|
Name |
Accession |
Description |
Interval |
E-value |
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
6-221 |
4.44e-102 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 298.13 E-value: 4.44e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 6 VKLENVRKKIGGTEIIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGHSIRTEREKALEQIGAIVE 85
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 86 NPELYDYMTGMQNLKHFANM--AITQISKERIAEIVKLVELEHAIHKKVKTYSLGMKQRLGIAQALLHQPKILILDEPTN 163
Cdd:COG1131 81 EPALYPDLTVRENLRFFARLygLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTS 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2753457674 164 GLDPAGIRQIRDYLQLLAkEENIAVIVSSHLLSEIELMCDRVVIIKQGEFVQEYNLHE 221
Cdd:COG1131 161 GLDPEARRELWELLRELA-AEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDE 217
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
6-217 |
1.27e-88 |
|
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: 262.92 E-value: 1.27e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 6 VKLENVRKKIGGTEIIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGHSIrTEREKALEQIGAIVE 85
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSY-QKNIEALRRIGALIE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 86 NPELYDYMTGMQNLKHFANmaITQISKERIAEIVKLVELEHAIHKKVKTYSLGMKQRLGIAQALLHQPKILILDEPTNGL 165
Cdd:cd03268 80 APGFYPNLTARENLRLLAR--LLGIRKKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2753457674 166 DPAGIRQIRDYLQLLAKeENIAVIVSSHLLSEIELMCDRVVIIKQGEFVQEY 217
Cdd:cd03268 158 DPDGIKELRELILSLRD-QGITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
6-213 |
2.49e-80 |
|
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: 240.76 E-value: 2.49e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 6 VKLENVRKKIGGTEIIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGHSIRTEREKALEQIGAIVE 85
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKRRIGYLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 86 NPELYDYMTGMQNLKhfanmaitqiskeriaeivklvelehaihkkvktYSLGMKQRLGIAQALLHQPKILILDEPTNGL 165
Cdd:cd03230 81 EPSLYENLTVRENLK----------------------------------LSGGMKQRLALAQALLHDPELLILDEPTSGL 126
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2753457674 166 DPAGIRQIRDYLQLLAKeENIAVIVSSHLLSEIELMCDRVVIIKQGEF 213
Cdd:cd03230 127 DPESRREFWELLRELKK-EGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
7-221 |
1.35e-75 |
|
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: 231.29 E-value: 1.35e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 7 KLENVRKKIGGTEIIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGHSIRTEREKALEQIGAIVEN 86
Cdd:COG4555 3 EVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQIGVLPDE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 87 PELYDYMTGMQNLKHFA---NMAITQIsKERIAEIVKLVELEHAIHKKVKTYSLGMKQRLGIAQALLHQPKILILDEPTN 163
Cdd:COG4555 83 RGLYDRLTVRENIRYFAelyGLFDEEL-KKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTN 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2753457674 164 GLDPAGIRQIRDYLQLLaKEENIAVIVSSHLLSEIELMCDRVVIIKQGEFVQEYNLHE 221
Cdd:COG4555 162 GLDVMARRLLREILRAL-KKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDE 218
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
13-296 |
7.51e-69 |
|
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: 216.10 E-value: 7.51e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 13 KKIGGTEIIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGHSIRTEREKALEQIGAIVENPELYDY 92
Cdd:TIGR01188 1 KVYGDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVVREPRKVRRSIGIVPQYASVDED 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 93 MTGMQNLKHFANM--AITQISKERIAEIVKLVELEHAIHKKVKTYSLGMKQRLGIAQALLHQPKILILDEPTNGLDPAGI 170
Cdd:TIGR01188 81 LTGRENLEMMGRLygLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPRTR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 171 RQIRDYLQLLaKEENIAVIVSSHLLSEIELMCDRVVIIKQGEFVQE---YNLHEQAKHDETVVVAFEVDQVQKAN----- 242
Cdd:TIGR01188 161 RAIWDYIRAL-KEEGVTILLTTHYMEEADKLCDRIAIIDHGRIIAEgtpEELKRRLGKDTLESRPRDIQSLKVEVsmlia 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2753457674 243 ---EIVQGKAQGNV------ILVSVTKEEIPQLVKKLVNDDVLVYGVTVQNKTLEDEFLAITG 296
Cdd:TIGR01188 240 elgETGLGLLAVTVdsdrikILVPDGDETVPEIVEAAIRNGIRIRSISTERPSLDDVFLKLTG 302
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
9-216 |
4.65e-68 |
|
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: 211.07 E-value: 4.65e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 9 ENVRKKIGGTEIIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGHSIRTEREKALEQIGAIVENPE 88
Cdd:cd03265 4 ENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREVRRRIGIVFQDLS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 89 LYDYMTGMQNLKHFANMA--ITQISKERIAEIVKLVELEHAIHKKVKTYSLGMKQRLGIAQALLHQPKILILDEPTNGLD 166
Cdd:cd03265 84 VDDELTGWENLYIHARLYgvPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLD 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2753457674 167 PAGIRQIRDYLQLLAKEENIAVIVSSHLLSEIELMCDRVVIIKQGEFVQE 216
Cdd:cd03265 164 PQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAE 213
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
7-221 |
1.91e-64 |
|
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 represents the family of all lantibiotics related to gallidermin, including epidermin, mutatin, and nisin. This protein family describes the ATP-binding subunit of a gallidermin/epidermin class lantibiotic protection transporter. It is largely restricted to gallidermin-family lantibiotic biosynthesis and export cassettes, but also occurs in orphan transporter cassettes in species that lack candidate lantibiotic precursor and synthetase genes.
Pssm-ID: 163452 [Multi-domain] Cd Length: 223 Bit Score: 202.24 E-value: 1.91e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 7 KLENVRKKIGGTEIIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGHSIRterEKALEQIGAIVEN 86
Cdd:TIGR03740 2 ETKNLSKRFGKQTAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGHPWT---RKDLHKIGSLIES 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 87 PELYDYMTGMQNLKHFANMaiTQISKERIAEIVKLVELEHAIHKKVKTYSLGMKQRLGIAQALLHQPKILILDEPTNGLD 166
Cdd:TIGR03740 79 PPLYENLTARENLKVHTTL--LGLPDSRIDEVLNIVDLTNTGKKKAKQFSLGMKQRLGIAIALLNHPKLLILDEPTNGLD 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2753457674 167 PAGIRQIRDYLQLLaKEENIAVIVSSHLLSEIELMCDRVVIIKQGEFVQEYNLHE 221
Cdd:TIGR03740 157 PIGIQELRELIRSF-PEQGITVILSSHILSEVQQLADHIGIISEGVLGYQGKINK 210
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
5-300 |
8.04e-62 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 197.64 E-value: 8.04e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 5 VVKLENVRKKIGGTEIIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGHSIrteREKALEQIGAIv 84
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPL---DPEDRRRIGYL- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 85 enPE---LYDYMTGMQNLKHFA---NMAITQIsKERIAEIVKLVELEHAIHKKVKTYSLGMKQRLGIAQALLHQPKILIL 158
Cdd:COG4152 77 --PEergLYPKMKVGEQLVYLArlkGLSKAEA-KRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLIL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 159 DEPTNGLDPAGIRQIRDYLQLLaKEENIAVIVSSHLLSEIELMCDRVVIIKQGEFVQEYNLHE----QAKHDETVVVAFE 234
Cdd:COG4152 154 DEPFSGLDPVNVELLKDVIREL-AAKGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEirrqFGRNTLRLEADGD 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2753457674 235 VDQVQKANEIVQGKAQGNVILVSVTKEEIPQLVKKLVNDDVLVYGVTVQNKTLEDEFLAITGGVKA 300
Cdd:COG4152 233 AGWLRALPGVTVVEEDGDGAELKLEDGADAQELLRALLARGPVREFEEVRPSLNEIFIEVVGEKAE 298
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
6-214 |
7.31e-61 |
|
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: 192.72 E-value: 7.31e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 6 VKLENVRKKIGGTE--IIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGHSIRTEREKALEQIGAI 83
Cdd:cd03263 1 LQIRNLTKTYKKGTkpAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAARQSLGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 84 VENPELYDYMTGMQNLKHFAnmAITQISKERIAEIV----KLVELEHAIHKKVKTYSLGMKQRLGIAQALLHQPKILILD 159
Cdd:cd03263 81 PQFDALFDELTVREHLRFYA--RLKGLPKSEIKEEVelllRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLD 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2753457674 160 EPTNGLDPAGIRQIRDYLQLLAKeeNIAVIVSSHLLSEIELMCDRVVIIKQGEFV 214
Cdd:cd03263 159 EPTSGLDPASRRAIWDLILEVRK--GRSIILTTHSMDEAEALCDRIAIMSDGKLR 211
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
6-216 |
1.10e-57 |
|
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: 184.32 E-value: 1.10e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 6 VKLENVRKKIGGTEIIRGLSFEVREGeVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGHSIRTEREKALEQIGAIVE 85
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRRIGYLPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 86 NPELYDYMTGMQNLKHFA---NMAITQiSKERIAEIVKLVELEHAIHKKVKTYSLGMKQRLGIAQALLHQPKILILDEPT 162
Cdd:cd03264 80 EFGVYPNFTVREFLDYIAwlkGIPSKE-VKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPT 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2753457674 163 NGLDPAGIRQIRDYLQLLAkeENIAVIVSSHLLSEIELMCDRVVIIKQGEFVQE 216
Cdd:cd03264 159 AGLDPEERIRFRNLLSELG--EDRIVILSTHIVEDVESLCNQVAVLNKGKLVFE 210
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
5-199 |
1.99e-56 |
|
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: 180.75 E-value: 1.99e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 5 VVKLENVRKKIGGTEIIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGHSIRTEREKALEQIGAIV 84
Cdd:COG4133 2 MLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRRLAYLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 85 ENPELYDYMTGMQNLKHFANMAITQISKERIAEIVKLVELEHAIHKKVKTYSLGMKQRLGIAQALLHQPKILILDEPTNG 164
Cdd:COG4133 82 HADGLKPELTVRENLRFWAALYGLRADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTA 161
|
170 180 190
....*....|....*....|....*....|....*
gi 2753457674 165 LDPAGIRQIRDYLQLLAKEENIaVIVSSHLLSEIE 199
Cdd:COG4133 162 LDAAGVALLAELIAAHLARGGA-VLLTTHQPLELA 195
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
12-216 |
6.04e-56 |
|
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: 180.26 E-value: 6.04e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 12 RKKIGGTEIIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGHSIRTEREKALEQIGAIVENPELYD 91
Cdd:cd03266 12 RDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARRRLGFVSDSTGLYD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 92 YMTGMQNLKHFAN---MAITQIsKERIAEIVKLVELEHAIHKKVKTYSLGMKQRLGIAQALLHQPKILILDEPTNGLDPA 168
Cdd:cd03266 92 RLTARENLEYFAGlygLKGDEL-TARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVM 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2753457674 169 GIRQIRDYLQLLaKEENIAVIVSSHLLSEIELMCDRVVIIKQGEFVQE 216
Cdd:cd03266 171 ATRALREFIRQL-RALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYE 217
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
6-214 |
1.01e-53 |
|
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: 174.01 E-value: 1.01e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 6 VKLENVRKKIGGTEIIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGHSIRTErekALEQIGAIVE 85
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIA---ARNRIGYLPE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 86 NPELYDYMTGMQNLKHFA---NMAITQIsKERIAEIVKLVELEHAIHKKVKTYSLGMKQRLGIAQALLHQPKILILDEPT 162
Cdd:cd03269 78 ERGLYPKMKVIDQLVYLAqlkGLKKEEA-RRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPF 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2753457674 163 NGLDPAGIRQIRDYLQLLaKEENIAVIVSSHLLSEIELMCDRVVIIKQGEFV 214
Cdd:cd03269 157 SGLDPVNVELLKDVIREL-ARAGKTVILSTHQMELVEELCDRVLLLNKGRAV 207
|
|
| PQQ_ABC_ATP |
TIGR03864 |
ABC transporter, ATP-binding subunit, PQQ-dependent alcohol dehydrogenase system; Members of ... |
9-215 |
5.50e-52 |
|
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: 170.55 E-value: 5.50e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 9 ENVRKKIGGTEIIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGHSIRTEREKALEQIGAIVENPE 88
Cdd:TIGR03864 5 AGLSFRYGARRALDDVSFTVRPGRFVALLGPNGAGKSTLFSLLTRLYVAQSGQISVAGHDLRRAPRAALARLGVVFQQPT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 89 LYDYMTGMQNLKHFAnmAITQISK----ERIAEIVKLVELEHAIHKKVKTYSLGMKQRLGIAQALLHQPKILILDEPTNG 164
Cdd:TIGR03864 85 LDLDLSVRQNLRYHA--ALHGLSRaearARIAELLARLGLAERADDKVRELNGGHRRRVEIARALLHRPALLLLDEPTVG 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2753457674 165 LDPAGIRQIRDYLQLLAKEENIAVIVSSHLLSEIElMCDRVVIIKQGEFVQ 215
Cdd:TIGR03864 163 LDPASRAAITAHVRALARDQGLSVLWATHLVDEIE-ASDRLVVLHRGRVLA 212
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
21-289 |
1.15e-50 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 169.88 E-value: 1.15e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 21 IRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGHSIRTEREKALEQIGAI-------------VENP 87
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPFKRRKEFARRIGVVfgqrsqlwwdlpaIDSF 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 88 ELydymtgmqnlkhfaNMAITQIS----KERIAEIVKLVELEHAIHKKVKTYSLGMKQRLGIAQALLHQPKILILDEPTN 163
Cdd:COG4586 118 RL--------------LKAIYRIPdaeyKKRLDELVELLDLGELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTI 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 164 GLDPAGIRQIRDYLQLLAKEENIAVIVSSHLLSEIELMCDRVVIIKQGEFVqeY-----NLHEQAKHDETVVVAFE--VD 236
Cdd:COG4586 184 GLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEALCDRVIVIDHGRII--YdgsleELKERFGPYKTIVLELAepVP 261
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 2753457674 237 QVQKANEIVQGKAQGNVILVSV-TKEEIPQLVKKLVNdDVLVYGVTVQNKTLED 289
Cdd:COG4586 262 PLELPRGGEVIEREGNRVRLEVdPRESLAEVLARLLA-RYPVRDLTIEEPPIEE 314
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
6-214 |
7.78e-49 |
|
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: 162.12 E-value: 7.78e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 6 VKLENVRKKI-GGTEIIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGHSIRTEREKAL-EQIGAI 83
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELrRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 84 VENPELYDYMT--------GMQNLKhfanMAITQIsKERIAEIVKLVELEHAIHKKVKTYSLGMKQRLGIAQALLHQPKI 155
Cdd:COG1122 81 FQNPDDQLFAPtveedvafGPENLG----LPREEI-RERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEV 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2753457674 156 LILDEPTNGLDPAGIRQIRDYLQLLaKEENIAVIVSSHLLSEIELMCDRVVIIKQGEFV 214
Cdd:COG1122 156 LVLDEPTAGLDPRGRRELLELLKRL-NKEGKTVIIVTHDLDLVAELADRVIVLDDGRIV 213
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-233 |
1.06e-48 |
|
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: 162.07 E-value: 1.06e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 1 MGNVVVKLENVRKKIGGTEIIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGHSIRTEREKALEQI 80
Cdd:COG1127 1 MSEPMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 81 ----------GAivenpeLYDYMTGMQN----LKHFanmaiTQISKERIAEIV----KLVELEHAIHKKVKTYSLGMKQR 142
Cdd:COG1127 81 rrrigmlfqgGA------LFDSLTVFENvafpLREH-----TDLSEAEIRELVleklELVGLPGAADKMPSELSGGMRKR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 143 LGIAQALLHQPKILILDEPTNGLDPAGIRQIRDYLQLLAKEENIAVIVSSHLLSEIELMCDRVVIIKQGEFVQEYNLHEQ 222
Cdd:COG1127 150 VALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEEL 229
|
250
....*....|.
gi 2753457674 223 AKHDETVVVAF 233
Cdd:COG1127 230 LASDDPWVRQF 240
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
6-233 |
7.20e-47 |
|
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: 157.28 E-value: 7.20e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 6 VKLENVRKKIGGTEIIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGHSIRTEREKALE----QIG 81
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYrlrrRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 82 AIVENPELYDYMTGMQNLKHFANMAiTQISKERIAEIVKL----VELEHAIHKKVKTYSLGMKQRLGIAQALLHQPKILI 157
Cdd:cd03261 81 MLFQSGALFDSLTVFENVAFPLREH-TRLSEEEIREIVLEkleaVGLRGAEDLYPAELSGGMKKRVALARALALDPELLL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2753457674 158 LDEPTNGLDPAGIRQIRDYLQLLAKEENIAVIVSSHLLSEIELMCDRVVIIKQGEFVQEYNLHEQAKHDETVVVAF 233
Cdd:cd03261 160 YDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRASDDPLVRQF 235
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
11-214 |
1.31e-46 |
|
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: 156.72 E-value: 1.31e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 11 VRKKIGGTEIIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGHSIRTEREKALEQIGAIV-ENPEL 89
Cdd:cd03267 27 FKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLRRIGVVFgQKTQL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 90 YDYMTGMQNLKhfANMAITQIS----KERIAEIVKLVELEHAIHKKVKTYSLGMKQRLGIAQALLHQPKILILDEPTNGL 165
Cdd:cd03267 107 WWDLPVIDSFY--LLAAIYDLPparfKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGL 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2753457674 166 DPAGIRQIRDYLQLLAKEENIAVIVSSHLLSEIELMCDRVVIIKQGEFV 214
Cdd:cd03267 185 DVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLL 233
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
6-212 |
1.40e-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: 156.11 E-value: 1.40e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 6 VKLENVRKKIGG----TEIIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGHSIRTEREKAL---- 77
Cdd:cd03255 1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 78 -EQIGAIVENPELYDYMTGMQNLK---HFANMAITQIsKERIAEIVKLVELEHAIHKKVKTYSLGMKQRLGIAQALLHQP 153
Cdd:cd03255 81 rRHIGFVFQSFNLLPDLTALENVElplLLAGVPKKER-RERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDP 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2753457674 154 KILILDEPTNGLDPAGIRQIRDYLQLLAKEENIAVIVSSHLLsEIELMCDRVVIIKQGE 212
Cdd:cd03255 160 KIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDP-ELAEYADRIIELRDGK 217
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
7-212 |
4.14e-46 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 154.55 E-value: 4.14e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 7 KLENVRKKIGGTE--IIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGHSIRTEREKAL-EQIGAI 83
Cdd:cd03225 1 ELKNLSFSYPDGArpALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELrRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 84 VENPELYDYMT--------GMQNLKhfanMAITQIsKERIAEIVKLVELEHAIHKKVKTYSLGMKQRLGIAQALLHQPKI 155
Cdd:cd03225 81 FQNPDDQFFGPtveeevafGLENLG----LPEEEI-EERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDI 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2753457674 156 LILDEPTNGLDPAGIRQIRDYLQLLaKEENIAVIVSSHLLSEIELMCDRVVIIKQGE 212
Cdd:cd03225 156 LLLDEPTAGLDPAGRRELLELLKKL-KAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
7-216 |
7.58e-46 |
|
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: 152.97 E-value: 7.58e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 7 KLENVRKKIGGTEIIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGHSIRTEREKALEQIGAIVEn 86
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVP- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 87 pelydymtgmQNLKhfanmaitqiskeriaeivkLVELEHAIHKKVKTYSLGMKQRLGIAQALLHQPKILILDEPTNGLD 166
Cdd:cd03214 80 ----------QALE--------------------LLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLD 129
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2753457674 167 PAgiRQIR--DYLQLLAKEENIAVIVSSHLLSEIELMCDRVVIIKQGEFVQE 216
Cdd:cd03214 130 IA--HQIEllELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQ 179
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
6-215 |
2.60e-45 |
|
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: 152.67 E-value: 2.60e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 6 VKLENVRKKIGGTEIIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGHSIrTEREKALEQIGAIVE 85
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDV-TGVPPERRNIGMVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 86 NPELYDYMTGMQN----LKHfANMAITQIsKERIAEIVKLVELEHAIHKKVKTYSLGMKQRLGIAQALLHQPKILILDEP 161
Cdd:cd03259 80 DYALFPHLTVAENiafgLKL-RGVPKAEI-RARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2753457674 162 TNGLDPAGIRQIRDYLQLLAKEENIAVIVSSHLLSEIELMCDRVVIIKQGEFVQ 215
Cdd:cd03259 158 LSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQ 211
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
6-212 |
5.24e-45 |
|
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: 150.80 E-value: 5.24e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 6 VKLENVRKKIGGTEIIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGHSIRTEREKALEQ---IGA 82
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPPLrrrIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 83 IVENPELYDYMTGMQNLkhfanmaitqiskeriaeivklvelehaihkkvkTYSL--GMKQRLGIAQALLHQPKILILDE 160
Cdd:cd03229 81 VFQDFALFPHLTVLENI----------------------------------ALGLsgGQQQRVALARALAMDPDVLLLDE 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2753457674 161 PTNGLDPAGIRQIRDYLQLLAKEENIAVIVSSHLLSEIELMCDRVVIIKQGE 212
Cdd:cd03229 127 PTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-221 |
1.81e-44 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 153.42 E-value: 1.81e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 1 MGNVVVKLENVRKKIGGTEIIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGHSIRTEREKALEQI 80
Cdd:PRK13537 3 MSVAPIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQRV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 81 GAIVENPELYDYMTGMQNLKHFA---NMAITQIsKERIAEIVKLVELEHAIHKKVKTYSLGMKQRLGIAQALLHQPKILI 157
Cdd:PRK13537 83 GVVPQFDNLDPDFTVRENLLVFGryfGLSAAAA-RALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLV 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2753457674 158 LDEPTNGLDPAGIRQIRDYLQ-LLAKEENIavIVSSHLLSEIELMCDRVVIIKQGEFVQEYNLHE 221
Cdd:PRK13537 162 LDEPTTGLDPQARHLMWERLRsLLARGKTI--LLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHA 224
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-214 |
2.84e-44 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 157.37 E-value: 2.84e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 1 MGNVVVKLENVRK-----KIGGTEIIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGHSIRTEREK 75
Cdd:COG1123 256 AAEPLLEVRNLSKrypvrGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRR 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 76 ALE----QIGAIVENPE--LYDYMT-------GMQNLKHFANMAItqisKERIAEIVKLVEL-EHAIHKKVKTYSLGMKQ 141
Cdd:COG1123 336 SLRelrrRVQMVFQDPYssLNPRMTvgdiiaePLRLHGLLSRAER----RERVAELLERVGLpPDLADRYPHELSGGQRQ 411
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2753457674 142 RLGIAQALLHQPKILILDEPTNGLDPAGIRQIRDYLQLLAKEENIAVIVSSHLLSEIELMCDRVVIIKQGEFV 214
Cdd:COG1123 412 RVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIV 484
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
7-214 |
9.41e-44 |
|
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: 149.26 E-value: 9.41e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 7 KLENVRKKIG-GTEIIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGHSIRTEREKALE----QIG 81
Cdd:cd03256 2 EVENLSKTYPnGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRqlrrQIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 82 AIVENPELYDYMTGMQNLKH--FANMAI--------TQISKERIAEIVKLVELEHAIHKKVKTYSLGMKQRLGIAQALLH 151
Cdd:cd03256 82 MIFQQFNLIERLSVLENVLSgrLGRRSTwrslfglfPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIARALMQ 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2753457674 152 QPKILILDEPTNGLDPAGIRQIRDYLQLLAKEENIAVIVSSHLLSEIELMCDRVVIIKQGEFV 214
Cdd:cd03256 162 QPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIV 224
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
5-214 |
2.43e-43 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 148.67 E-value: 2.43e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 5 VVKLENVRKK-IGGTEIIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGHSIRTEREKAL----EQ 79
Cdd:COG3638 2 MLELRNLSKRyPGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALrrlrRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 80 IGAIVENPELYDYMTGMQN-----------LKHFANMaITQISKERIAEIVKLVELEHAIHKKVKTYSLGMKQRLGIAQA 148
Cdd:COG3638 82 IGMIFQQFNLVPRLSVLTNvlagrlgrtstWRSLLGL-FPPEDRERALEALERVGLADKAYQRADQLSGGQQQRVAIARA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2753457674 149 LLHQPKILILDEPTNGLDPAGIRQIRDYLQLLAKEENIAVIVSSHLLSEIELMCDRVVIIKQGEFV 214
Cdd:COG3638 161 LVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRVV 226
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
7-212 |
2.64e-43 |
|
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: 145.47 E-value: 2.64e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 7 KLENVRKKIGGTEIIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGHSI-RTEREKALEQIGAIve 85
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIaKLPLEELRRRIGYV-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 86 nPELydymtgmqnlkhfanmaitqiskeriaeivklvelehaihkkvktySLGMKQRLGIAQALLHQPKILILDEPTNGL 165
Cdd:cd00267 79 -PQL----------------------------------------------SGGQRQRVALARALLLNPDLLLLDEPTSGL 111
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2753457674 166 DPAGIRQIRDYLQLLAkEENIAVIVSSHLLSEIELMCDRVVIIKQGE 212
Cdd:cd00267 112 DPASRERLLELLRELA-EEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-211 |
1.32e-42 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 146.39 E-value: 1.32e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 1 MGNVVVKLENVRKKIGGTEIIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGHSIRTEREKA--LE 78
Cdd:COG1121 2 MMMPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARRRIgyVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 79 QIGAIveNPEL----YDY-MTGMQNLKHFANMaITQISKERIAEIVKLVELEHAIHKKVKTYSLGMKQRLGIAQALLHQP 153
Cdd:COG1121 82 QRAEV--DWDFpitvRDVvLMGRYGRRGLFRR-PSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDP 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2753457674 154 KILILDEPTNGLDPAGIRQIRDYLQLLaKEENIAVIVSSHLLSEIELMCDRVVIIKQG 211
Cdd:COG1121 159 DLLLLDEPFAGVDAATEEALYELLREL-RREGKTILVVTHDLGAVREYFDRVLLLNRG 215
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
5-214 |
3.38e-42 |
|
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: 145.57 E-value: 3.38e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 5 VVKLENVRKKIGGTEIIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGHSIRTEREKALEQIGAIV 84
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 85 --ENP--------EL-----YDYMTGMQNLkhfanmaiTQISKERIAEIVKLVELEHAIHKKVKTYSLGMKQRLGIAQAL 149
Cdd:COG1120 81 pqEPPapfgltvrELvalgrYPHLGLFGRP--------SAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARAL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 150 LHQPKILILDEPTNGLDPAgiRQIR--DYLQLLAKEENIAVIVSSHllsEIELM---CDRVVIIKQGEFV 214
Cdd:COG1120 153 AQEPPLLLLDEPTSHLDLA--HQLEvlELLRRLARERGRTVVMVLH---DLNLAaryADRLVLLKDGRIV 217
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
7-213 |
5.92e-42 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 143.80 E-value: 5.92e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 7 KLENVRKKIGGTEIIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDI--------TICGHSIRTerekale 78
Cdd:COG4619 2 ELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIyldgkplsAMPPPEWRR------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 79 QIGAIVENPELYDyMTGMQNLKHFANMAITQISKERIAEIVKLVELEHAI-HKKVKTYSLGMKQRLGIAQALLHQPKILI 157
Cdd:COG4619 75 QVAYVPQEPALWG-GTVRDNLPFPFQLRERKFDRERALELLERLGLPPDIlDKPVERLSGGERQRLALIRALLLQPDVLL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2753457674 158 LDEPTNGLDPAGIRQIRDYLQLLAKEENIAVIVSSHLLSEIELMCDRVVIIKQGEF 213
Cdd:COG4619 154 LDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
3-216 |
1.65e-41 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 143.26 E-value: 1.65e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 3 NVVVKLENVRKKIG----GTEIIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGHSIRTEREKAL- 77
Cdd:COG1136 2 SPLLELRNLTKSYGtgegEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELa 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 78 ----EQIGAIVENPELYDYMTGMQNLK---HFANMAITQIsKERIAEIVKLVELEHAIHKKVKTYSLGMKQRLGIAQALL 150
Cdd:COG1136 82 rlrrRHIGFVFQFFNLLPELTALENVAlplLLAGVSRKER-RERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2753457674 151 HQPKILILDEPTNGLDPAGIRQIRDYLQLLAKEENIAVIVSSHllsEIEL--MCDRVVIIKQGEFVQE 216
Cdd:COG1136 161 NRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTH---DPELaaRADRVIRLRDGRIVSD 225
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
5-214 |
3.24e-41 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 142.82 E-value: 3.24e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 5 VVKLENVRKKIG-GTEIIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGHSIRTEREKALEQ---- 79
Cdd:TIGR02315 1 MLEVENLSKVYPnGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKLRKlrrr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 80 IGAIVENPELYDYMTGMQNLKH-------FANMAITQIS---KERIAEIVKLVELEHAIHKKVKTYSLGMKQRLGIAQAL 149
Cdd:TIGR02315 81 IGMIFQHYNLIERLTVLENVLHgrlgykpTWRSLLGRFSeedKERALSALERVGLADKAYQRADQLSGGQQQRVAIARAL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2753457674 150 LHQPKILILDEPTNGLDPAGIRQIRDYLQLLAKEENIAVIVSSHLLSEIELMCDRVVIIKQGEFV 214
Cdd:TIGR02315 161 AQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIV 225
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
7-211 |
5.65e-40 |
|
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: 138.82 E-value: 5.65e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 7 KLENVRKKIGGTEIIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGHSIRTEREKA--LEQIGAI- 83
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERKRIgyVPQRRSId 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 84 ------VENpelydyMTGMQNLKH-FANMAITQISKERIAEIVKLVELEHAIHKKVKTYSLGMKQRLGIAQALLHQPKIL 156
Cdd:cd03235 81 rdfpisVRD------VVLMGLYGHkGLFRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2753457674 157 ILDEPTNGLDPAGIRQIRDYLQLLaKEENIAVIVSSHLLSEIELMCDRVVIIKQG 211
Cdd:cd03235 155 LLDEPFAGVDPKTQEDIYELLREL-RREGMTILVVTHDLGLVLEYFDRVLLLNRT 208
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-221 |
1.10e-39 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 141.51 E-value: 1.10e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 1 MGNVVVKLENVRKKIGGTEIIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGHSIRTEREKALEQI 80
Cdd:PRK13536 37 MSTVAIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLARARI 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 81 GAIVENPELYDYMTGMQNLKHFA---NMAITQIsKERIAEIVKLVELEHAIHKKVKTYSLGMKQRLGIAQALLHQPKILI 157
Cdd:PRK13536 117 GVVPQFDNLDLEFTVRENLLVFGryfGMSTREI-EAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLI 195
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2753457674 158 LDEPTNGLDPAGIRQIRDYLQ-LLAKEENIavIVSSHLLSEIELMCDRVVIIKQGEFVQEYNLHE 221
Cdd:PRK13536 196 LDEPTTGLDPHARHLIWERLRsLLARGKTI--LLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHA 258
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
6-215 |
4.94e-39 |
|
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: 136.23 E-value: 4.94e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 6 VKLENVRKKIGGTEIIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGHSIrTEREKALEQIGAIVE 85
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDV-TDLPPKDRDIAMVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 86 NPELYDYMTGMQN------LKHFANMAItqisKERIAEIVKLVELEHAIHKKVKTYSLGMKQRLGIAQALLHQPKILILD 159
Cdd:cd03301 80 NYALYPHMTVYDNiafglkLRKVPKDEI----DERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2753457674 160 EPTNGLDpAGIR-QIRDYLQLLAKEENIAVIVSSHLLSEIELMCDRVVIIKQGEFVQ 215
Cdd:cd03301 156 EPLSNLD-AKLRvQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQ 211
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
5-216 |
5.26e-39 |
|
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: 136.94 E-value: 5.26e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 5 VVKLENVRKKIGGT----EIIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGHSIRTEREKAL--- 77
Cdd:cd03258 1 MIELKNVSKVFGDTggkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELrka 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 78 -EQIGAIVENPELYDYMTGMQN----LKHfANMAITQIsKERIAEIVKLVELEHAIHKKVKTYSLGMKQRLGIAQALLHQ 152
Cdd:cd03258 81 rRRIGMIFQHFNLLSSRTVFENvalpLEI-AGVPKAEI-EERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANN 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2753457674 153 PKILILDEPTNGLDPAGIRQIRDYLQLLAKEENIAVIVSSHLLSEIELMCDRVVIIKQGEFVQE 216
Cdd:cd03258 159 PKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEE 222
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-207 |
8.34e-39 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 137.14 E-value: 8.34e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 1 MGNVVVKLENVRK----KIGGTEIIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGHSIRtereKA 76
Cdd:COG1116 3 AAAPALELRGVSKrfptGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVT----GP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 77 LEQIGAIVENPELYDYMTGMQN----LKhFANMAITQIsKERIAEIVKLVELEHAIHKKVKTYSLGMKQRLGIAQALLHQ 152
Cdd:COG1116 79 GPDRGVVFQEPALLPWLTVLDNvalgLE-LRGVPKAER-RERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALAND 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2753457674 153 PKILILDEPTNGLDPAGIRQIRDYLQLLAKEENIAVIVSSHLLSEIELMCDRVVI 207
Cdd:COG1116 157 PEVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFLADRVVV 211
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
3-221 |
1.55e-38 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 135.98 E-value: 1.55e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 3 NVVVKLENVRKKIGGTEIIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEG-DITICGH-----SIRTEREKa 76
Cdd:COG1119 1 DPLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGErrggeDVWELRKR- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 77 leqIGaIVeNPELYDYMTGMQNLKH------FANM----AITQISKERIAEIVKLVELEHAIHKKVKTYSLGMKQRLGIA 146
Cdd:COG1119 80 ---IG-LV-SPALQLRFPRDETVLDvvlsgfFDSIglyrEPTDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2753457674 147 QALLHQPKILILDEPTNGLDPAGIRQIRDYLQLLAKEENIAVIVSSHLLSEIeLMC-DRVVIIKQGEFVQEYNLHE 221
Cdd:COG1119 155 RALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEI-PPGiTHVLLLKDGRVVAAGPKEE 229
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-214 |
2.02e-38 |
|
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: 141.58 E-value: 2.02e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 1 MGNVV-VKLENVRKKIGGTEIIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLI---SMTEGDITICGHSIRTEREKA 76
Cdd:COG1123 1 MTPLLeVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLphgGRISGEVLLDGRDLLELSEAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 77 L-EQIGAIVENPELYDYMT--GMQNLKHFANMAIT-QISKERIAEIVKLVELEHAIHKKVKTYSLGMKQRLGIAQALLHQ 152
Cdd:COG1123 81 RgRRIGMVFQDPMTQLNPVtvGDQIAEALENLGLSrAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALD 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2753457674 153 PKILILDEPTNGLDPAGIRQIRDYLQLLAKEENIAVIVSSHLLSEIELMCDRVVIIKQGEFV 214
Cdd:COG1123 161 PDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIV 222
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
6-208 |
5.49e-38 |
|
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: 133.75 E-value: 5.49e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 6 VKLENVRK----KIGGTEIIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGHSIRTEREkaleQIG 81
Cdd:cd03293 1 LEVRNVSKtyggGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGP----DRG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 82 AIVENPELYDYMTGMQN----LKhFANMAITQIsKERIAEIVKLVELEHAIHKKVKTYSLGMKQRLGIAQALLHQPKILI 157
Cdd:cd03293 77 YVFQQDALLPWLTVLDNvalgLE-LQGVPKAEA-RERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2753457674 158 LDEPTNGLDpAGIR-QIRDYLQLLAKEENIAVIVSSHLLSEIELMCDRVVII 208
Cdd:cd03293 155 LDEPFSALD-ALTReQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVL 205
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
5-216 |
5.55e-38 |
|
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: 134.17 E-value: 5.55e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 5 VVKLENVRKKI----GGTEIIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGHSIRTEREKALE-- 78
Cdd:cd03257 1 LLEVKNLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKir 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 79 --QIGAIVENP--ELYDYMT-GMQ----NLKHFANMAITQISKERIAEIVKLVELEHAIHKKVKTYSLGMKQRLGIAQAL 149
Cdd:cd03257 81 rkEIQMVFQDPmsSLNPRMTiGEQiaepLRIHGKLSKKEARKEAVLLLLVGVGLPEEVLNRYPHELSGGQRQRVAIARAL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2753457674 150 LHQPKILILDEPTNGLDPAGIRQIRDYLQLLAKEENIAVIVSSHLLSEIELMCDRVVIIKQGEFVQE 216
Cdd:cd03257 161 ALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEE 227
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
5-214 |
6.79e-38 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 133.64 E-value: 6.79e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 5 VVKLENVRKK-IGGTEIIRGLSFEVREGEVYgFL-GPNGSGKTTTIRMMTGLISMTEGDITICGHSIRTEREKALE---- 78
Cdd:COG2884 1 MIRFENVSKRyPGGREALSDVSLEIEKGEFV-FLtGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPylrr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 79 QIGAIVENPELYDYMTGMQNLKhFAnMAITQIS----KERIAEIVKLVELEHAIHKKVKTYSLGMKQRLGIAQALLHQPK 154
Cdd:COG2884 80 RIGVVFQDFRLLPDRTVYENVA-LP-LRVTGKSrkeiRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPE 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2753457674 155 ILILDEPTNGLDPAGIRQIrdyLQLLAK--EENIAVIVSSHLLSEIELMCDRVVIIKQGEFV 214
Cdd:COG2884 158 LLLADEPTGNLDPETSWEI---MELLEEinRRGTTVLIATHDLELVDRMPKRVLELEDGRLV 216
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-215 |
9.29e-38 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 136.77 E-value: 9.29e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 1 MGNVVVKLENVRKKIGGTEIIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGHSI-RTEREKalEQ 79
Cdd:COG3842 1 MAMPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVtGLPPEK--RN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 80 IGAIVENPELYDYMTGMQN----LKHfANMAITQIsKERIAEIVKLVELEHAIHKKVKTYSLGMKQRLGIAQALLHQPKI 155
Cdd:COG3842 79 VGMVFQDYALFPHLTVAENvafgLRM-RGVPKAEI-RARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRV 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 156 LILDEPTNGLDPAGIRQIRDYLQLLAKEENIAVIVSSHLLSEIELMCDRVVIIKQGEFVQ 215
Cdd:COG3842 157 LLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQ 216
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
2-212 |
1.07e-37 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 134.01 E-value: 1.07e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 2 GNVVVKLENVRKKIGGTEIIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGHSIRTEREKALEQIG 81
Cdd:COG0411 1 SDPLLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIARLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 82 aIV---ENPELYDYMTGMQNL--------KHFANMAITQISK---------ERIAEIVKLVELEHAIHKKVKTYSLGMKQ 141
Cdd:COG0411 81 -IArtfQNPRLFPELTVLENVlvaaharlGRGLLAALLRLPRarreerearERAEELLERVGLADRADEPAGNLSYGQQR 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2753457674 142 RLGIAQALLHQPKILILDEPTNGLDPAGIRQIRDYLQLLAKEENIAVIVSSHLLSEIELMCDRVVIIKQGE 212
Cdd:COG0411 160 RLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFGR 230
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
21-163 |
1.76e-37 |
|
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: 130.46 E-value: 1.76e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 21 IRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGHSIRTEREKALE-QIGAIVENPELYDYMTGMQNL 99
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRkEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 100 KHFANMAITQ--ISKERIAEIVKLVELEHAIHKKV----KTYSLGMKQRLGIAQALLHQPKILILDEPTN 163
Cdd:pfam00005 81 RLGLLLKGLSkrEKDARAEEALEKLGLGDLADRPVgerpGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
6-215 |
4.68e-37 |
|
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: 131.59 E-value: 4.68e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 6 VKLENVRKKIGGTEIIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGHSIrTEREKALEQIGAIVE 85
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDI-TNLPPHKRPVNTVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 86 NPELYDYMTGMQNLKHFANMAIT--QISKERIAEIVKLVELEHAIHKKVKTYSLGMKQRLGIAQALLHQPKILILDEPTN 163
Cdd:cd03300 80 NYALFPHLTVFENIAFGLRLKKLpkAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLG 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2753457674 164 GLDpagiRQIRDYLQL----LAKEENIAVIVSSHLLSEIELMCDRVVIIKQGEFVQ 215
Cdd:cd03300 160 ALD----LKLRKDMQLelkrLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQ 211
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
6-215 |
1.43e-36 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 133.66 E-value: 1.43e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 6 VKLENVRKKIGGTEIIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGHSIrTEREKALEQIGAIVE 85
Cdd:COG3839 4 LELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDV-TDLPPKDRNIAMVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 86 NPELYDYMTGMQN----LKhFANMAITQIsKERIAEIVKLVELEHAIHKKVKTYSLGMKQRLGIAQALLHQPKILILDEP 161
Cdd:COG3839 83 SYALYPHMTVYENiafpLK-LRKVPKAEI-DRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFLLDEP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2753457674 162 TNGLDPAGIRQIRDYLQLLAKEENIAVIVSSHLLSEIELMCDRVVIIKQGEFVQ 215
Cdd:COG3839 161 LSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQ 214
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
12-221 |
2.25e-36 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 130.20 E-value: 2.25e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 12 RKKIGGTEIIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGhsirterekaleQIGAIVE-----N 86
Cdd:COG1134 33 RTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNG------------RVSALLElgagfH 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 87 PELydymTGMQNLKHFA---NMAITQIsKERIAEIVKLVELEHAIHKKVKTYSLGMKQRLGIAQALLHQPKILILDEPTN 163
Cdd:COG1134 101 PEL----TGRENIYLNGrllGLSRKEI-DEKFDEIVEFAELGDFIDQPVKTYSSGMRARLAFAVATAVDPDILLVDEVLA 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2753457674 164 GLDPAGIRQIRDYLQLLAKEENIAVIVsSHLLSEIELMCDRVVIIKQGEFVQEYNLHE 221
Cdd:COG1134 176 VGDAAFQKKCLARIRELRESGRTVIFV-SHSMGAVRRLCDRAIWLEKGRLVMDGDPEE 232
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
6-221 |
2.26e-36 |
|
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: 129.97 E-value: 2.26e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 6 VKLENVRKKIGGTEIIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGHSIRTE--REKALEQIGAI 83
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLpmHKRARLGIGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 84 VENPELYDYMTGMQNLkhfanMAITQI----SKERIAEIVKLVE---LEHAIHKKVKTYSLGMKQRLGIAQALLHQPKIL 156
Cdd:cd03218 81 PQEASIFRKLTVEENI-----LAVLEIrglsKKEREEKLEELLEefhITHLRKSKASSLSGGERRRVEIARALATNPKFL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2753457674 157 ILDEPTNGLDPAGIRQIRDYLQLLaKEENIAVIVSSHLLSEIELMCDRVVIIKQGEFVQEYNLHE 221
Cdd:cd03218 156 LLDEPFAGVDPIAVQDIQKIIKIL-KDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEE 219
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
6-227 |
3.58e-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: 137.27 E-value: 3.58e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 6 VKLENVRKKIGGTE--IIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGHSIRTEREKAL-EQIGA 82
Cdd:COG2274 474 IELENVSFRYPGDSppVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLrRQIGV 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 83 IVENPELYdYMTGMQNLKhfanMAITQISKERIAEIVKLVELEHAIHKKVKTY-----------SLGMKQRLGIAQALLH 151
Cdd:COG2274 554 VLQDVFLF-SGTIRENIT----LGDPDATDEEIIEAARLAGLHDFIEALPMGYdtvvgeggsnlSGGQRQRLAIARALLR 628
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2753457674 152 QPKILILDEPTNGLDPAGIRQIRDYLQLLAKeeNIAVIVSSHLLSEIELmCDRVVIIKQGEFVqeynlhEQAKHDE 227
Cdd:COG2274 629 NPRILILDEATSALDAETEAIILENLRRLLK--GRTVIIIAHRLSTIRL-ADRIIVLDKGRIV------EDGTHEE 695
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
7-212 |
4.73e-36 |
|
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: 129.09 E-value: 4.73e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 7 KLENVRKKIGGTEIIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGHSIRTEREKALEQIGaIV-- 84
Cdd:cd03219 2 EVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARLG-IGrt 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 85 -ENPELYDYMTGMQNL--------KHFANMAITQISK----ERIAEIVKLVELEHAIHKKVKTYSLGMKQRLGIAQALLH 151
Cdd:cd03219 81 fQIPRLFPELTVLENVmvaaqartGSGLLLARARREErearERAEELLERVGLADLADRPAGELSYGQQRRLEIARALAT 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2753457674 152 QPKILILDEPTNGLDPAGIRQIRDYLQLLaKEENIAVIVSSHLLSEIELMCDRVVIIKQGE 212
Cdd:cd03219 161 DPKLLLLDEPAAGLNPEETEELAELIREL-RERGITVLLVEHDMDVVMSLADRVTVLDQGR 220
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
6-216 |
6.50e-36 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 129.86 E-value: 6.50e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 6 VKLENVRKKIGGTE--IIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGHSIRTE------REKA- 76
Cdd:TIGR04520 1 IEVENVSFSYPESEkpALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLDEenlweiRKKVg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 77 -LEQ------IGAIVENpelyDYMTGMQNLkhfanmaitQIS----KERIAEIVKLVELEHAIHKKVKTYSLGMKQRLGI 145
Cdd:TIGR04520 81 mVFQnpdnqfVGATVED----DVAFGLENL---------GVPreemRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAI 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2753457674 146 AQALLHQPKILILDEPTNGLDPAGIRQIRDYLQLLAKEENIAVIVSSHLLSEIeLMCDRVVIIKQGEFVQE 216
Cdd:TIGR04520 148 AGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEA-VLADRVIVMNKGKIVAE 217
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
7-212 |
9.25e-36 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 128.61 E-value: 9.25e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 7 KLENVRKKIGGTEIIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGHSIRT----ERekALEQIGA 82
Cdd:COG1137 5 EAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHlpmhKR--ARLGIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 83 IVENPELYDYMTGMQNLkhfanMAITQIS----KERIAEIVKLVE---LEHaiHKKVKTYSL--GMKQRLGIAQALLHQP 153
Cdd:COG1137 83 LPQEASIFRKLTVEDNI-----LAVLELRklskKEREERLEELLEefgITH--LRKSKAYSLsgGERRRVEIARALATNP 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2753457674 154 KILILDEPTNGLDPAGIRQIRDYLQLLaKEENIAVIVSSHLLSEIELMCDRVVIIKQGE 212
Cdd:COG1137 156 KFILLDEPFAGVDPIAVADIQKIIRHL-KERGIGVLITDHNVRETLGICDRAYIISEGK 213
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
21-214 |
2.26e-35 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275314 [Multi-domain] Cd Length: 277 Bit Score: 128.72 E-value: 2.26e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 21 IRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGHSIRTEREKALEQI----GAIVENPE-------- 88
Cdd:TIGR04521 21 LDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKLKDLrkkvGLVFQFPEhqlfeetv 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 89 LYDYMTGMQNLKHFANMAitqisKERIAEIVKLVELEHAIHKKvKTYSL--GMKQRLGIAQALLHQPKILILDEPTNGLD 166
Cdd:TIGR04521 101 YKDIAFGPKNLGLSEEEA-----EERVKEALELVGLDEEYLER-SPFELsgGQMRRVAIAGVLAMEPEVLILDEPTAGLD 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2753457674 167 PAGIRQIRDYLQLLAKEENIAVIVSSHLLSEIELMCDRVVIIKQGEFV 214
Cdd:TIGR04521 175 PKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIV 222
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
25-205 |
2.26e-35 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 135.25 E-value: 2.26e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 25 SFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGHS-----IRTERekaleQIGAIVENPELYDYMTGMQNL 99
Cdd:NF033858 286 SFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPvdagdIATRR-----RVGYMSQAFSLYGELTVRQNL 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 100 KHFA---NMAITQIsKERIAEIVKLVELEHAIHKKVKTYSLGMKQRLGIAQALLHQPKILILDEPTNGLDPAGirqiRD- 175
Cdd:NF033858 361 ELHArlfHLPAAEI-AARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVA----RDm 435
|
170 180 190
....*....|....*....|....*....|...
gi 2753457674 176 ---YLQLLAKEENIAVIVSSHLLSEIELmCDRV 205
Cdd:NF033858 436 fwrLLIELSREDGVTIFISTHFMNEAER-CDRI 467
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
3-221 |
6.01e-35 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 131.68 E-value: 6.01e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 3 NVVVKLENVRKKIGGTEIIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICG--HSIRTEREkALEQ- 79
Cdd:COG1129 2 EPLLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGepVRFRSPRD-AQAAg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 80 IGAIVENPELYDYMTGMQNLkhFANMAITQ---ISK----ERIAEIVKLVELEHAIHKKVKTYSLGMKQRLGIAQALLHQ 152
Cdd:COG1129 81 IAIIHQELNLVPNLSVAENI--FLGREPRRgglIDWramrRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRD 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2753457674 153 PKILILDEPTNGLDPAGI----RQIRDyLqllaKEENIAVIVSSHLLSEIELMCDRVVIIKQGEFVQEYNLHE 221
Cdd:COG1129 159 ARVLILDEPTASLTEREVerlfRIIRR-L----KAQGVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVAE 226
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
6-270 |
6.15e-35 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 129.04 E-value: 6.15e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 6 VKLENVRK----KIGGTEIIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGHSIRTEREKAL---- 77
Cdd:COG1135 2 IELENLSKtfptKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELraar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 78 EQIGAIVENPELYDYMTGMQN----LKHfANMAITQIsKERIAEIVKLVELEHAIHKKVKTYSLGMKQRLGIAQALLHQP 153
Cdd:COG1135 82 RKIGMIFQHFNLLSSRTVAENvalpLEI-AGVPKAEI-RKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 154 KILILDEPTNGLDPAGIRQIrdyLQLLA---KEENIAVIVSSHLLSEIELMCDRVVIIKQGEFVQEYNLHE---QAKHDE 227
Cdd:COG1135 160 KVLLCDEATSALDPETTRSI---LDLLKdinRELGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVLDvfaNPQSEL 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 2753457674 228 T-----VVVAFEVDQvQKANEIVQGKAQGNVILVSVTKEE-----IPQLVKKL 270
Cdd:COG1135 237 TrrflpTVLNDELPE-ELLARLREAAGGGRLVRLTFVGESadeplLSELARRF 288
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
6-212 |
9.13e-35 |
|
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: 124.03 E-value: 9.13e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 6 VKLENVRKKIGGT--EIIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGHSIRTEREKAL-EQIGA 82
Cdd:cd03228 1 IEFKNVSFSYPGRpkPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLrKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 83 IVENPELYDyMTGMQNLkhfanmaitqiskeriaeivklvelehaihkkvktYSLGMKQRLGIAQALLHQPKILILDEPT 162
Cdd:cd03228 81 VPQDPFLFS-GTIRENI-----------------------------------LSGGQRQRIAIARALLRDPPILILDEAT 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2753457674 163 NGLDPAGIRQIRDYLQLLAKeeNIAVIVSSHLLSEIElMCDRVVIIKQGE 212
Cdd:cd03228 125 SALDPETEALILEALRALAK--GKTVIVIAHRLSTIR-DADRIIVLDDGR 171
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
6-212 |
1.21e-34 |
|
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: 124.95 E-value: 1.21e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 6 VKLENVRKKIGGTEIIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGHSIRTEREKALE---QIGA 82
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNINElrqKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 83 IVENPELYDYMTGMQNLKhFANMAITQISK---ERIA-EIVKLVELEHAIHKKVKTYSLGMKQRLGIAQALLHQPKILIL 158
Cdd:cd03262 81 VFQQFNLFPHLTVLENIT-LAPIKVKGMSKaeaEERAlELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLF 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2753457674 159 DEPTNGLDPAGIRQIRDYLQLLAkEENIAVIVSSHLLSEIELMCDRVVIIKQGE 212
Cdd:cd03262 160 DEPTSALDPELVGEVLDVMKDLA-EEGMTMVVVTHEMGFAREVADRVIFMDDGR 212
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
7-216 |
1.44e-34 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 124.85 E-value: 1.44e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 7 KLENVRKKIGGTEIIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGHSI--RTEREKALEQIGAIV 84
Cdd:cd03224 2 EVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDItgLPPHERARAGIGYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 85 ENPELYDYMTGMQNLKhfanMAITQISKERIAEIVKLV-----ELEHAIHKKVKTYSLGMKQRLGIAQALLHQPKILILD 159
Cdd:cd03224 82 EGRRIFPELTVEENLL----LGAYARRRAKRKARLERVyelfpRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLD 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2753457674 160 EPTNGLDPAGIRQIRDYLQLLAKEEnIAVIVSSHLLSEIELMCDRVVIIKQGEFVQE 216
Cdd:cd03224 158 EPSEGLAPKIVEEIFEAIRELRDEG-VTILLVEQNARFALEIADRAYVLERGRVVLE 213
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
16-227 |
1.48e-34 |
|
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: 131.81 E-value: 1.48e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 16 GGTEIIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGHSIRTEREKAL-EQIGAIVENPELYDyMT 94
Cdd:COG4987 346 AGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLrRRIAVVPQRPHLFD-TT 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 95 GMQNLKhFANMAITQiskERIAEIVKLVELEHAIHKKVKTY-----------SLGMKQRLGIAQALLHQPKILILDEPTN 163
Cdd:COG4987 425 LRENLR-LARPDATD---EELWAALERVGLGDWLAALPDGLdtwlgeggrrlSGGERRRLALARALLRDAPILLLDEPTE 500
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2753457674 164 GLDPAGIRQI-RDYLQLLAkeeNIAVIVSSHLLSEIELMcDRVVIIKQGEFVqeynlhEQAKHDE 227
Cdd:COG4987 501 GLDAATEQALlADLLEALA---GRTVLLITHRLAGLERM-DRILVLEDGRIV------EQGTHEE 555
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
24-211 |
2.09e-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: 124.33 E-value: 2.09e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 24 LSFEVrEGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITIcGHSIRTEREKAL------EQIGAIVENPELYDYMTGMQ 97
Cdd:cd03297 17 IDFDL-NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVL-NGTVLFDSRKKInlppqqRKIGLVFQQYALFPHLNVRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 98 N----LKHFANMAITQiskeRIAEIVKLVELEHAIHKKVKTYSLGMKQRLGIAQALLHQPKILILDEPTNGLDPAGIRQI 173
Cdd:cd03297 95 NlafgLKRKRNREDRI----SVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQL 170
|
170 180 190
....*....|....*....|....*....|....*...
gi 2753457674 174 RDYLQLLAKEENIAVIVSSHLLSEIELMCDRVVIIKQG 211
Cdd:cd03297 171 LPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDG 208
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
5-221 |
2.61e-34 |
|
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: 124.69 E-value: 2.61e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 5 VVKLENVRKKIGGTEIIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGHSIRTE--REKALEQIGA 82
Cdd:TIGR04406 1 TLVAENLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHLpmHERARLGIGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 83 IVENPELYDYMTGMQNLkhfanMAITQISK-----ERIAEIVKLVE---LEHAIHKKVKTYSLGMKQRLGIAQALLHQPK 154
Cdd:TIGR04406 81 LPQEASIFRKLTVEENI-----MAVLEIRKdldraEREERLEALLEefqISHLRDNKAMSLSGGERRRVEIARALATNPK 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2753457674 155 ILILDEPTNGLDPAGIRQIRDYLQLLaKEENIAVIVSSHLLSEIELMCDRVVIIKQGEFVQEYNLHE 221
Cdd:TIGR04406 156 FILLDEPFAGVDPIAVGDIKKIIKHL-KERGIGVLITDHNVRETLDICDRAYIISDGKVLAEGTPAE 221
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
12-212 |
2.94e-34 |
|
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: 124.18 E-value: 2.94e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 12 RKKIGGTEIIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGhsirterekaleQIGAIVE-----N 86
Cdd:cd03220 29 KGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG------------RVSSLLGlgggfN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 87 PELydymTGMQNLKhfANMAITQISK----ERIAEIVKLVELEHAIHKKVKTYSLGMKQRLGIAQALLHQPKILILDEPT 162
Cdd:cd03220 97 PEL----TGRENIY--LNGRLLGLSRkeidEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVL 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2753457674 163 NGLDPAGIRQIRDYLQLLAKEENIAVIVsSHLLSEIELMCDRVVIIKQGE 212
Cdd:cd03220 171 AVGDAAFQEKCQRRLRELLKQGKTVILV-SHDPSSIKRLCDRALVLEKGK 219
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
10-211 |
4.97e-34 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 127.15 E-value: 4.97e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 10 NVRKKIGGTEIirGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGHSIRTEREKAL-----EQIGAIV 84
Cdd:TIGR02142 4 RFSKRLGDFSL--DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKGIFlppekRRIGYVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 85 ENPELYDYMTGMQNLKH---FANMAITQISKERIAEivkLVELEHAIHKKVKTYSLGMKQRLGIAQALLHQPKILILDEP 161
Cdd:TIGR02142 82 QEARLFPHLSVRGNLRYgmkRARPSERRISFERVIE---LLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEP 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2753457674 162 TNGLDPAGIRQIRDYLQLLAKEENIAVIVSSHLLSEIELMCDRVVIIKQG 211
Cdd:TIGR02142 159 LAALDDPRKYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDG 208
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
6-215 |
8.74e-34 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 123.56 E-value: 8.74e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 6 VKLENVRKKIGGTE-IIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGHSIRTEREKALEQ-IGAI 83
Cdd:cd03295 1 IEFENVTKRYGGGKkAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRkIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 84 VENPELYDYMTGMQN------LKHFANMAItqisKERIAEIVKLVELEHAIHKKVKTYSL--GMKQRLGIAQALLHQPKI 155
Cdd:cd03295 81 IQQIGLFPHMTVEENialvpkLLKWPKEKI----RERADELLALVGLDPAEFADRYPHELsgGQQQRVGVARALAADPPL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 156 LILDEPTNGLDPAGIRQIRDYLQLLAKEENIAVIVSSHLLSEIELMCDRVVIIKQGEFVQ 215
Cdd:cd03295 157 LLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQ 216
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
6-232 |
9.63e-34 |
|
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: 123.21 E-value: 9.63e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 6 VKLENVRKKIGGTEIiRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGHSIrTEREKALEQIGAIVE 85
Cdd:cd03299 1 LKVENLSKDWKEFKL-KNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDI-TNLPPEKRDISYVPQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 86 NPELYDYMTGMQN----LKHFANMAITQisKERIAEIVKLVELEHAIHKKVKTYSLGMKQRLGIAQALLHQPKILILDEP 161
Cdd:cd03299 79 NYALFPHMTVYKNiaygLKKRKVDKKEI--ERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEP 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2753457674 162 TNGLDPAGIRQIRDYLQLLAKEENIAVIVSSHLLSEIELMCDRVVIIKQGEFVQEYNLHEQAKHDETVVVA 232
Cdd:cd03299 157 FSALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPKNEFVA 227
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
16-193 |
3.51e-33 |
|
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: 120.61 E-value: 3.51e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 16 GGTEIIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGHSIRTEREKALE---QIGAIVENPELYDY 92
Cdd:TIGR01166 3 GGPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPLDYSRKGLLErrqRVGLVFQDPDDQLF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 93 MTGMQNLKHFA--NMAITQIS-KERIAEIVKLVELEHAIHKKVKTYSLGMKQRLGIAQALLHQPKILILDEPTNGLDPAG 169
Cdd:TIGR01166 83 AADVDQDVAFGplNLGLSEAEvERRVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAGLDPAG 162
|
170 180
....*....|....*....|....
gi 2753457674 170 IRQIRDYLQLLaKEENIAVIVSSH 193
Cdd:TIGR01166 163 REQMLAILRRL-RAEGMTVVISTH 185
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-227 |
3.82e-33 |
|
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: 127.57 E-value: 3.82e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 2 GNVVVKLENVR-KKIGGTEIIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGHSIRTEREKAL-EQ 79
Cdd:COG4988 333 GPPSIELEDVSfSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWrRQ 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 80 IGAIVENPELYdYMTGMQNLKhfanMAITQISKERIAEIVKLVELEHAIHKKVKTY-----------SLGMKQRLGIAQA 148
Cdd:COG4988 413 IAWVPQNPYLF-AGTIRENLR----LGRPDASDEELEAALEAAGLDEFVAALPDGLdtplgeggrglSGGQAQRLALARA 487
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2753457674 149 LLHQPKILILDEPTNGLDPAGIRQIRDYLQLLAKeeNIAVIVSSHLLSEIELMcDRVVIIKQGEfvqeynLHEQAKHDE 227
Cdd:COG4988 488 LLRDAPLLLLDEPTAHLDAETEAEILQALRRLAK--GRTVILITHRLALLAQA-DRILVLDDGR------IVEQGTHEE 557
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
6-214 |
2.38e-32 |
|
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: 117.14 E-value: 2.38e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 6 VKLENVRKKIGGTEIIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGHSIRTEREKALEQIGaive 85
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDARRAG---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 86 npelydymtgmqnlkhfanmaitqiskerIAEIVKLvelehaihkkvktySLGMKQRLGIAQALLHQPKILILDEPTNGL 165
Cdd:cd03216 77 -----------------------------IAMVYQL--------------SVGERQMVEIARALARNARLLILDEPTAAL 113
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2753457674 166 DPAGIRQIRDYLQLLaKEENIAVIVSSHLLSEIELMCDRVVIIKQGEFV 214
Cdd:cd03216 114 TPAEVERLFKVIRRL-RAQGVAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
9-215 |
4.06e-32 |
|
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: 119.67 E-value: 4.06e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 9 ENVRKKIGGTEIIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGHSIRTEREKALEQ-----IGAI 83
Cdd:cd03294 28 EEILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRElrrkkISMV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 84 VENPELYDYMTGMQN------LKHFANmaitQISKERIAEIVKLVELEHAIHKKVKTYSLGMKQRLGIAQALLHQPKILI 157
Cdd:cd03294 108 FQSFALLPHRTVLENvafgleVQGVPR----AEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILL 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2753457674 158 LDEPTNGLDPAGIRQIRDYLQLLAKEENIAVIVSSHLLSEIELMCDRVVIIKQGEFVQ 215
Cdd:cd03294 184 MDEAFSALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQ 241
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
16-227 |
5.27e-32 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 124.51 E-value: 5.27e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 16 GGTEIIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGHSIRTEREKAL-EQIGAIVENPELYDyMT 94
Cdd:COG1132 351 GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESLrRQIGVVPQDTFLFS-GT 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 95 GMQNLKhFANMAITQiskERIAEIVKLVELEHAIHKKVKTY-----------SLGMKQRLGIAQALLHQPKILILDEPTN 163
Cdd:COG1132 430 IRENIR-YGRPDATD---EEVEEAAKAAQAHEFIEALPDGYdtvvgergvnlSGGQRQRIAIARALLKDPPILILDEATS 505
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2753457674 164 GLDPAGIRQIRDYLQLLAKeeNIAVIVSSHLLSEIElMCDRVVIIKQGEFVqeynlhEQAKHDE 227
Cdd:COG1132 506 ALDTETEALIQEALERLMK--GRTTIVIAHRLSTIR-NADRILVLDDGRIV------EQGTHEE 560
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
5-216 |
2.06e-31 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 117.02 E-value: 2.06e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 5 VVKLENVRKKIGGTEIIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGHSI---RTEREKALEQIG 81
Cdd:COG1126 1 MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLtdsKKDINKLRRKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 82 AIVENPELYDYMTGMQNLKhFANMAITQISK---ERIA-EIVKLVELEHAIHKKVKTYSLGMKQRLGIAQALLHQPKILI 157
Cdd:COG1126 81 MVFQQFNLFPHLTVLENVT-LAPIKVKKMSKaeaEERAmELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKVML 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2753457674 158 LDEPTNGLDPAGIRQIRDYLQLLAKeENIAVIVSSHllsEIEL---MCDRVVIIKQGEFVQE 216
Cdd:COG1126 160 FDEPTSALDPELVGEVLDVMRDLAK-EGMTMVVVTH---EMGFareVADRVVFMDGGRIVEE 217
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
16-214 |
4.55e-31 |
|
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: 115.43 E-value: 4.55e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 16 GGTEIIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGHSI-RTEREKAleqIGAIVENPELYDYMT 94
Cdd:cd03226 11 KGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIkAKERRKS---IGYVMQDVDYQLFTD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 95 GMQNLKHFANMAITQiSKERIAEIVKLVELEHAIHKKVKTYSLGMKQRLGIAQALLHQPKILILDEPTNGLDPAGIRQIR 174
Cdd:cd03226 88 SVREELLLGLKELDA-GNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNMERVG 166
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2753457674 175 DYLQLLAKEENiAVIVSSHLLSEIELMCDRVVIIKQGEFV 214
Cdd:cd03226 167 ELIRELAAQGK-AVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
6-215 |
2.02e-30 |
|
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: 114.74 E-value: 2.02e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 6 VKLENVRKKIGGTEIIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGH--SIRTEREKaleQIGAI 83
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEdaTDVPVQER---NVGFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 84 VENPELYDYMTGMQNL------KHFANMAITQISKERIAEIVKLVELEHAIHKKVKTYSLGMKQRLGIAQALLHQPKILI 157
Cdd:cd03296 80 FQHYALFRHMTVFDNVafglrvKPRSERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2753457674 158 LDEPTNGLDPAGIRQIRDYLQLLAKEENIAVIVSSHLLSEIELMCDRVVIIKQGEFVQ 215
Cdd:cd03296 160 LDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQ 217
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
5-292 |
3.71e-30 |
|
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: 120.12 E-value: 3.71e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 5 VVKLENVRKKIGGTE--IIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGHSIRTEREKALEQIGA 82
Cdd:TIGR01257 1937 ILRLNELTKVYSGTSspAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISDVHQNMGY 2016
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 83 IVENPELYDYMTGMQNLKHFANM-AITQISKERIAEI-VKLVELEHAIHKKVKTYSLGMKQRLGIAQALLHQPKILILDE 160
Cdd:TIGR01257 2017 CPQFDAIDDLLTGREHLYLYARLrGVPAEEIEKVANWsIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDE 2096
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 161 PTNGLDPAGIRQIRDYLQLLAKEENiAVIVSSHLLSEIELMCDRVVIIKQGEF-----VQeynlHEQAKHDETVVVAFE- 234
Cdd:TIGR01257 2097 PTTGMDPQARRMLWNTIVSIIREGR-AVVLTSHSMEECEALCTRLAIMVKGAFqclgtIQ----HLKSKFGDGYIVTMKi 2171
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2753457674 235 -------------VDQVQKAN--EIVQGKAQGNVILVSVTKEEIPQLVKKLVN--DDVLVYGVTVQNKTLEDEFL 292
Cdd:TIGR01257 2172 kspkddllpdlnpVEQFFQGNfpGSVQRERHYNMLQFQVSSSSLARIFQLLIShkDSLLIEEYSVTQTTLDQVFV 2246
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
25-221 |
8.34e-30 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 115.58 E-value: 8.34e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 25 SFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITI---------CGHSIRTEREkaleQIGAIVENPELYDYMTG 95
Cdd:COG4148 19 DFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLggevlqdsaRGIFLPPHRR----RIGYVFQEARLFPHLSV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 96 MQNLKHFANMAITQISKERIAEIVKLVELEHAIHKKVKTYSLGMKQRLGIAQALLHQPKILILDEPTNGLDPAGIRQIRD 175
Cdd:COG4148 95 RGNLLYGRKRAPRAERRISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAEILP 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2753457674 176 YLQLLAKEENIAVIVSSHLLSEIELMCDRVVIIKQGEFVQEYNLHE 221
Cdd:COG4148 175 YLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAE 220
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
5-214 |
9.33e-30 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 114.77 E-value: 9.33e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 5 VVKLENVRK----KIGGTEIIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLIS---MTEGDITICGHSIRTEREKAL 77
Cdd:COG0444 1 LLEVRNLKVyfptRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPppgITSGEILFDGEDLLKLSEKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 78 EQ-----IGAIVENPelydyMT--------GMQ---NLKHFANMAITQIsKERIAEIVKLVELEHAiHKKVKTY----SL 137
Cdd:COG0444 81 RKirgreIQMIFQDP-----MTslnpvmtvGDQiaePLRIHGGLSKAEA-RERAIELLERVGLPDP-ERRLDRYphelSG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2753457674 138 GMKQRLGIAQALLHQPKILILDEPTNGLDpAGIR-QIRDYLQLLAKEENIAVIVSSHLLSEIELMCDRVVIIKQGEFV 214
Cdd:COG0444 154 GMRQRVMIARALALEPKLLIADEPTTALD-VTIQaQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIV 230
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1-215 |
1.41e-29 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 115.43 E-value: 1.41e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 1 MGNVVVKLENVRKKIGGTEIIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGHSI-RTEREKalEQ 79
Cdd:PRK09452 10 SLSPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDItHVPAEN--RH 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 80 IGAIVENPELYDYMTGMQNLKHFANMAIT---QIsKERIAEIVKLVELEHAIHKKVKTYSLGMKQRLGIAQALLHQPKIL 156
Cdd:PRK09452 88 VNTVFQSYALFPHMTVFENVAFGLRMQKTpaaEI-TPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVL 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2753457674 157 ILDEPTNGLDPAGIRQIRDYLQLLAKEENIAVIVSSHLLSEIELMCDRVVIIKQGEFVQ 215
Cdd:PRK09452 167 LLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQ 225
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
6-215 |
1.52e-29 |
|
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: 111.89 E-value: 1.52e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 6 VKLENVRKKIGGTEIIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISM-----TEGDITICGHSIRTEREKALE-- 78
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLipgapDEGEVLLDGKDIYDLDVDVLElr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 79 -QIGAIVENPELYDyMTGMQN----LKHFAnMAITQISKERIAEIVKLVELEHAIHKKVKTYSL--GMKQRLGIAQALLH 151
Cdd:cd03260 81 rRVGMVFQKPNPFP-GSIYDNvaygLRLHG-IKLKEELDERVEEALRKAALWDEVKDRLHALGLsgGQQQRLCLARALAN 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2753457674 152 QPKILILDEPTNGLDPAGIRQIRDYLQLLAKEenIAVIVSSHLLSEIELMCDRVVIIKQGEFVQ 215
Cdd:cd03260 159 EPEVLLLDEPTSALDPISTAKIEELIAELKKE--YTIVIVTHNMQQAARVADRTAFLLNGRLVE 220
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
17-221 |
8.63e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 111.48 E-value: 8.63e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 17 GTEIIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGHSIRTEREKAL---EQIGAIVENPELYDYM 93
Cdd:PRK13636 18 GTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRKGLMklrESVGMVFQDPDNQLFS 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 94 TGMQNLKHFANMAITQISKE---RIAEIVKLVELEHAIHKKVKTYSLGMKQRLGIAQALLHQPKILILDEPTNGLDPAGI 170
Cdd:PRK13636 98 ASVYQDVSFGAVNLKLPEDEvrkRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGV 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2753457674 171 RQIRDYLQLLAKEENIAVIVSSHLLSEIELMCDRVVIIKQGEFVQEYNLHE 221
Cdd:PRK13636 178 SEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKE 228
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
20-214 |
1.43e-28 |
|
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: 109.28 E-value: 1.43e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 20 IIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLI---SMTEGDITICGHSIrtEREKALEQIGAIVENPELYDYMTGM 96
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVeggGTTSGQILFNGQPR--KPDQFQKCVAYVRQDDILLPGLTVR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 97 QNLKHFANMAITQISKERI----AEIVKLVELEHAI--HKKVKTYSLGMKQRLGIAQALLHQPKILILDEPTNGLDPAGI 170
Cdd:cd03234 100 ETLTYTAILRLPRKSSDAIrkkrVEDVLLRDLALTRigGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFTA 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2753457674 171 RQIRDYLQLLAKeENIAVIVSSHL-LSEIELMCDRVVIIKQGEFV 214
Cdd:cd03234 180 LNLVSTLSQLAR-RNRIVILTIHQpRSDLFRLFDRILLLSSGEIV 223
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
5-211 |
2.08e-28 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 110.10 E-value: 2.08e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 5 VVKLENVRKKIGGTEIIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLI---SMTEGDITICGHSIRTERE------K 75
Cdd:PRK09984 4 IIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgdKSAGSHIELLGRTVQREGRlardirK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 76 ALEQIGAIVENPELYDYMTGMQN---------------LKHFanmaiTQISKERIAEIVKLVELEHAIHKKVKTYSLGMK 140
Cdd:PRK09984 84 SRANTGYIFQQFNLVNRLSVLENvligalgstpfwrtcFSWF-----TREQKQRALQALTRVGMVHFAHQRVSTLSGGQQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2753457674 141 QRLGIAQALLHQPKILILDEPTNGLDPAGIRQIRDYLQLLAKEENIAVIVSSHLLSEIELMCDRVVIIKQG 211
Cdd:PRK09984 159 QRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQG 229
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-214 |
2.80e-28 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 113.58 E-value: 2.80e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 1 MGNVVVKLENVRKKIGGTEIIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGH--SIRTEREkALE 78
Cdd:COG3845 1 MMPPALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKpvRIRSPRD-AIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 79 Q-IGAIVENPELYDYMTGMQNL--------KHFANMAITqisKERIAEIVKLVELEHAIHKKVKTYSLGMKQRLGIAQAL 149
Cdd:COG3845 80 LgIGMVHQHFMLVPNLTVAENIvlgleptkGGRLDRKAA---RARIRELSERYGLDVDPDAKVEDLSVGEQQRVEILKAL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2753457674 150 LHQPKILILDEPTNGLDPAGIRQIRDYLQLLAkEENIAVIVSSHLLSEIELMCDRVVIIKQGEFV 214
Cdd:COG3845 157 YRGARILILDEPTAVLTPQEADELFEILRRLA-AEGKSIIFITHKLREVMAIADRVTVLRRGKVV 220
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
8-212 |
1.02e-27 |
|
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: 105.38 E-value: 1.02e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 8 LENVRKKIGGTE--IIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGHSIRTEREKAL-EQIGAIv 84
Cdd:cd03246 3 VENVSFRYPGAEppVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELgDHVGYL- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 85 enpelydymtgMQNLKHFANmaitqiskeRIAEIVklvelehaihkkvktYSLGMKQRLGIAQALLHQPKILILDEPTNG 164
Cdd:cd03246 82 -----------PQDDELFSG---------SIAENI---------------LSGGQRQRLGLARALYGNPRILVLDEPNSH 126
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2753457674 165 LDPAGIRQIRDYLQLLAKEENIAVIVsSHLLSEIElMCDRVVIIKQGE 212
Cdd:cd03246 127 LDVEGERALNQAIAALKAAGATRIVI-AHRPETLA-SADRILVLEDGR 172
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
9-214 |
1.38e-27 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 107.29 E-value: 1.38e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 9 ENVRKKIGGTEIIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGH--SIRTEREKALEQIGAIVEN 86
Cdd:PRK10895 7 KNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEdiSLLPLHARARRGIGYLPQE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 87 PELYDYMTGMQNLkhfanMAITQISK--------ERIAEIVKLVELEHAIHKKVKTYSLGMKQRLGIAQALLHQPKILIL 158
Cdd:PRK10895 87 ASIFRRLSVYDNL-----MAVLQIRDdlsaeqreDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2753457674 159 DEPTNGLDPAGIRQIRDYLQLLaKEENIAVIVSSHLLSEIELMCDRVVIIKQGEFV 214
Cdd:PRK10895 162 DEPFAGVDPISVIDIKRIIEHL-RDSGLGVLITDHNVRETLAVCERAYIVSQGHLI 216
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
8-215 |
2.82e-27 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 108.70 E-value: 2.82e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 8 LENVRKKIGGTEIIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGHSIRT-----ERekaleQIGA 82
Cdd:COG1118 5 VRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFTnlpprER-----RVGF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 83 IVENPELYDYMTGMQNLKhFAnMAITQISKERIAEIV----KLVELEHAIHKKVKTYSLGMKQRLGIAQALLHQPKILIL 158
Cdd:COG1118 80 VFQHYALFPHMTVAENIA-FG-LRVRPPSKAEIRARVeellELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLLL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2753457674 159 DEPTNGLDpAGIR-QIRDYLQLLAKEENIAVIVSSHLLSEIELMCDRVVIIKQGEFVQ 215
Cdd:COG1118 158 DEPFGALD-AKVRkELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQ 214
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
19-227 |
4.10e-27 |
|
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: 105.70 E-value: 4.10e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 19 EIIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGHSIRTEREKAL-EQIGAIVENPELYDyMTGMQ 97
Cdd:cd03249 17 PILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLrSQIGLVSQEPVLFD-GTIAE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 98 NLKHFANMAitqiSKERIAEIVKLVELEHAIHKKVKTY-----------SLGMKQRLGIAQALLHQPKILILDEPTNGLD 166
Cdd:cd03249 96 NIRYGKPDA----TDEEVEEAAKKANIHDFIMSLPDGYdtlvgergsqlSGGQKQRIAIARALLRNPKILLLDEATSALD 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2753457674 167 PAGIRQIRDYLQLLAKeeNIAVIVSSHLLSEIElMCDRVVIIKQGEFVqeynlhEQAKHDE 227
Cdd:cd03249 172 AESEKLVQEALDRAMK--GRTTIVIAHRLSTIR-NADLIAVLQNGQVV------EQGTHDE 223
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
8-218 |
5.82e-27 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 109.77 E-value: 5.82e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 8 LENVRKKIGGTEIIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGHsIRTERekaLEQigaiveNP 87
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKG-LRIGY---LPQ------EP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 88 ELYDYMTGMQN-LKHFANMAITQISKERI--------AEIVKLVELEHAI--------------------------HKKV 132
Cdd:COG0488 71 PLDDDLTVLDTvLDGDAELRALEAELEELeaklaepdEDLERLAELQEEFealggweaearaeeilsglgfpeedlDRPV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 133 KTYSLGMKQRLGIAQALLHQPKILILDEPTNGLDPAGIRQIRDYLqllaKEENIAVIVSSH---LLSEIelmCDRVVIIK 209
Cdd:COG0488 151 SELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFL----KNYPGTVLVVSHdryFLDRV---ATRILELD 223
|
....*....
gi 2753457674 210 QGEfVQEYN 218
Cdd:COG0488 224 RGK-LTLYP 231
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
9-214 |
1.41e-26 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 104.85 E-value: 1.41e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 9 ENVRKKIGGTEIIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGHSIRTEREKALEQIGAI----- 83
Cdd:PRK13548 6 RNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVlpqhs 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 84 -------VEnpE-----LYDYMTGMQNLKHFANMAITQiskeriaeivklVELEHAIHKKVKTYSLGMKQRLGIAQALL- 150
Cdd:PRK13548 86 slsfpftVE--EvvamgRAPHGLSRAEDDALVAAALAQ------------VDLAHLAGRDYPQLSGGEQQRVQLARVLAq 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2753457674 151 -----HQPKILILDEPTNGLDPAgiRQIRdYLQL---LAKEENIAVIVSSHLLSEIELMCDRVVIIKQGEFV 214
Cdd:PRK13548 152 lwepdGPPRWLLLDEPTSALDLA--HQHH-VLRLarqLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLV 220
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
6-214 |
1.96e-26 |
|
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: 103.44 E-value: 1.96e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 6 VKLENVRKKIGGTEI--IRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGHSIRT-EREKALEQIGA 82
Cdd:cd03245 3 IEFRNVSFSYPNQEIpaLDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQlDPADLRRNIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 83 IVENPELYdYMTGMQNLkhfaNMAITQISKERIAEIVKLVELEHAIHKKVKTYSL-----------GMKQRLGIAQALLH 151
Cdd:cd03245 83 VPQDVTLF-YGTLRDNI----TLGAPLADDERILRAAELAGVTDFVNKHPNGLDLqigergrglsgGQRQAVALARALLN 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2753457674 152 QPKILILDEPTNGLDPAGIRQIRDYLQLLAKEEniAVIVSSHLLSEIELmCDRVVIIKQGEFV 214
Cdd:cd03245 158 DPPILLLDEPTSAMDMNSEERLKERLRQLLGDK--TLIIITHRPSLLDL-VDRIIVMDSGRIV 217
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
17-216 |
3.67e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 104.00 E-value: 3.67e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 17 GTEIIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGHSIRTEREKALE---QIGAIVENPE----- 88
Cdd:PRK13639 14 GTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSLLEvrkTVGIVFQNPDdqlfa 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 89 ---LYDYMTGMQNLKhfanmaitqISKE----RIAEIVKLVELEHAIHKKVKTYSLGMKQRLGIAQALLHQPKILILDEP 161
Cdd:PRK13639 94 ptvEEDVAFGPLNLG---------LSKEevekRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEP 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2753457674 162 TNGLDPAGIRQIRDYLQLLAKeENIAVIVSSHLLSEIELMCDRVVIIKQGEFVQE 216
Cdd:PRK13639 165 TSGLDPMGASQIMKLLYDLNK-EGITIIISTHDVDLVPVYADKVYVMSDGKIIKE 218
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
17-213 |
4.48e-26 |
|
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: 108.18 E-value: 4.48e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 17 GTEIIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGHSIRTEREKALEQIGAIVENPELYDYMTGM 96
Cdd:TIGR01257 942 GRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDAVRQSLGMCPQHNILFHHLTVA 1021
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 97 QNLKHFANMAiTQISKERIAEIVKLVE---LEHAIHKKVKTYSLGMKQRLGIAQALLHQPKILILDEPTNGLDPAGIRQI 173
Cdd:TIGR01257 1022 EHILFYAQLK-GRSWEEAQLEMEAMLEdtgLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSI 1100
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2753457674 174 RDYlqLLAKEENIAVIVSSHLLSEIELMCDRVVIIKQGEF 213
Cdd:TIGR01257 1101 WDL--LLKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRL 1138
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
7-216 |
5.00e-26 |
|
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: 102.75 E-value: 5.00e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 7 KLENVRKKIGGTEIIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGHSI---RTEReKALEQIGAI 83
Cdd:COG0410 5 EVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDItglPPHR-IARLGIGYV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 84 VENPELYDYMTGMQNLKhfanM-AITQISKERIAEIVKLV-----ELEHAIHKKVKTYSLGMKQRLGIAQALLHQPKILI 157
Cdd:COG0410 84 PEGRRIFPSLTVEENLL----LgAYARRDRAEVRADLERVyelfpRLKERRRQRAGTLSGGEQQMLAIGRALMSRPKLLL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2753457674 158 LDEPTNGLDPAGIRQIRDYLQLLaKEENIAVIVSSHLLSEIELMCDRVVIIKQGEFVQE 216
Cdd:COG0410 160 LDEPSLGLAPLIVEEIFEIIRRL-NREGVTILLVEQNARFALEIADRAYVLERGRIVLE 217
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1-217 |
5.67e-26 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 107.07 E-value: 5.67e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 1 MGNVVVKLENVRKKIGGTEIIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITIcGHSIRT-----EREk 75
Cdd:COG0488 311 LGKKVLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETVKIgyfdqHQE- 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 76 aleqigaivenpELYDYMTGMQNLKHFAnmaitqiSKERIAEIVKLVEL-----EHAiHKKVKTYSLGMKQRLGIAQALL 150
Cdd:COG0488 389 ------------ELDPDKTVLDELRDGA-------PGGTEQEVRGYLGRflfsgDDA-FKPVGVLSGGEKARLALAKLLL 448
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 151 HQPKILILDEPTNGLDPAGIRQIRDYLQllakEENIAVIVSSH---LLSEIelmCDRVVIIKQGEfVQEY 217
Cdd:COG0488 449 SPPNVLLLDEPTNHLDIETLEALEEALD----DFPGTVLLVSHdryFLDRV---ATRILEFEDGG-VREY 510
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
6-221 |
9.38e-26 |
|
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: 101.92 E-value: 9.38e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 6 VKLENVR-KKIGGTEIIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGHSIRTEREKAL-EQIGAI 83
Cdd:cd03254 3 IEFENVNfSYDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLrSMIGVV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 84 VENPELYDyMTGMQNLKHFANMAitqiSKERIAEIVKLVELEHAIHKKVKTY-----------SLGMKQRLGIAQALLHQ 152
Cdd:cd03254 83 LQDTFLFS-GTIMENIRLGRPNA----TDEEVIEAAKEAGAHDFIMKLPNGYdtvlgenggnlSQGERQLLAIARAMLRD 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2753457674 153 PKILILDEPTNGLDPAGIRQIRDYLQLLAKeeNIAVIVSSHLLSEIElMCDRVVIIKQGEFVQEYNLHE 221
Cdd:cd03254 158 PKILILDEATSNIDTETEKLIQEALEKLMK--GRTSIIIAHRLSTIK-NADKILVLDDGKIIEEGTHDE 223
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
1-215 |
1.01e-25 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 104.42 E-value: 1.01e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 1 MGNVVVKLENVRKKIGGTEIIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGHSIrTEREKALEQI 80
Cdd:PRK11432 2 TQKNFVVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDV-THRSIQQRDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 81 GAIVENPELYDYMTGMQNLKHFANM---AITQIsKERIAEIVKLVELEHAIHKKVKTYSLGMKQRLGIAQALLHQPKILI 157
Cdd:PRK11432 81 CMVFQSYALFPHMSLGENVGYGLKMlgvPKEER-KQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2753457674 158 LDEPTNGLDPAGIRQIRDYLQLLAKEENIAVIVSSHLLSEIELMCDRVVIIKQGEFVQ 215
Cdd:PRK11432 160 FDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQ 217
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
2-213 |
1.62e-25 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 99.81 E-value: 1.62e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 2 GNVVVKLENVRKKIGgteiIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGHSIRTER-EKALEQ- 79
Cdd:cd03215 1 GEPVLEVRGLSVKGA----VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSpRDAIRAg 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 80 IGAIVENPELYDYMTGMqNLKHfaNMAITQIskeriaeivklvelehaihkkvktYSLGMKQRLGIAQALLHQPKILILD 159
Cdd:cd03215 77 IAYVPEDRKREGLVLDL-SVAE--NIALSSL------------------------LSGGNQQKVVLARWLARDPRVLILD 129
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2753457674 160 EPTNGLDPAGIRQIRDYLQLLAkEENIAVIVSSHLLSEIELMCDRVVIIKQGEF 213
Cdd:cd03215 130 EPTRGVDVGAKAEIYRLIRELA-DAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
21-211 |
1.86e-25 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 101.00 E-value: 1.86e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 21 IRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGHSIRterEKALEQIgAIVENPELYDYMTGMQNLK 100
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQIT---EPGPDRM-VVFQNYSLLPWLTVRENIA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 101 HFANMAITQISKERIAEIVK----LVELEHAIHKKVKTYSLGMKQRLGIAQALLHQPKILILDEPTNGLDPAGIRQIRDY 176
Cdd:TIGR01184 77 LAVDRVLPDLSKSERRAIVEehiaLVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEE 156
|
170 180 190
....*....|....*....|....*....|....*
gi 2753457674 177 LQLLAKEENIAVIVSSHLLSEIELMCDRVVIIKQG 211
Cdd:TIGR01184 157 LMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
20-227 |
1.90e-25 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 105.68 E-value: 1.90e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 20 IIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGHSIRTEREKALEQIGAIVE------NPELYDym 93
Cdd:PRK11160 355 VLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQAISVVSqrvhlfSATLRD-- 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 94 tgmqNLKhfanMAITQISKERIAEIVKLVELEHAI--HKKVKTY--------SLGMKQRLGIAQALLHQPKILILDEPTN 163
Cdd:PRK11160 433 ----NLL----LAAPNASDEALIEVLQQVGLEKLLedDKGLNAWlgeggrqlSGGEQRRLGIARALLHDAPLLLLDEPTE 504
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2753457674 164 GLDPAGIRQIrdyLQLLAKE-ENIAVIVSSHLLSEIELMcDRVVIIKQGEFVqeynlhEQAKHDE 227
Cdd:PRK11160 505 GLDAETERQI---LELLAEHaQNKTVLMITHRLTGLEQF-DRICVMDNGQII------EQGTHQE 559
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
6-215 |
2.28e-25 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 103.62 E-value: 2.28e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 6 VKLENVRKKIGGTEIIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGHSIrtEREKALE-QIGAIV 84
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDV--SRLHARDrKVGFVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 85 ENPELYDYMTGMQNL---------KHFANMAITqisKERIAEIVKLVELEHAIHKKVKTYSLGMKQRLGIAQALLHQPKI 155
Cdd:PRK10851 81 QHYALFRHMTVFDNIafgltvlprRERPNAAAI---KAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQI 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 156 LILDEPTNGLDPAGIRQIRDYLQLLAKEENIAVIVSSHLLSEIELMCDRVVIIKQGEFVQ 215
Cdd:PRK10851 158 LLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQ 217
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
19-212 |
3.74e-25 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 101.24 E-value: 3.74e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 19 EIIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGHSIRTEREKAL---EQIGAIVENPELYDYMTG 95
Cdd:PRK13638 15 PVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKRGLLalrQQVATVFQDPEQQIFYTD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 96 MQNLKHFA--NMAITQIS-KERIAEIVKLVELEHAIHKKVKTYSLGMKQRLGIAQALLHQPKILILDEPTNGLDPAGIRQ 172
Cdd:PRK13638 95 IDSDIAFSlrNLGVPEAEiTRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQ 174
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2753457674 173 IRDYLQLLAKEENiAVIVSSHLLSEIELMCDRVVIIKQGE 212
Cdd:PRK13638 175 MIAIIRRIVAQGN-HVIISSHDIDLIYEISDAVYVLRQGQ 213
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
16-173 |
4.46e-25 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 99.36 E-value: 4.46e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 16 GGTEIIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGHSIRTEREKALEQIGAIVENPELYDYMTG 95
Cdd:TIGR01189 11 GERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYLGHLPGLKPELSA 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2753457674 96 MQNLKHFAnmAITQISKERIAEIVKLVELEHAIHKKVKTYSLGMKQRLGIAQALLHQPKILILDEPTNGLDPAGIRQI 173
Cdd:TIGR01189 91 LENLHFWA--AIHGGAQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVALL 166
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
6-215 |
6.69e-25 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 102.42 E-value: 6.69e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 6 VKLENVRKKIGGTEIIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITIcGHSIRTEREKALEQIGAIVE 85
Cdd:PRK11000 4 VTLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFI-GEKRMNDVPPAERGVGMVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 86 NPELYDYMTGMQN----LKhFANMAITQISKeRIAEIVKLVELEHAIHKKVKTYSLGMKQRLGIAQALLHQPKILILDEP 161
Cdd:PRK11000 83 SYALYPHLSVAENmsfgLK-LAGAKKEEINQ-RVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2753457674 162 TNGLDPAGIRQIRDYLQLLAKEENIAVIVSSHLLSEIELMCDRVVIIKQGEFVQ 215
Cdd:PRK11000 161 LSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQ 214
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
21-217 |
7.42e-25 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 101.72 E-value: 7.42e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 21 IRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLIS---MTEGDITICGHSIRTEREKAL-----EQIGAIVENP--ELY 90
Cdd:PRK09473 32 VNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAangRIGGSATFNGREILNLPEKELnklraEQISMIFQDPmtSLN 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 91 DYM-TG---MQNLKHFANMAITQISKE--RIAEIVKLVElehaIHKKVKTY----SLGMKQRLGIAQALLHQPKILILDE 160
Cdd:PRK09473 112 PYMrVGeqlMEVLMLHKGMSKAEAFEEsvRMLDAVKMPE----ARKRMKMYphefSGGMRQRVMIAMALLCRPKLLIADE 187
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2753457674 161 PTNGLDPAGIRQIRDYLQLLAKEENIAVIVSSHLLSEIELMCDRVVIIKQGEfVQEY 217
Cdd:PRK09473 188 PTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGR-TMEY 243
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-216 |
1.02e-24 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 100.47 E-value: 1.02e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 1 MGNVVVKLENVRKKIGGTE--IIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITIcGHSIRTERE--KA 76
Cdd:PRK13635 1 MKEEIIRVEHISFRYPDAAtyALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITV-GGMVLSEETvwDV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 77 LEQIGAIVENPELY--------DYMTGMQNlkhfanmaiTQISK----ERIAEIVKLVELEHAIHKKVKTYSLGMKQRLG 144
Cdd:PRK13635 80 RRQVGMVFQNPDNQfvgatvqdDVAFGLEN---------IGVPReemvERVDQALRQVGMEDFLNREPHRLSGGQKQRVA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2753457674 145 IAQALLHQPKILILDEPTNGLDPAGIRQIRDYLQLLAKEENIAVIVSSHLLSEIeLMCDRVVIIKQGEFVQE 216
Cdd:PRK13635 151 IAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEA-AQADRVIVMNKGEILEE 221
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
5-216 |
1.11e-24 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 101.42 E-value: 1.11e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 5 VVKLENVRK--KIGGTEII--RGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGHSIRTEREKAL--- 77
Cdd:PRK11153 1 MIELKNISKvfPQGGRTIHalNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELrka 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 78 -EQIGAIVENPELYDYMTGMQN----LKhFANMAITQIsKERIAEIVKLVELEHaihkKVKTY----SLGMKQRLGIAQA 148
Cdd:PRK11153 81 rRQIGMIFQHFNLLSSRTVFDNvalpLE-LAGTPKAEI-KARVTELLELVGLSD----KADRYpaqlSGGQKQRVAIARA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2753457674 149 LLHQPKILILDEPTNGLDPAGIRQIrdyLQLLAK---EENIAVIVSSHLLSEIELMCDRVVIIKQGEFVQE 216
Cdd:PRK11153 155 LASNPKVLLCDEATSALDPATTRSI---LELLKDinrELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQ 222
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
2-217 |
1.31e-24 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 102.79 E-value: 1.31e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 2 GNVVVKLENVRKKiggtEIIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGHSIR----------- 70
Cdd:COG1129 253 GEVVLEVEGLSVG----GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRirsprdairag 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 71 ----TE--REKALEQIGAIVENpelydyMTgMQNLKHFANMAITQISKER--IAEIVKLVELEHA-IHKKVKTYSLGMKQ 141
Cdd:COG1129 329 iayvPEdrKGEGLVLDLSIREN------IT-LASLDRLSRGGLLDRRRERalAEEYIKRLRIKTPsPEQPVGNLSGGNQQ 401
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2753457674 142 RLGIAQALLHQPKILILDEPTNGLDPAGIRQIRDYLQLLAkEENIAVIVSSHLLSEIELMCDRVVIIKQGEFVQEY 217
Cdd:COG1129 402 KVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELA-AEGKAVIVISSELPELLGLSDRILVMREGRIVGEL 476
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
6-229 |
1.59e-24 |
|
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: 98.71 E-value: 1.59e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 6 VKLENV--RKKIGGTEIIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGHSIRTEREKALE-QIGA 82
Cdd:cd03252 1 ITFEHVrfRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRrQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 83 IVENPELYdymtgmqNLKHFANMAITQ--ISKERIAEIVKLVELEHAIHKKVKTY-----------SLGMKQRLGIAQAL 149
Cdd:cd03252 81 VLQENVLF-------NRSIRDNIALADpgMSMERVIEAAKLAGAHDFISELPEGYdtivgeqgaglSGGQRQRIAIARAL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 150 LHQPKILILDEPTNGLDPAGIRQIRDYLQLLAKeeNIAVIVSSHLLSEIelMC-DRVVIIKQGEFVqeynlhEQAKHDET 228
Cdd:cd03252 154 IHNPRILIFDEATSALDYESEHAIMRNMHDICA--GRTVIIIAHRLSTV--KNaDRIIVMEKGRIV------EQGSHDEL 223
|
.
gi 2753457674 229 V 229
Cdd:cd03252 224 L 224
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
6-214 |
1.60e-24 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 102.94 E-value: 1.60e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 6 VKLENVRKKIGGTEIIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGHSIR--TEREKALEQIGAI 83
Cdd:PRK09700 6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNklDHKLAAQLGIGII 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 84 VENPELYDYMTGMQNL-------KHFANMAITQISK--ERIAEIVKLVELEHAIHKKVKTYSLGMKQRLGIAQALLHQPK 154
Cdd:PRK09700 86 YQELSVIDELTVLENLyigrhltKKVCGVNIIDWREmrVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAK 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2753457674 155 ILILDEPTNGLDPAGIrqirDYLQLLA---KEENIAVIVSSHLLSEIELMCDRVVIIKQGEFV 214
Cdd:PRK09700 166 VIIMDEPTSSLTNKEV----DYLFLIMnqlRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSV 224
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
6-211 |
2.11e-24 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 101.07 E-value: 2.11e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 6 VKLENVRKK-IGGTEIIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGHSIrTEREKALEQIGAIV 84
Cdd:PRK11650 4 LKLQAVRKSyDGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVV-NELEPADRDIAMVF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 85 ENPELYDYMTGMQN----LKHfANMAITQIsKERIAEIVKLVELEHAIHKKVKTYSLGMKQRLGIAQALLHQPKILILDE 160
Cdd:PRK11650 83 QNYALYPHMSVRENmaygLKI-RGMPKAEI-EERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLFDE 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2753457674 161 PTNGLDpAGIR-QIRDYLQLLAKEENIAVIVSSHllSEIELM--CDRVVIIKQG 211
Cdd:PRK11650 161 PLSNLD-AKLRvQMRLEIQRLHRRLKTTSLYVTH--DQVEAMtlADRVVVMNGG 211
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
6-212 |
2.44e-24 |
|
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: 95.59 E-value: 2.44e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 6 VKLENVRKKIGGTEIIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITicghsirterekaleqigaive 85
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVT---------------------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 86 npelydymtgmqnlkhfanmaitQISKERIAEIVKLvelehaihkkvktySLGMKQRLGIAQALLHQPKILILDEPTNGL 165
Cdd:cd03221 59 -----------------------WGSTVKIGYFEQL--------------SGGEKMRLALAKLLLENPNLLLLDEPTNHL 101
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2753457674 166 DPAGIRQIRDYLqllaKEENIAVIVSSH---LLSEIelmCDRVVIIKQGE 212
Cdd:cd03221 102 DLESIEALEEAL----KEYPGTVILVSHdryFLDQV---ATKIIELEDGK 144
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
6-248 |
4.16e-24 |
|
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: 101.80 E-value: 4.16e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 6 VKLENVRKKIGGTEIIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISM--TEGDI--------------------- 62
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQYepTSGRIiyhvalcekcgyverpskvge 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 63 --TICGHSIRTER----------EKALEQIGAIV---------ENPELYDYMTGMQNLKHFANMAItqiskERIAEIVKL 121
Cdd:TIGR03269 81 pcPVCGGTLEPEEvdfwnlsdklRRRIRKRIAIMlqrtfalygDDTVLDNVLEALEEIGYEGKEAV-----GRAVDLIEM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 122 VELEHAIHKKVKTYSLGMKQRLGIAQALLHQPKILILDEPTNGLDPAGIRQIRDYLQLLAKEENIAVIVSSHLLSEIELM 201
Cdd:TIGR03269 156 VQLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDL 235
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 2753457674 202 CDRVVIIKQGEFVQEYNlheqakHDETVVVAFE-VDQVQKANEIVQGK 248
Cdd:TIGR03269 236 SDKAIWLENGEIKEEGT------PDEVVAVFMEgVSEVEKECEVEVGE 277
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
4-212 |
4.39e-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: 96.47 E-value: 4.39e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 4 VVVKLENVRKKI------GGTEIIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISM--TEGDITICGHSIRTEREK 75
Cdd:cd03213 2 VTLSFRNLTVTVksspskSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGlgVSGEVLINGRPLDKRSFR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 76 AleQIGAIVENPELYDYMTGMQNLKHFANMaitqiskeriaeivklvelehaihkkvKTYSLGMKQRLGIAQALLHQPKI 155
Cdd:cd03213 82 K--IIGYVPQDDILHPTLTVRETLMFAAKL---------------------------RGLSGGERKRVSIALELVSNPSL 132
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2753457674 156 LILDEPTNGLDPAGIRQIRDYLQLLAKeENIAVIVSSH-LLSEIELMCDRVVIIKQGE 212
Cdd:cd03213 133 LFLDEPTSGLDSSSALQVMSLLRRLAD-TGRTIICSIHqPSSEIFELFDKLLLLSQGR 189
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
16-221 |
4.65e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 98.72 E-value: 4.65e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 16 GGTEIIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGHSIRTEREKALEQ-IGAIVENPELYDYMT 94
Cdd:PRK13652 15 GSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKfVGLVFQNPDDQIFSP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 95 GMQNLKHFA--NMAI-TQISKERIAEIVKLVELEHAIHKKVKTYSLGMKQRLGIAQALLHQPKILILDEPTNGLDPAGIR 171
Cdd:PRK13652 95 TVEQDIAFGpiNLGLdEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVK 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2753457674 172 QIRDYLQLLAKEENIAVIVSSHLLSEIELMCDRVVIIKQGEFVQEYNLHE 221
Cdd:PRK13652 175 ELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEE 224
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
12-216 |
5.46e-24 |
|
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: 101.30 E-value: 5.46e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 12 RKKIGGTEIIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISmTEGDITICGHSIRTEREKALEQ------------ 79
Cdd:COG4172 293 RRTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIP-SEGEIRFDGQDLDGLSRRALRPlrrrmqvvfqdp 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 80 ---------IGAIVENPelydymtgmqnLK-HFANMAITQIsKERIAEIVKLVELEHA-IHKKVKTYSLGMKQRLGIAQA 148
Cdd:COG4172 372 fgslsprmtVGQIIAEG-----------LRvHGPGLSAAER-RARVAEALEEVGLDPAaRHRYPHEFSGGQRQRIAIARA 439
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2753457674 149 LLHQPKILILDEPTNGLDpAGIR-QIRDYLQLLAKEENIAVIVSSHLLSEIELMCDRVVIIKQGEFVQE 216
Cdd:COG4172 440 LILEPKLLVLDEPTSALD-VSVQaQILDLLRDLQREHGLAYLFISHDLAVVRALAHRVMVMKDGKVVEQ 507
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
16-208 |
5.69e-24 |
|
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: 101.21 E-value: 5.69e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 16 GGTEIIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGHSIRTEREKAL-EQIGAIVENPELYdYMT 94
Cdd:TIGR02857 333 GRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWrDQIAWVPQHPFLF-AGT 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 95 GMQNLKHFANMAitqiSKERIAEIVKLV-------ELEHAIHKKV----KTYSLGMKQRLGIAQALLHQPKILILDEPTN 163
Cdd:TIGR02857 412 IAENIRLARPDA----SDAEIREALERAgldefvaALPQGLDTPIgeggAGLSGGQAQRLALARAFLRDAPLLLLDEPTA 487
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2753457674 164 GLDPAGIRQIRDYLQLLAkeENIAVIVSSHLLSEIELMcDRVVII 208
Cdd:TIGR02857 488 HLDAETEAEVLEALRALA--QGRTVLLVTHRLALAALA-DRIVVL 529
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
20-212 |
6.35e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 98.27 E-value: 6.35e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 20 IIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGHSIRTEREKAL-EQIGAIVENPELY-------- 90
Cdd:PRK13650 22 TLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIrHKIGMVFQNPDNQfvgatved 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 91 DYMTGMQN--LKHfanmaitQISKERIAEIVKLVELEHAIHKKVKTYSLGMKQRLGIAQALLHQPKILILDEPTNGLDPA 168
Cdd:PRK13650 102 DVAFGLENkgIPH-------EEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPE 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2753457674 169 GIRQIRDYLQLLAKEENIAVIVSSHLLSEIELmCDRVVIIKQGE 212
Cdd:PRK13650 175 GRLELIKTIKGIRDDYQMTVISITHDLDEVAL-SDRVLVMKNGQ 217
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
6-216 |
6.62e-24 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 97.51 E-value: 6.62e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 6 VKLENVRKKIGGTEIIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGHSIRTER----EKAL---- 77
Cdd:PRK11264 4 IEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTARslsqQKGLirql 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 78 -EQIGAIVENPELYDYMTGMQNL-------KHFANMAITQISKERIAEiVKLVELEHAIHKKVktySLGMKQRLGIAQAL 149
Cdd:PRK11264 84 rQHVGFVFQNFNLFPHRTVLENIiegpvivKGEPKEEATARARELLAK-VGLAGKETSYPRRL---SGGQQQRVAIARAL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2753457674 150 LHQPKILILDEPTNGLDPAGIRQIRDYLQLLAKEENIAVIVsSHLLSEIELMCDRVVIIKQGEFVQE 216
Cdd:PRK11264 160 AMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIV-THEMSFARDVADRAIFMDQGRIVEQ 225
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
24-214 |
7.36e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 98.20 E-value: 7.36e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 24 LSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGHSIRTEREKALE---QIGAIVENPE--LY------DY 92
Cdd:PRK13637 26 VNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKLSDirkKVGLVFQYPEyqLFeetiekDI 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 93 MTGMQNLkhfaNMAITQISKeRIAEIVKLVELEHAIHKKVKTYSL--GMKQRLGIAQALLHQPKILILDEPTNGLDPAGI 170
Cdd:PRK13637 106 AFGPINL----GLSEEEIEN-RVKRAMNIVGLDYEDYKDKSPFELsgGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGR 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2753457674 171 RQIRDYLQLLAKEENIAVIVSSHLLSEIELMCDRVVIIKQGEFV 214
Cdd:PRK13637 181 DEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCE 224
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
3-214 |
1.41e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 96.98 E-value: 1.41e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 3 NVVVKLENVRKKIGGTE--IIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGHSIRTEREKAL-EQ 79
Cdd:PRK13632 5 SVMIKVENVSFSYPNSEnnALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIrKK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 80 IGAIVENPELY--------DYMTGMQNlkhfaNMAITQISKERIAEIVKLVELEHAIHKKVKTYSLGMKQRLGIAQALLH 151
Cdd:PRK13632 85 IGIIFQNPDNQfigatvedDIAFGLEN-----KKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLAL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2753457674 152 QPKILILDEPTNGLDPAGIRQIRDYLQLLAKEENIAVIVSSHLLSEIeLMCDRVVIIKQGEFV 214
Cdd:PRK13632 160 NPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEA-ILADKVIVFSEGKLI 221
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
6-227 |
1.73e-23 |
|
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: 96.15 E-value: 1.73e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 6 VKLENVR-KKIGGTEIIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGHSIRTEREKAL-EQIGAI 83
Cdd:cd03253 1 IEFENVTfAYDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLrRAIGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 84 VENPELYDyMTGMQNLKhFANMAITQISKERIAEIVKlvelehaIHKKVKTY---------------SLGMKQRLGIAQA 148
Cdd:cd03253 81 PQDTVLFN-DTIGYNIR-YGRPDATDEEVIEAAKAAQ-------IHDKIMRFpdgydtivgerglklSGGEKQRVAIARA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2753457674 149 LLHQPKILILDEPTNGLDPAGIRQIRDYLQLLAKeeNIAVIVSSHLLSEIeLMCDRVVIIKQGEFVqeynlhEQAKHDE 227
Cdd:cd03253 152 ILKNPPILLLDEATSALDTHTEREIQAALRDVSK--GRTTIVIAHRLSTI-VNADKIIVLKDGRIV------ERGTHEE 221
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-216 |
1.81e-23 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 96.10 E-value: 1.81e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 1 MGNVVVKLENVRKKIGGTEIIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGHSIrTEREKA---L 77
Cdd:PRK11614 1 MEKVMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDI-TDWQTAkimR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 78 EQIGAIVENPELYDYMTGMQNLKHFANMAITQISKERIAEIVKLV-ELEHAIHKKVKTYSLGMKQRLGIAQALLHQPKIL 156
Cdd:PRK11614 80 EAVAIVPEGRRVFSRMTVEENLAMGGFFAERDQFQERIKWVYELFpRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 157 ILDEPTNGLDPAGIRQIRDYLQLLaKEENIAVIVSSHLLSEIELMCDRVVIIKQGEFVQE 216
Cdd:PRK11614 160 LLDEPSLGLAPIIIQQIFDTIEQL-REQGMTIFLVEQNANQALKLADRGYVLENGHVVLE 218
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
5-283 |
1.91e-23 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 98.75 E-value: 1.91e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 5 VVKLENVRKKIGGTEIIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGHSIrTEREKALEQIGAIV 84
Cdd:PRK11607 19 LLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDL-SHVPPYQRPINMMF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 85 ENPELYDYMTGMQN----LKHfANMAITQIsKERIAEIVKLVELEHAIHKKVKTYSLGMKQRLGIAQALLHQPKILILDE 160
Cdd:PRK11607 98 QSYALFPHMTVEQNiafgLKQ-DKLPKAEI-ASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDE 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 161 PTNGLDpagiRQIRDYLQLLAKE--ENIAV--IVSSHLLSEIELMCDRVVIIKQGEFVQEYNLHEQAKHDETVVVAFEVD 236
Cdd:PRK11607 176 PMGALD----KKLRDRMQLEVVDilERVGVtcVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAEFIG 251
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 2753457674 237 QVQKANEIVQGKAQGNVILVSvtkeeiPQLVKKL-VNDDV-LVYGVTVQ 283
Cdd:PRK11607 252 SVNVFEGVLKERQEDGLVIDS------PGLVHPLkVDADAsVVDNVPVH 294
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
6-227 |
2.54e-23 |
|
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: 95.38 E-value: 2.54e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 6 VKLENVRKKIGGTE--IIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGHSIRTEREKAL-EQIGA 82
Cdd:cd03251 1 VEFKNVTFRYPGDGppVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLrRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 83 IVENPELYDyMTGMQNLKHfanmAITQISKERIAEIVKLVELEHAIHKKVKTY-----------SLGMKQRLGIAQALLH 151
Cdd:cd03251 81 VSQDVFLFN-DTVAENIAY----GRPGATREEVEEAARAANAHEFIMELPEGYdtvigergvklSGGQRQRIAIARALLK 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2753457674 152 QPKILILDEPTNGLDPAGIRQIRDYLQLLAKeeNIAVIVSSHLLSEIElMCDRVVIIKQGEFVqeynlhEQAKHDE 227
Cdd:cd03251 156 DPPILILDEATSALDTESERLVQAALERLMK--NRTTFVIAHRLSTIE-NADRIVVLEDGKIV------ERGTHEE 222
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
17-216 |
4.20e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 95.96 E-value: 4.20e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 17 GTEIIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGHSIRTEREKALE-QIGAIVENPElyDYMTG 95
Cdd:PRK13647 17 GTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRsKVGLVFQDPD--DQVFS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 96 MQNLKHFA----NMAITQIS-KERIAEIVKLVELEHAIHKKVKTYSLGMKQRLGIAQALLHQPKILILDEPTNGLDPAGI 170
Cdd:PRK13647 95 STVWDDVAfgpvNMGLDKDEvERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQ 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2753457674 171 RQIRDYLQLLAKEENiAVIVSSHLLSEIELMCDRVVIIKQGEFVQE 216
Cdd:PRK13647 175 ETLMEILDRLHNQGK-TVIVATHDVDLAAEWADQVIVLKEGRVLAE 219
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
6-212 |
5.64e-23 |
|
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: 94.01 E-value: 5.64e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 6 VKLENVRKKI-GGTEIIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGHSIRTEREKAL----EQI 80
Cdd:cd03292 1 IEFINVTKTYpNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIpylrRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 81 GAIVENPELYDYMTGMQNLKhFAnMAITQIS----KERIAEIVKLVELEHAIHKKVKTYSLGMKQRLGIAQALLHQPKIL 156
Cdd:cd03292 81 GVVFQDFRLLPDRNVYENVA-FA-LEVTGVPpreiRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTIL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2753457674 157 ILDEPTNGLDPAGIRQIRDYLQLLAKeENIAVIVSSHLLSEIELMCDRVVIIKQGE 212
Cdd:cd03292 159 IADEPTGNLDPDTTWEIMNLLKKINK-AGTTVVVATHAKELVDTTRHRVIALERGK 213
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
20-229 |
5.71e-23 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 98.64 E-value: 5.71e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 20 IIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGHSIRTEREKAL-EQIGAIVENPELYDymtgmQN 98
Cdd:TIGR00958 496 VLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLhRQVALVGQEPVLFS-----GS 570
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 99 LKHFANMAITQISKERIAEIVKLVELEHAIHKKVKTY-----------SLGMKQRLGIAQALLHQPKILILDEPTNGLDP 167
Cdd:TIGR00958 571 VRENIAYGLTDTPDEEIMAAAKAANAHDFIMEFPNGYdtevgekgsqlSGGQKQRIAIARALVRKPRVLILDEATSALDA 650
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2753457674 168 agirQIRDYLQLLAKEENIAVIVSSHLLSEIElMCDRVVIIKQGEfVQEYNLHEQAKHDETV 229
Cdd:TIGR00958 651 ----ECEQLLQESRSRASRTVLLIAHRLSTVE-RADQILVLKKGS-VVEMGTHKQLMEDQGC 706
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-230 |
6.04e-23 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 94.80 E-value: 6.04e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 1 MGNVVVKLENVRKKIGGTEIIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGHSIRTEREKALEQ- 79
Cdd:COG4674 6 MHGPILYVEDLTVSFDGFKALNDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTRPDSGSVLFGGTDLTGLDEHEIARl 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 80 -IGAIVENPELYDYMTGMQNL--------KHFANMA--ITQISKERIAEIVKLVELEHAIHKKVKTYSLGMKQRLGIAQA 148
Cdd:COG4674 86 gIGRKFQKPTVFEELTVFENLelalkgdrGVFASLFarLTAEERDRIEEVLETIGLTDKADRLAGLLSHGQKQWLEIGML 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 149 LLHQPKILILDEPTNGLDPAGIRQIRDYLQLLAKEEniAVIVSSHLLSEIELMCDRVVIIKQGEFVQEYNLhEQAKHDET 228
Cdd:COG4674 166 LAQDPKLLLLDEPVAGMTDAETERTAELLKSLAGKH--SVVVVEHDMEFVRQIARKVTVLHQGSVLAEGSL-DEVQADPR 242
|
..
gi 2753457674 229 VV 230
Cdd:COG4674 243 VI 244
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1-215 |
9.56e-23 |
|
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: 97.95 E-value: 9.56e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 1 MGNVVVKLENVRKKI-----GGTEIIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEG-----------DITI 64
Cdd:TIGR03269 275 VGEPIIKVRNVSKRYisvdrGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGevnvrvgdewvDMTK 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 65 CGHSirtEREKALEQIGAIVENPELYDYMTGMQNLKHFANMAIT-QISKERIAEIVKLV-----ELEHAIHKKVKTYSLG 138
Cdd:TIGR03269 355 PGPD---GRGRAKRYIGILHQEYDLYPHRTVLDNLTEAIGLELPdELARMKAVITLKMVgfdeeKAEEILDKYPDELSEG 431
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2753457674 139 MKQRLGIAQALLHQPKILILDEPTNGLDPAGIRQIRDYLQLLAKEENIAVIVSSHLLSEIELMCDRVVIIKQGEFVQ 215
Cdd:TIGR03269 432 ERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVK 508
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
18-216 |
1.12e-22 |
|
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: 92.38 E-value: 1.12e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 18 TEIIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGHSIRTEREKALEQIGAIVENPELYDyMTGMQ 97
Cdd:cd03247 15 QQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSLISVLNQRPYLFD-TTLRN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 98 NLKhfanmaitqiskeriaeivklvelehaihkkvKTYSLGMKQRLGIAQALLHQPKILILDEPTNGLDPAGIRQIrdyL 177
Cdd:cd03247 94 NLG--------------------------------RRFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQL---L 138
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2753457674 178 QLLAKE-ENIAVIVSSHLLSEIELMcDRVVIIKQGEFVQE 216
Cdd:cd03247 139 SLIFEVlKDKTLIWITHHLTGIEHM-DKILFLENGKIIMQ 177
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
3-215 |
1.98e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 93.75 E-value: 1.98e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 3 NVVVKLENVRKKIGGTEIIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMT-----EGDITICGHSIRTEREKAL 77
Cdd:PRK14267 2 KFAIETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNeearvEGEVRLFGRNIYSPDVDPI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 78 E---QIGAIVENPELYDYMTGMQNLKHFANMAITQISKERIAEIVKLVELEHAIHKKVK--------TYSLGMKQRLGIA 146
Cdd:PRK14267 82 EvrrEVGMVFQYPNPFPHLTIYDNVAIGVKLNGLVKSKKELDERVEWALKKAALWDEVKdrlndypsNLSGGQRQRLVIA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2753457674 147 QALLHQPKILILDEPTNGLDPAGIRQIRDYLQLLAKEENIAVIvsSHLLSEIELMCDRVVIIKQGEFVQ 215
Cdd:PRK14267 162 RALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLV--THSPAQAARVSDYVAFLYLGKLIE 228
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
12-216 |
2.70e-22 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 96.70 E-value: 2.70e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 12 RKKIGGTEIIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISmTEGDITICGHSIRTEREKAL----EQIGAIVENP 87
Cdd:PRK15134 293 KRTVDHNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLIN-SQGEIWFDGQPLHNLNRRQLlpvrHRIQVVFQDP 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 88 --ELYDYMTGMQNLK-----HFANMAITQiSKERIAEIVKLVELEHAI-HKKVKTYSLGMKQRLGIAQALLHQPKILILD 159
Cdd:PRK15134 372 nsSLNPRLNVLQIIEeglrvHQPTLSAAQ-REQQVIAVMEEVGLDPETrHRYPAEFSGGQRQRIAIARALILKPSLIILD 450
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2753457674 160 EPTNGLDPAGIRQIRDYLQLLAKEENIAVIVSSHLLSEIELMCDRVVIIKQGEFVQE 216
Cdd:PRK15134 451 EPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQ 507
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
5-211 |
2.71e-22 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 92.85 E-value: 2.71e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 5 VVKLENVRKKIGGTEIIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGHSIR----TEREKALEQi 80
Cdd:PRK09493 1 MIEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNdpkvDERLIRQEA- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 81 GAIVENPELYDYMTGMQNLKhFANMAITQISK---ERIA-EIVKLVELEHAIHKKVKTYSLGMKQRLGIAQALLHQPKIL 156
Cdd:PRK09493 80 GMVFQQFYLFPHLTALENVM-FGPLRVRGASKeeaEKQArELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLM 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2753457674 157 ILDEPTNGLDPAGIRQIRDYLQLLAkEENIAVIVSSHLLSEIELMCDRVVIIKQG 211
Cdd:PRK09493 159 LFDEPTSALDPELRHEVLKVMQDLA-EEGMTMVIVTHEIGFAEKVASRLIFIDKG 212
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
6-222 |
2.99e-22 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 96.32 E-value: 2.99e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 6 VKLENVRKKIGGTEI--IRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGHSIRTEREKALE-QIGA 82
Cdd:TIGR02203 331 VEFRNVTFRYPGRDRpaLDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASLRrQVAL 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 83 IVENPELYDYMTgmqnlkhFANMA---ITQISKERIAEIVK---LVELEHAIHKKVKT--------YSLGMKQRLGIAQA 148
Cdd:TIGR02203 411 VSQDVVLFNDTI-------ANNIAygrTEQADRAEIERALAaayAQDFVDKLPLGLDTpigengvlLSGGQRQRLAIARA 483
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2753457674 149 LLHQPKILILDEPTNGLDPAGIRQIRDYLQLLAKEENIAVIvsSHLLSEIElMCDRVVIIKQGEFVqEYNLHEQ 222
Cdd:TIGR02203 484 LLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVI--AHRLSTIE-KADRIVVMDDGRIV-ERGTHNE 553
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
7-216 |
5.74e-22 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 92.05 E-value: 5.74e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 7 KLENVRKKIGGTEIIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLIS--MTEGDITICGHSIrTER---EKALEQIG 81
Cdd:COG0396 2 EIKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPKyeVTSGSILLDGEDI-LELspdERARAGIF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 82 aivenpelydymTGMQN--------LKHFANMAITQISKERI--AEIVKLVelehaihkKVKTYSLGM------------ 139
Cdd:COG0396 81 ------------LAFQYpveipgvsVSNFLRTALNARRGEELsaREFLKLL--------KEKMKELGLdedfldryvneg 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 140 -----KQRLGIAQALLHQPKILILDEPTNGLDPAGIRQIRDYLQLLAKEENiAVIVSSH---LLSEIElmCDRVVIIKQG 211
Cdd:COG0396 141 fsggeKKRNEILQMLLLEPKLAILDETDSGLDIDALRIVAEGVNKLRSPDR-GILIITHyqrILDYIK--PDFVHVLVDG 217
|
....*
gi 2753457674 212 EFVQE 216
Cdd:COG0396 218 RIVKS 222
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
9-206 |
5.76e-22 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 91.09 E-value: 5.76e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 9 ENVRKKIGGTEIIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGHSIRTERekALEQIGAIVENPE 88
Cdd:PRK13539 6 EDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPD--VAEACHYLGHRNA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 89 LYDYMTGMQNLKHFANMAITqiSKERIAEIVKLVELEHAIHKKVKTYSLGMKQRLGIAQALLHQPKILILDEPTNGLDPA 168
Cdd:PRK13539 84 MKPALTVAENLEFWAAFLGG--EELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAA 161
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2753457674 169 GIRQ----IRDYLqllakEENIAVIVSSHllSEIELMCDRVV 206
Cdd:PRK13539 162 AVALfaelIRAHL-----AQGGIVIAATH--IPLGLPGAREL 196
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
16-195 |
1.14e-21 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 94.73 E-value: 1.14e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 16 GGTEIIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGHSIRTEREKALEQ-IGAIVENPELYDyMT 94
Cdd:TIGR02868 346 GAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRrVSVCAQDAHLFD-TT 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 95 GMQNLKhFANMAITQISKERIAEIVKLVE----LEHAIHKKV----KTYSLGMKQRLGIAQALLHQPKILILDEPTNGLD 166
Cdd:TIGR02868 425 VRENLR-LARPDATDEELWAALERVGLADwlraLPDGLDTVLgeggARLSGGERQRLALARALLADAPILLLDEPTEHLD 503
|
170 180 190
....*....|....*....|....*....|
gi 2753457674 167 P-AGIRQIRDylqLLAKEENIAVIVSSHLL 195
Cdd:TIGR02868 504 AeTADELLED---LLAALSGRTVVLITHHL 530
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
9-283 |
1.53e-21 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 93.56 E-value: 1.53e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 9 ENVRKKIGGTEIIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGHSIRT-----EREKALEQIGAI 83
Cdd:PRK10070 32 EQILEKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKisdaeLREVRRKKIAMV 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 84 VENPELYDYMTGMQNLKHFANMA--ITQISKERIAEIVKLVELEHAIHKKVKTYSLGMKQRLGIAQALLHQPKILILDEP 161
Cdd:PRK10070 112 FQSFALMPHMTVLDNTAFGMELAgiNAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEA 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 162 TNGLDPAGIRQIRDYLQLLAKEENIAVIVSSHLLSEIELMCDRVVIIKQGEFVQ-----EYNLHEQAKHDETVVVAFEVD 236
Cdd:PRK10070 192 FSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQvgtpdEILNNPANDYVRTFFRGVDIS 271
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 2753457674 237 QVQKANEIVQGKAQGnviLVSVTKEEIPQLVKKLVNDDVLVYGVTVQ 283
Cdd:PRK10070 272 QVFSAKDIARRTPNG---LIRKTPGFGPRSALKLLQDEDREYGYVIE 315
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
6-216 |
1.84e-21 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 90.84 E-value: 1.84e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 6 VKLENVRKKIGGTEIIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGHS------IRTEREKALEQ 79
Cdd:COG4161 3 IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQfdfsqkPSEKAIRLLRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 80 -IGAIVENPELYDYMTGMQNLKHfANMAITQISK----ERIAEIVKLVELEHAIHKKVKTYSLGMKQRLGIAQALLHQPK 154
Cdd:COG4161 83 kVGMVFQQYNLWPHLTVMENLIE-APCKVLGLSKeqarEKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQ 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2753457674 155 ILILDEPTNGLDPAGIRQIRDYLQLLAKEENIAVIVsSHllsEIEL---MCDRVVIIKQGEFVQE 216
Cdd:COG4161 162 VLLFDEPTAALDPEITAQVVEIIRELSQTGITQVIV-TH---EVEFarkVASQVVYMEKGRIIEQ 222
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1-211 |
1.94e-21 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 90.82 E-value: 1.94e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 1 MGNVVVKLENVRKKIGGTEIIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGHSIRTEREKALEQI 80
Cdd:PRK11300 1 MSQPLLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIARM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 81 GAI--VENPELYDYMTGMQNL---KH-----------FANMAITQISKE---RIAEIVKLVELEHAIHKKVKTYSLGMKQ 141
Cdd:PRK11300 81 GVVrtFQHVRLFREMTVIENLlvaQHqqlktglfsglLKTPAFRRAESEaldRAATWLERVGLLEHANRQAGNLAYGQQR 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 142 RLGIAQALLHQPKILILDEPTNGLDPAGIRQIRDYLQLLAKEENIAVIVSSHLLSEIELMCDRVVIIKQG 211
Cdd:PRK11300 161 RLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQG 230
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
16-194 |
4.81e-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: 88.70 E-value: 4.81e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 16 GGTEIIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGHSIRTEREKALEQIGAIVENPELYDYMTG 95
Cdd:cd03231 11 DGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTLSV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 96 MQNLKHFANMAITQISKERIAEiVKLVELEHAIhkkVKTYSLGMKQRLGIAQALLHQPKILILDEPTNGLDPAGIRQIrd 175
Cdd:cd03231 91 LENLRFWHADHSDEQVEEALAR-VGLNGFEDRP---VAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARF-- 164
|
170 180
....*....|....*....|.
gi 2753457674 176 yLQLLAK--EENIAVIVSSHL 194
Cdd:cd03231 165 -AEAMAGhcARGGMVVLTTHQ 184
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
5-210 |
5.79e-21 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 89.40 E-value: 5.79e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 5 VVKLENVRKKIGGTEIIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDIticghsirtEREKALeQIGAIV 84
Cdd:PRK09544 4 LVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI---------KRNGKL-RIGYVP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 85 EnpELYDYMTGMQNLKHFANMAiTQISKERIAEIVKLVELEHAIHKKVKTYSLGMKQRLGIAQALLHQPKILILDEPTNG 164
Cdd:PRK09544 74 Q--KLYLDTTLPLTVNRFLRLR-PGTKKEDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQG 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2753457674 165 LDPAGIRQIRDYLQLLAKEENIAVIVSSHLLSEIELMCDRVVIIKQ 210
Cdd:PRK09544 151 VDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCLNH 196
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1-227 |
6.51e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 89.81 E-value: 6.51e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 1 MGNVVVKLENVRKKIGGTE--IIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGHSIRTEREKALE 78
Cdd:PRK13648 3 DKNSIIVFKNVSFQYQSDAsfTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 79 Q-IGAIVENPE--------LYDYMTGMQNlkhfaNMAITQISKERIAEIVKLVELEHAIHKKVKTYSLGMKQRLGIAQAL 149
Cdd:PRK13648 83 KhIGIVFQNPDnqfvgsivKYDVAFGLEN-----HAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2753457674 150 LHQPKILILDEPTNGLDPAGIRQIRDYLQLLAKEENIAVIVSSHLLSEiELMCDRVVIIKQGEFVQEYNLHEQAKHDE 227
Cdd:PRK13648 158 ALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSE-AMEADHVIVMNKGTVYKEGTPTEIFDHAE 234
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
6-212 |
7.50e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 89.71 E-value: 7.50e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 6 VKLENVRKKIGGTEIIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISM-----TEGDITICGHSIRTER---EKAL 77
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELesevrVEGRVEFFNQNIYERRvnlNRLR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 78 EQIGAIVENPEL-----YDYMT-GMQNLKHFANMAITQISKERIAEIVKLVELEHAIHKKVKTYSLGMKQRLGIAQALLH 151
Cdd:PRK14258 88 RQVSMVHPKPNLfpmsvYDNVAyGVKIVGWRPKLEIDDIVESALKDADLWDEIKHKIHKSALDLSGGQQQRLCIARALAV 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2753457674 152 QPKILILDEPTNGLDPAGIRQIRDYLQLLAKEENIAVIVSSHLLSEIELMCDRVVIIKQGE 212
Cdd:PRK14258 168 KPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGNE 228
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
7-212 |
8.54e-21 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 88.66 E-value: 8.54e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 7 KLENVRKKIGGTEIirGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGHSIrTEREKALEQIgAIV-- 84
Cdd:COG3840 3 RLDDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDL-TALPPAERPV-SMLfq 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 85 ENpELYDYMTGMQNLK---HfANMAITQISKERIAEIVKLVELEHAIHKKVKTYSLGMKQRLGIAQALLHQPKILILDEP 161
Cdd:COG3840 79 EN-NLFPHLTVAQNIGlglR-PGLKLTAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEP 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2753457674 162 TNGLDPAGIRQIRDYLQLLAKEENIAVIVSSHLLSEIELMCDRVVIIKQGE 212
Cdd:COG3840 157 FSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGR 207
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
16-214 |
1.11e-20 |
|
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: 91.67 E-value: 1.11e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 16 GGTEIIRGLSFEVREGEVYGFLGPNGSGKTTT----IRMMTGLISMTEGDITICGHSIRTEREKALEQ-----IGAIVEN 86
Cdd:COG4172 21 GTVEAVKGVSFDIAAGETLALVGESGSGKSVTalsiLRLLPDPAAHPSGSILFDGQDLLGLSERELRRirgnrIAMIFQE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 87 PelydyMT--------GMQ---NLKHFANMAITQIsKERIAEIVKLVELEHAiHKKVKTY----SLGMKQRLGIAQALLH 151
Cdd:COG4172 101 P-----MTslnplhtiGKQiaeVLRLHRGLSGAAA-RARALELLERVGIPDP-ERRLDAYphqlSGGQRQRVMIAMALAN 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2753457674 152 QPKILILDEPTNGLDPAGIRQIRDYLQLLAKEENIAVIVSSHLLSEIELMCDRVVIIKQGEFV 214
Cdd:COG4172 174 EPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFADRVAVMRQGEIV 236
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
6-214 |
1.37e-20 |
|
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: 87.55 E-value: 1.37e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 6 VKLENVRKKIGGTEIIRGLSFEvrEGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGHSIrTEREKALEQIGAIVE 85
Cdd:cd03298 1 VRLDKIRFSYGEQPMHFDLTFA--QGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDV-TAAPPADRPVSMLFQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 86 NPELYDYMTGMQN--LKHFANMAITQISKERIAEIVKLVELEHAIHKKVKTYSLGMKQRLGIAQALLHQPKILILDEPTN 163
Cdd:cd03298 78 ENNLFAHLTVEQNvgLGLSPGLKLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFA 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2753457674 164 GLDPAGIRQIRDYLQLLAKEENIAVIVSSHLLSEIELMCDRVVIIKQGEFV 214
Cdd:cd03298 158 ALDPALRAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIA 208
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
6-211 |
1.60e-20 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 90.67 E-value: 1.60e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 6 VKLENVRKKIGGTEIIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGHSIRTEREKALEQIGAIV- 84
Cdd:PRK09536 4 IDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVp 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 85 -ENPELYDY-------MTGMQNLKHFANMaiTQISKERIAEIVKLVELEHAIHKKVKTYSLGMKQRLGIAQALLHQPKIL 156
Cdd:PRK09536 84 qDTSLSFEFdvrqvveMGRTPHRSRFDTW--TETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2753457674 157 ILDEPTNGLDPAgiRQIRDyLQLLAK--EENIAVIVSSHLLSEIELMCDRVVIIKQG 211
Cdd:PRK09536 162 LLDEPTASLDIN--HQVRT-LELVRRlvDDGKTAVAAIHDLDLAARYCDELVLLADG 215
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
22-193 |
1.67e-20 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 87.17 E-value: 1.67e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 22 RGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGHSIRTEREKALEQ---IG---AIveNPELydymTG 95
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQDllyLGhqpGI--KTEL----TA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 96 MQNLKhfANMAITQ-ISKERIAEI---VKLVELEHAihkKVKTYSLGMKQRLGIAQALLHQPKILILDEPTNGLDPAGIR 171
Cdd:PRK13538 92 LENLR--FYQRLHGpGDDEALWEAlaqVGLAGFEDV---PVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGVA 166
|
170 180
....*....|....*....|....
gi 2753457674 172 QIrdyLQLLAK--EENIAVIVSSH 193
Cdd:PRK13538 167 RL---EALLAQhaEQGGMVILTTH 187
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-214 |
1.89e-20 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 91.14 E-value: 1.89e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 1 MGNVVVKLENVRKKIGGTEIIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLI--SMTEGDITICGHSIRTEREKALE 78
Cdd:PRK13549 1 MMEYLLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYphGTYEGEIIFEGEELQASNIRDTE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 79 QIGAIVENPEL--YDYMTGMQNL-----------KHFANMAItqiskeRIAEIVKLVELEHAIHKKVKTYSLGMKQRLGI 145
Cdd:PRK13549 81 RAGIAIIHQELalVKELSVLENIflgneitpggiMDYDAMYL------RAQKLLAQLKLDINPATPVGNLGLGQQQLVEI 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2753457674 146 AQALLHQPKILILDEPTNGLDPAGIRQIRDYLQLLaKEENIAVIVSSHLLSEIELMCDRVVIIKQGEFV 214
Cdd:PRK13549 155 AKALNKQARLLILDEPTASLTESETAVLLDIIRDL-KAHGIACIYISHKLNEVKAISDTICVIRDGRHI 222
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
10-216 |
1.90e-20 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 88.59 E-value: 1.90e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 10 NVRKKIGGTEIIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGHSI---RTEREKALEQ------- 79
Cdd:PRK10419 17 GLSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLaklNRAQRKAFRRdiqmvfq 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 80 -----------IGAIVENPelydymtgmqnLKHFANMAITQiSKERIAEIVKLVEL--EHAiHKKVKTYSLGMKQRLGIA 146
Cdd:PRK10419 97 dsisavnprktVREIIREP-----------LRHLLSLDKAE-RLARASEMLRAVDLddSVL-DKRPPQLSGGQLQRVCLA 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 147 QALLHQPKILILDEPTNGLDPAGIRQIRDYLQLLAKEENIAVIVSSHLLSEIELMCDRVVIIKQGEFVQE 216
Cdd:PRK10419 164 RALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVET 233
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
38-211 |
3.34e-20 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 89.16 E-value: 3.34e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 38 GPNGSGKTTTIRMMTGLISMTEGDITICGHS-IRTEREKAL--EQ--IGAIVENPELYDYMTGMQNLKHfanmAITQISK 112
Cdd:PRK11144 31 GRSGAGKTSLINAISGLTRPQKGRIVLNGRVlFDAEKGICLppEKrrIGYVFQDARLFPHYKVRGNLRY----GMAKSMV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 113 ERIAEIVKLVELEHAIHKKVKTYSLGMKQRLGIAQALLHQPKILILDEPTNGLDPAGIRQIRDYLQLLAKEENIAVIVSS 192
Cdd:PRK11144 107 AQFDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLERLAREINIPILYVS 186
|
170
....*....|....*....
gi 2753457674 193 HLLSEIELMCDRVVIIKQG 211
Cdd:PRK11144 187 HSLDEILRLADRVVVLEQG 205
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
6-215 |
4.77e-20 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 86.99 E-value: 4.77e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 6 VKLENVRKKIGGTEIIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGHSI---RTEREKALEQ--- 79
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFdfsKTPSDKAIRElrr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 80 -IGAIVENPELYDYMTGMQNLKHfANMAITQISKE----RIAEIVKLVELEHAIHKKVKTYSLGMKQRLGIAQALLHQPK 154
Cdd:PRK11124 83 nVGMVFQQYNLWPHLTVQQNLIE-APCRVLGLSKDqalaRAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQ 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2753457674 155 ILILDEPTNGLDPAGIRQIRDYLQLLAkEENIAVIVSSHllsEIEL---MCDRVVIIKQGEFVQ 215
Cdd:PRK11124 162 VLLFDEPTAALDPEITAQIVSIIRELA-ETGITQVIVTH---EVEVarkTASRVVYMENGHIVE 221
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
18-219 |
5.60e-20 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 86.41 E-value: 5.60e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 18 TEIIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGHSIRTEREKAL-----EQIGAIVENPELYDY 92
Cdd:PRK11629 22 TDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKaelrnQKLGFIYQFHHLLPD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 93 MTGMQNLKH---FANMAITQIsKERIAEIVKLVELEHAIHKKVKTYSLGMKQRLGIAQALLHQPKILILDEPTNGLDPAG 169
Cdd:PRK11629 102 FTALENVAMpllIGKKKPAEI-NSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARN 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2753457674 170 IRQIRDYLQLLAKEENIAVIVSSHLLSEIELMcDRVVIIKQGEFVQEYNL 219
Cdd:PRK11629 181 ADSIFQLLGELNRLQGTAFLVVTHDLQLAKRM-SRQLEMRDGRLTAELSL 229
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
18-212 |
5.79e-20 |
|
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: 86.37 E-value: 5.79e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 18 TEIIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGHSIRTEREKAL-EQIGAIVENPELYDymtgm 96
Cdd:cd03248 27 TLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLhSKVSLVGQEPVLFA----- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 97 QNLKHFANMAITQISKERIAEIVK-------LVELEHAIHKKV----KTYSLGMKQRLGIAQALLHQPKILILDEPTNGL 165
Cdd:cd03248 102 RSLQDNIAYGLQSCSFECVKEAAQkahahsfISELASGYDTEVgekgSQLSGGQKQRVAIARALIRNPQVLILDEATSAL 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2753457674 166 DPAGIRQIRDYLQllAKEENIAVIVSSHLLSEIElMCDRVVIIKQGE 212
Cdd:cd03248 182 DAESEQQVQQALY--DWPERRTVLVIAHRLSTVE-RADQILVLDGGR 225
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
23-215 |
6.43e-20 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 88.22 E-value: 6.43e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 23 GLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGHSIRTEREKAL----EQIGAIVENP--ELYDYMT-G 95
Cdd:PRK15079 39 GVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWravrSDIQMIFQDPlaSLNPRMTiG 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 96 ---MQNLKHFANMAITQISKERIAEIVKLVEL-EHAIHKKVKTYSLGMKQRLGIAQALLHQPKILILDEPTNGLDPAGIR 171
Cdd:PRK15079 119 eiiAEPLRTYHPKLSRQEVKDRVKAMMLKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQA 198
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2753457674 172 QIRDYLQLLAKEENIAVIVSSHLLSEIELMCDRVVIIKQGEFVQ 215
Cdd:PRK15079 199 QVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVE 242
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
5-211 |
6.67e-20 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 89.34 E-value: 6.67e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 5 VVKLENVRKKIGGTEIIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGHSI-RTEREKAlEQIGA- 82
Cdd:PRK15439 11 LLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCaRLTPAKA-HQLGIy 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 83 -IVENPELYDYMTGMQNLkhFANMAITQISKERIAEIVKLVELEHAIHKKVKTYSLGMKQRLGIAQALLHQPKILILDEP 161
Cdd:PRK15439 90 lVPQEPLLFPNLSVKENI--LFGLPKRQASMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILILDEP 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2753457674 162 TNGLDPAGI----RQIRdylQLLAKEENIAVIvsSHLLSEIELMCDRVVIIKQG 211
Cdd:PRK15439 168 TASLTPAETerlfSRIR---ELLAQGVGIVFI--SHKLPEIRQLADRISVMRDG 216
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
3-223 |
7.81e-20 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 85.92 E-value: 7.81e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 3 NVVVKLENVRKKIGGTEIIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGHSIRT-EREKALEQIG 81
Cdd:PRK10247 5 SPLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTlKPEIYRQQVS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 82 AIVENPELYDYmTGMQNLKHFANMAITQISKERIAEIVKLVEL-EHAIHKKVKTYSLGMKQRLGIAQALLHQPKILILDE 160
Cdd:PRK10247 85 YCAQTPTLFGD-TVYDNLIFPWQIRNQQPDPAIFLDDLERFALpDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDE 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2753457674 161 PTNGLDPAGIRQIRDYLQLLAKEENIAVIVSSHLLSEIElMCDRVVIIK-QGEFVQEYNlHEQA 223
Cdd:PRK10247 164 ITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDEIN-HADKVITLQpHAGEMQEAR-YELA 225
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
21-216 |
8.92e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 87.07 E-value: 8.92e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 21 IRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGhsIRTEREKALEQI----GAIVENPELYDYMTGM 96
Cdd:PRK13633 26 LDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDG--LDTSDEENLWDIrnkaGMVFQNPDNQIVATIV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 97 QNLKHFA--NMAITQIS-KERIAEIVKLVEL----EHAIHkkvkTYSLGMKQRLGIAQALLHQPKILILDEPTNGLDPAG 169
Cdd:PRK13633 104 EEDVAFGpeNLGIPPEEiRERVDESLKKVGMyeyrRHAPH----LLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSG 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2753457674 170 IRQIRDYLQLLAKEENIAVIVSSHLLSEIeLMCDRVVIIKQGEFVQE 216
Cdd:PRK13633 180 RREVVNTIKELNKKYGITIILITHYMEEA-VEADRIIVMDSGKVVME 225
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
2-214 |
9.50e-20 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 88.93 E-value: 9.50e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 2 GNVVVKLENVR-KKIGGTEIIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGH-----SIRTEREK 75
Cdd:COG3845 254 GEVVLEVENLSvRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEditglSPRERRRL 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 76 ALEQI-------GAIVEnpelydyMTGMQN--LKHFANMAITQ---ISKERIAEIVK-LVElEHAI-----HKKVKTYSL 137
Cdd:COG3845 334 GVAYIpedrlgrGLVPD-------MSVAENliLGRYRRPPFSRggfLDRKAIRAFAEeLIE-EFDVrtpgpDTPARSLSG 405
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2753457674 138 GMKQRLGIAQALLHQPKILILDEPTNGLDPAGIRQIRDYLqLLAKEENIAVIVSSHLLSEIELMCDRVVIIKQGEFV 214
Cdd:COG3845 406 GNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRL-LELRDAGAAVLLISEDLDEILALSDRIAVMYEGRIV 481
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
2-217 |
1.19e-19 |
|
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: 85.24 E-value: 1.19e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 2 GNVVVKLENVRKKIGGTEIIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGHSIRTEREKAL-EQI 80
Cdd:cd03244 1 GDIEFKNVSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLrSRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 81 GAIVENPELYDyMTGMQNLKHFanmaiTQISKERIAEIVKLVELEHAIHKKVKT-----------YSLGMKQRLGIAQAL 149
Cdd:cd03244 81 SIIPQDPVLFS-GTIRSNLDPF-----GEYSDEELWQALERVGLKEFVESLPGGldtvveeggenLSVGQRQLLCLARAL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 150 LHQPKILILDEPTNGLDPAGIRQIrdylQLLAKEE--NIAVIVSSHLLSEIeLMCDRVVIIKQGEfVQEY 217
Cdd:cd03244 155 LRKSKILVLDEATASVDPETDALI----QKTIREAfkDCTVLTIAHRLDTI-IDSDRILVLDKGR-VVEF 218
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
1-216 |
4.34e-19 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 84.64 E-value: 4.34e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 1 MGNVVVKLENVRKKIGGTEIIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGHSIRTEREKALE-- 78
Cdd:PRK10619 1 MSENKLNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKDGQlk 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 79 ------------QIGAIVENPELYDYMTGMQNLKHfANMAITQISK----ERIAEIVKLVELEHAIHKKVKTY-SLGMKQ 141
Cdd:PRK10619 81 vadknqlrllrtRLTMVFQHFNLWSHMTVLENVME-APIQVLGLSKqearERAVKYLAKVGIDERAQGKYPVHlSGGQQQ 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2753457674 142 RLGIAQALLHQPKILILDEPTNGLDPAGIRQIRDYLQLLAKEENIAVIVsSHLLSEIELMCDRVVIIKQGEFVQE 216
Cdd:PRK10619 160 RVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVV-THEMGFARHVSSHVIFLHQGKIEEE 233
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
5-216 |
4.81e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 84.19 E-value: 4.81e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 5 VVKLENVRKKIGGTEIIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISM-----TEGDITICGHSI----RTEREK 75
Cdd:PRK14247 3 KIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELypearVSGEVYLDGQDIfkmdVIELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 76 ALEQIGAIvENPelydymtgMQNLKHFANMAI----TQISK------ERIAEIVKLVELEHAIHKKVKT----YSLGMKQ 141
Cdd:PRK14247 83 RVQMVFQI-PNP--------IPNLSIFENVALglklNRLVKskkelqERVRWALEKAQLWDEVKDRLDApagkLSGGQQQ 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2753457674 142 RLGIAQALLHQPKILILDEPTNGLDPAGIRQIRDYLQLLAKEenIAVIVSSHLLSEIELMCDRVVIIKQGEFVQE 216
Cdd:PRK14247 154 RLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKD--MTIVLVTHFPQQAARISDYVAFLYKGQIVEW 226
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
19-215 |
5.16e-19 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 84.46 E-value: 5.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 19 EIIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGH-------SIRTEREKALEQIGAIVENPElyD 91
Cdd:PRK15112 27 EAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHplhfgdySYRSQRIRMIFQDPSTSLNPR--Q 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 92 YMTGMQNLKHFANMAITQISKE-RIAEIVKLVEL--EHAIHKKvKTYSLGMKQRLGIAQALLHQPKILILDEPTNGLDPA 168
Cdd:PRK15112 105 RISQILDFPLRLNTDLEPEQREkQIIETLRQVGLlpDHASYYP-HMLAPGQKQRLGLARALILRPKVIIADEALASLDMS 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2753457674 169 GIRQIRDYLQLLAKEENIAVIVSSHLLSEIELMCDRVVIIKQGEFVQ 215
Cdd:PRK15112 184 MRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVE 230
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
5-214 |
5.62e-19 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 86.80 E-value: 5.62e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 5 VVKLENVRKKIGGTEIIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLI--SMTEGDITICGHSIR------TER--- 73
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYphGTWDGEIYWSGSPLKasnirdTERagi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 74 -----EKALEQIGAIVENPELYDYMTGMQNLKHFANMAItqiskeRIAEIVKLVELEHA-IHKKVKTYSLGMKQRLGIAQ 147
Cdd:TIGR02633 81 viihqELTLVPELSVAENIFLGNEITLPGGRMAYNAMYL------RAKNLLRELQLDADnVTRPVGDYGGGQQQLVEIAK 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2753457674 148 ALLHQPKILILDEPTNGLDPAGIRQIRDYLQLLaKEENIAVIVSSHLLSEIELMCDRVVIIKQGEFV 214
Cdd:TIGR02633 155 ALNKQARLLILDEPSSSLTEKETEILLDIIRDL-KAHGVACVYISHKLNEVKAVCDTICVIRDGQHV 220
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
8-229 |
5.79e-19 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 86.50 E-value: 5.79e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 8 LENVRKKIGGTEIIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGHSIR-TEREKALEQIGAIVEN 86
Cdd:PRK11288 7 FDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRfASTTAALAAGVAIIYQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 87 -----PElydyMTGMQN--LKHFANMAITQISKERIAEIV-KLVELEHAI--HKKVKTYSLGMKQRLGIAQALLHQPKIL 156
Cdd:PRK11288 87 elhlvPE----MTVAENlyLGQLPHKGGIVNRRLLNYEAReQLEHLGVDIdpDTPLKYLSIGQRQMVEIAKALARNARVI 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2753457674 157 ILDEPTNGLDPAGIRQ----IRDYlqllaKEENIAVIVSSHLLSEIELMCDRVVIIKQGEFVQEYNLHEQAKHDETV 229
Cdd:PRK11288 163 AFDEPTSSLSAREIEQlfrvIREL-----RAEGRVILYVSHRMEEIFALCDAITVFKDGRYVATFDDMAQVDRDQLV 234
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
7-216 |
2.83e-18 |
|
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: 81.03 E-value: 2.83e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 7 KLENVRKKIGGTEIIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLIS--MTEGDITICGHSIrTE---REKALEQIG 81
Cdd:cd03217 2 EIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKyeVTEGEILFKGEDI-TDlppEERARLGIF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 82 AIVENPElydymtgmqnlkhfanmaitQISKERIAEIVKLVElehaihkkvKTYSLGMKQRLGIAQALLHQPKILILDEP 161
Cdd:cd03217 81 LAFQYPP--------------------EIPGVKNADFLRYVN---------EGFSGGEKKRNEILQLLLLEPDLAILDEP 131
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2753457674 162 TNGLDPAGIRQIRDYLQLLaKEENIAVIVSSH---LLSEIElmCDRVVIIKQGEFVQE 216
Cdd:cd03217 132 DSGLDIDALRLVAEVINKL-REEGKSVLIITHyqrLLDYIK--PDRVHVLYDGRIVKS 186
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
28-215 |
2.84e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 82.76 E-value: 2.84e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 28 VREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGHSIRTE-REKAL----EQIGAIVENPE--------LYDYMT 94
Cdd:PRK13634 30 IPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGkKNKKLkplrKKVGIVFQFPEhqlfeetvEKDICF 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 95 GMQNLKhfanmAITQISKERIAEIVKLVELEHAI-HKKVKTYSLGMKQRLGIAQALLHQPKILILDEPTNGLDPAGIRQI 173
Cdd:PRK13634 110 GPMNFG-----VSEEDAKQKAREMIELVGLPEELlARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEM 184
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2753457674 174 RDYLQLLAKEENIAVIVSSHLLSEIELMCDRVVIIKQGEFVQ 215
Cdd:PRK13634 185 MEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFL 226
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
3-216 |
2.90e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 82.83 E-value: 2.90e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 3 NVVVKLENV---RKKIGGTEIIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGHSIRTEREKAL-E 78
Cdd:PRK13642 2 NKILEVENLvfkYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLrR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 79 QIGAIVENPELYDYMTGMQNLKHFAnMAITQISKE----RIAEIVKLVELEHAIHKKVKTYSLGMKQRLGIAQALLHQPK 154
Cdd:PRK13642 82 KIGMVFQNPDNQFVGATVEDDVAFG-MENQGIPREemikRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPE 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2753457674 155 ILILDEPTNGLDPAGIRQIRDYLQLLAKEENIAVIVSSHLLSEIElMCDRVVIIKQGEFVQE 216
Cdd:PRK13642 161 IIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAA-SSDRILVMKAGEIIKE 221
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
19-227 |
4.87e-18 |
|
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: 84.10 E-value: 4.87e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 19 EIIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGHSIRTEREKAL-EQIGaIVenPElyDymTGMQ 97
Cdd:COG5265 372 PILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLrAAIG-IV--PQ--D--TVLF 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 98 NLKHFANMAI--TQISKERIAEIVKLVELEHAIHKKVKTY-----------SLGMKQRLGIAQALLHQPKILILDEPTNG 164
Cdd:COG5265 445 NDTIAYNIAYgrPDASEEEVEAAARAAQIHDFIESLPDGYdtrvgerglklSGGEKQRVAIARTLLKNPPILIFDEATSA 524
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2753457674 165 LDPAGIRQIRDYLQLLAKeeNIAVIVSSHLLSEIeLMCDRVVIIKQGEFVqeynlhEQAKHDE 227
Cdd:COG5265 525 LDSRTERAIQAALREVAR--GRTTLVIAHRLSTI-VDADEILVLEAGRIV------ERGTHAE 578
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
19-241 |
9.50e-18 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 83.18 E-value: 9.50e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 19 EIIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGHSIRTEREKAL------------EQIGAIVEN 86
Cdd:PRK15439 277 EGFRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRlarglvylpedrQSSGLYLDA 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 87 PELYDYMTGMQNLKHFanmaITQISKE-------RIAEIVKLVELEHAihkkVKTYSLGMKQRLGIAQALLHQPKILILD 159
Cdd:PRK15439 357 PLAWNVCALTHNRRGF----WIKPAREnavleryRRALNIKFNHAEQA----ARTLSGGNQQKVLIAKCLEASPQLLIVD 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 160 EPTNGLDPAGIRQIRDYLQLLAKeENIAVIVSSHLLSEIELMCDRVVIIKQGEFVQEYnLHEQAKHDETVVVAFEVDQVQ 239
Cdd:PRK15439 429 EPTRGVDVSARNDIYQLIRSIAA-QNVAVLFISSDLEEIEQMADRVLVMHQGEISGAL-TGAAINVDTIMRLAFGEHQAQ 506
|
..
gi 2753457674 240 KA 241
Cdd:PRK15439 507 EA 508
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
8-216 |
1.40e-17 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 80.60 E-value: 1.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 8 LENVRKKIGGTEIIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGHSIRTEREKALEQIGAIVenP 87
Cdd:PRK10575 14 LRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYL--P 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 88 ELYDYMTGMQNLK---------HFANMAITQISKERIAEIVKLVELEHAIHKKVKTYSLGMKQRLGIAQALLHQPKILIL 158
Cdd:PRK10575 92 QQLPAAEGMTVRElvaigrypwHGALGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2753457674 159 DEPTNGLDPAGIRQIRDYLQLLAKEENIAVIVSSHLLSEIELMCDRVVIIKQGEFVQE 216
Cdd:PRK10575 172 DEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQ 229
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
17-209 |
1.56e-17 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 80.70 E-value: 1.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 17 GTEIIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGHSIRtereKALEQ-IGAIVENPELYDY--- 92
Cdd:PRK15056 19 GHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTR----QALQKnLVAYVPQSEEVDWsfp 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 93 --MTGMQNLKHFANMAITQISKERIAEIVKL----VELEHAIHKKVKTYSLGMKQRLGIAQALLHQPKILILDEPTNGLD 166
Cdd:PRK15056 95 vlVEDVVMMGRYGHMGWLRRAKKRDRQIVTAalarVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVD 174
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2753457674 167 PAGIRQIRDYLQLLaKEENIAVIVSSHLLSEIELMCDRVVIIK 209
Cdd:PRK15056 175 VKTEARIISLLREL-RDEGKTMLVSTHNLGSVTEFCDYTVMVK 216
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
24-225 |
1.60e-17 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 82.63 E-value: 1.60e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 24 LSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGHSIRTEREKALEQIGAIVENPELYDYMTGMQNLKhfa 103
Cdd:PRK13545 43 ISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAALIAISSGLNGQLTGIENIELKGLMMGLTKEK--- 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 104 nmaitqiSKERIAEIVKLVELEHAIHKKVKTYSLGMKQRLGIAQALLHQPKILILDEPTNGLDPAGIRQIRDYLQLLaKE 183
Cdd:PRK13545 120 -------IKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKCLDKMNEF-KE 191
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2753457674 184 ENIAVIVSSHLLSEIELMCDRVVIIKQGEfVQEY-NLHEQAKH 225
Cdd:PRK13545 192 QGKTIFFISHSLSQVKSFCTKALWLHYGQ-VKEYgDIKEVVDH 233
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
17-211 |
1.63e-17 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 82.55 E-value: 1.63e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 17 GTEIIRGLSFEVREGEvyGFL--GPNGSGKTTTIRMMTGLISMTEGDITicghsiRTEREKAL--------------EQI 80
Cdd:COG4178 375 GRPLLEDLSLSLKPGE--RLLitGPSGSGKSTLLRAIAGLWPYGSGRIA------RPAGARVLflpqrpylplgtlrEAL 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 81 gaivenpeLYDYmtgmqnlkhfanmAITQISKERIAEIVKLVELEHAIHK--KV----KTYSLGMKQRLGIAQALLHQPK 154
Cdd:COG4178 447 --------LYPA-------------TAEAFSDAELREALEAVGLGHLAERldEEadwdQVLSLGEQQRLAFARLLLHKPD 505
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2753457674 155 ILILDEPTNGLDPAGIRQIrdYLQLLAKEENIAVIVSSHlLSEIELMCDRVVIIKQG 211
Cdd:COG4178 506 WLFLDEATSALDEENEAAL--YQLLREELPGTTVISVGH-RSTLAAFHDRVLELTGD 559
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
24-236 |
2.71e-17 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 79.21 E-value: 2.71e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 24 LSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISmTEGDITICGHSIRTEREKALEQIGAIV---ENP----ELYDYMTgm 96
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLLP-GSGSIQFAGQPLEAWSAAELARHRAYLsqqQTPpfamPVFQYLT-- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 97 qnlKHFANMAITQISKERIAEIVKLVELEHAIHKKVKTYSLGMKQRLGIAQALLH-------QPKILILDEPTNGLDpag 169
Cdd:PRK03695 92 ---LHQPDKTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVLQvwpdinpAGQLLLLDEPMNSLD--- 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2753457674 170 IRQIRDYLQLLAK--EENIAVIVSSHLLSEIELMCDRVVIIKQGefvqeyNLHEQAKHDE--TVVV---AFEVD 236
Cdd:PRK03695 166 VAQQAALDRLLSElcQQGIAVVMSSHDLNHTLRHADRVWLLKQG------KLLASGRRDEvlTPENlaqVFGVN 233
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
16-208 |
2.84e-17 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 78.04 E-value: 2.84e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 16 GGTEIIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGHSI------RTEREKALEqigAIVEnpel 89
Cdd:NF040873 3 GGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARvayvpqRSEVPDSLP---LTVR---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 90 yDYMT--------GMQNLKHFANMAItqiskERIAEIVKLVELEhaiHKKVKTYSLGMKQRLGIAQALLHQPKILILDEP 161
Cdd:NF040873 76 -DLVAmgrwarrgLWRRLTRDDRAAV-----DDALERVGLADLA---GRQLGELSGGQRQRALLAQGLAQEADLLLLDEP 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2753457674 162 TNGLDPAGIRQIRDYLQLLAkEENIAVIVSSHLLSEIELMcDRVVII 208
Cdd:NF040873 147 TTGLDAESRERIIALLAEEH-ARGATVVVVTHDLELVRRA-DPCVLL 191
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
20-215 |
3.51e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 80.28 E-value: 3.51e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 20 IIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITI----CGHSIRTERE------------KALEQIGAI 83
Cdd:PRK13631 41 ALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVgdiyIGDKKNNHELitnpyskkiknfKELRRRVSM 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 84 V-ENPELYDYMTGMQNLKHFANMAITQiSKERIAEIVK--LVEL---EHAIHKKVKTYSLGMKQRLGIAQALLHQPKILI 157
Cdd:PRK13631 121 VfQFPEYQLFKDTIEKDIMFGPVALGV-KKSEAKKLAKfyLNKMgldDSYLERSPFGLSGGQKRRVAIAGILAIQPEILI 199
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2753457674 158 LDEPTNGLDPAGIRQIRDyLQLLAKEENIAVIVSSHLLSEIELMCDRVVIIKQGEFVQ 215
Cdd:PRK13631 200 FDEPTAGLDPKGEHEMMQ-LILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKILK 256
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
9-215 |
3.80e-17 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 79.20 E-value: 3.80e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 9 ENVRKKIGGTEIIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITIcghsirTEREKALEQIGAIVE--- 85
Cdd:PRK11701 10 RGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHY------RMRDGQLRDLYALSEaer 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 86 -------------NPelydyMTGMQ-NLKHFAN-----MAITQISKERI----AEIVKLVELEHA-IHKKVKTYSLGMKQ 141
Cdd:PRK11701 84 rrllrtewgfvhqHP-----RDGLRmQVSAGGNigerlMAVGARHYGDIrataGDWLERVEIDAArIDDLPTTFSGGMQQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2753457674 142 RLGIAQALLHQPKILILDEPTNGLDPAGIRQIRDYLQLLAKEENIAVIVSSHLLSEIELMCDRVVIIKQGEFVQ 215
Cdd:PRK11701 159 RLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVVE 232
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
17-227 |
4.70e-17 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 81.32 E-value: 4.70e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 17 GTEIIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGHSIRTEREKALEQ-IGAIVENPELYDyMTG 95
Cdd:TIGR01193 486 GSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQfINYLPQEPYIFS-GSI 564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 96 MQNLKHFANMAITQiskERIAEIVKLVELEHAIHKKVKTY-----------SLGMKQRLGIAQALLHQPKILILDEPTNG 164
Cdd:TIGR01193 565 LENLLLGAKENVSQ---DEIWAACEIAEIKDDIENMPLGYqtelseegssiSGGQKQRIALARALLTDSKVLILDESTSN 641
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2753457674 165 LDPAGIRQIRDYLqLLAKEENIavIVSSHLLSeIELMCDRVVIIKQGEFVqeynlhEQAKHDE 227
Cdd:TIGR01193 642 LDTITEKKIVNNL-LNLQDKTI--IFVAHRLS-VAKQSDKIIVLDHGKII------EQGSHDE 694
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
6-215 |
5.53e-17 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 80.78 E-value: 5.53e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 6 VKLENVRKKIGGT-EIIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGHSIRTEREKALEQ-IGAI 83
Cdd:PRK13657 335 VEFDDVSFSYDNSrQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRnIAVV 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 84 VENPELYDYMTGmQNLkhfanmaitQISKERI--AEIVKLVELEHA---IHKKVKTY-----------SLGMKQRLGIAQ 147
Cdd:PRK13657 415 FQDAGLFNRSIE-DNI---------RVGRPDAtdEEMRAAAERAQAhdfIERKPDGYdtvvgergrqlSGGERQRLAIAR 484
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2753457674 148 ALLHQPKILILDEPTNGLDPAGIRQIRDYLQLLAKEENIAVIvsSHLLSEIElMCDRVVIIKQGEFVQ 215
Cdd:PRK13657 485 ALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFII--AHRLSTVR-NADRILVFDNGRVVE 549
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
21-222 |
5.80e-17 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 80.83 E-value: 5.80e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 21 IRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGHSIRTEREKAL-EQIGAIVENPELYDYmTGMQNL 99
Cdd:PRK11176 359 LRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLrNQVALVSQNVHLFND-TIANNI 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 100 KHFANmaiTQISKEriaEIVKLVELEHAIH--KKVK------------TYSLGMKQRLGIAQALLHQPKILILDEPTNGL 165
Cdd:PRK11176 438 AYART---EQYSRE---QIEEAARMAYAMDfiNKMDngldtvigengvLLSGGQRQRIAIARALLRDSPILILDEATSAL 511
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2753457674 166 DPAGIRQIRDYLQLLAKeeNIAVIVSSHLLSEIElMCDRVVIIKQGEFVqEYNLHEQ 222
Cdd:PRK11176 512 DTESERAIQAALDELQK--NRTSLVIAHRLSTIE-KADEILVVEDGEIV-ERGTHAE 564
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
23-214 |
5.93e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 79.02 E-value: 5.93e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 23 GLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGHSIR-TEREKALEQI----GAIVENPE--------L 89
Cdd:PRK13649 25 DVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITsTSKNKDIKQIrkkvGLVFQFPEsqlfeetvL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 90 YDYMTGMQNLkhfanmAITQISKERIA-EIVKLVEL-EHAIHKKVKTYSLGMKQRLGIAQALLHQPKILILDEPTNGLDP 167
Cdd:PRK13649 105 KDVAFGPQNF------GVSQEEAEALArEKLALVGIsESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDP 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2753457674 168 AGIRQIRDYLQLLaKEENIAVIVSSHLLSEIELMCDRVVIIKQGEFV 214
Cdd:PRK13649 179 KGRKELMTLFKKL-HQSGMTIVLVTHLMDDVANYADFVYVLEKGKLV 224
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
15-215 |
6.91e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 78.55 E-value: 6.91e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 15 IGGTEIIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGHSI-------RTEREKALEQIGAIVENP 87
Cdd:PRK14246 20 INDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLyfgkdifQIDAIKLRKEVGMVFQQP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 88 ELYDYMTGMQNLKH-------FANMAITQISKERIAEIVKLVELEHAIHKKVKTYSLGMKQRLGIAQALLHQPKILILDE 160
Cdd:PRK14246 100 NPFPHLSIYDNIAYplkshgiKEKREIKKIVEECLRKVGLWKEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDE 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2753457674 161 PTNGLDPAGIRQIRDYLQLLAKEenIAVIVSSHLLSEIELMCDRVVIIKQGEFVQ 215
Cdd:PRK14246 180 PTSMIDIVNSQAIEKLITELKNE--IAIVIVSHNPQQVARVADYVAFLYNGELVE 232
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
20-214 |
7.06e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 78.69 E-value: 7.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 20 IIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLI---SMTEGDITICGHSIRTE-----REKaleqIGAIVENPELY- 90
Cdd:PRK13640 22 ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLlpdDNPNSKITVDGITLTAKtvwdiREK----VGIVFQNPDNQf 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 91 -------DYMTGMQNlkhfanmaiTQISKERIAEIVKL----VELEHAIHKKVKTYSLGMKQRLGIAQALLHQPKILILD 159
Cdd:PRK13640 98 vgatvgdDVAFGLEN---------RAVPRPEMIKIVRDvladVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILD 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2753457674 160 EPTNGLDPAGIRQIRDYLQLLAKEENIAVIVSSHLLSEIElMCDRVVIIKQGEFV 214
Cdd:PRK13640 169 ESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEAN-MADQVLVLDDGKLL 222
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
8-212 |
9.11e-17 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 78.18 E-value: 9.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 8 LENVRKKIGGTEIIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDItICGhsiRTEREKALEQIGAIVENP 87
Cdd:PRK11247 15 LNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL-LAG---TAPLAEAREDTRLMFQDA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 88 ELYDYMTGMQNLkhfaNMAITQISKERIAEIVKLVELEHAIHKKVKTYSLGMKQRLGIAQALLHQPKILILDEPTNGLDP 167
Cdd:PRK11247 91 RLLPWKKVIDNV----GLGLKGQWRDAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDA 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2753457674 168 AGIRQIRDYLQLLAKEENIAVIVSSHLLSEIELMCDRVVIIKQGE 212
Cdd:PRK11247 167 LTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGK 211
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
10-214 |
9.54e-17 |
|
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: 76.92 E-value: 9.54e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 10 NVRKKIGGTEIIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMT---EGDITICGHSIRTEREKALEQIGAIVEN 86
Cdd:cd03233 12 TTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKEFAEKYPGEIIYVSEE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 87 PElydymtgmqnlkHFANMAITQIskeriaeivklveLEHAI----HKKVKTYSLGMKQRLGIAQALLHQPKILILDEPT 162
Cdd:cd03233 92 DV------------HFPTLTVRET-------------LDFALrckgNEFVRGISGGERKRVSIAEALVSRASVLCWDNST 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2753457674 163 NGLDPAGIRQIRDYLQLLAKEENIAVIVSSHLLS-EIELMCDRVVIIKQGEFV 214
Cdd:cd03233 147 RGLDSSTALEILKCIRTMADVLKTTTFVSLYQASdEIYDLFDKVLVLYEGRQI 199
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
24-215 |
1.05e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 78.33 E-value: 1.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 24 LSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGHSIRTER-EKALEQIGAIV------------ENPELY 90
Cdd:PRK13641 26 ISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETgNKNLKKLRKKVslvfqfpeaqlfENTVLK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 91 DYMTGMQNLKhfanmAITQISKERIAEIVKLVEL-EHAIHKKVKTYSLGMKQRLGIAQALLHQPKILILDEPTNGLDPAG 169
Cdd:PRK13641 106 DVEFGPKNFG-----FSEDEAKEKALKWLKKVGLsEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEG 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2753457674 170 IRQIRDYLQLLAKEENiAVIVSSHLLSEIELMCDRVVIIKQGEFVQ 215
Cdd:PRK13641 181 RKEMMQLFKDYQKAGH-TVILVTHNMDDVAEYADDVLVLEHGKLIK 225
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
24-234 |
1.13e-16 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 77.93 E-value: 1.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 24 LSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGhsirterekaleQIGAIVENPELYDYMTGMQNLK-HF 102
Cdd:PRK13546 43 ISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG------------EVSVIAISAGLSGQLTGIENIEfKM 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 103 ANMAITQIS-KERIAEIVKLVELEHAIHKKVKTYSLGMKQRLGIAQALLHQPKILILDEPTNGLDPAGIRQIRDYLQLLa 181
Cdd:PRK13546 111 LCMGFKRKEiKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKCLDKIYEF- 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2753457674 182 KEENIAVIVSSHLLSEIELMCDRVVIIKQGEFVQEYNLHEQAKHDETVVVAFE 234
Cdd:PRK13546 190 KEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDVLPKYEAFLNDFK 242
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
8-211 |
1.56e-16 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 77.43 E-value: 1.56e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 8 LENVRKKIGGTEIIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGHSIR---TERekaleqiGAIV 84
Cdd:PRK11248 4 ISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEgpgAER-------GVVF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 85 ENPELYDYMTGMQNLK---HFANMAITQiSKERIAEIVKLVELEHAIHKKVKTYSLGMKQRLGIAQALLHQPKILILDEP 161
Cdd:PRK11248 77 QNEGLLPWRNVQDNVAfglQLAGVEKMQ-RLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEP 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2753457674 162 TNGLDPAGIRQIRDYLQLLAKEENIAVIVSSHLLSEIELMCDRVVIIKQG 211
Cdd:PRK11248 156 FGALDAFTREQMQTLLLKLWQETGKQVLLITHDIEEAVFMATELVLLSPG 205
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
5-216 |
1.77e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 77.72 E-value: 1.77e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 5 VVKLENVRKKI-GGTEIIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGhsIRTEREKALEQI--- 80
Cdd:PRK13644 1 MIRLENVSYSYpDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSG--IDTGDFSKLQGIrkl 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 81 -GAIVENPELY--------DYMTGMQNLkhfaNMAITQISKeRIAEIVKLVELEHAIHKKVKTYSLGMKQRLGIAQALLH 151
Cdd:PRK13644 79 vGIVFQNPETQfvgrtveeDLAFGPENL----CLPPIEIRK-RVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTM 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2753457674 152 QPKILILDEPTNGLDP-AGIRQIRDYLQLLAKEENIAVIvsSHLLSEIElMCDRVVIIKQGEFVQE 216
Cdd:PRK13644 154 EPECLIFDEVTSMLDPdSGIAVLERIKKLHEKGKTIVYI--THNLEELH-DADRIIVMDRGKIVLE 216
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
5-214 |
2.41e-16 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 76.99 E-value: 2.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 5 VVKLENVRKKIGGTEIIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTG--LISMTEGDITICGHSIRTEREKALEQIGA 82
Cdd:CHL00131 7 ILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGhpAYKILEGDILFKGESILDLEPEERAHLGI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 83 I-----------VENPEL----YDYMTGMQNLKHFANMAITQIskerIAEIVKLVEL-EHAIHKKV-KTYSLGMKQRLGI 145
Cdd:CHL00131 87 FlafqypieipgVSNADFlrlaYNSKRKFQGLPELDPLEFLEI----INEKLKLVGMdPSFLSRNVnEGFSGGEKKRNEI 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2753457674 146 AQALLHQPKILILDEPTNGLDPAGIRQIRDYLQLLAKEENIAVIVSSH--LLSEIelMCDRVVIIKQGEFV 214
Cdd:CHL00131 163 LQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIILITHYqrLLDYI--KPDYVHVMQNGKII 231
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
10-228 |
2.47e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 77.44 E-value: 2.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 10 NVRKKIGGTEIIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEG-----DITICGHSIRTEREkALE---QIG 81
Cdd:PRK14271 26 NLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIFNYRD-VLEfrrRVG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 82 AIVENPELY------DYMTGMQNLKHFANMAITQISKERIAEIVKLVELEHAIHKKVKTYSLGMKQRLGIAQALLHQPKI 155
Cdd:PRK14271 105 MLFQRPNPFpmsimdNVLAGVRAHKLVPRKEFRGVAQARLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEV 184
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2753457674 156 LILDEPTNGLDPAGIRQIRDYLQLLAkeENIAVIVSSHLLSEIELMCDRVVIIKQGEFVQE---YNLHEQAKHDET 228
Cdd:PRK14271 185 LLLDEPTSALDPTTTEKIEEFIRSLA--DRLTVIIVTHNLAQAARISDRAALFFDGRLVEEgptEQLFSSPKHAET 258
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
4-190 |
2.88e-16 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 76.76 E-value: 2.88e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 4 VVVKLENVRKKIGGTEIIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGHSIRTEREKALE----- 78
Cdd:COG4598 7 PALEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIRLKPDRDGElvpad 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 79 ---------QIGAIVENPELYDYMTGMQNLKhFANMAITQISK-ERIAEIVKL---VELEHAIHKKVKTYSLGMKQRLGI 145
Cdd:COG4598 87 rrqlqrirtRLGMVFQSFNLWSHMTVLENVI-EAPVHVLGRPKaEAIERAEALlakVGLADKRDAYPAHLSGGQQQRAAI 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2753457674 146 AQALLHQPKILILDEPTNGLDP--AG--IRQIRDylqlLAKEENIAVIV 190
Cdd:COG4598 166 ARALAMEPEVMLFDEPTSALDPelVGevLKVMRD----LAEEGRTMLVV 210
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
19-214 |
3.40e-16 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 78.55 E-value: 3.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 19 EIIRGLSFEVREGEVYGFLGPNGSGKTTTI-----RMMTGLisMTEGDITICGHSIrtEREKaLEQIGAIVENPEL---- 89
Cdd:TIGR00955 39 HLLKNVSGVAKPGELLAVMGSSGAGKTTLMnalafRSPKGV--KGSGSVLLNGMPI--DAKE-MRAISAYVQQDDLfipt 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 90 ---YDYMTGMQNLKHFANMAITQiSKERIAEIVKLVELEHAIHKK------VKTYSLGMKQRLGIAQALLHQPKILILDE 160
Cdd:TIGR00955 114 ltvREHLMFQAHLRMPRRVTKKE-KRERVDEVLQALGLRKCANTRigvpgrVKGLSGGERKRLAFASELLTDPPLLFCDE 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2753457674 161 PTNGLDPAGIRQIRDYLQLLAKEENIaVIVSSHLLSEiELMC--DRVVIIKQGEFV 214
Cdd:TIGR00955 193 PTSGLDSFMAYSVVQVLKGLAQKGKT-IICTIHQPSS-ELFElfDKIILMAEGRVA 246
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
24-214 |
3.71e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 77.08 E-value: 3.71e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 24 LSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEG-----DITICGHSIRTEREKALEQIGAIVENPE--------LY 90
Cdd:PRK13643 25 IDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGkvtvgDIVVSSTSKQKEIKPVRKKVGVVFQFPEsqlfeetvLK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 91 DYMTGMQNLkhfanmAITQISKERIA-EIVKLVELEHAIHKKVK-TYSLGMKQRLGIAQALLHQPKILILDEPTNGLDPA 168
Cdd:PRK13643 105 DVAFGPQNF------GIPKEKAEKIAaEKLEMVGLADEFWEKSPfELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPK 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2753457674 169 GIRQIRDYLQLLAKEENIAVIVsSHLLSEIELMCDRVVIIKQGEFV 214
Cdd:PRK13643 179 ARIEMMQLFESIHQSGQTVVLV-THLMDDVADYADYVYLLEKGHII 223
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
19-269 |
5.80e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 76.36 E-value: 5.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 19 EIIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGHSIRTE-REKALEQI----GAIVENPE--LYD 91
Cdd:PRK13646 21 QAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKtKDKYIRPVrkriGMVFQFPEsqLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 92 YMTGMQNL---KHFaNMAITQISKERIAEIVKLVELEHAIHKKVKTYSLGMKQRLGIAQALLHQPKILILDEPTNGLDPA 168
Cdd:PRK13646 101 DTVEREIIfgpKNF-KMNLDEVKNYAHRLLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQ 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 169 GIRQIRDYLQLLAKEENIAVIVSSHLLSEIELMCDRVVIIKQGEFVQEYNLHEQAKHDETV----VVAFEVDQVQKANEI 244
Cdd:PRK13646 180 SKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFKDKKKLadwhIGLPEIVQLQYDFEQ 259
|
250 260
....*....|....*....|....*
gi 2753457674 245 vqgKAQGNVILVSVTKEEIPQLVKK 269
Cdd:PRK13646 260 ---KYQTKLKDIALTEEEFVSLYKE 281
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
16-222 |
5.91e-16 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 77.84 E-value: 5.91e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 16 GGTEIIRGLSFEVREGEV-----------YGFL---GPNGSGKTTTIRMMTGLISMTEGDITICGHSIRTEREKALEQIG 81
Cdd:PRK10790 338 SGRIDIDNVSFAYRDDNLvlqninlsvpsRGFValvGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGV 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 82 AIVE-NPE-LYDYMtgmqnlkhFANMAITQ-ISKERI---AEIVKLVELEHA----IHKKV----KTYSLGMKQRLGIAQ 147
Cdd:PRK10790 418 AMVQqDPVvLADTF--------LANVTLGRdISEEQVwqaLETVQLAELARSlpdgLYTPLgeqgNNLSVGQKQLLALAR 489
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2753457674 148 ALLHQPKILILDEPTNGLDPAGIRQIRDYLQLLAKEENIAVIvsSHLLSEIeLMCDRVVIIKQGEFVQEYNlHEQ 222
Cdd:PRK10790 490 VLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVI--AHRLSTI-VEADTILVLHRGQAVEQGT-HQQ 560
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
24-215 |
6.36e-16 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 77.96 E-value: 6.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 24 LSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMtEGDITICGHSIRT-EREKALEQIGAIVENPELYdYMTGMQNLKhf 102
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPY-QGSLKINGIELRElDPESWRKHLSWVGQNPQLP-HGTLRDNVL-- 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 103 anMAITQISKERI---------AEIVKLVE--LEHAIHKKVKTYSLGMKQRLGIAQALLHQPKILILDEPTNGLDPAGIR 171
Cdd:PRK11174 445 --LGNPDASDEQLqqalenawvSEFLPLLPqgLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQ 522
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2753457674 172 QIRDYLQLLAKEEniAVIVSSHLLSEIElMCDRVVIIKQGEFVQ 215
Cdd:PRK11174 523 LVMQALNAASRRQ--TTLMVTHQLEDLA-QWDQIWVMQDGQIVQ 563
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
2-232 |
9.47e-16 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 77.13 E-value: 9.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 2 GNVVVKLENVRKKIGGTeiIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGH--SIRTEREKALEQ 79
Cdd:PRK09700 262 HETVFEVRNVTSRDRKK--VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKdiSPRSPLDAVKKG 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 80 IGAIVENPELYDYMTgmqNLKHFANMAITQISK----------------ERIAEIV-KLVELE-HAIHKKVKTYSLGMKQ 141
Cdd:PRK09700 340 MAYITESRRDNGFFP---NFSIAQNMAISRSLKdggykgamglfhevdeQRTAENQrELLALKcHSVNQNITELSGGNQQ 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 142 RLGIAQALLHQPKILILDEPTNGLDPAGIRQIRDYLQLLAkEENIAVIVSSHLLSEIELMCDRVVIIKQGEFVQEYNLHE 221
Cdd:PRK09700 417 KVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLA-DDGKVILMVSSELPEIITVCDRIAVFCEGRLTQILTNRD 495
|
250
....*....|.
gi 2753457674 222 QAKHDETVVVA 232
Cdd:PRK09700 496 DMSEEEIMAWA 506
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
20-219 |
9.67e-16 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 74.61 E-value: 9.67e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 20 IIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGHSIRTEREKAL-EQIGAIVENPElydymtgmqn 98
Cdd:COG2401 45 VLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVDVPDNQFGREASLiDAIGRKGDFKD---------- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 99 lkhfanmaitqiSKERIAeIVKLVElEHAIHKKVKTYSLGMKQRLGIAQALLHQPKILILDEPTNGLDPAGIRQIRDYLQ 178
Cdd:COG2401 115 ------------AVELLN-AVGLSD-AVLWLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVARNLQ 180
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2753457674 179 LLAKEENIAVIVSSHlLSEIE--LMCDRVVIIKQGEFVQEYNL 219
Cdd:COG2401 181 KLARRAGITLVVATH-HYDVIddLQPDLLIFVGYGGVPEEKRR 222
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
25-214 |
9.76e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 75.81 E-value: 9.76e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 25 SFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGHSIRTEREKALE------QIGAIVENPELYDYMTGMQN 98
Cdd:PRK13645 31 SLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPANLKKIKEvkrlrkEIGLVFQFPEYQLFQETIEK 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 99 LKHFANMAITQISKE---RIAEIVKLVEL-EHAIHKKVKTYSLGMKQRLGIAQALLHQPKILILDEPTNGLDPAGIRQIR 174
Cdd:PRK13645 111 DIAFGPVNLGENKQEaykKVPELLKLVQLpEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFI 190
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2753457674 175 DYLQLLAKEENIAVIVSSHLLSEIELMCDRVVIIKQGEFV 214
Cdd:PRK13645 191 NLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVI 230
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
5-214 |
1.02e-15 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 74.53 E-value: 1.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 5 VVKLENVRKK-IGGTEIIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGHSIRTEREKAL----EQ 79
Cdd:PRK10908 1 MIRFEHVSKAyLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVpflrRQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 80 IGAIVENPELydymtgMQNLKHFANMAITQI----SKERIAEIVKLVELEHAIHKKVKTY----SLGMKQRLGIAQALLH 151
Cdd:PRK10908 81 IGMIFQDHHL------LMDRTVYDNVAIPLIiagaSGDDIRRRVSAALDKVGLLDKAKNFpiqlSGGEQQRVGIARAVVN 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2753457674 152 QPKILILDEPTNGLDPAgirqIRDYLQLLAKEEN---IAVIVSSHLLSEIELMCDRVVIIKQGEFV 214
Cdd:PRK10908 155 KPAVLLADEPTGNLDDA----LSEGILRLFEEFNrvgVTVLMATHDIGLISRRSYRMLTLSDGHLH 216
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
2-212 |
1.30e-15 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 76.89 E-value: 1.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 2 GNVVVKLENV---RKKIGGTEIIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLI-SMTEGDITICGH--SIRTEREK 75
Cdd:PRK13549 256 GEVILEVRNLtawDPVNPHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYpGRWEGEIFIDGKpvKIRNPQQA 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 76 ALEQIGAIVENPELYDYMTGMQNLKHFANMAITQISK-ERIAEIVKLVELEHAIHK-KVKTYSL---------GMKQRLG 144
Cdd:PRK13549 336 IAQGIAMVPEDRKRDGIVPVMGVGKNITLAALDRFTGgSRIDDAAELKTILESIQRlKVKTASPelaiarlsgGNQQKAV 415
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2753457674 145 IAQALLHQPKILILDEPTNGLDPAGIRQIRDYLQLLAKeENIAVIVSSHLLSEIELMCDRVVIIKQGE 212
Cdd:PRK13549 416 LAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQ-QGVAIIVISSELPEVLGLSDRVLVMHEGK 482
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
5-217 |
1.37e-15 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 76.58 E-value: 1.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 5 VVKLENVRKKIGGTEIIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGHSIRTEREKALEQ--IGA 82
Cdd:PRK10762 4 LLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQEagIGI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 83 IVENPELYDYMTGMQNL---KHFANmAITQIS-KERIAEIVKLVE---LEHAIHKKVKTYSLGMKQRLGIAQALLHQPKI 155
Cdd:PRK10762 84 IHQELNLIPQLTIAENIflgREFVN-RFGRIDwKKMYAEADKLLArlnLRFSSDKLVGELSIGEQQMVEIAKVLSFESKV 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2753457674 156 LILDEPTNGL----DPAGIRQIRDYlqllaKEENIAVIVSSHLLSEIELMCDRVVIIKQGEFVQEY 217
Cdd:PRK10762 163 IIMDEPTDALtdteTESLFRVIREL-----KSQGRGIVYISHRLKEIFEICDDVTVFRDGQFIAER 223
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
21-221 |
1.46e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 75.51 E-value: 1.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 21 IRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGHSIRT-----EREKALEQIgaIVENPelydYMTG 95
Cdd:PRK13651 23 LDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNkkktkEKEKVLEKL--VIQKT----RFKK 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 96 MQNLK----------HFA------------------NMAIT-QISKERIAEIVKLVEL-EHAIHKKVKTYSLGMKQRLGI 145
Cdd:PRK13651 97 IKKIKeirrrvgvvfQFAeyqlfeqtiekdiifgpvSMGVSkEEAKKRAAKYIELVGLdESYLQRSPFELSGGQKRRVAL 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2753457674 146 AQALLHQPKILILDEPTNGLDPAGIRQIRDYLQLLAKeENIAVIVSSHLLSEIELMCDRVVIIKQGEFVQEYNLHE 221
Cdd:PRK13651 177 AGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNK-QGKTIILVTHDLDNVLEWTKRTIFFKDGKIIKDGDTYD 251
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
27-207 |
2.12e-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: 73.98 E-value: 2.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 27 EVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGHSIRTERekalEQIGAivenpelyDYMTGMQNLKHfanmA 106
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSYKP----QYIKA--------DYEGTVRDLLS----S 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 107 ITQISKER---IAEIVKLVELEHAIHKKVKTYSLGMKQRLGIAQALLHQPKILILDEPTNGLDP----AGIRQIRDYlql 179
Cdd:cd03237 85 ITKDFYTHpyfKTEIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVeqrlMASKVIRRF--- 161
|
170 180
....*....|....*....|....*...
gi 2753457674 180 lAKEENIAVIVSSHLLSEIELMCDRVVI 207
Cdd:cd03237 162 -AENNEKTAFVVEHDIIMIDYLADRLIV 188
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
3-228 |
2.48e-15 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 73.92 E-value: 2.48e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 3 NVVVKLENVRKKIGGTEIIRGLSFEVREGEVYGFLGPNGSGKTTTIRM---MTGLIS--MTEGDITICGHSIRTEREKAL 77
Cdd:COG1117 9 EPKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRClnrMNDLIPgaRVEGEILLDGEDIYDPDVDVV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 78 E---QIGAIVENP-----ELYDymtgmqnlkhfaNMA----ITQI-SKERIAEIVklvE--LEHA---------IHKKVK 133
Cdd:COG1117 89 ElrrRVGMVFQKPnpfpkSIYD------------NVAyglrLHGIkSKSELDEIV---EesLRKAalwdevkdrLKKSAL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 134 TYSLGMKQRLGIAQALLHQPKILILDEPTNGLDPAGIRQIRDYLQLLAKEENIaVIVsSHLLSEIELMCDRVVIIKQGEF 213
Cdd:COG1117 154 GLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDYTI-VIV-THNMQQAARVSDYTAFFYLGEL 231
|
250
....*....|....*....
gi 2753457674 214 VqEYNLHEQ----AKHDET 228
Cdd:COG1117 232 V-EFGPTEQiftnPKDKRT 249
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
24-170 |
2.52e-15 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 73.34 E-value: 2.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 24 LSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGHSIRT-EREKALEQIGAIvenPELYDYMTGMQNLkHF 102
Cdd:PRK13543 30 LDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRgDRSRFMAYLGHL---PGLKADLSTLENL-HF 105
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2753457674 103 ANMAITQISKERIAEIVKLVELEHAIHKKVKTYSLGMKQRLGIAQALLHQPKILILDEPTNGLDPAGI 170
Cdd:PRK13543 106 LCGLHGRRAKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEGI 173
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-228 |
4.33e-15 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 73.27 E-value: 4.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 1 MGNVVVKLENVRKKIGGTEIIRGLSFEVREGEVYGFLGPNGSGKTT---TIRMMTGLIS--MTEGDITICGHSIRTEREK 75
Cdd:PRK14239 1 MTEPILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTllrSINRMNDLNPevTITGSIVYNGHNIYSPRTD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 76 ALE---QIGAIVENPELYDyMTGMQNLKHfaNMAITQI-SKERIAEIVKLVELEHAIHKKVK--------TYSLGMKQRL 143
Cdd:PRK14239 81 TVDlrkEIGMVFQQPNPFP-MSIYENVVY--GLRLKGIkDKQVLDEAVEKSLKGASIWDEVKdrlhdsalGLSGGQQQRV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 144 GIAQALLHQPKILILDEPTNGLDPAGIRQIRDYLQLLAKEENIAVIvsSHLLSEIELMCDRVVIIKQGEFVqEYNLHEQ- 222
Cdd:PRK14239 158 CIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLV--TRSMQQASRISDRTGFFLDGDLI-EYNDTKQm 234
|
....*....
gi 2753457674 223 ---AKHDET 228
Cdd:PRK14239 235 fmnPKHKET 243
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
17-193 |
4.56e-15 |
|
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: 71.42 E-value: 4.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 17 GTEIIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGHsirterekalEQIGAIVENPelydYMT-G 95
Cdd:cd03223 13 GRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEG----------EDLLFLPQRP----YLPlG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 96 mqNLKhfanmaitqiskeriaEIVklvelehaIHKKVKTYSLGMKQRLGIAQALLHQPKILILDEPTNGLDPAGIRQIrd 175
Cdd:cd03223 79 --TLR----------------EQL--------IYPWDDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRL-- 130
|
170
....*....|....*...
gi 2753457674 176 yLQLLaKEENIAVIVSSH 193
Cdd:cd03223 131 -YQLL-KELGITVISVGH 146
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
6-224 |
4.63e-15 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 73.20 E-value: 4.63e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 6 VKLENVRKKIG-GT----EIIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGHSIRTERE-KALEQ 79
Cdd:COG1101 2 LELKNLSKTFNpGTvnekRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEyKRAKY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 80 IGAIVENPelydyMTGM-QNLKHFANMAITQ-----------ISKERIAEIVKLVE-----LEHAIHKKVKTYSLGMKQR 142
Cdd:COG1101 82 IGRVFQDP-----MMGTaPSMTIEENLALAYrrgkrrglrrgLTKKRRELFRELLAtlglgLENRLDTKVGLLSGGQRQA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 143 LGIAQALLHQPKILILDEPTNGLDPAGIRQIrdyLQL---LAKEENIAVIVSSHLLSE-IELmCDRVVIIKQGEFVQEYN 218
Cdd:COG1101 157 LSLLMATLTKPKLLLLDEHTAALDPKTAALV---LELtekIVEENNLTTLMVTHNMEQaLDY-GNRLIMMHEGRIILDVS 232
|
....*.
gi 2753457674 219 LHEQAK 224
Cdd:COG1101 233 GEEKKK 238
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
21-215 |
4.73e-15 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 75.28 E-value: 4.73e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 21 IRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGHSIRTEREKALE---------------QIGAIVE 85
Cdd:PRK10261 32 VRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRRRSRQVIElseqsaaqmrhvrgaDMAMIFQ 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 86 NPelydyMTGM-----------------QNLKHFANMAitqiSKERIAEIVKLVELEHAIHKKVKTYSLGMKQRLGIAQA 148
Cdd:PRK10261 112 EP-----MTSLnpvftvgeqiaesirlhQGASREEAMV----EAKRMLDQVRIPEAQTILSRYPHQLSGGMRQRVMIAMA 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2753457674 149 LLHQPKILILDEPTNGLDPAGIRQIRDYLQLLAKEENIAVIVSSHLLSEIELMCDRVVIIKQGEFVQ 215
Cdd:PRK10261 183 LSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVE 249
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
6-193 |
5.71e-15 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 75.28 E-value: 5.71e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 6 VKLENVRKKIGGTEIIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMT-----GL-----ISMTE----GDITI---CGHS 68
Cdd:PLN03073 178 IHMENFSISVGGRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRYMAmhaidGIpkncqILHVEqevvGDDTTalqCVLN 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 69 IRTEREKALEQIGAIVENPELYDYMTGMQNLKHFANMAITQ-ISKERIAEIVKLVELEHAI------------------- 128
Cdd:PLN03073 258 TDIERTQLLEEEAQLVAQQRELEFETETGKGKGANKDGVDKdAVSQRLEEIYKRLELIDAYtaearaasilaglsftpem 337
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2753457674 129 -HKKVKTYSLGMKQRLGIAQALLHQPKILILDEPTNGLDPAGIRQIRDYLQLLAKeeniAVIVSSH 193
Cdd:PLN03073 338 qVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPK----TFIVVSH 399
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
21-223 |
1.32e-14 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 73.88 E-value: 1.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 21 IRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGHSI--RTEREKALEQIGAIVENPELYDYMTGM-- 96
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVvtRSPQDGLANGIVYISEDRKRDGLVLGMsv 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 97 -QN-----LKHFANMAITQISKERIAEIVKLVELehaihKKVKTYSL---------GMKQRLGIAQALLHQPKILILDEP 161
Cdd:PRK10762 348 kENmsltaLRYFSRAGGSLKHADEQQAVSDFIRL-----FNIKTPSMeqaigllsgGNQQKVAIARGLMTRPKVLILDEP 422
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2753457674 162 TNGLDPAGIRQIrdyLQLLA--KEENIAVIVSSHLLSEIELMCDRVVIIKQGEFVQEYNlHEQA 223
Cdd:PRK10762 423 TRGVDVGAKKEI---YQLINqfKAEGLSIILVSSEMPEVLGMSDRILVMHEGRISGEFT-REQA 482
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
23-207 |
1.43e-14 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 72.69 E-value: 1.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 23 GLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGHSIR---TEREKALEQ------------------IG 81
Cdd:PRK11308 33 GVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLkadPEAQKLLRQkiqivfqnpygslnprkkVG 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 82 AIVENPelydymtgmqnlkhfanMAI-TQIS----KERIAEIVKLVEL--EHAiHKKVKTYSLGMKQRLGIAQALLHQPK 154
Cdd:PRK11308 113 QILEEP-----------------LLInTSLSaaerREKALAMMAKVGLrpEHY-DRYPHMFSGGQRQRIAIARALMLDPD 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2753457674 155 ILILDEPTNGLDpAGIR-QIRDYLQLLAKEENIAVIVSSHLLSEIELMCDRVVI 207
Cdd:PRK11308 175 VVVADEPVSALD-VSVQaQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMV 227
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
24-216 |
1.50e-14 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 72.85 E-value: 1.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 24 LSFEVREGEVYGFLGPNGSGKTTTIRMMTGLIS-----MTEgDITICGHSIRTEREKALEQI-GAIVE----------NP 87
Cdd:PRK11022 26 ISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDypgrvMAE-KLEFNGQDLQRISEKERRNLvGAEVAmifqdpmtslNP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 88 ElydYMTG---MQNLK-HFANMAITQisKERIAEIVKLV-------ELEHAIHKkvktYSLGMKQRLGIAQALLHQPKIL 156
Cdd:PRK11022 105 C---YTVGfqiMEAIKvHQGGNKKTR--RQRAIDLLNQVgipdpasRLDVYPHQ----LSGGMSQRVMIAMAIACRPKLL 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 157 ILDEPTNGLDPAGIRQIRDYLQLLAKEENIAVIVSSHLLSEIELMCDRVVIIKQGEFVQE 216
Cdd:PRK11022 176 IADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVET 235
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
19-217 |
2.24e-14 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 70.52 E-value: 2.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 19 EIIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGHSIRTEREKAL-EQIGAIVENPELYDyMTGMQ 97
Cdd:cd03369 22 PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLrSSLTIIPQDPTLFS-GTIRS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 98 NLKHFanmaiTQISKERIAEIVKLVElehaihkKVKTYSLGMKQRLGIAQALLHQPKILILDEPTNGLDPAGIRQIrdyl 177
Cdd:cd03369 101 NLDPF-----DEYSDEEIYGALRVSE-------GGLNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDALI---- 164
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2753457674 178 QLLAKEE--NIAVIVSSHLLSEIeLMCDRVVIIKQGEfVQEY 217
Cdd:cd03369 165 QKTIREEftNSTILTIAHRLRTI-IDYDKILVMDAGE-VKEY 204
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
3-211 |
2.69e-14 |
|
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: 70.54 E-value: 2.69e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 3 NVVVKLENVRKK-----IGGTEI--IRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITIC--GHSI---- 69
Cdd:COG4778 2 TTLLEVENLSKTftlhlQGGKRLpvLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRhdGGWVdlaq 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 70 ----------RTE------------REKALEqigaIVENPELydyMTGMQnlkhfanmaiTQISKERIAEIVKLVEL-EH 126
Cdd:COG4778 82 aspreilalrRRTigyvsqflrvipRVSALD----VVAEPLL---ERGVD----------REEARARARELLARLNLpER 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 127 AIHKKVKTYSLGMKQRLGIAQALLHQPKILILDEPTNGLDPAGIRQIRDYLQlLAKEENIAVIVSSHLLSEIELMCDRVV 206
Cdd:COG4778 145 LWDLPPATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIE-EAKARGTAIIGIFHDEEVREAVADRVV 223
|
....*
gi 2753457674 207 IIKQG 211
Cdd:COG4778 224 DVTPF 228
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
21-215 |
3.55e-14 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 72.58 E-value: 3.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 21 IRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGHSIRTEREKALE----QIGAIVENPelYDYMTGM 96
Cdd:PRK10261 340 VEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQalrrDIQFIFQDP--YASLDPR 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 97 QNLKH-------FANMAITQISKERIAEIVKLVEL--EHAIhKKVKTYSLGMKQRLGIAQALLHQPKILILDEPTNGLDP 167
Cdd:PRK10261 418 QTVGDsimeplrVHGLLPGKAAAARVAWLLERVGLlpEHAW-RYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDV 496
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2753457674 168 AGIRQIRDYLQLLAKEENIAVIVSSHLLSEIELMCDRVVIIKQGEFVQ 215
Cdd:PRK10261 497 SIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVE 544
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
29-208 |
4.06e-14 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 72.51 E-value: 4.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 29 REGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDIticghsirtEREKALEQIGAIVENPELYDYMTGMQN------LKhf 102
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKILSGELKPNLGDY---------DEEPSWDEVLKRFRGTELQDYFKKLANgeikvaHK-- 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 103 aNMAITQISK--------------ER--IAEIVKLVELEHAIHKKVKTYSLGMKQRLGIAQALLHQPKILILDEPTNGLD 166
Cdd:COG1245 166 -PQYVDLIPKvfkgtvrellekvdERgkLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLD 244
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2753457674 167 pagIRQ-------IRDYLqllakEENIAVIVSSHLLSEIELMCDRVVII 208
Cdd:COG1245 245 ---IYQrlnvarlIRELA-----EEGKYVLVVEHDLAILDYLADYVHIL 285
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
24-212 |
4.37e-14 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 72.16 E-value: 4.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 24 LSFEVREGEVYGFLGPNGSGKTTTIRMMTGLI-SMTEGDITICGHSIRTER-EKALEQIGAIVENPELYDYMTGMQNLKH 101
Cdd:TIGR02633 279 VSFSLRRGEILGVAGLVGAGRTELVQALFGAYpGKFEGNVFINGKPVDIRNpAQAIRAGIAMVPEDRKRHGIVPILGVGK 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 102 FANMAITQ--ISKERIAEIVKLVELEHAIHK-KVKTYSL---------GMKQRLGIAQALLHQPKILILDEPTNGLDPAG 169
Cdd:TIGR02633 359 NITLSVLKsfCFKMRIDAAAELQIIGSAIQRlKVKTASPflpigrlsgGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGA 438
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2753457674 170 IRQIRDYLQLLAKeENIAVIVSSHLLSEIELMCDRVVIIKQGE 212
Cdd:TIGR02633 439 KYEIYKLINQLAQ-EGVAIIVVSSELAEVLGLSDRVLVIGEGK 480
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
10-198 |
4.81e-14 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 72.75 E-value: 4.81e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 10 NVRKKIggtEIIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITIC-GHSIRTEREKALE-QIGAIVENP 87
Cdd:PTZ00265 393 DTRKDV---EIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINdSHNLKDINLKWWRsKIGVVSQDP 469
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 88 ELY------------------DYMTGMQN--------------------LKHFANMAITQISKERI-----------AEI 118
Cdd:PTZ00265 470 LLFsnsiknnikyslyslkdlEALSNYYNedgndsqenknkrnscrakcAGDLNDMSNTTDSNELIemrknyqtikdSEV 549
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 119 VKLVE--LEH----AIHKKVKTY--------SLGMKQRLGIAQALLHQPKILILDEPTNGLDPAGIRQIRDYLQLLAKEE 184
Cdd:PTZ00265 550 VDVSKkvLIHdfvsALPDKYETLvgsnasklSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNE 629
|
250
....*....|....
gi 2753457674 185 NIAVIVSSHLLSEI 198
Cdd:PTZ00265 630 NRITIIIAHRLSTI 643
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
20-271 |
6.51e-14 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 71.83 E-value: 6.51e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 20 IIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGHSiRTEREKALEQIGAIVENPELYDYMTGMQNL 99
Cdd:PLN03211 83 ILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNFTGTILANN-RKPTKQILKRTGFVTQDDILYPHLTVRETL 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 100 KHFANM----AITQISKERIAEIV----KLVELEHAI--HKKVKTYSLGMKQRLGIAQALLHQPKILILDEPTNGLDPAG 169
Cdd:PLN03211 162 VFCSLLrlpkSLTKQEKILVAESViselGLTKCENTIigNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATA 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 170 IRQIRDYLQLLAKEENIAVIVSSHLLSEIELMCDRVVIIKQGEFVQEYNLHEQAKHDETV--VVAFEVDQVQKANEIVQG 247
Cdd:PLN03211 242 AYRLVLTLGSLAQKGKTIVTSMHQPSSRVYQMFDSVLVLSEGRCLFFGKGSDAMAYFESVgfSPSFPMNPADFLLDLANG 321
|
250 260
....*....|....*....|....
gi 2753457674 248 KAQgnviLVSVTKEEIPQLVKKLV 271
Cdd:PLN03211 322 VCQ----TDGVSEREKPNVKQSLV 341
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
25-211 |
8.15e-14 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 69.23 E-value: 8.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 25 SFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICG--HSIRTEREKA---LEQigaivENpELYDYMTGMQN- 98
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGqdHTTTPPSRRPvsmLFQ-----EN-NLFSHLTVAQNi 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 99 -LKHFANMAITQISKERIAEIVKLVELEHAIHKKVKTYSLGMKQRLGIAQALLHQPKILILDEPTNGLDPAgIRQirDYL 177
Cdd:PRK10771 93 gLGLNPGLKLNAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPA-LRQ--EML 169
|
170 180 190
....*....|....*....|....*....|....*..
gi 2753457674 178 QLLA---KEENIAVIVSSHLLSEIELMCDRVVIIKQG 211
Cdd:PRK10771 170 TLVSqvcQERQLTLLMVSHSLEDAARIAPRSLVVADG 206
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
2-218 |
9.69e-14 |
|
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: 71.48 E-value: 9.69e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 2 GNVVVKLENVRKKIGGTEIIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISmTEGDITICGHSIRT-EREKALEQI 80
Cdd:TIGR01271 1216 GQMDVQGLTAKYTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVSWNSvTLQTWRKAF 1294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 81 GAIvenPELYDYMTGM--QNLKHFAnmaitQISKERIAEIVKLVELEHAIHK---KVK--------TYSLGMKQRLGIAQ 147
Cdd:TIGR01271 1295 GVI---PQKVFIFSGTfrKNLDPYE-----QWSDEEIWKVAEEVGLKSVIEQfpdKLDfvlvdggyVLSNGHKQLMCLAR 1366
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2753457674 148 ALLHQPKILILDEPTNGLDPAGIRQIRDYLQllAKEENIAVIVSSHLLsEIELMCDRVVIIkQGEFVQEYN 218
Cdd:TIGR01271 1367 SILSKAKILLLDEPSAHLDPVTLQIIRKTLK--QSFSNCTVILSEHRV-EALLECQQFLVI-EGSSVKQYD 1433
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
20-193 |
1.24e-13 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 68.44 E-value: 1.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 20 IIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGHSIRTEREKALEQIGAIVENPELYDYMTGMQNL 99
Cdd:PRK13540 16 LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKQLCFVGHRSGINPYLTLRENC 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 100 K---HFANMAItqiskeRIAEIVKLVELEHAIHKKVKTYSLGMKQRLGIAQALLHQPKILILDEPTNGLDPAGIRQIRDY 176
Cdd:PRK13540 96 LydiHFSPGAV------GITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTIITK 169
|
170
....*....|....*..
gi 2753457674 177 LQLLAKEENiAVIVSSH 193
Cdd:PRK13540 170 IQEHRAKGG-AVLLTSH 185
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
19-216 |
1.26e-13 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 70.89 E-value: 1.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 19 EIIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGL-----ISMTEGDITICGHSIRTEREKAL-----EQIGAIVENPe 88
Cdd:PRK15134 23 TVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLlpsppVVYPSGDIRFHGESLLHASEQTLrgvrgNKIAMIFQEP- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 89 lydyMTGMQNLKHFANMAITQISKER-------IAEIVKLVE---LEHAiHKKVKTY----SLGMKQRLGIAQALLHQPK 154
Cdd:PRK15134 102 ----MVSLNPLHTLEKQLYEVLSLHRgmrreaaRGEILNCLDrvgIRQA-AKRLTDYphqlSGGERQRVMIAMALLTRPE 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2753457674 155 ILILDEPTNGLDPAGIRQIRDYLQLLAKEENIAVIVSSHLLSEIELMCDRVVIIKQGEFVQE 216
Cdd:PRK15134 177 LLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQ 238
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
3-194 |
2.45e-13 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 68.66 E-value: 2.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 3 NVVVKLENVRKKIGGTEIIRGLSFEVREGEVYGFLGPNGSGKTTTIR---MMTGLIS--MTEGDITICGHSIRTEREKAL 77
Cdd:PRK14243 8 ETVLRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRcfnRLNDLIPgfRVEGKVTFHGKNLYAPDVDPV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 78 E---QIGAIVENP-----ELYDYMT-GMQNLKHFANMaitqisKERIAEIVKLVELEHAIHKKVKTYSL----GMKQRLG 144
Cdd:PRK14243 88 EvrrRIGMVFQKPnpfpkSIYDNIAyGARINGYKGDM------DELVERSLRQAALWDEVKDKLKQSGLslsgGQQQRLC 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2753457674 145 IAQALLHQPKILILDEPTNGLDPAGIRQIRDYLQLLaKEENIAVIVSSHL 194
Cdd:PRK14243 162 IARAIAVQPEVILMDEPCSALDPISTLRIEELMHEL-KEQYTIIIVTHNM 210
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
28-208 |
2.52e-13 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 69.84 E-value: 2.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 28 VREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDiticgHSIRTEREKALEQI-GAivenpELYDYMTGMQN------LK 100
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILSGELIPNLGD-----YEEEPSWDEVLKRFrGT-----ELQNYFKKLYNgeikvvHK 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 101 hfaNMAITQISK--------------ER--IAEIVKLVELEHAIHKKVKTYSLGMKQRLGIAQALLHQPKILILDEPTNG 164
Cdd:PRK13409 166 ---PQYVDLIPKvfkgkvrellkkvdERgkLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSY 242
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2753457674 165 LDpagIRQ-------IRDYLqllakeENIAVIVSSHLLSEIELMCDRVVII 208
Cdd:PRK13409 243 LD---IRQrlnvarlIRELA------EGKYVLVVEHDLAVLDYLADNVHIA 284
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
2-207 |
3.14e-13 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 69.84 E-value: 3.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 2 GNVVVKLENVRKKIGG--TEIIRGlsfEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEG----DITIcghS-----IR 70
Cdd:PRK13409 337 RETLVEYPDLTKKLGDfsLEVEGG---EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGevdpELKI---SykpqyIK 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 71 TER----EKALEQIGAIVENPELYdymtgmqnlkhfanmaitqiskeriAEIVKLVELEHAIHKKVKTYSLGMKQRLGIA 146
Cdd:PRK13409 411 PDYdgtvEDLLRSITDDLGSSYYK-------------------------SEIIKPLQLERLLDKNVKDLSGGELQRVAIA 465
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2753457674 147 QALLHQPKILILDEPTNGLDP----AGIRQIRDYlqllAKEENIAVIVSSHLLSEIELMCDRVVI 207
Cdd:PRK13409 466 ACLSRDADLYLLDEPSAHLDVeqrlAVAKAIRRI----AEEREATALVVDHDIYMIDYISDRLMV 526
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
6-228 |
4.22e-13 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 69.62 E-value: 4.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 6 VKLENV--RKKIGGTEIIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGHSIR----TEREKALEq 79
Cdd:PLN03232 1235 IKFEDVhlRYRPGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAkfglTDLRRVLS- 1313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 80 igAIVENPELYDyMTGMQNLKHFA--NMAITQISKERiAEIVKLVE-----LEHAIHKKVKTYSLGMKQRLGIAQALLHQ 152
Cdd:PLN03232 1314 --IIPQSPVLFS-GTVRFNIDPFSehNDADLWEALER-AHIKDVIDrnpfgLDAEVSEGGENFSVGQRQLLSLARALLRR 1389
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2753457674 153 PKILILDEPTNGLDpagIRqIRDYLQLLAKEE--NIAVIVSSHLLSEIeLMCDRVVIIKQGEfVQEYNLHEQAKHDET 228
Cdd:PLN03232 1390 SKILVLDEATASVD---VR-TDSLIQRTIREEfkSCTMLVIAHRLNTI-IDCDKILVLSSGQ-VLEYDSPQELLSRDT 1461
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
6-214 |
4.34e-13 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 67.73 E-value: 4.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 6 VKLENVRKKIGGTEIIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGHSIR--TEREKA-----LE 78
Cdd:PRK11231 3 LRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISmlSSRQLArrlalLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 79 QIGAIVEN---PELYDYmtGMQ-NLKHFANMaiTQISKERIAEIVKLVELEHAIHKKVKTYSLGMKQRLGIAQALLHQPK 154
Cdd:PRK11231 83 QHHLTPEGitvRELVAY--GRSpWLSLWGRL--SAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 155 ILILDEPTNGLDPAGIRQIRDYLQLLaKEENIAVIVSSHLLSEIELMCDRVVIIKQGEFV 214
Cdd:PRK11231 159 VVLLDEPTTYLDINHQVELMRLMREL-NTQGKTVVTVLHDLNQASRYCDHLVVLANGHVM 217
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
1-207 |
5.50e-13 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 69.04 E-value: 5.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 1 MGNVVVKLENVRKKIGG--TEIIRGlsfEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDIticghsirterEKALE 78
Cdd:COG1245 337 EEETLVEYPDLTKSYGGfsLEVEGG---EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEV-----------DEDLK 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 79 qigaIVENPElY---DY-MTGMQNLKHFANMAITqiSKERIAEIVKLVELEHAIHKKVKTYSLGMKQRLGIAQALLHQPK 154
Cdd:COG1245 403 ----ISYKPQ-YispDYdGTVEEFLRSANTDDFG--SSYYKTEIIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDAD 475
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2753457674 155 ILILDEPTNGLDP----AGIRQIRDYlqllAKEENIAVIVSSHLLSEIELMCDRVVI 207
Cdd:COG1245 476 LYLLDEPSAHLDVeqrlAVAKAIRRF----AENRGKTAMVVDHDIYLIDYISDRLMV 528
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
6-296 |
6.34e-13 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 68.22 E-value: 6.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 6 VKLENVRKKIGGTEIIRGLSFEVREGEVYGFLGPNGSGKTTTI---------------RMMTGLISMTEGDITICGHS-I 69
Cdd:NF000106 14 VEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RGAlpahv*gpdagrrpwRF*TWCANRRALRRTIG*HRpV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 70 RTEREKALeqigaivenpelydymTGMQNLKHFANMA--ITQISKERIAEIVKLVELEHAIHKKVKTYSLGMKQRLGIAQ 147
Cdd:NF000106 94 R*GRRESF----------------SGRENLYMIGR*LdlSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 148 ALLHQPKILILDEPTNGLDPAGIRQIRDYLQLLAKeENIAVIVSSHLLSEIELMCDRVVIIKQGEFVQEYNLHEQAKHDE 227
Cdd:NF000106 158 SMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVR-DGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDELKTKVG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 228 TVVVAFEVDQVQKANEIVQGKAQ---------------GNVILVSVTKEEIPQLVKKLVNDDVLVYGVTVQNKTLEDEFL 292
Cdd:NF000106 237 GRTLQIRPAHAAELDRMVGAIAQagldgiagatadhedGVVNVPIVSDEQLSAVVGMLGERGFTISGHQHPSAQL*EVFL 316
|
....
gi 2753457674 293 AITG 296
Cdd:NF000106 317 AITG 320
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
5-216 |
6.49e-13 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 66.73 E-value: 6.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 5 VVKLENVRKKIGGTE----IIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGHSIRTEREKA---- 76
Cdd:PRK10584 6 IVEVHHLKKSVGQGEhelsILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEArakl 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 77 -LEQIGAIVENPELYDYMTGMQNLKHFANM--AITQISKERIAEIVKLVELEHAIHKKVKTYSLGMKQRLGIAQALLHQP 153
Cdd:PRK10584 86 rAKHVGFVFQSFMLIPTLNALENVELPALLrgESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRP 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2753457674 154 KILILDEPTNGLDPAGIRQIRDYLQLLAKEENIAVIVSSHlLSEIELMCDRVVIIKQGEFVQE 216
Cdd:PRK10584 166 DVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTH-DLQLAARCDRRLRLVNGQLQEE 227
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
25-215 |
7.13e-13 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 68.01 E-value: 7.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 25 SFEVREGEVYGFLGPNGSGKTTTIRMMTGLIS---------MTEGDITICGHSIRTEREKALEQIGAIVENPElyDYMTG 95
Cdd:COG4170 27 SLTLNEGEIRGLVGESGSGKSLIAKAICGITKdnwhvtadrFRWNGIDLLKLSPRERRKIIGREIAMIFQEPS--SCLDP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 96 MQNLKHFANMAITQIS---------KERIAEIVKLVeleHAI----HKKV-KTY----SLGMKQRLGIAQALLHQPKILI 157
Cdd:COG4170 105 SAKIGDQLIEAIPSWTfkgkwwqrfKWRKKRAIELL---HRVgikdHKDImNSYphelTEGECQKVMIAMAIANQPRLLI 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2753457674 158 LDEPTNGLDPAGIRQIRDYLQLLAKEENIAVIVSSHLLSEIELMCDRVVIIKQGEFVQ 215
Cdd:COG4170 182 ADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYCGQTVE 239
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
5-191 |
8.76e-13 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 68.61 E-value: 8.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 5 VVKLENVRKKIGGTEIIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGHSI--RTEREKALEQI-- 80
Cdd:NF033858 1 VARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMadARHRRAVCPRIay 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 81 -----GaivENpeLYDYMTGMQNLKHFANMaITQISKERIAEIVKLVE-------LEHAIHKkvktYSLGMKQRLGIAQA 148
Cdd:NF033858 81 mpqglG---KN--LYPTLSVFENLDFFGRL-FGQDAAERRRRIDELLRatglapfADRPAGK----LSGGMKQKLGLCCA 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2753457674 149 LLHQPKILILDEPTNGLDPAGIRQ-------IRdylqllAKEENIAVIVS 191
Cdd:NF033858 151 LIHDPDLLILDEPTTGVDPLSRRQfwelidrIR------AERPGMSVLVA 194
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
25-232 |
1.79e-12 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 67.24 E-value: 1.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 25 SFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGH--SIRTEREkALEQigAIVENPE--LYDYMTGM---- 96
Cdd:PRK11288 273 SFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKpiDIRSPRD-AIRA--GIMLCPEdrKAEGIIPVhsva 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 97 QNL-----KHF--ANMAITQISKERIAE--IVKLVELEHAIHKKVKTYSLGMKQRLGIAQALLHQPKILILDEPTNGLDP 167
Cdd:PRK11288 350 DNInisarRHHlrAGCLINNRWEAENADrfIRSLNIKTPSREQLIMNLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDV 429
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2753457674 168 AGIRQIRDYLQLLAkEENIAVIVSSHLLSEIELMCDRVVIIKQGEFVQEYnLHEQAKHDETVVVA 232
Cdd:PRK11288 430 GAKHEIYNVIYELA-AQGVAVLFVSSDLPEVLGVADRIVVMREGRIAGEL-AREQATERQALSLA 492
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
41-222 |
1.99e-12 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 67.75 E-value: 1.99e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 41 GSGKTTTIRMMTGLISMTegDITICGHSIRTerekaLEQIGAIV-ENPELYDyMTGMQNLKhFANMAITQISKERIAEIV 119
Cdd:PTZ00265 1265 GSGEDSTVFKNSGKILLD--GVDICDYNLKD-----LRNLFSIVsQEPMLFN-MSIYENIK-FGKEDATREDVKRACKFA 1335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 120 KLVELEHAIHKKV--------KTYSLGMKQRLGIAQALLHQPKILILDEPTNGLDPAGIRQIRDYLQLLAKEENIAVIVS 191
Cdd:PTZ00265 1336 AIDEFIESLPNKYdtnvgpygKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITI 1415
|
170 180 190
....*....|....*....|....*....|....*
gi 2753457674 192 SHLLSEIElMCDRVVII----KQGEFVQEYNLHEQ 222
Cdd:PTZ00265 1416 AHRIASIK-RSDKIVVFnnpdRTGSFVQAHGTHEE 1449
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
1-216 |
2.01e-12 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 65.78 E-value: 2.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 1 MGNVVVKL--ENVRKKIGGTEIIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGHSIRTEREKAL- 77
Cdd:PRK10253 1 MTESVARLrgEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVa 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 78 EQIGAIVENPELYDYMTgMQNL----KHFANMAITQISKE---RIAEIVKLVELEHAIHKKVKTYSLGMKQRLGIAQALL 150
Cdd:PRK10253 81 RRIGLLAQNATTPGDIT-VQELvargRYPHQPLFTRWRKEdeeAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2753457674 151 HQPKILILDEPTNGLDPAgiRQIrDYLQLLA---KEENIAVIVSSHLLSEIELMCDRVVIIKQGEFVQE 216
Cdd:PRK10253 160 QETAIMLLDEPTTWLDIS--HQI-DLLELLSelnREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQ 225
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
5-221 |
2.56e-12 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 65.49 E-value: 2.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 5 VVKLENVRKKIGGtEIIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGL----ISMTEGDITICGHSIRTEREKAlEQI 80
Cdd:PRK10418 4 QIELRNIALQAAQ-PLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGIlpagVRQTAGRVLLDGKPVAPCALRG-RKI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 81 GAIVENPElyDYMTGMQNLKHFANMAITQISKE----RIAEIVKLVELEHAiHKKVKTY----SLGMKQRLGIAQALLHQ 152
Cdd:PRK10418 82 ATIMQNPR--SAFNPLHTMHTHARETCLALGKPaddaTLTAALEAVGLENA-ARVLKLYpfemSGGMLQRMMIALALLCE 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2753457674 153 PKILILDEPTNGLDPAGIRQIRDYLQLLAKEENIAVIVSSHLLSEIELMCDRVVIIKQGEFVQEYNLHE 221
Cdd:PRK10418 159 APFIIADEPTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVET 227
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
2-218 |
2.70e-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: 65.65 E-value: 2.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 2 GNVVVKLENVRKKIGGTEIIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISmTEGDITICGHSIRT-EREKALEQI 80
Cdd:cd03289 1 GQMTVKDLTAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSvPLQKWRKAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 81 GAIvenPELYDYMTGM--QNLKHFANMAITQISKerIAEIVKLV--------ELEHAIHKKVKTYSLGMKQRLGIAQALL 150
Cdd:cd03289 80 GVI---PQKVFIFSGTfrKNLDPYGKWSDEEIWK--VAEEVGLKsvieqfpgQLDFVLVDGGCVLSHGHKQLMCLARSVL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2753457674 151 HQPKILILDEPTNGLDPAGIRQIRDYL-QLLAkeeNIAVIVSSHLLsEIELMCDRVVIIKQGEfVQEYN 218
Cdd:cd03289 155 SKAKILLLDEPSAHLDPITYQVIRKTLkQAFA---DCTVILSEHRI-EAMLECQRFLVIEENK-VRQYD 218
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
3-246 |
6.20e-12 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 65.90 E-value: 6.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 3 NVVVKLENVRKKI----GGTEIIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGHSIRTEREKAL- 77
Cdd:PRK10535 2 TALLELKDIRRSYpsgeEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALa 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 78 ----EQIGAIVENPELYDYMTGMQNLKH---FANMAITQiSKERIAEIVKLVELEHAIHKKVKTYSLGMKQRLGIAQALL 150
Cdd:PRK10535 82 qlrrEHFGFIFQRYHLLSHLTAAQNVEVpavYAGLERKQ-RLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 151 HQPKILILDEPTNGLDPAGIRQIRDYLQLLaKEENIAVIVSSHlLSEIELMCDRVVIIKQGEFVQEYNLHEQAKhdetvV 230
Cdd:PRK10535 161 NGGQVILADEPTGALDSHSGEEVMAILHQL-RDRGHTVIIVTH-DPQVAAQAERVIEIRDGEIVRNPPAQEKVN-----V 233
|
250
....*....|....*.
gi 2753457674 231 VAFEVDQVQKANEIVQ 246
Cdd:PRK10535 234 AGGTEPVVNTASGWRQ 249
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
1-191 |
6.42e-12 |
|
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: 65.73 E-value: 6.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 1 MGNVVVKLENVRKKIGGTEIIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITIcGHSIR-----TEREk 75
Cdd:TIGR03719 318 LGDKVIEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETVKlayvdQSRD- 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 76 aleqigAIVENPELYDYMTGMQNlkhfanmaITQISKERI---AEIVKLVELEHAIHKKVKTYSLGMKQRLGIAQALLHQ 152
Cdd:TIGR03719 396 ------ALDPNKTVWEEISGGLD--------IIKLGKREIpsrAYVGRFNFKGSDQQKKVGQLSGGERNRVHLAKTLKSG 461
|
170 180 190
....*....|....*....|....*....|....*....
gi 2753457674 153 PKILILDEPTNGLDPAGIRQIRDYLQLLAkeeNIAVIVS 191
Cdd:TIGR03719 462 GNVLLLDEPTNDLDVETLRALEEALLNFA---GCAVVIS 497
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
20-222 |
7.20e-12 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 65.50 E-value: 7.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 20 IIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGHSIRTEREKALEQIGAIV-ENPELY-DYMTGmq 97
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVsQTPFLFsDTVAN-- 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 98 nlkhfaNMAITQ--ISKERIAEIVKLVELEHAIHKKVKTY-----------SLGMKQRLGIAQALLHQPKILILDEPTNG 164
Cdd:PRK10789 408 ------NIALGRpdATQQEIEHVARLASVHDDILRLPQGYdtevgergvmlSGGQKQRISIARALLLNAEILILDDALSA 481
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2753457674 165 LDPAGIRQIrdyLQLLAK-EENIAVIVSSHLLSEIElMCDRVVIIKQGEFVQEYNlHEQ 222
Cdd:PRK10789 482 VDGRTEHQI---LHNLRQwGEGRTVIISAHRLSALT-EASEILVMQHGHIAQRGN-HDQ 535
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
2-166 |
7.52e-12 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 65.74 E-value: 7.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 2 GNVVVKLENVRKKIGGTEIIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITiCGhsirTEREKA-LEQI 80
Cdd:PRK11147 316 GKIVFEMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIH-CG----TKLEVAyFDQH 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 81 GAIVEnPElydyMTGMQNLkhfanmaitqiskeriAEIVKLVEL----EHAI--------HKK-----VKTYSLGMKQRL 143
Cdd:PRK11147 391 RAELD-PE----KTVMDNL----------------AEGKQEVMVngrpRHVLgylqdflfHPKramtpVKALSGGERNRL 449
|
170 180
....*....|....*....|...
gi 2753457674 144 GIAQALLHQPKILILDEPTNGLD 166
Cdd:PRK11147 450 LLARLFLKPSNLLILDEPTNDLD 472
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
8-222 |
7.91e-12 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 64.04 E-value: 7.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 8 LENVRKKIGGTEIIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGL--ISMTEGDITICGHSIR--TEREKALEQIGAI 83
Cdd:PRK09580 4 IKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKDLLelSPEDRAGEGIFMA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 84 VENPElydYMTGMQNlKHFANMAITQISKERIAEIVKLVELEHAIHKKVKT---------------YSLGMKQRLGIAQA 148
Cdd:PRK09580 84 FQYPV---EIPGVSN-QFFLQTALNAVRSYRGQEPLDRFDFQDLMEEKIALlkmpedlltrsvnvgFSGGEKKRNDILQM 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 149 LLHQPKILILDEPTNGLDPAGIRQIRDYLQLLaKEENIAVIVSSHLLSEIELMCDRVV-------IIKQGEFVQEYNLHE 221
Cdd:PRK09580 160 AVLEPELCILDESDSGLDIDALKIVADGVNSL-RDGKRSFIIVTHYQRILDYIKPDYVhvlyqgrIVKSGDFTLVKQLEE 238
|
.
gi 2753457674 222 Q 222
Cdd:PRK09580 239 Q 239
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
10-221 |
2.53e-11 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 63.66 E-value: 2.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 10 NVRKKIGGTEIIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGL--ISMTEGDITICGHSIRTEREKALEQIGAIVENP 87
Cdd:NF040905 6 GITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVypHGSYEGEILFDGEVCRFKDIRDSEALGIVIIHQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 88 EL--YDYMTGMQNL----KHFANMAIT-QISKERIAEIVKLVELEHAIHKKVKTYSLGMKQRLGIAQALLHQPKILILDE 160
Cdd:NF040905 86 ELalIPYLSIAENIflgnERAKRGVIDwNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLILDE 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2753457674 161 PTNGLDPAGIRQIrdyLQLLA--KEENIAVIVSSHLLSEIELMCDRVVIIKQGEFVQEYNLHE 221
Cdd:NF040905 166 PTAALNEEDSAAL---LDLLLelKAQGITSIIISHKLNEIRRVADSITVLRDGRTIETLDCRA 225
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
25-190 |
3.29e-11 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 63.50 E-value: 3.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 25 SFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDitiCGHSIRTEREKALEQIGAIVENpELYDYMTGM-----QNL 99
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGE---RQSQFSHITRLSFEQLQKLVSD-EWQRNNTDMlspgeDDT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 100 KHFANMAITQISK--ERIAEIVKLVELEHAIHKKVKTYSLGMKQRLGIAQALLHQPKILILDEPTNGLDPAGIRQIRDYL 177
Cdd:PRK10938 99 GRTTAEIIQDEVKdpARCEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELL 178
|
170
....*....|...
gi 2753457674 178 QLLAKEENIAVIV 190
Cdd:PRK10938 179 ASLHQSGITLVLV 191
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
8-214 |
3.49e-11 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 63.60 E-value: 3.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 8 LENVRKKIGGTEIIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGHSIRTEREK-ALEQ-IGAIVE 85
Cdd:PRK10982 1 MSNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKeALENgISMVHQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 86 NPELYDYMTGMQN--LKHFANMAI----TQISKERIAeIVKLVELEHAIHKKVKTYSLGMKQRLGIAQALLHQPKILILD 159
Cdd:PRK10982 81 ELNLVLQRSVMDNmwLGRYPTKGMfvdqDKMYRDTKA-IFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMD 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2753457674 160 EPTNGLDPAGIRQIRDYLQLLaKEENIAVIVSSHLLSEIELMCDRVVIIKQGEFV 214
Cdd:PRK10982 160 EPTSSLTEKEVNHLFTIIRKL-KERGCGIVYISHKMEEIFQLCDEITILRDGQWI 213
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
5-193 |
6.02e-11 |
|
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: 62.84 E-value: 6.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 5 VVKLENVRKKI-GGTEIIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITIcghsirtereKALEQIGAI 83
Cdd:TIGR00954 451 GIKFENIPLVTpNGDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTK----------PAKGKLFYV 520
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 84 VENPelydYMTgmqnLKHFANMAITQISKER----------IAEIVKLVELEHAIHKKV---------KTYSLGMKQRLG 144
Cdd:TIGR00954 521 PQRP----YMT----LGTLRDQIIYPDSSEDmkrrglsdkdLEQILDNVQLTHILEREGgwsavqdwmDVLSGGEKQRIA 592
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2753457674 145 IAQALLHQPKILILDEPTNGLDPagirQIRDYLQLLAKEENIAVIVSSH 193
Cdd:TIGR00954 593 MARLFYHKPQFAILDECTSAVSV----DVEGYMYRLCREFGITLFSVSH 637
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
6-166 |
1.57e-10 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 61.45 E-value: 1.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 6 VKLENVRKKIGGTEIIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICghsirterEKAleQIGAIVE 85
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWS--------ENA--NIGYYAQ 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 86 NPElYDYMTGMqNLkhFANMAitQISKERIAEIV------KLVELEHAIHKKVKTYSLGMKQRLGIAQALLHQPKILILD 159
Cdd:PRK15064 390 DHA-YDFENDL-TL--FDWMS--QWRQEGDDEQAvrgtlgRLLFSQDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLVMD 463
|
....*..
gi 2753457674 160 EPTNGLD 166
Cdd:PRK15064 464 EPTNHMD 470
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
2-64 |
1.58e-10 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 61.67 E-value: 1.58e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2753457674 2 GNVVVKLENVRKKIGGTEIIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITI 64
Cdd:PRK11819 321 GDKVIEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI 383
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
28-208 |
2.11e-10 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 60.07 E-value: 2.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 28 VREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGditicghsiRTEREKALEQIGAIVENPELYDYMTGM----------- 96
Cdd:cd03236 23 PREGQVLGLVGPNGIGKSTALKILAGKLKPNLG---------KFDDPPDWDEILDEFRGSELQNYFTKLlegdvkvivkp 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 97 QNL----KHFANMAITQISK----ERIAEIVKLVELEHAIHKKVKTYSLGMKQRLGIAQALLHQPKILILDEPTNGLDpa 168
Cdd:cd03236 94 QYVdlipKAVKGKVGELLKKkderGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLD-- 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2753457674 169 gIRQ-------IRDylqlLAKEENiAVIVSSHLLSEIELMCDRVVII 208
Cdd:cd03236 172 -IKQrlnaarlIRE----LAEDDN-YVLVVEHDLAVLDYLSDYIHCL 212
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
5-216 |
2.70e-10 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 59.78 E-value: 2.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 5 VVKLENVRKKIGGTEIIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGHSI----RTEREKALEQI 80
Cdd:PRK11831 7 LVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIpamsRSRLYTVRKRM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 81 GAIVENPELYDYMTGMQNLKhFANMAITQISKERIAEIV--KL--VELEHAIHKKVKTYSLGMKQRLGIAQALLHQPKIL 156
Cdd:PRK11831 87 SMLFQSGALFTDMNVFDNVA-YPLREHTQLPAPLLHSTVmmKLeaVGLRGAAKLMPSELSGGMARRAALARAIALEPDLI 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 157 ILDEPTNGLDPAGIRQIRDYLQLLAKEENIAVIVSSHLLSEIELMCDRVVIIKQGEFVQE 216
Cdd:PRK11831 166 MFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAH 225
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
2-211 |
8.46e-10 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 59.79 E-value: 8.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 2 GNVVVKLENVRKKIGGTEIIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGHSIRTEREKAL-EQI 80
Cdd:PTZ00243 1307 GSLVFEGVQMRYREGLPLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELrRQF 1386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 81 GAIVENPELYDyMTGMQNLKHFanmaiTQISKERIAEIVKLVEL-EH------AIHKKV----KTYSLGMKQRLGIAQAL 149
Cdd:PTZ00243 1387 SMIPQDPVLFD-GTVRQNVDPF-----LEASSAEVWAALELVGLrERvaseseGIDSRVleggSNYSVGQRQLMCMARAL 1460
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2753457674 150 LHQPKILIL-DEPTNGLDPAGIRQIRDylQLLAKEENIAVIVSSHLLSEIElMCDRVVIIKQG 211
Cdd:PTZ00243 1461 LKKGSGFILmDEATANIDPALDRQIQA--TVMSAFSAYTVITIAHRLHTVA-QYDKIIVMDHG 1520
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
24-215 |
1.25e-09 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 58.28 E-value: 1.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 24 LSFEVREGEVYGFLGPNGSGKTTTIRMMTGLIS---------MTEGDITICGHSIRTEREKALEQIGAIVENPElydymT 94
Cdd:PRK15093 26 VSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKdnwrvtadrMRFDDIDLLRLSPRERRKLVGHNVSMIFQEPQ-----S 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 95 GMQNLKHFANMAITQIS----KERIAEIV-----KLVELEHAI----HKKVK---TYSL--GMKQRLGIAQALLHQPKIL 156
Cdd:PRK15093 101 CLDPSERVGRQLMQNIPgwtyKGRWWQRFgwrkrRAIELLHRVgikdHKDAMrsfPYELteGECQKVMIAIALANQPRLL 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2753457674 157 ILDEPTNGLDPAGIRQIRDYLQLLAKEENIAVIVSSHLLSEIELMCDRVVIIKQGEFVQ 215
Cdd:PRK15093 181 IADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTVE 239
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
21-211 |
1.48e-09 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 58.59 E-value: 1.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 21 IRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGHSIRTEreKALEQIG---AIVENPE----LYDYM 93
Cdd:PRK10982 264 IRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNH--NANEAINhgfALVTEERrstgIYAYL 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 94 -----TGMQNLKHFANmAITQISKERIAEIVKLV----ELEHAIHK-KVKTYSLGMKQRLGIAQALLHQPKILILDEPTN 163
Cdd:PRK10982 342 digfnSLISNIRNYKN-KVGLLDNSRMKSDTQWVidsmRVKTPGHRtQIGSLSGGNQQKVIIGRWLLTQPEILMLDEPTR 420
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2753457674 164 GLDPAGIRQIRDYLQLLAKEENIAVIVSSHlLSEIELMCDRVVIIKQG 211
Cdd:PRK10982 421 GIDVGAKFEIYQLIAELAKKDKGIIIISSE-MPELLGITDRILVMSNG 467
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
6-217 |
1.71e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 58.60 E-value: 1.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 6 VKLENV--RKKIGGTEIIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGHSIR----TEREKALeq 79
Cdd:PLN03130 1238 IKFEDVvlRYRPELPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISkfglMDLRKVL-- 1315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 80 iGAIVENPELYDyMTGMQNLKHFA--NMAITQISKERiAEIVKLVE-----LEHAIHKKVKTYSLGMKQRLGIAQALLHQ 152
Cdd:PLN03130 1316 -GIIPQAPVLFS-GTVRFNLDPFNehNDADLWESLER-AHLKDVIRrnslgLDAEVSEAGENFSVGQRQLLSLARALLRR 1392
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2753457674 153 PKILILDEPTNGLDpagIRQirDYL-QLLAKEE--NIAVIVSSHLLSEIeLMCDRVVIIKQGEfVQEY 217
Cdd:PLN03130 1393 SKILVLDEATAAVD---VRT--DALiQKTIREEfkSCTMLIIAHRLNTI-IDCDRILVLDAGR-VVEF 1453
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
31-212 |
2.04e-09 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 55.07 E-value: 2.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 31 GEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITIcghsirterekaleqigaivenpelydymtgmqnlkhfanmaitqI 110
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIY---------------------------------------------I 36
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 111 SKERIAEIVKLVELEHAIHKKVKTYSLGMKQRLGIAQALLHQPKILILDEPTNGLDPAGIRQIRDY-----LQLLAKEEN 185
Cdd:smart00382 37 DGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLeelrlLLLLKSEKN 116
|
170 180 190
....*....|....*....|....*....|..
gi 2753457674 186 IAVIVSSHLLS-----EIELMCDRVVIIKQGE 212
Cdd:smart00382 117 LTVILTTNDEKdlgpaLLRRRFDRRIVLLLIL 148
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
2-218 |
3.13e-09 |
|
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: 58.03 E-value: 3.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 2 GNVVVKLENVRKKIGGTEIIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICG--------HSIRTer 73
Cdd:TIGR00957 1283 GRVEFRNYCLRYREDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGlniakiglHDLRF-- 1360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 74 ekaleQIGAIVENPELYDYMTGMqNLKHFAnmaitQISKERIAEIVKLV-----------ELEHAIHKKVKTYSLGMKQR 142
Cdd:TIGR00957 1361 -----KITIIPQDPVLFSGSLRM-NLDPFS-----QYSDEEVWWALELAhlktfvsalpdKLDHECAEGGENLSVGQRQL 1429
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2753457674 143 LGIAQALLHQPKILILDEPTNGLDPAGIRQIRDYLQllAKEENIAVIVSSHLLSEIeLMCDRVVIIKQGEfVQEYN 218
Cdd:TIGR00957 1430 VCLARALLRKTKILVLDEATAAVDLETDNLIQSTIR--TQFEDCTVLTIAHRLNTI-MDYTRVIVLDKGE-VAEFG 1501
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
24-212 |
4.57e-09 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 56.90 E-value: 4.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 24 LSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGHSIRTE-REKALEQIGAIVENPELYDYMTGMQNlkHF 102
Cdd:PRK10522 342 INLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEqPEDYRKLFSAVFTDFHLFDQLLGPEG--KP 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 103 ANMAITQISKERIaEIVKLVELEHaiHKKVKT-YSLGMKQRLGIAQALLHQPKILILDEPTNGLDPagirQIRD--YLQL 179
Cdd:PRK10522 420 ANPALVEKWLERL-KMAHKLELED--GRISNLkLSKGQKKRLALLLALAEERDILLLDEWAADQDP----HFRRefYQVL 492
|
170 180 190
....*....|....*....|....*....|....*
gi 2753457674 180 LA--KEENIAVIVSSHLLSEIElMCDRVVIIKQGE 212
Cdd:PRK10522 493 LPllQEMGKTIFAISHDDHYFI-HADRLLEMRNGQ 526
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
9-193 |
4.58e-09 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 56.82 E-value: 4.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 9 ENVRKKIGGteiirglsfevreGEVYGFLGPNGSGKTTTIRMMTGLISMTEG--------------------------DI 62
Cdd:PRK15064 18 ENISVKFGG-------------GNRYGLIGANGCGKSTFMKILGGDLEPSAGnvsldpnerlgklrqdqfafeeftvlDT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 63 TICGHsirTEREKALEQIGAIVENPELY--DYMTGMQNLKHFANM-AITQISkeRIAEIVKLVELEHAIHkkvktYSL-- 137
Cdd:PRK15064 85 VIMGH---TELWEVKQERDRIYALPEMSeeDGMKVADLEVKFAEMdGYTAEA--RAGELLLGVGIPEEQH-----YGLms 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 138 ----GMKQRLGIAQALLHQPKILILDEPTNGLDPAGIRQIRDYLqllaKEENIAVIVSSH 193
Cdd:PRK15064 155 evapGWKLRVLLAQALFSNPDILLLDEPTNNLDINTIRWLEDVL----NERNSTMIIISH 210
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
10-178 |
1.89e-08 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 55.33 E-value: 1.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 10 NVRKKIGGT-EIIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITIC-GHSI------------RTEREK 75
Cdd:TIGR03719 9 RVSKVVPPKkEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQpGIKVgylpqepqldptKTVREN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 76 ALEQIGAIVENPELYD--YMTGMQNLKHFANMAITQISKERIAEIVKLVELEHAIH------------KKVKTYSLGMKQ 141
Cdd:TIGR03719 89 VEEGVAEIKDALDRFNeiSAKYAEPDADFDKLAAEQAELQEIIDAADAWDLDSQLEiamdalrcppwdADVTKLSGGERR 168
|
170 180 190
....*....|....*....|....*....|....*..
gi 2753457674 142 RLGIAQALLHQPKILILDEPTNGLDPAGIRQIRDYLQ 178
Cdd:TIGR03719 169 RVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQ 205
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
20-214 |
2.67e-08 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 53.68 E-value: 2.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 20 IIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLIS--------MTEGDITICGHSIRTEREKALEQIGAIVEN----- 86
Cdd:PRK13547 16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTgggaprgaRVTGDVTLNGEPLAAIDAPRLARLRAVLPQaaqpa 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 87 -PELYDYMTGMQNLKHFANMAITQISKERIA-EIVKLVELEHAIHKKVKTYSLGMKQRLGIAQAL--LH-------QPKI 155
Cdd:PRK13547 96 fAFSAREIVLLGRYPHARRAGALTHRDGEIAwQALALAGATALVGRDVTTLSGGELARVQFARVLaqLWpphdaaqPPRY 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2753457674 156 LILDEPTNGLDPAGIRQIRDYLQLLAKEENIAVIVSSHLLSEIELMCDRVVIIKQGEFV 214
Cdd:PRK13547 176 LLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIV 234
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
19-166 |
2.72e-08 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 54.85 E-value: 2.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 19 EIIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLIS--MTEGDITICGHsirTEREKALEQIGAIVENPELYD-YMTG 95
Cdd:PLN03140 894 QLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTggYIEGDIRISGF---PKKQETFARISGYCEQNDIHSpQVTV 970
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 96 MQNLKHFANMAI-TQISKE-------RIAEIVKLVELEHAI--HKKVKTYSLGMKQRLGIAQALLHQPKILILDEPTNGL 165
Cdd:PLN03140 971 RESLIYSAFLRLpKEVSKEekmmfvdEVMELVELDNLKDAIvgLPGVTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGL 1050
|
.
gi 2753457674 166 D 166
Cdd:PLN03140 1051 D 1051
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
20-212 |
2.97e-08 |
|
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: 52.86 E-value: 2.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 20 IIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGhSIRTEREKALEQIGAIVENpelydymtgmqnl 99
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG-SIAYVSQEPWIQNGTIREN------------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 100 khfanmaIT---QISKERIAEIVK-------LVELEHA----IHKKVKTYSLGMKQRLGIAQALLHQPKILILDEPTNGL 165
Cdd:cd03250 86 -------ILfgkPFDEERYEKVIKacalepdLEILPDGdlteIGEKGINLSGGQKQRISLARAVYSDADIYLLDDPLSAV 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2753457674 166 DPAGIRQIRDYLQLLAKEENIAVIVSSHLLSEIELmCDRVVIIKQGE 212
Cdd:cd03250 159 DAHVGRHIFENCILGLLLNNKTRILVTHQLQLLPH-ADQIVVLDNGR 204
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
28-166 |
4.52e-08 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 54.34 E-value: 4.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 28 VREGEVYGFLGPNGSGKTTTI-----RMMTGLIsmTEGDITICGHsirtEREKALEQIGAIVENPELY-DYMTGMQNLKH 101
Cdd:TIGR00956 786 VKPGTLTALMGASGAGKTTLLnvlaeRVTTGVI--TGGDRLVNGR----PLDSSFQRSIGYVQQQDLHlPTSTVRESLRF 859
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2753457674 102 FANM----AITQISKER-IAEIVKLVELEHAIHKKVKTYSLGM----KQRLGIAQALLHQPKILI-LDEPTNGLD 166
Cdd:TIGR00956 860 SAYLrqpkSVSKSEKMEyVEEVIKLLEMESYADAVVGVPGEGLnveqRKRLTIGVELVAKPKLLLfLDEPTSGLD 934
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
28-211 |
6.83e-08 |
|
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: 51.86 E-value: 6.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 28 VREGEVYGFLGPNGSGKTTTI-----RMMTGLIsmtEGDITICGHsirtEREKALEQIGAIVEnpelydymtgmQNLKHF 102
Cdd:cd03232 30 VKPGTLTALMGESGAGKTTLLdvlagRKTAGVI---TGEILINGR----PLDKNFQRSTGYVE-----------QQDVHS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 103 ANmaitqiSKERIAeivklveLEhaIHKKVKTYSLGMKQRLGIAQALLHQPKILILDEPTNGLDPAGIRQIRDYLQLLAk 182
Cdd:cd03232 92 PN------LTVREA-------LR--FSALLRGLSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFLKKLA- 155
|
170 180 190
....*....|....*....|....*....|
gi 2753457674 183 EENIAVIVSSHLLSE-IELMCDRVVIIKQG 211
Cdd:cd03232 156 DSGQAILCTIHQPSAsIFEKFDRLLLLKRG 185
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
38-198 |
7.49e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 51.80 E-value: 7.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 38 GPNGSGKTTTIRMMTGLISMTEGDITICGHSIRTEREKALEQIGaivENPELYDYMTGMQNLKHFANMaitQISKERIAE 117
Cdd:PRK13541 33 GANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKPYCTYIG---HNLGLKLEMTVFENLKFWSEI---YNSAETLYA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 118 IVKLVELEHAIHKKVKTYSLGMKQRLGIAQALLHQPKILILDEPTNGLDpagiRQIRDYL-QLLAKEENIAVIV--SSHL 194
Cdd:PRK13541 107 AIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLS----KENRDLLnNLIVMKANSGGIVllSSHL 182
|
....
gi 2753457674 195 LSEI 198
Cdd:PRK13541 183 ESSI 186
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
24-193 |
8.40e-08 |
|
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: 53.26 E-value: 8.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 24 LSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGHSI-RTEREKALEQIGAIVENPELYDYMTGMQNlkhf 102
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVtADNREAYRQLFSAVFSDFHLFDRLLGLDG---- 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 103 anmaitQISKERIAEIVKLVELEHaihkKVK-------T--YSLGMKQRLGIAQALLHQPKILILDEPTNGLDPagirQI 173
Cdd:COG4615 427 ------EADPARARELLERLELDH----KVSvedgrfsTtdLSQGQRKRLALLVALLEDRPILVFDEWAADQDP----EF 492
|
170 180
....*....|....*....|....
gi 2753457674 174 RD--YLQLLA--KEENIAVIVSSH 193
Cdd:COG4615 493 RRvfYTELLPelKARGKTVIAISH 516
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
26-214 |
8.86e-08 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 53.03 E-value: 8.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 26 FEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGhSIRTERekaLEQIGAIVENPELYDYMT-GMQNL----- 99
Cdd:PRK11147 24 LHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQ-DLIVAR---LQQDPPRNVEGTVYDFVAeGIEEQaeylk 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 100 ---------------KHFANMAITQISKE---------RIAEIVKLVELEHaiHKKVKTYSLGMKQRLGIAQALLHQPKI 155
Cdd:PRK11147 100 ryhdishlvetdpseKNLNELAKLQEQLDhhnlwqlenRINEVLAQLGLDP--DAALSSLSGGWLRKAALGRALVSNPDV 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2753457674 156 LILDEPTNGLDPAGIrqirDYLQLLAKEENIAVIVSSHLLSEIELMCDRVVIIKQGEFV 214
Cdd:PRK11147 178 LLLDEPTNHLDIETI----EWLEGFLKTFQGSIIFISHDRSFIRNMATRIVDLDRGKLV 232
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
20-212 |
1.49e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 52.32 E-value: 1.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 20 IIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGliSMTEG---DITICGhsirtEREKALEQIGAI------VENPELY 90
Cdd:PRK10938 275 ILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITG--DHPQGysnDLTLFG-----RRRGSGETIWDIkkhigyVSSSLHL 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 91 DYM--TGMQNL---KHFANMAITQISKER----IAEIVKLVELEHAIHKK-VKTYSLGmKQRLG-IAQALLHQPKILILD 159
Cdd:PRK10938 348 DYRvsTSVRNVilsGFFDSIGIYQAVSDRqqklAQQWLDILGIDKRTADApFHSLSWG-QQRLAlIVRALVKHPTLLILD 426
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2753457674 160 EPTNGLDPAGIRQIRDYL-QLLAKEENIAVIVSSHLLSEIELMCDRVVIIKQGE 212
Cdd:PRK10938 427 EPLQGLDPLNRQLVRRFVdVLISEGETQLLFVSHHAEDAPACITHRLEFVPDGD 480
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
20-216 |
4.13e-07 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 50.94 E-value: 4.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 20 IIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGL-----ISmteGDITICGHSIR---------------TEREKA--L 77
Cdd:NF040905 275 VVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFGRsygrnIS---GTVFKDGKEVDvstvsdaidaglayvTEDRKGygL 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 78 EQIGAIVENpelydymTGMQNLKHFANMAITQISKE-RIAEIV--KLVELEHAIHKKVKTYSLGMKQRLGIAQALLHQPK 154
Cdd:NF040905 352 NLIDDIKRN-------ITLANLGKVSRRGVIDENEEiKVAEEYrkKMNIKTPSVFQKVGNLSGGNQQKVVLSKWLFTDPD 424
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2753457674 155 ILILDEPTNGLDPAGIRQIRDYLQLLAkEENIAVIVSSHLLSEIELMCDRVVIIKQGEFVQE 216
Cdd:NF040905 425 VLILDEPTRGIDVGAKYEIYTIINELA-AEGKGVIVISSELPELLGMCDRIYVMNEGRITGE 485
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
1-166 |
6.28e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 50.50 E-value: 6.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 1 MGNVVVKLENVRKKIGGT-EIIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITIC-GHSI--------- 69
Cdd:PRK11819 2 MAQYIYTMNRVSKVVPPKkQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPApGIKVgylpqepql 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 70 ---RTEREKALEQIGAIVE--------NPELYDYMTGMQNLkhFANMAITQiskERIaEIVKLVELEHAIH--------- 129
Cdd:PRK11819 82 dpeKTVRENVEEGVAEVKAaldrfneiYAAYAEPDADFDAL--AAEQGELQ---EII-DAADAWDLDSQLEiamdalrcp 155
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2753457674 130 ---KKVKTYSLGMKQRLGIAQALLHQPKILILDEPTNGLD 166
Cdd:PRK11819 156 pwdAKVTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLD 195
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
20-211 |
1.45e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 49.72 E-value: 1.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 20 IIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLIS----MTEGDITICGHSiRTEREKALEqiGAIVENPEL---YDY 92
Cdd:TIGR00956 76 ILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASNTDgfhiGVEGVITYDGIT-PEEIKKHYR--GDVVYNAETdvhFPH 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 93 MTGMQNLKHFANMAITQ-----ISKE-RIAEIVKLVE----LEHAIHKKV-----KTYSLGMKQRLGIAQALLHQPKILI 157
Cdd:TIGR00956 153 LTVGETLDFAARCKTPQnrpdgVSREeYAKHIADVYMatygLSHTRNTKVgndfvRGVSGGERKRVSIAEASLGGAKIQC 232
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2753457674 158 LDEPTNGLDPAGIRQIRDYLQLLAKEENIAVIVSSHLLSE--IELMcDRVVIIKQG 211
Cdd:TIGR00956 233 WDNATRGLDSATALEFIRALKTSANILDTTPLVAIYQCSQdaYELF-DKVIVLYEG 287
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
3-166 |
1.87e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 49.01 E-value: 1.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 3 NVVVKLENVRKKIGGTEIIRGLSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICG---------HSIRTER 73
Cdd:PRK10636 310 NPLLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKgiklgyfaqHQLEFLR 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 74 --EKALEQIGAIVEN---PELYDYMTGMQnlkhFANMAITQISKEriaeivklvelehaihkkvktYSLGMKQRLGIAQA 148
Cdd:PRK10636 390 adESPLQHLARLAPQeleQKLRDYLGGFG----FQGDKVTEETRR---------------------FSGGEKARLVLALI 444
|
170
....*....|....*...
gi 2753457674 149 LLHQPKILILDEPTNGLD 166
Cdd:PRK10636 445 VWQRPNLLLLDEPTNHLD 462
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
27-208 |
2.58e-06 |
|
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: 46.80 E-value: 2.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 27 EVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGHSIRTEREKaleqigaivenpelydymtgmqnlkhfanma 106
Cdd:cd03222 21 VVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITPVYKPQY------------------------------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 107 itqiskeriaeiVKLvelehaihkkvktySLGMKQRLGIAQALLHQPKILILDEPTNGLDPAGIRQIRDYLQLLAKEENI 186
Cdd:cd03222 70 ------------IDL--------------SGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKK 123
|
170 180
....*....|....*....|..
gi 2753457674 187 AVIVSSHLLSEIELMCDRVVII 208
Cdd:cd03222 124 TALVVEHDLAVLDYLSDRIHVF 145
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
136-199 |
1.25e-05 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 45.84 E-value: 1.25e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2753457674 136 SLGMKQRLGIAQALLHQPK---ILILDEPTNGLDPAGIRQIRDYLQLLAkEENIAVIVSSHLLSEIE 199
Cdd:pfam13304 238 SDGTKRLLALLAALLSALPkggLLLIDEPESGLHPKLLRRLLELLKELS-RNGAQLILTTHSPLLLD 303
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
24-243 |
1.70e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 46.51 E-value: 1.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 24 LSFEVREGEVYGFLGPNGSGKTTTIRMMTGLISMTEGDITICGHSIR-----------TEREKALeqIGAIVEnPELYDY 92
Cdd:PLN03232 636 INLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAETSSVVIRGSVAyvpqvswifnaTVRENIL--FGSDFE-SERYWR 712
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 93 MTGMQNLKH----FANMAITQISkERIAEIvklvelehaihkkvktySLGMKQRLGIAQALLHQPKILILDEPTNGLDPA 168
Cdd:PLN03232 713 AIDVTALQHdldlLPGRDLTEIG-ERGVNI-----------------SGGQKQRVSMARAVYSNSDIYIFDDPLSALDAH 774
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 169 GIRQIRDYLQLLAKEENIAVIVSS--HLLSEIelmcDRVVIIKQGEFVQEYNLHEQAKHDETVVVAFE----VDQVQKAN 242
Cdd:PLN03232 775 VAHQVFDSCMKDELKGKTRVLVTNqlHFLPLM----DRIILVSEGMIKEEGTFAELSKSGSLFKKLMEnagkMDATQEVN 850
|
.
gi 2753457674 243 E 243
Cdd:PLN03232 851 T 851
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
132-217 |
9.99e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 43.62 E-value: 9.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 132 VKTYSLGMKQRLGIAQALLHQPKILILDEPTNGLDPAGIRQIRDYLqllaKEENIAVIVSSHLLSEIELMCDRVVIIKQg 211
Cdd:PRK10636 147 VSDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLDLDAVIWLEKWL----KSYQGTLILISHDRDFLDPIVDKIIHIEQ- 221
|
....*.
gi 2753457674 212 EFVQEY 217
Cdd:PRK10636 222 QSLFEY 227
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
6-193 |
2.06e-04 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 41.53 E-value: 2.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 6 VKLENVRKkIGGTEIIRglsFEvreGEVYGFLGPNGSGKTT---------------TIRMMTGLISMT------EGDITI 64
Cdd:COG0419 5 LRLENFRS-YRDTETID---FD---DGLNLIVGPNGAGKSTileairyalygkarsRSKLRSDLINVGseeasvELEFEH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 65 CGHSIRTEREKAlEQIGAIVENP-ELYDYMTGMQNLKHFANM-----AITQISKERIAEIVKLVELEHAIHKK------V 132
Cdd:COG0419 78 GGKRYRIERRQG-EFAEFLEAKPsERKEALKRLLGLEIYEELkerlkELEEALESALEELAELQKLKQEILAQlsgldpI 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2753457674 133 KTYSLGMKQRLGIAQALLhqpkiLILDepTNGLDPAGIRQIRDYLqllakeENIAVIvsSH 193
Cdd:COG0419 157 ETLSGGERLRLALADLLS-----LILD--FGSLDEERLERLLDAL------EELAII--TH 202
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
38-193 |
2.67e-04 |
|
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: 41.05 E-value: 2.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 38 GPNGSGKTTTIRMM----TGLISMTEGDITICGHSIRTEREKAleQIGAIVENPELYDYmTGMQNLKHFANMAITqiske 113
Cdd:cd03240 29 GQNGAGKTTIIEALkyalTGELPPNSKGGAHDPKLIREGEVRA--QVKLAFENANGKKY-TITRSLAILENVIFC----- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 114 RIAEIVKLVELEhaihkkVKTYSLGMKQ------RLGIAQALLHQPKILILDEPTNGLDPAGIR-QIRDYLQLLAKEENI 186
Cdd:cd03240 101 HQGESNWPLLDM------RGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENIEeSLAEIIEERKSQKNF 174
|
....*..
gi 2753457674 187 AVIVSSH 193
Cdd:cd03240 175 QLIVITH 181
|
|
| PRK15177 |
PRK15177 |
Vi polysaccharide ABC transporter ATP-binding protein VexC; |
32-230 |
3.48e-04 |
|
Vi polysaccharide ABC transporter ATP-binding protein VexC;
Pssm-ID: 185099 [Multi-domain] Cd Length: 213 Bit Score: 41.20 E-value: 3.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 32 EVYGFLGPNGSGKTTTIRMMTGLISMTEGD-ITICGHSIrterekaleQIGAiveNPELYDYMTGMQNLKHFAnmAITQI 110
Cdd:PRK15177 14 EHIGILAAPGSGKTTLTRLLCGLDAPDEGDfIGLRGDAL---------PLGA---NSFILPGLTGEENARMMA--SLYGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 111 SKERIAEIV-KLVELEHAIHKKVKTYSLGMKQRLGIAQALLHQPKILILDEPTNGLDPAgiRQIRDYLQLLAKEENIAVI 189
Cdd:PRK15177 80 DGDEFSHFCyQLTQLEQCYTDRVSEYSVTMKTHLAFAINLLLPCRLYIADGKLYTGDNA--TQLRMQAALACQLQQKGLI 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2753457674 190 VSSHLLSEIELMCDRVVIIKQG------EFVQEYNLHEQAKHDETVV 230
Cdd:PRK15177 158 VLTHNPRLIKEHCHAFGVLLHGkitmceDLAQATALFEQYQSNQATI 204
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
143-212 |
5.21e-04 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 41.07 E-value: 5.21e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2753457674 143 LGIAqALLHQPK---ILILDEPTNGLDPAGIRQIRDYLQLLAkeENIAVIVSSH---LLSEIELmCDRVVIIKQGE 212
Cdd:COG4637 267 LALL-AALLSPRpppLLCIEEPENGLHPDLLPALAELLREAS--ERTQVIVTTHspaLLDALEP-EEVLVLEREDD 338
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
38-209 |
5.55e-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: 5.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 38 GPNGSGKTTTIRMMtglismtegdITICGHSIRTEREKALEQIGAIVenpelydymtgmqnlkhfanmaiTQISKERIAE 117
Cdd:cd03227 28 GPNGSGKSTILDAI----------GLALGGAQSATRRRSGVKAGCIV-----------------------AAVSAELIFT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 118 IVKLvelehaihkkvktySLGMKQRLGIAQAL---LHQPKIL-ILDEPTNGLDPAGIRQIRDYLQLLAKEENIaVIVSSH 193
Cdd:cd03227 75 RLQL--------------SGGEKELSALALILalaSLKPRPLyILDEIDRGLDPRDGQALAEAILEHLVKGAQ-VIVITH 139
|
170
....*....|....*.
gi 2753457674 194 LLsEIELMCDRVVIIK 209
Cdd:cd03227 140 LP-ELAELADKLIHIK 154
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
24-216 |
9.75e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 40.88 E-value: 9.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 24 LSFEVREGEVYGFLGPNGSGKTTTIRMMTG-LISMTEGDITICGHSI----------RTEREKALeqIGAIVEnPELYDY 92
Cdd:PLN03130 636 INLDVPVGSLVAIVGSTGEGKTSLISAMLGeLPPRSDASVVIRGTVAyvpqvswifnATVRDNIL--FGSPFD-PERYER 712
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 93 MTGMQNLKH----FANMAITQISkERIAEIvklvelehaihkkvktySLGMKQRLGIAQALLHQPKILILDEPTNGLDPA 168
Cdd:PLN03130 713 AIDVTALQHdldlLPGGDLTEIG-ERGVNI-----------------SGGQKQRVSMARAVYSNSDVYIFDDPLSALDAH 774
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2753457674 169 GIRQ-----IRDYLQllaKEENIAVIVSSHLLSEIelmcDRVVIIKQGEFVQE 216
Cdd:PLN03130 775 VGRQvfdkcIKDELR---GKTRVLVTNQLHFLSQV----DRIILVHEGMIKEE 820
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
130-194 |
2.05e-03 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 38.46 E-value: 2.05e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2753457674 130 KKVKTYSLGMKQRLGIAQALLHQPK--ILILDEPTNGLDPAGIRQIRDYLQLLAKEENIAVIVSSHL 194
Cdd:cd03238 83 QKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGLIDLGNTVILIEHNL 149
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| aroA |
TIGR01356 |
3-phosphoshikimate 1-carboxyvinyltransferase; This model represents ... |
10-93 |
2.82e-03 |
|
3-phosphoshikimate 1-carboxyvinyltransferase; This model represents 3-phosphoshikimate-1-carboxyvinyltransferase (aroA), which catalyzes the sixth of seven steps in the shikimate pathway of the biosynthesis of chorimate. Chorismate is last common precursor of all three aromatic amino acids. Sequences scoring between the trusted and noise cutoffs include fragmentary and aberrant sequences in which generally well-conserved motifs are missing or altererd, but no example of a protein known to have a different function. [Amino acid biosynthesis, Aromatic amino acid family]
Pssm-ID: 273574 Cd Length: 409 Bit Score: 38.80 E-value: 2.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 10 NVRKKiGGTEIIRGLSFEVREGEVYgflgPNGSGktTTIRMMTGLISMTEGDITICG-HSIRtERE-----KALEQIGAI 83
Cdd:TIGR01356 50 KIEDG-GEVAVIEGVGGKEPQAELD----LGNSG--TTARLLTGVLALADGEVVLTGdESLR-KRPmgrlvDALRQLGAE 121
|
90
....*....|
gi 2753457674 84 VENPELYDYM 93
Cdd:TIGR01356 122 ISSLEGGGSL 131
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| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
134-194 |
4.01e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 38.84 E-value: 4.01e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2753457674 134 TYSLGMKQRLGIAQALLHQ---PKILILDEPTNGLDPAGIRQIRDYLQLLAKEENIAVIVSSHL 194
Cdd:TIGR00630 829 TLSGGEAQRIKLAKELSKRstgRTLYILDEPTTGLHFDDIKKLLEVLQRLVDKGNTVVVIEHNL 892
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|
| AroA |
COG0128 |
5-enolpyruvylshikimate-3-phosphate synthase [Amino acid transport and metabolism]; ... |
11-85 |
6.74e-03 |
|
5-enolpyruvylshikimate-3-phosphate synthase [Amino acid transport and metabolism]; 5-enolpyruvylshikimate-3-phosphate synthase is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis
Pssm-ID: 439898 Cd Length: 421 Bit Score: 37.76 E-value: 6.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 11 VRKKIGGTEIIRGLSFEVREGEVYGFLGpnGSGktTTIRMMTGLISMTEGDITICGH-SIRtER-----EKALEQIGAIV 84
Cdd:COG0128 64 IEELDGGTLRVTGVGGGLKEPDAVLDCG--NSG--TTMRLLTGLLALQPGEVVLTGDeSLR-KRpmgrlLDPLRQLGARI 138
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.
gi 2753457674 85 E 85
Cdd:COG0128 139 E 139
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| EPSP_synthase |
cd01556 |
EPSP synthase domain. 3-phosphoshikimate 1-carboxyvinyltransferase ... |
13-93 |
8.79e-03 |
|
EPSP synthase domain. 3-phosphoshikimate 1-carboxyvinyltransferase (5-enolpyruvylshikimate-3-phosphate synthase) (EC 2.5.1.19) catalyses the reaction between shikimate-3-phosphate (S3P) and phosphoenolpyruvate (PEP) to form 5-enolpyruvylshkimate-3-phosphate (EPSP), an intermediate in the shikimate pathway leading to aromatic amino acid biosynthesis. The reaction is phosphoenolpyruvate + 3-phosphoshikimate = phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate. It is found in bacteria and plants but not animals. The enzyme is the target of the widely used herbicide glyphosate, which has been shown to occupy the active site. In bacteria and plants, it is a single domain protein, while in fungi, the domain is found as part of a multidomain protein with functions that are all part of the shikimate pathway.
Pssm-ID: 238797 Cd Length: 409 Bit Score: 37.54 E-value: 8.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753457674 13 KKIGGTEIIRGLSFEVREGEVYGFLGpnGSGktTTIRMMTGLISMTEGDITICG-HSIRtERE-----KALEQIGAIVEN 86
Cdd:cd01556 54 EEEGGTVEIVGGGGLGLPPEAVLDCG--NSG--TTMRLLTGLLALQGGDSVLTGdESLR-KRPmgrlvDALRQLGAEIEG 128
|
....*..
gi 2753457674 87 PELYDYM 93
Cdd:cd01556 129 REGGGYP 135
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