVWRTVKQLADGGTTVLLTTQYLDEAEQLADRIAILHEGRI 202
Cdd:TIGR02633 402 GRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGKL 481
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
1-156 |
3.04e-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: 62.65 E-value: 3.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 1 MRKSYGELDVLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASV----------QGHDVAAAAGRVRESI 70
Cdd:TIGR03719 328 LTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIgetvklayvdQSRDALDPNKTVWEEI 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 71 SlTGQfaavDEVLTGRenlvlvarlRHLPDPGAVaddmlARFSLTDAG-GRRAGEYSGGMRRRLDIAMSLVGDPPVIFLD 149
Cdd:TIGR03719 408 S-GGL----DIIKLGK---------REIPSRAYV-----GRFNFKGSDqQKKVGQLSGGERNRVHLAKTLKSGGNVLLLD 468
|
....*..
gi 2794531883 150 EPTTGLD 156
Cdd:TIGR03719 469 EPTNDLD 475
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
5-182 |
4.89e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 60.35 E-value: 4.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 5 YGELDVLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGHDVAAAAGRVRESISLTGQFAAVDEVLT 84
Cdd:PRK13540 11 YHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKQLCFVGHRSGINPYLT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 85 GRENLVLVArlrHLPDPGAVADDMLARFSLTDAGGRRAGEYSGGMRRRLDIAMSLVGDPPVIFLDEPTTGLDPQARAEVW 164
Cdd:PRK13540 91 LRENCLYDI---HFSPGAVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTII 167
|
170
....*....|....*...
gi 2794531883 165 RTVKQLADGGTTVLLTTQ 182
Cdd:PRK13540 168 TKIQEHRAKGGAVLLTSH 185
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
3-211 |
6.13e-11 |
|
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: 61.74 E-value: 6.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 3 KSYGELDVLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGH-DVAAAAGRVrESISLTGQ------ 75
Cdd:TIGR03269 8 KKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQYEPTSGRIIYHvALCEKCGYV-ERPSKVGEpcpvcg 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 76 ---------FAAVDEVLTGR-----------------ENLVLVARLRHLPDPGAVADDMLAR----FSLTDAGGRR---A 122
Cdd:TIGR03269 87 gtlepeevdFWNLSDKLRRRirkriaimlqrtfalygDDTVLDNVLEALEEIGYEGKEAVGRavdlIEMVQLSHRIthiA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 123 GEYSGGMRRRLDIAMSLVGDPPVIFLDEPTTGLDPQARAEVWRTVKQLA-DGGTTVLLTTQYLDEAEQLADRIAILHEGR 201
Cdd:TIGR03269 167 RDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVkASGISMVLTSHWPEVIEDLSDKAIWLENGE 246
|
250
....*....|
gi 2794531883 202 IIQNGTLAEL 211
Cdd:TIGR03269 247 IKEEGTPDEV 256
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
10-216 |
6.80e-11 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 61.03 E-value: 6.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 10 VLRGVDLGVAPGTIHALLGSNGAGKTTLVK-ILSTLVradagtasvqghdvaAAAGRVRES--ISLTGQFAAVDEVlTGR 86
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMlILGELE---------------PSEGKIKHSgrISFSSQFSWIMPG-TIK 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 87 ENLVLVA-----RLRHLPDPGAVADDmLARFSLTDAG--GRRAGEYSGGMRRRLDIAMSLVGDPPVIFLDEPTTGLDPQA 159
Cdd:cd03291 116 ENIIFGVsydeyRYKSVVKACQLEED-ITKFPEKDNTvlGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFT 194
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2794531883 160 RAEVWRT-VKQLADGGTTVLLTTQYldEAEQLADRIAILHEGRIIQNGTLAELKRLLP 216
Cdd:cd03291 195 EKEIFEScVCKLMANKTRILVTSKM--EHLKKADKILILHEGSSYFYGTFSELQSLRP 250
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
7-206 |
1.04e-10 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 61.41 E-value: 1.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 7 ELDVLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGHDVAAAAGR----VRESISLTGQ--FAAVD 80
Cdd:PRK10261 336 EVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGklqaLRRDIQFIFQdpYASLD 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 81 EVLTGRENLVLVARLRHLPDPGAVADD---MLARFSLT-DAGGRRAGEYSGGMRRRLDIAMSLVGDPPVIFLDEPTTGLD 156
Cdd:PRK10261 416 PRQTVGDSIMEPLRVHGLLPGKAAAARvawLLERVGLLpEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALD 495
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2794531883 157 PQARAEVWRTVKQLA-DGGTTVLLTTQYLDEAEQLADRIAILHEGRIIQNG 206
Cdd:PRK10261 496 VSIRGQIINLLLDLQrDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIG 546
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
126-202 |
1.11e-10 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 61.10 E-value: 1.11e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2794531883 126 SGGMRRRLDIAMSLVGDPPVIFLDEPTTGLDPQARAEVWRTVKQLADGGTTVLLTTQYLDEAEQLADRIAILHEGRI 202
Cdd:PRK13549 407 SGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQGVAIIVISSELPEVLGLSDRVLVMHEGKL 483
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
6-213 |
1.14e-10 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 61.02 E-value: 1.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 6 GELDVLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGHDVAAaagRVRESISLTGQFAA------- 78
Cdd:PRK10261 27 QKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRR---RSRQVIELSEQSAAqmrhvrg 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 79 -------------VDEVLTGRENLVLVARLRH---LPDPGAVADDMLARFSLTDAG---GRRAGEYSGGMRRRLDIAMSL 139
Cdd:PRK10261 104 admamifqepmtsLNPVFTVGEQIAESIRLHQgasREEAMVEAKRMLDQVRIPEAQtilSRYPHQLSGGMRQRVMIAMAL 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2794531883 140 VGDPPVIFLDEPTTGLDPQARAEVWRTVKQL-ADGGTTVLLTTQYLDEAEQLADRIAILHEGRIIQNGTLAELKR 213
Cdd:PRK10261 184 SCRPAVLIADEPTTALDVTIQAQILQLIKVLqKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQIFH 258
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
4-170 |
1.18e-10 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 59.74 E-value: 1.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 4 SYGELDVLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASvqgHDVAAAAGRVRESISLtgqfaavDEVL 83
Cdd:PRK09544 13 SFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK---RNGKLRIGYVPQKLYL-------DTTL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 84 TgrenlVLVARLRHLpDPGAVADDMLARFSLTDAG---GRRAGEYSGGMRRRLDIAMSLVGDPPVIFLDEPTTGLDPQAR 160
Cdd:PRK09544 83 P-----LTVNRFLRL-RPGTKKEDILPALKRVQAGhliDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQ 156
|
170
....*....|
gi 2794531883 161 AEVWRTVKQL 170
Cdd:PRK09544 157 VALYDLIDQL 166
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
124-207 |
2.41e-10 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 59.74 E-value: 2.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 124 EYSGGMRRRLDIAMSLVGDPPVIFLDEPTTGLDPQARAEVWRTVKQLA-DGGTTVLLTTQYLDEAEQLADRIAILHEGRI 202
Cdd:PRK09473 161 EFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKrEFNTAIIMITHDLGVVAGICDKVLVMYAGRT 240
|
....*
gi 2794531883 203 IQNGT 207
Cdd:PRK09473 241 MEYGN 245
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
1-207 |
2.80e-10 |
|
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: 58.27 E-value: 2.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 1 MRKSYGELDVLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGHDVAA-AAGRVRESISLTGQfaav 79
Cdd:cd03244 10 LRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKiGLHDLRSRISIIPQ---- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 80 DEVL---TGRENLvlvarlrhlpDP-GAVADDMLAR---------FSLTDAGGRRA-----GE-YSGGMRRRLDIAMSLV 140
Cdd:cd03244 86 DPVLfsgTIRSNL----------DPfGEYSDEELWQalervglkeFVESLPGGLDTvveegGEnLSVGQRQLLCLARALL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2794531883 141 GDPPVIFLDEPTTGLDPQARAEVWRTVKQlADGGTTVL-----LTTqYLDeaeqlADRIAILHEGRIIQNGT 207
Cdd:cd03244 156 RKSKILVLDEATASVDPETDALIQKTIRE-AFKDCTVLtiahrLDT-IID-----SDRILVLDKGRVVEFDS 220
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
10-216 |
3.70e-10 |
|
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: 59.92 E-value: 3.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 10 VLRGVDLGVAPGTIHALLGSNGAGKTTLVK-ILSTLVRADagtasvqghdvaaaaGRVRES--ISLTGQFAAVDEVlTGR 86
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMmIMGELEPSE---------------GKIKHSgrISFSPQTSWIMPG-TIK 504
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 87 ENLVLVA-----RLRHLPDPGAVADDmLARFSLTDAG--GRRAGEYSGGMRRRLDIAMSLVGDPPVIFLDEPTTGLDPQA 159
Cdd:TIGR01271 505 DNIIFGLsydeyRYTSVIKACQLEED-IALFPEKDKTvlGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVT 583
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2794531883 160 RAEVW-RTVKQLADGGTTVLLTTQYldEAEQLADRIAILHEGRIIQNGTLAELKRLLP 216
Cdd:TIGR01271 584 EKEIFeSCLCKLMSNKTRILVTSKL--EHLKKADKILLLHEGVCYFYGTFSELQAKRP 639
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
1-173 |
6.82e-10 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 58.67 E-value: 6.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 1 MRKSYGeldvlrGVDLGVAPGTIHA-----LLGSNGAGKTTLVKILSTLVRADAGTASVQghdvaaaagrvrESISLTGQ 75
Cdd:PRK13409 346 LTKKLG------DFSLEVEGGEIYEgevigIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE------------LKISYKPQ 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 76 FAAVDEVLTGRENLvlvarlrhlpdpGAVADDM---------LARFSLTDAGGRRAGEYSGGMRRRLDIAMSLVGDPPVI 146
Cdd:PRK13409 408 YIKPDYDGTVEDLL------------RSITDDLgssyykseiIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLY 475
|
170 180
....*....|....*....|....*..
gi 2794531883 147 FLDEPTTGLDPQARAEVWRTVKQLADG 173
Cdd:PRK13409 476 LLDEPSAHLDVEQRLAVAKAIRRIAEE 502
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
11-211 |
9.26e-10 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 58.05 E-value: 9.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 11 LRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGHDVA----AAAGRVRESISLTGQ--FAA------ 78
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLkadpEAQKLLRQKIQIVFQnpYGSlnprkk 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 79 VDEVLTgrENLVLVARLRHlPDPGAVADDMLARFSL-TDAGGRRAGEYSGGMRRRLDIAMSLVGDPPVIFLDEPTTGLDP 157
Cdd:PRK11308 111 VGQILE--EPLLINTSLSA-AERREKALAMMAKVGLrPEHYDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALDV 187
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2794531883 158 QARAEVWRTVKQL-ADGGTTVLLTTQYLDEAEQLADRIAILHEGRIIQNGTLAEL 211
Cdd:PRK11308 188 SVQAQVLNLMMDLqQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQI 242
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
18-198 |
9.47e-10 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 57.38 E-value: 9.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 18 VAPGTIHALLGSNGAGKTTLVKILS-----------------TLVRADAGTAsVQGHDVAAAAGRVRESISLtgQFaaVD 80
Cdd:cd03236 23 PREGQVLGLVGPNGIGKSTALKILAgklkpnlgkfddppdwdEILDEFRGSE-LQNYFTKLLEGDVKVIVKP--QY--VD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 81 EV---LTGRENLVLVARlrhlpDPGAVADDMLARFSLTDAGGRRAGEYSGGMRRRLDIAMSLVGDPPVIFLDEPTTGLDP 157
Cdd:cd03236 98 LIpkaVKGKVGELLKKK-----DERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDI 172
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2794531883 158 QARAEVWRTVKQLADGGTTVLLTTQYLDEAEQLADRIAILH 198
Cdd:cd03236 173 KQRLNAARLIRELAEDDNYVLVVEHDLAVLDYLSDYIHCLY 213
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
2-211 |
9.67e-10 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 57.93 E-value: 9.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 2 RKSY-GELDVLRGVDLGVAPGTIHALLGSNGAGKttlvkilSTLVRADAGTASVQGHDVAAAAGRVRE------SISLTG 74
Cdd:PRK11650 10 RKSYdGKTQVIKGIDLDVADGEFIVLVGPSGCGK-------STLLRMVAGLERITSGEIWIGGRVVNElepadrDIAMVF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 75 QFAAVDEVLTGRENLVLVARLRHLPDPG-----AVADDMLARFSLTDaggRRAGEYSGGMRRRldIAM--SLVGDPPVIF 147
Cdd:PRK11650 83 QNYALYPHMSVRENMAYGLKIRGMPKAEieervAEAARILELEPLLD---RKPRELSGGQRQR--VAMgrAIVREPAVFL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2794531883 148 LDEPTTGLDP----QARAEVWRTVKQLadgGTTVLLTTQYLDEAEQLADRIAILHEGRIIQNGTLAEL 211
Cdd:PRK11650 158 FDEPLSNLDAklrvQMRLEIQRLHRRL---KTTSLYVTHDQVEAMTLADRVVVMNGGVAEQIGTPVEV 222
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
20-173 |
1.10e-09 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 58.28 E-value: 1.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 20 PGTIHALLGSNGAGKTTLVKILS-----------------TLVRADAGTAsVQGHDVAAAAGRVResISLTGQFaaVD-- 80
Cdd:PRK13409 98 EGKVTGILGPNGIGKTTAVKILSgelipnlgdyeeepswdEVLKRFRGTE-LQNYFKKLYNGEIK--VVHKPQY--VDli 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 81 -EVLTGRenlvlVARLRHLPDPGAVADDMLARFSLTDAGGRRAGEYSGGMRRRLDIAMSLVGDPPVIFLDEPTTGLDPQA 159
Cdd:PRK13409 173 pKVFKGK-----VRELLKKVDERGKLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRQ 247
|
170
....*....|....
gi 2794531883 160 RAEVWRTVKQLADG 173
Cdd:PRK13409 248 RLNVARLIRELAEG 261
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
1-207 |
1.30e-09 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 57.03 E-value: 1.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 1 MRKSYGELDvlrgvdLGVAPGTIH-----ALLGSNGAGKTTLVKILSTLVRADAGTASVQGHDVAAAAGRVRESISLTgq 75
Cdd:cd03237 6 MKKTLGEFT------LEVEGGSISeseviGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSYKPQYIKADYEGT-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 76 faaVDEVLTGRENlvlvarlRHLPDPGAVADDM--LARFSLTDaggRRAGEYSGGMRRRLDIAMSLVGDPPVIFLDEPTT 153
Cdd:cd03237 78 ---VRDLLSSITK-------DFYTHPYFKTEIAkpLQIEQILD---REVPELSGGELQRVAIAACLSKDADIYLLDEPSA 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2794531883 154 GLDPQARAEVWRTVKQLADGG-TTVLLTTQYLDEAEQLADRIaILHEGRIIQNGT 207
Cdd:cd03237 145 YLDVEQRLMASKVIRRFAENNeKTAFVVEHDIIMIDYLADRL-IVFEGEPSVNGV 198
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
8-217 |
1.83e-09 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 56.72 E-value: 1.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 8 LDVLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGH-----DVAAAAGRVR-----ESISLT---- 73
Cdd:PRK15112 26 VEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHplhfgDYSYRSQRIRmifqdPSTSLNprqr 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 74 -GQFAAVDEVL------TGRENLVlVARLRH---LPDPGAVADDMLArfsltdaggrrageysGGMRRRLDIAMSLVGDP 143
Cdd:PRK15112 106 iSQILDFPLRLntdlepEQREKQI-IETLRQvglLPDHASYYPHMLA----------------PGQKQRLGLARALILRP 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 144 PVIFLDEPTTGLDPQARAEVWRTVKQLADG-GTTVLLTTQYLDEAEQLADRIAILHEGRIIQNGTLAEL---------KR 213
Cdd:PRK15112 169 KVIIADEALASLDMSMRSQLINLMLELQEKqGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVlasplheltKR 248
|
....
gi 2794531883 214 LLPS 217
Cdd:PRK15112 249 LIAG 252
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
1-204 |
2.25e-09 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 57.11 E-value: 2.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 1 MR---KSYGELDVLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGHDVAAAAGRVRES----ISLT 73
Cdd:NF040905 4 MRgitKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGSYEGEILFDGEVCRFKDIRDSealgIVII 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 74 GQFAAVDEVLTGRENLVL---VARlRHLPDPGAV---ADDMLARFSLTDAGGRRAGEYSGGMRRRLDIAMSLVGDPPVIF 147
Cdd:NF040905 84 HQELALIPYLSIAENIFLgneRAK-RGVIDWNETnrrARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLI 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2794531883 148 LDEPTTGLDPQARAEVWRTVKQLADGGTTVLLTTQYLDEAEQLADRIAILHEGRIIQ 204
Cdd:NF040905 163 LDEPTAALNEEDSAALLDLLLELKAQGITSIIISHKLNEIRRVADSITVLRDGRTIE 219
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
126-211 |
2.81e-09 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 57.02 E-value: 2.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 126 SGGMRRRLDIAMSLVGDPPVIFLDEPTTGLDPQARAEVWRTVKQL-ADGGTTVLLTTQYLDEAEQLADRIAILHEGRIIQ 204
Cdd:PRK15134 158 SGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELqQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVE 237
|
....*..
gi 2794531883 205 NGTLAEL 211
Cdd:PRK15134 238 QNRAATL 244
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
5-160 |
6.01e-09 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 55.95 E-value: 6.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 5 YGELDVLRGVDLGVAPGTIHALLGSNGAGKTTLVKILstlvradAGTASVQGHDVAAAAGrvresISLtGQFAAVD-EVL 83
Cdd:PRK10636 322 YGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLL-------AGELAPVSGEIGLAKG-----IKL-GYFAQHQlEFL 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 84 TGREnlvlvARLRHLP-----DPGAVADDMLARF-----SLTDAGGRrageYSGGMRRRLDIAMSLVGDPPVIFLDEPTT 153
Cdd:PRK10636 389 RADE-----SPLQHLArlapqELEQKLRDYLGGFgfqgdKVTEETRR----FSGGEKARLVLALIVWQRPNLLLLDEPTN 459
|
....*..
gi 2794531883 154 GLDPQAR 160
Cdd:PRK10636 460 HLDLDMR 466
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
1-178 |
8.40e-09 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 55.56 E-value: 8.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 1 MRKSYGELDvlrgvdLGVAPGTIH-----ALLGSNGAGKTTLVKILSTLVRADAGTASVQghdvaaaagrvrESISLTGQ 75
Cdd:COG1245 347 LTKSYGGFS------LEVEGGEIRegevlGIVGPNGIGKTTFAKILAGVLKPDEGEVDED------------LKISYKPQ 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 76 FAAVDEVLTGRENLVlvarlrhlpdpGAVADDM---------LARFSLTDAGGRRAGEYSGGMRRRLDIAMSLVGDPPVI 146
Cdd:COG1245 409 YISPDYDGTVEEFLR-----------SANTDDFgssyykteiIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLY 477
|
170 180 190
....*....|....*....|....*....|...
gi 2794531883 147 FLDEPTTGLDPQARAEVWRTVKQLADG-GTTVL 178
Cdd:COG1245 478 LLDEPSAHLDVEQRLAVAKAIRRFAENrGKTAM 510
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
89-182 |
1.49e-08 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 54.32 E-value: 1.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 89 LVLVARLRHLPDPGAVADDMLARFSLTDAGGRRAGEYSGGMRRRLDIAMSLVGDPP---VIFLDEPTTGLDPQARAEVWR 165
Cdd:pfam13304 201 DLGEGIEKSLLVDDRLRERGLILLENGGGGELPAFELSDGTKRLLALLAALLSALPkggLLLIDEPESGLHPKLLRRLLE 280
|
90
....*....|....*..
gi 2794531883 166 TVKQLADGGTTVLLTTQ 182
Cdd:pfam13304 281 LLKELSRNGAQLILTTH 297
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
10-211 |
3.07e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 54.21 E-value: 3.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 10 VLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGHDVAA-AAGRVRESISLTGQfaavDEVL---TG 85
Cdd:PLN03232 1251 VLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKfGLTDLRRVLSIIPQ----SPVLfsgTV 1326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 86 RENLvlvarlrhlpDPGAVADD-----MLARFSLTDAGGR----------RAGE-YSGGMRRRLDIAMSLVGDPPVIFLD 149
Cdd:PLN03232 1327 RFNI----------DPFSEHNDadlweALERAHIKDVIDRnpfgldaevsEGGEnFSVGQRQLLSLARALLRRSKILVLD 1396
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2794531883 150 EPTTGLDPQARAEVWRTVKQLADgGTTVLLTTQYLDEAEQlADRIAILHEGRIIQNGTLAEL 211
Cdd:PLN03232 1397 EATASVDVRTDSLIQRTIREEFK-SCTMLVIAHRLNTIID-CDKILVLSSGQVLEYDSPQEL 1456
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
14-210 |
4.76e-08 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 52.95 E-value: 4.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 14 VDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGHD-VAAAAG-----------------------RVRES 69
Cdd:PRK11144 17 VNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVlFDAEKGiclppekrrigyvfqdarlfphyKVRGN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 70 I------SLTGQFAAVDEVLtGRENLvlvarlrhlpdpgavaddmLARFSLTdaggrrageYSGGMRRRLDIAMSLVGDP 143
Cdd:PRK11144 97 LrygmakSMVAQFDKIVALL-GIEPL-------------------LDRYPGS---------LSGGEKQRVAIGRALLTAP 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2794531883 144 PVIFLDEPTTGLD-PQARaEVWRTVKQLA-DGGTTVLLTTQYLDEAEQLADRIAILHEGRIIQNGTLAE 210
Cdd:PRK11144 148 ELLLMDEPLASLDlPRKR-ELLPYLERLArEINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEE 215
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
124-211 |
4.87e-08 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 52.88 E-value: 4.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 124 EYSGGMRRRLDIAMSLVGDPPVIFLDEPTTGLDPQARAEVWRTVKQL-ADGGTTVLLTTQYLDEAEQLADRIAILHEGRI 202
Cdd:PRK15093 158 ELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLnQNNNTTILLISHDLQMLSQWADKINVLYCGQT 237
|
....*....
gi 2794531883 203 IQNGTLAEL 211
Cdd:PRK15093 238 VETAPSKEL 246
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
18-233 |
8.41e-08 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 51.47 E-value: 8.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 18 VAPGTIHALLGSNGAGKTTLVKILSTLVRAdAGTASVQGHDVAA--AAGRVRESISLTGQ----FA-AVDEVLTgrenlv 90
Cdd:PRK03695 19 VRAGEILHLVGPNGAGKSTLLARMAGLLPG-SGSIQFAGQPLEAwsAAELARHRAYLSQQqtppFAmPVFQYLT------ 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 91 lvarlRHLPDPGAVAD------DMLARFSLTDAGGRRAGEYSGGMRRRLDIAMSLVGDPPVI-------FLDEPTTGLDP 157
Cdd:PRK03695 92 -----LHQPDKTRTEAvasalnEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVLQVWPDInpagqllLLDEPMNSLDV 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2794531883 158 QARAEVWRTVKQLADGGTTVLLTTQYLDEAEQLADRIAILHEGRIIQNGTLAElkrllpsatveyVEKQPTLEEVF 233
Cdd:PRK03695 167 AQQAALDRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDE------------VLTPENLAQVF 230
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
68-222 |
8.60e-08 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 52.71 E-value: 8.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 68 ESISLTGQFAAV-DEVLTGrenlvLVARLRHLPDPGavaddmLARFSLtdagGRRAGEYSGGMRRRLDIAM----SLVGd 142
Cdd:TIGR00630 446 NQLTLTPEEKKIaEEVLKE-----IRERLGFLIDVG------LDYLSL----SRAAGTLSGGEAQRIRLATqigsGLTG- 509
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 143 ppVIF-LDEPTTGLDPQARAEVWRTVKQLADGGTTVLLtTQYLDEAEQLADRI------AILHEGRIIQNGTLAELKRLL 215
Cdd:TIGR00630 510 --VLYvLDEPSIGLHQRDNRRLINTLKRLRDLGNTLIV-VEHDEDTIRAADYVidigpgAGEHGGEVVASGTPEEILANP 586
|
....*..
gi 2794531883 216 PSATVEY 222
Cdd:TIGR00630 587 DSLTGQY 593
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
2-156 |
1.25e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 52.04 E-value: 1.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 2 RKSYGELDVLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVqGHDVaaaagrvresisltgQFAAVDE 81
Cdd:PRK11819 331 SKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GETV---------------KLAYVDQ 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 82 vltGRENLvlvarlrhlpDPG-----AVAD--DML-------------ARFSLTdaGG---RRAGEYSGGMRRRLDIAMS 138
Cdd:PRK11819 395 ---SRDAL----------DPNktvweEISGglDIIkvgnreipsrayvGRFNFK--GGdqqKKVGVLSGGERNRLHLAKT 459
|
170
....*....|....*...
gi 2794531883 139 LVGDPPVIFLDEPTTGLD 156
Cdd:PRK11819 460 LKQGGNVLLLDEPTNDLD 477
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
11-199 |
1.42e-07 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 50.56 E-value: 1.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 11 LRGVDLGVAPGTIHALLGSNGAGKttlvkilSTLVRADAGTASvqghDVAAAAGRVResisltgqfaavdevLTGRENLV 90
Cdd:COG4136 17 LAPLSLTVAPGEILTLMGPSGSGK-------STLLAAIAGTLS----PAFSASGEVL---------------LNGRRLTA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 91 LVARLRHL------------------------PDPG-----AVADDMLARFSLTDAGGRRAGEYSGGMRRRLDIAMSLVG 141
Cdd:COG4136 71 LPAEQRRIgilfqddllfphlsvgenlafalpPTIGraqrrARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLA 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2794531883 142 DPPVIFLDEPTTGLDPQARAEVWRTV-KQLADGGTTVLLTTQYLDEAEQlADRIAILHE 199
Cdd:COG4136 151 EPRALLLDEPFSKLDAALRAQFREFVfEQIRQRGIPALLVTHDEEDAPA-AGRVLDLGN 208
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
9-211 |
1.49e-07 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 51.64 E-value: 1.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 9 DVLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQG---HDVAAAAGRVRESISLTGQFAAVDEVLT- 84
Cdd:PRK10789 329 PALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDiplTKLQLDSWRSRLAVVSQTPFLFSDTVANn 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 85 ---GR-----ENLVLVARLrhlpdpGAVADDMLaRFS---LTDAgGRRAGEYSGGMRRRLDIAMSLVGDPPVIFLDEPTT 153
Cdd:PRK10789 409 ialGRpdatqQEIEHVARL------ASVHDDIL-RLPqgyDTEV-GERGVMLSGGQKQRISIARALLLNAEILILDDALS 480
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2794531883 154 GLDPQARAEVWRTVKQLADgGTTVLLTTQYLdEAEQLADRIAILHEGRIIQNGTLAEL 211
Cdd:PRK10789 481 AVDGRTEHQILHNLRQWGE-GRTVIISAHRL-SALTEASEILVMQHGHIAQRGNHDQL 536
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
124-213 |
1.57e-07 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 51.06 E-value: 1.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 124 EYSGGMRRRLDIAMSLVGDPPVIFLDEPTTGLDPQARAEVWRTVKQLAD-GGTTVLLTTQYLDEAEQLADRIAILHEGRI 202
Cdd:COG4170 158 ELTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQlQGTSILLISHDLESISQWADTITVLYCGQT 237
|
90
....*....|.
gi 2794531883 203 IQNGTLAELKR 213
Cdd:COG4170 238 VESGPTEQILK 248
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
8-211 |
3.35e-07 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 50.09 E-value: 3.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 8 LDVLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGHDV----AAAAGRVRESISLTGQ--FAAVDE 81
Cdd:PRK15079 34 LKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLlgmkDDEWRAVRSDIQMIFQdpLASLNP 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 82 VLTGREnlVLVARLR----HLPDpGAVAD---DMLARFSL-TDAGGRRAGEYSGGMRRRLDIAMSLVGDPPVIFLDEPTT 153
Cdd:PRK15079 114 RMTIGE--IIAEPLRtyhpKLSR-QEVKDrvkAMMLKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVS 190
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2794531883 154 GLDPQARAEVWRTVKQL-ADGGTTVLLTTQYLDEAEQLADRIAILHEGRIIQNGTLAEL 211
Cdd:PRK15079 191 ALDVSIQAQVVNLLQQLqREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEV 249
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
11-197 |
3.38e-07 |
|
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: 48.90 E-value: 3.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 11 LRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVradAGTASVQGHDVAAAAGRVRESISLTGQFAavdevltgrenlv 90
Cdd:cd03227 11 FVPNDVTFGEGSLTIITGPNGSGKSTILDAIGLAL---GGAQSATRRRSGVKAGCIVAAVSAELIFT------------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 91 lvarlrhlpdpgavaddmlaRFSLtdaggrrageySGGMRRRLDIAMSL----VGDPPVIFLDEPTTGLDPQARAEVWRT 166
Cdd:cd03227 75 --------------------RLQL-----------SGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALAEA 123
|
170 180 190
....*....|....*....|....*....|.
gi 2794531883 167 VKQLADGGTTVLLTTQYLDEAEqLADRIAIL 197
Cdd:cd03227 124 ILEHLVKGAQVIVITHLPELAE-LADKLIHI 153
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
71-230 |
3.86e-07 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 50.60 E-value: 3.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 71 SLTGQFAAVDEVLTGrenlvLVARLRHLPDPGavaddmLARFSLTdaggRRAGEYSGGMRRRLDIAMSLVGDPPVI--FL 148
Cdd:PRK00635 438 QLPSKSLSIEEVLQG-----LKSRLSILIDLG------LPYLTPE----RALATLSGGEQERTALAKHLGAELIGItyIL 502
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 149 DEPTTGLDPQARAEVWRTVKQLADGGTTVLLtTQYLDEAEQLADRI------AILHEGRIIQNGTLAELKRLLPSATVEY 222
Cdd:PRK00635 503 DEPSIGLHPQDTHKLINVIKKLRDQGNTVLL-VEHDEQMISLADRIidigpgAGIFGGEVLFNGSPREFLAKSDSLTAKY 581
|
....*...
gi 2794531883 223 VEKQPTLE 230
Cdd:PRK00635 582 LRQELTIP 589
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
10-201 |
5.66e-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: 5.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 10 VLRGVDLGVAPGTIHALLGSNGAGKTTLvkiLSTL---VRADAGTASVQGHdVAAAA-------GRVRESIsltgQFAAV 79
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSL---LSALlgeLEKLSGSVSVPGS-IAYVSqepwiqnGTIRENI----LFGKP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 80 ------DEVLtgrENLVLVARLRHLPDpgavADdmlarfsLTDAGGRRAGeYSGGMRRRLDIAMSLVGDPPVIFLDEPTT 153
Cdd:cd03250 92 fdeeryEKVI---KACALEPDLEILPD----GD-------LTEIGEKGIN-LSGGQKQRISLARAVYSDADIYLLDDPLS 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2794531883 154 GLDPQARAEVWRTV--KQLADGGTTVLLT--TQYLDEaeqlADRIAILHEGR 201
Cdd:cd03250 157 AVDAHVGRHIFENCilGLLLNNKTRILVThqLQLLPH----ADQIVVLDNGR 204
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
4-179 |
7.13e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 49.63 E-value: 7.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 4 SYGELDVLRGVDLGVAPGTIHALLGSNGAGKTTLVKILS-----------TL-------------VRADAGTASVQGHDV 59
Cdd:PRK10938 269 SYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITgdhpqgysndlTLfgrrrgsgetiwdIKKHIGYVSSSLHLD 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 60 AAAAGRVRESIsLTGQF------AAVDEvltgrenlvlvaRLRHLpdpgavADDMLARFSLTDAGGRRA-GEYSGGMRRR 132
Cdd:PRK10938 349 YRVSTSVRNVI-LSGFFdsigiyQAVSD------------RQQKL------AQQWLDILGIDKRTADAPfHSLSWGQQRL 409
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2794531883 133 LDIAMSLVGDPPVIFLDEPTTGLDPQARAEVWRTVKQLADGGTTVLL 179
Cdd:PRK10938 410 ALIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISEGETQLL 456
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
10-211 |
7.72e-07 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 49.72 E-value: 7.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 10 VLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGHDVAAAAGRV-RESISLTGQfaavDEVLTGREN 88
Cdd:PRK10790 356 VLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVlRQGVAMVQQ----DPVVLADTF 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 89 LVLVARLRHLPDPG------AVADDMLARfSLTDAGGRRAGE----YSGGMRRRLDIAMSLVGDPPVIFLDEPTTGLDP- 157
Cdd:PRK10790 432 LANVTLGRDISEEQvwqaleTVQLAELAR-SLPDGLYTPLGEqgnnLSVGQKQLLALARVLVQTPQILILDEATANIDSg 510
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2794531883 158 --QARAEVWRTVKQladgGTTVLLTTQYLDEAEQlADRIAILHEGRIIQNGTLAEL 211
Cdd:PRK10790 511 teQAIQQALAAVRE----HTTLVVIAHRLSTIVE-ADTILVLHRGQAVEQGTHQQL 561
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
122-203 |
8.55e-07 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 49.40 E-value: 8.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 122 AGEYSGGMRRRLDIAMSLVGDPPVIFLDEPTTGLDPQARAEVWRTVKQLADGGTTVLLTTQYLDEAEQLADRIAILHEGR 201
Cdd:NF040905 402 VGNLSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAEGKGVIVISSELPELLGMCDRIYVMNEGR 481
|
..
gi 2794531883 202 II 203
Cdd:NF040905 482 IT 483
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
25-181 |
1.00e-06 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 48.85 E-value: 1.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 25 ALLGSNGAGKTTLVKILSTLVRADaGTASVQGHDVAAAAGRVRESISLTGQFAAV-----DEVLTGRENLVLVARLRHLP 99
Cdd:COG3593 27 VLVGENNSGKSSILEALRLLLGPS-SSRKFDEEDFYLGDDPDLPEIEIELTFGSLlsrllRLLLKEEDKEELEEALEELN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 100 D------------------------------PGAVADDMLARFSLT-DAGGRRAGEYSG-GMRRRLDIAMSLV------- 140
Cdd:COG3593 106 EelkealkalnellseylkelldgldlelelSLDELEDLLKSLSLRiEDGKELPLDRLGsGFQRLILLALLSAlaelkra 185
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2794531883 141 GDPPVIFLDEPTTGLDPQARAEVWRTVKQLADGGTTVLLTT 181
Cdd:COG3593 186 PANPILLIEEPEAHLHPQAQRRLLKLLKELSEKPNQVIITT 226
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
110-211 |
1.01e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 49.24 E-value: 1.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 110 ARFSLTDAGGRRAGEYSGGMRRRLDIAMSLVGDPPVIFLDEPTTGLDPQARAEVWRTVKQLADGGTTVLLTTQYLDEAEQ 189
Cdd:PRK10938 121 QQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQSGITLVLVLNRFDEIPD 200
|
90 100
....*....|....*....|..
gi 2794531883 190 LADRIAILHEGRIIQNGTLAEL 211
Cdd:PRK10938 201 FVQFAGVLADCTLAETGEREEI 222
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
5-195 |
1.11e-06 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 48.24 E-value: 1.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 5 YGELDVLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTL------VRADaGTASVQGHDVAAA---AGRVRESISLTGQ 75
Cdd:PRK14243 20 YGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLndlipgFRVE-GKVTFHGKNLYAPdvdPVEVRRRIGMVFQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 76 ----FAAvdevlTGRENLVLVARLRhlpdpGAVAD-DMLARFSLTDAGG--------RRAG-EYSGGMRRRLDIAMSLVG 141
Cdd:PRK14243 99 kpnpFPK-----SIYDNIAYGARIN-----GYKGDmDELVERSLRQAALwdevkdklKQSGlSLSGGQQQRLCIARAIAV 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2794531883 142 DPPVIFLDEPTTGLDPQARAEVWRTVKQLADgGTTVLLTTQYLDEAEQLADRIA 195
Cdd:PRK14243 169 QPEVILMDEPCSALDPISTLRIEELMHELKE-QYTIIIVTHNMQQAARVSDMTA 221
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
11-206 |
1.64e-06 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 46.93 E-value: 1.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 11 LRGVDLGVAPGTIHALLGSNGAGKTTLVKilstlvradagtasvqghDVAAAAGRVRESISLTgqfaavdevLTGRENLV 90
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVN------------------EGLYASGKARLISFLP---------KFSRNKLI 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 91 LVARLRHLPDPGavaddmLARFSLtdagGRRAGEYSGGMRRRLDIAMSLVGDPP--VIFLDEPTTGLDPQARAEVWRTVK 168
Cdd:cd03238 64 FIDQLQFLIDVG------LGYLTL----GQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIK 133
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2794531883 169 QLADGGTTVLLTTQYLDEAEQlADRI------AILHEGRIIQNG 206
Cdd:cd03238 134 GLIDLGNTVILIEHNLDVLSS-ADWIidfgpgSGKSGGKVVFSG 176
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
126-213 |
1.92e-06 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 47.81 E-value: 1.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 126 SGGMRRRLDIAMSLVGDPPVIFLDEPTTGLDPQARAEVWRTVKQLADGGTTVL-LTTQYLDEAEQLADRIAILHEGRIIQ 204
Cdd:PRK11022 155 SGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALvLITHDLALVAEAAHKIIVMYAGQVVE 234
|
....*....
gi 2794531883 205 NGTLAELKR 213
Cdd:PRK11022 235 TGKAHDIFR 243
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
123-202 |
2.41e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 47.80 E-value: 2.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 123 GEYSGGMRRRLDIAMSLVGDPPVIFLDEPTTGLDPQARAEVWRTVKQLADGGTTVLLTTQYLDEAEQLADRIAILHEGRI 202
Cdd:PRK10982 390 GSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNGLV 469
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
23-162 |
3.05e-06 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 46.45 E-value: 3.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 23 IHALLGSNGAGKTTLVKIL--STLVRADAGTASVQGHDVAAAAGRVRESISLTGQFAAVDEVLTGR-----ENLVLVarl 95
Cdd:cd03240 24 LTLIVGQNGAGKTTIIEALkyALTGELPPNSKGGAHDPKLIREGEVRAQVKLAFENANGKKYTITRslailENVIFC--- 100
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2794531883 96 rHLPDPGAVADDMLARFSltdaGGRRAgeySGGMRRRLDIAMSLVGDPPVIFLDEPTTGLDPQARAE 162
Cdd:cd03240 101 -HQGESNWPLLDMRGRCS----GGEKV---LASLIIRLALAETFGSNCGILALDEPTTNLDEENIEE 159
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
4-156 |
3.80e-06 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 47.64 E-value: 3.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 4 SYGELDVLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGhDVA----------AAAGRVRESISlt 73
Cdd:PRK11147 12 SFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQ-DLIvarlqqdpprNVEGTVYDFVA-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 74 GQFAAVDEVLTGRENL-VLVAR------LRHLPDPGAVAD------------DMLARFSLtDAGGRRAgEYSGGMRRRLD 134
Cdd:PRK11147 89 EGIEEQAEYLKRYHDIsHLVETdpseknLNELAKLQEQLDhhnlwqlenrinEVLAQLGL-DPDAALS-SLSGGWLRKAA 166
|
170 180
....*....|....*....|..
gi 2794531883 135 IAMSLVGDPPVIFLDEPTTGLD 156
Cdd:PRK11147 167 LGRALVSNPDVLLLDEPTNHLD 188
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
18-210 |
6.52e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 46.70 E-value: 6.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 18 VAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGHdvAAAAGRVRESISLtgQFAAVDEVLTG-RENLVLVARLR 96
Cdd:PRK10636 24 INPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGN--WQLAWVNQETPAL--PQPALEYVIDGdREYRQLEAQLH 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 97 HLP---DPGAVAD-----DMLARF-------SLTDAGG-------RRAGEYSGGMRRRLDIAMSLVGDPPVIFLDEPTTG 154
Cdd:PRK10636 100 DANernDGHAIATihgklDAIDAWtirsraaSLLHGLGfsneqleRPVSDFSGGWRMRLNLAQALICRSDLLLLDEPTNH 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2794531883 155 LDpqARAEVWRTvKQLADGGTTVLLTTQYLDEAEQLADRiaILHegriIQNGTLAE 210
Cdd:PRK10636 180 LD--LDAVIWLE-KWLKSYQGTLILISHDRDFLDPIVDK--IIH----IEQQSLFE 226
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
120-170 |
6.62e-06 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 46.62 E-value: 6.62e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 2794531883 120 RRAGEYSGGMRRRLDIAMSLVGDPPVIFLDEPTTGLDPQARAEVWRTVKQL 170
Cdd:PRK15134 421 RYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSL 471
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
1-156 |
6.75e-06 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 46.81 E-value: 6.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 1 MRKSYGELDVLRGVDLGVAPGTIHALLGSNGAGKTTLVKilsTLVradagtasvqgHDVAAAAGRVR--ESISLtGQFA- 77
Cdd:PRK15064 325 LTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLR---TLV-----------GELEPDSGTVKwsENANI-GYYAq 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 78 ------AVDEVLTGrenlvLVARLRHLPDPGAVADDMLAR--FSLTDAgGRRAGEYSGGMRRRLDIAMSLVGDPPVIFLD 149
Cdd:PRK15064 390 dhaydfENDLTLFD-----WMSQWRQEGDDEQAVRGTLGRllFSQDDI-KKSVKVLSGGEKGRMLFGKLMMQKPNVLVMD 463
|
....*..
gi 2794531883 150 EPTTGLD 156
Cdd:PRK15064 464 EPTNHMD 470
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
14-212 |
9.29e-06 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 46.12 E-value: 9.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 14 VDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGHDVAAAAGRVRESisltgQFAAV-------DEVLTGR 86
Cdd:PRK10522 342 INLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRK-----LFSAVftdfhlfDQLLGPE 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 87 enlvlvarlRHLPDPGAVaDDMLARFSLTD----AGGRRAG-EYSGGMRRRLDIAMSLVGDPPVIFLDEPTTGLDPQARA 161
Cdd:PRK10522 417 ---------GKPANPALV-EKWLERLKMAHklelEDGRISNlKLSKGQKKRLALLLALAEERDILLLDEWAADQDPHFRR 486
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2794531883 162 EVWRT-VKQLADGGTTVLLTTQ---YLDeaeqLADRIAilhegrIIQNGTLAELK 212
Cdd:PRK10522 487 EFYQVlLPLLQEMGKTIFAISHddhYFI----HADRLL------EMRNGQLSELT 531
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
6-244 |
1.65e-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: 45.71 E-value: 1.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 6 GELDVLRGVDLGVAPGTIHALLGSNGAGKTTLVKILstLVRADagtaSVQGHdVAaaagrVRESISLTGQFAAVDEVlTG 85
Cdd:TIGR00957 649 DLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSAL--LAEMD----KVEGH-VH-----MKGSVAYVPQQAWIQND-SL 715
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 86 RENLVLVARLRHlPDPGAV--ADDMLARFSLTDAG-----GRRAGEYSGGMRRRLDIAMSLVGDPPVIFLDEPTTGLDPQ 158
Cdd:TIGR00957 716 RENILFGKALNE-KYYQQVleACALLPDLEILPSGdrteiGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAH 794
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 159 ARAEVWRTV---KQLADGGTTVLLT--TQYLDEaeqlADRIAILHEGRIIQ----------NGTLAELKRLLPSAtveyv 223
Cdd:TIGR00957 795 VGKHIFEHVigpEGVLKNKTRILVThgISYLPQ----VDVIIVMSGGKISEmgsyqellqrDGAFAEFLRTYAPD----- 865
|
250 260
....*....|....*....|.
gi 2794531883 224 EKQPTLEEVFLAVVGETDGSA 244
Cdd:TIGR00957 866 EQQGHLEDSWTALVSGEGKEA 886
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
8-188 |
1.70e-05 |
|
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: 44.63 E-value: 1.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 8 LDVLRGVDLGVAPGTIHALLGSNGAGKTTLvkILSTL-----VRADAGTASVQGHDVAAAAGRVRESISLTgqFAAVDEV 82
Cdd:cd03290 14 LATLSNINIRIPTGQLTMIVGQVGCGKSSL--LLAILgemqtLEGKVHWSNKNESEPSFEATRSRNRYSVA--YAAQKPW 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 83 L---TGRENLVLVA-----RLRHLPDPGAVADDM-LARFSLTDAGGRRAGEYSGGMRRRLDIAMSLVGDPPVIFLDEPTT 153
Cdd:cd03290 90 LlnaTVEENITFGSpfnkqRYKAVTDACSLQPDIdLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFS 169
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2794531883 154 GLDPQARAEVWRT--VKQLADGGTTVLLTT---QYLDEAE 188
Cdd:cd03290 170 ALDIHLSDHLMQEgiLKFLQDDKRTLVLVThklQYLPHAD 209
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
126-211 |
2.00e-05 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 45.41 E-value: 2.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 126 SGGMRRRLDIAMSLVGDPPVIFLDEPTTGLDPQARAEVWRTVKQLADGGTTVLLTTQYLDEAEQLADRIAILHE----GR 201
Cdd:PTZ00265 1360 SGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASIKRSDKIVVFNNpdrtGS 1439
|
90
....*....|.
gi 2794531883 202 IIQ-NGTLAEL 211
Cdd:PTZ00265 1440 FVQaHGTHEEL 1450
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
26-156 |
5.01e-05 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 44.11 E-value: 5.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 26 LLGSNGAGKTTLVKILSTLVRADAGTASVqghDVAAAAGRVRESisltgQFA-----AVDEVLTGRENLVLVA----RLR 96
Cdd:PRK15064 32 LIGANGCGKSTFMKILGGDLEPSAGNVSL---DPNERLGKLRQD-----QFAfeeftVLDTVIMGHTELWEVKqerdRIY 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 97 HLP----DPGAVADDMLARFSLTD--AGGRRAGE-----------YSGGMRR-------RLDIAMSLVGDPPVIFLDEPT 152
Cdd:PRK15064 104 ALPemseEDGMKVADLEVKFAEMDgyTAEARAGElllgvgipeeqHYGLMSEvapgwklRVLLAQALFSNPDILLLDEPT 183
|
....
gi 2794531883 153 TGLD 156
Cdd:PRK15064 184 NNLD 187
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
91-206 |
7.33e-05 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 42.63 E-value: 7.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 91 LVARLRHLPDPGavaddmLARFSLTdaggRRAGEYSGGMRRRLDIA----MSLVGdppVIF-LDEPTTGLDPQARAEVWR 165
Cdd:cd03270 114 IRERLGFLVDVG------LGYLTLS----RSAPTLSGGEAQRIRLAtqigSGLTG---VLYvLDEPSIGLHPRDNDRLIE 180
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 2794531883 166 TVKQLADGGTTVLLtTQYLDEAEQLADRI------AILHEGRIIQNG 206
Cdd:cd03270 181 TLKRLRDLGNTVLV-VEHDEDTIRAADHVidigpgAGVHGGEIVAQG 226
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
119-170 |
7.39e-05 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 43.86 E-value: 7.39e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 2794531883 119 GRRAGEYSGGMRRRLDIAMSLVGDPPVIFLDEPTTGLDPQARAEVWRTVKQL 170
Cdd:PTZ00265 574 GSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNL 625
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
1-211 |
7.86e-05 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 43.61 E-value: 7.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 1 MRKSYGELDVLRGVDLGVAPGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGHDVAAAAGR-VRESISLTGQfaav 79
Cdd:PTZ00243 1316 MRYREGLPLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLReLRRQFSMIPQ---- 1391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 80 DEVL---TGRENLvlvarlrhlpDP--GAVADDMLARFSLTDAGGRRAGE--------------YSGGMRRRLDIAMSLV 140
Cdd:PTZ00243 1392 DPVLfdgTVRQNV----------DPflEASSAEVWAALELVGLRERVASEsegidsrvleggsnYSVGQRQLMCMARALL 1461
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2794531883 141 G-DPPVIFLDEPTTGLDPQARAEVWRTVKQlADGGTTVLLTTQYLDEAEQLaDRIAILHEGRIIQNGTLAEL 211
Cdd:PTZ00243 1462 KkGSGFILMDEATANIDPALDRQIQATVMS-AFSAYTVITIAHRLHTVAQY-DKIIVMDHGAVAEMGSPREL 1531
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
126-215 |
2.08e-04 |
|
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: 41.02 E-value: 2.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 126 SGGMRRRLDIAMSLVGDPPVIFLDEPTTGLDPQARAEVWRTVKQLAD-GGTTVLLTTQYLDEAEQLADRIaILHEGRIIQ 204
Cdd:cd03222 73 SGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEeGKKTALVVEHDLAVLDYLSDRI-HVFEGEPGV 151
|
90
....*....|.
gi 2794531883 205 NGTLAELKRLL 215
Cdd:cd03222 152 YGIASQPKGTR 162
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
126-206 |
2.23e-04 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 42.14 E-value: 2.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 126 SGGMRRRLDIAMSLVGDPPVIFLDEPTTGLDPQARAEVWRTVKQLA--DGGTTVLLTTQYLDEAEQLADRIAILHEGRII 203
Cdd:PLN03140 338 SGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQQIVhlTEATVLMSLLQPAPETFDLFDDIILLSEGQIV 417
|
...
gi 2794531883 204 QNG 206
Cdd:PLN03140 418 YQG 420
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
20-181 |
3.85e-04 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 40.24 E-value: 3.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 20 PGTIHALLGSNGAGKTTLVKILSTLVRADAGTASVQGHDVAAAAgrvRESISLTGQFAAVDEVLTGRENLVLVARLRhlp 99
Cdd:PRK13541 25 PSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIA---KPYCTYIGHNLGLKLEMTVFENLKFWSEIY--- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 100 DPGAVADDMLARFSLTDAGGRRAGEYSGGMRRRLDIAMSLVGDPPVIFLDEPTTGLDPQARAEVWRTVKQLADGGTTVLL 179
Cdd:PRK13541 99 NSAETLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNNLIVMKANSGGIVLL 178
|
..
gi 2794531883 180 TT 181
Cdd:PRK13541 179 SS 180
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
25-196 |
8.56e-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: 38.89 E-value: 8.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 25 ALLGSNGAGKTTLVKILstlvradAGTASVQGHDVaaaagrvrESISLTGQFAAVDEVLtgrenlvlvarlrhlpdpgav 104
Cdd:smart00382 6 LIVGPPGSGKTTLARAL-------ARELGPPGGGV--------IYIDGEDILEEVLDQL--------------------- 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 105 addmlarfsLTDAGGRRAGEYSGGMRRRLDIAMSLVGDPPVIFLDEPTTGLDPQARAEVWRTV------KQLADGGTTVL 178
Cdd:smart00382 50 ---------LLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEelrlllLLKSEKNLTVI 120
|
170
....*....|....*...
gi 2794531883 179 LTTQYLDEAEQLADRIAI 196
Cdd:smart00382 121 LTTNDEKDLGPALLRRRF 138
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
126-178 |
1.26e-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: 38.29 E-value: 1.26e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 2794531883 126 SGGMRRRLDIAMSLVGDPPVIFLDEPTTGLDPQARAEVWRTVKQLadgGTTVL 178
Cdd:cd03223 93 SGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLKEL---GITVI 142
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
103-159 |
1.54e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 39.46 E-value: 1.54e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 2794531883 103 AVADDMLARFSLT-DAGGRRAGEYSGGMRRRLDIAMSLVGDPPVIFLDEPTTGLDPQA 159
Cdd:PLN03073 322 ARAASILAGLSFTpEMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHA 379
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
120-222 |
1.91e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 39.24 E-value: 1.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 120 RRAGEYSGG-MRR-RL--DIAMSLVGdppVIF-LDEPTTGLDPQARAEVWRTVKQLADGGTTVLLTTQylDEAEQL-ADR 193
Cdd:COG0178 481 RSAGTLSGGeAQRiRLatQIGSGLVG---VLYvLDEPSIGLHQRDNDRLIETLKRLRDLGNTVIVVEH--DEDTIRaADY 555
|
90 100 110
....*....|....*....|....*....|....*
gi 2794531883 194 I------AILHEGRIIQNGTLAELKRLLPSATVEY 222
Cdd:COG0178 556 IidigpgAGEHGGEVVAQGTPEEILKNPDSLTGQY 590
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
10-178 |
3.77e-03 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 38.25 E-value: 3.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 10 VLRGVDLGVAPGtiHALL--GSNGAGKTTLVKILSTLVRADAGTASV-QGHDVAAAA-------GRVRESISLTGQFAAV 79
Cdd:COG4178 378 LLEDLSLSLKPG--ERLLitGPSGSGKSTLLRAIAGLWPYGSGRIARpAGARVLFLPqrpylplGTLREALLYPATAEAF 455
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 80 -DEVLtgRENLVLVaRLRHLPDpgavaddmlaRFsltDAGGRRAGEYSGGMRRRLDIAMSLVGDPPVIFLDEPTTGLDPQ 158
Cdd:COG4178 456 sDAEL--REALEAV-GLGHLAE----------RL---DEEADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEE 519
|
170 180
....*....|....*....|
gi 2794531883 159 ARAEVWRTVKQlADGGTTVL 178
Cdd:COG4178 520 NEAALYQLLRE-ELPGTTVI 538
|
|
| PRK13764 |
PRK13764 |
ATPase; Provisional |
165-241 |
3.98e-03 |
|
ATPase; Provisional
Pssm-ID: 184311 [Multi-domain] Cd Length: 602 Bit Score: 38.28 E-value: 3.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794531883 165 RTVKQLADGGTTVLLTTQYLDEAEQLADRiailheGRIIQNGTLAELKRLLPSA-----TVEYVEKQPTLEEVFLAVVGE 239
Cdd:PRK13764 17 ELIEKGEYIGGTIIIPEAVVAELEAQANQ------GREIGFSGLEELKKLRELAeegliELEFVGERPTLEQIKLAKGGE 90
|
..
gi 2794531883 240 TD 241
Cdd:PRK13764 91 ID 92
|
|
| |
