|
Name |
Accession |
Description |
Interval |
E-value |
| PQQ_ABC_ATP |
TIGR03864 |
ABC transporter, ATP-binding subunit, PQQ-dependent alcohol dehydrogenase system; Members of ... |
3-212 |
8.97e-96 |
|
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: 279.95 E-value: 8.97e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 3 IAVQAVSHQYGGHHALDNINLCLKPG-LTMLLGPNGAGKSTLFALITGLQKLTQGSITFDGATLSQSRTSIMAKMGVVFQ 81
Cdd:TIGR03864 2 LEVAGLSFRYGARRALDDVSFTVRPGrFVALLGPNGAGKSTLFSLLTRLYVAQSGQISVAGHDLRRAPRAALARLGVVFQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 82 QSTLDIDLSVKQNLSYFASLHGISTASALSHIQGLLDELDLTSKLNTKIRNLNGGHRRRVELARCLIHKPSLLLLDEPTV 161
Cdd:TIGR03864 82 QPTLDLDLSVRQNLRYHAALHGLSRAEARARIAELLARLGLAERADDKVRELNGGHRRRVEIARALLHRPALLLLDEPTV 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 521328941 162 GLDIESRHLILRVVQALAHSQSVSVLWATHLFEEVKHNNNLIVLSKGRVLA 212
Cdd:TIGR03864 162 GLDPASRAAITAHVRALARDQGLSVLWATHLVDEIEASDRLVVLHRGRVLA 212
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
3-223 |
3.48e-79 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 237.65 E-value: 3.48e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 3 IAVQAVSHQYGGHHALDNINLCLKPG-LTMLLGPNGAGKSTLFALITGLQKLTQGSITFDGATLSQSRTSIMAKMGVVFQ 81
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGeIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 82 QSTLDIDLSVKQNLSYFASLHGISTASALSHIQGLLDELDLTSKLNTKIRNLNGGHRRRVELARCLIHKPSLLLLDEPTV 161
Cdd:COG1131 81 EPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTS 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 521328941 162 GLDIESRHLILRVVQALAhSQSVSVLWATHLFEEVKHN-NNLIVLSKGRVLAHDQCEALLAKY 223
Cdd:COG1131 161 GLDPEARRELWELLRELA-AEGKTVLLSTHYLEEAERLcDRVAIIDKGRIVADGTPDELKARL 222
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
3-229 |
1.07e-64 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 201.24 E-value: 1.07e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 3 IAVQAVSHQYGGHHALDNINLCLKPG-LTMLLGPNGAGKSTLFALITGLQKLTQGSITFDGATLSQSRTSIMAKMGVVFQ 81
Cdd:COG4555 2 IEVENLSKKYGKVPALKDVSFTAKDGeITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQIGVLPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 82 QSTLDIDLSVKQNLSYFASLHGISTASALSHIQGLLDELDLTSKLNTKIRNLNGGHRRRVELARCLIHKPSLLLLDEPTV 161
Cdd:COG4555 82 ERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTN 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 521328941 162 GLDIESRHLILRVVQALAHSQSVsVLWATHLFEEVKH-NNNLIVLSKGRVLAHDQCEALLAKYHQQDIE 229
Cdd:COG4555 162 GLDVMARRLLREILRALKKEGKT-VLFSSHIMQEVEAlCDRVVILHKGKVVAQGSLDELREEIGEENLE 229
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
3-213 |
4.65e-55 |
|
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: 175.46 E-value: 4.65e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 3 IAVQAVSHQYGGHHALDNINLCLKPGLTMLLGPNGAGKSTLFALITGLQKLTQGSITFDGATLSQSRTSIMAKMGVVFQQ 82
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPGMYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRRIGYLPQE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 83 STLDIDLSVKQNLSYFASLHGISTASALSHIQGLLDELDLTSKLNTKIRNLNGGHRRRVELARCLIHKPSLLLLDEPTVG 162
Cdd:cd03264 81 FGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAG 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 521328941 163 LDIESRHLILRVVQALAhsQSVSVLWATHLFEEVK-HNNNLIVLSKGRVLAH 213
Cdd:cd03264 161 LDPEERIRFRNLLSELG--EDRIVILSTHIVEDVEsLCNQVAVLNKGKLVFE 210
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
3-219 |
9.23e-51 |
|
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: 164.85 E-value: 9.23e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 3 IAVQAVSHQYGGHHALDNINLCLKPGLTM-LLGPNGAGKSTLFALITGLQKLTQGSITFDGATLSQSRTSIMAKMGVVFQ 81
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFgLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREVRRRIGIVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 82 QSTLDIDLSVKQNLSYFASLHGISTASALSHIQGLLDELDLTSKLNTKIRNLNGGHRRRVELARCLIHKPSLLLLDEPTV 161
Cdd:cd03265 81 DLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTI 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 521328941 162 GLDIESRHLILRVVQALAHSQSVSVLWATHLFEEV-KHNNNLIVLSKGRVLAHDQCEAL 219
Cdd:cd03265 161 GLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAeQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
5-212 |
2.67e-49 |
|
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: 161.13 E-value: 2.67e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 5 VQAVSHQYGG--HHALDNINLCLKPG-LTMLLGPNGAGKSTLFALITGLQKLTQGSITFDGATLSQSRTSIMAKMGVVFQ 81
Cdd:cd03263 3 IRNLTKTYKKgtKPAVDDLSLNVYKGeIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAARQSLGYCPQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 82 QSTLDIDLSVKQNLSYFASLHGISTASALSHIQGLLDELDLTSKLNTKIRNLNGGHRRRVELARCLIHKPSLLLLDEPTV 161
Cdd:cd03263 83 FDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTS 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 521328941 162 GLDIESRHLILRVVQALAHSQsvSVLWATHLFEEVKH-NNNLIVLSKGRVLA 212
Cdd:cd03263 163 GLDPASRRAIWDLILEVRKGR--SIILTTHSMDEAEAlCDRIAIMSDGKLRC 212
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
3-210 |
3.44e-48 |
|
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: 156.40 E-value: 3.44e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 3 IAVQAVSHQYGGHHALDNINLCLKPGLTM-LLGPNGAGKSTLFALITGLQKLTQGSITFDGATLSQSRTSIMAKMGVVFQ 81
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYgLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKRRIGYLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 82 QSTLDIDLSVKQNLSYfaslhgistasalshiqglldeldltSKlntkirnlngGHRRRVELARCLIHKPSLLLLDEPTV 161
Cdd:cd03230 81 EPSLYENLTVRENLKL--------------------------SG----------GMKQRLALAQALLHDPELLILDEPTS 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 521328941 162 GLDIESRHLILRVVQALAhSQSVSVLWATHLFEEV-KHNNNLIVLSKGRV 210
Cdd:cd03230 125 GLDPESRREFWELLRELK-KEGKTILLSSHILEEAeRLCDRVAILNNGRI 173
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
5-212 |
1.32e-47 |
|
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: 157.89 E-value: 1.32e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 5 VQAVSHQYGGHHALDNINLCLKPG-LTMLLGPNGAGKSTLFALITGLQKLTQGSITFDGATLSQSRTSIMAKMGVV--FQ 81
Cdd:COG0411 7 VRGLTKRFGGLVAVDDVSLEVERGeIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIARLGIArtFQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 82 QSTLDIDLSVKQNL----------SYFASLHGI-----STASALSHIQGLLDELDLTSKLNTKIRNLNGGHRRRVELARC 146
Cdd:COG0411 87 NPRLFPELTVLENVlvaaharlgrGLLAALLRLprarrEEREARERAEELLERVGLADRADEPAGNLSYGQQRRLEIARA 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 521328941 147 LIHKPSLLLLDEPTVGLDIESRHLILRVVQALAHSQSVSVLWathlfeeVKHN--------NNLIVLSKGRVLA 212
Cdd:COG0411 167 LATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILL-------IEHDmdlvmglaDRIVVLDFGRVIA 233
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
3-237 |
2.74e-47 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 156.79 E-value: 2.74e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 3 IAVQAVSHQYGGHHALDNINLCLKPG-LTMLLGPNGAGKSTLFALITGLQKLTQGSITFDGATLSQSRTSImakmGVVFQ 81
Cdd:COG1121 7 IELENLTVSYGGRPVLEDVSLTIPPGeFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARRRI----GYVPQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 82 QSTLDID--LSVKQ----NLSYFASLHGISTASALSHIQGLLDELDLTSKLNTKIRNLNGGHRRRVELARCLIHKPSLLL 155
Cdd:COG1121 83 RAEVDWDfpITVRDvvlmGRYGRRGLFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDPDLLL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 156 LDEPTVGLDIESRHLILRVVQALaHSQSVSVLWATHLFEEVKHNNNLIVLSKGRVLAHDQCEALLAkyhQQDIEHLWQHL 235
Cdd:COG1121 163 LDEPFAGVDAATEEALYELLREL-RREGKTILVVTHDLGAVREYFDRVLLLNRGLVAHGPPEEVLT---PENLSRAYGGP 238
|
..
gi 521328941 236 MQ 237
Cdd:COG1121 239 VA 240
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
12-219 |
1.80e-46 |
|
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin resistance ABC transporter, ATP binding subunit in bacteria and archaea. This model is restricted in its scope to preferentially recognize the ATP binding subunit associated with effux of the drug, daunorubicin. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. In eukaryotes proteins of similar function include p-gyco proteins, multidrug resistance protein etc. [Transport and binding proteins, Other]
Pssm-ID: 130256 [Multi-domain] Cd Length: 302 Bit Score: 156.40 E-value: 1.80e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 12 YGGHHALDNINLCLKPGLTM-LLGPNGAGKSTLFALITGLQKLTQGSITFDGATLSQSRTSIMAKMGVVFQQSTLDIDLS 90
Cdd:TIGR01188 3 YGDFKAVDGVNFKVREGEVFgFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVVREPRKVRRSIGIVPQYASVDEDLT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 91 VKQNLSYFASLHGISTASALSHIQGLLDELDLTSKLNTKIRNLNGGHRRRVELARCLIHKPSLLLLDEPTVGLDIESRHL 170
Cdd:TIGR01188 83 GRENLEMMGRLYGLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPRTRRA 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 521328941 171 ILRVVQALaHSQSVSVLWATHLFEEV-KHNNNLIVLSKGRVLAHDQCEAL 219
Cdd:TIGR01188 163 IWDYIRAL-KEEGVTILLTTHYMEEAdKLCDRIAIIDHGRIIAEGTPEEL 211
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
3-210 |
3.31e-46 |
|
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: 153.03 E-value: 3.31e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 3 IAVQAVSHQYGG----HHALDNINLCLKPG-LTMLLGPNGAGKSTLFALITGLQKLTQGSITFDGATLSQSRTSIMA--- 74
Cdd:cd03255 1 IELKNLSKTYGGggekVQALKGVSLSIEKGeFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 75 --KMGVVFQQSTLDIDLSVKQNLSYFASLHGISTASALSHIQGLLDELDLTSKLNTKIRNLNGGHRRRVELARCLIHKPS 152
Cdd:cd03255 81 rrHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 521328941 153 LLLLDEPTVGLDIESRHLILRVVQALAHSQSVSVLWATHLFEEVKHNNNLIVLSKGRV 210
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
3-220 |
6.96e-45 |
|
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: 150.58 E-value: 6.96e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 3 IAVQAVSHQYGGHHALDNINLCLKPG-LTMLLGPNGAGKSTLFALITGLQKLTQGSITFDGATLSQ-SRTSIMAKMGVVF 80
Cdd:COG1120 2 LEAENLSVGYGGRPVLDDVSLSLPPGeVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASlSRRELARRIAYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 81 QQSTLDIDLSVKQNLSY----FASLHGISTASALSHIQGLLDELDLTSKLNTKIRNLNGGHRRRVELARCLIHKPSLLLL 156
Cdd:COG1120 82 QEPPAPFGLTVRELVALgrypHLGLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLLL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 521328941 157 DEPTVGLDIESRHLILRVVQALAHSQSVSVLWATH-LFEEVKHNNNLIVLSKGRVLAHDQCEALL 220
Cdd:COG1120 162 DEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHdLNLAARYADRLVLLKDGRIVAQGPPEEVL 226
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
3-213 |
1.62e-44 |
|
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: 149.12 E-value: 1.62e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 3 IAVQAVSHQYGGHHALDNINLCLKPG-LTMLLGPNGAGKSTLFALITGLQKLTQGSITFDGATLSQSRTSIMAKMGVV-- 79
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGeIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARLGIGrt 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 80 FQQSTLDIDLSVKQNLSYFASLHGISTASALSHIQG----------LLDELDLTSKLNTKIRNLNGGHRRRVELARCLIH 149
Cdd:cd03219 81 FQIPRLFPELTVLENVMVAAQARTGSGLLLARARREereareraeeLLERVGLADLADRPAGELSYGQQRRLEIARALAT 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 521328941 150 KPSLLLLDEPTVGLDIESRHLILRVVQALAHsQSVSVLWathlfeeVKHN--------NNLIVLSKGRVLAH 213
Cdd:cd03219 161 DPKLLLLDEPAAGLNPEETEELAELIRELRE-RGITVLL-------VEHDmdvvmslaDRVTVLDQGRVIAE 224
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-191 |
5.95e-44 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 146.86 E-value: 5.95e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 1 MEIAVQAVSHQYGGHHALDNINLCLKPG-LTMLLGPNGAGKSTLFALITGLQKLTQGSITFDGATLSQSRTSIMAKMGVV 79
Cdd:COG4133 1 MMLEAENLSCRRGERLLFSGLSFTLAAGeALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRRLAYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 80 FQQSTLDIDLSVKQNLSYFASLHGISTASALshIQGLLDELDLTSKLNTKIRNLNGGHRRRVELARCLIHKPSLLLLDEP 159
Cdd:COG4133 81 GHADGLKPELTVRENLRFWAALYGLRADREA--IDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEP 158
|
170 180 190
....*....|....*....|....*....|..
gi 521328941 160 TVGLDIESRHLILRVVQALAhSQSVSVLWATH 191
Cdd:COG4133 159 FTALDAAGVALLAELIAAHL-ARGGAVLLTTH 189
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
3-223 |
6.39e-44 |
|
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: 147.48 E-value: 6.39e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 3 IAVQAVSHQY-GGHHALDNINLCLKPG-LTMLLGPNGAGKSTLFALITGLQKLTQGSITFDGATLSQ-SRTSIMAKMGVV 79
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGeFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKkNLRELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 80 FQQStlD---IDLSVKQNLSYfaSL--HGISTASALSHIQGLLDELDLTSKLNTKIRNLNGGHRRRVELARCLIHKPSLL 154
Cdd:COG1122 81 FQNP--DdqlFAPTVEEDVAF--GPenLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 155 LLDEPTVGLDIESRHLILRVVQALaHSQSVSVLWATHLFEEVKHN-NNLIVLSKGRVLAHDQCEALLAKY 223
Cdd:COG1122 157 VLDEPTAGLDPRGRRELLELLKRL-NKEGKTVIIVTHDLDLVAELaDRVIVLDDGRIVADGTPREVFSDY 225
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
12-214 |
8.98e-44 |
|
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: 146.52 E-value: 8.98e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 12 YGGHHALDNINLCLKPG-LTMLLGPNGAGKSTLFALITGLQKLTQGSITFDGATLSQSRTSImakmGVVFQQSTLDID-- 88
Cdd:cd03235 9 YGGHPVLEDVSFEVKPGeFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERKRI----GYVPQRRSIDRDfp 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 89 LSVKQ----NLSYFASLHGISTASALSHIQGLLDELDLTSKLNTKIRNLNGGHRRRVELARCLIHKPSLLLLDEPTVGLD 164
Cdd:cd03235 85 ISVRDvvlmGLYGHKGLFRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAGVD 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 521328941 165 IESRHLILRVVQALaHSQSVSVLWATHLFEEVKHNNNLIVLSKGRVLAHD 214
Cdd:cd03235 165 PKTQEDIYELLREL-RREGMTILVVTHDLGLVLEYFDRVLLLNRTVVASG 213
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
3-212 |
5.64e-43 |
|
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: 144.92 E-value: 5.64e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 3 IAVQAVSHQYGG----HHALDNINLCLKPG-LTMLLGPNGAGKSTLFALITGLQKLTQGSITFDGATLSQSRtsimAKMG 77
Cdd:cd03293 1 LEVRNVSKTYGGgggaVTALEDISLSVEEGeFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPG----PDRG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 78 VVFQQSTLDIDLSVKQNLSYFASLHGISTASALSHIQGLLDELDLTSKLNTKIRNLNGGHRRRVELARCLIHKPSLLLLD 157
Cdd:cd03293 77 YVFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLD 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 521328941 158 EPTVGLDIESRHLILRVVQALAHSQSVSVLWATH-LFEEVKHNNNLIVLSK--GRVLA 212
Cdd:cd03293 157 EPFSALDALTREQLQEELLDIWRETGKTVLLVTHdIDEAVFLADRVVVLSArpGRIVA 214
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
3-215 |
7.31e-43 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 144.42 E-value: 7.31e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 3 IAVQAVSHQY-GGHHALDNINLCLKPG-LTMLLGPNGAGKSTLFALITGLQKLTQGSITFDGATLSQSRTSIMA----KM 76
Cdd:COG2884 2 IRFENVSKRYpGGREALSDVSLEIEKGeFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPylrrRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 77 GVVFQQSTLDIDLSVKQNLSYFASLHGISTASALSHIQGLLDELDLTSKLNTKIRNLNGGHRRRVELARCLIHKPSLLLL 156
Cdd:COG2884 82 GVVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLLA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 521328941 157 DEPTVGLDIESRHLILRVVQALaHSQSVSVLWATH---LFEEVKHnnNLIVLSKGRVLAHDQ 215
Cdd:COG2884 162 DEPTGNLDPETSWEIMELLEEI-NRRGTTVLIATHdleLVDRMPK--RVLELEDGRLVRDEA 220
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
3-221 |
1.45e-42 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 146.49 E-value: 1.45e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 3 IAVQAVSHQYGGHHALDNINLCLKPGLTM-LLGPNGAGKSTLFALITGLQKLTQGSITFDGATLSQSRTSIMAKMGVVFQ 81
Cdd:PRK13537 8 IDFRNVEKRYGDKLVVDGLSFHVQRGECFgLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQRVGVVPQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 82 QSTLDIDLSVKQNLSYFASLHGISTASALSHIQGLLDELDLTSKLNTKIRNLNGGHRRRVELARCLIHKPSLLLLDEPTV 161
Cdd:PRK13537 88 FDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTT 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 521328941 162 GLDIESRHLILRVVQALAhSQSVSVLWATHLFEEVKH-NNNLIVLSKGRVLAHDQCEALLA 221
Cdd:PRK13537 168 GLDPQARHLMWERLRSLL-ARGKTILLTTHFMEEAERlCDRLCVIEEGRKIAEGAPHALIE 227
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
16-212 |
2.09e-42 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 143.28 E-value: 2.09e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 16 HALDNINLCLKPG-LTMLLGPNGAGKSTLFALITGLQKLTQGSITFDGATLSQSRTSIMAKMGVVFQQSTLDIDLSVKQN 94
Cdd:cd03266 19 QAVDGVSFTVKPGeVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARRRLGFVSDSTGLYDRLTAREN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 95 LSYFASLHGISTASALSHIQGLLDELDLTSKLNTKIRNLNGGHRRRVELARCLIHKPSLLLLDEPTVGLDIESRHLILRV 174
Cdd:cd03266 99 LEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRALREF 178
|
170 180 190
....*....|....*....|....*....|....*....
gi 521328941 175 VQALaHSQSVSVLWATHLFEEVKH-NNNLIVLSKGRVLA 212
Cdd:cd03266 179 IRQL-RALGKCILFSTHIMQEVERlCDRVVVLHRGRVVY 216
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-191 |
9.47e-42 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 141.72 E-value: 9.47e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 1 MEIAVQA--VSHQYG----GHHALDNINLCLKPG-LTMLLGPNGAGKSTLFALITGLQKLTQGSITFDG---ATLSQSRT 70
Cdd:COG1136 1 MSPLLELrnLTKSYGtgegEVTALRGVSLSIEAGeFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGqdiSSLSEREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 71 SIM--AKMGVVFQQSTLDIDLSVKQNLSYFASLHGISTASALSHIQGLLDELDLTSKLNTKIRNLNGGHRRRVELARCLI 148
Cdd:COG1136 81 ARLrrRHIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALV 160
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 521328941 149 HKPSLLLLDEPTVGLDIESRHLILRVVQALAHSQSVSVLWATH 191
Cdd:COG1136 161 NRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTH 203
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
3-213 |
1.26e-41 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 143.71 E-value: 1.26e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 3 IAVQAVSHQYGGHHALDNINLCLKPG-LTMLLGPNGAGKSTLFALITGLQKLTQGSITFDGATLSQS-RTSI-------- 72
Cdd:COG4152 2 LELKGLTKRFGDKTAVDDVSFTVPKGeIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEdRRRIgylpeerg 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 73 -MAKMgvvfqqstldidlSVKQNLSYFASLHGISTASALSHIQGLLDELDLTSKLNTKIRNLNGGHRRRVELARCLIHKP 151
Cdd:COG4152 82 lYPKM-------------KVGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDP 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 521328941 152 SLLLLDEPTVGLDIESRHLILRVVQALAhSQSVSVLWATHLFEEV-KHNNNLIVLSKGRVLAH 213
Cdd:COG4152 149 ELLILDEPFSGLDPVNVELLKDVIRELA-AKGTTVIFSSHQMELVeELCDRIVIINKGRKVLS 210
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
3-221 |
2.13e-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: 141.14 E-value: 2.13e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 3 IAVQAVSHQYGGHHALDNINLCLKPG-LTMLLGPNGAGKSTLFALITGLQKLTQGSITFDGATLSQSRTSIMAKMGVVF- 80
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGeIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRARLGIGYl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 81 -QQSTLDIDLSVKQNLSYFASLHGISTASALSHIQGLLDELDLTSKLNTKIRNLNGGHRRRVELARCLIHKPSLLLLDEP 159
Cdd:cd03218 81 pQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 521328941 160 TVGLDIESRHLILRVVQALAhSQSVSVLWATHlfeEVKHNNNLI----VLSKGRVLAHDQCEALLA 221
Cdd:cd03218 161 FAGVDPIAVQDIQKIIKILK-DRGIGVLITDH---NVRETLSITdrayIIYEGKVLAEGTPEEIAA 222
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
5-214 |
2.22e-41 |
|
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: 140.35 E-value: 2.22e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 5 VQAVSHQYGGHHALDNINLCLKPG-LTMLLGPNGAGKSTLFALITGLQKLTQGSITFDGATLSQ---SRTSImakmGVVF 80
Cdd:cd03259 3 LKGLSKTYGSVRALDDLSLTVEPGeFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGvppERRNI----GMVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 81 QQSTLDIDLSVKQNLSYFASLHGISTASALSHIQGLLDELDLTSKLNTKIRNLNGGHRRRVELARCLIHKPSLLLLDEPT 160
Cdd:cd03259 79 QDYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 521328941 161 VGLDIESRHLILRVVQALAHSQSVSVLWATH-LFEEVKHNNNLIVLSKGRVLAHD 214
Cdd:cd03259 159 SALDAKLREELREELKELQRELGITTIYVTHdQEEALALADRIAVMNEGRIVQVG 213
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-220 |
6.32e-41 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 143.05 E-value: 6.32e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 1 MEIAVQAVSHQYGGHHALDNINLCLKPGLTM-LLGPNGAGKSTLFALITGLQKLTQGSITFDGATLSQSRTSIMAKMGVV 79
Cdd:PRK13536 40 VAIDLAGVSKSYGDKAVVNGLSFTVASGECFgLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLARARIGVV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 80 FQQSTLDIDLSVKQNLSYFASLHGISTASALSHIQGLLDELDLTSKLNTKIRNLNGGHRRRVELARCLIHKPSLLLLDEP 159
Cdd:PRK13536 120 PQFDNLDLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEP 199
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 521328941 160 TVGLDIESRHLILRVVQALAhSQSVSVLWATHLFEEVKH-NNNLIVLSKGRVLAHDQCEALL 220
Cdd:PRK13536 200 TTGLDPHARHLIWERLRSLL-ARGKTILLTTHFMEEAERlCDRLCVLEAGRKIAEGRPHALI 260
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
3-191 |
1.67e-40 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 139.45 E-value: 1.67e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 3 IAVQAVSHQY----GGHHALDNINLCLKPG-LTMLLGPNGAGKSTLFALITGLQKLTQGSITFDGATLSQSRtsimAKMG 77
Cdd:COG1116 8 LELRGVSKRFptggGGVTALDDVSLTVAAGeFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPG----PDRG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 78 VVFQQSTLdidL---SVKQNLSYFASLHGISTASALSHIQGLLDELDLTSKLNTKIRNLNGGHRRRVELARCLIHKPSLL 154
Cdd:COG1116 84 VVFQEPAL---LpwlTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPEVL 160
|
170 180 190
....*....|....*....|....*....|....*..
gi 521328941 155 LLDEPTVGLDIESRHLILRVVQALAHSQSVSVLWATH 191
Cdd:COG1116 161 LMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTH 197
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
18-161 |
1.78e-40 |
|
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: 136.24 E-value: 1.78e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 18 LDNINLCLKPG-LTMLLGPNGAGKSTLFALITGLQKLTQGSITFDGATLS-QSRTSIMAKMGVVFQQSTLDIDLSVKQNL 95
Cdd:pfam00005 1 LKNVSLTLNPGeILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTdDERKSLRKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 96 SYFASLHGISTASALSHIQGLLDELDLTSKLNTKIRN----LNGGHRRRVELARCLIHKPSLLLLDEPTV 161
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEALEKLGLGDLADRPVGErpgtLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-222 |
2.28e-39 |
|
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: 142.59 E-value: 2.28e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 2 EIAVQAVSHQY-GGHHALDNINLCLKPG-LTMLLGPNGAGKSTLFALITGLQKLTQGSITFDGATLSQ-SRTSIMAKMGV 78
Cdd:COG4988 336 SIELEDVSFSYpGGRPALDGLSLTIPPGeRVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDlDPASWRRQIAW 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 79 VFQQSTLdIDLSVKQNLSYF---ASLHGISTASALSHIQGLLDELDLtsKLNTKI----RNLNGGHRRRVELARCLIHKP 151
Cdd:COG4988 416 VPQNPYL-FAGTIRENLRLGrpdASDEELEAALEAAGLDEFVAALPD--GLDTPLgeggRGLSGGQAQRLALARALLRDA 492
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 521328941 152 SLLLLDEPTVGLDIESRHLILRVVQALAHSQsvSVLWATHLFEEVKHNNNLIVLSKGRVLAHDQCEALLAK 222
Cdd:COG4988 493 PLLLLDEPTAHLDAETEAEILQALRRLAKGR--TVILITHRLALLAQADRILVLDDGRIVEQGTHEELLAK 561
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
17-212 |
2.59e-39 |
|
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: 135.92 E-value: 2.59e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 17 ALDNINLCLKPG-LTMLLGPNGAGKSTLFALITGLQKLTQGSITFDGATLSQSRTSIMAKMGVVF-QQSTLDIDLSVKQN 94
Cdd:cd03267 36 ALKGISFTIEKGeIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLRRIGVVFgQKTQLWWDLPVIDS 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 95 LSYFASLHGISTASALSHIQGLLDELDLTSKLNTKIRNLNGGHRRRVELARCLIHKPSLLLLDEPTVGLDIESRHLILRV 174
Cdd:cd03267 116 FYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNF 195
|
170 180 190
....*....|....*....|....*....|....*....
gi 521328941 175 VQALAHSQSVSVLWATHLFEEV-KHNNNLIVLSKGRVLA 212
Cdd:cd03267 196 LKEYNRERGTTVLLTSHYMKDIeALARRVLVIDKGRLLY 234
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
3-213 |
3.97e-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: 134.72 E-value: 3.97e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 3 IAVQAVSHQYGGHHALDNINLCLKPGLTM-LLGPNGAGKSTLFALITGLQKLTQGSITFDGATLSqsrTSIMAKMGVVFQ 81
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFgLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLD---IAARNRIGYLPE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 82 QSTLDIDLSVKQNLSYFASLHGISTASALSHIQGLLDELDLTSKLNTKIRNLNGGHRRRVELARCLIHKPSLLLLDEPTV 161
Cdd:cd03269 78 ERGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFS 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 521328941 162 GLDIESRHLILRVVQALAhSQSVSVLWATHLFEEVKH-NNNLIVLSKGRVLAH 213
Cdd:cd03269 158 GLDPVNVELLKDVIRELA-RAGKTVILSTHQMELVEElCDRVLLLNKGRAVLY 209
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
3-221 |
5.49e-39 |
|
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: 135.11 E-value: 5.49e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 3 IAVQAVSHQYGGHHALDNINLCLKPG-LTMLLGPNGAGKSTLFALITGLQKLTQGSITFDG---ATLSQS-RTSIMAKMG 77
Cdd:COG1127 6 IEVRNLTKSFGDRVVLDGVSLDVPRGeILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGqdiTGLSEKeLYELRRRIG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 78 VVFQQSTL-DiDLSVKQNLSYFASLH-GISTASALSHIQGLLDELDLTSKLNTKIRNLNGGHRRRVELARCLIHKPSLLL 155
Cdd:COG1127 86 MLFQGGALfD-SLTVFENVAFPLREHtDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDPEILL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 521328941 156 LDEPTVGLDIESRHLILRVVQALAHSQSVSVLWATHLFEEVKHN-NNLIVLSKGRVLAHDQCEALLA 221
Cdd:COG1127 165 YDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIaDRVAVLADGKIIAEGTPEELLA 231
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
3-219 |
9.63e-39 |
|
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: 134.23 E-value: 9.63e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 3 IAVQAVSHQYGGHHALDNINLCLKPG-LTMLLGPNGAGKSTLFALITGLQKL-----TQGSITFDGATLSQSRTSIMA-- 74
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGeITALIGPSGCGKSTLLRLLNRLNDLipgapDEGEVLLDGKDIYDLDVDVLElr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 75 -KMGVVFQQSTLdIDLSVKQNLSYFASLHGISTASALSHI-------QGLLDELdltsKLNTKIRNLNGGHRRRVELARC 146
Cdd:cd03260 81 rRVGMVFQKPNP-FPGSIYDNVAYGLRLHGIKLKEELDERveealrkAALWDEV----KDRLHALGLSGGQQQRLCLARA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 521328941 147 LIHKPSLLLLDEPTVGLDIESRHLILRVVQALAHsqSVSVLWATHLFEEVKH-NNNLIVLSKGRVLAHDQCEAL 219
Cdd:cd03260 156 LANEPEVLLLDEPTSALDPISTAKIEELIAELKK--EYTIVIVTHNMQQAARvADRTAFLLNGRLVEFGPTEQI 227
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
8-209 |
1.09e-38 |
|
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: 131.60 E-value: 1.09e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 8 VSHQYGGHHALDNINLCLKPG-LTMLLGPNGAGKSTLFALITGLQKLTQGSITFDGATLSQ-SRTSIMAKMGVVFQQStl 85
Cdd:cd00267 5 LSFRYGGRTALDNVSLTLKAGeIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKlPLEELRRRIGYVPQLS-- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 86 didlsvkqnlsyfaslhgistasalshiqglldeldltsklntkirnlnGGHRRRVELARCLIHKPSLLLLDEPTVGLDI 165
Cdd:cd00267 83 -------------------------------------------------GGQRQRVALARALLLNPDLLLLDEPTSGLDP 113
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 521328941 166 ESRHLILRVVQALAhSQSVSVLWATHLFEEV-KHNNNLIVLSKGR 209
Cdd:cd00267 114 ASRERLLELLRELA-EEGRTVIIVTHDPELAeLAADRVIVLKDGK 157
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
5-209 |
4.93e-38 |
|
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: 131.82 E-value: 4.93e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 5 VQAVSHQYGGHH--ALDNINLCLKPG-LTMLLGPNGAGKSTLFALITGLQKLTQGSITFDGATLSQSRTSIMAKM-GVVF 80
Cdd:cd03225 2 LKNLSFSYPDGArpALDDISLTIKKGeFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKvGLVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 81 QQStlD---IDLSVKQNLSYFASLHGISTASALSHIQGLLDELDLTSKLNTKIRNLNGGHRRRVELARCLIHKPSLLLLD 157
Cdd:cd03225 82 QNP--DdqfFGPTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLD 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 521328941 158 EPTVGLDIESRHLILRVVQALaHSQSVSVLWATHLFEEVKHN-NNLIVLSKGR 209
Cdd:cd03225 160 EPTAGLDPAGRRELLELLKKL-KAEGKTIIIVTHDLDLLLELaDRVIVLEDGK 211
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
3-210 |
9.94e-38 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 131.09 E-value: 9.94e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 3 IAVQAVSHQYGGHHALDNINLCLKPGLTMLL-GPNGAGKSTLFALITGLQKLTQGSITFDGATLSQ-SRTSIMAKMGVVF 80
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAItGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAmPPPEWRRQVAYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 81 QQSTLdIDLSVKQNLSYFASLHGISTASAlsHIQGLLDELDLT-SKLNTKIRNLNGGHRRRVELARCLIHKPSLLLLDEP 159
Cdd:COG4619 81 QEPAL-WGGTVRDNLPFPFQLRERKFDRE--RALELLERLGLPpDILDKPVERLSGGERQRLALIRALLLQPDVLLLDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 521328941 160 TVGLDIESRHLILRVVQALAHSQSVSVLWATHLFEEVKH-NNNLIVLSKGRV 210
Cdd:COG4619 158 TSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERvADRVLTLEAGRL 209
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
4-212 |
3.09e-37 |
|
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: 128.71 E-value: 3.09e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 4 AVQAVSHQYGGHHALDNINLCLKPG-LTMLLGPNGAGKSTLFALITGLQKLTQGSITFDGATLSQSRTSIMAK-MGVVFQ 81
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGeIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARkIAYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 82 qstldidlsvkqnlsyfaslhgistasalshiqgLLDELDLTSKLNTKIRNLNGGHRRRVELARCLIHKPSLLLLDEPTV 161
Cdd:cd03214 81 ----------------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTS 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 521328941 162 GLDIESRHLILRVVQALAHSQSVSVLWATH-LFEEVKHNNNLIVLSKGRVLA 212
Cdd:cd03214 127 HLDIAHQIELLELLRRLARERGKTVVMVLHdLNLAARYADRVILLKDGRIVA 178
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
3-220 |
3.49e-37 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 130.59 E-value: 3.49e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 3 IAVQAVSHQYGGHHALDNINLCLKPG-LTMLLGPNGAGKSTLFALITG-LQKLTQGSITFDGATLSqsRTSIM---AKMG 77
Cdd:COG1119 4 LELRNVTVRRGGKTILDDISWTVKPGeHWAILGPNGAGKSTLLSLITGdLPPTYGNDVRLFGERRG--GEDVWelrKRIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 78 VV--FQQSTLDIDLSVKQN-LS-YFAS--LHGISTASALSHIQGLLDELDLTSKLNTKIRNLNGGHRRRVELARCLIHKP 151
Cdd:COG1119 82 LVspALQLRFPRDETVLDVvLSgFFDSigLYREPTDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIARALVKDP 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 521328941 152 SLLLLDEPTVGLDIESRHLILRVVQALAHSQSVSVLWATH----LFEEVKHnnnLIVLSKGRVLAHDQCEALL 220
Cdd:COG1119 162 ELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHhveeIPPGITH---VLLLKDGRVVAAGPKEEVL 231
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
3-191 |
6.15e-37 |
|
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: 128.80 E-value: 6.15e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 3 IAVQAVSHQYGGHHALDNINLCLKPG-LTMLLGPNGAGKSTLFALITGLQKLTQGSITFDGATLSQSRTSIM---AKMGV 78
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGeVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNINelrQKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 79 VFQQSTLDIDLSVKQNLSyFA--SLHGISTASALSHIQGLLDELDLTSKLNTKIRNLNGGHRRRVELARCLIHKPSLLLL 156
Cdd:cd03262 81 VFQQFNLFPHLTVLENIT-LApiKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLF 159
|
170 180 190
....*....|....*....|....*....|....*
gi 521328941 157 DEPTVGLDIESRHLILRVVQALAHSQSVSVLwATH 191
Cdd:cd03262 160 DEPTSALDPELVGEVLDVMKDLAEEGMTMVV-VTH 193
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
3-209 |
1.19e-36 |
|
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: 126.73 E-value: 1.19e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 3 IAVQAVSHQYGG--HHALDNINLCLKPG-LTMLLGPNGAGKSTLFALITGLQKLTQGSITFDGATLSQ-SRTSIMAKMGV 78
Cdd:cd03228 1 IEFKNVSFSYPGrpKPVLKDVSLTIKPGeKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDlDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 79 VFQQSTLdIDLSVKQNLsyfaslhgistasaLShiqglldeldltsklntkirnlnGGHRRRVELARCLIHKPSLLLLDE 158
Cdd:cd03228 81 VPQDPFL-FSGTIRENI--------------LS-----------------------GGQRQRIAIARALLRDPPILILDE 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 521328941 159 PTVGLDIESRHLILRVVQALahSQSVSVLWATHLFEEVKHNNNLIVLSKGR 209
Cdd:cd03228 123 ATSALDPETEALILEALRAL--AKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
2-222 |
1.69e-36 |
|
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: 135.73 E-value: 1.69e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 2 EIAVQAVSHQYGGHH--ALDNINLCLKPG-LTMLLGPNGAGKSTLFALITGLQKLTQGSITFDGATLSQ-SRTSIMAKMG 77
Cdd:COG2274 473 DIELENVSFRYPGDSppVLDNISLTIKPGeRVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQiDPASLRRQIG 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 78 VVFQqstlDIDL---SVKQNLSYF---ASLHGISTASALSHIQGLLDELDLtsKLNTKI----RNLNGGHRRRVELARCL 147
Cdd:COG2274 553 VVLQ----DVFLfsgTIRENITLGdpdATDEEIIEAARLAGLHDFIEALPM--GYDTVVgeggSNLSGGQRQRLAIARAL 626
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 521328941 148 IHKPSLLLLDEPTVGLDIESRHLILRVVQALAHSQSVSVlwATHLFEEVKHNNNLIVLSKGRVLAHDQCEALLAK 222
Cdd:COG2274 627 LRNPRILILDEATSALDAETEAIILENLRRLLKGRTVII--IAHRLSTIRLADRIIVLDKGRIVEDGTHEELLAR 699
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1-212 |
2.26e-36 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 128.74 E-value: 2.26e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 1 MEIAVQAVSHQYGGHHALDNINLCLKPG-LTMLLGPNGAGKSTLFALITGLQKLTQGSITFDGATLSQSRTSIMAKM-GV 78
Cdd:PRK13548 1 AMLEARNLSVRLGGRTLLDDVSLTLRPGeVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRrAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 79 VFQQSTLDIDLSVKQNLSYFASLHGISTASALSHIQGLLDELDLTSKLNTKIRNLNGGHRRRVELARCLI------HKPS 152
Cdd:PRK13548 81 LPQHSSLSFPFTVEEVVAMGRAPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAqlwepdGPPR 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 521328941 153 LLLLDEPTVGLDIESRHLILRVVQALAHSQSVSVLwathlfeEVKHNNNL--------IVLSKGRVLA 212
Cdd:PRK13548 161 WLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVI-------VVLHDLNLaaryadriVLLHQGRLVA 221
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
16-223 |
2.86e-36 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 130.21 E-value: 2.86e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 16 HALDNINLCLKPG-LTMLLGPNGAGKSTLFALITGLQKLTQGSITFDGATLSQSRTSIMAKMGVVF-QQSTLDIDLSVKQ 93
Cdd:COG4586 36 EAVDDISFTIEPGeIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPFKRRKEFARRIGVVFgQRSQLWWDLPAID 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 94 NLSYFASLHGISTASALSHIQGLLDELDLTSKLNTKIRNLNGGHRRRVELARCLIHKPSLLLLDEPTVGLDIESRHLILR 173
Cdd:COG4586 116 SFRLLKAIYRIPDAEYKKRLDELVELLDLGELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIRE 195
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 521328941 174 VVQALAHSQSVSVLWATHLFEEVKH-NNNLIVLSKGRVLAHDQCEALLAKY 223
Cdd:COG4586 196 FLKEYNRERGTTILLTSHDMDDIEAlCDRVIVIDHGRIIYDGSLEELKERF 246
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
3-226 |
7.86e-36 |
|
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: 126.85 E-value: 7.86e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 3 IAVQAVSHQYGGHHALDNINLCLKPG-LTMLLGPNGAGKSTLFALITGLQKLTQGSITFDG---ATLSQS-RTSIMAKMG 77
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGeILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGediSGLSEAeLYRLRRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 78 VVFQQSTLDIDLSVKQNLSYFASLHgistaSALSH--IQGL----LDELDLTSKLNTKIRNLNGGHRRRVELARCLIHKP 151
Cdd:cd03261 81 MLFQSGALFDSLTVFENVAFPLREH-----TRLSEeeIREIvlekLEAVGLRGAEDLYPAELSGGMKKRVALARALALDP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 521328941 152 SLLLLDEPTVGLDIESRHLILRVVQALAHSQSVSVLWATHLFEEV-KHNNNLIVLSKGRVLAHDQCEALLAKYHQQ 226
Cdd:cd03261 156 ELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAfAIADRIAVLYDGKIVAEGTPEELRASDDPL 231
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
3-211 |
1.29e-35 |
|
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: 125.41 E-value: 1.29e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 3 IAVQAVSHQYGGHHALDNINLCLKPG-LTMLLGPNGAGKSTLFALITGLQKLTQGSITFDGATLsQSRTSIMAKMGVVFQ 81
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGeIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSY-QKNIEALRRIGALIE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 82 QSTLDIDLSVKQNLSYFASLHGISTASalshIQGLLDELDLTSKLNTKIRNLNGGHRRRVELARCLIHKPSLLLLDEPTV 161
Cdd:cd03268 80 APGFYPNLTARENLRLLARLLGIRKKR----IDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTN 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 521328941 162 GLDIESRHLILRVVQALAhSQSVSVLWATHLFEEV-KHNNNLIVLSKGRVL 211
Cdd:cd03268 156 GLDPDGIKELRELILSLR-DQGITVLISSHLLSEIqKVADRIGIINKGKLI 205
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
3-225 |
2.45e-35 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 128.29 E-value: 2.45e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 3 IAVQAVSHQYGGHHALDNINLCLKPG--LTmLLGPNGAGKSTLFALITGLQKLTQGSITFDGATLS----QSRtsimaKM 76
Cdd:COG3842 6 LELENVSKRYGDVTALDDVSLSIEPGefVA-LLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTglppEKR-----NV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 77 GVVFQQSTLDIDLSVKQNLSYFASLHGISTASALSHIQGLLDELDLTSKLNTKIRNLNGGHRRRVELARCLIHKPSLLLL 156
Cdd:COG3842 80 GMVFQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 157 DEPTVGLD----IESRHLILRVVQALAhsqsVSVLWATHLFEE-------VkhnnnlIVLSKGRVLAHDQCEALlakYHQ 225
Cdd:COG3842 160 DEPLSALDaklrEEMREELRRLQRELG----ITFIYVTHDQEEalaladrI------AVMNDGRIEQVGTPEEI---YER 226
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
3-221 |
4.73e-35 |
|
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: 130.41 E-value: 4.73e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 3 IAVQAVSHQY-----GGHHALDNINLCLKPGLTM-LLGPNGAGKSTLFALITGLQKLTQGSITFDGATLS----QSRTSI 72
Cdd:COG1123 261 LEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLgLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTklsrRSLREL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 73 MAKMGVVFQ--QSTLDIDLSVKQNLSYFASLHGISTASALS-HIQGLLDELDLTSK-LNTKIRNLNGGHRRRVELARCLI 148
Cdd:COG1123 341 RRRVQMVFQdpYSSLNPRMTVGDIIAEPLRLHGLLSRAERReRVAELLERVGLPPDlADRYPHELSGGQRQRVAIARALA 420
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 521328941 149 HKPSLLLLDEPTVGLDIESRHLILRVVQALAHSQSVSVLWATHLFEEVKH-NNNLIVLSKGRVLAHDQCEALLA 221
Cdd:COG1123 421 LEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYiADRVAVMYDGRIVEDGPTEEVFA 494
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
3-209 |
1.39e-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: 1.39e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 3 IAVQAVSHQYGGHHALDNINLCLKPG-LTMLLGPNGAGKSTLFALITGLQKLTQGSITFDG---ATLSQSRTSIMAKMGV 78
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGeIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGedlTDLEDELPPLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 79 VFQQSTLDIDLSVKQNLSYfaslhgistasALShiqglldeldltsklntkirnlnGGHRRRVELARCLIHKPSLLLLDE 158
Cdd:cd03229 81 VFQDFALFPHLTVLENIAL-----------GLS-----------------------GGQQQRVALARALAMDPDVLLLDE 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 521328941 159 PTVGLDIESRHLILRVVQALAHSQSVSVLWATHLFEEVKH-NNNLIVLSKGR 209
Cdd:cd03229 127 PTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARlADRVVVLRDGK 178
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
20-212 |
2.11e-34 |
|
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: 122.40 E-value: 2.11e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 20 NINLCLKPGLTMLLGPNGAGKSTLFALITGLQKLTQGSITFDGATLSQSRTSIMA-----KMGVVFQQSTLDIDLSVKQN 94
Cdd:cd03297 16 KIDFDLNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRKKINLppqqrKIGLVFQQYALFPHLNVREN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 95 LSYfaSLHGISTASALSHIQGLLDELDLTSKLNTKIRNLNGGHRRRVELARCLIHKPSLLLLDEPTVGLDIESRHLILRV 174
Cdd:cd03297 96 LAF--GLKRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPE 173
|
170 180 190
....*....|....*....|....*....|....*....
gi 521328941 175 VQALAHSQSVSVLWATHLFEEV-KHNNNLIVLSKGRVLA 212
Cdd:cd03297 174 LKQIKKNLNIPVIFVTHDLSEAeYLADRIVVMEDGRLQY 212
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-164 |
2.57e-34 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 122.83 E-value: 2.57e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 1 MEIAVQAVSHQYGGHHALDNINLCLKPG-LTMLLGPNGAGKSTLFALITGLQKLTQGSITFDGATLSQSRTSIMAKMGV- 78
Cdd:COG1137 2 MTLEAENLVKSYGKRTVVKDVSLEVNQGeIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMHKRARLGIg 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 79 -------VFQqstldiDLSVKQNLSYFASLHGISTASALSHIQGLLDELDLTSKLNTKIRNLNGGHRRRVELARCLIHKP 151
Cdd:COG1137 82 ylpqeasIFR------KLTVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNP 155
|
170
....*....|...
gi 521328941 152 SLLLLDEPTVGLD 164
Cdd:COG1137 156 KFILLDEPFAGVD 168
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
3-212 |
5.80e-34 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 122.53 E-value: 5.80e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 3 IAVQAVSHQYGGHHALDNINLCLKPG-LTMLLGPNGAGKSTLFALITGLQKLTQGSITFDGATLSQSRTSIMAKM-GVVF 80
Cdd:COG4559 2 LEAENLSVRLGGRTLLDDVSLTLRPGeLTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRrAVLP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 81 QQSTLDIDLSVKQNLSYFASLHGISTASALSHIQGLLDELDLTSKLNTKIRNLNGGHRRRVELARCLI-------HKPSL 153
Cdd:COG4559 82 QHSSLAFPFTVEEVVALGRAPHGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLAqlwepvdGGPRW 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 521328941 154 LLLDEPTVGLDIESRHLILRVVQALAHsQSVSVLwathlfeEVKHNNNL--------IVLSKGRVLA 212
Cdd:COG4559 162 LFLDEPTSALDLAHQHAVLRLARQLAR-RGGGVV-------AVLHDLNLaaqyadriLLLHQGRLVA 220
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
3-210 |
9.36e-34 |
|
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: 121.52 E-value: 9.36e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 3 IAVQAVSHQYG-GHHALDNINLCLKPG-LTMLLGPNGAGKSTLFALITGLQKLTQGSITFDGATLSQSRT----SIMAKM 76
Cdd:cd03256 1 IEVENLSKTYPnGKKALKDVSLSINPGeFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGkalrQLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 77 GVVFQQSTLDIDLSVKQN-----LSYFASLHGISTASALSHIQG---LLDELDLTSKLNTKIRNLNGGHRRRVELARCLI 148
Cdd:cd03256 81 GMIFQQFNLIERLSVLENvlsgrLGRRSTWRSLFGLFPKEEKQRalaALERVGLLDKAYQRADQLSGGQQQRVAIARALM 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 521328941 149 HKPSLLLLDEPTVGLDIESRHLILRVVQALAHSQSVSVLWATHLFEEVKHNNNLIV-LSKGRV 210
Cdd:cd03256 161 QQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVgLKDGRI 223
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
3-222 |
3.64e-33 |
|
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: 125.65 E-value: 3.64e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 3 IAVQAVSHQYGGHH--ALDNINLCLKPG-LTMLLGPNGAGKSTLFALITGLQKLTQGSITFDGATLSQ-SRTSIMAKMGV 78
Cdd:COG4987 334 LELEDVSFRYPGAGrpVLDGLSLTLPPGeRVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDlDEDDLRRRIAV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 79 VFQQSTLdIDLSVKQNLsyfasLHGISTAS------ALsHIQGLLDELD-LTSKLNTKI----RNLNGGHRRRVELARCL 147
Cdd:COG4987 414 VPQRPHL-FDTTLRENL-----RLARPDATdeelwaAL-ERVGLGDWLAaLPDGLDTWLgeggRRLSGGERRRLALARAL 486
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 521328941 148 IHKPSLLLLDEPTVGLDIESRHLILRVVQALAHSQsvSVLWATHLFEEVKHNNNLIVLSKGRVLAHDQCEALLAK 222
Cdd:COG4987 487 LRDAPILLLDEPTEGLDAATEQALLADLLEALAGR--TVLLITHRLAGLERMDRILVLEDGRIVEQGTHEELLAQ 559
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
2-222 |
6.24e-33 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 125.28 E-value: 6.24e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 2 EIAVQAVSHQY-GGHHALDNINLCLKPGLTM-LLGPNGAGKSTLFALITGLQKLTQGSITFDGATLSQ-SRTSIMAKMGV 78
Cdd:COG1132 339 EIEFENVSFSYpGDRPVLKDISLTIPPGETVaLVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDlTLESLRRQIGV 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 79 VFQQSTLdIDLSVKQNLSYF---ASLHGISTASALSHIQGLLDELDltSKLNTKI----RNLNGGHRRRVELARCLIHKP 151
Cdd:COG1132 419 VPQDTFL-FSGTIRENIRYGrpdATDEEVEEAAKAAQAHEFIEALP--DGYDTVVgergVNLSGGQRQRIAIARALLKDP 495
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 521328941 152 SLLLLDEPTVGLDIESRHLILRVVQALahSQSVSVLWATHLFEEVKHNNNLIVLSKGRVLA---HDQceaLLAK 222
Cdd:COG1132 496 PILILDEATSALDTETEALIQEALERL--MKGRTTIVIAHRLSTIRNADRILVLDDGRIVEqgtHEE---LLAR 564
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
3-221 |
1.02e-32 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 118.70 E-value: 1.02e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 3 IAVQAVSHQYGGHHAldNINLCLKPG-LTMLLGPNGAGKSTLFALITGLQKLTQGSITFDGATLSqsRTSIMA-KMGVVF 80
Cdd:COG3840 2 LRLDDLTYRYGDFPL--RFDLTIAAGeRVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLT--ALPPAErPVSMLF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 81 QQSTLDIDLSVKQNLSYfaslhGIS-----TASALSHIQGLLDELDLTSKLNTKIRNLNGGHRRRVELARCLIHKPSLLL 155
Cdd:COG3840 78 QENNLFPHLTVAQNIGL-----GLRpglklTAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 521328941 156 LDEPTVGLDIESRHLILRVVQALAHSQSVSVLWATHLFEEVKHN-NNLIVLSKGRVLAHDQCEALLA 221
Cdd:COG3840 153 LDEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIaDRVLLVADGRIAADGPTAALLD 219
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
3-214 |
1.11e-32 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 118.66 E-value: 1.11e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 3 IAVQAVSHQYGGHHALDNINLCLKPG-LTMLLGPNGAGKSTLFALITGLQKLTQGSITFDGATLSQSRTS---IMAKMGV 78
Cdd:PRK09493 2 IEFKNVSKHFGPTQVLHNIDLNIDQGeVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDerlIRQEAGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 79 VFQQSTLDIDLSVKQNLSyFASLH--GISTASALSHIQGLLDELDLTSKLNTKIRNLNGGHRRRVELARCLIHKPSLLLL 156
Cdd:PRK09493 82 VFQQFYLFPHLTALENVM-FGPLRvrGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLF 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 521328941 157 DEPTVGLDIESRHLILRVVQALAhSQSVSVLWATHlfeEV----KHNNNLIVLSKGRVlAHD 214
Cdd:PRK09493 161 DEPTSALDPELRHEVLKVMQDLA-EEGMTMVIVTH---EIgfaeKVASRLIFIDKGRI-AED 217
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
3-229 |
1.43e-32 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 124.85 E-value: 1.43e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 3 IAVQAVSHQYGGHHALDNINLCLKPGLTM-LLGPNGAGKSTLFALITGLQKLTQGSITFDGATLSQS--RTSI---MAKM 76
Cdd:NF033858 2 ARLEGVSHRYGKTVALDDVSLDIPAGCMVgLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMADArhRRAVcprIAYM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 77 ----GvvfqqSTLDIDLSVKQNLSYFASLHGISTASALSHIQGLLDELDLTSKLNTKIRNLNGGHRRRVELARCLIHKPS 152
Cdd:NF033858 82 pqglG-----KNLYPTLSVFENLDFFGRLFGQDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCALIHDPD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 153 LLLLDEPTVGLDIESRH----LI--LRvvqalAHSQSVSVLWATHLFEEVKHNNNLIVLSKGRVLAHDQCEALLAKYHQQ 226
Cdd:NF033858 157 LLILDEPTTGVDPLSRRqfweLIdrIR-----AERPGMSVLVATAYMEEAERFDWLVAMDAGRVLATGTPAELLARTGAD 231
|
...
gi 521328941 227 DIE 229
Cdd:NF033858 232 TLE 234
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
3-210 |
3.06e-32 |
|
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: 116.74 E-value: 3.06e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 3 IAVQAVSHQY-GGHHALDNINLCLKPG-LTMLLGPNGAGKSTLFALITGLQKLTQGSITFDGATLSQSRTSIMA----KM 76
Cdd:cd03292 1 IEFINVTKTYpNGTAALDGINISISAGeFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPylrrKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 77 GVVFQQSTLDIDLSVKQNLSYFASLHGISTASALSHIQGLLDELDLTSKLNTKIRNLNGGHRRRVELARCLIHKPSLLLL 156
Cdd:cd03292 81 GVVFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 521328941 157 DEPTVGLDIESRHLILRVVQALaHSQSVSVLWATH---LFEEVKHnnNLIVLSKGRV 210
Cdd:cd03292 161 DEPTGNLDPDTTWEIMNLLKKI-NKAGTTVVVATHakeLVDTTRH--RVIALERGKL 214
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1-212 |
4.51e-32 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 119.87 E-value: 4.51e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 1 MEIAVQAVSHQYGGHHALDNINLCLKPG-LTMLLGPNGAGKSTLFALITGLQKLTQGSITFDGATL-----SQSRtsima 74
Cdd:COG1118 1 MSIEVRNISKRFGSFTLLDDVSLEIASGeLVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLftnlpPRER----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 75 KMGVVFQQSTLDIDLSVKQNLSYFASLHGISTASALSHIQGLLDELDLTSKLNTKIRNLNGGHRRRVELARCLIHKPSLL 154
Cdd:COG1118 76 RVGFVFQHYALFPHMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 521328941 155 LLDEPTVGLDIESRHLILRVVQALAHSQSVSVLWATHLFEEVKHN-NNLIVLSKGRVLA 212
Cdd:COG1118 156 LLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELaDRVVVMNQGRIEQ 214
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
5-213 |
1.16e-31 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 116.34 E-value: 1.16e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 5 VQAVSHQYGGHHALDNINLCLKPG-LTMLLGPNGAGKSTLFALITGLQKLTQGSITFDGATLSQSRtsimAKMGVVFQQS 83
Cdd:PRK11248 4 ISHLYADYGGKPALEDINLTLESGeLLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPG----AERGVVFQNE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 84 TLDIDLSVKQNLSYFASLHGISTASALSHIQGLLDELDLTSKLNTKIRNLNGGHRRRVELARCLIHKPSLLLLDEPTVGL 163
Cdd:PRK11248 80 GLLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGAL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 521328941 164 DIESRHLILRVVQALAHSQSVSVLWATHLFEE-VKHNNNLIVLS--KGRVLAH 213
Cdd:PRK11248 160 DAFTREQMQTLLLKLWQETGKQVLLITHDIEEaVFMATELVLLSpgPGRVVER 212
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1-210 |
1.43e-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: 115.90 E-value: 1.43e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 1 MEIAVQAVSHQYGGHHALDNINLCLKPG-LTMLLGPNGAGKSTLFALITGLQKLTQGSITFDGATLSQsRTSIMAKMGVV 79
Cdd:cd03296 1 MSIEVRNVSKRFGDFVALDDVSLDIPSGeLVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATD-VPVQERNVGFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 80 FQQSTLDIDLSVKQNLSYFASLHGISTASALSHIQG----LLDELDLTSKLNTKIRNLNGGHRRRVELARCLIHKPSLLL 155
Cdd:cd03296 80 FQHYALFRHMTVFDNVAFGLRVKPRSERPPEAEIRAkvheLLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 521328941 156 LDEPTVGLDIESRHLILRVVQALAHSQSVSVLWATHLFEE-VKHNNNLIVLSKGRV 210
Cdd:cd03296 160 LDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEaLEVADRVVVMNKGRI 215
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
2-191 |
2.33e-31 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 117.87 E-value: 2.33e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 2 EIAVQAVSHQYGGHHALDNINLCLKPG-LTMLLGPNGAGKSTLFALITGLQKLTQGSITFDGATLsqsrTSIMAK---MG 77
Cdd:COG3839 3 SLELENVSKSYGGVEALKDIDLDIEDGeFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDV----TDLPPKdrnIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 78 VVFQQSTLDIDLSVKQNLSYFASLHGISTASALSHIQGLLDELDLTSKLNTKIRNLNGGHRRRVELARCLIHKPSLLLLD 157
Cdd:COG3839 79 MVFQSYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFLLD 158
|
170 180 190
....*....|....*....|....*....|....*...
gi 521328941 158 EPTVGLD----IESRHLILRVVQALahsqSVSVLWATH 191
Cdd:COG3839 159 EPLSNLDaklrVEMRAEIKRLHRRL----GTTTIYVTH 192
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
3-210 |
3.51e-31 |
|
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: 114.64 E-value: 3.51e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 3 IAVQAVSHQYGGHHALDNINLCLKPG--LTmLLGPNGAGKSTLFALITGLQKLTQGSITFDGatlsQSRTSIMA---KMG 77
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGefFT-LLGPSGCGKTTLLRLIAGFETPTSGEILLDG----KDITNLPPhkrPVN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 78 VVFQQSTLDIDLSVKQNLSYFASLHGISTASALSHIQGLLDELDLTSKLNTKIRNLNGGHRRRVELARCLIHKPSLLLLD 157
Cdd:cd03300 76 TVFQNYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 521328941 158 EPTVGLDIESRHLILRVVQALAHSQSVSVLWATHLFEE-VKHNNNLIVLSKGRV 210
Cdd:cd03300 156 EPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEaLTMSDRIAVMNKGKI 209
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
3-210 |
3.59e-31 |
|
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: 114.60 E-value: 3.59e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 3 IAVQAVSHQYGGH----HALDNINLCLKPG-LTMLLGPNGAGKSTLFALITGLQKLTQGSITFDGATLSQ----SRTSIM 73
Cdd:cd03258 2 IELKNVSKVFGDTggkvTALKDVSLSVPKGeIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLlsgkELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 74 AKMGVVFQQSTLDIDLSVKQNLSYFASLHGISTASALSHIQGLLDELDLTSKLNTKIRNLNGGHRRRVELARCLIHKPSL 153
Cdd:cd03258 82 RRIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKV 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 521328941 154 LLLDEPTVGLDIESRHLILRVVQALAHSQSVSVLWATHLFEEVKH-NNNLIVLSKGRV 210
Cdd:cd03258 162 LLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRiCDRVAVMEKGEV 219
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
3-197 |
4.13e-31 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 119.35 E-value: 4.13e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 3 IAVQAVSHQYGGHHALDNINLCLKPG-LTMLLGPNGAGKSTLFALITGLQKLTQGSITFDGATLSQS--RTSIMAKMGVV 79
Cdd:COG1129 5 LEMRGISKSFGGVKALDGVSLELRPGeVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRspRDAQAAGIAII 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 80 FQQSTLDIDLSVKQNL---SYFASLHGISTASALSHIQGLLDELDLTSKLNTKIRNLNGGHRRRVELARCLIHKPSLLLL 156
Cdd:COG1129 85 HQELNLVPNLSVAENIflgREPRRGGLIDWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRDARVLIL 164
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 521328941 157 DEPTVGL-DIESRHLiLRVVQALAhSQSVSVLWATHLFEEVK 197
Cdd:COG1129 165 DEPTASLtEREVERL-FRIIRRLK-AQGVAIIYISHRLDEVF 204
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
3-213 |
6.91e-31 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 114.32 E-value: 6.91e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 3 IAVQAVSHQYGGHHALDNINLCLKPG-LTMLLGPNGAGKSTLFALITGLQKLTQGSITFDGATLSQSRTSIMAKMGVV-- 79
Cdd:PRK11300 6 LSVSGLMMRFGGLLAVNNVNLEVREQeIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIARMGVVrt 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 80 FQQSTLDIDLSVKQNL----------SYFASLHGI-----STASALSHIQGLLDELDLTSKLNTKIRNLNGGHRRRVELA 144
Cdd:PRK11300 86 FQHVRLFREMTVIENLlvaqhqqlktGLFSGLLKTpafrrAESEALDRAATWLERVGLLEHANRQAGNLAYGQQRRLEIA 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 521328941 145 RCLIHKPSLLLLDEPTVGLD----IESRHLILRvvqaLAHSQSVSVLWATHLFEEVKHNNNLI-VLSKGRVLAH 213
Cdd:PRK11300 166 RCMVTQPEILMLDEPAAGLNpketKELDELIAE----LRNEHNVTVLLIEHDMKLVMGISDRIyVVNQGTPLAN 235
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
3-213 |
2.79e-30 |
|
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: 110.21 E-value: 2.79e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 3 IAVQAVSHQYGGHHALDNINLCLKPG-LTMLLGPNGAGKSTLFALITGLQKLTQGSITFDG--ATLSQSRTSIMAKMGVV 79
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGeVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGkeVSFASPRDARRAGIAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 80 FQqstldidlsvkqnlsyfaslhgistasalshiqglldeldltsklntkirnLNGGHRRRVELARCLIHKPSLLLLDEP 159
Cdd:cd03216 81 YQ---------------------------------------------------LSVGERQMVEIARALARNARLLILDEP 109
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 521328941 160 TVGLDI-ESRHLiLRVVQALAhSQSVSVLWATHLFEEVKHN-NNLIVLSKGRVLAH 213
Cdd:cd03216 110 TAALTPaEVERL-FKVIRRLR-AQGVAVIFISHRLDEVFEIaDRVTVLRDGRVVGT 163
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
1-219 |
6.02e-30 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 111.64 E-value: 6.02e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 1 MEIAVQAVSHQYGGHHALDNINLCLKPGLTM-LLGPNGAGKSTLFALITGLQKLTQGSIT-----FDGATLSQSRTSIM- 73
Cdd:COG4161 1 MSIQLKNINCFYGSHQALFDINLECPSGETLvLLGPSGAGKSSLLRVLNLLETPDSGQLNiaghqFDFSQKPSEKAIRLl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 74 -AKMGVVFQQSTLDIDLSVKQNLSYF-ASLHGISTASALSHIQGLLDELDLTSKLNTKIRNLNGGHRRRVELARCLIHKP 151
Cdd:COG4161 81 rQKVGMVFQQYNLWPHLTVMENLIEApCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEP 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 521328941 152 SLLLLDEPTVGLDIESRHLILRVVQALAHSQSVSVLwATHlfeEV----KHNNNLIVLSKGRVLAHDQCEAL 219
Cdd:COG4161 161 QVLLFDEPTAALDPEITAQVVEIIRELSQTGITQVI-VTH---EVefarKVASQVVYMEKGRIIEQGDASHF 228
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
9-210 |
7.45e-30 |
|
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: 111.06 E-value: 7.45e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 9 SHQYGGHHALDNINLCLKPGLTM-LLGPNGAGKSTLFALITGLQKLTQGSITFDG---ATLSQSRTSIMAK-MGVVFQ-- 81
Cdd:cd03257 12 PTGGGSVKALDDVSFSIKKGETLgLVGESGSGKSTLARAILGLLKPTSGSIIFDGkdlLKLSRRLRKIRRKeIQMVFQdp 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 82 QSTLDIDLSVKQNLSYFASLHGISTASALSHIQG--LLDELDLTSK-LNTKIRNLNGGHRRRVELARCLIHKPSLLLLDE 158
Cdd:cd03257 92 MSSLNPRMTIGEQIAEPLRIHGKLSKKEARKEAVllLLVGVGLPEEvLNRYPHELSGGQRQRVAIARALALNPKLLIADE 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 521328941 159 PTVGLDIESRHLILRVVQALAHSQSVSVLWATHLFEEVKH-NNNLIVLSKGRV 210
Cdd:cd03257 172 PTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKiADRVAVMYAGKI 224
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
5-221 |
1.58e-29 |
|
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: 109.83 E-value: 1.58e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 5 VQAVSHQYGGHHALDNINLCLKPG-LTMLLGPNGAGKSTLFALITGLQKLTQGSITFDGATLSQSRTSIMAKMGVVFQQS 83
Cdd:cd03224 3 VENLNAGYGKSQILFGVSLTVPEGeIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARAGIGYVPE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 84 TLDI--DLSVKQNLsyfasLHGiSTASALSHIQGLLDEL-----DLTSKLNTKIRNLNGGHRRRVELARCLIHKPSLLLL 156
Cdd:cd03224 83 GRRIfpELTVEENL-----LLG-AYARRRAKRKARLERVyelfpRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 521328941 157 DEPTVGLDIESRHLILRVVQALAhSQSVSVLwathLfeeVKHNNNLI--------VLSKGRVLAHDQCEALLA 221
Cdd:cd03224 157 DEPSEGLAPKIVEEIFEAIRELR-DEGVTIL----L---VEQNARFAleiadrayVLERGRVVLEGTAAELLA 221
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
5-164 |
3.12e-29 |
|
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: 109.67 E-value: 3.12e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 5 VQAVSHQYGGHHALDNINLCLKPG-LTMLLGPNGAGKSTLFALITGLQKLTQGSITFDGATLSQSRTSIMAKMGVVF--Q 81
Cdd:TIGR04406 4 AENLIKSYKKRKVVNDVSLSVKSGeIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHLPMHERARLGIGYlpQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 82 QSTLDIDLSVKQNLSYFASLHGISTASALSH-IQGLLDELDLTSKLNTKIRNLNGGHRRRVELARCLIHKPSLLLLDEPT 160
Cdd:TIGR04406 84 EASIFRKLTVEENIMAVLEIRKDLDRAEREErLEALLEEFQISHLRDNKAMSLSGGERRRVEIARALATNPKFILLDEPF 163
|
....
gi 521328941 161 VGLD 164
Cdd:TIGR04406 164 AGVD 167
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-213 |
3.32e-29 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 113.97 E-value: 3.32e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 1 MEIAVQA--VSHQYGGHHALDNINLCLKPG-LTMLLGPNGAGKSTLFALITGLQKLTQGSITFDGA--TLSQSRTSIMAK 75
Cdd:COG3845 2 MPPALELrgITKRFGGVVANDDVSLTVRPGeIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKpvRIRSPRDAIALG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 76 MGVVFQQSTLdID-LSVKQNLSYFA---SLHGISTASALSHIQGLLDELDLTSKLNTKIRNLNGGHRRRVELARCLIHKP 151
Cdd:COG3845 82 IGMVHQHFML-VPnLTVAENIVLGLeptKGGRLDRKAARARIRELSERYGLDVDPDAKVEDLSVGEQQRVEILKALYRGA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 521328941 152 SLLLLDEPTVGL-DIESRHLiLRVVQALAhSQSVSVLWATHLFEEVKHN-NNLIVLSKGRVLAH 213
Cdd:COG3845 161 RILILDEPTAVLtPQEADEL-FEILRRLA-AEGKSIIFITHKLREVMAIaDRVTVLRRGKVVGT 222
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
3-222 |
3.81e-29 |
|
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: 109.50 E-value: 3.81e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 3 IAVQAVSHQYG--GHHALDNINLCLKPG-LTMLLGPNGAGKSTLFALITGLQKLTQGSITFDGATLSQ-SRTSIMAKMGV 78
Cdd:cd03252 1 ITFEHVRFRYKpdGPVILDNISLRIKPGeVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALaDPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 79 VFQQSTLdIDLSVKQNLSYF---ASLHGISTASALSHIQGLLDELDL--TSKLNTKIRNLNGGHRRRVELARCLIHKPSL 153
Cdd:cd03252 81 VLQENVL-FNRSIRDNIALAdpgMSMERVIEAAKLAGAHDFISELPEgyDTIVGEQGAGLSGGQRQRIAIARALIHNPRI 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 521328941 154 LLLDEPTVGLDIESRHLILRVVQALAHSQSVSVLwaTHLFEEVKHNNNLIVLSKGRVLAHDQCEALLAK 222
Cdd:cd03252 160 LIFDEATSALDYESEHAIMRNMHDICAGRTVIII--AHRLSTVKNADRIIVMEKGRIVEQGSHDELLAE 226
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
12-221 |
5.01e-29 |
|
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: 108.92 E-value: 5.01e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 12 YGGHHALDNINLCLKPG-LTMLLGPNGAGKSTLFALITGLQKLTQGSITFDGATLSQSRTSIMAKMGV--------VFQq 82
Cdd:COG0410 13 YGGIHVLHGVSLEVEEGeIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIARLGIgyvpegrrIFP- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 83 stldiDLSVKQNLsyfasLHGISTASALSHIQGLLDEL-----DLTSKLNTKIRNLNGGHRRRVELARCLIHKPSLLLLD 157
Cdd:COG0410 92 -----SLTVEENL-----LLGAYARRDRAEVRADLERVyelfpRLKERRRQRAGTLSGGEQQMLAIGRALMSRPKLLLLD 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 521328941 158 EPTVGL--DIesRHLILRVVQALAhSQSVSVLwathLfeeVKHNNNLI--------VLSKGRVLAHDQCEALLA 221
Cdd:COG0410 162 EPSLGLapLI--VEEIFEIIRRLN-REGVTIL----L---VEQNARFAleiadrayVLERGRIVLEGTAAELLA 225
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
3-210 |
2.03e-28 |
|
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: 105.86 E-value: 2.03e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 3 IAVQAVSHQYGG--HHALDNINLCLKPGLTM-LLGPNGAGKSTLFALITGLQKLTQGSITFDGATLSQSRTSIMAKMGVV 79
Cdd:cd03247 1 LSINNVSFSYPEqeQQVLKNLSLELKQGEKIaLLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSLISVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 80 FQQSTLdIDLSVKQNLSyfaslhgistasalshiqglldeldltsklntkiRNLNGGHRRRVELARCLIHKPSLLLLDEP 159
Cdd:cd03247 81 NQRPYL-FDTTLRNNLG----------------------------------RRFSGGERQRLALARILLQDAPIVLLDEP 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 521328941 160 TVGLDIESRHLILRVVqaLAHSQSVSVLWATHLFEEVKHNNNLIVLSKGRV 210
Cdd:cd03247 126 TVGLDPITERQLLSLI--FEVLKDKTLIWITHHLTGIEHMDKILFLENGKI 174
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
3-223 |
3.93e-28 |
|
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: 107.54 E-value: 3.93e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 3 IAVQAVSHQYGG-----HHALDNINLCLKPG-LTMLLGPNGAGKSTLFALITGLQKLTQGSITFDGATLSQS----RTSI 72
Cdd:TIGR04521 1 IKLKNVSYIYQPgtpfeKKALDDVSLTIEDGeFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKkkkkLKDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 73 MAKMGVVFQQS-------TLDIDLS-VKQNLsyfaslhGISTASALSHIQGLLDELDLTSKLntKIRN---LNGGHRRRV 141
Cdd:TIGR04521 81 RKKVGLVFQFPehqlfeeTVYKDIAfGPKNL-------GLSEEEAEERVKEALELVGLDEEY--LERSpfeLSGGQMRRV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 142 ELARCLIHKPSLLLLDEPTVGLDIESRHLILRVVQALAHSQSVSVLWATHLFEEV-KHNNNLIVLSKGRVLAHDQCEALL 220
Cdd:TIGR04521 152 AIAGVLAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVaEYADRVIVMHKGKIVLDGTPREVF 231
|
...
gi 521328941 221 AKY 223
Cdd:TIGR04521 232 SDV 234
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
12-196 |
4.69e-28 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 105.39 E-value: 4.69e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 12 YGGHHALDNINLCLKPG-LTMLLGPNGAGKSTLFALITGLQKLTQGSITFDGAtlsqsrtsimAKMGVVFQQSTLD--ID 88
Cdd:NF040873 2 YGGRPVLHGVDLTIPAGsLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGG----------ARVAYVPQRSEVPdsLP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 89 LSVKQ--NLSYFA--SLHGISTASALSHIQGLLDELDLTSKLNTKIRNLNGGHRRRVELARCLIHKPSLLLLDEPTVGLD 164
Cdd:NF040873 72 LTVRDlvAMGRWArrGLWRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLD 151
|
170 180 190
....*....|....*....|....*....|..
gi 521328941 165 IESRHLILRVVqALAHSQSVSVLWATHLFEEV 196
Cdd:NF040873 152 AESRERIIALL-AEEHARGATVVVVTHDLELV 182
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
2-212 |
5.05e-28 |
|
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: 106.13 E-value: 5.05e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 2 EIAVQAVSHQYGG--HHALDNINLCLKPGLTM-LLGPNGAGKSTLFALITGLQKLTQGSITFDGATLSQ-SRTSIMAKMG 77
Cdd:cd03245 2 RIEFRNVSFSYPNqeIPALDNVSLTIRAGEKVaIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQlDPADLRRNIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 78 VVFQQSTLdIDLSVKQNLSYFASLHGISTASALSHIQGLLDELDLTSK-LNTKI----RNLNGGHRRRVELARCLIHKPS 152
Cdd:cd03245 82 YVPQDVTL-FYGTLRDNITLGAPLADDERILRAAELAGVTDFVNKHPNgLDLQIgergRGLSGGQRQAVALARALLNDPP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 521328941 153 LLLLDEPTVGLDIES-RHLILRVVQALAHSqsvSVLWATH---LFEEVkhnNNLIVLSKGRVLA 212
Cdd:cd03245 161 ILLLDEPTSAMDMNSeERLKERLRQLLGDK---TLIIITHrpsLLDLV---DRIIVMDSGRIVA 218
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
5-167 |
7.09e-28 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 110.54 E-value: 7.09e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 5 VQAVSHQYGGHHALDNINLCLKPGLTM-LLGPNGAGKSTLFALITGLQKLTQGSITFDGAtlsqsrtsimAKMGVVFQQS 83
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIgLVGRNGAGKSTLLKILAGELEPDSGEVSIPKG----------LRIGYLPQEP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 84 TLDIDLSVKQNL--------SYFASLHGISTASA--------LSHIQGLLDELD-----------------LTSKLNTKI 130
Cdd:COG0488 71 PLDDDLTVLDTVldgdaelrALEAELEELEAKLAepdedlerLAELQEEFEALGgweaearaeeilsglgfPEEDLDRPV 150
|
170 180 190
....*....|....*....|....*....|....*..
gi 521328941 131 RNLNGGHRRRVELARCLIHKPSLLLLDEPTVGLDIES 167
Cdd:COG0488 151 SELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLES 187
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
3-210 |
1.19e-27 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 105.34 E-value: 1.19e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 3 IAVQAVSHQY-GGHHALDNINLCLKPG-LTMLLGPNGAGKSTLFALITGLQKLTQGSITFDGATLSQSRTS----IMAKM 76
Cdd:PRK10908 2 IRFEHVSKAYlGGRQALQGVTFHMRPGeMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNRevpfLRRQI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 77 GVVFQQSTLDIDLSVKQNLSYFASLHGISTASALSHIQGLLDELDLTSKLNTKIRNLNGGHRRRVELARCLIHKPSLLLL 156
Cdd:PRK10908 82 GMIFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 521328941 157 DEPTVGLDIESRHLILRVVQALaHSQSVSVLWATHLFEEV-KHNNNLIVLSKGRV 210
Cdd:PRK10908 162 DEPTGNLDDALSEGILRLFEEF-NRVGVTVLMATHDIGLIsRRSYRMLTLSDGHL 215
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
3-171 |
1.77e-27 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 109.38 E-value: 1.77e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 3 IAVQAVSHQYGGHHALDNINLCLKPG-LTMLLGPNGAGKSTLFALITGLQKLTQGSITFdGATLsqsrtsimaKMGVVFQ 81
Cdd:COG0488 316 LELEGLSKSYGDKTLLDDLSLRIDRGdRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETV---------KIGYFDQ 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 82 -QSTLDIDLSVKQNLSYFASlhGISTASALSHIQGLL---DELDltsklnTKIRNLNGGHRRRVELARCLIHKPSLLLLD 157
Cdd:COG0488 386 hQEELDPDKTVLDELRDGAP--GGTEQEVRGYLGRFLfsgDDAF------KPVGVLSGGEKARLALAKLLLSPPNVLLLD 457
|
170
....*....|....
gi 521328941 158 EPTVGLDIESRHLI 171
Cdd:COG0488 458 EPTNHLDIETLEAL 471
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
8-221 |
2.51e-27 |
|
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: 108.84 E-value: 2.51e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 8 VSHQYGGHHALDNINLCLKPGLTMLL-GPNGAGKSTLFALITGL---QKLTQGSITFDGATLSQSRTSIMAK-MGVVFQQ 82
Cdd:COG1123 12 VRYPGGDVPAVDGVSLTIAPGETVALvGESGSGKSTLALALMGLlphGGRISGEVLLDGRDLLELSEALRGRrIGMVFQD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 83 STLDID-LSVKQNLSYFASLHGISTASALSHIQGLLDELDLTSKLNTKIRNLNGGHRRRVELARCLIHKPSLLLLDEPTV 161
Cdd:COG1123 92 PMTQLNpVTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPDLLIADEPTT 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 521328941 162 GLDIESRHLILRVVQALAHSQSVSVLWATHLFEEVKHN-NNLIVLSKGRVLAHDQCEALLA 221
Cdd:COG1123 172 ALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIaDRVVVMDDGRIVEDGPPEEILA 232
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
3-222 |
3.24e-27 |
|
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: 104.23 E-value: 3.24e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 3 IAVQAVSHQYGGHH--ALDNINLCLKPGLTM-LLGPNGAGKSTLFALITGLQKLTQGSITFDGATLSQ-SRTSIMAKMGV 78
Cdd:cd03251 1 VEFKNVTFRYPGDGppVLRDISLDIPAGETVaLVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDyTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 79 VFQQSTLDIDlSVKQNLSYF---ASLHGISTASALSHIQGLLDELDLtsKLNTKI----RNLNGGHRRRVELARCLIHKP 151
Cdd:cd03251 81 VSQDVFLFND-TVAENIAYGrpgATREEVEEAARAANAHEFIMELPE--GYDTVIgergVKLSGGQRQRIAIARALLKDP 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 521328941 152 SLLLLDEPTVGLDIESRHLILRVVQALAHSQSVSVLwaTHLFEEVKHNNNLIVLSKGRVLAHDQCEALLAK 222
Cdd:cd03251 158 PILILDEATSALDTESERLVQAALERLMKNRTTFVI--AHRLSTIENADRIVVLEDGKIVERGTHEELLAQ 226
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
15-210 |
7.78e-27 |
|
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: 103.32 E-value: 7.78e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 15 HHALDNINLCLKPG-LTMLLGPNGAGKSTLFALITGLQKLTQGSITFDGATLSQSRTSIM-AKMGVVFQQSTLdIDLSVK 92
Cdd:cd03248 27 TLVLQDVSFTLHPGeVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLhSKVSLVGQEPVL-FARSLQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 93 QNLSY---FASLHGISTASALSHIQGLLDELDL--TSKLNTKIRNLNGGHRRRVELARCLIHKPSLLLLDEPTVGLDIES 167
Cdd:cd03248 106 DNIAYglqSCSFECVKEAAQKAHAHSFISELASgyDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAES 185
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 521328941 168 RHLILRVVQALAHSQSVSVLwaTHLFEEVKHNNNLIVLSKGRV 210
Cdd:cd03248 186 EQQVQQALYDWPERRTVLVI--AHRLSTVERADQILVLDGGRI 226
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
3-222 |
1.16e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 104.16 E-value: 1.16e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 3 IAVQAVSHQYG-GHHALDNINLCLKPG-LTMLLGPNGAGKSTLFALITGLQKLTQGSITFDGATLSQSRTSIM---AKMG 77
Cdd:PRK13636 6 LKVEELNYNYSdGTHALKGININIKKGeVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRKGLMklrESVG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 78 VVFQQSTLDI-DLSVKQNLSYFASLHGISTASALSHIQGLLDELDLTSKLNTKIRNLNGGHRRRVELARCLIHKPSLLLL 156
Cdd:PRK13636 86 MVFQDPDNQLfSASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 521328941 157 DEPTVGLDIESRHLILRVVQALAHSQSVSVLWATHLFEEVK-HNNNLIVLSKGRVLAHDQCEALLAK 222
Cdd:PRK13636 166 DEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPlYCDNVFVMKEGRVILQGNPKEVFAE 232
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
13-191 |
7.14e-26 |
|
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: 99.80 E-value: 7.14e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 13 GGHHALDNINLCLKPG-LTMLLGPNGAGKSTLFALITGLQKLTQGSITFDGATLSQSRTSIMA---KMGVVFQQSTLDI- 87
Cdd:TIGR01166 3 GGPEVLKGLNFAAERGeVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPLDYSRKGLLErrqRVGLVFQDPDDQLf 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 88 DLSVKQNLSYFASLHGISTASALSHIQGLLDELDLTSKLNTKIRNLNGGHRRRVELARCLIHKPSLLLLDEPTVGLDIES 167
Cdd:TIGR01166 83 AADVDQDVAFGPLNLGLSEAEVERRVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAGLDPAG 162
|
170 180
....*....|....*....|....
gi 521328941 168 RHLILRVVQALaHSQSVSVLWATH 191
Cdd:TIGR01166 163 REQMLAILRRL-RAEGMTVVISTH 185
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
30-212 |
7.36e-26 |
|
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: 100.26 E-value: 7.36e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 30 TMLLGPNGAGKSTLFALITGLQKLTQGSITFDGATLSQSRTSiMAKMGVVFQQSTLDIDLSVKQN--LSYFASLHgiSTA 107
Cdd:cd03298 27 TAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPA-DRPVSMLFQENNLFAHLTVEQNvgLGLSPGLK--LTA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 108 SALSHIQGLLDELDLTSKLNTKIRNLNGGHRRRVELARCLIHKPSLLLLDEPTVGLDIESRHLILRVVQALAHSQSVSVL 187
Cdd:cd03298 104 EDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDLHAETKMTVL 183
|
170 180
....*....|....*....|....*.
gi 521328941 188 WATHLFEEVKH-NNNLIVLSKGRVLA 212
Cdd:cd03298 184 MVTHQPEDAKRlAQRVVFLDNGRIAA 209
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
1-213 |
7.74e-26 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 100.86 E-value: 7.74e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 1 MEIAVQAVSHQYGGHHALDNINLCLKPGLTM-LLGPNGAGKSTLFALITGLQKLTQGSIT-----FDGATLSQSRT--SI 72
Cdd:PRK11124 1 MSIQLNGINCFYGAHQALFDITLDCPQGETLvLLGPSGAGKSSLLRVLNLLEMPRSGTLNiagnhFDFSKTPSDKAirEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 73 MAKMGVVFQQSTLDIDLSVKQNL-SYFASLHGISTASALSHIQGLLDELDLTSKLNTKIRNLNGGHRRRVELARCLIHKP 151
Cdd:PRK11124 81 RRNVGMVFQQYNLWPHLTVQQNLiEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 521328941 152 SLLLLDEPTVGLDIESRHLILRVVQALAHSQSVSVLwATHlfeEV----KHNNNLIVLSKGRVLAH 213
Cdd:PRK11124 161 QVLLFDEPTAALDPEITAQIVSIIRELAETGITQVI-VTH---EVevarKTASRVVYMENGHIVEQ 222
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
18-210 |
1.02e-25 |
|
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: 100.49 E-value: 1.02e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 18 LDNINLCLKPG-LTMLLGPNGAGKSTLFALITGLQKLTQGSITFDGATLSqSRTSIMAKMGVVFQQSTLDIDLSVKQNLS 96
Cdd:cd03299 15 LKNVSLEVERGdYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDIT-NLPPEKRDISYVPQNYALFPHMTVYKNIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 97 YFASLHGISTASALSHIQGLLDELDLTSKLNTKIRNLNGGHRRRVELARCLIHKPSLLLLDEPTVGLDIESRHLILRVVQ 176
Cdd:cd03299 94 YGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLREELK 173
|
170 180 190
....*....|....*....|....*....|....*
gi 521328941 177 ALAHSQSVSVLWATHLFEEVKH-NNNLIVLSKGRV 210
Cdd:cd03299 174 KIRKEFGVTVLHVTHDFEEAWAlADKVAIMLNGKL 208
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
17-222 |
1.79e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 101.03 E-value: 1.79e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 17 ALDNINLCLKPG-LTMLLGPNGAGKSTLFALITGL---QKLTQGSITFDGATLSQSRT-SIMAKMGVVFQQSTLD-IDLS 90
Cdd:PRK13640 22 ALNDISFSIPRGsWTALIGHNGSGKSTISKLINGLllpDDNPNSKITVDGITLTAKTVwDIREKVGIVFQNPDNQfVGAT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 91 VKQNLSYFASLHGISTASALSHIQGLLDELDLTSKLNTKIRNLNGGHRRRVELARCLIHKPSLLLLDEPTVGLDIESRHL 170
Cdd:PRK13640 102 VGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQ 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 521328941 171 ILRVVQALAHSQSVSVLWATHLFEEVKHNNNLIVLSKGRVLAHDQCEALLAK 222
Cdd:PRK13640 182 ILKLIRKLKKKNNLTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEIFSK 233
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
3-235 |
1.88e-25 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 104.14 E-value: 1.88e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 3 IAVQAVSHQY--GGHHALDNINLCLKPGLTM-LLGPNGAGKSTLFALITGLQKLTQGSITFDGATLSQ-SRTSIMAKMGV 78
Cdd:PRK11160 339 LTLNNVSFTYpdQPQPVLKGLSLQIKAGEKVaLLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADySEAALRQAISV 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 79 VFQQstldIDL---SVKQNLsyfasLHGISTAS--ALSHIQ---GLLDELDLTSKLNTKI----RNLNGGHRRRVELARC 146
Cdd:PRK11160 419 VSQR----VHLfsaTLRDNL-----LLAAPNASdeALIEVLqqvGLEKLLEDDKGLNAWLgeggRQLSGGEQRRLGIARA 489
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 147 LIHKPSLLLLDEPTVGLDIESRHLILRVVqaLAHSQSVSVLWATHLFEEVKHNNNLIVLSKGRVLAHDQCEALLAK---Y 223
Cdd:PRK11160 490 LLHDAPLLLLDEPTEGLDAETERQILELL--AEHAQNKTVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQELLAQqgrY 567
|
250
....*....|..
gi 521328941 224 HQqdiehLWQHL 235
Cdd:PRK11160 568 YQ-----LKQRL 574
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
8-211 |
2.00e-25 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 102.11 E-value: 2.00e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 8 VSHQYGGHHALDNINLCLKPGlTM--LLGPNGAGKSTLFALITGLQKLTQGSITFDGATLSQSrtSIMAK-MGVVFQQST 84
Cdd:PRK11432 12 ITKRFGSNTVIDNLNLTIKQG-TMvtLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHR--SIQQRdICMVFQSYA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 85 LDIDLSVKQNLSYFASLHGISTASALSHIQGLLDELDLTSKLNTKIRNLNGGHRRRVELARCLIHKPSLLLLDEPTVGLD 164
Cdd:PRK11432 89 LFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSNLD 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 521328941 165 IESRHLILRVVQALAHSQSVSVLWATH-LFEEVKHNNNLIVLSKGRVL 211
Cdd:PRK11432 169 ANLRRSMREKIRELQQQFNITSLYVTHdQSEAFAVSDTVIVMNKGKIM 216
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
3-191 |
3.37e-25 |
|
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: 98.48 E-value: 3.37e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 3 IAVQAVSHQYGGHHALDNINLCLKPG-LTMLLGPNGAGKSTLFALITGLQKLTQGSITFDGATLsqsrTSIMAK---MGV 78
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGeFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDV----TDLPPKdrdIAM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 79 VFQQSTLDIDLSVKQNLSYFASLHGISTASALSHIQGLLDELDLTSKLNTKIRNLNGGHRRRVELARCLIHKPSLLLLDE 158
Cdd:cd03301 77 VFQNYALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDE 156
|
170 180 190
....*....|....*....|....*....|....*..
gi 521328941 159 PTVGLD----IESRHLILRVVQALahsqSVSVLWATH 191
Cdd:cd03301 157 PLSNLDaklrVQMRAELKRLQQRL----GTTTIYVTH 189
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
5-191 |
3.37e-25 |
|
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: 103.21 E-value: 3.37e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 5 VQAVSHQY-GGHHALDNINLCLKPG-LTMLLGPNGAGKSTLFALITGLQKLTQGSITFDGATLSQSRTSIMAKMGVVFQQ 82
Cdd:TIGR02868 337 LRDLSAGYpGAPPVLDGVSLDLPPGeRVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQ 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 83 STLDIDLSVKQNLsyfasLHGISTAS------ALSHIqGLLDELD-LTSKLNTKI----RNLNGGHRRRVELARCLIHKP 151
Cdd:TIGR02868 417 DAHLFDTTVRENL-----RLARPDATdeelwaALERV-GLADWLRaLPDGLDTVLgeggARLSGGERQRLALARALLADA 490
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 521328941 152 SLLLLDEPTVGLDIESRHLILRVVqaLAHSQSVSVLWATH 191
Cdd:TIGR02868 491 PILLLDEPTEHLDAETADELLEDL--LAALSGRTVVLITH 528
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
3-212 |
6.24e-25 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 99.32 E-value: 6.24e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 3 IAVQAVSHQYGG--HHALDNINLCLKPG-LTMLLGPNGAGKSTLFALITGLQKLTQGSITFDGATLSQSRT-SIMAKMGV 78
Cdd:PRK13635 6 IRVEHISFRYPDaaTYALKDVSFSVYEGeWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVwDVRRQVGM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 79 VFQQStlD---IDLSVKQNLSYFASLHGISTASALSHIQGLLDELDLTSKLNTKIRNLNGGHRRRVELARCLIHKPSLLL 155
Cdd:PRK13635 86 VFQNP--DnqfVGATVQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIII 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 521328941 156 LDEPTVGLDIESRHLILRVVQALAHSQSVSVLWATHLFEEVKHNNNLIVLSKGRVLA 212
Cdd:PRK13635 164 LDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQADRVIVMNKGEILE 220
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
3-180 |
6.82e-25 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 98.62 E-value: 6.82e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 3 IAVQAVSHQYGGHHALDNINLCL-KPGLTMLLGPNGAGKSTLFALITGLQKLTQGSITFDGATLSQSRTSIMAK-MGVVF 80
Cdd:COG4604 2 IEIKNVSKRYGGKVVLDDVSLTIpKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKrLAILR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 81 QQSTLDIDLSVKQNLSY--FASLHGISTASALSHIQGLLDELDLTSKLNTKIRNLNGGHRRRVELARCLIHKPSLLLLDE 158
Cdd:COG4604 82 QENHINSRLTVRELVAFgrFPYSKGRLTAEDREIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQDTDYVLLDE 161
|
170 180
....*....|....*....|....
gi 521328941 159 PTVGLDIesRHL--ILRVVQALAH 180
Cdd:COG4604 162 PLNNLDM--KHSvqMMKLLRRLAD 183
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
15-210 |
7.76e-25 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 98.62 E-value: 7.76e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 15 HHALDNINLCLKPG--LTmLLGPNGAGKSTLFALITGLQKLTQGSITFDGATLSQSRTSIMAKM-GVVFQQSTLDI--DL 89
Cdd:COG1101 19 KRALDGLNLTIEEGdfVT-VIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRAKYiGRVFQDPMMGTapSM 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 90 SVKQNLSyFASLHGIS-------TASALSHIQGLLDELD--LTSKLNTKIRNLNGGHRRRVELARCLIHKPSLLLLDEPT 160
Cdd:COG1101 98 TIEENLA-LAYRRGKRrglrrglTKKRRELFRELLATLGlgLENRLDTKVGLLSGGQRQALSLLMATLTKPKLLLLDEHT 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 521328941 161 VGLDIESRHLILRVVQALAHSQSVSVLWATHLFEE-VKHNNNLIVLSKGRV 210
Cdd:COG1101 177 AALDPKTAALVLELTEKIVEENNLTTLMVTHNMEQaLDYGNRLIMMHEGRI 227
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
2-191 |
9.00e-25 |
|
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: 101.98 E-value: 9.00e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 2 EIAVQAVSHQYGGH-HALDNINLCLKPG-LTMLLGPNGAGKSTLFALITGLQKLTQGSITFDGATLSQ-SRTSIMAKMGV 78
Cdd:TIGR02857 321 SLEFSGVSVAYPGRrPALRPVSFTVPPGeRVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADaDADSWRDQIAW 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 79 VFQQSTLdIDLSVKQNLSYF---ASLHGISTASALSHIQGLLDELDLTskLNTKI----RNLNGGHRRRVELARCLIHKP 151
Cdd:TIGR02857 401 VPQHPFL-FAGTIAENIRLArpdASDAEIREALERAGLDEFVAALPQG--LDTPIgeggAGLSGGQAQRLALARAFLRDA 477
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 521328941 152 SLLLLDEPTVGLDIESRHLILRVVQALAhsQSVSVLWATH 191
Cdd:TIGR02857 478 PLLLLDEPTAHLDAETEAEVLEALRALA--QGRTVLLVTH 515
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1-191 |
1.03e-24 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 96.87 E-value: 1.03e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 1 MEIAVQAVSHQYGGHHALDNINLCLKPGLTMLL-GPNGAGKSTLFALITGLQKLTQGSITFDG--ATLSQSRTSiMAKMG 77
Cdd:PRK13539 1 MMLEGEDLACVRGGRVLFSGLSFTLAAGEALVLtGPNGSGKTTLLRLIAGLLPPAAGTIKLDGgdIDDPDVAEA-CHYLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 78 vvfQQSTLDIDLSVKQNLSYFASLHGistaSALSHIQGLLDELDLTSKLNTKIRNLNGGHRRRVELARCLIHKPSLLLLD 157
Cdd:PRK13539 80 ---HRNAMKPALTVAENLEFWAAFLG----GEELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILD 152
|
170 180 190
....*....|....*....|....*....|....*
gi 521328941 158 EPTVGLDIESRHLILRVVQalAHS-QSVSVLWATH 191
Cdd:PRK13539 153 EPTAALDAAAVALFAELIR--AHLaQGGIVIAATH 185
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
2-222 |
1.42e-24 |
|
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: 97.30 E-value: 1.42e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 2 EIAVQAVSHQY-GGHHALDNINLCLKPGLTM-LLGPNGAGKSTLFALITGLQKLTQGSITFDGATLSQ-SRTSIMAKMGV 78
Cdd:cd03254 2 EIEFENVNFSYdEKKPVLKDINFSIKPGETVaIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDiSRKSLRSMIGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 79 VFQQSTLDIDlSVKQNLSYF---ASLHGISTASALSHIQGLLDEL--DLTSKLNTKIRNLNGGHRRRVELARCLIHKPSL 153
Cdd:cd03254 82 VLQDTFLFSG-TIMENIRLGrpnATDEEVIEAAKEAGAHDFIMKLpnGYDTVLGENGGNLSQGERQLLAIARAMLRDPKI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 521328941 154 LLLDEPTVGLDIESRHLILRVVQALAHSQSVSVLwaTHLFEEVKHNNNLIVLSKGRVLAHDQCEALLAK 222
Cdd:cd03254 161 LILDEATSNIDTETEKLIQEALEKLMKGRTSIII--AHRLSTIKNADKILVLDDGKIIEEGTHDELLAK 227
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
3-206 |
2.22e-24 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 96.71 E-value: 2.22e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 3 IAVQAVSHQYGGHHALDNINLCLKPG-LTMLLGPNGAGKSTLFALITGLQKLTQGSITFDG---ATLSQSRTSimAKMGV 78
Cdd:PRK10247 8 LQLQNVGYLAGDAKILNNISFSLRAGeFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGediSTLKPEIYR--QQVSY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 79 VFQQSTLDIDlSVKQNLSYFASLHGIstASALSHIQGLLDELDL-TSKLNTKIRNLNGGHRRRVELARCLIHKPSLLLLD 157
Cdd:PRK10247 86 CAQTPTLFGD-TVYDNLIFPWQIRNQ--QPDPAIFLDDLERFALpDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLD 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 521328941 158 EPTVGLDIESRHLILRVVQALAHSQSVSVLWATHLFEEVKHNNNLIVLS 206
Cdd:PRK10247 163 EITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDEINHADKVITLQ 211
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
3-233 |
2.54e-24 |
|
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: 96.53 E-value: 2.54e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 3 IAVQAVSHQYGGHH-ALDNINLCLKPGLTM-LLGPNGAGKSTLFALITGLQKLTQGSITFDGATLSQ-SRTSIMAKMGVV 79
Cdd:cd03253 1 IEFENVTFAYDPGRpVLKDVSFTIPAGKKVaIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREvTLDSLRRAIGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 80 FQQSTLDIDlSVKQNLSY---FASLHGISTASALSHIQGLLdeLDLTSKLNTKI--RN--LNGGHRRRVELARCLIHKPS 152
Cdd:cd03253 81 PQDTVLFND-TIGYNIRYgrpDATDEEVIEAAKAAQIHDKI--MRFPDGYDTIVgeRGlkLSGGEKQRVAIARAILKNPP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 153 LLLLDEPTVGLDIESRHLILRVVQALAHSQSVSVLwaTHLFEEVKHNNNLIVLSKGRVLAHDQCEALLAK---YHQqdie 229
Cdd:cd03253 158 ILLLDEATSALDTHTEREIQAALRDVSKGRTTIVI--AHRLSTIVNADKIIVLKDGRIVERGTHEELLAKgglYAE---- 231
|
....
gi 521328941 230 hLWQ 233
Cdd:cd03253 232 -MWK 234
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
18-213 |
3.02e-24 |
|
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: 95.31 E-value: 3.02e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 18 LDNINLCLKPG-LTMLLGPNGAGKSTLFALITGL--QKLTQGSITFDGATLSQSrtSIMAKMGVVFQQSTLDIDLSVKQN 94
Cdd:cd03213 25 LKNVSGKAKPGeLTAIMGPSGAGKSTLLNALAGRrtGLGVSGEVLINGRPLDKR--SFRKIIGYVPQDDILHPTLTVRET 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 95 LSYFASLHGIStasalshiqglldeldltsklntkirnlnGGHRRRVELARCLIHKPSLLLLDEPTVGLDIESRHLILRV 174
Cdd:cd03213 103 LMFAAKLRGLS-----------------------------GGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSL 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 521328941 175 VQALAhSQSVSVLWATH--------LFEEvkhnnnLIVLSKGRVLAH 213
Cdd:cd03213 154 LRRLA-DTGRTIICSIHqpsseifeLFDK------LLLLSQGRVIYF 193
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
3-210 |
3.74e-24 |
|
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: 94.59 E-value: 3.74e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 3 IAVQAVSHQYGG--HHALDNINLCLKPG-LTMLLGPNGAGKSTLFALITGLQKLTQGSITFDGATLSQSRTSIMAKM-GV 78
Cdd:cd03246 1 LEVENVSFRYPGaePPVLRNVSFSIEPGeSLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHvGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 79 VFQqstlDIDL---SVKQNLsyfaslhgistasalshiqglldeldltsklntkirnLNGGHRRRVELARCLIHKPSLLL 155
Cdd:cd03246 81 LPQ----DDELfsgSIAENI-------------------------------------LSGGQRQRLGLARALYGNPRILV 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 521328941 156 LDEPTVGLDIESRHLILRVVQALaHSQSVSVLWATHLFEEVKHNNNLIVLSKGRV 210
Cdd:cd03246 120 LDEPNSHLDVEGERALNQAIAAL-KAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1-210 |
5.64e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 97.04 E-value: 5.64e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 1 MEIAVQAVSHQYG-----GHHALDNINLCLKPG-LTMLLGPNGAGKSTLFALITGLQKLTQGSITFDGATLSQSR---TS 71
Cdd:PRK13637 1 MSIKIENLTHIYMegtpfEKKALDNVNIEIEDGeFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKvklSD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 72 IMAKMGVVFQ-------QSTLDIDLSV-KQNLsyfaslhGISTASALSHIQGLLD--ELDLTSKLNTKIRNLNGGHRRRV 141
Cdd:PRK13637 81 IRKKVGLVFQypeyqlfEETIEKDIAFgPINL-------GLSEEEIENRVKRAMNivGLDYEDYKDKSPFELSGGQKRRV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 142 ELARCLIHKPSLLLLDEPTVGLDIESRHLILRVVQALAHSQSVSVLWATHLFEEV-KHNNNLIVLSKGRV 210
Cdd:PRK13637 154 AIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVaKLADRIIVMNKGKC 223
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
1-222 |
1.21e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 96.24 E-value: 1.21e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 1 MEIAVQAVSHQYG-----GHHALDNINLCLKPG-LTMLLGPNGAGKSTLFALITGLQKLTQGSITFdGATLSQSRTS--- 71
Cdd:PRK13634 1 MDITFQKVEHRYQyktpfERRALYDVNVSIPSGsYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTI-GERVITAGKKnkk 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 72 ---IMAKMGVVFQ--QSTLdIDLSVKQNLSYFASLHGISTASALSHIQGLLDELDLTSKLNTKIR-NLNGGHRRRVELAR 145
Cdd:PRK13634 80 lkpLRKKVGIVFQfpEHQL-FEETVEKDICFGPMNFGVSEEDAKQKAREMIELVGLPEELLARSPfELSGGQMRRVAIAG 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 521328941 146 CLIHKPSLLLLDEPTVGLDIESRHLILRVVQALAHSQSVSVLWATHLFEEV-KHNNNLIVLSKGRVLAHDQCEALLAK 222
Cdd:PRK13634 159 VLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAaRYADQIVVMHKGTVFLQGTPREIFAD 236
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
3-212 |
1.21e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 96.03 E-value: 1.21e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 3 IAVQAVSHQYGGH-HALDNINLCL-KPGLTMLLGPNGAGKSTLFALITGLQKLTQGSITFDGATLSQSRTSIMAK-MGVV 79
Cdd:PRK13652 4 IETRDLCYSYSGSkEALNNINFIApRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKfVGLV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 80 FQQSTLDI-DLSVKQNLSYFASLHGISTASALSHIQGLLDELDLTSKLNTKIRNLNGGHRRRVELARCLIHKPSLLLLDE 158
Cdd:PRK13652 84 FQNPDDQIfSPTVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDE 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 521328941 159 PTVGLDIESRHLILRVVQALAHSQSVSVLWATHLFEEVKHNNNLI-VLSKGRVLA 212
Cdd:PRK13652 164 PTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIyVMDKGRIVA 218
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
5-195 |
3.17e-23 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 96.44 E-value: 3.17e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 5 VQAVSHQYGGHHALDNINLCLKPG-LTMLLGPNGAGKSTLFALITGLQKLTQGSITFDGATLSQSrTSIMAKMGVVFQQS 83
Cdd:PRK11607 22 IRNLTKSFDGQHAVDDVSLTIYKGeIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHV-PPYQRPINMMFQSY 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 84 TLDIDLSVKQNLSYFASLHGISTASALSHIQGLLDELDLTSKLNTKIRNLNGGHRRRVELARCLIHKPSLLLLDEPTVGL 163
Cdd:PRK11607 101 ALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGAL 180
|
170 180 190
....*....|....*....|....*....|...
gi 521328941 164 DIESR-HLILRVVQALAHSQSVSVLwATHLFEE 195
Cdd:PRK11607 181 DKKLRdRMQLEVVDILERVGVTCVM-VTHDQEE 212
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
3-174 |
3.91e-23 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 95.53 E-value: 3.91e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 3 IAVQAVSHQY----GGHHALDNINLCLKPG-LTMLLGPNGAGKSTLFALITGLQKLTQGSITFDGATLSQ-SRTSIMA-- 74
Cdd:COG1135 2 IELENLSKTFptkgGPVTALDDVSLTIEKGeIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTAlSERELRAar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 75 -KMGVVFQQSTLdidLS---VKQNLSYFASLHGISTASALSHIQGLLDELDLTSKLNTKIRNLNGGHRRRVELARCLIHK 150
Cdd:COG1135 82 rKIGMIFQHFNL---LSsrtVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANN 158
|
170 180
....*....|....*....|....
gi 521328941 151 PSLLLLDEPTVGLDIESRHLILRV 174
Cdd:COG1135 159 PKVLLCDEATSALDPETTRSILDL 182
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
8-194 |
4.38e-23 |
|
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: 92.71 E-value: 4.38e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 8 VSHQYGGHH-ALDNINLCLKPG-LTMLLGPNGAGKSTLFALITGLQKLTQGSITFDGATLSQSRTSimAKMGVVFQqsTL 85
Cdd:cd03226 5 ISFSYKKGTeILDDLSLDLYAGeIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKERR--KSIGYVMQ--DV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 86 DIDL---SVKQNLSYFASLhgisTASALSHIQGLLDELDLTSKLNTKIRNLNGGHRRRVELARCLIHKPSLLLLDEPTVG 162
Cdd:cd03226 81 DYQLftdSVREELLLGLKE----LDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSG 156
|
170 180 190
....*....|....*....|....*....|..
gi 521328941 163 LDIESRHLILRVVQALAhSQSVSVLWATHLFE 194
Cdd:cd03226 157 LDYKNMERVGELIRELA-AQGKAVIVITHDYE 187
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
14-212 |
5.50e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 93.99 E-value: 5.50e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 14 GHHALDNINLCLKPG-LTMLLGPNGAGKSTLFALITGLQKLTQGSITFDGATLSQSRTSIMA---KMGVVFQQStlDIDL 89
Cdd:PRK13639 14 GTEALKGINFKAEKGeMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSLLEvrkTVGIVFQNP--DDQL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 90 ---SVKQNLSyFASLH-GISTASALSHIQGLLDELDLTSKLNTKIRNLNGGHRRRVELARCLIHKPSLLLLDEPTVGLDI 165
Cdd:PRK13639 92 fapTVEEDVA-FGPLNlGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDP 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 521328941 166 ESRHLILRVVQALaHSQSVSVLWATHLFEEV-KHNNNLIVLSKGRVLA 212
Cdd:PRK13639 171 MGASQIMKLLYDL-NKEGITIIISTHDVDLVpVYADKVYVMSDGKIIK 217
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
13-221 |
7.73e-23 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 96.24 E-value: 7.73e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 13 GGHHALDNINLCLKPG----LTMLLGpngAGKSTLFALITGLQKLTQGSITFDGATLSQSRTSIMAKMGVVF-----QQS 83
Cdd:COG1129 263 SVGGVVRDVSFSVRAGeilgIAGLVG---AGRTELARALFGADPADSGEIRLDGKPVRIRSPRDAIRAGIAYvpedrKGE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 84 TLDIDLSVKQNLSyFASLHGISTASALSH------IQGLLDELDL-TSKLNTKIRNLNGGHRRRVELARCLIHKPSLLLL 156
Cdd:COG1129 340 GLVLDLSIRENIT-LASLDRLSRGGLLDRrreralAEEYIKRLRIkTPSPEQPVGNLSGGNQQKVVLAKWLATDPKVLIL 418
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 521328941 157 DEPTVGLDIESRHLILRVVQALAhSQSVSVLWATHLFEEVKHN-NNLIVLSKGRV---LAHDQC--EALLA 221
Cdd:COG1129 419 DEPTRGIDVGAKAEIYRLIRELA-AEGKAVIVISSELPELLGLsDRILVMREGRIvgeLDREEAteEAIMA 488
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
3-210 |
8.14e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 93.66 E-value: 8.14e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 3 IAVQAVSHQYGGHHA--LDNINLCLKPG-LTMLLGPNGAGKSTLFALITGLQKLTQGSITF-DGATLSQSRTSIMAKMGV 78
Cdd:PRK13648 8 IVFKNVSFQYQSDASftLKDVSFNIPKGqWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYnNQAITDDNFEKLRKHIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 79 VFQQSTLDIDLS-VKQNLSYFASLHGISTASALSHIQGLLDELDLTSKLNTKIRNLNGGHRRRVELARCLIHKPSLLLLD 157
Cdd:PRK13648 88 VFQNPDNQFVGSiVKYDVAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILD 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 521328941 158 EPTVGLDIESRHLILRVVQALAHSQSVSVLWATHLFEEVKHNNNLIVLSKGRV 210
Cdd:PRK13648 168 EATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAMEADHVIVMNKGTV 220
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-220 |
8.29e-23 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 95.68 E-value: 8.29e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 1 MEIAVQAVSHQYGGHHALDNINLCLKPG-LTMLLGPNGAGKSTLFALITGLQKLTQGSITFDG-ATLSQSRTSIMAKMGV 78
Cdd:PRK09536 2 PMIDVSDLSVEFGDTTVLDGVDLSVREGsLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGdDVEALSARAASRRVAS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 79 VFQQSTLDIDLSVKQ--------NLSYFASLHGISTASalshIQGLLDELDLTSKLNTKIRNLNGGHRRRVELARCLIHK 150
Cdd:PRK09536 82 VPQDTSLSFEFDVRQvvemgrtpHRSRFDTWTETDRAA----VERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 521328941 151 PSLLLLDEPTVGLDIESRHLILRVVQALAHSQSvSVLWATHLFE-EVKHNNNLIVLSKGRVLAHDQCEALL 220
Cdd:PRK09536 158 TPVLLLDEPTASLDINHQVRTLELVRRLVDDGK-TAVAAIHDLDlAARYCDELVLLADGRVRAAGPPADVL 227
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
13-211 |
8.30e-23 |
|
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: 91.82 E-value: 8.30e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 13 GGHHALDNINLCLKPGLT-MLLGPNGAGKSTLFALITGLQ--KLTQGSITFDGATLSQSRTSIMAKMGV--VFQqstldi 87
Cdd:cd03217 11 GGKEILKGVNLTIKKGEVhALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKGEDITDLPPEERARLGIflAFQ------ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 88 dlsvkqnlsYFASLHGIstasalshiqglldeldltsKLNTKIRNLN----GGHRRRVELARCLIHKPSLLLLDEPTVGL 163
Cdd:cd03217 85 ---------YPPEIPGV--------------------KNADFLRYVNegfsGGEKKRNEILQLLLLEPDLAILDEPDSGL 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 521328941 164 DIESRHLILRVVQALaHSQSVSVLWATH---LFEEVK----HnnnliVLSKGRVL 211
Cdd:cd03217 136 DIDALRLVAEVINKL-REEGKSVLIITHyqrLLDYIKpdrvH-----VLYDGRIV 184
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
3-191 |
1.97e-22 |
|
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: 90.88 E-value: 1.97e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 3 IAVQAVSHQYGGHHALDNINLCLKPG-LTMLLGPNGAGKSTLFALITGLQKLTQGSITFDGATLSQSRTSIMAKMGVVFQ 81
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGeALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 82 QSTLDIDLSVKQNLSYFASLHGistaSALSHIQGLLDELDLTSKLNTKIRNLNGGHRRRVELARCLIHKPSLLLLDEPTV 161
Cdd:TIGR01189 81 LPGLKPELSALENLHFWAAIHG----GAQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTT 156
|
170 180 190
....*....|....*....|....*....|
gi 521328941 162 GLDIESRHLILRVVQALAHSQSvSVLWATH 191
Cdd:TIGR01189 157 ALDKAGVALLAGLLRAHLARGG-IVLLTTH 185
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
12-221 |
3.13e-22 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 91.49 E-value: 3.13e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 12 YGGHHALDNINLCLKPG-LTMLLGPNGAGKSTLFALITGLQKLTQGSITFDGATLSQSRTSIMAKMGVVF--QQSTLDID 88
Cdd:PRK10895 13 YKGRRVVEDVSLTVNSGeIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRGIGYlpQEASIFRR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 89 LSVKQNLSYFASL-HGISTASALSHIQGLLDELDLTSKLNTKIRNLNGGHRRRVELARCLIHKPSLLLLDEPTVGLDIES 167
Cdd:PRK10895 93 LSVYDNLMAVLQIrDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPIS 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 521328941 168 RHLILRVVQALAHSqSVSVLWATH-LFEEVKHNNNLIVLSKGRVLAHDQCEALLA 221
Cdd:PRK10895 173 VIDIKRIIEHLRDS-GLGVLITDHnVRETLAVCERAYIVSQGHLIAHGTPTEILQ 226
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
14-210 |
3.84e-22 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 95.08 E-value: 3.84e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 14 GHHALDNINLCL-KPGLTMLLGPNGAGKSTLFALITGLQKLTQGSITFDGATLSQSRTSIMAKMGVVFQQSTLDIDLSVK 92
Cdd:TIGR01257 942 GRPAVDRLNITFyENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDAVRQSLGMCPQHNILFHHLTVA 1021
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 93 QNLSYFASLHGISTASALSHIQGLLDELDLTSKLNTKIRNLNGGHRRRVELARCLIHKPSLLLLDEPTVGLDIESRHLIL 172
Cdd:TIGR01257 1022 EHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIW 1101
|
170 180 190
....*....|....*....|....*....|....*....
gi 521328941 173 RVVqaLAHSQSVSVLWATHLFEEVK-HNNNLIVLSKGRV 210
Cdd:TIGR01257 1102 DLL--LKYRSGRTIIMSTHHMDEADlLGDRIAIISQGRL 1138
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
10-217 |
4.73e-22 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 92.63 E-value: 4.73e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 10 HQYGGHHALDnINLCLKP-GLTMLLGPNGAGKSTLFALITGLQKLTQGSITFDGATLSQSRTSI-----MAKMGVVFQQS 83
Cdd:PRK11144 7 KQQLGDLCLT-VNLTLPAqGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEKGIclppeKRRIGYVFQDA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 84 TLDIDLSVKQNLSYfaslhGIStASALSHIQGLLDELDLTSKLNTKIRNLNGGHRRRVELARCLIHKPSLLLLDEPTVGL 163
Cdd:PRK11144 86 RLFPHYKVRGNLRY-----GMA-KSMVAQFDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 521328941 164 DIESRHLILRVVQALAHSQSVSVLWATHLFEEVKH-NNNLIVLSKGRVLAHDQCE 217
Cdd:PRK11144 160 DLPRKRELLPYLERLAREINIPILYVSHSLDEILRlADRVVVLEQGKVKAFGPLE 214
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
18-211 |
7.30e-22 |
|
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: 90.02 E-value: 7.30e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 18 LDNINLCLKPGLTM-LLGPNGAGKSTLFALITGLQ---KLTQGSITFDGATLS--QSRTSImakmGVVFQQSTLDIDLSV 91
Cdd:cd03234 23 LNDVSLHVESGQVMaILGSSGSGKTTLLDAISGRVeggGTTSGQILFNGQPRKpdQFQKCV----AYVRQDDILLPGLTV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 92 KQNLSYFA--SLHGISTASALSHI--QGLLDELDLTSKLNTKIRNLNGGHRRRVELARCLIHKPSLLLLDEPTVGLDIES 167
Cdd:cd03234 99 RETLTYTAilRLPRKSSDAIRKKRveDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFT 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 521328941 168 RHLILRVVQALAHSQSVsVLWATH-----LFEevkHNNNLIVLSKGRVL 211
Cdd:cd03234 179 ALNLVSTLSQLARRNRI-VILTIHqprsdLFR---LFDRILLLSSGEIV 223
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
1-211 |
1.13e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 90.57 E-value: 1.13e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 1 MEIAVQAVSHQYGG-----HHALDNINLCLKPG-LTMLLGPNGAGKSTLFALITGLQKLTQGSITFDGATL-SQSRT--- 70
Cdd:PRK13649 1 MGINLQNVSYTYQAgtpfeGRALFDVNLTIEDGsYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLItSTSKNkdi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 71 -SIMAKMGVVFQ--QSTLdIDLSVKQNLSYFASLHGIST--ASALS----HIQGLLDELdltskLNTKIRNLNGGHRRRV 141
Cdd:PRK13649 81 kQIRKKVGLVFQfpESQL-FEETVLKDVAFGPQNFGVSQeeAEALAreklALVGISESL-----FEKNPFELSGGQMRRV 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 521328941 142 ELARCLIHKPSLLLLDEPTVGLDIESRHLILRVVQALaHSQSVSVLWATHLFEEVKHNNNLI-VLSKGRVL 211
Cdd:PRK13649 155 AIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKL-HQSGMTIVLVTHLMDDVANYADFVyVLEKGKLV 224
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
3-164 |
1.20e-21 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 91.93 E-value: 1.20e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 3 IAVQAVSHQYGGHHALDNINLCLKPG--LTmLLGPNGAGKSTLFALITGLQKLTQGSITFDGatlsQSRTSIMAK---MG 77
Cdd:PRK09452 15 VELRGISKSFDGKEVISNLDLTINNGefLT-LLGPSGCGKTTVLRLIAGFETPDSGRIMLDG----QDITHVPAEnrhVN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 78 VVFQQSTLDIDLSVKQNLSYFASLHGISTAS-------ALSHIQglLDELdltskLNTKIRNLNGGHRRRVELARCLIHK 150
Cdd:PRK09452 90 TVFQSYALFPHMTVFENVAFGLRMQKTPAAEitprvmeALRMVQ--LEEF-----AQRKPHQLSGGQQQRVAIARAVVNK 162
|
170
....*....|....
gi 521328941 151 PSLLLLDEPTVGLD 164
Cdd:PRK09452 163 PKVLLLDESLSALD 176
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
18-210 |
1.20e-21 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 93.25 E-value: 1.20e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 18 LDNINLCLKPG-LTMLLGPNGAGKSTLFALITGLQKLTQGSITFDGATLSQ-SRTSIMAKMGVVFQQSTLdIDLSVKQNL 95
Cdd:TIGR00958 497 LKGLTFTLHPGeVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQyDHHYLHRQVALVGQEPVL-FSGSVRENI 575
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 96 SY---FASLHGISTASALSHIQGLLDELdlTSKLNTKI----RNLNGGHRRRVELARCLIHKPSLLLLDEPTVGLDIESR 168
Cdd:TIGR00958 576 AYgltDTPDEEIMAAAKAANAHDFIMEF--PNGYDTEVgekgSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECE 653
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 521328941 169 HLilrvVQALAHSQSVSVLWATHLFEEVKHNNNLIVLSKGRV 210
Cdd:TIGR00958 654 QL----LQESRSRASRTVLLIAHRLSTVERADQILVLKKGSV 691
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
32-192 |
1.65e-21 |
|
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: 88.32 E-value: 1.65e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 32 LLGPNGAGKSTLFALITGLQKLTQGSITFDGATLSQSRTSIMAKMGVVFQQSTLDIDLSVKQNLSYFASLHGISTasals 111
Cdd:cd03231 31 VTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTLSVLENLRFWHADHSDEQ----- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 112 hIQGLLDELDLTSKLNTKIRNLNGGHRRRVELARCLIHKPSLLLLDEPTVGLDIESrhlILRVVQALAH--SQSVSVLWA 189
Cdd:cd03231 106 -VEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAG---VARFAEAMAGhcARGGMVVLT 181
|
...
gi 521328941 190 THL 192
Cdd:cd03231 182 THQ 184
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
16-210 |
1.69e-21 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 92.80 E-value: 1.69e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 16 HALDNINLCLKPG-LTMLLGPNGAGKSTLFALI-----TGLQKltQGSITFDGATLSQSRtsiMAKMGVVFQQSTLDI-D 88
Cdd:TIGR00955 39 HLLKNVSGVAKPGeLLAVMGSSGAGKTTLMNALafrspKGVKG--SGSVLLNGMPIDAKE---MRAISAYVQQDDLFIpT 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 89 LSVKQNLSYFASL---HGISTASALSHIQGLLDELDLTSKLNTKI------RNLNGGHRRRVELARCLIHKPSLLLLDEP 159
Cdd:TIGR00955 114 LTVREHLMFQAHLrmpRRVTKKEKRERVDEVLQALGLRKCANTRIgvpgrvKGLSGGERKRLAFASELLTDPPLLFCDEP 193
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 521328941 160 TVGLDIESRHLILRVVQALAHSQSVSVLW----ATHLFEEVkhnNNLIVLSKGRV 210
Cdd:TIGR00955 194 TSGLDSFMAYSVVQVLKGLAQKGKTIICTihqpSSELFELF---DKIILMAEGRV 245
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
3-164 |
1.79e-21 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 89.71 E-value: 1.79e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 3 IAVQAVSHQYGGHHALDNINLCLKPG-LTMLLGPNGAGKSTL-------FALITGLQklTQGSITFDGATLSQSRTSIMA 74
Cdd:COG1117 12 IEVRNLNVYYGDKQALKDINLDIPENkVTALIGPSGCGKSTLlrclnrmNDLIPGAR--VEGEILLDGEDIYDPDVDVVE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 75 ---KMGVVFQQSTLdIDLSVKQNLSYFASLHGISTASALSHI-------QGLLDEL-DltsKLNTKIRNLNGGHRRRVEL 143
Cdd:COG1117 90 lrrRVGMVFQKPNP-FPKSIYDNVAYGLRLHGIKSKSELDEIveeslrkAALWDEVkD---RLKKSALGLSGGQQQRLCI 165
|
170 180
....*....|....*....|.
gi 521328941 144 ARCLIHKPSLLLLDEPTVGLD 164
Cdd:COG1117 166 ARALAVEPEVLLMDEPTSALD 186
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
3-197 |
2.31e-21 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 92.15 E-value: 2.31e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 3 IAVQAVSHQYGGHHALDNINLCLKPG-LTMLLGPNGAGKSTLFALITGLQKLTQGSITFDGATLSQSRTSIMAKMG--VV 79
Cdd:PRK09700 6 ISMAGIGKSFGPVHALKSVNLTVYPGeIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLGigII 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 80 FQQSTLDIDLSVKQNL-------SYFASLHGISTASALSHIQGLLDELDLTSKLNTKIRNLNGGHRRRVELARCLIHKPS 152
Cdd:PRK09700 86 YQELSVIDELTVLENLyigrhltKKVCGVNIIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAK 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 521328941 153 LLLLDEPTVGL---DIESRHLILRVVQalahSQSVSVLWATHLFEEVK 197
Cdd:PRK09700 166 VIIMDEPTSSLtnkEVDYLFLIMNQLR----KEGTAIVYISHKLAEIR 209
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
3-172 |
3.45e-21 |
|
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: 88.26 E-value: 3.45e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 3 IAVQAVSHQYGGH----HALDNINLCLKPGLTM-LLGPNGAGKSTLFALITGLQKLTQGSITFDGATLSQ----SRTSIM 73
Cdd:COG4181 9 IELRGLTKTVGTGagelTILKGISLEVEAGESVaIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFAldedARARLR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 74 A-KMGVVFQQSTLDIDLSVKQNLSYFASLHGISTASALShiQGLLDELDLTSKLNTKIRNLNGGHRRRVELARCLIHKPS 152
Cdd:COG4181 89 ArHVGFVFQSFQLLPTLTALENVMLPLELAGRRDARARA--RALLERVGLGHRLDHYPAQLSGGEQQRVALARAFATEPA 166
|
170 180
....*....|....*....|
gi 521328941 153 LLLLDEPTVGLDIESRHLIL 172
Cdd:COG4181 167 ILFADEPTGNLDAATGEQII 186
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
13-233 |
5.14e-21 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 91.31 E-value: 5.14e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 13 GGHHALDNINLCLKPGLTM-LLGPNGAGKSTlfaliTGLQKL----TQGSITFDGATLSQSRTSIM----AKMGVVFQ-- 81
Cdd:PRK15134 297 DHNVVVKNISFTLRPGETLgLVGESGSGKST-----TGLALLrlinSQGEIWFDGQPLHNLNRRQLlpvrHRIQVVFQdp 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 82 QSTLDIDLSVKQNLSYFASLH--GISTASALSHIQGLLDELDLTSKlnTKIR---NLNGGHRRRVELARCLIHKPSLLLL 156
Cdd:PRK15134 372 NSSLNPRLNVLQIIEEGLRVHqpTLSAAQREQQVIAVMEEVGLDPE--TRHRypaEFSGGQRQRIAIARALILKPSLIIL 449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 157 DEPTVGLDIESRHLILRVVQALAHSQSVSVLWATHLFEEVK---HnnNLIVLSKGRVLAHDQCEALLAKYHQQDIEHLWQ 233
Cdd:PRK15134 450 DEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRalcH--QVIVLRQGEVVEQGDCERVFAAPQQEYTRQLLA 527
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
3-196 |
5.88e-21 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 88.67 E-value: 5.88e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 3 IAVQAVSHQYGGHHALDNINLCLKPG-LTMLLGPNGAGKSTLFALITGLQKLTQGSITFDG---ATLSQSRT-SIMAKMG 77
Cdd:PRK11831 8 VDMRGVSFTRGNRCIFDNISLTVPRGkITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGeniPAMSRSRLyTVRKRMS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 78 VVFQQSTLDIDLSVKQNLSYFASLHGISTASAL-SHIQGLLDELDLTSKLNTKIRNLNGGHRRRVELARCLIHKPSLLLL 156
Cdd:PRK11831 88 MLFQSGALFTDMNVFDNVAYPLREHTQLPAPLLhSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMF 167
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 521328941 157 DEPTVGLDIESRHLILRVVQALAHSQSVSVLWATHLFEEV 196
Cdd:PRK11831 168 DEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEV 207
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
3-210 |
6.89e-21 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 88.20 E-value: 6.89e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 3 IAVQAVSHQYGGHHALDNINLCLKPG-LTMLLGPNGAGKSTLFALITGLQKLTQGSITFDGATLSQSR--TSIMakmgvv 79
Cdd:PRK11247 13 LLLNAVSKRYGERTVLNQLDLHIPAGqFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEARedTRLM------ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 80 FQQSTLDIDLSVKQNLSYfaSLHGISTASALShiqgLLDELDLTSKLNTKIRNLNGGHRRRVELARCLIHKPSLLLLDEP 159
Cdd:PRK11247 87 FQDARLLPWKKVIDNVGL--GLKGQWRDAALQ----ALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 521328941 160 TVGLD----IESRHLILRVVQalahSQSVSVLWATH-LFEEVKHNNNLIVLSKGRV 210
Cdd:PRK11247 161 LGALDaltrIEMQDLIESLWQ----QHGFTVLLVTHdVSEAVAMADRVLLIEEGKI 212
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1-212 |
7.63e-21 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 87.76 E-value: 7.63e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 1 MEIAVQAVSHQYGGHHALDNINLCLKPG-LTMLLGPNGAGKSTLFALITGLQKLTQGSITFDGATLSQSRTSIMAK-MGV 78
Cdd:PRK11231 1 MTLRTENLTVGYGTKRILNDLSLSLPTGkITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARrLAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 79 VFQQSTLDIDLSVKQNLSY----FASLHGISTASALSHIQGLLDELDLTSKLNTKIRNLNGGHRRRVELARCLIHKPSLL 154
Cdd:PRK11231 81 LPQHHLTPEGITVRELVAYgrspWLSLWGRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVV 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 521328941 155 LLDEPTVGLDIESRHLILRVVQALAhSQSVSVLWATH-LFEEVKHNNNLIVLSKGRVLA 212
Cdd:PRK11231 161 LLDEPTTYLDINHQVELMRLMRELN-TQGKTVVTVLHdLNQASRYCDHLVVLANGHVMA 218
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
11-197 |
7.94e-21 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 90.37 E-value: 7.94e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 11 QYGGHHALDNINLCLKPGLTM-LLGPNGAGKSTLFALITGLQKLT--QGSITFDGATLSQS--RTSIMAKMGVVFQQSTL 85
Cdd:PRK13549 14 TFGGVKALDNVSLKVRAGEIVsLCGENGAGKSTLMKVLSGVYPHGtyEGEIIFEGEELQASniRDTERAGIAIIHQELAL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 86 DIDLSVKQNLSYFASL--HGISTASALSH-IQGLLDELDLTSKLNTKIRNLNGGHRRRVELARCLIHKPSLLLLDEPTVG 162
Cdd:PRK13549 94 VKELSVLENIFLGNEItpGGIMDYDAMYLrAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQARLLILDEPTAS 173
|
170 180 190
....*....|....*....|....*....|....*.
gi 521328941 163 L-DIESRHLiLRVVQALaHSQSVSVLWATHLFEEVK 197
Cdd:PRK13549 174 LtESETAVL-LDIIRDL-KAHGIACIYISHKLNEVK 207
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
3-212 |
1.17e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 87.74 E-value: 1.17e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 3 IAVQAVSHQYGGHH--ALDNINLCLKPG-LTMLLGPNGAGKSTLFALITGLQKLTQGSITFDGATLSQSR-TSIMAKMGV 78
Cdd:PRK13632 8 IKVENVSFSYPNSEnnALKNVSFEINEGeYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENlKEIRKKIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 79 VFQQStlD---IDLSVKQNLSYFASLHGISTASALSHIQGLLDELDLTSKLNTKIRNLNGGHRRRVELARCLIHKPSLLL 155
Cdd:PRK13632 88 IFQNP--DnqfIGATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIII 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 521328941 156 LDEPTVGLDIESRHLILRVVQALAHSQSVSVLWATHLFEEVKHNNNLIVLSKGRVLA 212
Cdd:PRK13632 166 FDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAILADKVIVFSEGKLIA 222
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
14-210 |
1.55e-20 |
|
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: 85.18 E-value: 1.55e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 14 GHHALDNINLCLKPG----LTMLLGpngAGKSTLFALITGLQKLTQGSITFDGATLSQSRTSIMAKMGVVF-----QQST 84
Cdd:cd03215 12 VKGAVRDVSFEVRAGeivgIAGLVG---NGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAGIAYvpedrKREG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 85 LDIDLSVKQNlsyfaslhgISTASALShiqglldeldltsklntkirnlnGGHRRRVELARCLIHKPSLLLLDEPTVGLD 164
Cdd:cd03215 89 LVLDLSVAEN---------IALSSLLS-----------------------GGNQQKVVLARWLARDPRVLILDEPTRGVD 136
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 521328941 165 IESRHLILRVVQALAhSQSVSVLWATHLFEEVKHN-NNLIVLSKGRV 210
Cdd:cd03215 137 VGAKAEIYRLIRELA-DAGKAVLLISSELDELLGLcDRILVMYEGRI 182
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
3-228 |
2.18e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 86.96 E-value: 2.18e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 3 IAVQAVSHQY-GGHHALDNINLCLKPGLTM-LLGPNGAGKSTLFALITGLQKLTQGSITFDGA-TLSQSRTSIMAKM-GV 78
Cdd:PRK13644 2 IRLENVSYSYpDGTPALENINLVIKKGEYIgIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIdTGDFSKLQGIRKLvGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 79 VFQQ-STLDIDLSVKQNLSYFASLHGISTASALSHIQGLLDELDLTSKLNTKIRNLNGGHRRRVELARCLIHKPSLLLLD 157
Cdd:PRK13644 82 VFQNpETQFVGRTVEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFD 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 521328941 158 EPTVGLDIESRHLILRVVQALaHSQSVSVLWATHLFEEVKHNNNLIVLSKGRVLAHDQCEALLAKYHQQDI 228
Cdd:PRK13644 162 EVTSMLDPDSGIAVLERIKKL-HEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLSDVSLQTL 231
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1-219 |
3.93e-20 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 87.45 E-value: 3.93e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 1 MEIAVQAVSHQYGGHHALDNINLCLKPG-LTMLLGPNGAGKSTLFALITGLQKLTQGSITFDGATLSQ--SRTSimaKMG 77
Cdd:PRK10851 1 MSIEIANIKKSFGRTQVLNDISLDIPSGqMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRlhARDR---KVG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 78 VVFQQSTLDIDLSVKQNLSYfaslhGI---------STASALSHIQGLLDELDLTSKLNTKIRNLNGGHRRRVELARCLI 148
Cdd:PRK10851 78 FVFQHYALFRHMTVFDNIAF-----GLtvlprrerpNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 521328941 149 HKPSLLLLDEPTVGLDIESRHLILRvvqalahsqsvsvlWATHLFEEVKHNNNLIvlskgrvlAHDQCEAL 219
Cdd:PRK10851 153 VEPQILLLDEPFGALDAQVRKELRR--------------WLRQLHEELKFTSVFV--------THDQEEAM 201
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
13-170 |
3.98e-20 |
|
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: 88.45 E-value: 3.98e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 13 GGHHALDNINLCLKPGLTM-LLGPNGAGKSTLFALITGLQKltqgsiTFDGatlsQSRTSIMAKMGVVFQQSTLDIDLSV 91
Cdd:TIGR03719 16 PKKEILKDISLSFFPGAKIgVLGLNGAGKSTLLRIMAGVDK------DFNG----EARPQPGIKVGYLPQEPQLDPTKTV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 92 KQNLsyfaslhgistASALSHIQGLLDEL----------------------------------DLTSKL----------- 126
Cdd:TIGR03719 86 RENV-----------EEGVAEIKDALDRFneisakyaepdadfdklaaeqaelqeiidaadawDLDSQLeiamdalrcpp 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 521328941 127 -NTKIRNLNGGHRRRVELARCLIHKPSLLLLDEPTVGLDIES-----RHL 170
Cdd:TIGR03719 155 wDADVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESvawleRHL 204
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
3-191 |
5.84e-20 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 85.89 E-value: 5.84e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 3 IAVQAVSHQYGGH---------HALDNINLCLKPGLTM-LLGPNGAGKSTLFALITGLQKLTQGSITFDGATLSQSRTSI 72
Cdd:PRK10419 4 LNVSGLSHHYAHGglsgkhqhqTVLNNVSLSLKSGETVaLLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 73 MA----KMGVVFQQS------TLDIDLSVKQNLSYFASLhgiSTASALSHIQGLLDELDLTSKLNTKI-RNLNGGHRRRV 141
Cdd:PRK10419 84 RKafrrDIQMVFQDSisavnpRKTVREIIREPLRHLLSL---DKAERLARASEMLRAVDLDDSVLDKRpPQLSGGQLQRV 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 521328941 142 ELARCLIHKPSLLLLDEPTVGLDIESRHLILRVVQALAHSQSVSVLWATH 191
Cdd:PRK10419 161 CLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITH 210
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
32-210 |
6.53e-20 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 84.53 E-value: 6.53e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 32 LLGPNGAGKSTLFALITGLQKLTQGSITFDGATLSQSRTSiMAKMGVVFQQSTLDIDLSVKQNLSYFASLHGISTASALS 111
Cdd:TIGR01277 29 IMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPY-QRPVSMLFQENNLFAHLTVRQNIGLGLHPGLKLNAEQQE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 112 HIQGLLDELDLTSKLNTKIRNLNGGHRRRVELARCLIHKPSLLLLDEPTVGLDIESRHLILRVVQALAHSQSVSVLWATH 191
Cdd:TIGR01277 108 KVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALVKQLCSERQRTLLMVTH 187
|
170 180
....*....|....*....|
gi 521328941 192 LFEEVKHN-NNLIVLSKGRV 210
Cdd:TIGR01277 188 HLSDARAIaSQIAVVSQGKI 207
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
8-164 |
7.52e-20 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 87.01 E-value: 7.52e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 8 VSHQYGGHHALDNINLCLKPG-LTMLLGPNGAGKSTLFALITGLQKLTQGSITFDGATLSQ---SRTSImakmGVVFQQS 83
Cdd:PRK11000 9 VTKAYGDVVISKDINLDIHEGeFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDvppAERGV----GMVFQSY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 84 TLDIDLSVKQNLSYFASLHGISTASALSHIQGLLDELDLTSKLNTKIRNLNGGHRRRVELARCLIHKPSLLLLDEPTVGL 163
Cdd:PRK11000 85 ALYPHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNL 164
|
.
gi 521328941 164 D 164
Cdd:PRK11000 165 D 165
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
2-222 |
1.03e-19 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 87.38 E-value: 1.03e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 2 EIAVQAVSHQYGG--HHALDNINLCLKPGLTM-LLGPNGAGKSTLFALITGLQKLTQGSITFDGATLSQSR-TSIMAKMG 77
Cdd:PRK11176 341 DIEFRNVTFTYPGkeVPALRNINFKIPAGKTVaLVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTlASLRNQVA 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 78 VVFQQSTLDIDlSVKQNLSYFA----SLHGISTASALSHIQGLLDELDltSKLNTKI----RNLNGGHRRRVELARCLIH 149
Cdd:PRK11176 421 LVSQNVHLFND-TIANNIAYARteqySREQIEEAARMAYAMDFINKMD--NGLDTVIgengVLLSGGQRQRIAIARALLR 497
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 521328941 150 KPSLLLLDEPTVGLDIESRHLILRVVQALAHSQSVSVLwaTHLFEEVKHNNNLIVLSKGRVLAHDQCEALLAK 222
Cdd:PRK11176 498 DSPILILDEATSALDTESERAIQAALDELQKNRTSLVI--AHRLSTIEKADEILVVEDGEIVERGTHAELLAQ 568
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
17-212 |
1.03e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 85.56 E-value: 1.03e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 17 ALDNINLCLKPG-LTMLLGPNGAGKSTLFALITGLQKLTQGSITF-DGATLSQSRTS----IMAKMGVVFQ--QSTLdID 88
Cdd:PRK13643 21 ALFDIDLEVKKGsYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVgDIVVSSTSKQKeikpVRKKVGVVFQfpESQL-FE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 89 LSVKQNLSYFASLHGISTASALSHIQGLLDELDLTSKLNTKIR-NLNGGHRRRVELARCLIHKPSLLLLDEPTVGLDIES 167
Cdd:PRK13643 100 ETVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLADEFWEKSPfELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKA 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 521328941 168 RHLILRVVQALaHSQSVSVLWATHLFEEV-KHNNNLIVLSKGRVLA 212
Cdd:PRK13643 180 RIEMMQLFESI-HQSGQTVVLVTHLMDDVaDYADYVYLLEKGHIIS 224
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
18-220 |
1.06e-19 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 84.51 E-value: 1.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 18 LDNINLCLKPG-LTMLLGPNGAGKSTLFALITGLQkLTQGSITFDGATLSQSRTSIMAKM-GVVFQQSTLDIDLSVKQNL 95
Cdd:COG4138 12 LGPISAQVNAGeLIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGRPLSDWSAAELARHrAYLSQQQSPPFAMPVFQYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 96 SYFASlHGISTASALSHIQGLLDELDLTSKLNTKIRNLNGGHRRRVELARCL--IH-----KPSLLLLDEPTVGLDIESR 168
Cdd:COG4138 91 ALHQP-AGASSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLlqVWptinpEGQLLLLDEPMNSLDVAQQ 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 521328941 169 HLILRVVQALAHsQSVSVLWATH-LFEEVKHNNNLIVLSKGRVLAHDQCEALL 220
Cdd:COG4138 170 AALDRLLRELCQ-QGITVVMSSHdLNHTLRHADRVWLLKQGKLVASGETAEVM 221
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
18-170 |
1.10e-19 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 87.10 E-value: 1.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 18 LDNINLCLKPGLTM-LLGPNGAGKSTLFALITGLQKLTQGSitfdgATLSQSrtsimAKMGVVFQQSTLDIDLSVKQNLs 96
Cdd:PRK11819 23 LKDISLSFFPGAKIgVLGLNGAGKSTLLRIMAGVDKEFEGE-----ARPAPG-----IKVGYLPQEPQLDPEKTVRENV- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 97 yfaslhgistASALSHIQGLLDEL----------------------------------DLTSKL------------NTKI 130
Cdd:PRK11819 92 ----------EEGVAEVKAALDRFneiyaayaepdadfdalaaeqgelqeiidaadawDLDSQLeiamdalrcppwDAKV 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 521328941 131 RNLNGGHRRRVELARCLIHKPSLLLLDEPTVGLDIES-----RHL 170
Cdd:PRK11819 162 TKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESvawleQFL 206
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
2-221 |
1.89e-19 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 84.25 E-value: 1.89e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 2 EIAVQAVSHQYGGHHALDNINLCLKPG-LTMLLGPNGAGKSTLFALITGLQKLTQGSITFDGATLSQSRTS--------- 71
Cdd:PRK10619 5 KLNVIDLHKRYGEHEVLKGVSLQANAGdVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKdgqlkvadk 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 72 -----IMAKMGVVFQQSTLDIDLSVKQN-LSYFASLHGISTASALSHIQGLLDELDLTSKLNTKI-RNLNGGHRRRVELA 144
Cdd:PRK10619 85 nqlrlLRTRLTMVFQHFNLWSHMTVLENvMEAPIQVLGLSKQEARERAVKYLAKVGIDERAQGKYpVHLSGGQQQRVSIA 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 521328941 145 RCLIHKPSLLLLDEPTVGLDIESRHLILRVVQALAHSQSVSVLwATHLFEEVKH-NNNLIVLSKGRVLAHDQCEALLA 221
Cdd:PRK10619 165 RALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVV-VTHEMGFARHvSSHVIFLHQGKIEEEGAPEQLFG 241
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
17-195 |
1.91e-19 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 86.99 E-value: 1.91e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 17 ALDNINLCLKPGLTM-LLGPNGAGKSTLFALITGLQKLTQGSITFDGATLSQSRTSIMAKMGVVFQQSTLDIDLSVKQNL 95
Cdd:TIGR01257 1954 AVDRLCVGVRPGECFgLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISDVHQNMGYCPQFDAIDDLLTGREHL 2033
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 96 SYFASLHGISTASALSHIQGLLDELDLTSKLNTKIRNLNGGHRRRVELARCLIHKPSLLLLDEPTVGLDIESRHLILRVV 175
Cdd:TIGR01257 2034 YLYARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTI 2113
|
170 180
....*....|....*....|
gi 521328941 176 QALAHSQSVSVLwATHLFEE 195
Cdd:TIGR01257 2114 VSIIREGRAVVL-TSHSMEE 2132
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
3-221 |
2.13e-19 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 84.03 E-value: 2.13e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 3 IAVQAVSHQYGGHHALDNINLCLKPG-LTMLLGPNGAGKSTLFALITGLQKLTQGSI-----TFDGA-TLSQSRTSIMA- 74
Cdd:PRK11264 4 IEVKNLVKKFHGQTVLHGIDLEVKPGeVVAIIGPSGSGKTTLLRCINLLEQPEAGTIrvgdiTIDTArSLSQQKGLIRQl 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 75 --KMGVVFQQSTLDIDLSVKQN-LSYFASLHGISTASALSHIQGLLDELDLTSKLNTKIRNLNGGHRRRVELARCLIHKP 151
Cdd:PRK11264 84 rqHVGFVFQNFNLFPHRTVLENiIEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRP 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 521328941 152 SLLLLDEPTVGLDIESRHLILRVVQALAHSQSVSVLwATH---LFEEVKhnNNLIVLSKGRVLAHDQCEALLA 221
Cdd:PRK11264 164 EVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVI-VTHemsFARDVA--DRAIFMDQGRIVEQGPAKALFA 233
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
1-233 |
2.43e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 84.45 E-value: 2.43e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 1 MEIAVQAVSHQYGG-----HHALDNINLCLKPG-LTMLLGPNGAGKSTLFALITGLQKLTQGSITFDGATLSqSRTS--- 71
Cdd:PRK13646 1 MTIRFDNVSYTYQKgtpyeHQAIHDVNTEFEQGkYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIT-HKTKdky 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 72 ---IMAKMGVVFQ--QSTLDIDlSVKQNLSYFASLHGISTASALSHIQGLLDELDLTSKLNTKIR-NLNGGHRRRVELAR 145
Cdd:PRK13646 80 irpVRKRIGMVFQfpESQLFED-TVEREIIFGPKNFKMNLDEVKNYAHRLLMDLGFSRDVMSQSPfQMSGGQMRKIAIVS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 146 CLIHKPSLLLLDEPTVGLDIESRHLILRVVQALAHSQSVSVLWATHLFEEV-KHNNNLIVLSKGRVLAHDQCEAL----- 219
Cdd:PRK13646 159 ILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVaRYADEVIVMKEGSIVSQTSPKELfkdkk 238
|
250 260
....*....|....*....|....
gi 521328941 220 -LAKYH---------QQDIEHLWQ 233
Cdd:PRK13646 239 kLADWHiglpeivqlQYDFEQKYQ 262
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
3-164 |
3.09e-19 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 83.67 E-value: 3.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 3 IAVQAVSHQYGGHHALDNINLCLKP-GLTMLLGPNGAGKSTLFALITGLQKL-----TQGSITFDGATLSQSRT---SIM 73
Cdd:PRK14239 6 LQVSDLSVYYNKKKALNSVSLDFYPnEITALIGPSGSGKSTLLRSINRMNDLnpevtITGSIVYNGHNIYSPRTdtvDLR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 74 AKMGVVFQQSTlDIDLSVKQNLSYFASLHGISTASALSH-----IQG--LLDELdlTSKLNTKIRNLNGGHRRRVELARC 146
Cdd:PRK14239 86 KEIGMVFQQPN-PFPMSIYENVVYGLRLKGIKDKQVLDEaveksLKGasIWDEV--KDRLHDSALGLSGGQQQRVCIARV 162
|
170
....*....|....*...
gi 521328941 147 LIHKPSLLLLDEPTVGLD 164
Cdd:PRK14239 163 LATSPKIILLDEPTSALD 180
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
32-191 |
4.50e-19 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 82.71 E-value: 4.50e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 32 LLGPNGAGKSTLFALITGLQKLTQGSITFDGA-----TLSQSRTSIMakmgvvFQQSTLDIDLSVKQNLSYfaslhGIST 106
Cdd:PRK10771 30 ILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQdhtttPPSRRPVSML------FQENNLFSHLTVAQNIGL-----GLNP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 107 ASALSHIQ-----GLLDELDLTSKLNTKIRNLNGGHRRRVELARCLIHKPSLLLLDEPTVGLDIESRHLILRVVQALAHS 181
Cdd:PRK10771 99 GLKLNAAQreklhAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLVSQVCQE 178
|
170
....*....|
gi 521328941 182 QSVSVLWATH 191
Cdd:PRK10771 179 RQLTLLMVSH 188
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
17-211 |
4.92e-19 |
|
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: 83.08 E-value: 4.92e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 17 ALDNINLCLKPG-LTMLLGPNGAGKSTLFALITGLQKLTQGSITFDGATLSQ-SRTSIMA----KMGVVFQQSTLDIDLS 90
Cdd:cd03294 39 GVNDVSLDVREGeIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAmSRKELRElrrkKISMVFQSFALLPHRT 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 91 VKQNLSYFASLHGISTASALSHIQGLLDELDLTSKLNTKIRNLNGGHRRRVELARCLIHKPSLLLLDEPTVGLDiesrHL 170
Cdd:cd03294 119 VLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALD----PL 194
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 521328941 171 ILRVVQ----ALAHSQSVSVLWATH-LFEEVKHNNNLIVLSKGRVL 211
Cdd:cd03294 195 IRREMQdellRLQAELQKTIVFITHdLDEALRLGDRIAIMKDGRLV 240
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
3-213 |
5.02e-19 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 83.52 E-value: 5.02e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 3 IAVQAVSHQYGGHHALDNINLCLKP-GLTMLLGPNGAGKSTLFALITGLQKLTQGSITFDGATLSQSRTSIMA---KMGV 78
Cdd:PRK13638 2 LATSDLWFRYQDEPVLKGLNLDFSLsPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKRGLLAlrqQVAT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 79 VFQQST-----LDIDLSVKQNLSYFaslhGISTASALSHIQGLLDELDLTSKLNTKIRNLNGGHRRRVELARCLIHKPSL 153
Cdd:PRK13638 82 VFQDPEqqifyTDIDSDIAFSLRNL----GVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARY 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 521328941 154 LLLDEPTVGLDIESRHLILRVVQALAhSQSVSVLWATH---LFEEVkhNNNLIVLSKGRVLAH 213
Cdd:PRK13638 158 LLLDEPTAGLDPAGRTQMIAIIRRIV-AQGNHVIISSHdidLIYEI--SDAVYVLRQGQILTH 217
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
18-210 |
5.06e-19 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 82.81 E-value: 5.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 18 LDNINLCLKPG-LTMLLGPNGAGKSTLFALITGL--QKLTQGSITFDGATLSQSRTSIMAKMGV--VFQQSTlDID-LSV 91
Cdd:COG0396 16 LKGVNLTIKPGeVHAIMGPNGSGKSTLAKVLMGHpkYEVTSGSILLDGEDILELSPDERARAGIflAFQYPV-EIPgVSV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 92 KQ--NLSYFA-SLHGISTASALSHIQGLLDELDLTSKLNTkiRNLN----GGHRRRVELARCLIHKPSLLLLDEPTVGLD 164
Cdd:COG0396 95 SNflRTALNArRGEELSAREFLKLLKEKMKELGLDEDFLD--RYVNegfsGGEKKRNEILQMLLLEPKLAILDETDSGLD 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 521328941 165 IESRHLILRVVQALaHSQSVSVLWATH---LFEEVK----HnnnliVLSKGRV 210
Cdd:COG0396 173 IDALRIVAEGVNKL-RSPDRGILIITHyqrILDYIKpdfvH-----VLVDGRI 219
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
18-238 |
5.63e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 83.34 E-value: 5.63e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 18 LDNINLCLKPG-LTMLLGPNGAGKSTLFALITGLQKLTQGSITFDGATL-----SQSRTSIMAKMGVVFQQSTLDI-DLS 90
Cdd:PRK13641 23 LDNISFELEEGsFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHItpetgNKNLKKLRKKVSLVFQFPEAQLfENT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 91 VKQNLSYFASLHGISTASALSHIQGLLDELDLTSKLNTKIR-NLNGGHRRRVELARCLIHKPSLLLLDEPTVGLDIESRH 169
Cdd:PRK13641 103 VLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLSEDLISKSPfELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRK 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 521328941 170 LILRVV---QALAHsqsvSVLWATHLFEEV-KHNNNLIVLSKGRVLAHDQCEALLAkyhqqDIEHLWQHLMQE 238
Cdd:PRK13641 183 EMMQLFkdyQKAGH----TVILVTHNMDDVaEYADDVLVLEHGKLIKHASPKEIFS-----DKEWLKKHYLDE 246
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
14-222 |
5.85e-19 |
|
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: 82.59 E-value: 5.85e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 14 GHHALDNINLCLKPGLTM-LLGPNGAGKSTLFALITGLQKLTQGSITFDGATLSQ-SRTSIMAKMGVVFQQSTLdIDLSV 91
Cdd:cd03249 15 DVPILKGLSLTIPPGKTVaLVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDlNLRWLRSQIGLVSQEPVL-FDGTI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 92 KQNLSY---FASLHGISTASALSHIQGLLDelDLTSKLNTKIRN----LNGGHRRRVELARCLIHKPSLLLLDEPTVGLD 164
Cdd:cd03249 94 AENIRYgkpDATDEEVEEAAKKANIHDFIM--SLPDGYDTLVGErgsqLSGGQKQRIAIARALLRNPKILLLDEATSALD 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 521328941 165 IESRHLILRVVQALAHSQSVSVLwaTHLFEEVKHNNNLIVLSKGRVL---AHDQceaLLAK 222
Cdd:cd03249 172 AESEKLVQEALDRAMKGRTTIVI--AHRLSTIRNADLIAVLQNGQVVeqgTHDE---LMAQ 227
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
18-191 |
7.85e-19 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 82.17 E-value: 7.85e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 18 LDNINLCLKPGLTM-LLGPNGAGKSTLFALITGLQKLTQGSITFDGATLSQSRTSIMA-----KMGVVFQQSTLDIDLSV 91
Cdd:PRK11629 25 LHNVSFSIGEGEMMaIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAelrnqKLGFIYQFHHLLPDFTA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 92 KQNLSYFASLHGISTASALSHIQGLLDELDLTSKLNTKIRNLNGGHRRRVELARCLIHKPSLLLLDEPTVGLDIESRHLI 171
Cdd:PRK11629 105 LENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADSI 184
|
170 180
....*....|....*....|
gi 521328941 172 LRVVQALAHSQSVSVLWATH 191
Cdd:PRK11629 185 FQLLGELNRLQGTAFLVVTH 204
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
32-212 |
1.07e-18 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 81.90 E-value: 1.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 32 LLGPNGAGKSTLFALITGLqkLT-QGSITFDGATLSQSRTSIMAKM-GVVFQQSTLDIDLSVKQNLsyfaSLH---GIST 106
Cdd:PRK03695 27 LVGPNGAGKSTLLARMAGL--LPgSGSIQFAGQPLEAWSAAELARHrAYLSQQQTPPFAMPVFQYL----TLHqpdKTRT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 107 ASALSHIQGLLDELDLTSKLNTKIRNLNGGHRRRVELAR-CLIHKPS------LLLLDEPTVGLDIESRHLILRVVQALA 179
Cdd:PRK03695 101 EAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAvVLQVWPDinpagqLLLLDEPMNSLDVAQQAALDRLLSELC 180
|
170 180 190
....*....|....*....|....*....|....
gi 521328941 180 hSQSVSVLWATH-LFEEVKHNNNLIVLSKGRVLA 212
Cdd:PRK03695 181 -QQGIAVVMSSHdLNHTLRHADRVWLLKQGKLLA 213
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
18-191 |
1.15e-18 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 81.36 E-value: 1.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 18 LDNINLCLKPGLTM-LLGPNGAGKSTLFALITGLQKLTQGSITFDGATLSQ----SRTSIMAK-MGVVFQQSTLDIDLSV 91
Cdd:PRK10584 26 LTGVELVVKRGETIaLIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQmdeeARAKLRAKhVGFVFQSFMLIPTLNA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 92 KQNLSYFASLHGISTASALSHIQGLLDELDLTSKLNTKIRNLNGGHRRRVELARCLIHKPSLLLLDEPTVGLDIESRHLI 171
Cdd:PRK10584 106 LENVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKI 185
|
170 180
....*....|....*....|
gi 521328941 172 LRVVQALAHSQSVSVLWATH 191
Cdd:PRK10584 186 ADLLFSLNREHGTTLILVTH 205
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
18-214 |
2.34e-18 |
|
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six proteins and believed to act in Fe-S cluster formation during oxidative stress. SufC forms a complex with SufB and SufD. SufC belongs to the ATP-binding cassette transporter family (pfam00005) but is no longer thought to be part of a transporter. The complex is reported as cytosolic () or associated with the membrane (). The SUF system also includes a cysteine desulfurase (SufS, enhanced by SufE) and a probable iron-sulfur cluster assembly scaffold protein, SufA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 273907 [Multi-domain] Cd Length: 243 Bit Score: 80.77 E-value: 2.34e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 18 LDNINLCLKPG-LTMLLGPNGAGKSTLFALITGLQK--LTQGSITFDGATLSQSRTSIMAKMGVVFQ-QSTLDI-DLSVK 92
Cdd:TIGR01978 16 LKGVNLTVKKGeIHAIMGPNGSGKSTLSKTIAGHPSyeVTSGTILFKGQDLLELEPDERARAGLFLAfQYPEEIpGVSNL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 93 QnlsyFasLHGISTASALSHIQGLLDELDLTSKLNTKI-----------RNLN----GGHRRRVELARCLIHKPSLLLLD 157
Cdd:TIGR01978 96 E----F--LRSALNARRSARGEEPLDLLDFEKLLKEKLalldmdeeflnRSVNegfsGGEKKRNEILQMALLEPKLAILD 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 521328941 158 EPTVGLDIESRHLILRVVQALAhSQSVSVLWATH---LFEEVKHN------NNLIVLSKGRVLAHD 214
Cdd:TIGR01978 170 EIDSGLDIDALKIVAEGINRLR-EPDRSFLIITHyqrLLNYIKPDyvhvllDGRIVKSGDVELAKE 234
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
8-210 |
3.06e-18 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 82.97 E-value: 3.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 8 VSHQygGHHALDNINLCLKPG-LTMLLGPNGAGKSTLFALITGLQKLtQGSITFDGATLSQ-SRTSIMAKMGVVFQQSTL 85
Cdd:PRK11174 358 LSPD--GKTLAGPLNFTLPAGqRIALVGPSGAGKTSLLNALLGFLPY-QGSLKINGIELRElDPESWRKHLSWVGQNPQL 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 86 dIDLSVKQNLS---YFASLHGISTASALSHIQGLLDELDLtsKLNTKIRN----LNGGHRRRVELARCLIHKPSLLLLDE 158
Cdd:PRK11174 435 -PHGTLRDNVLlgnPDASDEQLQQALENAWVSEFLPLLPQ--GLDTPIGDqaagLSVGQAQRLALARALLQPCQLLLLDE 511
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 521328941 159 PTVGLDIESRHLILRVVQALAHSQsvSVLWATHLFEEVKHNNNLIVLSKGRV 210
Cdd:PRK11174 512 PTASLDAHSEQLVMQALNAASRRQ--TTLMVTHQLEDLAQWDQIWVMQDGQI 561
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
2-226 |
4.35e-18 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 80.13 E-value: 4.35e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 2 EIAVQAVSHQYGGHHALDNINLCLKPGLTM-LLGPNGAGKSTLFALITGLQKLTQGSITFDGatlsqsRTSIMAKMGVVF 80
Cdd:COG1134 26 ELLLRRRRTRREEFWALKDVSFEVERGESVgIIGRNGAGKSTLLKLIAGILEPTSGRVEVNG------RVSALLELGAGF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 81 QQstldiDLSVKQNLSYFASLHGISTASalshIQGLLDEL----DLTSKLNTKIRNLNGGHRRRVELArCLIH-KPSLLL 155
Cdd:COG1134 100 HP-----ELTGRENIYLNGRLLGLSRKE----IDEKFDEIvefaELGDFIDQPVKTYSSGMRARLAFA-VATAvDPDILL 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 521328941 156 LDEPT-VGlDIESRHLILRVVQALAhSQSVSVLWATHLFEEVKHN-NNLIVLSKGRVLAHDQCEALLAKYHQQ 226
Cdd:COG1134 170 VDEVLaVG-DAAFQKKCLARIRELR-ESGRTVIFVSHSMGAVRRLcDRAIWLEKGRLVMDGDPEEVIAAYEAL 240
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
18-208 |
4.44e-18 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 79.21 E-value: 4.44e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 18 LDNINLCLKPG-LTMLLGPNGAGKSTLFALITG--LQKLTQGSITFDGATLSQS--RTSimakmGVVFQQSTLDIDLSVK 92
Cdd:cd03232 23 LNNISGYVKPGtLTALMGESGAGKTTLLDVLAGrkTAGVITGEILINGRPLDKNfqRST-----GYVEQQDVHSPNLTVR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 93 QNLSYFASLHGISTAsalshiqglldeldltsklntkirnlnggHRRRVELARCLIHKPSLLLLDEPTVGLDIESRHLIL 172
Cdd:cd03232 98 EALRFSALLRGLSVE-----------------------------QRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIV 148
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 521328941 173 RVVQALAhSQSVSVLWATH-----LFEevkHNNNLIVLSKG 208
Cdd:cd03232 149 RFLKKLA-DSGQAILCTIHqpsasIFE---KFDRLLLLKRG 185
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
2-226 |
6.35e-18 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 82.10 E-value: 6.35e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 2 EIAVQAVSHQYGGHHA--LDNINLCLKPGLTM-LLGPNGAGKSTLFALITGLQKLTQGSITFDGATLSQ-SRTSIMAKMG 77
Cdd:COG4618 330 RLSVENLTVVPPGSKRpiLRGVSFSLEPGEVLgVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQwDREELGRHIG 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 78 VVFQQSTLdIDLSVKQNLSYF-----------ASLHGIstasalsH--IQGLLDELDltsklnTKI----RNLNGGHRRR 140
Cdd:COG4618 410 YLPQDVEL-FDGTIAENIARFgdadpekvvaaAKLAGV-------HemILRLPDGYD------TRIgeggARLSGGQRQR 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 141 VELARCLIHKPSLLLLDEPTVGLDIE-SRHLilrvVQALAH--SQSVSVLWATH---LFEEVKHnnnLIVLSKGRVLAHD 214
Cdd:COG4618 476 IGLARALYGDPRLVVLDEPNSNLDDEgEAAL----AAAIRAlkARGATVVVITHrpsLLAAVDK---LLVLRDGRVQAFG 548
|
250
....*....|..
gi 521328941 215 QCEALLAKYHQQ 226
Cdd:COG4618 549 PRDEVLARLARP 560
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
8-219 |
6.63e-18 |
|
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: 82.18 E-value: 6.63e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 8 VSHQYGGHHALDNINLCLKPG-LTMLLGPNGAGKSTLFALITGL--QKLTQGSITFDGATLSQSRTSIMAKMGVVF--QQ 82
Cdd:TIGR02633 7 IVKTFGGVKALDGIDLEVRPGeCVGLCGENGAGKSTLMKILSGVypHGTWDGEIYWSGSPLKASNIRDTERAGIVIihQE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 83 STLDIDLSVKQN--LSYFASLHGISTASALSHI--QGLLDELDLTSKLNTK-IRNLNGGHRRRVELARCLIHKPSLLLLD 157
Cdd:TIGR02633 87 LTLVPELSVAENifLGNEITLPGGRMAYNAMYLraKNLLRELQLDADNVTRpVGDYGGGQQQLVEIAKALNKQARLLILD 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 521328941 158 EPTVGLDIESRHLILRVVQALaHSQSVSVLWATHLFEEVKHNNNLI-VLSKGRVLAHDQCEAL 219
Cdd:TIGR02633 167 EPSSSLTEKETEILLDIIRDL-KAHGVACVYISHKLNEVKAVCDTIcVIRDGQHVATKDMSTM 228
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
14-164 |
7.93e-18 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 78.69 E-value: 7.93e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 14 GHHAL-DNINLCLKPG-LTMLLGPNGAGKSTLFALITGLQKLTQGSITFDGATLSQSRTSIMAKMGVVFQQSTLDIDLSV 91
Cdd:PRK13538 12 DERILfSGLSFTLNAGeLVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQDLLYLGHQPGIKTELTA 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 521328941 92 KQNLSYFASLHGISTA----SALSHIqGLLDELDLTsklntkIRNLNGGHRRRVELARCLIHKPSLLLLDEPTVGLD 164
Cdd:PRK13538 92 LENLRFYQRLHGPGDDealwEALAQV-GLAGFEDVP------VRQLSAGQQRRVALARLWLTRAPLWILDEPFTAID 161
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
18-210 |
8.79e-18 |
|
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: 78.46 E-value: 8.79e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 18 LDNINLCLKPG-LTMLLGPNGAGKSTLFALITGLQKLT---QGSITFDGATLSQSRTSIMAKMGVVFQQSTLDIDLSVKQ 93
Cdd:cd03233 23 LKDFSGVVKPGeMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKEFAEKYPGEIIYVSEEDVHFPTLTVRE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 94 NLSYFASLHGistasalshiqglldeldltsklNTKIRNLNGGHRRRVELARCLIHKPSLLLLDEPTVGLDIESRHLILR 173
Cdd:cd03233 103 TLDFALRCKG-----------------------NEFVRGISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTALEILK 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 521328941 174 VVQALAHSQS----VSVLWA----THLFEEVkhnnnlIVLSKGRV 210
Cdd:cd03233 160 CIRTMADVLKtttfVSLYQAsdeiYDLFDKV------LVLYEGRQ 198
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
3-166 |
1.06e-17 |
|
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: 81.52 E-value: 1.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 3 IAVQAVSHQYGGHHALDNINLCLKPG-LTMLLGPNGAGKSTLFALITGLQKLTQGSITFdGATLsqsrtsimaKMGVVFQ 81
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGgIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETV---------KLAYVDQ 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 82 Q-STLDIDLSVKQNLSyfaslhgistasalshiqGLLDELDL----------TSKLN-------TKIRNLNGGHRRRVEL 143
Cdd:TIGR03719 393 SrDALDPNKTVWEEIS------------------GGLDIIKLgkreipsrayVGRFNfkgsdqqKKVGQLSGGERNRVHL 454
|
170 180
....*....|....*....|...
gi 521328941 144 ARCLIHKPSLLLLDEPTVGLDIE 166
Cdd:TIGR03719 455 AKTLKSGGNVLLLDEPTNDLDVE 477
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
3-191 |
1.12e-17 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 79.39 E-value: 1.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 3 IAVQAVSHQYGGHHALDNINLCLKPG-LTMLLGPNGAGKSTLFALITGLQKLTQGSITFDGATlsqsrtsimaKMGVVFQ 81
Cdd:PRK09544 5 VSLENVSVSFGQRRVLSDVSLELKPGkILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKL----------RIGYVPQ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 82 QSTLDIDLSVkqNLSYFASLH-GISTASALShiqgLLDELDLTSKLNTKIRNLNGGHRRRVELARCLIHKPSLLLLDEPT 160
Cdd:PRK09544 75 KLYLDTTLPL--TVNRFLRLRpGTKKEDILP----ALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPT 148
|
170 180 190
....*....|....*....|....*....|.
gi 521328941 161 VGLDIESRHLILRVVQALAHSQSVSVLWATH 191
Cdd:PRK09544 149 QGVDVNGQVALYDLIDQLRRELDCAVLMVSH 179
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
2-210 |
1.23e-17 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 81.55 E-value: 1.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 2 EIAVQAVSHQYGGH-HALDNINLCLKPGLTM-LLGPNGAGKSTLFALITGLQKLTQGSITFDGATLSQ-SRTSIMAKMGV 78
Cdd:PRK13657 334 AVEFDDVSFSYDNSrQGVEDVSFEAKPGQTVaIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTvTRASLRRNIAV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 79 VFQQSTLdIDLSVKQNLSYfaslhGISTAS------ALSHIQGLLDELDLTSKLNTKI----RNLNGGHRRRVELARCLI 148
Cdd:PRK13657 414 VFQDAGL-FNRSIEDNIRV-----GRPDATdeemraAAERAQAHDFIERKPDGYDTVVgergRQLSGGERQRLAIARALL 487
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 521328941 149 HKPSLLLLDEPTVGLDIESRHLILRVVQALAHSQSVSVLwaTHLFEEVKHNNNLIVLSKGRV 210
Cdd:PRK13657 488 KDPPILILDEATSALDVETEAKVKAALDELMKGRTTFII--AHRLSTVRNADRILVFDNGRV 547
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
18-211 |
1.56e-17 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 81.08 E-value: 1.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 18 LDNINLCLKPGLTM-LLGPNGAGKSTLFALITGLqklTQGSiTFDGATLSQSRT---SIMAKMGVVFQQSTLDIDLSVKQ 93
Cdd:PLN03211 84 LNGVTGMASPGEILaVLGPSGSGKSTLLNALAGR---IQGN-NFTGTILANNRKptkQILKRTGFVTQDDILYPHLTVRE 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 94 NLSYFASL---HGISTASALSHIQGLLDELDLTSKLNTK-----IRNLNGGHRRRVELARCLIHKPSLLLLDEPTVGLDI 165
Cdd:PLN03211 160 TLVFCSLLrlpKSLTKQEKILVAESVISELGLTKCENTIignsfIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDA 239
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 521328941 166 ESRHLILRVVQALAHsQSVSVLWATH--------LFEEVkhnnnlIVLSKGRVL 211
Cdd:PLN03211 240 TAAYRLVLTLGSLAQ-KGKTIVTSMHqpssrvyqMFDSV------LVLSEGRCL 286
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
3-210 |
2.08e-17 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 79.84 E-value: 2.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 3 IAVQAVSHQYGG----HHALDNINLCLKPG-LTMLLGPNGAGKSTLFALITGLQKLTQGSITFDG--------ATLSQSR 69
Cdd:PRK11153 2 IELKNISKVFPQggrtIHALNNVSLHIPAGeIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGqdltalseKELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 70 TSImakmGVVFQQSTLdidLS---VKQNLSYFASLHGISTASALSHIQGLLDELDLTSKLNTKIRNLNGGHRRRVELARC 146
Cdd:PRK11153 82 RQI----GMIFQHFNL---LSsrtVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 521328941 147 LIHKPSLLLLDEPTVGLDIESRHLILRVVQALAHSQSVSVLWATHLFEEVKH-NNNLIVLSKGRV 210
Cdd:PRK11153 155 LASNPKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRiCDRVAVIDAGRL 219
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
8-221 |
2.34e-17 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 78.00 E-value: 2.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 8 VSHQYGGHHALDNINLCLKPG-LTMLLGPNGAGKSTLFALITGLQKLTQGSITFDGATLSQSRTS-IMAK-MGVVFQQST 84
Cdd:PRK11614 11 VSAHYGKIQALHEVSLHINQGeIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAkIMREaVAIVPEGRR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 85 LDIDLSVKQNLS---YFASLHGISTasALSHIQGLLDEldLTSKLNTKIRNLNGGHRRRVELARCLIHKPSLLLLDEPTV 161
Cdd:PRK11614 91 VFSRMTVEENLAmggFFAERDQFQE--RIKWVYELFPR--LHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 162 GLDIESRHLILRVVQALAHSQSVSVLWATHLFEEVKHNNNLIVLSKGRVLAHDQCEALLA 221
Cdd:PRK11614 167 GLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHVVLEDTGDALLA 226
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
32-221 |
2.49e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 78.98 E-value: 2.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 32 LLGPNGAGKSTLFALITGLQKLTQGSITFDGATLSQSRT-SIMAKMGVVFQQSTLD-IDLSVKQNLSYFASLHGISTASA 109
Cdd:PRK13642 38 IIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVwNLRRKIGMVFQNPDNQfVGATVEDDVAFGMENQGIPREEM 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 110 LSHIQGLLDELDLTSKLNTKIRNLNGGHRRRVELARCLIHKPSLLLLDEPTVGLDIESRHLILRVVQALAHSQSVSVLWA 189
Cdd:PRK13642 118 IKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSI 197
|
170 180 190
....*....|....*....|....*....|..
gi 521328941 190 THLFEEVKHNNNLIVLSKGRVLAHDQCEALLA 221
Cdd:PRK13642 198 THDLDEAASSDRILVMKAGEIIKEAAPSELFA 229
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
3-210 |
2.82e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 78.62 E-value: 2.82e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 3 IAVQAVSHQYGG---HHALDNINLCLKPGLTM-LLGPNGAGKSTLFALITGLQKLTQGSITFDGATLSQSRT-SIMAKMG 77
Cdd:PRK13650 5 IEVKNLTFKYKEdqeKYTLNDVSFHVKQGEWLsIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVwDIRHKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 78 VVFQQSTLD-IDLSVKQNLSYFASLHGISTASALSHIQgllDELDLTSKLNTKIRN---LNGGHRRRVELARCLIHKPSL 153
Cdd:PRK13650 85 MVFQNPDNQfVGATVEDDVAFGLENKGIPHEEMKERVN---EALELVGMQDFKEREparLSGGQKQRVAIAGAVAMRPKI 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 521328941 154 LLLDEPTVGLDIESRHLILRVVQALAHSQSVSVLWATHLFEEVKHNNNLIVLSKGRV 210
Cdd:PRK13650 162 IILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEVALSDRVLVMKNGQV 218
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
32-187 |
3.51e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 78.17 E-value: 3.51e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 32 LLGPNGAGKSTLFALITGLQKLTQGSITFDGATLSQSR-------TSIMAKMGVVFQQSTLDIDLSVKQNLSYFASLHGI 104
Cdd:PRK14246 41 IMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYFGKdifqidaIKLRKEVGMVFQQPNPFPHLSIYDNIAYPLKSHGI 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 105 STASALSHIQ-------GLLDELdlTSKLNTKIRNLNGGHRRRVELARCLIHKPSLLLLDEPTVGLDIESRHLILRVVQA 177
Cdd:PRK14246 121 KEKREIKKIVeeclrkvGLWKEV--YDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITE 198
|
170
....*....|
gi 521328941 178 LAHSQSVSVL 187
Cdd:PRK14246 199 LKNEIAIVIV 208
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
17-214 |
3.94e-17 |
|
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: 77.15 E-value: 3.94e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 17 ALDNINLCLKPGLTM-LLGPNGAGKSTLFALITGLQKLTQGSITFDGATLSQ-SRTSIMAKMGVVFQQSTLdIDLSVKQN 94
Cdd:cd03244 19 VLKNISFSIKPGEKVgIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKiGLHDLRSRISIIPQDPVL-FSGTIRSN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 95 LSYFAS------LHGISTASALSHIQGLLDELDLTSKLNTKirNLNGGHRRRVELARCLIHKPSLLLLDEPTVGLDIESR 168
Cdd:cd03244 98 LDPFGEysdeelWQALERVGLKEFVESLPGGLDTVVEEGGE--NLSVGQRQLLCLARALLRKSKILVLDEATASVDPETD 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 521328941 169 HLILRVVQ-ALAHSqsvSVLWATHLFEEVKHNNNLIVLSKGRVLAHD 214
Cdd:cd03244 176 ALIQKTIReAFKDC---TVLTIAHRLDTIIDSDRILVLDKGRVVEFD 219
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
3-178 |
4.04e-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: 77.09 E-value: 4.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 3 IAVQAVS-----HQYGGH--HALDNINLCLKPG-LTMLLGPNGAGKSTLFALITGLQKLTQGSITF-------DGATLSQ 67
Cdd:COG4778 5 LEVENLSktftlHLQGGKrlPVLDGVSFSVAAGeCVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrhdggwvDLAQASP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 68 SRtsIMA----KMGVVFQ-------QSTLDIdlsVKQNLsyFAslHGISTASALSHIQGLLDELDLTSKL-----NTkir 131
Cdd:COG4778 85 RE--ILAlrrrTIGYVSQflrviprVSALDV---VAEPL--LE--RGVDREEARARARELLARLNLPERLwdlppAT--- 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 521328941 132 nLNGGHRRRVELARCLIHKPSLLLLDEPTVGLDIESRHLILRVVQAL 178
Cdd:COG4778 153 -FSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEA 198
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
3-197 |
4.20e-17 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 79.71 E-value: 4.20e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 3 IAVQAVSHQYGGHHALDNINLCLKPG-LTMLLGPNGAGKSTLFALITGLQKLTQGSITFDGATLSQSRTSIMAKMGV--V 79
Cdd:PRK15439 12 LCARSISKQYSGVEVLKGIDFTLHAGeVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQLGIylV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 80 FQQSTLDIDLSVKQNLsyfasLHGIS-TASALSHIQGLLDELDLTSKLNTKIRNLNGGHRRRVELARCLIHKPSLLLLDE 158
Cdd:PRK15439 92 PQEPLLFPNLSVKENI-----LFGLPkRQASMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILILDE 166
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 521328941 159 PTVGLD-IESRHLILRvVQALaHSQSVSVLWATHLFEEVK 197
Cdd:PRK15439 167 PTASLTpAETERLFSR-IREL-LAQGVGIVFISHKLPEIR 204
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
14-213 |
4.87e-17 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 77.94 E-value: 4.87e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 14 GHHALDNINLCLKPG-LTMLLGPNGAGKSTLFALITGlqKLT----------QGSITFDGATLSQSRTSIMAKMGVVF-Q 81
Cdd:PRK13547 13 HRAILRDLSLRIEPGrVTALLGRNGAGKSTLLKALAG--DLTgggaprgarvTGDVTLNGEPLAAIDAPRLARLRAVLpQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 82 QSTLDIDLSVKQNLSYFASLHGiSTASALSHIQG-----LLDELDLTSKLNTKIRNLNGGHRRRVELARCL--------- 147
Cdd:PRK13547 91 AAQPAFAFSAREIVLLGRYPHA-RRAGALTHRDGeiawqALALAGATALVGRDVTTLSGGELARVQFARVLaqlwpphda 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 521328941 148 IHKPSLLLLDEPTVGLDIESRHLILRVVQALAHSQSVSVLWATHLFE-EVKHNNNLIVLSKGRVLAH 213
Cdd:PRK13547 170 AQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNlAARHADRIAMLADGAIVAH 236
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
12-214 |
5.11e-17 |
|
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: 76.80 E-value: 5.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 12 YGGHHALDNINLCLKPGLTM-LLGPNGAGKSTLFALITGLQKLTQGSITFDGATlsqsrTSIMAkMGVVFQQstldiDLS 90
Cdd:cd03220 32 VGEFWALKDVSFEVPRGERIgLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRV-----SSLLG-LGGGFNP-----ELT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 91 VKQNLSYFASLHGISTASALSHIQGLLDELDLTSKLNTKIRNLNGGHRRRVELARCLIHKPSLLLLDEPT-VGlDiesRH 169
Cdd:cd03220 101 GRENIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLaVG-D---AA 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 521328941 170 LILRVVQALAH--SQSVSVLWATHLFEEVKHN-NNLIVLSKGRVLAHD 214
Cdd:cd03220 177 FQEKCQRRLREllKQGKTVILVSHDPSSIKRLcDRALVLEKGKIRFDG 224
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
13-221 |
6.35e-17 |
|
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: 79.34 E-value: 6.35e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 13 GGHHALDNINLCLKPGLTM-LLGPNGAGKSTLFALITGLQKlTQGSITFDGATLSQSRTSIM----AKMGVVFQQ--STL 85
Cdd:COG4172 297 GHVKAVDGVSLTLRRGETLgLVGESGSGKSTLGLALLRLIP-SEGEIRFDGQDLDGLSRRALrplrRRMQVVFQDpfGSL 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 86 DIDLSVKQNLSYFASLHGI--STASALSHIQGLLDELDLTSKLntkiRN-----LNGGHRRRVELARCLIHKPSLLLLDE 158
Cdd:COG4172 376 SPRMTVGQIIAEGLRVHGPglSAAERRARVAEALEEVGLDPAA----RHrypheFSGGQRQRIAIARALILEPKLLVLDE 451
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 159 PTVGLD-------------IESRH-----LI---LRVVQALAHsqsvsvlwathlfeEVkhnnnlIVLSKGRVLAHDQCE 217
Cdd:COG4172 452 PTSALDvsvqaqildllrdLQREHglaylFIshdLAVVRALAH--------------RV------MVMKDGKVVEQGPTE 511
|
....
gi 521328941 218 ALLA 221
Cdd:COG4172 512 QVFD 515
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
2-214 |
6.43e-17 |
|
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: 76.30 E-value: 6.43e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 2 EIAVQAVSHQYGGH--HALDNINLCLKPGLTM-LLGPNGAGKSTLFALITGLQKLTQGSITFDGATLSQ-SRTSIMAKMG 77
Cdd:cd03369 6 EIEVENLSVRYAPDlpPVLKNVSFKVKAGEKIgIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTiPLEDLRSSLT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 78 VVFQQSTLdIDLSVKQNLSYFASLHGISTASALSHIQGLLdeldltsklntkirNLNGGHRRRVELARCLIHKPSLLLLD 157
Cdd:cd03369 86 IIPQDPTL-FSGTIRSNLDPFDEYSDEEIYGALRVSEGGL--------------NLSQGQRQLLCLARALLKRPRVLVLD 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 521328941 158 EPTVGLDIESRHLILRVVQALahSQSVSVLWATHLFEEVKHNNNLIVLSKGRVLAHD 214
Cdd:cd03369 151 EATASIDYATDALIQKTIREE--FTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYD 205
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
8-196 |
7.21e-17 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 79.18 E-value: 7.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 8 VSHQYGGHHALDNINLCLKPG-LTMLLGPNGAGKSTLFALITGLQKLTQGSITFDGATL--SQSRTSIMAKMGVVFQQST 84
Cdd:PRK11288 10 IGKTFPGVKALDDISFDCRAGqVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMrfASTTAALAAGVAIIYQELH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 85 LDIDLSVKQN--LSYFASLHGISTASAL-SHIQGLLDELDLTSKLNTKIRNLNGGHRRRVELARCLIHKPSLLLLDEPTV 161
Cdd:PRK11288 90 LVPEMTVAENlyLGQLPHKGGIVNRRLLnYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAFDEPTS 169
|
170 180 190
....*....|....*....|....*....|....*.
gi 521328941 162 GLDI-ESRHLiLRVVQALaHSQSVSVLWATHLFEEV 196
Cdd:PRK11288 170 SLSArEIEQL-FRVIREL-RAEGRVILYVSHRMEEI 203
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
25-187 |
1.96e-16 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 75.27 E-value: 1.96e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 25 LKPGLTMLL-GPNGAGKSTLFALITGLQKLTQGSITFDGATLSQS-RTSIMAKMGvvfQQSTLDIDLSVKQNLSYFASLH 102
Cdd:PRK13543 34 VDAGEALLVqGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGdRSRFMAYLG---HLPGLKADLSTLENLHFLCGLH 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 103 GI----STASALShIQGLLDELDltsklnTKIRNLNGGHRRRVELARCLIHKPSLLLLDEPTVGLDIESRHLILRVVQAL 178
Cdd:PRK13543 111 GRrakqMPGSALA-IVGLAGYED------TLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEGITLVNRMISAH 183
|
....*....
gi 521328941 179 AHSQSVSVL 187
Cdd:PRK13543 184 LRGGGAALV 192
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
3-212 |
2.41e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 75.93 E-value: 2.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 3 IAVQAVSHQY-GGHHALDNINLCLKPG-LTMLLGPNGAGKSTLFALITGLQKLTQGSITFDGATLSQSRTS-IMAKMGVV 79
Cdd:PRK13647 5 IEVEDLHFRYkDGTKALKGLSLSIPEGsKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKwVRSKVGLV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 80 FQQ-------STLDIDLSV-KQNLsyfaslhGISTASALSHIQGLLDELDLTSKLNTKIRNLNGGHRRRVELARCLIHKP 151
Cdd:PRK13647 85 FQDpddqvfsSTVWDDVAFgPVNM-------GLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDP 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 521328941 152 SLLLLDEPTVGLDIESRHLILRVVQALaHSQSVSVLWATHLFE-EVKHNNNLIVLSKGRVLA 212
Cdd:PRK13647 158 DVIVLDEPMAYLDPRGQETLMEILDRL-HNQGKTVIVATHDVDlAAEWADQVIVLKEGRVLA 218
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
3-166 |
3.23e-16 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 77.08 E-value: 3.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 3 IAVQAVSHQYGGHHALDNINLCLKPG-LTMLLGPNGAGKSTLFALITGLQKLTQGSITFdGATlsqsrtsimAKMGVVFQ 81
Cdd:PRK11819 325 IEAENLSKSFGDRLLIDDLSFSLPPGgIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GET---------VKLAYVDQ 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 82 Q-STLDIDLSVKQNLSyfaslhgistasalshiqGLLDELDL----------TSKLN-------TKIRNLNGGHRRRVEL 143
Cdd:PRK11819 395 SrDALDPNKTVWEEIS------------------GGLDIIKVgnreipsrayVGRFNfkggdqqKKVGVLSGGERNRLHL 456
|
170 180
....*....|....*....|...
gi 521328941 144 ARCLIHKPSLLLLDEPTVGLDIE 166
Cdd:PRK11819 457 AKTLKQGGNVLLLDEPTNDLDVE 479
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
20-198 |
3.45e-16 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 77.01 E-value: 3.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 20 NINLCLKPGLTM-LLGPNGAGKSTLFALITGLQKLTQGSITFDGATLSQSRTSIMAKMGVVF-----QQSTLDIDLSVKQ 93
Cdd:PRK15439 281 NISLEVRAGEILgLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRLARGLVYlpedrQSSGLYLDAPLAW 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 94 NLSyfASLHG-----ISTASALSHIQGLLDELDLT-SKLNTKIRNLNGGHRRRVELARCLIHKPSLLLLDEPTVGLDIES 167
Cdd:PRK15439 361 NVC--ALTHNrrgfwIKPARENAVLERYRRALNIKfNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSA 438
|
170 180 190
....*....|....*....|....*....|.
gi 521328941 168 RHLILRVVQALAhSQSVSVLWATHLFEEVKH 198
Cdd:PRK15439 439 RNDIYQLIRSIA-AQNVAVLFISSDLEEIEQ 468
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
3-168 |
3.71e-16 |
|
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: 72.87 E-value: 3.71e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 3 IAVQAVSHQYGGHHALDNINLCLKPGLTM-LLGPNGAGKSTLFALITGLQKLTQGSITFDGATlsqsrtsimakmgvvfq 81
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIgLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTV----------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 82 qstldidlsvkqNLSYFAslhgistasalshiqglldeldltsklntkirNLNGGHRRRVELARCLIHKPSLLLLDEPTV 161
Cdd:cd03221 64 ------------KIGYFE--------------------------------QLSGGEKMRLALAKLLLENPNLLLLDEPTN 99
|
....*..
gi 521328941 162 GLDIESR 168
Cdd:cd03221 100 HLDLESI 106
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
12-212 |
3.76e-16 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 75.41 E-value: 3.76e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 12 YGGHHALDNINLCLKPG-LTMLLGPNGAGKSTLFALITGLQKLTQGSITFDGATLSQSRTSIMAK-MGVVFQQSTLDIDL 89
Cdd:PRK10253 17 YGKYTVAENLTVEIPDGhFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARrIGLLAQNATTPGDI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 90 SVKQNLSYFASLHG-IST---ASALSHIQGLLDELDLTSKLNTKIRNLNGGHRRRVELARCLIHKPSLLLLDEPTVGLDI 165
Cdd:PRK10253 97 TVQELVARGRYPHQpLFTrwrKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDI 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 521328941 166 ESRHLILRVVQALAHSQSVSVLWATH-LFEEVKHNNNLIVLSKGRVLA 212
Cdd:PRK10253 177 SHQIDLLELLSELNREKGYTLAAVLHdLNQACRYASHLIALREGKIVA 224
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
18-191 |
3.83e-16 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 74.22 E-value: 3.83e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 18 LDNINLCL-KPGLTMLLGPNGAGKSTLFALITGLQKLTQGSITFDGATLSQSRTSIMAKMGVVFQQSTLDIDLSVKQNls 96
Cdd:PRK13540 17 LQQISFHLpAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKQLCFVGHRSGINPYLTLREN-- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 97 yfaSLHGISTASALSHIQGLLDELDLTSKLNTKIRNLNGGHRRRVELARCLIHKPSLLLLDEPTVGLDIESRHLILRVVQ 176
Cdd:PRK13540 95 ---CLYDIHFSPGAVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTIITKIQ 171
|
170
....*....|....*
gi 521328941 177 AlAHSQSVSVLWATH 191
Cdd:PRK13540 172 E-HRAKGGAVLLTSH 185
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
2-233 |
5.87e-16 |
|
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: 76.40 E-value: 5.87e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 2 EIAVQAVSHQYGGHHA-LDNINLCLKPGLTM-LLGPNGAGKSTLFALITGLQKLTQGSITFDGATLSQ-SRTSIMAKMGV 78
Cdd:COG5265 357 EVRFENVSFGYDPERPiLKGVSFEVPAGKTVaIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDvTQASLRAAIGI 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 79 VFQQSTLDIDlSVKQNLSYF---ASLHGISTASALSHIQGLLDEldLTSKLNTKI--R--NLNGGHRRRVELARCLIHKP 151
Cdd:COG5265 437 VPQDTVLFND-TIAYNIAYGrpdASEEEVEAAARAAQIHDFIES--LPDGYDTRVgeRglKLSGGEKQRVAIARTLLKNP 513
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 152 SLLLLDEPTVGLDIESRHLILRVVQALAHSQSVSVLwaTHLFEEVKHNNNLIVLSKGRVL---AHDQceaLLAK---YHQ 225
Cdd:COG5265 514 PILIFDEATSALDSRTERAIQAALREVARGRTTLVI--AHRLSTIVDADEILVLEAGRIVergTHAE---LLAQgglYAQ 588
|
....*...
gi 521328941 226 qdiehLWQ 233
Cdd:COG5265 589 -----MWA 591
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
3-235 |
8.50e-16 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 74.28 E-value: 8.50e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 3 IAVQAVSHQYGGHHALDNINLCLKPG-LTMLLGPNGAGKSTLFALITGL---QKLTQGSITFDGATLSQS-------RTS 71
Cdd:PRK09984 5 IRVEKLAKTFNQHQALHAVDLNIHHGeMVALLGPSGSGKSTLLRHLSGLitgDKSAGSHIELLGRTVQREgrlardiRKS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 72 iMAKMGVVFQQSTLDIDLSVKQN---------------LSYFASLHGISTASALSHIqglldelDLTSKLNTKIRNLNGG 136
Cdd:PRK09984 85 -RANTGYIFQQFNLVNRLSVLENvligalgstpfwrtcFSWFTREQKQRALQALTRV-------GMVHFAHQRVSTLSGG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 137 HRRRVELARCLIHKPSLLLLDEPTVGLDIESRHLILRVVQALAHSQSVSVLWATHLFE-EVKHNNNLIVLSKGRVLaHDQ 215
Cdd:PRK09984 157 QQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDyALRYCERIVALRQGHVF-YDG 235
|
250 260
....*....|....*....|
gi 521328941 216 CEallAKYHQQDIEHLWQHL 235
Cdd:PRK09984 236 SS---QQFDNERFDHLYRSI 252
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
32-179 |
1.13e-15 |
|
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: 73.60 E-value: 1.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 32 LLGPNGAGKSTLFALITGLQKLTQGSITFDGATLSQSRTSIMAKmgvvfQQSTLDidlsvkqnlsyfASLHGIsTASALS 111
Cdd:cd03237 30 ILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSYKPQYIKAD-----YEGTVR------------DLLSSI-TKDFYT 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 521328941 112 HIQ---GLLDELDLTSKLNTKIRNLNGGHRRRVELARCLIHKPSLLLLDEPTVGLDIESRHLILRVVQALA 179
Cdd:cd03237 92 HPYfktEIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFA 162
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
3-212 |
2.39e-15 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 73.38 E-value: 2.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 3 IAVQAVSHQY-GGHHALDNINLCLKPG-LTMLLGPNGAGKSTLFALITGLQKLTQGSITFDGATLSQS-RTSIMAkmgVV 79
Cdd:PRK15056 7 IVVNDVTVTWrNGHTALRDASFTVPGGsIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQAlQKNLVA---YV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 80 FQQSTLDIDLSVKQNLSYFASLHG------ISTASALSHIQGLLDELDLTSKLNTKIRNLNGGHRRRVELARCLIHKPSL 153
Cdd:PRK15056 84 PQSEEVDWSFPVLVEDVVMMGRYGhmgwlrRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQV 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 521328941 154 LLLDEPTVGLDIESRHLILRVVQALaHSQSVSVLWATHLFEEVKHNNNLIVLSKGRVLA 212
Cdd:PRK15056 164 ILLDEPFTGVDVKTEARIISLLREL-RDEGKTMLVSTHNLGSVTEFCDYTVMVKGTVLA 221
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
33-229 |
3.18e-15 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 74.39 E-value: 3.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 33 LGPNGAGKSTLFALITGLQKLTQGSITFDGATLSQSRTSIMAKMGVVFQQSTLDIDLSVKQNLSYFASLHGISTASALSH 112
Cdd:NF033858 298 LGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDAGDIATRRRVGYMSQAFSLYGELTVRQNLELHARLFHLPAAEIAAR 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 113 IQGLLDELDLTSKLNTKIRNLNGGHRRRVELARCLIHKPSLLLLDEPTVGLDIESRHLILRVVQALAHSQSVSVLWATHL 192
Cdd:NF033858 378 VAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVARDMFWRLLIELSREDGVTIFISTHF 457
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 521328941 193 FEEVK--------HnnnlivlsKGRVLAHDQCEALLAKYHQQDIE 229
Cdd:NF033858 458 MNEAErcdrislmH--------AGRVLASDTPAALVAARGAATLE 494
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
1-229 |
6.05e-15 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 73.59 E-value: 6.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 1 MEIAVQAVSHQYGGHHALDNINLCLKPGLTM-LLGPNGAGKSTLFALITGLQKLTQGSITFDGATLSQSR-TSIMAKMGV 78
Cdd:PRK10789 314 LDVNIRQFTYPQTDHPALENVNFTLKPGQMLgICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQlDSWRSRLAV 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 79 VFQQSTLDIDlSVKQNLSY---FASLHGISTASALSHIQGllDELDLTSKLNTKIRN----LNGGHRRRVELARCLIHKP 151
Cdd:PRK10789 394 VSQTPFLFSD-TVANNIALgrpDATQQEIEHVARLASVHD--DILRLPQGYDTEVGErgvmLSGGQKQRISIARALLLNA 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 152 SLLLLDEPTVGLDIESRHLILRVVQALAHSQSVSVlwATHLFEEVKHNNNLIVLSKGRVLAHDQCEALLAK-------YH 224
Cdd:PRK10789 471 EILILDDALSAVDGRTEHQILHNLRQWGEGRTVII--SAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQsgwyrdmYR 548
|
....*
gi 521328941 225 QQDIE 229
Cdd:PRK10789 549 YQQLE 553
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
3-210 |
6.71e-15 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 72.57 E-value: 6.71e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 3 IAVQAVSHQY-GGHHALDNINLCLKPG-LTMLLGPNGAGKSTLFALITGLQKLTQGSITFDGATLSQ----SRTSIMakm 76
Cdd:PRK11650 4 LKLQAVRKSYdGKTQVIKGIDLDVADGeFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNElepaDRDIAM--- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 77 gvVFQQSTLDIDLSVKQNLSYFASLHGISTASALSHIQGLLDELDLTSKLNTKIRNLNGGHRRRVELARCLIHKPSLLLL 156
Cdd:PRK11650 81 --VFQNYALYPHMSVRENMAYGLKIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLF 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 157 DEPTVGLDIEsrhliLRV-----VQALAHSQSVSVLWATH-LFEEVKHNNNLIVLSKGRV 210
Cdd:PRK11650 159 DEPLSNLDAK-----LRVqmrleIQRLHRRLKTTSLYVTHdQVEAMTLADRVVVMNGGVA 213
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
3-226 |
9.98e-15 |
|
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: 9.98e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 3 IAVQAVSHQYGGHHALDNINLCLKPGLTM-LLGPNGAGKSTLFALITGLQKL--TQGSITFD------------------ 61
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLgILGRSGAGKSVLMHVLRGMDQYepTSGRIIYHvalcekcgyverpskvge 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 62 -----GATLSQS-----------RTSIMAKMGVVFQQS-TLDIDLSVKQNLsyFASLH--GISTASALSHIQGLLDELDL 122
Cdd:TIGR03269 81 pcpvcGGTLEPEevdfwnlsdklRRRIRKRIAIMLQRTfALYGDDTVLDNV--LEALEeiGYEGKEAVGRAVDLIEMVQL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 123 TSKLNTKIRNLNGGHRRRVELARCLIHKPSLLLLDEPTVGLDIESRHLILRVVQALAHSQSVSVLWATHlFEEV--KHNN 200
Cdd:TIGR03269 159 SHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSH-WPEVieDLSD 237
|
250 260
....*....|....*....|....*.
gi 521328941 201 NLIVLSKGRVLAHDQCEALLAKYHQQ 226
Cdd:TIGR03269 238 KAIWLENGEIKEEGTPDEVVAVFMEG 263
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
2-164 |
1.04e-14 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 71.35 E-value: 1.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 2 EIAVQAVSHQYGGHHALDNINLCL-KPGLTMLLGPNGAGKSTLFALITGLQKL-----TQGSITFDGATLSQSR---TSI 72
Cdd:PRK14243 10 VLRTENLNVYYGSFLAVKNVWLDIpKNQITAFIGPSGCGKSTILRCFNRLNDLipgfrVEGKVTFHGKNLYAPDvdpVEV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 73 MAKMGVVFQQSTlDIDLSVKQNLSYFASLHGistasalshIQGLLDEL------------DLTSKLNTKIRNLNGGHRRR 140
Cdd:PRK14243 90 RRRIGMVFQKPN-PFPKSIYDNIAYGARING---------YKGDMDELverslrqaalwdEVKDKLKQSGLSLSGGQQQR 159
|
170 180
....*....|....*....|....
gi 521328941 141 VELARCLIHKPSLLLLDEPTVGLD 164
Cdd:PRK14243 160 LCIARAIAVQPEVILMDEPCSALD 183
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
7-221 |
1.57e-14 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 72.05 E-value: 1.57e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 7 AVSHQYGGHHALDNINLCLKPGLTM-LLGPNGAGKStlfalITGLQKL----------TQGSITFDG--------ATLSQ 67
Cdd:PRK15134 14 AFRQQQTVRTVVNDVSLQIEAGETLaLVGESGSGKS-----VTALSILrllpsppvvyPSGDIRFHGesllhaseQTLRG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 68 SRTSimaKMGVVFQQ--STLDIDLSVKQNLSYFASLH-GISTASALSHIQGLLDELDL---TSKLNTKIRNLNGGHRRRV 141
Cdd:PRK15134 89 VRGN---KIAMIFQEpmVSLNPLHTLEKQLYEVLSLHrGMRREAARGEILNCLDRVGIrqaAKRLTDYPHQLSGGERQRV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 142 ELARCLIHKPSLLLLDEPTVGLDIESRHLILRVVQALAHSQSVSVLWATHLFEEVKH-NNNLIVLSKGRVLAHDQCEALL 220
Cdd:PRK15134 166 MIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKlADRVAVMQNGRCVEQNRAATLF 245
|
.
gi 521328941 221 A 221
Cdd:PRK15134 246 S 246
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
3-208 |
1.74e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 70.84 E-value: 1.74e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 3 IAVQAVSHQYGGHHALDNINLCL-KPGLTMLLGPNGAGKSTLFALITGLQKL-----TQGSITFDGATLSQSRTSI---M 73
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIyQSKVTAIIGPSGCGKSTFLKCLNRMNELesevrVEGRVEFFNQNIYERRVNLnrlR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 74 AKMGVVFQQSTLdIDLSVKQNLSYFASLHGISTASALSHI-QGLLDELDLTSKLNTKIR----NLNGGHRRRVELARCLI 148
Cdd:PRK14258 88 RQVSMVHPKPNL-FPMSVYDNVAYGVKIVGWRPKLEIDDIvESALKDADLWDEIKHKIHksalDLSGGQQQRLCIARALA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 149 HKPSLLLLDEPTVGLDIESRHLILRVVQALAHSQSVSVLWATHLFEEVKHNNNLIVLSKG 208
Cdd:PRK14258 167 VKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKG 226
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
3-222 |
2.49e-14 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 71.30 E-value: 2.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 3 IAVQAVSHQYGGHHALDNINLCLKPGLTM-LLGPNGAG--KSTLFALITGLQKltqGSITFDGATLSQSRTSIMAKMGVV 79
Cdd:NF000106 14 VEVRGLVKHFGEVKAVDGVDLDVREGTVLgVLGP*GAA**RGALPAHV*GPDA---GRRPWRF*TWCANRRALRRTIG*H 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 80 FQ-QSTLDIDLSVKQNLSYFASLHGISTASALSHIQGLLDELDLTSKLNTKIRNLNGGHRRRVELARCLIHKPSLLLLDE 158
Cdd:NF000106 91 RPvR*GRRESFSGRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDE 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 521328941 159 PTVGLDIESRHLILRVVQALAHSQSVSVLWATHLFEEVKHNNNLIVLSKGRVLAHDQCEALLAK 222
Cdd:NF000106 171 PTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDELKTK 234
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
32-215 |
2.60e-14 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 71.48 E-value: 2.60e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 32 LLGPNGAGKSTLFALITGLQKLTQGSITFDGATLS--QSRTSIMAKM----------GVVFQQSTLD-IDLSVKQNLSYF 98
Cdd:PRK11288 284 LFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDirSPRDAIRAGImlcpedrkaeGIIPVHSVADnINISARRHHLRA 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 99 ASL--HGISTASALSHIQGLLDEldlTSKLNTKIRNLNGGHRRRVELARCLIHKPSLLLLDEPTVGLDIESRHLILRVVQ 176
Cdd:PRK11288 364 GCLinNRWEAENADRFIRSLNIK---TPSREQLIMNLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIY 440
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 521328941 177 ALAhSQSVSVLWATHLFEEVKH-NNNLIVLSKGRV---LAHDQ 215
Cdd:PRK11288 441 ELA-AQGVAVLFVSSDLPEVLGvADRIVVMREGRIageLAREQ 482
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
18-208 |
3.21e-14 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 71.68 E-value: 3.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 18 LDNINLCLKPG-LTMLLGPNGAGKSTLFALITglQKLTQGSITfDGATLSQSR---TSIMAKMGVVFQQstlDIDL---S 90
Cdd:TIGR00956 779 LNNVDGWVKPGtLTALMGASGAGKTTLLNVLA--ERVTTGVIT-GGDRLVNGRpldSSFQRSIGYVQQQ---DLHLptsT 852
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 91 VKQNLSYFASLH---GISTASALSHIQGLLDELDLTSKLNTKI----RNLNGGHRRRVELARCLIHKPSLLL-LDEPTVG 162
Cdd:TIGR00956 853 VRESLRFSAYLRqpkSVSKSEKMEYVEEVIKLLEMESYADAVVgvpgEGLNVEQRKRLTIGVELVAKPKLLLfLDEPTSG 932
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 521328941 163 LDIESRHLILRVVQALA-HSQsvSVLWATH-----LFEEVkhnNNLIVLSKG 208
Cdd:TIGR00956 933 LDSQTAWSICKLMRKLAdHGQ--AILCTIHqpsaiLFEEF---DRLLLLQKG 979
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
18-209 |
3.40e-14 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 71.68 E-value: 3.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 18 LDNINLCLKPG-LTMLLGPNGAGKSTLFALIT----GLQKLTQGSITFDGATLSQSRTSimaKMGVVFQQSTLDI---DL 89
Cdd:TIGR00956 77 LKPMDGLIKPGeLTVVLGRPGSGCSTLLKTIAsntdGFHIGVEGVITYDGITPEEIKKH---YRGDVVYNAETDVhfpHL 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 90 SVKQNLSYFASLH-------GISTASALSHIQGL-LDELDLTSKLNTK-----IRNLNGGHRRRVELARCLIHKPSLLLL 156
Cdd:TIGR00956 154 TVGETLDFAARCKtpqnrpdGVSREEYAKHIADVyMATYGLSHTRNTKvgndfVRGVSGGERKRVSIAEASLGGAKIQCW 233
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 521328941 157 DEPTVGLDIESRHLILRVVQALAHSQSVSVLWATH--------LFEEVkhnnnlIVLSKGR 209
Cdd:TIGR00956 234 DNATRGLDSATALEFIRALKTSANILDTTPLVAIYqcsqdayeLFDKV------IVLYEGY 288
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
32-222 |
6.10e-14 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 70.78 E-value: 6.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 32 LLGPNGAGKSTLFALITGLQKLTQGSITFDGATLSQSRTSIMAKMGVVFQQSTLDIDLSVKQNLSYFASLHGISTASAL- 110
Cdd:PLN03232 1267 VVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNIDPFSEHNDADLWEALe 1346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 111 -SHIQGLLDE--LDLTSKLNTKIRNLNGGHRRRVELARCLIHKPSLLLLDEPTVGLDIESRHLILRVVQalAHSQSVSVL 187
Cdd:PLN03232 1347 rAHIKDVIDRnpFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIR--EEFKSCTML 1424
|
170 180 190
....*....|....*....|....*....|....*
gi 521328941 188 WATHLFEEVKHNNNLIVLSKGRVLAHDQCEALLAK 222
Cdd:PLN03232 1425 VIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSR 1459
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
15-210 |
8.23e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 68.96 E-value: 8.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 15 HHALDNINLCLKPG-LTMLLGPNGAGKSTLFALITGLQKLTQGSITFDGATLSQSRT--SIMAKMGVVFQQSTLDIDLS- 90
Cdd:PRK13633 23 KLALDDVNLEVKKGeFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENlwDIRNKAGMVFQNPDNQIVATi 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 91 VKQNLSYFASLHGISTASALSHIQGLLDELDLTSKLNTKIRNLNGGHRRRVELARCLIHKPSLLLLDEPTVGLDIESRHL 170
Cdd:PRK13633 103 VEEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGRRE 182
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 521328941 171 ILRVVQALAHSQSVSVLWATHLFEEVKHNNNLIVLSKGRV 210
Cdd:PRK13633 183 VVNTIKELNKKYGITIILITHYMEEAVEADRIIVMDSGKV 222
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-164 |
9.44e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 68.33 E-value: 9.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 1 MEIAVQAVSHQ--YGGHHALDNINLCL-KPGLTMLLGPNGAGKSTLFALITGLQKLTQ-----GSITFDGATLSQSRTS- 71
Cdd:PRK14267 1 MKFAIETVNLRvyYGSNHVIKGVDLKIpQNGVFALMGPSGCGKSTLLRTFNRLLELNEearveGEVRLFGRNIYSPDVDp 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 72 --IMAKMGVVFQQSTLDIDLSVKQNLSYFASLHGistasaLSHIQGLLDEL------------DLTSKLNTKIRNLNGGH 137
Cdd:PRK14267 81 ieVRREVGMVFQYPNPFPHLTIYDNVAIGVKLNG------LVKSKKELDERvewalkkaalwdEVKDRLNDYPSNLSGGQ 154
|
170 180
....*....|....*....|....*..
gi 521328941 138 RRRVELARCLIHKPSLLLLDEPTVGLD 164
Cdd:PRK14267 155 RQRLVIARALAMKPKILLMDEPTANID 181
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
18-191 |
1.03e-13 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 69.75 E-value: 1.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 18 LDNINLCLKPG-LTMLLGPNGAGKSTLFALITGLQKLTQGSITFDGATLSQSRTSIMAKM-----GVVFQQSTLDIDLSV 91
Cdd:PRK10535 24 LKGISLDIYAGeMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQLrrehfGFIFQRYHLLSHLTA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 92 KQNLSYFASLHGISTASALSHIQGLLDELDLTSKLNTKIRNLNGGHRRRVELARCLIHKPSLLLLDEPTVGLDIESRHLI 171
Cdd:PRK10535 104 AQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDSHSGEEV 183
|
170 180
....*....|....*....|
gi 521328941 172 LRVVQALaHSQSVSVLWATH 191
Cdd:PRK10535 184 MAILHQL-RDRGHTVIIVTH 202
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
13-165 |
1.20e-13 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 69.67 E-value: 1.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 13 GGHHALDNINLCLKPG-LTMLLGPNGAGKSTLFALITGLQKLTQGSITFDGATLSQSRTSIMAKMGVVF-----QQSTLD 86
Cdd:COG3845 269 RGVPALKDVSLEVRAGeILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLGVAYipedrLGRGLV 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 87 IDLSVKQNL-------SYFASLHGISTASALSHIQGLLDELDL-TSKLNTKIRNLNGGHRRRVELARCLIHKPSLLLLDE 158
Cdd:COG3845 349 PDMSVAENLilgryrrPPFSRGGFLDRKAIRAFAEELIEEFDVrTPGPDTPARSLSGGNQQKVILARELSRDPKLLIAAQ 428
|
....*..
gi 521328941 159 PTVGLDI 165
Cdd:COG3845 429 PTRGLDV 435
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
1-211 |
1.24e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 68.57 E-value: 1.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 1 MEIAVQAVSHQYGGH-----HALDNINLCLKPG-LTMLLGPNGAGKSTLFALITGLQKLTQGSITF-------------- 60
Cdd:PRK13651 1 MQIKVKNIVKIFNKKlptelKALDNVSVEINQGeFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWifkdeknkkktkek 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 61 ----DGATLSQSRT-------SIMAKMGVVFQ-------QSTLDIDLSVKQnLSYfaslhGISTASALSHIQGLLDELDL 122
Cdd:PRK13651 81 ekvlEKLVIQKTRFkkikkikEIRRRVGVVFQfaeyqlfEQTIEKDIIFGP-VSM-----GVSKEEAKKRAAKYIELVGL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 123 -TSKLNTKIRNLNGGHRRRVELARCLIHKPSLLLLDEPTVGLDIESRHLILRVVQALaHSQSVSVLWATHLFEEV-KHNN 200
Cdd:PRK13651 155 dESYLQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNL-NKQGKTIILVTHDLDNVlEWTK 233
|
250
....*....|.
gi 521328941 201 NLIVLSKGRVL 211
Cdd:PRK13651 234 RTIFFKDGKII 244
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
17-209 |
1.72e-13 |
|
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: 66.72 E-value: 1.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 17 ALDNINLCLKPG-LTMLLGPNGAGKSTLFALITGLQKLTQGSITFDGatlsqsrtsimaKMGVVFQQSTLdIDLSVKQNL 95
Cdd:cd03250 20 TLKDINLEVPKGeLVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG------------SIAYVSQEPWI-QNGTIRENI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 96 ---------SYFASLHgistASALshiqglldELDL---TSKLNTKI----RNLNGGHRRRVELARCLIHKPSLLLLDEP 159
Cdd:cd03250 87 lfgkpfdeeRYEKVIK----ACAL--------EPDLeilPDGDLTEIgekgINLSGGQKQRISLARAVYSDADIYLLDDP 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 521328941 160 TVGLDIE-SRHLILRVVQ-ALAHSQsvSVLWATHLFEEVKHNNNLIVLSKGR 209
Cdd:cd03250 155 LSAVDAHvGRHIFENCILgLLLNNK--TRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
3-196 |
1.99e-13 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 68.88 E-value: 1.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 3 IAVQAVSHQYGGHHALDNINLCLKPGLTM-LLGPNGAGKSTLFALITGLQKLTQGSITFDG--ATLSQSRTSIMAKMGVV 79
Cdd:PRK10762 5 LQLKGIDKAFPGVKALSGAALNVYPGRVMaLVGENGAGKSTMMKVLTGIYTRDAGSILYLGkeVTFNGPKSSQEAGIGII 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 80 FQQSTLDIDLSVKQNL----SYFASLHGISTASALSHIQGLLDELDLTSKLNTKIRNLNGGHRRRVELARCLIHKPSLLL 155
Cdd:PRK10762 85 HQELNLIPQLTIAENIflgrEFVNRFGRIDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVII 164
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 521328941 156 LDEPTVGL-DIESRHLiLRVVQALaHSQSVSVLWATHLFEEV 196
Cdd:PRK10762 165 MDEPTDALtDTETESL-FRVIREL-KSQGRGIVYISHRLKEI 204
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
18-186 |
2.09e-13 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 69.07 E-value: 2.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 18 LDNINLCLKPGLTMLL-GPNGAGKSTLFALITGLQKLTQGSITFDgatlsqsrtsimAKMGVVF--QQSTLdIDLSVKQN 94
Cdd:COG4178 379 LEDLSLSLKPGERLLItGPSGSGKSTLLRAIAGLWPYGSGRIARP------------AGARVLFlpQRPYL-PLGTLREA 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 95 LSYFASLHGISTASA--------LSHIQGLLDELDLTSKLntkirnLNGGHRRRVELARCLIHKPSLLLLDEPTVGLDIE 166
Cdd:COG4178 446 LLYPATAEAFSDAELrealeavgLGHLAERLDEEADWDQV------LSLGEQQRLAFARLLLHKPDWLFLDEATSALDEE 519
|
170 180
....*....|....*....|.
gi 521328941 167 SRHLILRVVQA-LAHSQSVSV 186
Cdd:COG4178 520 NEAALYQLLREeLPGTTVISV 540
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
3-167 |
2.10e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 67.63 E-value: 2.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 3 IAVQAVSHQYGGHHALDNINLCLKPG-LTMLLGPNGAGKSTLFALITGLQKL-----TQGSITFDGATLSQSRTSIMAK- 75
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNtITALMGPSGSGKSTLLRVFNRLIELypearVSGEVYLDGQDIFKMDVIELRRr 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 76 MGVVFQQSTLDIDLSVKQNLSYFASLHGISTAS---------ALSHIQgLLDELdlTSKLNTKIRNLNGGHRRRVELARC 146
Cdd:PRK14247 84 VQMVFQIPNPIPNLSIFENVALGLKLNRLVKSKkelqervrwALEKAQ-LWDEV--KDRLDAPAGKLSGGQQQRLCIARA 160
|
170 180
....*....|....*....|.
gi 521328941 147 LIHKPSLLLLDEPTVGLDIES 167
Cdd:PRK14247 161 LAFQPEVLLADEPTANLDPEN 181
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
18-222 |
3.48e-13 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 68.43 E-value: 3.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 18 LDNINLCLKPGLTM-LLGPNGAGKSTLFALITGLQKLTQGSITFDGATLS-------QSRTSIMAKMGVVFQQStldidl 89
Cdd:TIGR00957 1302 LRHINVTIHGGEKVgIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAkiglhdlRFKITIIPQDPVLFSGS------ 1375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 90 sVKQNLSYFASL--HGISTASALSHIQGLLDELdlTSKLNTKI----RNLNGGHRRRVELARCLIHKPSLLLLDEPTVGL 163
Cdd:TIGR00957 1376 -LRMNLDPFSQYsdEEVWWALELAHLKTFVSAL--PDKLDHECaeggENLSVGQRQLVCLARALLRKTKILVLDEATAAV 1452
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 521328941 164 DIESRHLIlrvvQALAHSQ--SVSVLWATHLFEEVKHNNNLIVLSKGRVLAHDQCEALLAK 222
Cdd:TIGR00957 1453 DLETDNLI----QSTIRTQfeDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQ 1509
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
2-211 |
4.69e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 66.96 E-value: 4.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 2 EIAVQAVSHQYGGH-----HALDNINLCLKPG-LTMLLGPNGAGKSTLFALITGLQkLTQGSITFDG-----ATLSQSR- 69
Cdd:PRK13645 6 DIILDNVSYTYAKKtpfefKALNNTSLTFKKNkVTCVIGTTGSGKSTMIQLTNGLI-ISETGQTIVGdyaipANLKKIKe 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 70 -TSIMAKMGVVFQ-------QSTLDIDLSvkqnlsyFASLH-GISTASALSHIQGLLDELDLTSKLNTKIR-NLNGGHRR 139
Cdd:PRK13645 85 vKRLRKEIGLVFQfpeyqlfQETIEKDIA-------FGPVNlGENKQEAYKKVPELLKLVQLPEDYVKRSPfELSGGQKR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 521328941 140 RVELARCLIHKPSLLLLDEPTVGLDIESRHLILRVVQALAHSQSVSVLWATHLFEEV-KHNNNLIVLSKGRVL 211
Cdd:PRK13645 158 RVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVlRIADEVIVMHEGKVI 230
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
12-167 |
6.48e-13 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 67.67 E-value: 6.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 12 YGGHHALDNINLCLKPGLTM-LLGPNGAGKSTLFALITGLQKLTQGSITFDG----ATLSQSRTSimAKMGVVFQQstld 86
Cdd:PRK11147 13 FSDAPLLDNAELHIEDNERVcLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQdlivARLQQDPPR--NVEGTVYDF---- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 87 IDLSVKQNLSYFASLHGISTASA----------LSHIQGLLDELD---LTSKLN-----------TKIRNLNGGHRRRVE 142
Cdd:PRK11147 87 VAEGIEEQAEYLKRYHDISHLVEtdpseknlneLAKLQEQLDHHNlwqLENRINevlaqlgldpdAALSSLSGGWLRKAA 166
|
170 180
....*....|....*....|....*
gi 521328941 143 LARCLIHKPSLLLLDEPTVGLDIES 167
Cdd:PRK11147 167 LGRALVSNPDVLLLDEPTNHLDIET 191
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
3-225 |
7.06e-13 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 67.44 E-value: 7.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 3 IAVQAVSHQY-GGHHALDNINLCLKP-GLTMLLGPNGAGKSTLFALITGLQKLTQGSITFDGATLSQSRTSIMAKMGVVF 80
Cdd:PRK10790 341 IDIDNVSFAYrDDNLVLQNINLSVPSrGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMV 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 81 QQSTLDIDLSVKQNLSYFASLHGISTASALSHIQglLDEL--DLTSKLNTKI----RNLNGGHRRRVELARCLIHKPSLL 154
Cdd:PRK10790 421 QQDPVVLADTFLANVTLGRDISEEQVWQALETVQ--LAELarSLPDGLYTPLgeqgNNLSVGQKQLLALARVLVQTPQIL 498
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 521328941 155 LLDEPTVGLDIESRHLILRVVQALAHSQSVSVLwaTHLFEEVKHNNNLIVLSKGRVLAHDQCEALLAK---YHQ 225
Cdd:PRK10790 499 ILDEATANIDSGTEQAIQQALAAVREHTTLVVI--AHRLSTIVEADTILVLHRGQAVEQGTHQQLLAAqgrYWQ 570
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
18-165 |
1.48e-12 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 66.18 E-value: 1.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 18 LDNINLCLKPGltMLLGPNG---AGKSTLFALITGLQKLTQGSITFDGATLSQSRTSIMAKMGVVF-----QQSTLDIDL 89
Cdd:PRK10762 268 VNDVSFTLRKG--EILGVSGlmgAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDGLANGIVYisedrKRDGLVLGM 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 90 SVKQNLSYFASLHGISTASALSH---IQGLLDELDL----TSKLNTKIRNLNGGHRRRVELARCLIHKPSLLLLDEPTVG 162
Cdd:PRK10762 346 SVKENMSLTALRYFSRAGGSLKHadeQQAVSDFIRLfnikTPSMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRG 425
|
...
gi 521328941 163 LDI 165
Cdd:PRK10762 426 VDV 428
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
18-214 |
1.76e-12 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 65.05 E-value: 1.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 18 LDNINLCLKPGLT-MLLGPNGAGKSTLFALITG--LQKLTQGSITFDGATLSQSRTSIMAKMGV--VFQQ-------STL 85
Cdd:CHL00131 23 LKGLNLSINKGEIhAIMGPNGSGKSTLSKVIAGhpAYKILEGDILFKGESILDLEPEERAHLGIflAFQYpieipgvSNA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 86 D-IDLSVKQNLSYfaslHGISTASALSHIQGLLDELDLT----SKLNtkiRNLN----GGHRRRVELARCLIHKPSLLLL 156
Cdd:CHL00131 103 DfLRLAYNSKRKF----QGLPELDPLEFLEIINEKLKLVgmdpSFLS---RNVNegfsGGEKKRNEILQMALLDSELAIL 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 521328941 157 DEPTVGLDIESRHLILRVVQALAHSQSvSVLWATH---LFEEVKHN------NNLIVLSKGRVLAHD 214
Cdd:CHL00131 176 DETDSGLDIDALKIIAEGINKLMTSEN-SIILITHyqrLLDYIKPDyvhvmqNGKIIKTGDAELAKE 241
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
7-211 |
1.87e-12 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 64.21 E-value: 1.87e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 7 AVSHQYGGHHALDNINLCLKPG-LTMLLGPNGAGKSTLFALITGLQKLTQGSITFDgatlsqsrtsimakmgvvFQQSTL 85
Cdd:COG2401 35 GVELRVVERYVLRDLNLEIEPGeIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVD------------------VPDNQF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 86 DIDLSVKQNLsyfASLHGISTASALSHIQGLLDeldlTSKLNTKIRNLNGGHRRRVELARCLIHKPSLLLLDEPTVGLDI 165
Cdd:COG2401 97 GREASLIDAI---GRKGDFKDAVELLNAVGLSD----AVLWLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDR 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 521328941 166 ESRHLILRVVQALAHSQSVSVLWATHlFEEVKHN---NNLIVLSKGRVL 211
Cdd:COG2401 170 QTAKRVARNLQKLARRAGITLVVATH-HYDVIDDlqpDLLIFVGYGGVP 217
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
8-196 |
2.28e-12 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 65.91 E-value: 2.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 8 VSHQYGGHHALDNINLCLKPG-LTMLLGPNGAGKSTLFALITGLQKLTQGSITFDGATL--SQSRTSIMAKMGVVFQQST 84
Cdd:PRK10982 4 ISKSFPGVKALDNVNLKVRPHsIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIdfKSSKEALENGISMVHQELN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 85 LDIDLSVKQNL---SYFASLHGISTASALSHIQGLLDELDLTSKLNTKIRNLNGGHRRRVELARCLIHKPSLLLLDEPTV 161
Cdd:PRK10982 84 LVLQRSVMDNMwlgRYPTKGMFVDQDKMYRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTS 163
|
170 180 190
....*....|....*....|....*....|....*.
gi 521328941 162 GL-DIESRHLiLRVVQALaHSQSVSVLWATHLFEEV 196
Cdd:PRK10982 164 SLtEKEVNHL-FTIIRKL-KERGCGIVYISHKMEEI 197
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
33-187 |
2.40e-12 |
|
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: 65.96 E-value: 2.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 33 LGPNGAGKSTLFALITGLQKLTQGSITFDgatlsqsrtsimAKMGVVFQQSTLDIDLSVKQNLsYFASLHGISTASALSH 112
Cdd:COG1245 372 VGPNGIGKTTFAKILAGVLKPDEGEVDED------------LKISYKPQYISPDYDGTVEEFL-RSANTDDFGSSYYKTE 438
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 521328941 113 IqglLDELDLTSKLNTKIRNLNGGHRRRVELARCLIHKPSLLLLDEPTVGLDIESRHLILRVVQALAHSQSVSVL 187
Cdd:COG1245 439 I---IKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAENRGKTAM 510
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
4-191 |
3.02e-12 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 64.18 E-value: 3.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 4 AVQAVSHQYGGHHALDNINLCLKPGLTM-LLGPNGAGKSTLFALITGLQKLTQGSITFDG--------ATLSQSRTSIMA 74
Cdd:PRK11701 8 SVRGLTKLYGPRKGCRDVSFDLYPGEVLgIVGESGSGKTTLLNALSARLAPDAGEVHYRMrdgqlrdlYALSEAERRRLL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 75 KM--GVVFQQST--LDIDLSVKQN-----LSYFASLHGISTASALSHIQGLldELDLtSKLNTKIRNLNGGHRRRVELAR 145
Cdd:PRK11701 88 RTewGFVHQHPRdgLRMQVSAGGNigerlMAVGARHYGDIRATAGDWLERV--EIDA-ARIDDLPTTFSGGMQQRLQIAR 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 521328941 146 CLIHKPSLLLLDEPTVGLDIESRHLILRVVQALAHSQSVSVLWATH 191
Cdd:PRK11701 165 NLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTH 210
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
17-213 |
3.15e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 64.87 E-value: 3.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 17 ALDNINLCL-KPGLTMLLGPNGAGKSTLFALITGLQKLTQGSIT----FDGATLSQSRTSIMAK-------------MGV 78
Cdd:PRK13631 41 ALNNISYTFeKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQvgdiYIGDKKNNHELITNPYskkiknfkelrrrVSM 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 79 VFQ--QSTLDIDlSVKQNLSYFASLHGISTASALSHIQGLLDELDL-TSKLNTKIRNLNGGHRRRVELARCLIHKPSLLL 155
Cdd:PRK13631 121 VFQfpEYQLFKD-TIEKDIMFGPVALGVKKSEAKKLAKFYLNKMGLdDSYLERSPFGLSGGQKRRVAIAGILAIQPEILI 199
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 521328941 156 LDEPTVGLDIESRHLILRVVQAlAHSQSVSVLWATHLFEEV-KHNNNLIVLSKGRVLAH 213
Cdd:PRK13631 200 FDEPTAGLDPKGEHEMMQLILD-AKANNKTVFVITHTMEHVlEVADEVIVMDKGKILKT 257
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
2-230 |
3.88e-12 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 64.11 E-value: 3.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 2 EIAVQAVSHQY--GGHHALDNINLCLKPGLTM-LLGPNGAGKSTLFALITGLQKlTQGSITFDGATLSQSRTSIMAKMGV 78
Cdd:cd03289 2 QMTVKDLTAKYteGGNAVLENISFSISPGQRVgLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQKWRKAFG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 79 VFQQSTLDIDLSVKQNLSYFA-----SLHGISTASAL-SHIQGLLDELDLTSKLNTKIrnLNGGHRRRVELARCLIHKPS 152
Cdd:cd03289 81 VIPQKVFIFSGTFRKNLDPYGkwsdeEIWKVAEEVGLkSVIEQFPGQLDFVLVDGGCV--LSHGHKQLMCLARSVLSKAK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 153 LLLLDEPTVGLDIESRHLILRVV-QALAhsqSVSVLWATHLFEEVKHNNNLIVLSKGRVLAHDQCEALLAK--YHQQDIE 229
Cdd:cd03289 159 ILLLDEPSAHLDPITYQVIRKTLkQAFA---DCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEksHFKQAIS 235
|
.
gi 521328941 230 H 230
Cdd:cd03289 236 P 236
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
33-187 |
7.75e-12 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 64.44 E-value: 7.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 33 LGPNGAGKSTLFALITGLQKLTQGSITFDgatlsqsrtsimAKMGVVFQQSTLDIDLSVKQNLSyfaslhGISTASALSH 112
Cdd:PRK13409 371 VGPNGIGKTTFAKLLAGVLKPDEGEVDPE------------LKISYKPQYIKPDYDGTVEDLLR------SITDDLGSSY 432
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 521328941 113 IQG-LLDELDLTSKLNTKIRNLNGGHRRRVELARCLIHKPSLLLLDEPTVGLDIESRHLILRVVQALAHSQSVSVL 187
Cdd:PRK13409 433 YKSeIIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAEEREATAL 508
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
19-187 |
1.01e-11 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 63.79 E-value: 1.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 19 DNINLCLKPGLTM-LLGPNGAGKSTLFALITGL-QKLTQGSITFDG--ATLSQSRTSIMAKMGVVFQQSTLD---IDLSV 91
Cdd:PRK13549 279 DDVSFSLRRGEILgIAGLVGAGRTELVQCLFGAyPGRWEGEIFIDGkpVKIRNPQQAIAQGIAMVPEDRKRDgivPVMGV 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 92 KQN-----LSYFASLHGISTASALSHIQGLLDELDL-TSKLNTKIRNLNGGHRRRVELARCLIHKPSLLLLDEPTVGLDI 165
Cdd:PRK13549 359 GKNitlaaLDRFTGGSRIDDAAELKTILESIQRLKVkTASPELAIARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDV 438
|
170 180
....*....|....*....|..
gi 521328941 166 ESRHLILRVVQALAhSQSVSVL 187
Cdd:PRK13549 439 GAKYEIYKLINQLV-QQGVAII 459
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
11-178 |
1.27e-11 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 63.50 E-value: 1.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 11 QYGGHHALDNINLCLKPGLT-MLLGPNGAGKSTLFALITG------LQKLT-----QGSitfdGATLSQsrtsIMAKMGV 78
Cdd:PRK10938 269 SYNDRPILHNLSWQVNPGEHwQIVGPNGAGKSTLLSLITGdhpqgySNDLTlfgrrRGS----GETIWD----IKKHIGY 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 79 VfqQSTLDIDLSVKQN-----LS-YFASlhgISTASALSHIQGL-----LDELDLTSKL-NTKIRNLNGGHRRRVELARC 146
Cdd:PRK10938 341 V--SSSLHLDYRVSTSvrnviLSgFFDS---IGIYQAVSDRQQKlaqqwLDILGIDKRTaDAPFHSLSWGQQRLALIVRA 415
|
170 180 190
....*....|....*....|....*....|..
gi 521328941 147 LIHKPSLLLLDEPTVGLDIESRHLILRVVQAL 178
Cdd:PRK10938 416 LVKHPTLLILDEPLQGLDPLNRQLVRRFVDVL 447
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
31-211 |
1.34e-11 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 63.51 E-value: 1.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 31 MLLGPNGAGKSTLFALITGLQKLTQGSITFDGATLS-----QSRTSIMAKMGVVFQQSTLDIDLSVKQNLSYFASLHGIS 105
Cdd:PRK10070 58 VIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAkisdaELREVRRKKIAMVFQSFALMPHMTVLDNTAFGMELAGIN 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 106 TASALSHIQGLLDELDLTSKLNTKIRNLNGGHRRRVELARCLIHKPSLLLLDEPTVGLDIESR-HLILRVVQALAHSQSV 184
Cdd:PRK10070 138 AEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRtEMQDELVKLQAKHQRT 217
|
170 180
....*....|....*....|....*..
gi 521328941 185 SVLWATHLFEEVKHNNNLIVLSKGRVL 211
Cdd:PRK10070 218 IVFISHDLDEAMRIGDRIAIMQNGEVV 244
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
18-191 |
1.69e-11 |
|
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: 60.63 E-value: 1.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 18 LDNINLCLKPGLTMLL-GPNGAGKSTLFALITGLQKLTQGSItfdgatlsqsrtSIMAKMGVVF--QQSTLdIDLSVKQN 94
Cdd:cd03223 17 LKDLSFEIKPGDRLLItGPSGTGKSSLFRALAGLWPWGSGRI------------GMPEGEDLLFlpQRPYL-PLGTLREQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 95 LSYFASlhgistasalshiqglldeldltsklntkiRNLNGGHRRRVELARCLIHKPSLLLLDEPTVGLDIESRHLILRV 174
Cdd:cd03223 84 LIYPWD------------------------------DVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQL 133
|
170 180
....*....|....*....|....
gi 521328941 175 VQAL-------AHSQSvsvLWATH 191
Cdd:cd03223 134 LKELgitvisvGHRPS---LWKFH 154
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
2-158 |
3.32e-11 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 62.51 E-value: 3.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 2 EIAVQAVSHQY----GGHH-ALDNINLCLKPG-LTMLLGPNGAGKSTLFALITGLQKLTQGSITFDGATLS-QSRTSIMA 74
Cdd:COG4615 327 TLELRGVTYRYpgedGDEGfTLGPIDLTIRRGeLVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTaDNREAYRQ 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 75 KMGVVFQqstlDIDLsvkqnlsyFASLHGISTASALSHIQGLLDELDLTSKlnTKIRN-------LNGGHRRRVELARCL 147
Cdd:COG4615 407 LFSAVFS----DFHL--------FDRLLGLDGEADPARARELLERLELDHK--VSVEDgrfsttdLSQGQRKRLALLVAL 472
|
170
....*....|.
gi 521328941 148 IHKPSLLLLDE 158
Cdd:COG4615 473 LEDRPILVFDE 483
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
25-197 |
3.39e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 60.27 E-value: 3.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 25 LKPGLTMLLGPNGAGKSTLFALITGLQKLTQGSITFDGATLSQSRTSIMAKMGvvfQQSTLDIDLSVKQNLSYFASLHGI 104
Cdd:PRK13541 24 LPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKPYCTYIG---HNLGLKLEMTVFENLKFWSEIYNS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 105 STAsalshIQGLLDELDLTSKLNTKIRNLNGGHRRRVELARCLIHKPSLLLLDEPTVGLDIESRHLILRVVQALAHSQSV 184
Cdd:PRK13541 101 AET-----LYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNNLIVMKANSGGI 175
|
170
....*....|...
gi 521328941 185 sVLWATHLFEEVK 197
Cdd:PRK13541 176 -VLLSSHLESSIK 187
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
17-191 |
4.32e-11 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 62.18 E-value: 4.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 17 ALDNINLCLKPGLTM-LLGPNGAGKS-TLFALI-----TG---------LQKLTQGSITFDGATLSQSRTSIMAKMGVVF 80
Cdd:PRK10261 31 AVRNLSFSLQRGETLaIVGESGSGKSvTALALMrlleqAGglvqcdkmlLRRRSRQVIELSEQSAAQMRHVRGADMAMIF 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 81 QQ--STLDIDLSVKQNLSYFASLH-GISTASALSHIQGLLDEL---DLTSKLNTKIRNLNGGHRRRVELARCLIHKPSLL 154
Cdd:PRK10261 111 QEpmTSLNPVFTVGEQIAESIRLHqGASREEAMVEAKRMLDQVripEAQTILSRYPHQLSGGMRQRVMIAMALSCRPAVL 190
|
170 180 190
....*....|....*....|....*....|....*..
gi 521328941 155 LLDEPTVGLDIESRHLILRVVQALAHSQSVSVLWATH 191
Cdd:PRK10261 191 IADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITH 227
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
18-208 |
4.94e-11 |
|
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: 60.42 E-value: 4.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 18 LDNINLCLKPG-LTMLLGPNGAGKSTLFALITGLQKLTQGSITF-----DGATLSQSRTSIMAKMGVVFQQSTLdIDLSV 91
Cdd:cd03290 17 LSNINIRIPTGqLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWsnkneSEPSFEATRSRNRYSVAYAAQKPWL-LNATV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 92 KQNLSyFASLHGISTASALSHIQGLLDELDL-----TSKLNTKIRNLNGGHRRRVELARCLIHKPSLLLLDEPTVGLDIE 166
Cdd:cd03290 96 EENIT-FGSPFNKQRYKAVTDACSLQPDIDLlpfgdQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIH 174
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 521328941 167 -SRHLILRVVQALAHSQSVSVLWATHLFEEVKHNNNLIVLSKG 208
Cdd:cd03290 175 lSDHLMQEGILKFLQDDKRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
32-210 |
6.64e-11 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 61.80 E-value: 6.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 32 LLGPNGAGKSTLFALITGLQKLTQGsitfdgaTLSQSRTSIMAkmgvVFQQSTLD-IDLSVKQNLSYFASLHGISTASAL 110
Cdd:PLN03073 540 MVGPNGIGKSTILKLISGELQPSSG-------TVFRSAKVRMA----VFSQHHVDgLDLSSNPLLYMMRCFPGVPEQKLR 608
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 111 SHiqglLDELDLTSKLNTK-IRNLNGGHRRRVELARCLIHKPSLLLLDEPtvgldieSRHLILRVVQALAhsQSVSVLWA 189
Cdd:PLN03073 609 AH----LGSFGVTGNLALQpMYTLSGGQKSRVAFAKITFKKPHILLLDEP-------SNHLDLDAVEALI--QGLVLFQG 675
|
170 180
....*....|....*....|....*....
gi 521328941 190 THLFeeVKHNNNLI--------VLSKGRV 210
Cdd:PLN03073 676 GVLM--VSHDEHLIsgsvdelwVVSEGKV 702
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
17-191 |
6.91e-11 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 60.89 E-value: 6.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 17 ALDNINLCLKPGLTM-LLGPNGAGKS-TLFALITGLQK--LTQGSITFDGATLSQSRTSIMAKM-----GVVFQQ--STL 85
Cdd:PRK09473 31 AVNDLNFSLRAGETLgIVGESGSGKSqTAFALMGLLAAngRIGGSATFNGREILNLPEKELNKLraeqiSMIFQDpmTSL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 86 DIDLSVKQNLSYFASLH-GISTASALSHIQGLLDELDLTS---KLNTKIRNLNGGHRRRVELARCLIHKPSLLLLDEPTV 161
Cdd:PRK09473 111 NPYMRVGEQLMEVLMLHkGMSKAEAFEESVRMLDAVKMPEarkRMKMYPHEFSGGMRQRVMIAMALLCRPKLLIADEPTT 190
|
170 180 190
....*....|....*....|....*....|
gi 521328941 162 GLDIESRHLILRVVQALAHSQSVSVLWATH 191
Cdd:PRK09473 191 ALDVTVQAQIMTLLNELKREFNTAIIMITH 220
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
4-220 |
1.48e-10 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 59.42 E-value: 1.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 4 AVQAVSHQYGGHHALDNINLCLKPG-LTMLLGPNGAGKSTLFALITGLQKLTQGSITFDGATLSQSRTSIMA-KMGVVFQ 81
Cdd:PRK10575 13 ALRNVSFRVPGRTLLHPLSLTFPAGkVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFArKVAYLPQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 82 QSTLDIDLSVKQNLS-----YFASLhGISTASALSHIQGLLDELDLTSKLNTKIRNLNGGHRRRVELARCLIHKPSLLLL 156
Cdd:PRK10575 93 QLPAAEGMTVRELVAigrypWHGAL-GRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLL 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 521328941 157 DEPTVGLDIESRHLILRVVQALAHSQSVSVLWATH-LFEEVKHNNNLIVLSKGRVLAHDQCEALL 220
Cdd:PRK10575 172 DEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHdINMAARYCDYLVALRGGEMIAQGTPAELM 236
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
37-210 |
2.19e-10 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 59.80 E-value: 2.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 37 GAGKSTLFALITGLQKLTQGSITFDGATLSQSRTSIMAKMGVVF-----QQSTLDIDLSVKQNLSYFASLhgisTASALS 111
Cdd:PRK09700 299 GSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDAVKKGMAYitesrRDNGFFPNFSIAQNMAISRSL----KDGGYK 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 112 HIQGLLDELD--------------LTSKLNTKIRNLNGGHRRRVELARCLIHKPSLLLLDEPTVGLDIESRHLILRVVQA 177
Cdd:PRK09700 375 GAMGLFHEVDeqrtaenqrellalKCHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQ 454
|
170 180 190
....*....|....*....|....*....|...
gi 521328941 178 LAHSQSVSVLWATHLFEEVKHNNNLIVLSKGRV 210
Cdd:PRK09700 455 LADDGKVILMVSSELPEIITVCDRIAVFCEGRL 487
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
18-167 |
2.61e-10 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 59.80 E-value: 2.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 18 LDNINLCLKPGLTM-LLGPNGAGKSTLFALITGLQKLTQGSITFDG----ATLSQSRTSI-MAKMGVV------FQQSTL 85
Cdd:PRK10636 17 LDNATATINPGQKVgLVGKNGCGKSTLLALLKNEISADGGSYTFPGnwqlAWVNQETPALpQPALEYVidgdreYRQLEA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 86 DIDLSVKQNLSY-FASLHGI----------STASALSHIQGLLDEldltsKLNTKIRNLNGGHRRRVELARCLIHKPSLL 154
Cdd:PRK10636 97 QLHDANERNDGHaIATIHGKldaidawtirSRAASLLHGLGFSNE-----QLERPVSDFSGGWRMRLNLAQALICRSDLL 171
|
170
....*....|...
gi 521328941 155 LLDEPTVGLDIES 167
Cdd:PRK10636 172 LLDEPTNHLDLDA 184
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
12-170 |
3.02e-10 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 59.42 E-value: 3.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 12 YGGHHALDNINLCLKPG-LTMLLGPNGAGKSTLFALITGL--QKLTQGSITFDGATLSQSRTSIMAKMGVVF--QQSTLD 86
Cdd:NF040905 11 FPGVKALDDVNLSVREGeIHALCGENGAGKSTLMKVLSGVypHGSYEGEILFDGEVCRFKDIRDSEALGIVIihQELALI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 87 IDLSVKQNLsyF-----ASLHGISTASALSHIQGLLDELDLTSKLNTKIRNLNGGHRRRVELARCLIHKPSLLLLDEPTV 161
Cdd:NF040905 91 PYLSIAENI--FlgnerAKRGVIDWNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLILDEPTA 168
|
170
....*....|
gi 521328941 162 GL-DIESRHL 170
Cdd:NF040905 169 ALnEEDSAAL 178
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
56-206 |
4.96e-10 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 59.27 E-value: 4.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 56 GSITFDGATLSQSRTSIMAKMGVVFQQSTLDIDLSVKQNLSYF---ASLHGISTASALSHIQGLLDELdlTSKLNTKI-- 130
Cdd:PTZ00265 1277 GKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGkedATREDVKRACKFAAIDEFIESL--PNKYDTNVgp 1354
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 521328941 131 --RNLNGGHRRRVELARCLIHKPSLLLLDEPTVGLDIESRHLILRVVQALAHSQSVSVLWATHLFEEVKHNNNLIVLS 206
Cdd:PTZ00265 1355 ygKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASIKRSDKIVVFN 1432
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
16-211 |
6.31e-10 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 58.71 E-value: 6.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 16 HALDNINLCLKPGLTM-LLGPNGAGKSTLFALITGLQKLTQGSITFDGA---TLSQSR-TSIMAKMGVVFQQ--STLDID 88
Cdd:PRK10261 338 HAVEKVSFDLWPGETLsLVGESGSGKSTTGRALLRLVESQGGEIIFNGQridTLSPGKlQALRRDIQFIFQDpyASLDPR 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 89 LSVKQNLSYFASLHGI-STASALSHIQGLLDELDLTSKLNTKI-RNLNGGHRRRVELARCLIHKPSLLLLDEPTVGLDIE 166
Cdd:PRK10261 418 QTVGDSIMEPLRVHGLlPGKAAAARVAWLLERVGLLPEHAWRYpHEFSGGQRQRICIARALALNPKVIIADEAVSALDVS 497
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 521328941 167 SRHLILRVVQALAHSQSVSVLWATH---LFEEVKHnnNLIVLSKGRVL 211
Cdd:PRK10261 498 IRGQIINLLLDLQRDFGIAYLFISHdmaVVERISH--RVAVMYLGQIV 543
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
18-212 |
9.03e-10 |
|
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: 58.30 E-value: 9.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 18 LDNINLCLKPGLTM-LLGPNGAGKSTLFALITGL-QKLTQGSITFDGATLS--QSRTSIMAKMGVVFQQSTLD---IDLS 90
Cdd:TIGR02633 276 VDDVSFSLRRGEILgVAGLVGAGRTELVQALFGAyPGKFEGNVFINGKPVDirNPAQAIRAGIAMVPEDRKRHgivPILG 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 91 VKQN-----LSYFASLHGISTASALSHIQGLLDELDL-TSKLNTKIRNLNGGHRRRVELARCLIHKPSLLLLDEPTVGLD 164
Cdd:TIGR02633 356 VGKNitlsvLKSFCFKMRIDAAAELQIIGSAIQRLKVkTASPFLPIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVD 435
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 521328941 165 IESRHLILRVVQALAHSQSVSVLWATHLFEEVKHNNNLIVLSKGRVLA 212
Cdd:TIGR02633 436 VGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGKLKG 483
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
5-167 |
9.14e-10 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 57.98 E-value: 9.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 5 VQAVSHQYGGHHALDNINLCLKPGLTM-LLGPNGAGKSTLFALITGLQKLTQGSITFdgatlsqsrtSIMAKMGVVFQQS 83
Cdd:PRK15064 322 VENLTKGFDNGPLFKNLNLLLEAGERLaIIGENGVGKTTLLRTLVGELEPDSGTVKW----------SENANIGYYAQDH 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 84 T--LDIDLSVKQNLSYFASLHGISTAsalshIQGLLDELDLTSK-LNTKIRNLNGGHRRRVELARCLIHKPSLLLLDEPT 160
Cdd:PRK15064 392 AydFENDLTLFDWMSQWRQEGDDEQA-----VRGTLGRLLFSQDdIKKSVKVLSGGEKGRMLFGKLMMQKPNVLVMDEPT 466
|
....*..
gi 521328941 161 VGLDIES 167
Cdd:PRK15064 467 NHMDMES 473
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
2-231 |
9.32e-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: 58.38 E-value: 9.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 2 EIAVQAVSHQY--GGHHALDNINLCLKPGLTM-LLGPNGAGKSTLFALITGLQKlTQGSITFDGA-----TLSQSRTSim 73
Cdd:TIGR01271 1217 QMDVQGLTAKYteAGRAVLQDLSFSVEGGQRVgLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVswnsvTLQTWRKA-- 1293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 74 akMGVVfQQSTLDIDLSVKQNLSYFASLHGistasalSHIQGLLDELDLTS-------KLNTKIRN----LNGGHRRRVE 142
Cdd:TIGR01271 1294 --FGVI-PQKVFIFSGTFRKNLDPYEQWSD-------EEIWKVAEEVGLKSvieqfpdKLDFVLVDggyvLSNGHKQLMC 1363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 143 LARCLIHKPSLLLLDEPTVGLDIESRHLILRvvqALAHSQS-VSVLWATHLFEEVKHNNNLIVLSKGRVLAHDQCEALL- 220
Cdd:TIGR01271 1364 LARSILSKAKILLLDEPSAHLDPVTLQIIRK---TLKQSFSnCTVILSEHRVEALLECQQFLVIEGSSVKQYDSIQKLLn 1440
|
250
....*....|..
gi 521328941 221 -AKYHQQDIEHL 231
Cdd:TIGR01271 1441 eTSLFKQAMSAA 1452
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
16-222 |
9.49e-10 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 57.67 E-value: 9.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 16 HALDNINLCLKPGLTM-LLGPNGAGKSTLFALITGLQKLTQGSITFDG--------ATLSQSRTSIMakmgVVFQQStld 86
Cdd:PRK11308 29 KALDGVSFTLERGKTLaVVGESGCGKSTLARLLTMIETPTGGELYYQGqdllkadpEAQKLLRQKIQ----IVFQNP--- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 87 idlsvkqnlsyFASLHGISTASALshiqglLDE-LDLTSKLNTKIRN-----------------------LNGGHRRRVE 142
Cdd:PRK11308 102 -----------YGSLNPRKKVGQI------LEEpLLINTSLSAAERRekalammakvglrpehydryphmFSGGQRQRIA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 143 LARCLIHKPSLLLLDEPTVGLDIESRHLILRVVQALAHSQSVSVLWATHLFEEVKH-NNNLIVLSKGRVLAHDQCEALLA 221
Cdd:PRK11308 165 IARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHiADEVMVMYLGRCVEKGTKEQIFN 244
|
.
gi 521328941 222 K 222
Cdd:PRK11308 245 N 245
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
20-206 |
1.04e-09 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 58.12 E-value: 1.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 20 NINLCLKPGLT-MLLGPNGAGKSTLFALITGLQKLTQGSITFDGatlSQSRTSI-----MAKMGVVFQQSTLdIDLSVKQ 93
Cdd:PTZ00265 403 DLNFTLTEGKTyAFVGESGCGKSTILKLIERLYDPTEGDIIIND---SHNLKDInlkwwRSKIGVVSQDPLL-FSNSIKN 478
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 94 NLSYfaSLHGISTASALSH----------------------IQGLLDEL------------------------------- 120
Cdd:PTZ00265 479 NIKY--SLYSLKDLEALSNyynedgndsqenknkrnscrakCAGDLNDMsnttdsneliemrknyqtikdsevvdvskkv 556
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 121 ---DLTSKLNTKIRNL--------NGGHRRRVELARCLIHKPSLLLLDEPTVGLDIESRHLILRVVQALAHSQSVSVLWA 189
Cdd:PTZ00265 557 lihDFVSALPDKYETLvgsnasklSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIII 636
|
250
....*....|....*..
gi 521328941 190 THLFEEVKHNNNLIVLS 206
Cdd:PTZ00265 637 AHRLSTIRYANTIFVLS 653
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
32-171 |
1.26e-09 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 57.65 E-value: 1.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 32 LLGPNGAGKSTLFALITGLQKLTQGSI----TFDGATLSQSRtsimakmgvvfqqSTLDIDLSVKQNLS---YFASLHGI 104
Cdd:PRK11147 350 LIGPNGCGKTTLLKLMLGQLQADSGRIhcgtKLEVAYFDQHR-------------AELDPEKTVMDNLAegkQEVMVNGR 416
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 521328941 105 StasalSHIQGLL-DELDLTSKLNTKIRNLNGGHRRRVELARCLIhKPS-LLLLDEPTVGLDIESRHLI 171
Cdd:PRK11147 417 P-----RHVLGYLqDFLFHPKRAMTPVKALSGGERNRLLLARLFL-KPSnLLILDEPTNDLDVETLELL 479
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
18-178 |
1.34e-09 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 56.72 E-value: 1.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 18 LDNINLCLKPG-LTMLLGPNGAGKSTLFALITGLQ--KLTQGSITFDGATLSQSRTSIMAKMGV--VFQqstldidlsvk 92
Cdd:PRK09580 17 LRGLNLEVRPGeVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLELSPEDRAGEGIfmAFQ----------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 93 qnlsYFASLHGIST----ASALSHI-----QGLLDELDLTSKLNTKIRNLN---------------GGHRRRVELARCLI 148
Cdd:PRK09580 86 ----YPVEIPGVSNqfflQTALNAVrsyrgQEPLDRFDFQDLMEEKIALLKmpedlltrsvnvgfsGGEKKRNDILQMAV 161
|
170 180 190
....*....|....*....|....*....|
gi 521328941 149 HKPSLLLLDEPTVGLDIESRHLILRVVQAL 178
Cdd:PRK09580 162 LEPELCILDESDSGLDIDALKIVADGVNSL 191
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
18-210 |
1.65e-09 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 57.48 E-value: 1.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 18 LDNINLCLKPG-LTMLLGPNGAGKSTLFALITGLQKLTQGSItfdgatlsQSRTSImakmGVVFQQSTLdIDLSVKQNLS 96
Cdd:PTZ00243 676 LRDVSVSVPRGkLTVVLGATGSGKSTLLQSLLSQFEISEGRV--------WAERSI----AYVPQQAWI-MNATVRGNIL 742
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 97 YFASLHGISTASALSHIQGLLDELDLTSKLNTKIR----NLNGGHRRRVELARCLIHKPSLLLLDEPTVGLDIesrHLIL 172
Cdd:PTZ00243 743 FFDEEDAARLADAVRVSQLEADLAQLGGGLETEIGekgvNLSGGQKARVSLARAVYANRDVYLLDDPLSALDA---HVGE 819
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 521328941 173 RVVQ-----ALAHSQSVsvlWATHLFEEVKHNNNLIVLSKGRV 210
Cdd:PTZ00243 820 RVVEecflgALAGKTRV---LATHQVHVVPRADYVVALGDGRV 859
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
3-164 |
1.94e-09 |
|
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: 57.12 E-value: 1.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 3 IAVQAVSHQY-----GGHHALDNINLCLKPG-LTMLLGPNGAGKSTLFALITGLQKLTQGSITF----DGATLSQSRTSI 72
Cdd:TIGR03269 280 IKVRNVSKRYisvdrGVVKAVDNVSLEVKEGeIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdEWVDMTKPGPDG 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 73 MAK----MGVVFQQSTLDIDLSVKQNLS---------YFASLHGISTASALShiqglLDELDLTSKLNTKIRNLNGGHRR 139
Cdd:TIGR03269 360 RGRakryIGILHQEYDLYPHRTVLDNLTeaiglelpdELARMKAVITLKMVG-----FDEEKAEEILDKYPDELSEGERH 434
|
170 180
....*....|....*....|....*
gi 521328941 140 RVELARCLIHKPSLLLLDEPTVGLD 164
Cdd:TIGR03269 435 RVALAQVLIKEPRIVILDEPTGTMD 459
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
26-205 |
2.16e-09 |
|
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: 56.22 E-value: 2.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 26 KPG-LTMLLGPNGAGKSTLFALITGLQKLTQGSIT-----------FDGATLSQSRTSIM-AKMGVVFQQSTLD-IDLSV 91
Cdd:cd03236 24 REGqVLGLVGPNGIGKSTALKILAGKLKPNLGKFDdppdwdeildeFRGSELQNYFTKLLeGDVKVIVKPQYVDlIPKAV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 92 KQNLSYFaslhgISTASALSHIQGLLDELDLTSKLNTKIRNLNGGHRRRVELARCLIHKPSLLLLDEPTVGLDIESRHLI 171
Cdd:cd03236 104 KGKVGEL-----LKKKDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRLNA 178
|
170 180 190
....*....|....*....|....*....|....*
gi 521328941 172 LRVVQALA-HSQSVSVlwathlfeeVKHnnNLIVL 205
Cdd:cd03236 179 ARLIRELAeDDNYVLV---------VEH--DLAVL 202
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
13-221 |
2.29e-09 |
|
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: 57.00 E-value: 2.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 13 GGHHALDNINLCLKPGLTM-LLGPNGAGKStLFAL-ITGL----QKLTQGSITFDGATLSQSRTSIM-----AKMGVVFQ 81
Cdd:COG4172 21 GTVEAVKGVSFDIAAGETLaLVGESGSGKS-VTALsILRLlpdpAAHPSGSILFDGQDLLGLSERELrrirgNRIAMIFQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 82 Q--STLDIDLSVKQNLSYFASLH-GISTASALSHIQGLLDEldltsklnTKIRN-----------LNGGHRRRVELARCL 147
Cdd:COG4172 100 EpmTSLNPLHTIGKQIAEVLRLHrGLSGAAARARALELLER--------VGIPDperrldayphqLSGGQRQRVMIAMAL 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 521328941 148 IHKPSLLLLDEPTVGLDIESRHLILRVVQALAHSQSVSVLWATHLFEEVKH-NNNLIVLSKGRVLAHDQCEALLA 221
Cdd:COG4172 172 ANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRfADRVAVMRQGEIVEQGPTAELFA 246
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
2-222 |
2.49e-09 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 56.07 E-value: 2.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 2 EIAVQAVSHQYGGH--HALDNINLCLKPGLTM-LLGPNGAGKSTLFALITGLQKLTQGSITFDGATLSQ-------SRTS 71
Cdd:cd03288 19 EIKIHDLCVRYENNlkPVLKHVKAYIKPGQKVgICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKlplhtlrSRLS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 72 IMAKMGVVFQqSTLDIDLSVKQNLSYFASLHGISTASALSHIQGLLDELDltSKLNTKIRNLNGGHRRRVELARCLIHKP 151
Cdd:cd03288 99 IILQDPILFS-GSIRFNLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLD--AVVTEGGENFSVGQRQLFCLARAFVRKS 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 521328941 152 SLLLLDEPTVGLDIESRHLILRVVQ-ALAHSQSVSVlwaTHLFEEVKHNNNLIVLSKGRVLAHDQCEALLAK 222
Cdd:cd03288 176 SILIMDEATASIDMATENILQKVVMtAFADRTVVTI---AHRVSTILDADLVLVLSRGILVECDTPENLLAQ 244
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
16-224 |
3.09e-09 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 56.07 E-value: 3.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 16 HALDNINLCLKPG-LTMLLGPNGAGKSTLFALITGLQK----LTQGSITFDGATL----SQSRTSIMAK-MGVVFQ--QS 83
Cdd:COG4170 21 KAVDRVSLTLNEGeIRGLVGESGSGKSLIAKAICGITKdnwhVTADRFRWNGIDLlklsPRERRKIIGReIAMIFQepSS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 84 TLD----IDLSVKQNL------SYFASLHG--ISTASALSHIQGLLDELDLtskLNTKIRNLNGGHRRRVELARCLIHKP 151
Cdd:COG4170 101 CLDpsakIGDQLIEAIpswtfkGKWWQRFKwrKKRAIELLHRVGIKDHKDI---MNSYPHELTEGECQKVMIAMAIANQP 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 521328941 152 SLLLLDEPTVGLDIESRHLILRVVQALAHSQSVSVLWATHLFEEVKHN-NNLIVLSKGRVLAHDQCEALLAKYH 224
Cdd:COG4170 178 RLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWaDTITVLYCGQTVESGPTEQILKSPH 251
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
12-221 |
3.20e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 55.87 E-value: 3.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 12 YGGHHALDNINLCLKP-GLTMLLGPNGAGKSTLFALITGLQKLTQGsITFDGATLSQSRT--------SIMAKMGVVFQQ 82
Cdd:PRK14271 31 FAGKTVLDQVSMGFPArAVTSLMGPTGSGKTTFLRTLNRMNDKVSG-YRYSGDVLLGGRSifnyrdvlEFRRRVGMLFQR 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 83 STlDIDLSVKQNLSYFASLHGISTASALSHI-QGLLDELDLTSKLNTKIRN----LNGGHRRRVELARCLIHKPSLLLLD 157
Cdd:PRK14271 110 PN-PFPMSIMDNVLAGVRAHKLVPRKEFRGVaQARLTEVGLWDAVKDRLSDspfrLSGGQQQLLCLARTLAVNPEVLLLD 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 521328941 158 EPTVGLDIESRHLILRVVQALAhsQSVSVLWATH-LFEEVKHNNNLIVLSKGRVLAHDQCEALLA 221
Cdd:PRK14271 189 EPTSALDPTTTEKIEEFIRSLA--DRLTVIIVTHnLAQAARISDRAALFFDGRLVEEGPTEQLFS 251
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
3-168 |
4.81e-09 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 55.95 E-value: 4.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 3 IAVQAVSHQYGGHHALDNINLCLKPGLTM-LLGPNGAGKSTLFALITGLQKLTQGsitfdgatlsqsrtsimakmgvvfq 81
Cdd:PRK10636 313 LKMEKVSAGYGDRIILDSIKLNLVPGSRIgLLGRNGAGKSTLIKLLAGELAPVSG------------------------- 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 82 qstlDIDLSVKQNLSYFASlHGI----STASALSHI---------QGLLDELD----LTSKLNTKIRNLNGGHRRRVELA 144
Cdd:PRK10636 368 ----EIGLAKGIKLGYFAQ-HQLeflrADESPLQHLarlapqeleQKLRDYLGgfgfQGDKVTEETRRFSGGEKARLVLA 442
|
170 180
....*....|....*....|....
gi 521328941 145 RCLIHKPSLLLLDEPTVGLDIESR 168
Cdd:PRK10636 443 LIVWQRPNLLLLDEPTNHLDLDMR 466
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
17-198 |
8.92e-09 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 54.71 E-value: 8.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 17 ALDNINLCLKPGLTM-LLGPNGAGKSTLFALITGLQKLTQGSITFDGATLSQ----SRTSIMAKMGVVFQQ--STLDIDL 89
Cdd:PRK15079 36 AVDGVTLRLYEGETLgVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGmkddEWRAVRSDIQMIFQDplASLNPRM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 90 SVKQNLS-----YFASLhgiSTASALSHIQGLLDELDLTSKL-NTKIRNLNGGHRRRVELARCLIHKPSLLLLDEPTVGL 163
Cdd:PRK15079 116 TIGEIIAeplrtYHPKL---SRQEVKDRVKAMMLKVGLLPNLiNRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSAL 192
|
170 180 190
....*....|....*....|....*....|....*
gi 521328941 164 DIESRHLILRVVQALAHSQSVSVLWATHLFEEVKH 198
Cdd:PRK15079 193 DVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKH 227
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
17-221 |
2.17e-08 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 53.25 E-value: 2.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 17 ALDNINLCLKPGLTM-LLGPNGAGKSTLFALITGLQKLTQGSITFDGATLSQSRTSIMA-KMGVVFQQST---------- 84
Cdd:PRK15112 28 AVKPLSFTLREGQTLaIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSqRIRMIFQDPStslnprqris 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 85 --LDIDLSVKQNLSYFASLHGISTasALSHIqGLLDEldltsKLNTKIRNLNGGHRRRVELARCLIHKPSLLLLDEPTVG 162
Cdd:PRK15112 108 qiLDFPLRLNTDLEPEQREKQIIE--TLRQV-GLLPD-----HASYYPHMLAPGQKQRLGLARALILRPKVIIADEALAS 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 163 LDIESRHLILRVVQALAHSQSVSVLWATHLFEEVKH-NNNLIVLSKGRVLAHDQCEALLA 221
Cdd:PRK15112 180 LDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHiSDQVLVMHQGEVVERGSTADVLA 239
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
32-222 |
3.06e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 53.97 E-value: 3.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 32 LLGPNGAGKSTLFALITGLQKLTQGSITFDGATLSQSRTSIMAKMGVVFQQSTLDIDLSVKQNLSYFASLHGISTASAL- 110
Cdd:PLN03130 1270 IVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSGTVRFNLDPFNEHNDADLWESLe 1349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 111 -SHIQGLL--DELDLTSKLNTKIRNLNGGHRRRVELARCLIHKPSLLLLDEPTVGLDIESRHLILRVVQalAHSQSVSVL 187
Cdd:PLN03130 1350 rAHLKDVIrrNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDALIQKTIR--EEFKSCTML 1427
|
170 180 190
....*....|....*....|....*....|....*
gi 521328941 188 WATHLFEEVKHNNNLIVLSKGRVLAHDQCEALLAK 222
Cdd:PLN03130 1428 IIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLSN 1462
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
37-210 |
4.78e-08 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 52.81 E-value: 4.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 37 GAGKSTLFALITGLQKLTQGSITFDGATLSQSRT--SIMAKMGVVFQQ-------STLDIDL-SVKQNL-SYFASLHGIS 105
Cdd:PRK10982 284 GAKRTDIVETLFGIREKSAGTITLHGKKINNHNAneAINHGFALVTEErrstgiyAYLDIGFnSLISNIrNYKNKVGLLD 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 106 TASALSHIQGLLDELDL-TSKLNTKIRNLNGGHRRRVELARCLIHKPSLLLLDEPTVGLDIESRHLILRVVQALAHSQSV 184
Cdd:PRK10982 364 NSRMKSDTQWVIDSMRVkTPGHRTQIGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKG 443
|
170 180
....*....|....*....|....*.
gi 521328941 185 SVLWATHLFEEVKHNNNLIVLSKGRV 210
Cdd:PRK10982 444 IIIISSEMPELLGITDRILVMSNGLV 469
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
26-222 |
6.31e-08 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 53.03 E-value: 6.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 26 KPGLTMLLGPNGAGKSTLF-ALITGLQKLtQGSITFDGAtlsqsrtsimakMGVVFQQSTLDIDlSVKQNLSYFASLHGI 104
Cdd:TIGR00957 663 EGALVAVVGQVGCGKSSLLsALLAEMDKV-EGHVHMKGS------------VAYVPQQAWIQND-SLRENILFGKALNEK 728
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 105 STASALSHIQGLLDELDLTSKLNTKIR----NLNGGHRRRVELARCLIHKPSLLLLDEPTVGLDIE-SRHLILRVVQALA 179
Cdd:TIGR00957 729 YYQQVLEACALLPDLEILPSGDRTEIGekgvNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHvGKHIFEHVIGPEG 808
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 521328941 180 HSQSVSVLWATHLFEEVKHNNNLIVLSKGRVLAHDQCEALLAK 222
Cdd:TIGR00957 809 VLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQR 851
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
116-205 |
1.79e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 51.35 E-value: 1.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 116 LLDELDLTSKLNTKIRNLNGGHRRRVELARCLIHKPSLLLLDEPTVGLDIESRHLILRVVQALAHSQSVSVlwathlfee 195
Cdd:PRK13409 196 VVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRQRLNVARLIRELAEGKYVLV--------- 266
|
90
....*....|
gi 521328941 196 VKHnnNLIVL 205
Cdd:PRK13409 267 VEH--DLAVL 274
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
25-211 |
2.24e-07 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 51.39 E-value: 2.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 25 LKPG-LTMLLGPNGAGKSTLFALITGlqKL-----TQGSITFDGATLSQsrtSIMAKMGVVFQQSTLDI-DLSVKQNLSY 97
Cdd:PLN03140 188 IKPSrMTLLLGPPSSGKTTLLLALAG--KLdpslkVSGEITYNGYRLNE---FVPRKTSAYISQNDVHVgVMTVKETLDF 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 98 FASLHGISTASAL-------------------------SHIQGLLDEL--DLTSKL------------NTKIRNLNGGHR 138
Cdd:PLN03140 263 SARCQGVGTRYDLlselarrekdagifpeaevdlfmkaTAMEGVKSSLitDYTLKIlgldickdtivgDEMIRGISGGQK 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 139 RRVELARCLIHKPSLLLLDEPTVGLDIESRHLILRVVQALAHSQSVSVLWAT--------HLFEEVkhnnnlIVLSKGRV 210
Cdd:PLN03140 343 KRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQQIVHLTEATVLMSLlqpapetfDLFDDI------ILLSEGQI 416
|
.
gi 521328941 211 L 211
Cdd:PLN03140 417 V 417
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
2-158 |
2.33e-07 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 50.74 E-value: 2.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 2 EIAVQAVSHQYG-GHHALDNINLCLKPG-LTMLLGPNGAGKSTLFALITGLQKLTQGSITFDGATLS-QSRTSIMAKMGV 78
Cdd:PRK10522 322 TLELRNVTFAYQdNGFSVGPINLTIKRGeLLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTaEQPEDYRKLFSA 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 79 VFQqstlDIDLsvkqnlsyFASL---HGISTASALshIQGLLDELDLTSKL---NTKIRNLN--GGHRRRVELARCLIHK 150
Cdd:PRK10522 402 VFT----DFHL--------FDQLlgpEGKPANPAL--VEKWLERLKMAHKLeleDGRISNLKlsKGQKKRLALLLALAEE 467
|
....*...
gi 521328941 151 PSLLLLDE 158
Cdd:PRK10522 468 RDILLLDE 475
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
17-211 |
2.89e-07 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 50.13 E-value: 2.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 17 ALDNINLCLKPGLTM-LLGPNGAGKSTLFALITGL----QKLTQGSITFDGATL-----SQSRTSIMAKMGVVFQqstld 86
Cdd:PRK11022 22 AVDRISYSVKQGEVVgIVGESGSGKSVSSLAIMGLidypGRVMAEKLEFNGQDLqriseKERRNLVGAEVAMIFQ----- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 87 iDLSVKQNLSYFAslhGISTASALSHIQG------------LLDEL---DLTSKLNTKIRNLNGGHRRRVELARCLIHKP 151
Cdd:PRK11022 97 -DPMTSLNPCYTV---GFQIMEAIKVHQGgnkktrrqraidLLNQVgipDPASRLDVYPHQLSGGMSQRVMIAMAIACRP 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 521328941 152 SLLLLDEPTVGLDIESRHLILRVVQALAHSQSVSVLWATH---LFEEVKHnnNLIVLSKGRVL 211
Cdd:PRK11022 173 KLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHdlaLVAEAAH--KIIVMYAGQVV 233
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
26-176 |
3.07e-07 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 51.00 E-value: 3.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 26 KPG-LTMLLGPNGAGKSTLFALITGLQK--LTQGSITFDGATLSQSrtsIMAKMGVVFQQStlDI---DLSVKQNLSYFA 99
Cdd:PLN03140 904 RPGvLTALMGVSGAGKTTLMDVLAGRKTggYIEGDIRISGFPKKQE---TFARISGYCEQN--DIhspQVTVRESLIYSA 978
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 100 SLH---GISTASALSHIQGLLDELDLTSkLNTKIRNLNG------GHRRRVELARCLIHKPSLLLLDEPTVGLDIESRHL 170
Cdd:PLN03140 979 FLRlpkEVSKEEKMMFVDEVMELVELDN-LKDAIVGLPGvtglstEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAI 1057
|
....*.
gi 521328941 171 ILRVVQ 176
Cdd:PLN03140 1058 VMRTVR 1063
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
18-208 |
3.33e-07 |
|
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: 49.86 E-value: 3.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 18 LDNINLCLKPG-LTMLLGPNGAGKSTLFALITGLQKLTQGSITFDGATLSQSRTS-IMAKmgvvfqqstldidlSVKQNL 95
Cdd:cd03291 53 LKNINLKIEKGeMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGRISFSSQFSwIMPG--------------TIKENI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 96 SYFASLHGISTASALSHIQGLLDELDLTSKLNTKIR----NLNGGHRRRVELARCLIHKPSLLLLDEPTVGLDIESRHLI 171
Cdd:cd03291 119 IFGVSYDEYRYKSVVKACQLEEDITKFPEKDNTVLGeggiTLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEI 198
|
170 180 190
....*....|....*....|....*....|....*....
gi 521328941 172 LR--VVQALAHSQSVSVlwaTHLFEEVKHNNNLIVLSKG 208
Cdd:cd03291 199 FEscVCKLMANKTRILV---TSKMEHLKKADKILILHEG 234
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
7-193 |
3.51e-07 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 48.72 E-value: 3.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 7 AVSHQYGGHHALDNINLCLKPGLTMLLGPNGAGKSTLFALITGLQKLTQGSITFDGATLSQSRTSImakmgvvfqqstld 86
Cdd:cd03222 5 DCVKRYGVFFLLVELGVVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITPVYKPQYI-------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 87 idlsvkqnlsyfaslhgistasalshiqglldeldltsklntkirNLNGGHRRRVELARCLIHKPSLLLLDEPTVGLDIE 166
Cdd:cd03222 71 ---------------------------------------------DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIE 105
|
170 180
....*....|....*....|....*..
gi 521328941 167 SRHLILRVVQALAHSQSVSVLWATHLF 193
Cdd:cd03222 106 QRLNAARAIRRLSEEGKKTALVVEHDL 132
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
81-209 |
6.58e-07 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 49.86 E-value: 6.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 81 QQSTLDIDLSVKQNLSYFASLHGISTASALSHIQGLLDELDLTSKLNTK-IRNLNGGHRRRVELARCLIHKPSLLLLDEP 159
Cdd:PLN03073 292 NKDGVDKDAVSQRLEEIYKRLELIDAYTAEARAASILAGLSFTPEMQVKaTKTFSGGWRMRIALARALFIEPDLLLLDEP 371
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 521328941 160 TVGLDIEsrhlilrvvqalahsqsvSVLW-ATHLfeeVKHNNNLIVLSKGR 209
Cdd:PLN03073 372 TNHLDLH------------------AVLWlETYL---LKWPKTFIVVSHAR 401
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
116-179 |
1.16e-06 |
|
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: 48.63 E-value: 1.16e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 521328941 116 LLDELDLTSKLNTKIRNLNGGHRRRVELARCLIHKPSLLLLDEPTVGLDIESRHLILRVVQALA 179
Cdd:COG1245 196 LAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIYQRLNVARLIRELA 259
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
18-208 |
3.07e-06 |
|
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: 47.98 E-value: 3.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 18 LDNINLCLKPG-LTMLLGPNGAGKSTLFALITGLQKLTQGSITFDGATLSQSRTS-IMAKmgvvfqqstldidlSVKQNL 95
Cdd:TIGR01271 442 LKNISFKLEKGqLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGRISFSPQTSwIMPG--------------TIKDNI 507
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 96 SYFASLHGISTASALSHIQGLLDELDLTSKLNTKIRN----LNGGHRRRVELARCLIHKPSLLLLDEPTVGLDIESRHLI 171
Cdd:TIGR01271 508 IFGLSYDEYRYTSVIKACQLEEDIALFPEKDKTVLGEggitLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEI 587
|
170 180 190
....*....|....*....|....*....|....*....
gi 521328941 172 LR--VVQALAHSQSVSVlwaTHLFEEVKHNNNLIVLSKG 208
Cdd:TIGR01271 588 FEscLCKLMSNKTRILV---TSKLEHLKKADKILLLHEG 623
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
17-224 |
5.77e-06 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 46.33 E-value: 5.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 17 ALDNINLCLKPG-LTMLLGPNGAGKSTLFALITGLQK----LTQGSITFDGATL-----SQSRTSIMAKMGVVFQ--QST 84
Cdd:PRK15093 22 AVDRVSMTLTEGeIRGLVGESGSGKSLIAKAICGVTKdnwrVTADRMRFDDIDLlrlspRERRKLVGHNVSMIFQepQSC 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 85 LDIDLSVKQNLsyFASLHGIS--------------TASALSHIQGLLDELDLTSKLNTKirnLNGGHRRRVELARCLIHK 150
Cdd:PRK15093 102 LDPSERVGRQL--MQNIPGWTykgrwwqrfgwrkrRAIELLHRVGIKDHKDAMRSFPYE---LTEGECQKVMIAIALANQ 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 521328941 151 PSLLLLDEPTVGLDIESRHLILRVVQALAHSQSVSVLWATHLFEEVKHNNNLI-VLSKGRVLAHDQCEALLAKYH 224
Cdd:PRK15093 177 PRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKInVLYCGQTVETAPSKELVTTPH 251
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
27-207 |
6.31e-06 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 45.68 E-value: 6.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 27 PGLTMLLGPNGAGKSTL-----FALiTGLQKLTQGSITFDGATLSQSRTSIMAKMGVvfqQSTLDIDLSVKQNLSYFASl 101
Cdd:cd03240 22 SPLTLIVGQNGAGKTTIiealkYAL-TGELPPNSKGGAHDPKLIREGEVRAQVKLAF---ENANGKKYTITRSLAILEN- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 102 hgistaSALSHiQG-----LLDELDltsklntkirNLNGGHRR------RVELARCLIHKPSLLLLDEPTVGLDIESR-- 168
Cdd:cd03240 97 ------VIFCH-QGesnwpLLDMRG----------RCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENIee 159
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 521328941 169 --HLILRVVQALAHSQSVSVlwaTHLFEEVKHNNNLIVLSK 207
Cdd:cd03240 160 slAEIIEERKSQKNFQLIVI---THDEELVDAADHIYRVEK 197
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
31-168 |
1.75e-05 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 45.12 E-value: 1.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 31 MLLGPNGAGKSTLFALITGLQKLTQGSITFDGA------------TLSQSRTSIMAKMGV--VFQQSTLDIDLsvKQNLS 96
Cdd:TIGR00954 482 LICGPNGCGKSSLFRILGELWPVYGGRLTKPAKgklfyvpqrpymTLGTLRDQIIYPDSSedMKRRGLSDKDL--EQILD 559
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 521328941 97 YFASLHGISTASALSHIQGLLDELdltsklntkirnlNGGHRRRVELARCLIHKPSLLLLDEPT--VGLDIESR 168
Cdd:TIGR00954 560 NVQLTHILEREGGWSAVQDWMDVL-------------SGGEKQRIAMARLFYHKPQFAILDECTsaVSVDVEGY 620
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
90-179 |
2.43e-05 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 44.78 E-value: 2.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 90 SVKQNLSyFASLHGISTASALSHIQGLLDELDLTSKLNTK-------IRNLNGGHRRRVELARCLIHKPSLLLLDEPTVG 162
Cdd:NF040905 356 DIKRNIT-LANLGKVSRRGVIDENEEIKVAEEYRKKMNIKtpsvfqkVGNLSGGNQQKVVLSKWLFTDPDVLILDEPTRG 434
|
90
....*....|....*..
gi 521328941 163 LDIESRHLILRVVQALA 179
Cdd:NF040905 435 IDVGAKYEIYTIINELA 451
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
122-187 |
3.54e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 44.24 E-value: 3.54e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 521328941 122 LTSKLNTKIRNLNGGHRRRVELARCLIHKPSLLLLDEPTVGLDIESRHLILRVVQALAHSQSVSVL 187
Cdd:PRK10938 125 ITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQSGITLVL 190
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
64-197 |
5.13e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 44.05 E-value: 5.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 64 TLSQSRTSIMAKM--GVVFQQSTLDIDLSVK------QNLSYFASLHGISTASALSHIQGL----LDELDLTSKLNTkir 131
Cdd:PRK00635 733 TTTDNRTSIPCPSclGKRFLPQVLEVRYKGKniadilEMTAYEAEKFFLDEPSIHEKIHALcslgLDYLPLGRPLSS--- 809
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 521328941 132 nLNGGHRRRVELARCLIH---KPSLLLLDEPTVGLDIESRHLILRVVQALAHsQSVSVLWATHLFEEVK 197
Cdd:PRK00635 810 -LSGGEIQRLKLAYELLApskKPTLYVLDEPTTGLHTHDIKALIYVLQSLTH-QGHTVVIIEHNMHVVK 876
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
18-48 |
1.01e-04 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 41.71 E-value: 1.01e-04
10 20 30
....*....|....*....|....*....|.
gi 521328941 18 LDNINLCLKPGLTMLLGPNGAGKSTLFALIT 48
Cdd:pfam13476 9 FRDQTIDFSKGLTLITGPNGSGKTTILDAIK 39
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
18-210 |
1.66e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 42.66 E-value: 1.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 18 LDNINLCLKPG-LTMLLGPNGAGKSTLFALITGlqkltqgsitfdgaTLSQSRTSIMAKMGVV--FQQSTLDIDLSVKQN 94
Cdd:PLN03232 633 LSDINLEIPVGsLVAIVGGTGEGKTSLISAMLG--------------ELSHAETSSVVIRGSVayVPQVSWIFNATVREN 698
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 95 L----SYFASLHGIST-ASALSHIQGLLDELDLTsKLNTKIRNLNGGHRRRVELARCLIHKPSLLLLDEPTVGLDIESRH 169
Cdd:PLN03232 699 IlfgsDFESERYWRAIdVTALQHDLDLLPGRDLT-EIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAH 777
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 521328941 170 LILR--VVQALAHSQSVSVLWATHLFEEVkhnNNLIVLSKGRV 210
Cdd:PLN03232 778 QVFDscMKDELKGKTRVLVTNQLHFLPLM---DRIILVSEGMI 817
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
87-180 |
1.91e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 42.31 E-value: 1.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 87 IDLSVKQNLSYFASLHGIStasalSHIQGLLDeLDLTS-KLNTKIRNLNGGHRRRVELARCLIHK---PSLLLLDEPTVG 162
Cdd:TIGR00630 789 LDMTVEEAYEFFEAVPSIS-----RKLQTLCD-VGLGYiRLGQPATTLSGGEAQRIKLAKELSKRstgRTLYILDEPTTG 862
|
90
....*....|....*...
gi 521328941 163 LDIESRHLILRVVQALAH 180
Cdd:TIGR00630 863 LHFDDIKKLLEVLQRLVD 880
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
26-207 |
4.20e-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: 39.66 E-value: 4.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 26 KPGLTMLLGPNGAGKSTLFALITG-LQKLTQGSITFDGatlsqsrtsimakmgvvfqqstldidlsvkqnlsyfaslhgi 104
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALAReLGPPGGGVIYIDG------------------------------------------ 38
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 105 stasalSHIQGLLDELDLTSKLNTKIRNLNGGHRRRVELARCLIHKPSLLLLDEPTVGLDIESRHLIL-----RVVQALA 179
Cdd:smart00382 39 ------EDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLlleelRLLLLLK 112
|
170 180
....*....|....*....|....*...
gi 521328941 180 HSQSVSVLWATHLFEEVKHNNNLIVLSK 207
Cdd:smart00382 113 SEKNLTVILTTNDEKDLGPALLRRRFDR 140
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
20-119 |
4.34e-04 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 40.37 E-value: 4.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 20 NINLCLKPGLTMLLGPNGAGKSTLF-ALITGLQKLTQGSITFDGATLSQSRTSIMAKMGVVFQQST----LDIDLSVKQN 94
Cdd:COG3950 18 EIDFDNPPRLTVLVGENGSGKTTLLeAIALALSGLLSRLDDVKFRKLLIRNGEFGDSAKLILYYGTsrllLDGPLKKLER 97
|
90 100
....*....|....*....|....*
gi 521328941 95 LSyfaslhgISTASALSHIQGLLDE 119
Cdd:COG3950 98 LK-------EEYFSRLDGYDSLLDE 115
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
10-50 |
4.52e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.91 E-value: 4.52e-04
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 521328941 10 HQYGGHHaldNINLCLKPGLTMLLGPNGAGKSTLFALITGL 50
Cdd:COG4717 9 YGFGKFR---DRTIEFSPGLNVIYGPNEAGKSTLLAFIRAM 46
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
15-194 |
4.67e-04 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 39.65 E-value: 4.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 15 HHALDNINLCLKPGLTMLLGPNGAGKSTLF---ALITGLQKLTQGSITFDGATlSQSRTSIMAKMGVVFQQStldidlsv 91
Cdd:cd03227 9 SYFVPNDVTFGEGSLTIITGPNGSGKSTILdaiGLALGGAQSATRRRSGVKAG-CIVAAVSAELIFTRLQLS-------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 92 kqnlsyfaslhgistasalshiqglldeldltsklntkirnlnGGHRRRVELARCLIH---KP-SLLLLDEPTVGLDIES 167
Cdd:cd03227 80 -------------------------------------------GGEKELSALALILALaslKPrPLYILDEIDRGLDPRD 116
|
170 180
....*....|....*....|....*..
gi 521328941 168 RHLILRVVQALAHSQSvSVLWATHLFE 194
Cdd:cd03227 117 GQALAEAILEHLVKGA-QVIVITHLPE 142
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
15-158 |
1.29e-03 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 39.49 E-value: 1.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 15 HHALDNINLCLKPG-LTMLLGPNGAGKSTLFALITGLQKLTQGSITFDGatlSQSRTSImakmgvvfqQSTLDIDLSVKQ 93
Cdd:PRK13545 37 HYALNNISFEVPEGeIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKG---SAALIAI---------SSGLNGQLTGIE 104
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 521328941 94 NLSYFASLHGISTASALSHIQGLLDELDLTSKLNTKIRNLNGGHRRRVELARCLIHKPSLLLLDE 158
Cdd:PRK13545 105 NIELKGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDE 169
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
140-165 |
3.13e-03 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 38.33 E-value: 3.13e-03
10 20
....*....|....*....|....*.
gi 521328941 140 RVELARCLIHKPSLLLLDEPTVGLDI 165
Cdd:PRK15064 163 RVLLAQALFSNPDILLLDEPTNNLDI 188
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
133-178 |
3.13e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 38.47 E-value: 3.13e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 521328941 133 LNGGHRRRVELARCLiHKPS----LLLLDEPTVGL---DIesRHLiLRVVQAL 178
Cdd:COG0178 827 LSGGEAQRVKLASEL-SKRStgktLYILDEPTTGLhfhDI--RKL-LEVLHRL 875
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
11-179 |
4.86e-03 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 36.91 E-value: 4.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 11 QYGGHHALDninlcLKPGLTMLLGPNGAGKSTLFALIT---GLQKLTQGSITFDGATLSQSRTSIMakmgVVFQ------ 81
Cdd:COG0419 12 SYRDTETID-----FDDGLNLIVGPNGAGKSTILEAIRyalYGKARSRSKLRSDLINVGSEEASVE----LEFEhggkry 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 82 -------QSTLDIDLSVKQNLSYFASLHGISTASALSH--------IQGLLDELDLTSKLNTKI----------RNLNGG 136
Cdd:COG0419 83 rierrqgEFAEFLEAKPSERKEALKRLLGLEIYEELKErlkeleeaLESALEELAELQKLKQEIlaqlsgldpiETLSGG 162
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 521328941 137 HRRRVELARCLihkpsLLLLDepTVGLDIESRHLILRVVQALA 179
Cdd:COG0419 163 ERLRLALADLL-----SLILD--FGSLDEERLERLLDALEELA 198
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
15-178 |
5.00e-03 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 37.21 E-value: 5.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 15 HHALDNINLCLKPG-LTMLLGPNGAGKSTL----------------------FALITGLQKL-------------TQGSI 58
Cdd:cd03271 8 ENNLKNIDVDIPLGvLTCVTGVSGSGKSSLindtlypalarrlhlkkeqpgnHDRIEGLEHIdkvividqspigrTPRSN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521328941 59 TfdgATLSQSRTSIMAKM-----GVVFQQSTLDI-----------DLSVKQNLSYFASLHGIStasalSHIQGL----LD 118
Cdd:cd03271 88 P---ATYTGVFDEIRELFcevckGKRYNRETLEVrykgksiadvlDMTVEEALEFFENIPKIA-----RKLQTLcdvgLG 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 521328941 119 ELDLTSKLNTkirnLNGGHRRRVELARCLiHKPS----LLLLDEPTVGLDIESRHLILRVVQAL 178
Cdd:cd03271 160 YIKLGQPATT----LSGGEAQRIKLAKEL-SKRStgktLYILDEPTTGLHFHDVKKLLEVLQRL 218
|
|
| ABC_SMC5_euk |
cd03277 |
ATP-binding cassette domain of eukaryotic SMC5 proteins; The structural maintenance of ... |
19-47 |
5.81e-03 |
|
ATP-binding cassette domain of eukaryotic SMC5 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213244 [Multi-domain] Cd Length: 213 Bit Score: 36.80 E-value: 5.81e-03
10 20
....*....|....*....|....*....
gi 521328941 19 DNINLCLKPGLTMLLGPNGAGKSTLFALI 47
Cdd:cd03277 15 DETEFRPGPSLNMIIGPNGSGKSSIVCAI 43
|
|
| SR_beta |
cd04105 |
Signal recognition particle receptor, beta subunit (SR-beta), together with SR-alpha, forms ... |
32-64 |
8.76e-03 |
|
Signal recognition particle receptor, beta subunit (SR-beta), together with SR-alpha, forms the heterodimeric signal recognition particle (SRP); Signal recognition particle receptor, beta subunit (SR-beta). SR-beta and SR-alpha form the heterodimeric signal recognition particle (SRP or SR) receptor that binds SRP to regulate protein translocation across the ER membrane. Nascent polypeptide chains are synthesized with an N-terminal hydrophobic signal sequence that binds SRP54, a component of the SRP. SRP directs targeting of the ribosome-nascent chain complex (RNC) to the ER membrane via interaction with the SR, which is localized to the ER membrane. The RNC is then transferred to the protein-conducting channel, or translocon, which facilitates polypeptide translation across the ER membrane or integration into the ER membrane. SR-beta is found only in eukaryotes; it is believed to control the release of the signal sequence from SRP54 upon binding of the ribosome to the translocon. High expression of SR-beta has been observed in human colon cancer, suggesting it may play a role in the development of this type of cancer.
Pssm-ID: 206691 [Multi-domain] Cd Length: 202 Bit Score: 36.15 E-value: 8.76e-03
10 20 30
....*....|....*....|....*....|....
gi 521328941 32 LLGPNGAGKSTLFA-LITGLQKLTQGSITFDGAT 64
Cdd:cd04105 5 LLGPSDSGKTALFTkLTTGKVRSTVTSIEPNVAS 38
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
10-50 |
9.24e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 37.20 E-value: 9.24e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 521328941 10 HQYGGHHALDninlcLKPGLTMLLGPNGAGKSTLF-ALITGL 50
Cdd:COG4913 12 GTFDGVHTID-----FDGRGTLLTGDNGSGKSTLLdAIQTLL 48
|
|
| |
