|
Name |
Accession |
Description |
Interval |
E-value |
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
4-224 |
8.51e-100 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 292.74 E-value: 8.51e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 4 VKTTQLIKVFKGAEAVNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELFGERIknHRQHIQALKKIGSL 83
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDV--ARDPAEVRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 84 VESPSYYAHLTARENLEVLRKILGVS----KNRVDEVLDIVKLAKEANRPVKGFSLGMKQRLGIASALLGNPRLLILDEP 159
Cdd:COG1131 79 PQEPALYPDLTVRENLRFFARLYGLPrkeaRERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1265835877 160 TNGLDPAGIQEIRSLIKEMpGKNGVTVLISSHLLYEIDHLATQVGIITKGKMLFNGSIESLRKKA 224
Cdd:COG1131 159 TSGLDPEARRELWELLREL-AAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKARL 222
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
4-215 |
2.51e-96 |
|
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: 282.95 E-value: 2.51e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 4 VKTTQLIKVFKGAEAVNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELFGERIKNHrqhIQALKKIGSL 83
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKN---IEALRRIGAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 84 VESPSYYAHLTARENLEVLRKILGVSKNRVDEVLDIVKLAKEANRPVKGFSLGMKQRLGIASALLGNPRLLILDEPTNGL 163
Cdd:cd03268 78 IEAPGFYPNLTARENLRLLARLLGIRKKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1265835877 164 DPAGIQEIRSLIKEMPgKNGVTVLISSHLLYEIDHLATQVGIITKGKMLFNG 215
Cdd:cd03268 158 DPDGIKELRELILSLR-DQGITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
5-217 |
1.23e-81 |
|
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: 246.16 E-value: 1.23e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 5 KTTQLIKVFKGAEAVNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIelfgeRIKNHRQHIQALKKIGSLV 84
Cdd:TIGR03740 2 ETKNLSKRFGKQTAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEI-----IFDGHPWTRKDLHKIGSLI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 85 ESPSYYAHLTARENLEVLRKILGVSKNRVDEVLDIVKLAKEANRPVKGFSLGMKQRLGIASALLGNPRLLILDEPTNGLD 164
Cdd:TIGR03740 77 ESPPLYENLTARENLKVHTTLLGLPDSRIDEVLNIVDLTNTGKKKAKQFSLGMKQRLGIAIALLNHPKLLILDEPTNGLD 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1265835877 165 PAGIQEIRSLIKEMPgKNGVTVLISSHLLYEIDHLATQVGIITKGKMLFNGSI 217
Cdd:TIGR03740 157 PIGIQELRELIRSFP-EQGITVILSSHILSEVQQLADHIGIISEGVLGYQGKI 208
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
4-211 |
2.47e-72 |
|
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: 220.73 E-value: 2.47e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 4 VKTTQLIKVFKGAEAVNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELFGERIKNHRqhIQALKKIGSL 83
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEP--EEVKRRIGYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 84 VESPSYYAHLTARENLEvlrkilgvsknrvdevldivklakeanrpvkgFSLGMKQRLGIASALLGNPRLLILDEPTNGL 163
Cdd:cd03230 79 PEEPSLYENLTVRENLK--------------------------------LSGGMKQRLALAQALLHDPELLILDEPTSGL 126
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1265835877 164 DPAGIQEIRSLIKEMpGKNGVTVLISSHLLYEIDHLATQVGIITKGKM 211
Cdd:cd03230 127 DPESRREFWELLREL-KKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
11-298 |
1.49e-70 |
|
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: 220.72 E-value: 1.49e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 11 KVFKGAEAVNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELFGERIKnhRQHIQALKKIGSLVESPSYY 90
Cdd:TIGR01188 1 KVYGDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVV--REPRKVRRSIGIVPQYASVD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 91 AHLTARENLEVLRKILGVSKN----RVDEVLDIVKLAKEANRPVKGFSLGMKQRLGIASALLGNPRLLILDEPTNGLDPA 166
Cdd:TIGR01188 79 EDLTGRENLEMMGRLYGLPKDeaeeRAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 167 GIQEIRSLIKEMpGKNGVTVLISSHLLYEIDHLATQVGIITKGKMLFNGSIESLRKKA-------------KHQVAFTTG 233
Cdd:TIGR01188 159 TRRAIWDYIRAL-KEEGVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPEELKRRLgkdtlesrprdiqSLKVEVSML 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1265835877 234 EIEKSKTILLANGFVPTIDKNSLLLDYIDhEQVAHLVYQLVQENVSIYRVEEKSKSLEDIFLKLT 298
Cdd:TIGR01188 238 IAELGETGLGLLAVTVDSDRIKILVPDGD-ETVPEIVEAAIRNGIRIRSISTERPSLDDVFLKLT 301
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
5-227 |
3.51e-70 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 217.80 E-value: 3.51e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 5 KTTQLIKVFKGAEAVNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELFGERIknHRQHIQALKKIGSLV 84
Cdd:COG4555 3 EVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDV--RKEPREARRQIGVLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 85 ESPSYYAHLTARENLEVLRKILGVS----KNRVDEVLDIVKLAKEANRPVKGFSLGMKQRLGIASALLGNPRLLILDEPT 160
Cdd:COG4555 81 DERGLYDRLTVRENIRYFAELYGLFdeelKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPT 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1265835877 161 NGLDPAGIQEIRSLIKEMpGKNGVTVLISSHLLYEIDHLATQVGIITKGKMLFNGSIESLRKKAKHQ 227
Cdd:COG4555 161 NGLDVMARRLLREILRAL-KKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREEIGEE 226
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
3-302 |
2.64e-69 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 217.28 E-value: 2.64e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 3 IVKTTQLIKVFKGAEAVNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELFGERIknHRQHIQalkKIGS 82
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPL--DPEDRR---RIGY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 83 LVESPSYYAHLTARENLEVLRKILGVSKN----RVDEVLDIVKLAKEANRPVKGFSLGMKQRLGIASALLGNPRLLILDE 158
Cdd:COG4152 76 LPEERGLYPKMKVGEQLVYLARLKGLSKAeakrRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLILDE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 159 PTNGLDPAGIQEIRSLIKEMpGKNGVTVLISSHLLYEIDHLATQVGIITKGKMLFNGSIESLRKKAKHQVAFTTGEIEKS 238
Cdd:COG4152 156 PFSGLDPVNVELLKDVIREL-AAKGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEIRRQFGRNTLRLEADGDAG 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1265835877 239 KTILLANGFVPTIDKNSLLLDyIDHEQVAHLVYQLVQENVSIYRVEEKSKSLEDIFLKLTSEEN 302
Cdd:COG4152 235 WLRALPGVTVVEEDGDGAELK-LEDGADAQELLRALLARGPVREFEEVRPSLNEIFIEVVGEKA 297
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
4-221 |
1.39e-66 |
|
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: 207.99 E-value: 1.39e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 4 VKTTQLIKVFKGAEAVNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELFGERIKnhRQHIQALKKIGSL 83
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVV--REPREVRRRIGIV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 84 VESPSYYAHLTARENLEVLRKILGVS----KNRVDEVLDIVKLAKEANRPVKGFSLGMKQRLGIASALLGNPRLLILDEP 159
Cdd:cd03265 79 FQDLSVDDELTGWENLYIHARLYGVPgaerRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1265835877 160 TNGLDPAGIQEIRSLIKEMPGKNGVTVLISSHLLYEIDHLATQVGIITKGKMLFNGSIESLR 221
Cdd:cd03265 159 TIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEELK 220
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
9-215 |
5.25e-61 |
|
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: 193.18 E-value: 5.25e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 9 LIKVFKGAEAVNEVNLSIKEGeIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELFGERIKNHRQHIQalKKIGSLVESPS 88
Cdd:cd03264 6 LTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLR--RRIGYLPQEFG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 89 YYAHLTARENLEVLRKILGVS----KNRVDEVLDIVKLAKEANRPVKGFSLGMKQRLGIASALLGNPRLLILDEPTNGLD 164
Cdd:cd03264 83 VYPNFTVREFLDYIAWLKGIPskevKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLD 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1265835877 165 PAGIQEIRSLIKEMpGKNgVTVLISSHLLYEIDHLATQVGIITKGKMLFNG 215
Cdd:cd03264 163 PEERIRFRNLLSEL-GED-RIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
17-297 |
3.97e-56 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 184.14 E-value: 3.97e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 17 EAVNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELFGERIknHRQHIQALKKIGS-------Lvespsy 89
Cdd:COG4586 36 EAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVP--FKRRKEFARRIGVvfgqrsqL------ 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 90 YAHLTARENLEVLRKILGVS----KNRVDEVLDIVKLAKEANRPVKGFSLGMKQRLGIASALLGNPRLLILDEPTNGLDP 165
Cdd:COG4586 108 WWDLPAIDSFRLLKAIYRIPdaeyKKRLDELVELLDLGELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDV 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 166 AGIQEIRSLIKEMPGKNGVTVLISSHLLYEIDHLATQVGIITKGKMLFNGSIESLRKK--AKHQVAFTTGEiEKSKTILL 243
Cdd:COG4586 188 VSKEAIREFLKEYNRERGTTILLTSHDMDDIEALCDRVIVIDHGRIIYDGSLEELKERfgPYKTIVLELAE-PVPPLELP 266
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1265835877 244 ANGFVPTIDKNSLLLDYIDHEQVAHLVYQLVQE-NVSIYRVEEksKSLEDIFLKL 297
Cdd:COG4586 267 RGGEVIEREGNRVRLEVDPRESLAEVLARLLARyPVRDLTIEE--PPIEEVIRRI 319
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
9-221 |
9.82e-54 |
|
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: 175.00 E-value: 9.82e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 9 LIKVFKGAE--AVNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELFGERIKNHRQHIQalKKIGSLVES 86
Cdd:cd03263 6 LTKTYKKGTkpAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAAR--QSLGYCPQF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 87 PSYYAHLTARENLEVLRKILGVSKNRVDEV----LDIVKLAKEANRPVKGFSLGMKQRLGIASALLGNPRLLILDEPTNG 162
Cdd:cd03263 84 DALFDELTVREHLRFYARLKGLPKSEIKEEvellLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSG 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1265835877 163 LDPAGIQEIRSLIKEMpgKNGVTVLISSHLLYEIDHLATQVGIITKGKMLFNGSIESLR 221
Cdd:cd03263 164 LDPASRRAIWDLILEV--RKGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQELK 220
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
12-201 |
5.65e-53 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 172.28 E-value: 5.65e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 12 VFKGaeavneVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELFGERIKNHRQHIQAlkKIGSLVESPSYYA 91
Cdd:COG4133 17 LFSG------LSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRR--RLAYLGHADGLKP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 92 HLTARENLEVLRKILGVSKNR--VDEVLDIVKLAKEANRPVKGFSLGMKQRLGIASALLGNPRLLILDEPTNGLDPAGIQ 169
Cdd:COG4133 89 ELTVRENLRFWAALYGLRADReaIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGVA 168
|
170 180 190
....*....|....*....|....*....|..
gi 1265835877 170 EIRSLIKEMpGKNGVTVLISSHLLYEIDHLAT 201
Cdd:COG4133 169 LLAELIAAH-LARGGAVLLTTHQPLELAAARV 199
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
11-215 |
7.33e-53 |
|
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: 172.55 E-value: 7.33e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 11 KVFKGAEAVNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELFGerIKNHRQHIQALKKIGSLVESPSYY 90
Cdd:cd03266 13 DVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDG--FDVVKEPAEARRRLGFVSDSTGLY 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 91 AHLTARENLEVLRKILGVS----KNRVDEVLDIVKLAKEANRPVKGFSLGMKQRLGIASALLGNPRLLILDEPTNGLDPA 166
Cdd:cd03266 91 DRLTARENLEYFAGLYGLKgdelTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVM 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1265835877 167 GIQEIRSLIKEMPgKNGVTVLISSHLLYEIDHLATQVGIITKGKMLFNG 215
Cdd:cd03266 171 ATRALREFIRQLR-ALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
4-215 |
9.60e-50 |
|
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: 164.38 E-value: 9.60e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 4 VKTTQLIKVFKGAEAVNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELFGERIKNHRQHiqalkKIGSL 83
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARN-----RIGYL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 84 VESPSYYAHLTARENLEVLRKILGVSK----NRVDEVLDIVKLAKEANRPVKGFSLGMKQRLGIASALLGNPRLLILDEP 159
Cdd:cd03269 76 PEERGLYPKMKVIDQLVYLAQLKGLKKeearRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEP 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1265835877 160 TNGLDPAGIQEIRSLIKEMPGkNGVTVLISSHLLYEIDHLATQVGIITKGKMLFNG 215
Cdd:cd03269 156 FSGLDPVNVELLKDVIRELAR-AGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
14-220 |
4.39e-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: 163.27 E-value: 4.39e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 14 KGAEAVNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELFGERIKnhRQHIQAL-KKIGS--------LV 84
Cdd:COG1122 12 GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDIT--KKNLRELrRKVGLvfqnpddqLF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 85 ESpsyyahlTAREnlEV---LRKiLGVSKN----RVDEVLDIVKLAKEANRPVKGFSLGMKQRLGIASALLGNPRLLILD 157
Cdd:COG1122 90 AP-------TVEE--DVafgPEN-LGLPREeireRVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLVLD 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1265835877 158 EPTNGLDPAGIQEIRSLIKEMPgKNGVTVLISSHLLYEIDHLATQVGIITKGKMLFNGSIESL 220
Cdd:COG1122 160 EPTAGLDPRGRRELLELLKRLN-KEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREV 221
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
13-215 |
6.08e-49 |
|
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: 162.89 E-value: 6.08e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 13 FKGAEAVNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELFGERikNHRQHIQALKKIGSLVESPSYYA- 91
Cdd:cd03267 31 YREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLV--PWKRRKKFLRRIGVVFGQKTQLWw 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 92 HLTARENLEVLRKILGVS----KNRVDEVLDIVKLAKEANRPVKGFSLGMKQRLGIASALLGNPRLLILDEPTNGLDPAG 167
Cdd:cd03267 109 DLPVIDSFYLLAAIYDLPparfKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVA 188
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1265835877 168 IQEIRSLIKEMPGKNGVTVLISSHLLYEIDHLATQVGIITKGKMLFNG 215
Cdd:cd03267 189 QENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
4-210 |
5.46e-47 |
|
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: 156.19 E-value: 5.46e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 4 VKTTQLIKVFKGAEAVNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELFGERIKNHRQHIQALK-KIGS 82
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPPLRrRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 83 LVESPSYYAHLTARENLevlrkilgvsknrvdevldivklakeanrpVKGFSLGMKQRLGIASALLGNPRLLILDEPTNG 162
Cdd:cd03229 81 VFQDFALFPHLTVLENI------------------------------ALGLSGGQQQRVALARALAMDPDVLLLDEPTSA 130
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1265835877 163 LDPAGIQEIRSLIKEMPGKNGVTVLISSHLLYEIDHLATQVGIITKGK 210
Cdd:cd03229 131 LDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-188 |
6.41e-47 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 158.28 E-value: 6.41e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 1 MEIVKTTQLIKVFKGAEAVNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELFGERI---KNHR------ 71
Cdd:COG0411 2 DPLLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDItglPPHRiarlgi 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 72 ----QHIQALKkigslvespsyyaHLTARENLEV----------LRKILGVSKN---------RVDEVLDIVKLAKEANR 128
Cdd:COG0411 82 artfQNPRLFP-------------ELTVLENVLVaaharlgrglLAALLRLPRArreereareRAEELLERVGLADRADE 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 129 PVKGFSLGMKQRLGIASALLGNPRLLILDEPTNGLDPAGIQEIRSLIKEMPGKNGVTVLI 188
Cdd:COG0411 149 PAGNLSYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILL 208
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
5-222 |
1.55e-46 |
|
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: 156.83 E-value: 1.55e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 5 KTTQLIKVFKGAEAVNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELFGERIKNHRQHIQALKKIGSLV 84
Cdd:cd03219 2 EVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARLGIGRTF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 85 ESPSYYAHLTARENLEV--------------LRKILGVSKNRVDEVLDIVKLAKEANRPVKGFSLGMKQRLGIASALLGN 150
Cdd:cd03219 82 QIPRLFPELTVLENVMVaaqartgsglllarARREEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALATD 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1265835877 151 PRLLILDEPTNGLDPAGIQEIRSLIKEMPgKNGVTVLISSHLLYEIDHLATQVGIITKGKMLFNGSIESLRK 222
Cdd:cd03219 162 PKLLLLDEPAAGLNPEETEELAELIRELR-ERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRN 232
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
18-210 |
3.06e-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: 155.32 E-value: 3.06e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 18 AVNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELFGERIKNHRQHiQALKKIGSLVESP-SYYAHLTAR 96
Cdd:cd03225 16 ALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLK-ELRRKVGLVFQNPdDQFFGPTVE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 97 ENLEVLRKILGVS----KNRVDEVLDIVKLAKEANRPVKGFSLGMKQRLGIASALLGNPRLLILDEPTNGLDPAGIQEIR 172
Cdd:cd03225 95 EEVAFGLENLGLPeeeiEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDPAGRRELL 174
|
170 180 190
....*....|....*....|....*....|....*...
gi 1265835877 173 SLIKEMPgKNGVTVLISSHLLYEIDHLATQVGIITKGK 210
Cdd:cd03225 175 ELLKKLK-AEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
4-220 |
4.08e-46 |
|
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: 155.78 E-value: 4.08e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 4 VKTTQLIKVFKGAEAVNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELFGERIKNHRQHIQALKKIGSL 83
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRARLGIGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 84 VESPSYYAHLTARENLEVLRKILGVSK----NRVDEVLDIVKLAKEANRPVKGFSLGMKQRLGIASALLGNPRLLILDEP 159
Cdd:cd03218 81 PQEASIFRKLTVEENILAVLEIRGLSKkereEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1265835877 160 TNGLDPAGIQEIRSLIKEMPGKnGVTVLISSHLLYEIDHLATQVGIITKGKMLFNGSIESL 220
Cdd:cd03218 161 FAGVDPIAVQDIQKIIKILKDR-GIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEI 220
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
18-226 |
3.60e-45 |
|
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: 160.07 E-value: 3.60e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 18 AVNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELFGE--------RIKNHRQHIQ-----------ALK 78
Cdd:COG1123 280 AVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKdltklsrrSLRELRRRVQmvfqdpysslnPRM 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 79 KIG-SLVESPSYYAHLTAREnlevlrkilgvSKNRVDEVLDIVKLAKE-ANRPVKGFSLGMKQRLGIASALLGNPRLLIL 156
Cdd:COG1123 360 TVGdIIAEPLRLHGLLSRAE-----------RRERVAELLERVGLPPDlADRYPHELSGGQRQRVAIARALALEPKLLIL 428
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 157 DEPTNGLDPAGIQEIRSLIKEMPGKNGVTVLISSHLLYEIDHLATQVGIITKGKMLFNGSIESLRKKAKH 226
Cdd:COG1123 429 DEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVFANPQH 498
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
19-301 |
4.11e-43 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 149.96 E-value: 4.11e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 19 VNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELFGERIKNHRQHiqALKKIGSLVESPSYYAHLTAREN 98
Cdd:PRK13537 23 VDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARH--ARQRVGVVPQFDNLDPDFTVREN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 99 LEVLRKILGVS----KNRVDEVLDIVKLAKEANRPVKGFSLGMKQRLGIASALLGNPRLLILDEPTNGLDPAG---IQE- 170
Cdd:PRK13537 101 LLVFGRYFGLSaaaaRALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQArhlMWEr 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 171 IRSLIKEmpgknGVTVLISSHLLYEIDHLATQVGIITKGKMLFNGSIESLrkkAKHQVAFTTGEIEKSKTILLANGFVPT 250
Cdd:PRK13537 181 LRSLLAR-----GKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHAL---IESEIGCDVIEIYGPDPVALRDELAPL 252
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1265835877 251 IDKNSL----LLDYIDHEQvaHLVYQLVQENVsiYRVEEKSKSLEDIFLKLTSEE 301
Cdd:PRK13537 253 AERTEIsgetLFCYVRDPE--PLHARLKGRAG--LRYLHRPANLEDVFLRLTGRE 303
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-216 |
4.43e-43 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 147.87 E-value: 4.43e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 1 MEIVKTTQLIKVFKGAEAVNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELFGERIKNHRQHIQALKKI 80
Cdd:COG1137 1 MMTLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMHKRARLGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 81 GSLVESPSYYAHLTARENLEVLRKILGVSK----NRVDEVLD---IVKLAKeanrpVKGFSL--GMKQRLGIASALLGNP 151
Cdd:COG1137 81 GYLPQEASIFRKLTVEDNILAVLELRKLSKkereERLEELLEefgITHLRK-----SKAYSLsgGERRRVEIARALATNP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1265835877 152 RLLILDEPTNGLDPAGIQEIRSLIKEMPGKnGVTVLISSHLLYE----IDHLAtqvgIITKGKMLFNGS 216
Cdd:COG1137 156 KFILLDEPFAGVDPIAVADIQKIIRHLKER-GIGVLITDHNVREtlgiCDRAY----IISEGKVLAEGT 219
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
15-200 |
1.27e-42 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 146.14 E-value: 1.27e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 15 GAEAVNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELFGERIKNHRqhiqalKKIGSL--VESPSYYAH 92
Cdd:cd03235 11 GHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKER------KRIGYVpqRRSIDRDFP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 93 LTARE--------NLEVLRKILGVSKNRVDEVLDIVKLAKEANRPVKGFSLGMKQRLGIASALLGNPRLLILDEPTNGLD 164
Cdd:cd03235 85 ISVRDvvlmglygHKGLFRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAGVD 164
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1265835877 165 PAGIQEIRSLIKEMpGKNGVTVLISSH----LLYEIDHLA 200
Cdd:cd03235 165 PKTQEDIYELLREL-RREGMTILVVTHdlglVLEYFDRVL 203
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
9-222 |
1.61e-42 |
|
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: 146.66 E-value: 1.61e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 9 LIKVFKGAEAVNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELFGERIK--NHRQHIQALKKIGSLVES 86
Cdd:COG1127 11 LTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITglSEKELYELRRRIGMLFQG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 87 PSYYAHLTARENLEV-LRKILGVSK----NRVDEVLDIVKLAKEANRPVKGFSLGMKQRLGIASALLGNPRLLILDEPTN 161
Cdd:COG1127 91 GALFDSLTVFENVAFpLREHTDLSEaeirELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDPEILLYDEPTA 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1265835877 162 GLDPAGIQEIRSLIKEMPGKNGVTVLISSHLLYEIDHLATQVGIITKGKMLFNGSIESLRK 222
Cdd:COG1127 171 GLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLA 231
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
15-203 |
2.99e-42 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 146.00 E-value: 2.99e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 15 GAEAVNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELFGERIKNHRqhiqalKKIGSLVESPSYYAH-- 92
Cdd:COG1121 18 GRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRAR------RRIGYVPQRAEVDWDfp 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 93 LTARE--------NLEVLRKILGVSKNRVDEVLDIVKLAKEANRPVKGFSLGMKQRLGIASALLGNPRLLILDEPTNGLD 164
Cdd:COG1121 92 ITVRDvvlmgrygRRGLFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDPDLLLLDEPFAGVD 171
|
170 180 190
....*....|....*....|....*....|....*....
gi 1265835877 165 PAGIQEIRSLIKEMPgKNGVTVLISSHLLYEIDHLATQV 203
Cdd:COG1121 172 AATEEALYELLRELR-REGKTILVVTHDLGAVREYFDRV 209
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
4-212 |
4.11e-42 |
|
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: 144.58 E-value: 4.11e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 4 VKTTQLIKVFKGAEAVNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELFGERIKN---HRQHIqalkki 80
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGvppERRNI------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 81 gSLV-ESPSYYAHLTAREN----LEVLRKILGVSKNRVDEVLDIVKLAKEANRPVKGFSLGMKQRLGIASALLGNPRLLI 155
Cdd:cd03259 75 -GMVfQDYALFPHLTVAENiafgLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1265835877 156 LDEPTNGLDPAGIQEIRSLIKEMPGKNGVTVLISSHLLYEIDHLATQVGIITKGKML 212
Cdd:cd03259 154 LDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIV 210
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
9-220 |
9.73e-42 |
|
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: 144.34 E-value: 9.73e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 9 LIKVFKGAEAVNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELFGERIKNHRQHIQALKKIGSLVESPS 88
Cdd:TIGR04406 7 LIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHLPMHERARLGIGYLPQEAS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 89 YYAHLTARENLEV---LRKIL--GVSKNRVDEVLDIVKLAKEANRPVKGFSLGMKQRLGIASALLGNPRLLILDEPTNGL 163
Cdd:TIGR04406 87 IFRKLTVEENIMAvleIRKDLdrAEREERLEALLEEFQISHLRDNKAMSLSGGERRRVEIARALATNPKFILLDEPFAGV 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1265835877 164 DPAGIQEIRSLIKEMPGKnGVTVLISSHLLYEIDHLATQVGIITKGKMLFNGSIESL 220
Cdd:TIGR04406 167 DPIAVGDIKKIIKHLKER-GIGVLITDHNVRETLDICDRAYIISDGKVLAEGTPAEI 222
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
11-301 |
6.12e-41 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 145.36 E-value: 6.12e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 11 KVFKGAEAVNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELFGERIKnhRQHIQALKKIGSLVESPSYY 90
Cdd:PRK13536 49 KSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVP--ARARLARARIGVVPQFDNLD 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 91 AHLTARENLEVLRKILGVSKNRVDEV----LDIVKLAKEANRPVKGFSLGMKQRLGIASALLGNPRLLILDEPTNGLDPA 166
Cdd:PRK13536 127 LEFTVRENLLVFGRYFGMSTREIEAVipslLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPH 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 167 G---IQE-IRSLIKEmpgknGVTVLISSHLLYEIDHLATQVGIITKGKMLFNGSIESLrkkAKHQVAFTTGEIEKSKTIL 242
Cdd:PRK13536 207 ArhlIWErLRSLLAR-----GKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHAL---IDEHIGCQVIEIYGGDPHE 278
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1265835877 243 LANGFVP-----TIDKNSLLLDYIDHEQV-AHLvyqlvqENVSIYRVEEKSKSLEDIFLKLTSEE 301
Cdd:PRK13536 279 LSSLVKPyarriEVSGETLFCYAPDPEQVrVQL------RGRAGLRLLQRPPNLEDVFLRLTGRE 337
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
3-220 |
1.20e-40 |
|
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: 141.56 E-value: 1.20e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 3 IVKTTQLIKVFKG----AEAVNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELFGERIK--NHRQHIQA 76
Cdd:cd03258 1 MIELKNVSKVFGDtggkVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTllSGKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 77 LKKIGSLVESPSYYAHLTARENLEVLRKILGVSKN----RVDEVLDIVKLAKEANRPVKGFSLGMKQRLGIASALLGNPR 152
Cdd:cd03258 81 RRRIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAeieeRVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPK 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1265835877 153 LLILDEPTNGLDPAGIQEIRSLIKEMPGKNGVTVLISSHLLYEIDHLATQVGIITKGKMLFNGSIESL 220
Cdd:cd03258 161 VLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEV 228
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
15-221 |
1.31e-40 |
|
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: 141.03 E-value: 1.31e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 15 GAEAVNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELFGERIKNHRQHIQALKKIGSLVESPSYYAHLT 94
Cdd:cd03224 12 KSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARAGIGYVPEGRRIFPELT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 95 ARENLEVLRKILGVSKN--RVDEVLDIV-KLAKEANRPVKGFSLGMKQRLGIASALLGNPRLLILDEPTNGLDPAGIQEI 171
Cdd:cd03224 92 VEENLLLGAYARRRAKRkaRLERVYELFpRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLAPKIVEEI 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1265835877 172 RSLIKEMPGKnGVTVLISSHLLYEIDHLATQVGIITKGKMLFNGSIESLR 221
Cdd:cd03224 172 FEAIRELRDE-GVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELL 220
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
18-191 |
1.19e-39 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 147.96 E-value: 1.19e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 18 AVNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELFGERIKNHrqHIQALKKIGSLVESPSYYAHLTARE 97
Cdd:NF033858 281 AVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDAG--DIATRRRVGYMSQAFSLYGELTVRQ 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 98 NLEVLRKILGVSKN----RVDEVLDIVKLAKEANRPVKGFSLGMKQRLGIASALLGNPRLLILDEPTNGLDPAGIQEIRS 173
Cdd:NF033858 359 NLELHARLFHLPAAeiaaRVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVARDMFWR 438
|
170
....*....|....*...
gi 1265835877 174 LIKEMPGKNGVTVLISSH 191
Cdd:NF033858 439 LLIELSREDGVTIFISTH 456
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
8-211 |
1.48e-39 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 138.26 E-value: 1.48e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 8 QLIKVFK----GAEAVNEVNLSIKEGEIYgFL-GPNGAGKTTTIRMLLGLMKPTSGKIELFGERIKN-HRQHIQAL-KKI 80
Cdd:COG2884 3 RFENVSKrypgGREALSDVSLEIEKGEFV-FLtGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRlKRREIPYLrRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 81 G------SLVEspsyyaHLTARENLE-VLRkILGVS----KNRVDEVLDIVKLAKEANRPVKGFSLGMKQRLGIASALLG 149
Cdd:COG2884 82 GvvfqdfRLLP------DRTVYENVAlPLR-VTGKSrkeiRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVN 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1265835877 150 NPRLLILDEPTNGLDPAGIQEIRSLIKEMpGKNGVTVLISSHLLYEIDHLATQVGIITKGKM 211
Cdd:COG2884 155 RPELLLADEPTGNLDPETSWEIMELLEEI-NRRGTTVLIATHDLELVDRMPKRVLELEDGRL 215
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
4-191 |
2.41e-39 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 137.62 E-value: 2.41e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 4 VKTTQLIKVFKGA----EAVNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELFGERIKNHRQHIQAL-- 77
Cdd:cd03255 1 IELKNLSKTYGGGgekvQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAfr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 78 -KKIGSLVESPSYYAHLTARENLEVLRKILGVSK----NRVDEVLDIVKLAKEANRPVKGFSLGMKQRLGIASALLGNPR 152
Cdd:cd03255 81 rRHIGFVFQSFNLLPDLTALENVELPLLLAGVPKkerrERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190
....*....|....*....|....*....|....*....
gi 1265835877 153 LLILDEPTNGLDPAGIQEIRSLIKEMPGKNGVTVLISSH 191
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTH 199
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
19-161 |
2.65e-39 |
|
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: 135.47 E-value: 2.65e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 19 VNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELFGERIkNHRQHIQALKKIGSLVESPSYYAHLTAREN 98
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDL-TDDERKSLRKEIGYVFQDPQLFPRLTVREN 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1265835877 99 LEVLRKILGVSK----NRVDEVLDIVKLAKEANRPV----KGFSLGMKQRLGIASALLGNPRLLILDEPTN 161
Cdd:pfam00005 80 LRLGLLLKGLSKrekdARAEEALEKLGLGDLADRPVgerpGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
11-229 |
8.52e-39 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 139.44 E-value: 8.52e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 11 KVFKGA----EAVNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELFGERIK--NHRQHIQALKKIG--- 81
Cdd:COG1135 9 KTFPTKggpvTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTalSERELRAARRKIGmif 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 82 ---SLVESpsyyahLTAREN----LEvlrkILGVSKN----RVDEVLDIVKLAKEANRPVKGFSLGMKQRLGIASALLGN 150
Cdd:COG1135 89 qhfNLLSS------RTVAENvalpLE----IAGVPKAeirkRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 151 PRLLILDEPTNGLDPAGIQEIRSLIKEMPGKNGVTVLISSHllyEID---HLATQVGIITKGKMLFNGSIESLRKKAKHQ 227
Cdd:COG1135 159 PKVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITH---EMDvvrRICDRVAVLENGRIVEQGPVLDVFANPQSE 235
|
..
gi 1265835877 228 VA 229
Cdd:COG1135 236 LT 237
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
20-222 |
1.53e-38 |
|
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: 136.09 E-value: 1.53e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 20 NEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELFGERIK--NHRQHIQALKKIGSLVESPSYYAHLTARE 97
Cdd:cd03261 17 KGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISglSEAELYRLRRRMGMLFQSGALFDSLTVFE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 98 NLEV-LRKILGVSKNRVDEV----LDIVKLAKEANRPVKGFSLGMKQRLGIASALLGNPRLLILDEPTNGLDPAGIQEIR 172
Cdd:cd03261 97 NVAFpLREHTRLSEEEIREIvlekLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLYDEPTAGLDPIASGVID 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1265835877 173 SLIKEMPGKNGVTVLISSHLLYEIDHLATQVGIITKGKMLFNGSIESLRK 222
Cdd:cd03261 177 DLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRA 226
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
5-210 |
3.48e-38 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 132.75 E-value: 3.48e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 5 KTTQLIKVFKGAEAVNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELFGERIknhrqhiqalkkigslv 84
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDI----------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 85 espsyyahltARENLEVLRKILGVsknrvdevldivklakeanrpVKGFSLGMKQRLGIASALLGNPRLLILDEPTNGLD 164
Cdd:cd00267 64 ----------AKLPLEELRRRIGY---------------------VPQLSGGQRQRVALARALLLNPDLLLLDEPTSGLD 112
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1265835877 165 PAGIQEIRSLIKEMPgKNGVTVLISSHLLYEIDHLATQVGIITKGK 210
Cdd:cd00267 113 PASRERLLELLRELA-EEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
15-218 |
6.93e-38 |
|
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: 134.79 E-value: 6.93e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 15 GAEAVNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELFGERIknHRQHIQAL-KKIGSLVESPSYYAHL 93
Cdd:COG1120 13 GRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDL--ASLSRRELaRRIAYVPQEPPAPFGL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 94 TARENLEV-----LRKILGVSKN---RVDEVLDIVKLAKEANRPVKGFSLGMKQRLGIASALLGNPRLLILDEPTNGLDP 165
Cdd:COG1120 91 TVRELVALgryphLGLFGRPSAEdreAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLLLDEPTSHLDL 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1265835877 166 AGIQEIRSLIKEMPGKNGVTVLISSHllyEIDH---LATQVGIITKGKMLFNGSIE 218
Cdd:COG1120 171 AHQLEVLELLRRLARERGRTVVMVLH---DLNLaarYADRLVLLKDGRIVAQGPPE 223
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
17-211 |
5.10e-37 |
|
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: 131.86 E-value: 5.10e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 17 EAVNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELFGERIKNHRQHIQAL--KKIG--------SLveS 86
Cdd:cd03257 19 KALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIrrKEIQmvfqdpmsSL--N 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 87 PSyyahLTARENL-EVLRKILGVSKN-----RVDEVLDIVKLAKE-ANRPVKGFSLGMKQRLGIASALLGNPRLLILDEP 159
Cdd:cd03257 97 PR----MTIGEQIaEPLRIHGKLSKKearkeAVLLLLVGVGLPEEvLNRYPHELSGGQRQRVAIARALALNPKLLIADEP 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1265835877 160 TNGLDPAGIQEIRSLIKEMPGKNGVTVLISSHLLYEIDHLATQVGIITKGKM 211
Cdd:cd03257 173 TSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKI 224
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
17-220 |
2.07e-36 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 136.57 E-value: 2.07e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 17 EAVNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPT---SGKIELFGERIKNHRQHIQAlKKIGSLVESPSyyAHL 93
Cdd:COG1123 20 PAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRG-RRIGMVFQDPM--TQL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 94 T----ARENLEVLRkILGVSKN----RVDEVLDIVKLAKEANRPVKGFSLGMKQRLGIASALLGNPRLLILDEPTNGLDP 165
Cdd:COG1123 97 NpvtvGDQIAEALE-NLGLSRAearaRVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPDLLIADEPTTALDV 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1265835877 166 AGIQEIRSLIKEMPGKNGVTVLISSHLLYEIDHLATQVGIITKGKMLFNGSIESL 220
Cdd:COG1123 176 TTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEI 230
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
8-220 |
3.14e-36 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 130.18 E-value: 3.14e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 8 QLIKVFKGA-EAVNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELFGERI-KNHRQHIQALK-KIG--- 81
Cdd:COG3638 7 NLSKRYPGGtPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVtALRGRALRRLRrRIGmif 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 82 ---SLVESpsyyahLTARENleVL----------RKILGV----SKNRVDEVLDIVKLAKEANRPVKGFSLGMKQRLGIA 144
Cdd:COG3638 87 qqfNLVPR------LSVLTN--VLagrlgrtstwRSLLGLfppeDRERALEALERVGLADKAYQRADQLSGGQQQRVAIA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1265835877 145 SALLGNPRLLILDEPTNGLDPAGIQEIRSLIKEMPGKNGVTVLISSHLLYEIDHLATQVGIITKGKMLFNGSIESL 220
Cdd:COG3638 159 RALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRVVFDGPPAEL 234
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-191 |
4.22e-36 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 132.53 E-value: 4.22e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 1 MEIVKTTQLIKVFKGAEAVNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELFGERIKN---HRQHI--- 74
Cdd:COG3842 3 MPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGlppEKRNVgmv 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 75 -QAlkkigslvespsyYA---HLTAREN----LevlrKILGVSKN----RVDEVLDIVKLAKEANRPVKGFSLGMKQRLG 142
Cdd:COG3842 83 fQD-------------YAlfpHLTVAENvafgL----RMRGVPKAeiraRVAELLELVGLEGLADRYPHQLSGGQQQRVA 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1265835877 143 IASALLGNPRLLILDEPTNGLDPAGIQEIRSLIKEMPGKNGVTVLISSH 191
Cdd:COG3842 146 LARALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTH 194
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
13-215 |
4.68e-36 |
|
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: 127.94 E-value: 4.68e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 13 FKGAEAVNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELFGERIknhrqhiqalkkigslvespsyyAH 92
Cdd:cd03214 9 YGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDL-----------------------AS 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 93 LTAREnlevLRKILGVsknrVDEVLDIVKLAKEANRPVKGFSLGMKQRLGIASALLGNPRLLILDEPTNGLDPAGIQEIR 172
Cdd:cd03214 66 LSPKE----LARKIAY----VPQALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQIELL 137
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1265835877 173 SLIKEMPGKNGVTVLISSHllyEIDH---LATQVGIITKGKMLFNG 215
Cdd:cd03214 138 ELLRRLARERGKTVVMVLH---DLNLaarYADRVILLKDGRIVAQG 180
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
13-212 |
7.67e-36 |
|
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: 128.84 E-value: 7.67e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 13 FKGAEAVNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGL-----MKPTSGKIELFGERIKNHRQHIQAL-KKIGSLVES 86
Cdd:cd03260 10 YGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLndlipGAPDEGEVLLDGKDIYDLDVDVLELrRRVGMVFQK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 87 PSYYaHLTARENLEVLRKILGVSKN-----RVDEVLDIVKLAKEANRPVKGFSL--GMKQRLGIASALLGNPRLLILDEP 159
Cdd:cd03260 90 PNPF-PGSIYDNVAYGLRLHGIKLKeeldeRVEEALRKAALWDEVKDRLHALGLsgGQQQRLCLARALANEPEVLLLDEP 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1265835877 160 TNGLDPAGIQEIRSLIKEMpgKNGVTVLISSHLLYEIDHLATQVGIITKGKML 212
Cdd:cd03260 169 TSALDPISTAKIEELIAEL--KKEYTIVIVTHNMQQAARVADRTAFLLNGRLV 219
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
4-191 |
1.52e-35 |
|
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: 127.65 E-value: 1.52e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 4 VKTTQLIKVFKGAEAVNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELFGERIKNHRQHIQAL-KKIGS 82
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNINELrQKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 83 LVESPSYYAHLTARENL-EVLRKILGVSKNRVDE----VLDIVKLAKEANRPVKGFSLGMKQRLGIASALLGNPRLLILD 157
Cdd:cd03262 81 VFQQFNLFPHLTVLENItLAPIKVKGMSKAEAEEraleLLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFD 160
|
170 180 190
....*....|....*....|....*....|....
gi 1265835877 158 EPTNGLDPAGIQEIRSLIKEMpGKNGVTVLISSH 191
Cdd:cd03262 161 EPTSALDPELVGEVLDVMKDL-AEEGMTMVVVTH 193
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
22-220 |
3.95e-35 |
|
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: 127.51 E-value: 3.95e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 22 VNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGK-IELFGERIKnhRQHIQALKK-IGsLVeSPS----YYAHLTA 95
Cdd:COG1119 22 ISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNdVRLFGERRG--GEDVWELRKrIG-LV-SPAlqlrFPRDETV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 96 RE--------NLEVLRKILGVSKNRVDEVLDIVKLAKEANRPVKGFSLGMKQRLGIASALLGNPRLLILDEPTNGLDPAG 167
Cdd:COG1119 98 LDvvlsgffdSIGLYREPTDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGA 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1265835877 168 IQEIRSLIKEMPGKNGVTVLISSHLLYEIDHLATQVGIITKGKMLFNGSIESL 220
Cdd:COG1119 178 RELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRVVAAGPKEEV 230
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
15-191 |
4.14e-35 |
|
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: 125.61 E-value: 4.14e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 15 GAEAVNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELFGERIKNHRQHIQAL-KKIGSLVESPS---YY 90
Cdd:TIGR01166 4 GPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPLDYSRKGLLERrQRVGLVFQDPDdqlFA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 91 AhlTARENLEVLRKILGVS----KNRVDEVLDIVKLAKEANRPVKGFSLGMKQRLGIASALLGNPRLLILDEPTNGLDPA 166
Cdd:TIGR01166 84 A--DVDQDVAFGPLNLGLSeaevERRVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAGLDPA 161
|
170 180
....*....|....*....|....*
gi 1265835877 167 GIQEIRSLIKEMPGKnGVTVLISSH 191
Cdd:TIGR01166 162 GREQMLAILRRLRAE-GMTVVISTH 185
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
13-218 |
5.03e-35 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 127.16 E-value: 5.03e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 13 FKGAEAVNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELFGERIKNHRQHIQALKKIGSLVESPSYYAH 92
Cdd:COG4674 20 FDGFKALNDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTRPDSGSVLFGGTDLTGLDEHEIARLGIGRKFQKPTVFEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 93 LTARENLEV------------LRKILGVSKNRVDEVLDIVKLAKEANRPVKGFSLGMKQRLGIASALLGNPRLLILDEPT 160
Cdd:COG4674 100 LTVFENLELalkgdrgvfaslFARLTAEERDRIEEVLETIGLTDKADRLAGLLSHGQKQWLEIGMLLAQDPKLLLLDEPV 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1265835877 161 NGLDPAGIQEIRSLIKEMPGKNGVTVlisshllyeIDH-------LATQVGIITKGKMLFNGSIE 218
Cdd:COG4674 180 AGMTDAETERTAELLKSLAGKHSVVV---------VEHdmefvrqIARKVTVLHQGSVLAEGSLD 235
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
11-208 |
1.85e-34 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 124.89 E-value: 1.85e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 11 KVFKGA----EAVNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELFGERIKNHRQHiqalkkIGSLVES 86
Cdd:cd03293 8 KTYGGGggavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPD------RGYVFQQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 87 PSYYAHLTARENLEVLRKILGVSKN----RVDEVLDIVKLAKEANRPVKGFSLGMKQRLGIASALLGNPRLLILDEPTNG 162
Cdd:cd03293 82 DALLPWLTVLDNVALGLELQGVPKAeareRAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDEPFSA 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1265835877 163 LDPAGIQEIRSLIKEMPGKNGVTVLISSHLLYEIDHLATQVGIITK 208
Cdd:cd03293 162 LDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLSA 207
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
11-191 |
2.32e-34 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 125.59 E-value: 2.32e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 11 KVFKGA----EAVNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELFGERIKNHRQHI----Qalkkigs 82
Cdd:COG1116 15 KRFPTGgggvTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPDRgvvfQ------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 83 lveSPSYYAHLTARENLEVLRKILGVSKN----RVDEVLDIVKLAKEANRPVKGFSLGMKQRLGIASALLGNPRLLILDE 158
Cdd:COG1116 88 ---EPALLPWLTVLDNVALGLELRGVPKAerreRARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPEVLLMDE 164
|
170 180 190
....*....|....*....|....*....|....*..
gi 1265835877 159 PTNGLDP---AGIQ-EIRSLIKEmpgkNGVTVLISSH 191
Cdd:COG1116 165 PFGALDAltrERLQdELLRLWQE----TGKTVLFVTH 197
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
15-221 |
2.80e-34 |
|
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: 124.71 E-value: 2.80e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 15 GAEAVNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELFGERIKNHRQHIQALKKIGsLV-ESPSYYAHL 93
Cdd:COG0410 15 GIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIARLGIG-YVpEGRRIFPSL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 94 TARENLEV---LRKILGVSKNRVDEVLDIV-KLAKEANRPvkGFSL--GMKQRLGIASALLGNPRLLILDEPTNGLDPAG 167
Cdd:COG0410 94 TVEENLLLgayARRDRAEVRADLERVYELFpRLKERRRQR--AGTLsgGEQQMLAIGRALMSRPKLLLLDEPSLGLAPLI 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1265835877 168 IQEIRSLIKEMPgKNGVTVLISSHLLYEIDHLATQVGIITKGKMLFNGSIESLR 221
Cdd:COG0410 172 VEEIFEIIRRLN-REGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELL 224
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
11-211 |
3.84e-34 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 130.15 E-value: 3.84e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 11 KVFKGAEAVNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELFGE--RIKNHRQHIQAlkKIG------S 82
Cdd:COG3845 13 KRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKpvRIRSPRDAIAL--GIGmvhqhfM 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 83 LVESpsyyahLTARENLevlrkILGvSKNRVDEVLDIVKLAKEA-------------NRPVKGFSLGMKQRLGIASALLG 149
Cdd:COG3845 91 LVPN------LTVAENI-----VLG-LEPTKGGRLDRKAARARIrelserygldvdpDAKVEDLSVGEQQRVEILKALYR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1265835877 150 NPRLLILDEPTNGLDPagiQEIRSLIKEMPG--KNGVTVLISSHLLYEIDHLATQVGIITKGKM 211
Cdd:COG3845 159 GARILILDEPTAVLTP---QEADELFEILRRlaAEGKSIIFITHKLREVMAIADRVTVLRRGKV 219
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-191 |
4.63e-34 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 127.11 E-value: 4.63e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 1 MEIVKTTQLIKVFKGAEAVNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELFGERIKN----HRqhiqa 76
Cdd:COG3839 1 MASLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDlppkDR----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 77 lkKIGSLVESPSYYAHLTARENLEVLRKILGVSKN----RVDEVLDIVKLAKEANRPVKGFSLGMKQRLGIASALLGNPR 152
Cdd:COG3839 76 --NIAMVFQSYALYPHMTVYENIAFPLKLRKVPKAeidrRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPK 153
|
170 180 190
....*....|....*....|....*....|....*....
gi 1265835877 153 LLILDEPTNGLDPAGIQEIRSLIKEMPGKNGVTVLISSH 191
Cdd:COG3839 154 VFLLDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTH 192
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-191 |
6.82e-34 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 123.61 E-value: 6.82e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 1 ME-IVKTTQLIKVFKGAE----AVNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELFGERIKN------ 69
Cdd:COG1136 1 MSpLLELRNLTKSYGTGEgevtALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSlserel 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 70 ---HRQHI----QalkkigslvespSYY--AHLTARENLEVLRKILGVSKN----RVDEVLDIVKLAKEANRPVKGFSLG 136
Cdd:COG1136 81 arlRRRHIgfvfQ------------FFNllPELTALENVALPLLLAGVSRKerreRARELLERVGLGDRLDHRPSQLSGG 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1265835877 137 MKQRLGIASALLGNPRLLILDEPTNGLDPAGIQEIRSLIKEMPGKNGVTVLISSH 191
Cdd:COG1136 149 QQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTH 203
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
4-210 |
1.25e-33 |
|
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: 123.12 E-value: 1.25e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 4 VKTTQLIKVFKGAEAVNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELFGERIKN---HRQHiqalkkI 80
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNlppHKRP------V 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 81 GSLVESPSYYAHLTARENLEVLRKILGVSKN----RVDEVLDIVKLAKEANRPVKGFSLGMKQRLGIASALLGNPRLLIL 156
Cdd:cd03300 75 NTVFQNYALFPHLTVFENIAFGLRLKKLPKAeikeRVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1265835877 157 DEPTNGLDPAGIQEIRSLIKEMPGKNGVTVLISSHLLYEIDHLATQVGIITKGK 210
Cdd:cd03300 155 DEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGK 208
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
20-211 |
1.36e-33 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 122.23 E-value: 1.36e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 20 NEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELFGERIKNHrqHIQAL-KKIGSLVESPSYYAHlTAREN 98
Cdd:COG4619 17 SPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAM--PPPEWrRQVAYVPQEPALWGG-TVRDN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 99 LE---VLRKiLGVSKNRVDEVLDIVKLAKEA-NRPVKGFSLGMKQRLGIASALLGNPRLLILDEPTNGLDPAGIQEIRSL 174
Cdd:COG4619 94 LPfpfQLRE-RKFDRERALELLERLGLPPDIlDKPVERLSGGERQRLALIRALLLQPDVLLLDEPTSALDPENTRRVEEL 172
|
170 180 190
....*....|....*....|....*....|....*..
gi 1265835877 175 IKEMPGKNGVTVLISSHLLYEIDHLATQVGIITKGKM 211
Cdd:COG4619 173 LREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
18-216 |
1.77e-33 |
|
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: 124.10 E-value: 1.77e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 18 AVNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELFGERIK-NHRQHIQAL-KKIGSLVESPSYyaHLTA 95
Cdd:TIGR04521 20 ALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITaKKKKKLKDLrKKVGLVFQFPEH--QLFE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 96 REnleVLRKI------LGVS----KNRVDEVLDIVKLAKE-ANR-PvkgFSL--GMKQRLGIASALLGNPRLLILDEPTN 161
Cdd:TIGR04521 98 ET---VYKDIafgpknLGLSeeeaEERVKEALELVGLDEEyLERsP---FELsgGQMRRVAIAGVLAMEPEVLILDEPTA 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1265835877 162 GLDPAGIQEIRSLIKEMPGKNGVTVLISSHLLYEIDHLATQVGIITKGKMLFNGS 216
Cdd:TIGR04521 172 GLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGT 226
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
14-191 |
2.62e-33 |
|
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: 121.60 E-value: 2.62e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 14 KGAEAVNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELFGERIKNHRQhiqaLKKIGSLVESPSYyaHL 93
Cdd:cd03226 11 KGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKER----RKSIGYVMQDVDY--QL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 94 ---TARENLEVLRKILGVSKNRVDEVLDIVKLAKEANRPVKGFSLGMKQRLGIASALLGNPRLLILDEPTNGLDPAGIQE 170
Cdd:cd03226 85 ftdSVREELLLGLKELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNMER 164
|
170 180
....*....|....*....|.
gi 1265835877 171 IRSLIKEMPGKnGVTVLISSH 191
Cdd:cd03226 165 VGELIRELAAQ-GKAVIVITH 184
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
17-251 |
3.33e-33 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 123.62 E-value: 3.33e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 17 EAVNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELFGERIKNHRQHIQAL-KKIGSLVESPSYYA-HLT 94
Cdd:PRK13637 21 KALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKLSDIrKKVGLVFQYPEYQLfEET 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 95 ARENLEVLRKILGVS----KNRVDEVLDIVKLAKEANRPVKGFSL--GMKQRLGIASALLGNPRLLILDEPTNGLDPAGI 168
Cdd:PRK13637 101 IEKDIAFGPINLGLSeeeiENRVKRAMNIVGLDYEDYKDKSPFELsgGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGR 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 169 QEIRSLIKEMPGKNGVTVLISSHLLYEIDHLATQVGIITKGKMLFNGSIESLRKkakhqvafttgEIEKSKTILLAngfV 248
Cdd:PRK13637 181 DEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVFK-----------EVETLESIGLA---V 246
|
...
gi 1265835877 249 PTI 251
Cdd:PRK13637 247 PQV 249
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
8-211 |
3.83e-33 |
|
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: 122.02 E-value: 3.83e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 8 QLIKVFKGAE-AVNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELFGERIKNHRQhIQALKKIGSLVES 86
Cdd:cd03295 5 NVTKRYGGGKkAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDP-VELRRKIGYVIQQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 87 PSYYAHLTARENLEVLRKILGVSK----NRVDEVLDIVKL--AKEANRPVKGFSLGMKQRLGIASALLGNPRLLILDEPT 160
Cdd:cd03295 84 IGLFPHMTVEENIALVPKLLKWPKekirERADELLALVGLdpAEFADRYPHELSGGQQQRVGVARALAADPPLLLMDEPF 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1265835877 161 NGLDP---AGIQEIRSLIKEMPGKngvTVLISSHLLYEIDHLATQVGIITKGKM 211
Cdd:cd03295 164 GALDPitrDQLQEEFKRLQQELGK---TIVFVTHDIDEAFRLADRIAIMKNGEI 214
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
28-215 |
4.74e-33 |
|
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: 121.25 E-value: 4.74e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 28 EGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELFGERIKNHRQHIQ---ALKKIGSLVESPSYYAHLTARENLE--VL 102
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRKKINlppQQRKIGLVFQQYALFPHLNVRENLAfgLK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 103 RKILGVSKNRVDEVLDIVKLAKEANRPVKGFSLGMKQRLGIASALLGNPRLLILDEPTNGLDPAGIQEIRSLIKEMPGKN 182
Cdd:cd03297 102 RKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELKQIKKNL 181
|
170 180 190
....*....|....*....|....*....|...
gi 1265835877 183 GVTVLISSHLLYEIDHLATQVGIITKGKMLFNG 215
Cdd:cd03297 182 NIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
18-220 |
4.78e-33 |
|
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: 122.54 E-value: 4.78e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 18 AVNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELFGERIKNHRQHIQALKKIG------------SLVE 85
Cdd:TIGR04520 17 ALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLDEENLWEIRKKVGmvfqnpdnqfvgATVE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 86 -----SPsyyahltarENLEVLRKILgvsKNRVDEVLDIVKLAKEANRPVKGFSLGMKQRLGIASALLGNPRLLILDEPT 160
Cdd:TIGR04520 97 ddvafGL---------ENLGVPREEM---RKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLAMRPDIIILDEAT 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 161 NGLDPAGIQEIRSLIKEMPGKNGVTVLISSHLLYEIdHLATQVGIITKGKMLFNGSIESL 220
Cdd:TIGR04520 165 SMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEA-VLADRVIVMNKGKIVAEGTPREI 223
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1-220 |
5.42e-33 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 121.92 E-value: 5.42e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 1 MEIVKTTQLIKVFKGAEAVNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELFGERIKNHRQHIQALKKI 80
Cdd:PRK10895 1 MATLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 81 GSLVESPSYYAHLTARENLEV---LRKILGVS--KNRVDEVLDIVKLAKEANRPVKGFSLGMKQRLGIASALLGNPRLLI 155
Cdd:PRK10895 81 GYLPQEASIFRRLSVYDNLMAvlqIRDDLSAEqrEDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFIL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1265835877 156 LDEPTNGLDPAGIQEIRSLIKEMPgKNGVTVLISSHLLYEIDHLATQVGIITKGKMLFNGSIESL 220
Cdd:PRK10895 161 LDEPFAGVDPISVIDIKRIIEHLR-DSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEI 224
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
4-210 |
2.22e-32 |
|
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: 119.28 E-value: 2.22e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 4 VKTTQLIKVFKGAEAVNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIeLFGERIKNHRQhiQALKKIGSL 83
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRI-YIGGRDVTDLP--PKDRDIAMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 84 VESPSYYAHLTARENLEVLRKILGVSKN----RVDEVLDIVKLAKEANRPVKGFSLGMKQRLGIASALLGNPRLLILDEP 159
Cdd:cd03301 78 FQNYALYPHMTVYDNIAFGLKLRKVPKDeideRVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1265835877 160 TNGLDPAGIQEIRSLIKEMPGKNGVTVLISSHLLYEIDHLATQVGIITKGK 210
Cdd:cd03301 158 LSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQ 208
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
3-191 |
3.03e-32 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 119.71 E-value: 3.03e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 3 IVKTTQLIKVFKGAEAVNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELFGERIKNHRQHIQAL-KKIG 81
Cdd:COG1126 1 MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKKDINKLrRKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 82 SLVESPSYYAHLTARENL-EVLRKILGVSK----NRVDEVLDIVKLAKEANRPVKGFSLGMKQRLGIASALLGNPRLLIL 156
Cdd:COG1126 81 MVFQQFNLFPHLTVLENVtLAPIKVKKMSKaeaeERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKVMLF 160
|
170 180 190
....*....|....*....|....*....|....*
gi 1265835877 157 DEPTNGLDPAGIQEIRSLIKEMpGKNGVTVLISSH 191
Cdd:COG1126 161 DEPTSALDPELVGEVLDVMRDL-AKEGMTMVVVTH 194
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
15-228 |
6.19e-32 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 118.82 E-value: 6.19e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 15 GAEAVNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELFGERIKNHRQHI--QALKKIGSLVESPSYYAH 92
Cdd:cd03256 13 GKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKAlrQLRRQIGMIFQQFNLIER 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 93 LTARENLEV--------LRKILGV----SKNRVDEVLDIVKLAKEANRPVKGFSLGMKQRLGIASALLGNPRLLILDEPT 160
Cdd:cd03256 93 LSVLENVLSgrlgrrstWRSLFGLfpkeEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIARALMQQPKLILADEPV 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1265835877 161 NGLDPAGIQEIRSLIKEMPGKNGVTVLISSHLLYEIDHLATQVGIITKGKMLFNGSIESLRKKAKHQV 228
Cdd:cd03256 173 ASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAELTDEVLDEI 240
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1-210 |
6.26e-32 |
|
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: 118.98 E-value: 6.26e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 1 MEIVkTTQLIKVFKGAEAVNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELFGERIKNHrqHIQAlKKI 80
Cdd:cd03296 1 MSIE-VRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDV--PVQE-RNV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 81 GSLVESPSYYAHLTAREN----LEVLRKILGVSKN----RVDEVLDIVKLAKEANRPVKGFSLGMKQRLGIASALLGNPR 152
Cdd:cd03296 77 GFVFQHYALFRHMTVFDNvafgLRVKPRSERPPEAeiraKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPK 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1265835877 153 LLILDEPTNGLDPAGIQEIRSLIKEMPGKNGVTVLISSHLLYEIDHLATQVGIITKGK 210
Cdd:cd03296 157 VLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGR 214
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
4-229 |
1.67e-31 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 120.29 E-value: 1.67e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 4 VKTTQLIKVFKGA----EAVNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELFGERIK--NHRQHIQAL 77
Cdd:PRK11153 2 IELKNISKVFPQGgrtiHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTalSEKELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 78 KKIG------SLVESPsyyahlTARENLEVLRKILGVSKN----RVDEVLDIVKLAKEANRPVKGFSLGMKQRLGIASAL 147
Cdd:PRK11153 82 RQIGmifqhfNLLSSR------TVFDNVALPLELAGTPKAeikaRVTELLELVGLSDKADRYPAQLSGGQKQRVAIARAL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 148 LGNPRLLILDEPTNGLDPAGIQEIRSLIKEMPGKNGVTVLISSHLLYEIDHLATQVGIITKGKMLFNGSIESLRKKAKHQ 227
Cdd:PRK11153 156 ASNPKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHPKHP 235
|
..
gi 1265835877 228 VA 229
Cdd:PRK11153 236 LT 237
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
21-225 |
2.09e-31 |
|
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: 117.44 E-value: 2.09e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 21 EVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELFGERIKNHRQHiqaLKKIGSLVESPSYYAHLTARENLE 100
Cdd:cd03299 17 NVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE---KRDISYVPQNYALFPHMTVYKNIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 101 V-LRKILGVSKNRVDEVLDIVKLAKEA---NRPVKGFSLGMKQRLGIASALLGNPRLLILDEPTNGLDPAGIQEIRSLIK 176
Cdd:cd03299 94 YgLKKRKVDKKEIERKVLEIAEMLGIDhllNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLREELK 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1265835877 177 EMPGKNGVTVLISSHLLYEIDHLATQVGIITKGKMLFNGSIESLRKKAK 225
Cdd:cd03299 174 KIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPK 222
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
15-220 |
2.18e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 118.80 E-value: 2.18e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 15 GAEAVNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELFGERIKNHRQHIQALKK-IGSLVESP------ 87
Cdd:PRK13636 18 GTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRKGLMKLREsVGMVFQDPdnqlfs 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 88 -SYYAHLT-ARENLEVLRKILgvsKNRVDEVLDIVKLAKEANRPVKGFSLGMKQRLGIASALLGNPRLLILDEPTNGLDP 165
Cdd:PRK13636 98 aSVYQDVSfGAVNLKLPEDEV---RKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDP 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1265835877 166 AGIQEIRSLIKEMPGKNGVTVLISSHLLYEIDHLATQVGIITKGKMLFNGSIESL 220
Cdd:PRK13636 175 MGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEV 229
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
14-216 |
2.67e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 118.26 E-value: 2.67e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 14 KGAEAVNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELFGERIK-NHRQHIQALKKIGSLVESP--SYY 90
Cdd:PRK13639 13 DGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKyDKKSLLEVRKTVGIVFQNPddQLF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 91 AHlTARENLEVLRKILGVSK----NRVDEVLDIVKLAKEANRPVKGFSLGMKQRLGIASALLGNPRLLILDEPTNGLDPA 166
Cdd:PRK13639 93 AP-TVEEDVAFGPLNLGLSKeeveKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPM 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1265835877 167 GIQEIRSLIKEMpGKNGVTVLISSHLLYEIDHLATQVGIITKGKMLFNGS 216
Cdd:PRK13639 172 GASQIMKLLYDL-NKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGT 220
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
6-221 |
6.21e-31 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 116.63 E-value: 6.21e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 6 TTQLIKV------FKGAEAVNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELFGERIKNHRQHIQALKK 79
Cdd:PRK11300 2 SQPLLSVsglmmrFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIARMG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 80 IGSLVESPSYYAHLTARENLEV-------------------LRKILGVSKNRVDEVLDIVKLAKEANRPVKGFSLGMKQR 140
Cdd:PRK11300 82 VVRTFQHVRLFREMTVIENLLVaqhqqlktglfsgllktpaFRRAESEALDRAATWLERVGLLEHANRQAGNLAYGQQRR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 141 LGIASALLGNPRLLILDEPTNGLDPAGIQEIRSLIKEMPGKNGVTVLISSHLLYEIDHLATQVGIITKGKMLFNGSIESL 220
Cdd:PRK11300 162 LEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEI 241
|
.
gi 1265835877 221 R 221
Cdd:PRK11300 242 R 242
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
18-218 |
1.05e-30 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 115.56 E-value: 1.05e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 18 AVNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELFGeriknhrqhiqalkKIGSLVE-----SPSyyah 92
Cdd:COG1134 41 ALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNG--------------RVSALLElgagfHPE---- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 93 LTARENLEVLRKILGVSKNRVDEVLD-IVKLA---KEANRPVKGFSLGMKQRLGIASALLGNPRLLILDEPTNGLDPA-- 166
Cdd:COG1134 103 LTGRENIYLNGRLLGLSRKEIDEKFDeIVEFAelgDFIDQPVKTYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAfq 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1265835877 167 --GIQEIRSLIKEmpgknGVTVLISSHLLYEIDHLATQVGIITKGKMLFNGSIE 218
Cdd:COG1134 183 kkCLARIRELRES-----GRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPE 231
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
18-212 |
1.26e-30 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 116.20 E-value: 1.26e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 18 AVNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELFGERIKN-HRQHIQAL--KKIGSLVESPSYYAHLT 94
Cdd:cd03294 39 GVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAmSRKELRELrrKKISMVFQSFALLPHRT 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 95 ARENLEVLRKILGVSKN----RVDEVLDIVKLAKEANRPVKGFSLGMKQRLGIASALLGNPRLLILDEPTNGLDPAGIQE 170
Cdd:cd03294 119 VLENVAFGLEVQGVPRAereeRAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRRE 198
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1265835877 171 IRSLIKEMPGKNGVTVLISSHLLYEIDHLATQVGIITKGKML 212
Cdd:cd03294 199 MQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLV 240
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
8-211 |
1.69e-30 |
|
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: 114.43 E-value: 1.69e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 8 QLIKVFK----GAEAVNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELFGERIKN-HRQHIQALK-KIG 81
Cdd:cd03292 2 EFINVTKtypnGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDlRGRAIPYLRrKIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 82 SLVESPSYYAHLTARENLEVLRKILGVS----KNRVDEVLDIVKLAKEANRPVKGFSLGMKQRLGIASALLGNPRLLILD 157
Cdd:cd03292 82 VVFQDFRLLPDRNVYENVAFALEVTGVPpreiRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIAD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1265835877 158 EPTNGLDPAGIQEIRSLIKEMpGKNGVTVLISSHLLYEIDHLATQVGIITKGKM 211
Cdd:cd03292 162 EPTGNLDPDTTWEIMNLLKKI-NKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
9-216 |
2.24e-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: 121.27 E-value: 2.24e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 9 LIKVFK--GAEAVNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELFGERIKNHRQHIQalKKIGSLVES 86
Cdd:TIGR01257 934 LVKIFEpsGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDAVR--QSLGMCPQH 1011
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 87 PSYYAHLTARENLEVLRKILGVSKN----RVDEVLDIVKLAKEANRPVKGFSLGMKQRLGIASALLGNPRLLILDEPTNG 162
Cdd:TIGR01257 1012 NILFHHLTVAEHILFYAQLKGRSWEeaqlEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSG 1091
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1265835877 163 LDPAGIQEIRSLIkeMPGKNGVTVLISSHLLYEIDHLATQVGIITKGKMLFNGS 216
Cdd:TIGR01257 1092 VDPYSRRSIWDLL--LKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGT 1143
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
4-211 |
2.54e-30 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 112.14 E-value: 2.54e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 4 VKTTQLIKVFKGAEAVNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELFGERIKNHrqhiqalkkigsl 83
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFA------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 84 veSPSyyahlTAREnlevlrkiLGVsknrvdevldivklakeanRPVKGFSLGMKQRLGIASALLGNPRLLILDEPTNGL 163
Cdd:cd03216 68 --SPR-----DARR--------AGI-------------------AMVYQLSVGERQMVEIARALARNARLLILDEPTAAL 113
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1265835877 164 DPAGIQEIRSLIKEMpGKNGVTVLISSHLLYEIDHLATQVGIITKGKM 211
Cdd:cd03216 114 TPAEVERLFKVIRRL-RAQGVAVIFISHRLDEVFEIADRVTVLRDGRV 160
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
14-210 |
2.88e-30 |
|
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: 112.48 E-value: 2.88e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 14 KGAEAVNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELFGERIKNH-----RQHIqalkkigSLVESPS 88
Cdd:cd03228 13 RPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLdleslRKNI-------AYVPQDP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 89 YYAHLTARENLevlrkilgvsknrvdevldivklakeanrpvkgFSLGMKQRLGIASALLGNPRLLILDEPTNGLDPAGI 168
Cdd:cd03228 86 FLFSGTIRENI---------------------------------LSGGQRQRIAIARALLRDPPILILDEATSALDPETE 132
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1265835877 169 QEIRSLIKEMPGknGVTVLISSHLLYEIDHlATQVGIITKGK 210
Cdd:cd03228 133 ALILEALRALAK--GKTVIVIAHRLSTIRD-ADRIIVLDDGR 171
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
11-220 |
3.64e-30 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 116.74 E-value: 3.64e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 11 KVFKGAEAVNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELFGERIkNHRQhIQAlKKIGSLVESPSYY 90
Cdd:PRK11432 14 KRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDV-THRS-IQQ-RDICMVFQSYALF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 91 AHLTARENLEVLRKILGVSK----NRVDEVLDIVKLAKEANRPVKGFSLGMKQRLGIASALLGNPRLLILDEPTNGLDPA 166
Cdd:PRK11432 91 PHMSLGENVGYGLKMLGVPKeerkQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDAN 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1265835877 167 GIQEIRSLIKEMPGKNGVTVLISSHLLYEIDHLATQVGIITKGKMLFNGSIESL 220
Cdd:PRK11432 171 LRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQEL 224
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
18-226 |
4.19e-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: 115.92 E-value: 4.19e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 18 AVNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKP---TSGKIELFGERI--------KNHR-QHIQ--------AL 77
Cdd:COG0444 20 AVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLlklsekelRKIRgREIQmifqdpmtSL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 78 ---KKIGSLVEspsyyahltarenlEVLRKILGVSKN----RVDEVLDIVKLAKEANR----PVKgFSLGMKQRLGIASA 146
Cdd:COG0444 100 npvMTVGDQIA--------------EPLRIHGGLSKAeareRAIELLERVGLPDPERRldryPHE-LSGGMRQRVMIARA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 147 LLGNPRLLILDEPTNGLDpAGIQ-EIRSLIKEMPGKNGVTVLISSHLLYEIDHLATQVGIITKGKMLFNGSIESLRKKAK 225
Cdd:COG0444 165 LALEPKLLIADEPTTALD-VTIQaQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGPVEELFENPR 243
|
.
gi 1265835877 226 H 226
Cdd:COG0444 244 H 244
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
21-220 |
4.53e-30 |
|
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: 116.75 E-value: 4.53e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 21 EVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELFGERIKNHRQHIQA---LKKIGSLVESPSYYAHLTARE 97
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKGIFLppeKRRIGYVFQEARLFPHLSVRG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 98 NLEVLRKILGVSKNRV--DEVLDIVKLAKEANRPVKGFSLGMKQRLGIASALLGNPRLLILDEPTNGLDPAGIQEIRSLI 175
Cdd:TIGR02142 95 NLRYGMKRARPSERRIsfERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILPYL 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1265835877 176 KEMPGKNGVTVLISSHLLYEIDHLATQVGIITKGKMLFNGSIESL 220
Cdd:TIGR02142 175 ERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEV 219
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
22-193 |
7.71e-30 |
|
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: 112.07 E-value: 7.71e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 22 VNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELFGERIknHRQHIQALKKIGSLVESPSYYAHLTARENLEV 101
Cdd:TIGR01189 19 LSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPL--AEQRDEPHENILYLGHLPGLKPELSALENLHF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 102 LRKILGVSKNRVDEVLDIVKLAKEANRPVKGFSLGMKQRLGIASALLGNPRLLILDEPTNGLDPAGIQEIRSLIKEMPGK 181
Cdd:TIGR01189 97 WAAIHGGAQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVALLAGLLRAHLAR 176
|
170
....*....|..
gi 1265835877 182 NGVTVLISSHLL 193
Cdd:TIGR01189 177 GGIVLLTTHQDL 188
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
21-220 |
1.03e-29 |
|
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: 1.03e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 21 EVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELFGERIKNHRQHIqALK----KIGSLVESPSYYAHLTAR 96
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLQDSARGI-FLPphrrRIGYVFQEARLFPHLSVR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 97 ENLEVLRKILGVSKNRV--DEVLDIVKLAKEANRPVKGFSLGMKQRLGIASALLGNPRLLILDEPTNGLDPAGIQEIRSL 174
Cdd:COG4148 96 GNLLYGRKRAPRAERRIsfDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAEILPY 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1265835877 175 IKEMPGKNGVTVLISSHLLYEIDHLATQVGIITKGKMLFNGSIESL 220
Cdd:COG4148 176 LERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEV 221
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
15-223 |
2.07e-29 |
|
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: 117.55 E-value: 2.07e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 15 GAEAVNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELFGERIKNH-----RQHIqalkkigSLVESPSY 89
Cdd:COG4988 349 GRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLdpaswRRQI-------AWVPQNPY 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 90 YAHLTARENLEVLRKilGVSKNRVDEVLDIVKLAKEANR-------PV----KGFSLGMKQRLGIASALLGNPRLLILDE 158
Cdd:COG4988 422 LFAGTIRENLRLGRP--DASDEELEAALEAAGLDEFVAAlpdgldtPLgeggRGLSGGQAQRLALARALLRDAPLLLLDE 499
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1265835877 159 PTNGLDPAGIQEIRSLIKEMpgKNGVTVLISSHLLYEIDHlATQVGIITKGKMLFNGSIESLRKK 223
Cdd:COG4988 500 PTAHLDAETEAEILQALRRL--AKGRTVILITHRLALLAQ-ADRILVLDDGRIVEQGTHEELLAK 561
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
18-215 |
2.25e-29 |
|
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: 111.47 E-value: 2.25e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 18 AVNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELFGeriknhrqhiqalkKIGSLVE-----SPSyyah 92
Cdd:cd03220 37 ALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG--------------RVSSLLGlgggfNPE---- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 93 LTARENLEVLRKILGVSK----NRVDEVLDIVKLAKEANRPVKGFSLGMKQRLGIASALLGNPRLLILDEPTNGLDPAGI 168
Cdd:cd03220 99 LTGRENIYLNGRLLGLSRkeidEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQ 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1265835877 169 QEIRSLIKEMpGKNGVTVLISSHLLYEIDHLATQVGIITKGKMLFNG 215
Cdd:cd03220 179 EKCQRRLREL-LKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1-210 |
4.93e-29 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 113.70 E-value: 4.93e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 1 MEIVkTTQLIKVFKGAEAVNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELFGERIKNHRqHIQAlKKI 80
Cdd:COG1118 1 MSIE-VRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFTNL-PPRE-RRV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 81 GSLVESpsyYA---HLTAREN----LEVLRKILGVSKNRVDEVLDIVKLAKEANRPVKGFSLGMKQRLGIASALLGNPRL 153
Cdd:COG1118 78 GFVFQH---YAlfpHMTVAENiafgLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEV 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1265835877 154 LILDEPTNGLDPAGIQEIRSLIKEMPGKNGVTVLISSHLLYEIDHLATQVGIITKGK 210
Cdd:COG1118 155 LLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGR 211
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
1-218 |
1.14e-28 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 110.49 E-value: 1.14e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 1 MEIvKTTQLIKVFKGAEAVNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELFGERI----KNHRQHIQA 76
Cdd:COG4161 1 MSI-QLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFdfsqKPSEKAIRL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 77 L-KKIGSLVESPSYYAHLTARENL-EVLRKILGVSKN----RVDEVLDIVKLAKEANRPVKGFSLGMKQRLGIASALLGN 150
Cdd:COG4161 80 LrQKVGMVFQQYNLWPHLTVMENLiEAPCKVLGLSKEqareKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMME 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1265835877 151 PRLLILDEPTNGLDPAGIQEIRSLIKEMpGKNGVTVLISSHllyEID---HLATQVGIITKGKMLFNGSIE 218
Cdd:COG4161 160 PQVLLFDEPTAALDPEITAQVVEIIREL-SQTGITQVIVTH---EVEfarKVASQVVYMEKGRIIEQGDAS 226
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
2-223 |
1.30e-28 |
|
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: 116.27 E-value: 1.30e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 2 EIVKTTQLIKVFKGAE--AVNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELFGERIKNHRQHIQalKK 79
Cdd:TIGR01257 1936 DILRLNELTKVYSGTSspAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISDVH--QN 2013
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 80 IGSLVESPSYYAHLTARENLEVLRKILGVSKNRVDEV----LDIVKLAKEANRPVKGFSLGMKQRLGIASALLGNPRLLI 155
Cdd:TIGR01257 2014 MGYCPQFDAIDDLLTGREHLYLYARLRGVPAEEIEKVanwsIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVL 2093
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1265835877 156 LDEPTNGLDPAGIQ----EIRSLIKEmpgknGVTVLISSHLLYEIDHLATQVGIITKGKMLFNGSIESLRKK 223
Cdd:TIGR01257 2094 LDEPTTGMDPQARRmlwnTIVSIIRE-----GRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGTIQHLKSK 2160
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
10-215 |
1.84e-28 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 109.72 E-value: 1.84e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 10 IKVFKGA-EAVNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELFGERI----KNHRQHIQAL-KKIGSL 83
Cdd:PRK11124 8 INCFYGAhQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFdfskTPSDKAIRELrRNVGMV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 84 VESPSYYAHLTARENL-EVLRKILGVSKN----RVDEVLDIVKLAKEANRPVKGFSLGMKQRLGIASALLGNPRLLILDE 158
Cdd:PRK11124 88 FQQYNLWPHLTVQQNLiEAPCRVLGLSKDqalaRAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDE 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 159 PTNGLDPAGIQEIRSLIKEMPGkNGVTVLISSHllyEID---HLATQVGIITKGKMLFNG 215
Cdd:PRK11124 168 PTAALDPEITAQIVSIIRELAE-TGITQVIVTH---EVEvarKTASRVVYMENGHIVEQG 223
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
9-220 |
2.31e-28 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 112.62 E-value: 2.31e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 9 LIKVFKGAEAVNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELFGERIknhrQHIQALKK-IGSLVESP 87
Cdd:PRK11607 25 LTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDL----SHVPPYQRpINMMFQSY 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 88 SYYAHLTARENLEVLRKILGVSK----NRVDEVLDIVKLAKEANRPVKGFSLGMKQRLGIASALLGNPRLLILDEPTNGL 163
Cdd:PRK11607 101 ALFPHMTVEQNIAFGLKQDKLPKaeiaSRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGAL 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1265835877 164 DPAGIQEIRSLIKEMPGKNGVTVLISSHLLYEIDHLATQVGIITKGKMLFNGSIESL 220
Cdd:PRK11607 181 DKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEI 237
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
15-220 |
3.00e-28 |
|
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: 114.09 E-value: 3.00e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 15 GAEAVNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELFGERIKNH-----RQHIqalkkigSLVESPSY 89
Cdd:COG4987 347 GRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLdeddlRRRI-------AVVPQRPH 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 90 YAHLTARENLEVLRKilGVSKNRVDEVLDIVKLAKEANRPVKG-----------FSLGMKQRLGIASALLGNPRLLILDE 158
Cdd:COG4987 420 LFDTTLRENLRLARP--DATDEELWAALERVGLGDWLAALPDGldtwlgeggrrLSGGERRRLALARALLRDAPILLLDE 497
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1265835877 159 PTNGLDPAGIQEIRSLIKE-MPGKngvTVLISSHLLYEIDHlATQVGIITKGKMLFNGSIESL 220
Cdd:COG4987 498 PTEGLDAATEQALLADLLEaLAGR---TVLLITHRLAGLER-MDRILVLEDGRIVEQGTHEEL 556
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
15-223 |
6.16e-28 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 113.78 E-value: 6.16e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 15 GAEAVNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELFGERIKNH-----RQHIqalkkigSLVESPSY 89
Cdd:COG2274 487 SPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIdpaslRRQI-------GVVLQDVF 559
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 90 YAHLTARENLevlrkILG---VSKNRVDEVLDIVKLAKEANR-------PV----KGFSLGMKQRLGIASALLGNPRLLI 155
Cdd:COG2274 560 LFSGTIRENI-----TLGdpdATDEEIIEAARLAGLHDFIEAlpmgydtVVgeggSNLSGGQRQRLAIARALLRNPRILI 634
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1265835877 156 LDEPTNGLDPAGIQEIRSLIKEMpgKNGVTVLISSHLLYEIDHlATQVGIITKGKMLFNGSIESLRKK 223
Cdd:COG2274 635 LDEATSALDAETEAIILENLRRL--LKGRTVIIIAHRLSTIRL-ADRIIVLDKGRIVEDGTHEELLAR 699
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
3-216 |
8.30e-28 |
|
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: 108.15 E-value: 8.30e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 3 IVKTTQLIKVF-KGAEAVNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELFGERIKNHRQH--IQALKK 79
Cdd:TIGR02315 1 MLEVENLSKVYpNGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKklRKLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 80 IGSLVESPSYYAHLTARENLEV--------LRKILGV----SKNRVDEVLDIVKLAKEANRPVKGFSLGMKQRLGIASAL 147
Cdd:TIGR02315 81 IGMIFQHYNLIERLTVLENVLHgrlgykptWRSLLGRfseeDKERALSALERVGLADKAYQRADQLSGGQQQRVAIARAL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1265835877 148 LGNPRLLILDEPTNGLDPAGIQEIRSLIKEMPGKNGVTVLISSHLLYEIDHLATQVGIITKGKMLFNGS 216
Cdd:TIGR02315 161 AQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGA 229
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
12-191 |
9.25e-28 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 106.88 E-value: 9.25e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 12 VFKGaeavneVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELFGERIKnhrqhiqalkkIGSLVESPSYYA 91
Cdd:PRK13539 17 LFSG------LSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDID-----------DPDVAEACHYLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 92 H-------LTARENLEVLRKILGVSKNRVDEVLDIVKLAKEANRPVKGFSLGMKQRLGIASALLGNPRLLILDEPTNGLD 164
Cdd:PRK13539 80 HrnamkpaLTVAENLEFWAAFLGGEELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALD 159
|
170 180
....*....|....*....|....*..
gi 1265835877 165 PAGIQEIRSLIKEMPGKNGvTVLISSH 191
Cdd:PRK13539 160 AAAVALFAELIRAHLAQGG-IVIAATH 185
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
11-196 |
1.46e-27 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 111.65 E-value: 1.46e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 11 KVFKGAEAVNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELFGERIKnHRQHIQALKK-IG------SL 83
Cdd:COG1129 12 KSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVR-FRSPRDAQAAgIAiihqelNL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 84 VEspsyyaHLTARENL----EVLRKILgVSKNRV----DEVLDIVKLAKEANRPVKGFSLGMKQRLGIASALLGNPRLLI 155
Cdd:COG1129 91 VP------NLSVAENIflgrEPRRGGL-IDWRAMrrraRELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRDARVLI 163
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1265835877 156 LDEPTNGLDPAGIQEIRSLIKEMPGKnGVTVLISSHLLYEI 196
Cdd:COG1129 164 LDEPTASLTEREVERLFRIIRRLKAQ-GVAIIYISHRLDEV 203
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
4-301 |
1.04e-26 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 107.51 E-value: 1.04e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 4 VKTTQLIKVFKGAEAVNEVNLSIKEGEIYGFLGPNGAGKTTTIrMLLGLMKPTSGKIEL-FGERIKNHRqhiqALKK-IG 81
Cdd:NF000106 14 VEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RGA-LPAHV*GPDAGRRPWrF*TWCANRR----ALRRtIG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 82 SlvESPSYYAH---LTARENLEVLRKILGVSKN----RVDEVLDIVKLAKEANRPVKGFSLGMKQRLGIASALLGNPRLL 154
Cdd:NF000106 89 *--HRPVR*GRresFSGRENLYMIGR*LDLSRKdaraRADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 155 ILDEPTNGLDPAGIQEIRSLIKEMPgKNGVTVLISSHLLYEIDHLATQVGIITKGKMLFNGSIESLRKKA---------- 224
Cdd:NF000106 167 YLDEPTTGLDPRTRNEVWDEVRSMV-RDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDELKTKVggrtlqirpa 245
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1265835877 225 -KHQVAFTTGEIEKSKTILLAnGFVPTIDKNSLLLDYIDHEQVAHLVYQLVQENVSIYRVEEKSKSLEDIFLKLTSEE 301
Cdd:NF000106 246 hAAELDRMVGAIAQAGLDGIA-GATADHEDGVVNVPIVSDEQLSAVVGMLGERGFTISGHQHPSAQL*EVFLAITGQK 322
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
14-193 |
1.19e-26 |
|
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: 103.73 E-value: 1.19e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 14 KGAEAVNE-VNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELFGERIKNHRQHI-QALKKIGSLvesPSYYA 91
Cdd:cd03231 10 RDGRALFSgLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIaRGLLYLGHA---PGIKT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 92 HLTARENLEVLRKILGVSKnrVDEVLDIVKLAKEANRPVKGFSLGMKQRLGIASALLGNPRLLILDEPTNGLDPAGIQEI 171
Cdd:cd03231 87 TLSVLENLRFWHADHSDEQ--VEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARF 164
|
170 180
....*....|....*....|..
gi 1265835877 172 RSLIKEMPGKNGVTVLISSHLL 193
Cdd:cd03231 165 AEAMAGHCARGGMVVLTTHQDL 186
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1-220 |
3.92e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 104.50 E-value: 3.92e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 1 MEIVKTTQLIKVFKGA-EAVNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELFGERIKnhRQHIQALKK 79
Cdd:PRK13652 1 MHLIETRDLCYSYSGSkEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPIT--KENIREVRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 80 -IGSLVESPSYYAHLTARENLEVLRKI-LGVS----KNRVDEVLDIVKLAKEANRPVKGFSLGMKQRLGIASALLGNPRL 153
Cdd:PRK13652 79 fVGLVFQNPDDQIFSPTVEQDIAFGPInLGLDeetvAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQV 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1265835877 154 LILDEPTNGLDPAGIQEIRSLIKEMPGKNGVTVLISSHLLYEIDHLATQVGIITKGKMLFNGSIESL 220
Cdd:PRK13652 159 LVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEI 225
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
19-215 |
4.86e-26 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 101.86 E-value: 4.86e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 19 VNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKP--TSGKIelfgeRIKNHRQHIQALKK-IGSLVESPSYYAHLTA 95
Cdd:cd03213 25 LKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGlgVSGEV-----LINGRPLDKRSFRKiIGYVPQDDILHPTLTV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 96 RENLEVLRKIlgvsknrvdevldivklakeanrpvKGFSLGMKQRLGIASALLGNPRLLILDEPTNGLDPAGIQEIRSLI 175
Cdd:cd03213 100 RETLMFAAKL-------------------------RGLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLL 154
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1265835877 176 KEMpGKNGVTVLISSH-LLYEIDHLATQVGIITKGKMLFNG 215
Cdd:cd03213 155 RRL-ADTGRTIICSIHqPSSEIFELFDKLLLLSQGRVIYFG 194
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
3-216 |
1.20e-25 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 103.16 E-value: 1.20e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 3 IVKTTQLIKVFKGAEAVNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELFGERIKNHRQHIQALKK-IG 81
Cdd:PRK13638 1 MLATSDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKRGLLALRQqVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 82 SLVESPS---YYAHLTAreNLEVLRKILGVSKN----RVDEVLDIVKLAKEANRPVKGFSLGMKQRLGIASALLGNPRLL 154
Cdd:PRK13638 81 TVFQDPEqqiFYTDIDS--DIAFSLRNLGVPEAeitrRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1265835877 155 ILDEPTNGLDPAGIQEIRSLIKEMPGKnGVTVLISSH---LLYEIdhlATQVGIITKGKMLFNGS 216
Cdd:PRK13638 159 LLDEPTAGLDPAGRTQMIAIIRRIVAQ-GNHVIISSHdidLIYEI---SDAVYVLRQGQILTHGA 219
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
3-191 |
1.56e-25 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 104.64 E-value: 1.56e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 3 IVKTTQLIKVFKGAEAVNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELFGERIKN----HRQhiqalk 78
Cdd:PRK09452 14 LVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHvpaeNRH------ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 79 kIGSLVESPSYYAHLTARENLEVLRKILGVSKN----RVDEVLDIVKLAKEANRPVKGFSLGMKQRLGIASALLGNPRLL 154
Cdd:PRK09452 88 -VNTVFQSYALFPHMTVFENVAFGLRMQKTPAAeitpRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVL 166
|
170 180 190
....*....|....*....|....*....|....*..
gi 1265835877 155 ILDEPTNGLDPAGIQEIRSLIKEMPGKNGVTVLISSH 191
Cdd:PRK09452 167 LLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTH 203
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
18-257 |
3.19e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 101.61 E-value: 3.19e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 18 AVNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELFGERIKNHR-QHIQalKKIGSLVESP-SYYAHLTA 95
Cdd:PRK13632 24 ALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENlKEIR--KKIGIIFQNPdNQFIGATV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 96 R-------ENLEVLRKILgvsKNRVDEVLDIVKLAKEANRPVKGFSLGMKQRLGIASALLGNPRLLILDEPTNGLDPAGI 168
Cdd:PRK13632 102 EddiafglENKKVPPKKM---KDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFDESTSMLDPKGK 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 169 QEIRSLIKEMPGKNGVTVLISSHLLYEIdHLATQVGIITKGKMLFNGS-IESLRKK-----AKHQVAFTtgeIEKSKTIl 242
Cdd:PRK13632 179 REIKKIMVDLRKTRKKTLISITHDMDEA-ILADKVIVFSEGKLIAQGKpKEILNNKeilekAKIDSPFI---YKLSKKL- 253
|
250
....*....|....*
gi 1265835877 243 laNGFVPTIDKNSLL 257
Cdd:PRK13632 254 --KGIDPTYNEEELI 266
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
15-224 |
3.95e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 101.74 E-value: 3.95e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 15 GAEAVNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELFGERIknHRQHIQAL-KKIGSLVESP--SYYA 91
Cdd:PRK13647 17 GTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREV--NAENEKWVrSKVGLVFQDPddQVFS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 92 hLTARENLEVLRKILGVSK----NRVDEVLDIVKLAKEANRPVKGFSLGMKQRLGIASALLGNPRLLILDEPTNGLDPAG 167
Cdd:PRK13647 95 -STVWDDVAFGPVNMGLDKdeveRRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRG 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1265835877 168 IQEIRSLIKEMpGKNGVTVLISSHLLYEIDHLATQVGIITKGKMLFNGSIESLRKKA 224
Cdd:PRK13647 174 QETLMEILDRL-HNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKSLLTDED 229
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
20-225 |
6.45e-25 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 104.38 E-value: 6.45e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 20 NEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIEL----------------------------FGERIKNHR 71
Cdd:COG0488 15 DDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIpkglrigylpqeppldddltvldtvldgDAELRALEA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 72 QHIQALKKIGSLVESPSYYAHLTARE------NLEvlrkilgvskNRVDEVLDIVKLAKE-ANRPVKGFSLGMKQRLGIA 144
Cdd:COG0488 95 ELEELEAKLAEPDEDLERLAELQEEFealggwEAE----------ARAEEILSGLGFPEEdLDRPVSELSGGWRRRVALA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 145 SALLGNPRLLILDEPTNGLDPAGIQEIRSLIKEMPGkngvTVLISSHLLYEIDHLATQVGIITKGKM-LFNGSIES-LRK 222
Cdd:COG0488 165 RALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYPG----TVLVVSHDRYFLDRVATRILELDRGKLtLYPGNYSAyLEQ 240
|
...
gi 1265835877 223 KAK 225
Cdd:COG0488 241 RAE 243
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
19-191 |
1.07e-24 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 97.67 E-value: 1.07e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 19 VNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELFGERIK-----NHRQHIQALKKIGSLVESpsyyahl 93
Cdd:cd03246 18 LRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISqwdpnELGDHVGYLPQDDELFSG------- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 94 TARENLevlrkilgvsknrvdevldivklakeanrpvkgFSLGMKQRLGIASALLGNPRLLILDEPTNGLDPAGIQEIRS 173
Cdd:cd03246 91 SIAENI---------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQ 137
|
170
....*....|....*...
gi 1265835877 174 LIKEMPgKNGVTVLISSH 191
Cdd:cd03246 138 AIAALK-AAGATRIVIAH 154
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
21-193 |
1.81e-24 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 97.95 E-value: 1.81e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 21 EVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELFGERIKNHR-QHIQALKKIGSLvesPSYYAHLTARENL 99
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRdEYHQDLLYLGHQ---PGIKTELTALENL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 100 EVLRKILG-VSKNRVDEVLDIVKLAKEANRPVKGFSLGMKQRLGIASALLGNPRLLILDEPTNGLDPAGIQEIRSLIKEM 178
Cdd:PRK13538 96 RFYQRLHGpGDDEALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGVARLEALLAQH 175
|
170
....*....|....*
gi 1265835877 179 PGKNGVTVLISSHLL 193
Cdd:PRK13538 176 AEQGGMVILTTHQDL 190
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
23-220 |
2.64e-24 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 98.29 E-value: 2.64e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 23 NLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELFGErikNHRQHIQALKKIGSLVESPSYYAHLTARENLEvl 102
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQ---DLTALPPAERPVSMLFQENNLFPHLTVAQNIG-- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 103 rkiLGVS---------KNRVDEVLDIVKLAKEANRPVKGFSLGMKQRLGIASALLGNPRLLILDEPTNGLDPAGIQEIRS 173
Cdd:COG3840 94 ---LGLRpglkltaeqRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDPALRQEMLD 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1265835877 174 LIKEMPGKNGVTVLISSHLLYEIDHLATQVGIITKGKMLFNGSIESL 220
Cdd:COG3840 171 LVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAAL 217
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
17-215 |
3.70e-24 |
|
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: 97.66 E-value: 3.70e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 17 EAVNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELFGERIKN-HRQHIQalKKIGSLVESPSYYAHlTA 95
Cdd:cd03245 18 PALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQlDPADLR--RNIGYVPQDVTLFYG-TL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 96 RENLEVLRKIlgVSKNRVDEVLDIVKLAKEANRPVKGFSL-----------GMKQRLGIASALLGNPRLLILDEPTNGLD 164
Cdd:cd03245 95 RDNITLGAPL--ADDERILRAAELAGVTDFVNKHPNGLDLqigergrglsgGQRQAVALARALLNDPPILLLDEPTSAMD 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1265835877 165 PAGIQEIRSLIKEMPGknGVTVLISSHlLYEIDHLATQVGIITKGKMLFNG 215
Cdd:cd03245 173 MNSEERLKERLRQLLG--DKTLIIITH-RPSLLDLVDRIIVMDSGRIVADG 220
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
3-218 |
4.55e-24 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 101.68 E-value: 4.55e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 3 IVKTTQLIKVFKGAEAVNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELfGERIKnhrqhiqalkkIGs 82
Cdd:COG0488 315 VLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETVK-----------IG- 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 83 lvespsYYA--HLTARENLEVLRKILGVSKNRVD-EVLDIVKL----AKEANRPVKGFSLGMKQRLGIASALLGNPRLLI 155
Cdd:COG0488 382 ------YFDqhQEELDPDKTVLDELRDGAPGGTEqEVRGYLGRflfsGDDAFKPVGVLSGGEKARLALAKLLLSPPNVLL 455
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1265835877 156 LDEPTNGLDPAGIQEIRSLIKEMPGkngvTVLISSHLLYEIDHLATQVGIITKGKM-LFNGSIE 218
Cdd:COG0488 456 LDEPTNHLDIETLEALEEALDDFPG----TVLLVSHDRYFLDRVATRILEFEDGGVrEYPGGYD 515
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
14-191 |
8.37e-24 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 101.39 E-value: 8.37e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 14 KGAEAVNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELFGERIKNH-----RQHIqalkkigSLVESPS 88
Cdd:COG1132 351 GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLtleslRRQI-------GVVPQDT 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 89 YYAHLTARENLEVLRKilGVSKNRVDEVLDIVKLAKEANRPVKGF-----------SLGMKQRLGIASALLGNPRLLILD 157
Cdd:COG1132 424 FLFSGTIRENIRYGRP--DATDEEVEEAAKAAQAHEFIEALPDGYdtvvgergvnlSGGQRQRIAIARALLKDPPILILD 501
|
170 180 190
....*....|....*....|....*....|....*..
gi 1265835877 158 EPTNGLDP---AGIQEirSLIKEMPGKngvTVLISSH 191
Cdd:COG1132 502 EATSALDTeteALIQE--ALERLMKGR---TTIVIAH 533
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
18-280 |
1.10e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 97.85 E-value: 1.10e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 18 AVNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELFGERIKNHRQHIQALKKIGSLVESPSYYAHLT--- 94
Cdd:PRK13633 25 ALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLWDIRNKAGMVFQNPDNQIVATive 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 95 -----ARENLEVLRKILgvsKNRVDEVLDIVKLAKEANRPVKGFSLGMKQRLGIASALLGNPRLLILDEPTNGLDPAGIQ 169
Cdd:PRK13633 105 edvafGPENLGIPPEEI---RERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGRR 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 170 EIRSLIKEMPGKNGVTVLISSHLLYEIDHlATQVGIITKGKMLFNGSIESLRKkakhqvafttgEIEKSKTILLangfvp 249
Cdd:PRK13633 182 EVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIFK-----------EVEMMKKIGL------ 243
|
250 260 270
....*....|....*....|....*....|.
gi 1265835877 250 tidknsllldyiDHEQVAHLVYQLVQENVSI 280
Cdd:PRK13633 244 ------------DVPQVTELAYELKKEGVDI 262
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
11-178 |
3.67e-23 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 97.85 E-value: 3.67e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 11 KVFKGAEAVNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELFGERIKnhRQHIQAlKKIGSLVESPSYY 90
Cdd:PRK10851 10 KSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVS--RLHARD-RKVGFVFQHYALF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 91 AHLTAREN----LEVL----RKILGVSKNRVDEVLDIVKLAKEANRPVKGFSLGMKQRLGIASALLGNPRLLILDEPTNG 162
Cdd:PRK10851 87 RHMTVFDNiafgLTVLprreRPNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGA 166
|
170
....*....|....*.
gi 1265835877 163 LDPAGIQEIRSLIKEM 178
Cdd:PRK10851 167 LDAQVRKELRRWLRQL 182
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
17-199 |
3.73e-23 |
|
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: 99.28 E-value: 3.73e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 17 EAVNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELFGERIknhrQHIQA---LKKIGSLVESPSYYAHl 93
Cdd:TIGR02857 336 PALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPL----ADADAdswRDQIAWVPQHPFLFAG- 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 94 TARENLEVLRKilGVSKNRVDEVLDIVKLAK-EANRPV----------KGFSLGMKQRLGIASALLGNPRLLILDEPTNG 162
Cdd:TIGR02857 411 TIAENIRLARP--DASDAEIREALERAGLDEfVAALPQgldtpigeggAGLSGGQAQRLALARAFLRDAPLLLLDEPTAH 488
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1265835877 163 LDPAGIQEIRSLIKEMpgKNGVTVLISSH---LLYEIDHL 199
Cdd:TIGR02857 489 LDAETEAEVLEALRAL--AQGRTVLLVTHrlaLAALADRI 526
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1-191 |
4.26e-23 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 97.79 E-value: 4.26e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 1 MEIVKTTQLIKVFKGAEAVNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIeLFGERIKNHRQhiQALKKI 80
Cdd:PRK11000 1 MASVTLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDL-FIGEKRMNDVP--PAERGV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 81 GSLVESPSYYAHLTARENLEVLRKILGVSKN----RVDEVLDIVKLAKEANRPVKGFSLGMKQRLGIASALLGNPRLLIL 156
Cdd:PRK11000 78 GMVFQSYALYPHLSVAENMSFGLKLAGAKKEeinqRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLL 157
|
170 180 190
....*....|....*....|....*....|....*
gi 1265835877 157 DEPTNGLDPAGIQEIRSLIKEMPGKNGVTVLISSH 191
Cdd:PRK11000 158 DEPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTH 192
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
13-216 |
4.33e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 96.35 E-value: 4.33e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 13 FKGAeAVNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELFGERIKNHRQHI---QALKKIGSLVESP-S 88
Cdd:PRK13649 18 FEGR-ALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNKdikQIRKKVGLVFQFPeS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 89 YYAHLTARENLEVLRKILGVSKNRVD----EVLDIVKLAKEA-NRPVKGFSLGMKQRLGIASALLGNPRLLILDEPTNGL 163
Cdd:PRK13649 97 QLFEETVLKDVAFGPQNFGVSQEEAEalarEKLALVGISESLfEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGL 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1265835877 164 DPAGIQEIRSLIKEMpGKNGVTVLISSHLLYEIDHLATQVGIITKGKMLFNGS 216
Cdd:PRK13649 177 DPKGRKELMTLFKKL-HQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGK 228
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
15-211 |
4.81e-23 |
|
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: 93.65 E-value: 4.81e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 15 GAEAVNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELFGE--RIKNHRQHIQAlkKIGSLVESPSYYA- 91
Cdd:cd03215 12 VKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKpvTRRSPRDAIRA--GIAYVPEDRKREGl 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 92 --HLTARENLeVLRKILgvsknrvdevldivklakeanrpvkgfSLGMKQRLGIASALLGNPRLLILDEPTNGLDPAGIQ 169
Cdd:cd03215 90 vlDLSVAENI-ALSSLL---------------------------SGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKA 141
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1265835877 170 EIRSLIKEMpGKNGVTVLISSHLLYEIDHLATQVGIITKGKM 211
Cdd:cd03215 142 EIYRLIREL-ADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
22-209 |
6.25e-23 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 94.84 E-value: 6.25e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 22 VNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELFGeriknhrQHIQALKKIGSLV-ESPSYYAHLTARENL- 99
Cdd:TIGR01184 4 VNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEG-------KQITEPGPDRMVVfQNYSLLPWLTVRENIa 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 100 ----EVLRKiLGVSKNR--VDEVLDIVKLAKEANRPVKGFSLGMKQRLGIASALLGNPRLLILDEPTNGLDPAGIQEIRS 173
Cdd:TIGR01184 77 lavdRVLPD-LSKSERRaiVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQE 155
|
170 180 190
....*....|....*....|....*....|....*.
gi 1265835877 174 LIKEMPGKNGVTVLISSHLLYEIDHLATQVGIITKG 209
Cdd:TIGR01184 156 ELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
19-211 |
6.69e-23 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 95.52 E-value: 6.69e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 19 VNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKI--------ELFGERIKNHRQHIQALkkigsLVESPSYY 90
Cdd:PRK10419 28 LNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVswrgeplaKLNRAQRKAFRRDIQMV-----FQDSISAV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 91 -AHLTARENL-EVLRKILGVSKN----RVDEVLDIVKLAKE-ANRPVKGFSLGMKQRLGIASALLGNPRLLILDEPTNGL 163
Cdd:PRK10419 103 nPRKTVREIIrEPLRHLLSLDKAerlaRASEMLRAVDLDDSvLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNL 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1265835877 164 DPAGIQEIRSLIKEMPGKNGVTVLISSHLLYEIDHLATQVGIITKGKM 211
Cdd:PRK10419 183 DLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQI 230
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
20-210 |
7.19e-23 |
|
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: 92.13 E-value: 7.19e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 20 NEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELfGERIKnhrqhiqalkkigslvesPSYYAHLtarenl 99
Cdd:cd03221 17 KDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTW-GSTVK------------------IGYFEQL------ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 100 evlrkilgvsknrvdevldivklakeanrpvkgfSLGMKQRLGIASALLGNPRLLILDEPTNGLDPAGIQEIRSLIKEMP 179
Cdd:cd03221 72 ----------------------------------SGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEEALKEYP 117
|
170 180 190
....*....|....*....|....*....|.
gi 1265835877 180 GkngvTVLISSHLLYEIDHLATQVGIITKGK 210
Cdd:cd03221 118 G----TVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
18-250 |
1.21e-22 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 95.93 E-value: 1.21e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 18 AVNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELFG--------ERIKNHRQHIQALKK---------- 79
Cdd:PRK15079 36 AVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGkdllgmkdDEWRAVRSDIQMIFQdplaslnprm 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 80 -IGSLVESP--SYYAHLTAREnlevlrkilgvSKNRVDEVLDIVKLAKEA-NRPVKGFSLGMKQRLGIASALLGNPRLLI 155
Cdd:PRK15079 116 tIGEIIAEPlrTYHPKLSRQE-----------VKDRVKAMMLKVGLLPNLiNRYPHEFSGGQCQRIGIARALILEPKLII 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 156 LDEPTNGLDpAGIQ-EIRSLIKEMPGKNGVTVLISSHLLYEIDHLATQVGIITKGKMLFNGSIESLRKKAKH-------- 226
Cdd:PRK15079 185 CDEPVSALD-VSIQaQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNPLHpytkalms 263
|
250 260
....*....|....*....|....
gi 1265835877 227 QVAFTTGEIEKSKTILLANGFVPT 250
Cdd:PRK15079 264 AVPIPDPDLERNKTIQLLEGELPS 287
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-227 |
2.05e-22 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 93.66 E-value: 2.05e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 1 MEIVKTTQLIKVFKGAEAVNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKI-----ELFGERIKNHRQH-I 74
Cdd:PRK11264 1 MSAIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIrvgdiTIDTARSLSQQKGlI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 75 QALK-KIGSLVESPSYYAHLTAREN-----LEVLRKILGVSKNRVDEVLDIVKLAKEANRPVKGFSLGMKQRLGIASALL 148
Cdd:PRK11264 81 RQLRqHVGFVFQNFNLFPHRTVLENiiegpVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1265835877 149 GNPRLLILDEPTNGLDPAGIQEIRSLIKEMPGKNGVTVLISSHLLYEIDhLATQVGIITKGKMLFNGSIESLRKKAKHQ 227
Cdd:PRK11264 161 MRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARD-VADRAIFMDQGRIVEQGPAKALFADPQQP 238
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
15-192 |
2.05e-22 |
|
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: 97.05 E-value: 2.05e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 15 GAEAVNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELFGERIKNHRQhiQALKKIGSLVESPsyyAHL- 93
Cdd:TIGR02868 347 APPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQ--DEVRRRVSVCAQD---AHLf 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 94 --TARENLEVLRKilGVSKNRVDEVLDIVKLAKEANRPVKG-----------FSLGMKQRLGIASALLGNPRLLILDEPT 160
Cdd:TIGR02868 422 dtTVRENLRLARP--DATDEELWAALERVGLADWLRALPDGldtvlgeggarLSGGERQRLALARALLADAPILLLDEPT 499
|
170 180 190
....*....|....*....|....*....|...
gi 1265835877 161 NGLDPAGIQE-IRSLIKEMPGKngVTVLISSHL 192
Cdd:TIGR02868 500 EHLDAETADElLEDLLAALSGR--TVVLITHHL 530
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
4-217 |
2.33e-22 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 96.78 E-value: 2.33e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 4 VKTTQLIKVFKGAEAVNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELFGERIKNHRQHIQALKKIGSL 83
Cdd:PRK09700 6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLGIGII 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 84 VESPSYYAHLTARENLEV----LRKILGVS-------KNRVDEVLDIVKLAKEANRPVKGFSLGMKQRLGIASALLGNPR 152
Cdd:PRK09700 86 YQELSVIDELTVLENLYIgrhlTKKVCGVNiidwremRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAK 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1265835877 153 LLILDEPTNGLDPAGIQEIRSLIKEMPGKNGVTVLIsSHLLYEIDHLATQVGIITKGKMLFNGSI 217
Cdd:PRK09700 166 VIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYI-SHKLAEIRRICDRYTVMKDGSSVCSGMV 229
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-194 |
2.96e-22 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 93.25 E-value: 2.96e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 1 MEIVKTTQLIKVFKGAEAV-NEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIElfgeriknhrqHIQALkK 79
Cdd:PRK09544 1 MTSLVSLENVSVSFGQRRVlSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK-----------RNGKL-R 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 80 IGSLVESpsyyAHLTARENLEVLRKIL---GVSKNRVDEVLDIVKLAKEANRPVKGFSLGMKQRLGIASALLGNPRLLIL 156
Cdd:PRK09544 69 IGYVPQK----LYLDTTLPLTVNRFLRlrpGTKKEDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVL 144
|
170 180 190
....*....|....*....|....*....|....*...
gi 1265835877 157 DEPTNGLDPAGIQEIRSLIKEMPGKNGVTVLISSHLLY 194
Cdd:PRK09544 145 DEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLH 182
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
18-277 |
3.09e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 93.93 E-value: 3.09e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 18 AVNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELfGERI----KNHRQHIQALKKIGSLVESPSyyaHL 93
Cdd:PRK13634 22 ALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTI-GERVitagKKNKKLKPLRKKVGIVFQFPE---HQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 94 TARENleVLRKI------LGVS----KNRVDEVLDIVKLAKE--ANRPvkgFSL--GMKQRLGIASALLGNPRLLILDEP 159
Cdd:PRK13634 98 LFEET--VEKDIcfgpmnFGVSeedaKQKAREMIELVGLPEEllARSP---FELsgGQMRRVAIAGVLAMEPEVLVLDEP 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 160 TNGLDPAGIQEIRSLIKEMPGKNGVTVLISSHLLYEIDHLATQVGIITKGKMLFNGSIESLRKKAKHQVAFTTG---EIE 236
Cdd:PRK13634 173 TAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADPDELEAIGLDlpeTVK 252
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1265835877 237 KSKTILLANGFvpTIDKNSLLLdyidhEQVAHLVYQLVQEN 277
Cdd:PRK13634 253 FKRALEEKFGI--SFPKPCLTL-----EELAHEVVQLLRKG 286
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
24-215 |
3.75e-22 |
|
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: 92.17 E-value: 3.75e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 24 LSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELFGErikNHRQHIQALKKIGSLVESPSYYAHLTARENLEVLR 103
Cdd:cd03298 19 LTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGV---DVTAAPPADRPVSMLFQENNLFAHLTVEQNVGLGL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 104 ----KILGVSKNRVDEVLDIVKLAKEANRPVKGFSLGMKQRLGIASALLGNPRLLILDEPTNGLDPAGIQEIRSLIKEMP 179
Cdd:cd03298 96 spglKLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDLH 175
|
170 180 190
....*....|....*....|....*....|....*.
gi 1265835877 180 GKNGVTVLISSHLLYEIDHLATQVGIITKGKMLFNG 215
Cdd:cd03298 176 AETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
13-218 |
4.24e-22 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 93.54 E-value: 4.24e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 13 FKGAE--AVNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELFGeRIKNHRQHIQALKKIGSLVESP-SY 89
Cdd:PRK13635 15 YPDAAtyALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGG-MVLSEETVWDVRRQVGMVFQNPdNQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 90 YAHLTARENLEVLRKILGVSKN----RVDEVLDIVKLAKEANRPVKGFSLGMKQRLGIASALLGNPRLLILDEPTNGLDP 165
Cdd:PRK13635 94 FVGATVQDDVAFGLENIGVPREemveRVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDP 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1265835877 166 AGIQEIRSLIKEMPGKNGVTVLISSHLLYEIDHlATQVGIITKGKMLFNGSIE 218
Cdd:PRK13635 174 RGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPE 225
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
14-215 |
4.25e-22 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 92.33 E-value: 4.25e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 14 KGAEAVNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLM---KPTSGKIELFGERIKNHrqhiQALKKIGSLVESPSYY 90
Cdd:cd03234 18 KYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVeggGTTSGQILFNGQPRKPD----QFQKCVAYVRQDDILL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 91 AHLTARENLEVLRKILG--VSKNRVDEVLDIVKLAKE------ANRPVKGFSLGMKQRLGIASALLGNPRLLILDEPTNG 162
Cdd:cd03234 94 PGLTVRETLTYTAILRLprKSSDAIRKKRVEDVLLRDlaltriGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSG 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1265835877 163 LDPAGIQEIRSLIKEMpGKNGVTVLISSHL-LYEIDHLATQVGIITKGKMLFNG 215
Cdd:cd03234 174 LDSFTALNLVSTLSQL-ARRNRIVILTIHQpRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
15-191 |
6.18e-22 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 92.53 E-value: 6.18e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 15 GAEAVNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELFGeRIKNHRQHIQALKKIGSLVESPSYYAHLT 94
Cdd:PRK13548 14 GRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNG-RPLADWSPAELARRRAVLPQHSSLSFPFT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 95 ARENLEVLRKILGVSKNR----VDEVLDIVKLAKEANRPVKGFSLGMKQRLGIASALL------GNPRLLILDEPTNGLD 164
Cdd:PRK13548 93 VEEVVAMGRAPHGLSRAEddalVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAqlwepdGPPRWLLLDEPTSALD 172
|
170 180
....*....|....*....|....*..
gi 1265835877 165 PAGIQEIRSLIKEMPGKNGVTVLISSH 191
Cdd:PRK13548 173 LAHQHHVLRLARQLAHERGLAVIVVLH 199
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
3-216 |
7.08e-22 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 92.38 E-value: 7.08e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 3 IVKTTQLIKVFKGAEAVNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLM---KPTSGKIELFGERIKNHRQHIQALKK 79
Cdd:PRK09984 4 IIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgdKSAGSHIELLGRTVQREGRLARDIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 80 ----IGSLVESPSYYAHLTARENLEV------------LRKILGVSKNRVDEVLDIVKLAKEANRPVKGFSLGMKQRLGI 143
Cdd:PRK09984 84 sranTGYIFQQFNLVNRLSVLENVLIgalgstpfwrtcFSWFTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAI 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1265835877 144 ASALLGNPRLLILDEPTNGLDPAGIQEIRSLIKEMPGKNGVTVLISSHLLYEIDHLATQVGIITKGKMLFNGS 216
Cdd:PRK09984 164 ARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGS 236
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
19-210 |
9.53e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 92.49 E-value: 9.53e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 19 VNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELFGERIK-----NHRQHIQALKK------IGSLVESP 87
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTeenvwDIRHKIGMVFQnpdnqfVGATVEDD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 88 SYYAhltaRENLEVLRKILgvsKNRVDEVLDIVKLAKEANRPVKGFSLGMKQRLGIASALLGNPRLLILDEPTNGLDPAG 167
Cdd:PRK13650 103 VAFG----LENKGIPHEEM---KERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEG 175
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1265835877 168 IQEIRSLIKEMPGKNGVTVLISSHLLYEIdHLATQVGIITKGK 210
Cdd:PRK13650 176 RLELIKTIKGIRDDYQMTVISITHDLDEV-ALSDRVLVMKNGQ 217
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
3-220 |
1.16e-21 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 91.31 E-value: 1.16e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 3 IVKTTQLIKVFKGAEAVNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELFGERIKNHRQHIQALKKIGS 82
Cdd:PRK09493 1 MIEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLIRQEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 83 LVESPSY-YAHLTARENLEV-LRKILGVSK----NRVDEVLDIVKLAKEANRPVKGFSLGMKQRLGIASALLGNPRLLIL 156
Cdd:PRK09493 81 MVFQQFYlFPHLTALENVMFgPLRVRGASKeeaeKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLF 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1265835877 157 DEPTNGLDPAGIQEIRSLIKEMpGKNGVTVLISSHllyEIDhLATQVG----IITKGKMLFNGSIESL 220
Cdd:PRK09493 161 DEPTSALDPELRHEVLKVMQDL-AEEGMTMVIVTH---EIG-FAEKVAsrliFIDKGRIAEDGDPQVL 223
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
17-225 |
1.64e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 92.15 E-value: 1.64e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 17 EAVNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELFGERI--KNHRQHIQAL-KKIGSLVESPSyyAHL 93
Cdd:PRK13646 21 QAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIthKTKDKYIRPVrKRIGMVFQFPE--SQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 94 TaRENLEvlRKILGVSKN---RVDEVLD-----IVKLAKEAN----RPVKgFSLGMKQRLGIASALLGNPRLLILDEPTN 161
Cdd:PRK13646 99 F-EDTVE--REIIFGPKNfkmNLDEVKNyahrlLMDLGFSRDvmsqSPFQ-MSGGQMRKIAIVSILAMNPDIIVLDEPTA 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1265835877 162 GLDPAGIQEIRSLIKEMPGKNGVTVLISSHLLYEIDHLATQVGIITKGKMLFNGSIESLRKKAK 225
Cdd:PRK13646 175 GLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFKDKK 238
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
18-189 |
1.72e-21 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 94.81 E-value: 1.72e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 18 AVNEVNLSIKEGEIYGFLGPNGAGKTTtirmLLGLM----KPTSGKIELFGE--RIKNHRQHI--------QALKKigsl 83
Cdd:NF033858 16 ALDDVSLDIPAGCMVGLIGPDGVGKSS----LLSLIagarKIQQGRVEVLGGdmADARHRRAVcpriaympQGLGK---- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 84 vespSYYAHLTARENLEVLRKILGVSKN----RVDEVLDIVKLAKEANRPVKGFSLGMKQRLGIASALLGNPRLLILDEP 159
Cdd:NF033858 88 ----NLYPTLSVFENLDFFGRLFGQDAAerrrRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCALIHDPDLLILDEP 163
|
170 180 190
....*....|....*....|....*....|....*..
gi 1265835877 160 TNGLDPAG-------IQEIRSlikEMPgknGVTVLIS 189
Cdd:NF033858 164 TTGVDPLSrrqfwelIDRIRA---ERP---GMSVLVA 194
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
18-225 |
4.33e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 90.58 E-value: 4.33e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 18 AVNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELFGERIKNH-----RQHIQALKK------IGSLVEs 86
Cdd:PRK13648 24 TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDnfeklRKHIGIVFQnpdnqfVGSIVK- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 87 psyYAHLTARENLEVLRKILgvsKNRVDEVLDIVKLAKEANRPVKGFSLGMKQRLGIASALLGNPRLLILDEPTNGLDPA 166
Cdd:PRK13648 103 ---YDVAFGLENHAVPYDEM---HRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPD 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1265835877 167 GIQEIRSLIKEMPGKNGVTVLISSHLLYEIDHlATQVGIITKGKMLFNGSIESLRKKAK 225
Cdd:PRK13648 177 ARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIFDHAE 234
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
18-210 |
4.75e-21 |
|
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: 93.21 E-value: 4.75e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 18 AVNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMkPTSGKIELFGERI--------KNHRQHIQalkkI------GSL 83
Cdd:COG4172 301 AVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLI-PSEGEIRFDGQDLdglsrralRPLRRRMQ----VvfqdpfGSL 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 84 veSPsyyaHLTAR----ENLEVLRKILGVS--KNRVDEVLDIVKLAKEA-NRPVKGFSLGMKQRLGIASALLGNPRLLIL 156
Cdd:COG4172 376 --SP----RMTVGqiiaEGLRVHGPGLSAAerRARVAEALEEVGLDPAArHRYPHEFSGGQRQRIAIARALILEPKLLVL 449
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1265835877 157 DEPTNGLDpAGIQ-EIRSLIKEMPGKNGVTVLISSHLLYEIDHLATQVGIITKGK 210
Cdd:COG4172 450 DEPTSALD-VSVQaQILDLLRDLQREHGLAYLFISHDLAVVRALAHRVMVMKDGK 503
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-233 |
6.24e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 89.90 E-value: 6.24e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 1 MEIVKTTQLIKVFKGA-EAVNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMK-----PTSGKIELFGERIKNHR-QH 73
Cdd:PRK14267 1 MKFAIETVNLRVYYGSnHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElneeaRVEGEVRLFGRNIYSPDvDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 74 IQALKKIGSLVESPSYYAHLTARENLEVLRKILGVSKNRvDEVLDIVKLA-KEA----------NRPVKGFSLGMKQRLG 142
Cdd:PRK14267 81 IEVRREVGMVFQYPNPFPHLTIYDNVAIGVKLNGLVKSK-KELDERVEWAlKKAalwdevkdrlNDYPSNLSGGQRQRLV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 143 IASALLGNPRLLILDEPTNGLDPAGIQEIRSLIKEMpgKNGVTVLISSHLLYEIDHLATQVGIITKGKMLFNGSIESLRK 222
Cdd:PRK14267 160 IARALAMKPKILLMDEPTANIDPVGTAKIEELLFEL--KKEYTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFE 237
|
250
....*....|...
gi 1265835877 223 KAKHQVA--FTTG 233
Cdd:PRK14267 238 NPEHELTekYVTG 250
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
19-228 |
6.63e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 89.72 E-value: 6.63e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 19 VNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMK------PTSGKIELFGERIkNHRQHIQALKKIGSLVESPSYYAH 92
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiydskiKVDGKVLYFGKDI-FQIDAIKLRKEVGMVFQQPNPFPH 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 93 LTARENLEVLRKILGVSKNR-----VDEVLDIVKLAKEA----NRPVKGFSLGMKQRLGIASALLGNPRLLILDEPTNGL 163
Cdd:PRK14246 105 LSIYDNIAYPLKSHGIKEKReikkiVEECLRKVGLWKEVydrlNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSMI 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1265835877 164 DPAGIQEIRSLIKEMpgKNGVTVLISSHLLYEIDHLATQVGIITKGKMLFNGSIESLRKKAKHQV 228
Cdd:PRK14246 185 DIVNSQAIEKLITEL--KNEIAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNEL 247
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
14-223 |
7.43e-21 |
|
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: 88.82 E-value: 7.43e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 14 KGAEAVNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELFGERIKNhRQHIQALKKIGSLVESPSYYAHl 93
Cdd:cd03254 14 EKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRD-ISRKSLRSMIGVVLQDTFLFSG- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 94 TARENLevlrkILGVSKNRVDEVLDIVKLAK--------------EANRPVKGFSLGMKQRLGIASALLGNPRLLILDEP 159
Cdd:cd03254 92 TIMENI-----RLGRPNATDEEVIEAAKEAGahdfimklpngydtVLGENGGNLSQGERQLLAIARAMLRDPKILILDEA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1265835877 160 TNGLDPAGIQEIRSLIKEMpgKNGVTVLISSHLLYEIDHlATQVGIITKGKMLFNGSIESLRKK 223
Cdd:cd03254 167 TSNIDTETEKLIQEALEKL--MKGRTSIIIAHRLSTIKN-ADKILVLDDGKIIEEGTHDELLAK 227
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
13-209 |
8.06e-21 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 89.37 E-value: 8.06e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 13 FKGAEAVNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELFGERIKnhrqhiqalkkiGSLVESPSYYAH 92
Cdd:PRK11248 11 YGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVE------------GPGAERGVVFQN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 93 ------LTARENLEVLRKILGVSK----NRVDEVLDIVKLAKEANRPVKGFSLGMKQRLGIASALLGNPRLLILDEPTNG 162
Cdd:PRK11248 79 egllpwRNVQDNVAFGLQLAGVEKmqrlEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGA 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1265835877 163 LDPAGIQEIRSLIKEMPGKNGVTVLISSHLLYEIDHLATQVGIITKG 209
Cdd:PRK11248 159 LDAFTREQMQTLLLKLWQETGKQVLLITHDIEEAVFMATELVLLSPG 205
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
18-215 |
9.32e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 90.15 E-value: 9.32e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 18 AVNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELFGERIKNHRQHIQALKKIGSLVESPSYYAHLtarE 97
Cdd:PRK13651 22 ALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKKKTKEKEKVLEKLVIQKTRFKKI---K 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 98 NLEVLRKILGV-------------------------------SKNRVDEVLDIVKLAKE-ANRPVKGFSLGMKQRLGIAS 145
Cdd:PRK13651 99 KIKEIRRRVGVvfqfaeyqlfeqtiekdiifgpvsmgvskeeAKKRAAKYIELVGLDESyLQRSPFELSGGQKRRVALAG 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 146 ALLGNPRLLILDEPTNGLDPAGIQEIRSLIKEMpGKNGVTVLISSHLLYEIDHLATQVGIITKGKMLFNG 215
Cdd:PRK13651 179 ILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNL-NKQGKTIILVTHDLDNVLEWTKRTIFFKDGKIIKDG 247
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
26-220 |
9.69e-21 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 92.42 E-value: 9.69e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 26 IKEGEIYGFLGPNGAGKTTTIRMLLGLMKP---TSGKIELFGERIkNHRQhiqaLKKIGSLV-ESPSYYAHLTARENLEV 101
Cdd:TIGR00955 48 AKPGELLAVMGSSGAGKTTLMNALAFRSPKgvkGSGSVLLNGMPI-DAKE----MRAISAYVqQDDLFIPTLTVREHLMF 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 102 ---LRKILGVSK----NRVDEVLDIVKLAKEAN------RPVKGFSLGMKQRLGIASALLGNPRLLILDEPTNGLDPAGI 168
Cdd:TIGR00955 123 qahLRMPRRVTKkekrERVDEVLQALGLRKCANtrigvpGRVKGLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMA 202
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1265835877 169 QEIRSLIKEMPGKnGVTVLISSHL-LYEIDHLATQVGIITKGKMLFNGSIESL 220
Cdd:TIGR00955 203 YSVVQVLKGLAQK-GKTIICTIHQpSSELFELFDKIILMAEGRVAYLGSPDQA 254
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
25-210 |
1.00e-20 |
|
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: 89.00 E-value: 1.00e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 25 SIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELFGERIKNHRQHIQAlkkigslvESPSyyahlTARENLEVLRK 104
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSYKPQYIKA--------DYEG-----TVRDLLSSITK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 105 ILGVSKNRVDEVLDIVKLAKEANRPVKGFSLGMKQRLGIASALLGNPRLLILDEPTNGLDpagiQEIRSL----IKEMPG 180
Cdd:cd03237 88 DFYTHPYFKTEIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLD----VEQRLMaskvIRRFAE 163
|
170 180 190
....*....|....*....|....*....|
gi 1265835877 181 KNGVTVLISSHLLYEIDHLATQVgIITKGK 210
Cdd:cd03237 164 NNEKTAFVVEHDIIMIDYLADRL-IVFEGE 192
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
22-216 |
1.21e-20 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 88.84 E-value: 1.21e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 22 VNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMkPTSGKIELFGERIKNHRQHIQALKKiGSLVESPS---------YYA- 91
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAWSAAELARHR-AYLSQQQTppfampvfqYLTl 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 92 HLTARENLEVLRKILgvsknrvDEVLDIVKLAKEANRPVKGFSLGMKQRLGIASALL-----GNP--RLLILDEPTNGLD 164
Cdd:PRK03695 93 HQPDKTRTEAVASAL-------NEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVLqvwpdINPagQLLLLDEPMNSLD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1265835877 165 PAGIQEIRSLIKEMPGKnGVTVLISSHLLYEIDHLATQVGIITKGKMLFNGS 216
Cdd:PRK03695 166 VAQQAALDRLLSELCQQ-GIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGR 216
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
13-239 |
1.77e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 89.00 E-value: 1.77e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 13 FKGAEAVNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSG-----KIELFGERIKNHRQHIQALKKIGSLVESP 87
Cdd:PRK14271 31 FAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIFNYRDVLEFRRRVGMLFQRP 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 88 SYYAHLTARENLEVLR--------KILGVSKNRVDEV--LDIVKlAKEANRPVKgFSLGMKQRLGIASALLGNPRLLILD 157
Cdd:PRK14271 111 NPFPMSIMDNVLAGVRahklvprkEFRGVAQARLTEVglWDAVK-DRLSDSPFR-LSGGQQQLLCLARTLAVNPEVLLLD 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 158 EPTNGLDPAGIQEIRSLIKEMPGKngVTVLISSHLLYEIDHLATQVGIITKGKMLFNGSIESLRKKAKHQ-----VAFTT 232
Cdd:PRK14271 189 EPTSALDPTTTEKIEEFIRSLADR--LTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKHAetaryVAGLS 266
|
....*..
gi 1265835877 233 GEIEKSK 239
Cdd:PRK14271 267 GDVKDAK 273
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
13-235 |
1.86e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 88.43 E-value: 1.86e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 13 FKGAEAVNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMK-----PTSGKIELFGERIKNhRQHIQALKKIGSLVESP 87
Cdd:PRK14247 13 FGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElypeaRVSGEVYLDGQDIFK-MDVIELRRRVQMVFQIP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 88 SYYAHLTARENLEVLRKILGVSKN------RVDEVLDIVKLAKEA----NRPVKGFSLGMKQRLGIASALLGNPRLLILD 157
Cdd:PRK14247 92 NPIPNLSIFENVALGLKLNRLVKSkkelqeRVRWALEKAQLWDEVkdrlDAPAGKLSGGQQQRLCIARALAFQPEVLLAD 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 158 EPTNGLDPAGIQEIRSLIKEMpgKNGVTVLISSHLLYEIDHLATQVGIITKGKMLFNGSIESLRKKAKHQVA--FTTGEI 235
Cdd:PRK14247 172 EPTANLDPENTAKIESLFLEL--KKDMTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTNPRHELTekYVTGRL 249
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
2-220 |
2.38e-20 |
|
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: 91.02 E-value: 2.38e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 2 EIVKTTQLIKVFKGAE-----AVNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIE-LFGERI-----KNH 70
Cdd:TIGR03269 278 PIIKVRNVSKRYISVDrgvvkAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNvRVGDEWvdmtkPGP 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 71 RQHIQALKKIGSLVESPSYYAHLTARENL----------EVLR-------KILGVSKNRVDEVLDivKLAKEanrpvkgF 133
Cdd:TIGR03269 358 DGRGRAKRYIGILHQEYDLYPHRTVLDNLteaiglelpdELARmkavitlKMVGFDEEKAEEILD--KYPDE-------L 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 134 SLGMKQRLGIASALLGNPRLLILDEPTNGLDPAGIQEIRSLIKEMPGKNGVTVLISSHLLYEIDHLATQVGIITKGKMLF 213
Cdd:TIGR03269 429 SEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVK 508
|
....*..
gi 1265835877 214 NGSIESL 220
Cdd:TIGR03269 509 IGDPEEI 515
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
15-220 |
2.65e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 88.51 E-value: 2.65e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 15 GAEAVNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELFGERIKNHRQHIQALKKIGSLVESP-SYYAHL 93
Cdd:PRK13644 14 GTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKLQGIRKLVGIVFQNPeTQFVGR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 94 TARENLEVLRKILGVS----KNRVDEVLDIVKLAKEANRPVKGFSLGMKQRLGIASALLGNPRLLILDEPTNGLDPAGIQ 169
Cdd:PRK13644 94 TVEEDLAFGPENLCLPpieiRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGI 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1265835877 170 EIRSLIKEMPGKnGVTVLISSHLLYEIdHLATQVGIITKGKMLFNGSIESL 220
Cdd:PRK13644 174 AVLERIKKLHEK-GKTIVYITHNLEEL-HDADRIIVMDRGKIVLEGEPENV 222
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
15-226 |
8.21e-20 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 85.27 E-value: 8.21e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 15 GAEAVNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLM--KPTSGKIELFGERIKNHRQHIQALKKIGSLVESPSYYAH 92
Cdd:cd03217 12 GKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKGEDITDLPPEERARLGIFLAFQYPPEIPG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 93 LTareNLEVLRKilgvsknrVDEvldivklakeanrpvkGFSLGMKQRLGIASALLGNPRLLILDEPTNGLDPAGIQEIR 172
Cdd:cd03217 92 VK---NADFLRY--------VNE----------------GFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVA 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1265835877 173 SLIKEMpGKNGVTVLISSHLLYEIDHL-ATQVGIITKGKMLFNGSIESLRKKAKH 226
Cdd:cd03217 145 EVINKL-REEGKSVLIITHYQRLLDYIkPDRVHVLYDGRIVKSGDKELALEIEKK 198
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
15-211 |
1.00e-19 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 85.70 E-value: 1.00e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 15 GAEAVNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELFGE---RIKNhRQHIQALKKIGSLVESPSYYA 91
Cdd:PRK10908 14 GRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHditRLKN-REVPFLRRQIGMIFQDHHLLM 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 92 HLTARENLEVLRKILGVS----KNRVDEVLDIVKLAKEA-NRPVKgFSLGMKQRLGIASALLGNPRLLILDEPTNGLDPA 166
Cdd:PRK10908 93 DRTVYDNVAIPLIIAGASgddiRRRVSAALDKVGLLDKAkNFPIQ-LSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDA 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1265835877 167 GIQEIRSLIKEMpGKNGVTVLISSHLLYEIDHLATQVGIITKGKM 211
Cdd:PRK10908 172 LSEGILRLFEEF-NRVGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
15-190 |
1.05e-19 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 88.92 E-value: 1.05e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 15 GAEAVNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELFGE--RIKNHRQHIQAlkKIG---------SL 83
Cdd:COG1129 264 VGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKpvRIRSPRDAIRA--GIAyvpedrkgeGL 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 84 VespsyyAHLTAREN-----LEVLRKILGVSKNRVDEV-------LDIVklAKEANRPVKGFSLGMKQRLGIASALLGNP 151
Cdd:COG1129 342 V------LDLSIRENitlasLDRLSRGGLLDRRRERALaeeyikrLRIK--TPSPEQPVGNLSGGNQQKVVLAKWLATDP 413
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1265835877 152 RLLILDEPTNGLDPAGIQEIRSLIKEMpGKNGVTVL-ISS 190
Cdd:COG1129 414 KVLILDEPTRGIDVGAKAEIYRLIREL-AAEGKAVIvISS 452
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
21-249 |
1.10e-19 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 86.74 E-value: 1.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 21 EVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELFGERIKN-HRQHI-QALKKIGSLVESPSYYAHLTAREN 98
Cdd:PRK11831 25 NISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAmSRSRLyTVRKRMSMLFQSGALFTDMNVFDN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 99 L-----EVLRKILGVSKNRVDEVLDIVKLAKEANRPVKGFSLGMKQRLGIASALLGNPRLLILDEPTNGLDPAGIQEIRS 173
Cdd:PRK11831 105 VayplrEHTQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDPITMGVLVK 184
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1265835877 174 LIKEMPGKNGVTVLISSHLLYEIDHLATQVGIITKGKMLFNGSIESLRKKAKHQV-AFTTGeieksktilLANGFVP 249
Cdd:PRK11831 185 LISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQANPDPRVrQFLDG---------IADGPVP 252
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
12-223 |
1.10e-19 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 89.40 E-value: 1.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 12 VFKGaeavneVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELFGERIKNHrQHIQALKKIGSLVESPSYYA 91
Cdd:TIGR00958 496 VLKG------LTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQY-DHHYLHRQVALVGQEPVLFS 568
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 92 HlTARENLevlrkILGVSKNRVDEVLDIVKLAKeANRPVKGF---------------SLGMKQRLGIASALLGNPRLLIL 156
Cdd:TIGR00958 569 G-SVRENI-----AYGLTDTPDEEIMAAAKAAN-AHDFIMEFpngydtevgekgsqlSGGQKQRIAIARALVRKPRVLIL 641
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1265835877 157 DEPTNGLDpagiQEIRSLIKEMPGKNGVTVLISSHLLYEIDHlATQVGIITKGKMLFNGSIESLRKK 223
Cdd:TIGR00958 642 DEATSALD----AECEQLLQESRSRASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQLMED 703
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
19-200 |
1.10e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 86.63 E-value: 1.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 19 VNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTS-----GKIELFGERIKNHRQHIQALKKIGSLVESPSYYAHL 93
Cdd:PRK14258 23 LEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNIYERRVNLNRLRRQVSMVHPKPNLFPM 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 94 TARENLEVLRKILG-VSKNRVDEVLDIVKLAKEANRPVKG--------FSLGMKQRLGIASALLGNPRLLILDEPTNGLD 164
Cdd:PRK14258 103 SVYDNVAYGVKIVGwRPKLEIDDIVESALKDADLWDEIKHkihksaldLSGGQQQRLCIARALAVKPKVLLMDEPCFGLD 182
|
170 180 190
....*....|....*....|....*....|....*.
gi 1265835877 165 PAGIQEIRSLIKEMPGKNGVTVLISSHLLYEIDHLA 200
Cdd:PRK14258 183 PIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLS 218
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
23-220 |
2.23e-19 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 85.02 E-value: 2.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 23 NLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELFGErikNHRQHIQALKKIGSLVESPSYYAHLTAREN---- 98
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQ---DHTTTPPSRRPVSMLFQENNLFSHLTVAQNiglg 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 99 LEVLRKILGVSKNRVDEVLDIVKLAKEANRPVKGFSLGMKQRLGIASALLGNPRLLILDEPTNGLDPAGIQEIRSLIKEM 178
Cdd:PRK10771 96 LNPGLKLNAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLVSQV 175
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1265835877 179 PGKNGVTVLISSHLLYEIDHLATQVGIITKGKMLFNGSIESL 220
Cdd:PRK10771 176 CQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDEL 217
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
10-193 |
2.85e-19 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 84.90 E-value: 2.85e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 10 IKVFKGaeavneVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELFGERIKNhrQHIQAL-KKIGSLVESPS 88
Cdd:cd03249 16 VPILKG------LSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRD--LNLRWLrSQIGLVSQEPV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 89 YYAhLTARENLEvlrkiLGVSKNRVDEVLD----------IVKLAKEANRPV--KGFSL--GMKQRLGIASALLGNPRLL 154
Cdd:cd03249 88 LFD-GTIAENIR-----YGKPDATDEEVEEaakkanihdfIMSLPDGYDTLVgeRGSQLsgGQKQRIAIARALLRNPKIL 161
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1265835877 155 ILDEPTNGLD---PAGIQEirSLIKEMPGKngvTVLISSHLL 193
Cdd:cd03249 162 LLDEATSALDaesEKLVQE--ALDRAMKGR---TTIVIAHRL 198
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
2-195 |
3.06e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 85.53 E-value: 3.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 2 EIVKTTQLIKVFKGAEAVNEVN---LSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELFGERIKnhRQHIQALK 78
Cdd:PRK13642 3 KILEVENLVFKYEKESDVNQLNgvsFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLT--AENVWNLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 79 -KIGSLVESP-SYYAHLTARENLEVLRKILGVSK----NRVDEVLDIVKLAKEANRPVKGFSLGMKQRLGIASALLGNPR 152
Cdd:PRK13642 81 rKIGMVFQNPdNQFVGATVEDDVAFGMENQGIPReemiKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPE 160
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1265835877 153 LLILDEPTNGLDPAGIQEIRSLIKEMPGKNGVTVLISSHLLYE 195
Cdd:PRK13642 161 IIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDE 203
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
18-223 |
3.31e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 85.62 E-value: 3.31e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 18 AVNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKP--------TSGKIELFGERIKNHRQhiqalkKIGSLVESP-S 88
Cdd:PRK13640 22 ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPddnpnskiTVDGITLTAKTVWDIRE------KVGIVFQNPdN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 89 YYAHLTARENLEVLRKILGVSKNR----VDEVLDIVKLAKEANRPVKGFSLGMKQRLGIASALLGNPRLLILDEPTNGLD 164
Cdd:PRK13640 96 QFVGATVGDDVAFGLENRAVPRPEmikiVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLD 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1265835877 165 PAGIQEIRSLIKEMPGKNGVTVLISSHLLYEIDHlATQVGIITKGKMLFNGSIESLRKK 223
Cdd:PRK13640 176 PAGKEQILKLIRKLKKKNNLTVISITHDIDEANM-ADQVLVLDDGKLLAQGSPVEIFSK 233
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
18-220 |
3.72e-19 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 87.57 E-value: 3.72e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 18 AVNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELFGERIKNHRQhiQALKKIGSLVespSYYAHL---T 94
Cdd:PRK11160 355 VLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSE--AALRQAISVV---SQRVHLfsaT 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 95 ARENLevLRKILGVSKNRVDEVLDIVKLAK-------------EANRPVKGfslGMKQRLGIASALLGNPRLLILDEPTN 161
Cdd:PRK11160 430 LRDNL--LLAAPNASDEALIEVLQQVGLEKlleddkglnawlgEGGRQLSG---GEQRRLGIARALLHDAPLLLLDEPTE 504
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 162 GLDPAGIQEIRSLIKE-MPGKngvTVLISSHLLYEIDHLaTQVGIITKGKMLFNGSIESL 220
Cdd:PRK11160 505 GLDAETERQILELLAEhAQNK---TVLMITHRLTGLEQF-DRICVMDNGQIIEQGTHQEL 560
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
18-216 |
4.06e-19 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 87.01 E-value: 4.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 18 AVNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELFG---ERIKNHRQHIQALKKIGSLVESPSYYAHLT 94
Cdd:PRK10070 43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGvdiAKISDAELREVRRKKIAMVFQSFALMPHMT 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 95 ARENLEVLRKILGV-SKNRVDEVLDIVK---LAKEANRPVKGFSLGMKQRLGIASALLGNPRLLILDEPTNGLDPAGIQE 170
Cdd:PRK10070 123 VLDNTAFGMELAGInAEERREKALDALRqvgLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTE 202
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1265835877 171 IRSLIKEMPGKNGVTVLISSHLLYEIDHLATQVGIITKGKMLFNGS 216
Cdd:PRK10070 203 MQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGT 248
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
17-211 |
4.38e-19 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 87.41 E-value: 4.38e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 17 EAVNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELFGERIkNHRQHIQALKK-----------IGSLVE 85
Cdd:PRK15439 277 EGFRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEI-NALSTAQRLARglvylpedrqsSGLYLD 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 86 SP------SYYAHL------TAREN--LEVLRKILGVSKNrvdevldivklakEANRPVKGFSLGMKQRLGIASALLGNP 151
Cdd:PRK15439 356 APlawnvcALTHNRrgfwikPARENavLERYRRALNIKFN-------------HAEQAARTLSGGNQQKVLIAKCLEASP 422
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 152 RLLILDEPTNGLDPAGIQEIRSLIKEMPGKNGVTVLISSHlLYEIDHLATQVGIITKGKM 211
Cdd:PRK15439 423 QLLIVDEPTRGVDVSARNDIYQLIRSIAAQNVAVLFISSD-LEEIEQMADRVLVMHQGEI 481
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
18-215 |
7.19e-19 |
|
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: 82.36 E-value: 7.19e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 18 AVNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELFGERIKNHRQHIQalKKIGSLVESPSYYAHlTARE 97
Cdd:cd03247 17 VLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALS--SLISVLNQRPYLFDT-TLRN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 98 NLEvlrkilgvsknrvdevldivklakeanrpvKGFSLGMKQRLGIASALLGNPRLLILDEPTNGLDPAGIQEIRSLI-K 176
Cdd:cd03247 94 NLG------------------------------RRFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQLLSLIfE 143
|
170 180 190
....*....|....*....|....*....|....*....
gi 1265835877 177 EMPGKngvTVLISSHLLYEIDHlATQVGIITKGKMLFNG 215
Cdd:cd03247 144 VLKDK---TLIWITHHLTGIEH-MDKILFLENGKIIMQG 178
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-164 |
9.38e-19 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 85.66 E-value: 9.38e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 1 MEIVKTTQLIKVFKGAEAVNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELFGERIKNhRQHIQALKKI 80
Cdd:PRK09536 1 MPMIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEA-LSARAASRRV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 81 GSLVESPSYYAHLTARENLEVLR--------KILGVSKNRVDEVLDIVKLAKEANRPVKGFSLGMKQRLGIASALLGNPR 152
Cdd:PRK09536 80 ASVPQDTSLSFEFDVRQVVEMGRtphrsrfdTWTETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATP 159
|
170
....*....|..
gi 1265835877 153 LLILDEPTNGLD 164
Cdd:PRK09536 160 VLLLDEPTASLD 171
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
19-216 |
1.21e-18 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 83.52 E-value: 1.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 19 VNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELFGERIKNH--RQHIQALK------------KIGSLV 84
Cdd:PRK11231 18 LNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLssRQLARRLAllpqhhltpegiTVRELV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 85 E---SP--SYYAHLTAREnlevlrkilgvsKNRVDEVLDIVKLAKEANRPVKGFSLGMKQRLGIASALLGNPRLLILDEP 159
Cdd:PRK11231 98 AygrSPwlSLWGRLSAED------------NARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEP 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1265835877 160 TNGLDPAGIQEIRSLIKEM--PGKNGVTVLissHLLYE----IDHLAtqvgIITKGKMLFNGS 216
Cdd:PRK11231 166 TTYLDINHQVELMRLMRELntQGKTVVTVL---HDLNQasryCDHLV----VLANGHVMAQGT 221
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
22-211 |
1.41e-18 |
|
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: 82.52 E-value: 1.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 22 VNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELFGERIKNHrQHIQALKKIGSLVESPSYYAHlTARENLEV 101
Cdd:cd03248 33 VSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQY-EHKYLHSKVSLVGQEPVLFAR-SLQDNIAY 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 102 lrKILGVSKNRVDEVLD-------IVKLAKEANRPV--KG--FSLGMKQRLGIASALLGNPRLLILDEPTNGLDPAGIQE 170
Cdd:cd03248 111 --GLQSCSFECVKEAAQkahahsfISELASGYDTEVgeKGsqLSGGQKQRVAIARALIRNPQVLILDEATSALDAESEQQ 188
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1265835877 171 IRSLIKEMPGKNgvTVLISSHLLYEIDHlATQVGIITKGKM 211
Cdd:cd03248 189 VQQALYDWPERR--TVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
19-166 |
1.71e-18 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 83.24 E-value: 1.71e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 19 VNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELFGERIKNH------------RQHiqalkkigSLVES 86
Cdd:COG4559 17 LDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWspwelarrravlPQH--------SSLAF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 87 PsyyahLTARenlEVLRkiLGVS---------KNRVDEVLDIVKLAKEANRPVKGFSLGMKQRLGIASALL-------GN 150
Cdd:COG4559 89 P-----FTVE---EVVA--LGRAphgssaaqdRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLAqlwepvdGG 158
|
170
....*....|....*.
gi 1265835877 151 PRLLILDEPTNGLDPA 166
Cdd:COG4559 159 PRWLFLDEPTSALDLA 174
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
18-227 |
2.06e-18 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 85.53 E-value: 2.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 18 AVNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMkPTSGKIELFGERIK--NHRQHIQALKKIGSLVESPsyYAHLTA 95
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLI-NSQGEIWFDGQPLHnlNRRQLLPVRHRIQVVFQDP--NSSLNP 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 96 R--------ENLEVLRKILGVSK--NRVDEVLDIVKLAKEA-NRPVKGFSLGMKQRLGIASALLGNPRLLILDEPTNGLD 164
Cdd:PRK15134 378 RlnvlqiieEGLRVHQPTLSAAQreQQVIAVMEEVGLDPETrHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLD 457
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1265835877 165 PAGIQEIRSLIKEMPGKNGVTVLISSHLLYEIDHLATQVGIITKGKMLFNGSIESLRKKAKHQ 227
Cdd:PRK15134 458 KTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERVFAAPQQE 520
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
18-193 |
2.99e-18 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 83.62 E-value: 2.99e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 18 AVNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKP---TSGKIELFGERIKNHRQH----IQAlKKIGSLVESP--S 88
Cdd:PRK09473 31 AVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAAngrIGGSATFNGREILNLPEKelnkLRA-EQISMIFQDPmtS 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 89 YYAHLTARENL-EVLRKILGVSKNRVDE----VLDIVKLAkEANRPVK----GFSLGMKQRLGIASALLGNPRLLILDEP 159
Cdd:PRK09473 110 LNPYMRVGEQLmEVLMLHKGMSKAEAFEesvrMLDAVKMP-EARKRMKmyphEFSGGMRQRVMIAMALLCRPKLLIADEP 188
|
170 180 190
....*....|....*....|....*....|....
gi 1265835877 160 TNGLDPAGIQEIRSLIKEMPGKNGVTVLISSHLL 193
Cdd:PRK09473 189 TTALDVTVQAQIMTLLNELKREFNTAIIMITHDL 222
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
14-211 |
3.48e-18 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 84.69 E-value: 3.48e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 14 KGAEAVNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELFGERIKNH--RQHIQAlkKIGSLVESPSYYA 91
Cdd:COG3845 269 RGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLspRERRRL--GVAYIPEDRLGRG 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 92 ---HLTARENLeVLRKI--LGVSKNRvdeVLD---IVKLAKE-----------ANRPVKGFSLGMKQRLGIASALLGNPR 152
Cdd:COG3845 347 lvpDMSVAENL-ILGRYrrPPFSRGG---FLDrkaIRAFAEElieefdvrtpgPDTPARSLSGGNQQKVILARELSRDPK 422
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1265835877 153 LLILDEPTNGLDPAGIQEIRSLIKEMpGKNGVTVLISSHLLYEIDHLATQVGIITKGKM 211
Cdd:COG3845 423 LLIAAQPTRGLDVGAIEFIHQRLLEL-RDAGAAVLLISEDLDEILALSDRIAVMYEGRI 480
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
7-220 |
4.59e-18 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 81.94 E-value: 4.59e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 7 TQLIKVFKGAEAVNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELFGERIKNHR-----------QHIQ 75
Cdd:PRK10619 9 IDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRdkdgqlkvadkNQLR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 76 ALKKIGSLV-ESPSYYAHLTAREN-LEVLRKILGVSK----NRVDEVLDIVKLAKEANR--PVKgFSLGMKQRLGIASAL 147
Cdd:PRK10619 89 LLRTRLTMVfQHFNLWSHMTVLENvMEAPIQVLGLSKqearERAVKYLAKVGIDERAQGkyPVH-LSGGQQQRVSIARAL 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1265835877 148 LGNPRLLILDEPTNGLDPAGIQEIRSLIKEMpGKNGVTVLISSHLLYEIDHLATQVGIITKGKMLFNGSIESL 220
Cdd:PRK10619 168 AMEPEVLLFDEPTSALDPELVGEVLRIMQQL-AEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQL 239
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
11-210 |
6.00e-18 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 83.81 E-value: 6.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 11 KVFKGAEAVNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELFGE--RIKNHRQHIQAlkKIGSLVESPS 88
Cdd:PRK11288 12 KTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQemRFASTTAALAA--GVAIIYQELH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 89 YYAHLTARENLevlrkILGVSKNRVDeVLDIVKLAKEA-------------NRPVKGFSLGMKQRLGIASALLGNPRLLI 155
Cdd:PRK11288 90 LVPEMTVAENL-----YLGQLPHKGG-IVNRRLLNYEAreqlehlgvdidpDTPLKYLSIGQRQMVEIAKALARNARVIA 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1265835877 156 LDEPTNGLDPAGIQEIRSLIKEMPgKNGVTVLISSHLLYEIDHLATQVGIITKGK 210
Cdd:PRK11288 164 FDEPTSSLSAREIEQLFRVIRELR-AEGRVILYVSHRMEEIFALCDAITVFKDGR 217
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
22-218 |
6.32e-18 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 81.27 E-value: 6.32e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 22 VNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMK--PTSGKIELFGERIKNHRQHIQALKKIG----SLVESP----SYYA 91
Cdd:COG0396 19 VNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPKyeVTSGSILLDGEDILELSPDERARAGIFlafqYPVEIPgvsvSNFL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 92 HLTARENLEVLRKILGVSKnRVDEVLDIVKLAKE-ANRPV-KGFSLGMKQRLGIASALLGNPRLLILDEPTNGLDPAGIQ 169
Cdd:COG0396 99 RTALNARRGEELSAREFLK-LLKEKMKELGLDEDfLDRYVnEGFSGGEKKRNEILQMLLLEPKLAILDETDSGLDIDALR 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1265835877 170 EIRSLIKEMPGKNGvTVLISSHLLYEIDHL-ATQVGIITKGKMLFNGSIE 218
Cdd:COG0396 178 IVAEGVNKLRSPDR-GILIITHYQRILDYIkPDFVHVLVDGRIVKSGGKE 226
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
11-210 |
6.46e-18 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 81.65 E-value: 6.46e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 11 KVFKGAEAVNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIelfgeriknhrqhiqaLKKIGSLVEspsyy 90
Cdd:PRK11247 20 KRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL----------------LAGTAPLAE----- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 91 ahltARENLEVL---------RKI-----LGVSKN---RVDEVLDIVKLAKEANRPVKGFSLGMKQRLGIASALLGNPRL 153
Cdd:PRK11247 79 ----AREDTRLMfqdarllpwKKVidnvgLGLKGQwrdAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1265835877 154 LILDEPTNGLDPAGIQEIRSLIKEMPGKNGVTVLISSHLLYEIDHLATQVGIITKGK 210
Cdd:PRK11247 155 LLLDEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGK 211
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
15-216 |
6.74e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 82.09 E-value: 6.74e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 15 GAEAVNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELfGERI---KNHRQHIQAL-KKIGSLVESP-SY 89
Cdd:PRK13643 18 ASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTV-GDIVvssTSKQKEIKPVrKKVGVVFQFPeSQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 90 YAHLTARENLEVLRKILGVSKNRVDEV----LDIVKLAKE--ANRPVKgFSLGMKQRLGIASALLGNPRLLILDEPTNGL 163
Cdd:PRK13643 97 LFEETVLKDVAFGPQNFGIPKEKAEKIaaekLEMVGLADEfwEKSPFE-LSGGQMRRVAIAGILAMEPEVLVLDEPTAGL 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1265835877 164 DPAGIQEIRSLIKEMpGKNGVTVLISSHLLYEIDHLATQVGIITKGKMLFNGS 216
Cdd:PRK13643 176 DPKARIEMMQLFESI-HQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGT 227
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
17-203 |
8.07e-18 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 80.63 E-value: 8.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 17 EAVNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELFGERIKNHRQHIQAL---KKIGSLVESPSYYAHL 93
Cdd:PRK11629 23 DVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAElrnQKLGFIYQFHHLLPDF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 94 TARENLEVLRKILGV----SKNRVDEVLDIVKLAKEANRPVKGFSLGMKQRLGIASALLGNPRLLILDEPTNGLDPAGIQ 169
Cdd:PRK11629 103 TALENVAMPLLIGKKkpaeINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNAD 182
|
170 180 190
....*....|....*....|....*....|....
gi 1265835877 170 EIRSLIKEMPGKNGVTVLISSHLLYEIDHLATQV 203
Cdd:PRK11629 183 SIFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQL 216
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
11-224 |
9.38e-18 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 83.30 E-value: 9.38e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 11 KVFKGAEAVNEVNLSIKEGEIYGFLGPNGAGKTTtirmllgLMKPTSG---------KIELFGERIKNHrqHIQALKKIG 81
Cdd:NF040905 9 KTFPGVKALDDVNLSVREGEIHALCGENGAGKST-------LMKVLSGvyphgsyegEILFDGEVCRFK--DIRDSEALG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 82 ------SLVESPsyyaHLTARENL----EVLRKilGV-----SKNRVDEVLDIVKLAKEANRPVKGFSLGMKQRLGIASA 146
Cdd:NF040905 80 iviihqELALIP----YLSIAENIflgnERAKR--GVidwneTNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1265835877 147 LLGNPRLLILDEPTNGLDPAGIQEIRSLIKEMPGKnGVTVLISSHLLYEIDHLATQVGIITKGKmlfngSIESLRKKA 224
Cdd:NF040905 154 LSKDVKLLILDEPTAALNEEDSAALLDLLLELKAQ-GITSIIISHKLNEIRRVADSITVLRDGR-----TIETLDCRA 225
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
18-216 |
1.72e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 81.44 E-value: 1.72e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 18 AVNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIEL----FGERIKNHRQHIQALKK-----------IGS 82
Cdd:PRK13631 41 ALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVgdiyIGDKKNNHELITNPYSKkiknfkelrrrVSM 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 83 LVESPSYYAHLTARENLEVLRKI-LGVSKNRVDEV----LDIVKLAKE-ANRPVKGFSLGMKQRLGIASALLGNPRLLIL 156
Cdd:PRK13631 121 VFQFPEYQLFKDTIEKDIMFGPVaLGVKKSEAKKLakfyLNKMGLDDSyLERSPFGLSGGQKRRVAIAGILAIQPEILIF 200
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 157 DEPTNGLDPAGIQEIRSLIKEMPgKNGVTVLISSHLLYEIDHLATQVGIITKGKMLFNGS 216
Cdd:PRK13631 201 DEPTAGLDPKGEHEMMQLILDAK-ANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTGT 259
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
4-252 |
1.83e-17 |
|
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: 82.54 E-value: 1.83e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 4 VKTTQLIKVFKGAEAVNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGL--MKPTSGKI----------------ELFGE 65
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIiyhvalcekcgyverpSKVGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 66 RI------------------KNHRQHIQalKKIGSLVESP-SYYAHLTAREN-LEVLRKILGVSKNRVDEVLDIVKLAKE 125
Cdd:TIGR03269 81 PCpvcggtlepeevdfwnlsDKLRRRIR--KRIAIMLQRTfALYGDDTVLDNvLEALEEIGYEGKEAVGRAVDLIEMVQL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 126 ANRPV---KGFSLGMKQRLGIASALLGNPRLLILDEPTNGLDPAGIQEIRSLIKEMPGKNGVTVLISSHLLYEIDHLATQ 202
Cdd:TIGR03269 159 SHRIThiaRDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDLSDK 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1265835877 203 VGIITKGKMLFNGSIESLRKKAKHQVAfttgEIEKSKTILLANGFVPTID 252
Cdd:TIGR03269 239 AIWLENGEIKEEGTPDEVVAVFMEGVS----EVEKECEVEVGEPIIKVRN 284
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
11-222 |
2.17e-17 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 82.41 E-value: 2.17e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 11 KVFKGAEAVNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELFGERIkNHRQHIQALKKIGSLV-ESPSY 89
Cdd:PRK15439 19 KQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPC-ARLTPAKAHQLGIYLVpQEPLL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 90 YAHLTARENLevlrkILGVSKNRVDE--VLDIVK-LAKEANRPVKGFSLGM--KQRLGIASALLGNPRLLILDEPTNGLD 164
Cdd:PRK15439 98 FPNLSVKENI-----LFGLPKRQASMqkMKQLLAaLGCQLDLDSSAGSLEVadRQIVEILRGLMRDSRILILDEPTASLT 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1265835877 165 PAGI----QEIRSLIKEmpgknGVTVLISSHLLYEIDHLATQVGIITKGKMLFNGSIESLRK 222
Cdd:PRK15439 173 PAETerlfSRIRELLAQ-----GVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTADLST 229
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
19-191 |
2.25e-17 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 78.84 E-value: 2.25e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 19 VNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELFGERIKNHRQHIQalKKIGSLVESPSYYAHLTAREN 98
Cdd:PRK13540 17 LQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQ--KQLCFVGHRSGINPYLTLREN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 99 leVLRKILGVSKN-RVDEVLDIVKLAKEANRPVKGFSLGMKQRLGIASALLGNPRLLILDEPTNGLDPAGIQEIRSLIKE 177
Cdd:PRK13540 95 --CLYDIHFSPGAvGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTIITKIQE 172
|
170
....*....|....
gi 1265835877 178 MPGKNGvTVLISSH 191
Cdd:PRK13540 173 HRAKGG-AVLLTSH 185
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
17-188 |
2.41e-17 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 79.54 E-value: 2.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 17 EAVNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELFGERIKNHRQHIQALKKIGSLVESPSYYAHLTAR 96
Cdd:PRK11614 19 QALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMREAVAIVPEGRRVFSRMTVE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 97 ENLE-----VLRKILgvsKNRVDEVLDIV-KLAKEANRPVKGFSLGMKQRLGIASALLGNPRLLILDEPTNGLDPAGIQE 170
Cdd:PRK11614 99 ENLAmggffAERDQF---QERIKWVYELFpRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPIIIQQ 175
|
170
....*....|....*...
gi 1265835877 171 IRSLIKEMPgKNGVTVLI 188
Cdd:PRK11614 176 IFDTIEQLR-EQGMTIFL 192
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
14-220 |
2.71e-17 |
|
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: 79.20 E-value: 2.71e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 14 KGAEAVNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELFGERIKNHRqhIQALKKIGSLVESPSYYAHL 93
Cdd:cd03251 13 DGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYT--LASLRRQIGLVSQDVFLFND 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 94 TARENLEVLRkiLGVSKNRVDEVldivklAKEAN------------------RPVKgFSLGMKQRLGIASALLGNPRLLI 155
Cdd:cd03251 91 TVAENIAYGR--PGATREEVEEA------ARAANahefimelpegydtvigeRGVK-LSGGQRQRIAIARALLKDPPILI 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1265835877 156 LDEPTNGLD---PAGIQEirSLIKEMPGKngvTVLISSHLLYEIDHlATQVGIITKGKMLFNGSIESL 220
Cdd:cd03251 162 LDEATSALDtesERLVQA--ALERLMKNR---TTFVIAHRLSTIEN-ADRIVVLEDGKIVERGTHEEL 223
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
11-210 |
2.82e-17 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 81.90 E-value: 2.82e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 11 KVFKGAEAVNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMkPT---SGKIELFGERIKNHrqHIQALKKIGSLVesp 87
Cdd:PRK13549 13 KTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PHgtyEGEIIFEGEELQAS--NIRDTERAGIAI--- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 88 sYYAHLTARENLEVLRKI-LG--VSKN----------RVDEVLDIVKLAKEANRPVKGFSLGMKQRLGIASALLGNPRLL 154
Cdd:PRK13549 87 -IHQELALVKELSVLENIfLGneITPGgimdydamylRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQARLL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1265835877 155 ILDEPTNGLDPAGIQEIRSLIKEMPgKNGVTVLISSHLLYEIDHLATQVGIITKGK 210
Cdd:PRK13549 166 ILDEPTASLTESETAVLLDIIRDLK-AHGIACIYISHKLNEVKAISDTICVIRDGR 220
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
26-215 |
2.84e-17 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 82.16 E-value: 2.84e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 26 IKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIElFGERIKNHRQHIQA---------LKKIGSLVESpSYYahltar 96
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVD-PELKISYKPQYIKPdydgtvedlLRSITDDLGS-SYY------ 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 97 eNLEVLRKIlgvsknRVDEVLDivklakeanRPVKGFSLGMKQRLGIASALLGNPRLLILDEPTNGLDpagIQE------ 170
Cdd:PRK13409 434 -KSEIIKPL------QLERLLD---------KNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD---VEQrlavak 494
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1265835877 171 -IRSLIKEmpgkNGVTVLISSHLLYEIDHLATQVgiitkgkMLFNG 215
Cdd:PRK13409 495 aIRRIAEE----REATALVVDHDIYMIDYISDRL-------MVFEG 529
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
26-194 |
3.43e-17 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 78.74 E-value: 3.43e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 26 IKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELFGERIKN--HRQHIQALKKIGSLvespsyYAHLTARENLEVLR 103
Cdd:PRK13543 34 VDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRgdRSRFMAYLGHLPGL------KADLSTLENLHFLC 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 104 KILGVSKNRV-DEVLDIVKLAKEANRPVKGFSLGMKQRLGIASALLGNPRLLILDEPTNGLDPAGIQEIRSLIKEMPGKN 182
Cdd:PRK13543 108 GLHGRRAKQMpGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEGITLVNRMISAHLRGG 187
|
170
....*....|..
gi 1265835877 183 GVTvLISSHLLY 194
Cdd:PRK13543 188 GAA-LVTTHGAY 198
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
22-220 |
5.98e-17 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 79.06 E-value: 5.98e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 22 VNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELFGERIKNHRQHIQAlKKIGSLVESPSYYAHLTARENLEV 101
Cdd:PRK10575 30 LSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFA-RKVAYLPQQLPAAEGMTVRELVAI 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 102 LR----KILG----VSKNRVDEVLDIVKLAKEANRPVKGFSLGMKQRLGIASALLGNPRLLILDEPTNGLDPAGIQEIRS 173
Cdd:PRK10575 109 GRypwhGALGrfgaADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLA 188
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1265835877 174 LIKEMPGKNGVTVLIsshLLYEI-------DHLATQVGiitkGKMLFNGSIESL 220
Cdd:PRK10575 189 LVHRLSQERGLTVIA---VLHDInmaarycDYLVALRG----GEMIAQGTPAEL 235
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
20-191 |
7.25e-17 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 77.69 E-value: 7.25e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 20 NEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMK--PTSGKIELFGERIKNHRQHIQALKKIGSLVEspsyyahltare 97
Cdd:COG2401 47 RDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKgtPVAGCVDVPDNQFGREASLIDAIGRKGDFKD------------ 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 98 nlevlrkilgvsknrVDEVLDIVKLAKEAN--RPVKGFSLGMKQRLGIASALLGNPRLLILDEPTNGLDPAGIQEIRSLI 175
Cdd:COG2401 115 ---------------AVELLNAVGLSDAVLwlRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVARNL 179
|
170
....*....|....*.
gi 1265835877 176 KEMPGKNGVTVLISSH 191
Cdd:COG2401 180 QKLARRAGITLVVATH 195
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
19-215 |
7.34e-17 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 81.08 E-value: 7.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 19 VNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSgkieLFGERIKNHRQHI-QALKKIGSLVESPSYYAHLTARE 97
Cdd:PLN03211 84 LNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNN----FTGTILANNRKPTkQILKRTGFVTQDDILYPHLTVRE 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 98 NL---EVLRKILGVSKNR----VDEVLDIVKLAKEANRPV-----KGFSLGMKQRLGIASALLGNPRLLILDEPTNGLDP 165
Cdd:PLN03211 160 TLvfcSLLRLPKSLTKQEkilvAESVISELGLTKCENTIIgnsfiRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDA 239
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1265835877 166 AGIQEIRSLIKEMPGKnGVTVLISSHL----LYEIDHlatQVGIITKGKMLFNG 215
Cdd:PLN03211 240 TAAYRLVLTLGSLAQK-GKTIVTSMHQpssrVYQMFD---SVLVLSEGRCLFFG 289
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
15-220 |
8.38e-17 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 77.91 E-value: 8.38e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 15 GAEAVNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELFGeriknhrqHIQAL-------KKIGSLVESP 87
Cdd:cd03252 14 GPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDG--------HDLALadpawlrRQVGVVLQEN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 88 SYYAHlTARENLEVLRKilGVSKNRVDEVLD-------IVKLAKEANRPV----KGFSLGMKQRLGIASALLGNPRLLIL 156
Cdd:cd03252 86 VLFNR-SIRDNIALADP--GMSMERVIEAAKlagahdfISELPEGYDTIVgeqgAGLSGGQRQRIAIARALIHNPRILIF 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1265835877 157 DEPTNGLDpagIQEIRSLIKEMPG-KNGVTVLISSHLLYEIDHlATQVGIITKGKMLFNGSIESL 220
Cdd:cd03252 163 DEATSALD---YESEHAIMRNMHDiCAGRTVIIIAHRLSTVKN-ADRIIVMEKGRIVEQGSHDEL 223
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
17-216 |
1.76e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 78.13 E-value: 1.76e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 17 EAVNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELFGERIKNHRQHIQALKK----IGSLVESPSYYAH 92
Cdd:PRK13645 25 KALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPANLKKIKEVKRlrkeIGLVFQFPEYQLF 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 93 LTARENLEVLRKI-LGVSKN----RVDEVLDIVKLAKE-ANRPVKGFSLGMKQRLGIASALLGNPRLLILDEPTNGLDPA 166
Cdd:PRK13645 105 QETIEKDIAFGPVnLGENKQeaykKVPELLKLVQLPEDyVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPK 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1265835877 167 GIQEIRSLIKEMPGKNGVTVLISSHLLYEIDHLATQVGIITKGKMLFNGS 216
Cdd:PRK13645 185 GEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGS 234
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
25-215 |
2.51e-16 |
|
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: 79.06 E-value: 2.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 25 SIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIElFGERIKNHRQHIqalkkigslveSPSYyaHLTARENLE-VLR 103
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVD-EDLKISYKPQYI-----------SPDY--DGTVEEFLRsANT 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 104 KILGVSKNRVdEVLDIVKLAKEANRPVKGFSLGMKQRLGIASALLGNPRLLILDEPTNGLDPAGIQEIRSLIKEMPGKNG 183
Cdd:COG1245 428 DDFGSSYYKT-EIIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAENRG 506
|
170 180 190
....*....|....*....|....*....|..
gi 1265835877 184 VTVLISSHLLYEIDHLATQVgiitkgkMLFNG 215
Cdd:COG1245 507 KTAMVVDHDIYLIDYISDRL-------MVFEG 531
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
19-229 |
2.76e-16 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 77.05 E-value: 2.76e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 19 VNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKP----TSGKIELFGERIknhrqHIQAL--KKIGSLVESP----- 87
Cdd:PRK10418 19 VHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGRVLLDGKPV-----APCALrgRKIATIMQNPrsafn 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 88 ---SYYAHltARENLEVLRKIlgVSKNRVDEVLDIVKLAkEANRPVKGF----SLGMKQRLGIASALLGNPRLLILDEPT 160
Cdd:PRK10418 94 plhTMHTH--ARETCLALGKP--ADDATLTAALEAVGLE-NAARVLKLYpfemSGGMLQRMMIALALLCEAPFIIADEPT 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1265835877 161 NGLDPAGIQEIRSLIKEMPGKNGVTVLISSHLLYEIDHLATQVGIITKGKMLFNGSIESLRKKAKHQVA 229
Cdd:PRK10418 169 TDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPKHAVT 237
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
15-220 |
2.92e-16 |
|
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: 79.01 E-value: 2.92e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 15 GAEAVNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELFGERIKNHRQHIqaLKKIGSLVESPSYYAHLT 94
Cdd:TIGR01193 486 GSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHT--LRQFINYLPQEPYIFSGS 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 95 ARENLeVLRKILGVSKNRVDEVLDIVKLAKEANRPVKGF-----------SLGMKQRLGIASALLGNPRLLILDEPTNGL 163
Cdd:TIGR01193 564 ILENL-LLGAKENVSQDEIWAACEIAEIKDDIENMPLGYqtelseegssiSGGQKQRIALARALLTDSKVLILDESTSNL 642
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1265835877 164 DPAGIQEIRSLIKEMPGKngvTVLISSHLLyEIDHLATQVGIITKGKMLFNGSIESL 220
Cdd:TIGR01193 643 DTITEKKIVNNLLNLQDK---TIIFVAHRL-SVAKQSDKIIVLDHGKIIEQGSHDEL 695
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
15-220 |
4.50e-16 |
|
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: 78.60 E-value: 4.50e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 15 GAEAVNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELFGERIKNHRqhIQALKKIGSLVespSYYAHL- 93
Cdd:TIGR02203 344 DRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYT--LASLRRQVALV---SQDVVLf 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 94 --TARENLEVLRKiLGVSKNRVDEVLDIVKLAKEANRPVKGF-----------SLGMKQRLGIASALLGNPRLLILDEPT 160
Cdd:TIGR02203 419 ndTIANNIAYGRT-EQADRAEIERALAAAYAQDFVDKLPLGLdtpigengvllSGGQRQRLAIARALLKDAPILILDEAT 497
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1265835877 161 NGLDPAGIQEIR-SLIKEMPGKngvTVLISSHLLYEIDHlATQVGIITKGKMLFNGSIESL 220
Cdd:TIGR02203 498 SALDNESERLVQaALERLMQGR---TTLVIAHRLSTIEK-ADRIVVMDDGRIVERGTHNEL 554
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
9-210 |
6.08e-16 |
|
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: 77.94 E-value: 6.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 9 LIKVFKGAEAVNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMK--PTSGKIELFGERIKnhRQHIQALKKIGSLVes 86
Cdd:TIGR02633 7 IVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPhgTWDGEIYWSGSPLK--ASNIRDTERAGIVI-- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 87 psYYAHLTARENLEVLRKIL--------GVSKN------RVDEVLDIVKL-AKEANRPVKGFSLGMKQRLGIASALLGNP 151
Cdd:TIGR02633 83 --IHQELTLVPELSVAENIFlgneitlpGGRMAynamylRAKNLLRELQLdADNVTRPVGDYGGGQQQLVEIAKALNKQA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1265835877 152 RLLILDEPTNGLDPAGIQEIRSLIKEMPGKNGVTVLIsSHLLYEIDHLATQVGIITKGK 210
Cdd:TIGR02633 161 RLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYI-SHKLNEVKAVCDTICVIRDGQ 218
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
19-215 |
6.76e-16 |
|
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: 74.61 E-value: 6.76e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 19 VNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLmkpTSGKIELFGE-RIKNHRQHIQALKKIGSLV---ESPSYYAHLT 94
Cdd:cd03233 23 LKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANR---TEGNVSVEGDiHYNGIPYKEFAEKYPGEIIyvsEEDVHFPTLT 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 95 ARENLEVLRKILGvsknrvdevldivklakeaNRPVKGFSLGMKQRLGIASALLGNPRLLILDEPTNGLDPAGIQEIRSL 174
Cdd:cd03233 100 VRETLDFALRCKG-------------------NEFVRGISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTALEILKC 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1265835877 175 IKEMPGKNGVTVLISshlLY----EIDHLATQVGIITKGKMLFNG 215
Cdd:cd03233 161 IRTMADVLKTTTFVS---LYqasdEIYDLFDKVLVLYEGRQIYYG 202
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
15-223 |
8.73e-16 |
|
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: 74.96 E-value: 8.73e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 15 GAEAVNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELFGERIKNHRQHiqAL-KKIGsLVESPSYYAHL 93
Cdd:cd03253 13 GRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLD--SLrRAIG-VVPQDTVLFND 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 94 TARENLEVLRkiLGVSKNRVDEVLDIVKLAKEANRPVKGF-----------SLGMKQRLGIASALLGNPRLLILDEPTNG 162
Cdd:cd03253 90 TIGYNIRYGR--PDATDEEVIEAAKAAQIHDKIMRFPDGYdtivgerglklSGGEKQRVAIARAILKNPPILLLDEATSA 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1265835877 163 LDPAGIQEI-RSLIKEMPGKngvTVLISSHLLYEIDHlATQVGIITKGKMLFNGSIESLRKK 223
Cdd:cd03253 168 LDTHTEREIqAALRDVSKGR---TTIVIAHRLSTIVN-ADKIIVLKDGRIVERGTHEELLAK 225
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
19-190 |
9.72e-16 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 77.35 E-value: 9.72e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 19 VNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELFGERIKNHRQH---------IQALKKIGSLVESpsy 89
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQdglangivyISEDRKRDGLVLG--- 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 90 yahLTAREN--LEVLRKI--LGVSKNRVDEVL---DIVKL--AKEANR--PVKGFSLGMKQRLGIASALLGNPRLLILDE 158
Cdd:PRK10762 345 ---MSVKENmsLTALRYFsrAGGSLKHADEQQavsDFIRLfnIKTPSMeqAIGLLSGGNQQKVAIARGLMTRPKVLILDE 421
|
170 180 190
....*....|....*....|....*....|..
gi 1265835877 159 PTNGLDPAGIQEIRSLIKEMPGKNGVTVLISS 190
Cdd:PRK10762 422 PTRGVDVGAKKEIYQLINQFKAEGLSIILVSS 453
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
22-216 |
1.04e-15 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 75.41 E-value: 1.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 22 VNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELFGERIKNHRQHiQALKKIGSLVESPSYYAHLTARE---- 97
Cdd:PRK10253 26 LTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASK-EVARRIGLLAQNATTPGDITVQElvar 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 98 ----NLEVLRKILGVSKNRVDEVLDIVKLAKEANRPVKGFSLGMKQRLGIASALLGNPRLLILDEPTNGLDPAGIQEIRS 173
Cdd:PRK10253 105 grypHQPLFTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLE 184
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1265835877 174 LIKEMPGKNGVTVLISSHLLYEIDHLATQVGIITKGKMLFNGS 216
Cdd:PRK10253 185 LLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGA 227
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
18-202 |
1.14e-15 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 77.24 E-value: 1.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 18 AVNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELFGEriknhrqhiQALKKIGSLVESpsyyaHLTARE 97
Cdd:PRK13545 39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGS---------AALIAISSGLNG-----QLTGIE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 98 NLEVLRKILGVSKNRVDE----VLDIVKLAKEANRPVKGFSLGMKQRLGIASALLGNPRLLILDEPTNGLDPAGIQEIRS 173
Cdd:PRK13545 105 NIELKGLMMGLTKEKIKEiipeIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKCLD 184
|
170 180
....*....|....*....|....*....
gi 1265835877 174 LIKEMPgKNGVTVLISSHLLYEIDHLATQ 202
Cdd:PRK13545 185 KMNEFK-EQGKTIFFISHSLSQVKSFCTK 212
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
18-203 |
1.17e-15 |
|
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: 74.78 E-value: 1.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 18 AVNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELfgerikNHRqhiqalkkiGSLVEspsyYAHLTARE 97
Cdd:COG4778 26 VLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILV------RHD---------GGWVD----LAQASPRE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 98 NLEVLRKILG-VSK-----NRVdEVLDIVKL--------AKEANRPVKG------------------FSLGMKQRLGIAS 145
Cdd:COG4778 87 ILALRRRTIGyVSQflrviPRV-SALDVVAEpllergvdREEARARAREllarlnlperlwdlppatFSGGEQQRVNIAR 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1265835877 146 ALLGNPRLLILDEPTNGLDPAGIQEIRSLIKEMPgKNGVTVLISSHLLYEIDHLATQV 203
Cdd:COG4778 166 GFIADPPLLLLDEPTASLDAANRAVVVELIEEAK-ARGTAIIGIFHDEEVREAVADRV 222
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
22-218 |
1.48e-15 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 74.88 E-value: 1.48e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 22 VNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMkPTSGKIELFGERIKN--------HR----QHIQALKKIgslvesPSY 89
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGRPLSDwsaaelarHRaylsQQQSPPFAM------PVF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 90 -YAHLTARENLEVlrkilGVSKNRVDEVLDIVKLAKEANRPVKGFSLGMKQRLGIASALL-----GNP--RLLILDEPTN 161
Cdd:COG4138 88 qYLALHQPAGASS-----EAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLqvwptINPegQLLLLDEPMN 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1265835877 162 GLDPAgiQEIR--SLIKEMPGKnGVTVLISSHLLYEIDHLATQVGIITKGKMLFNGSIE 218
Cdd:COG4138 163 SLDVA--QQAAldRLLRELCQQ-GITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETA 218
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
17-226 |
1.50e-15 |
|
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: 76.65 E-value: 1.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 17 EAVNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKP----TSGKIELFGERI--KNHRQhIQAL--KKIG------- 81
Cdd:COG4172 24 EAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLLPDpaahPSGSILFDGQDLlgLSERE-LRRIrgNRIAmifqepm 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 82 -SLveSPsyyaHLTARENL-EVLRKILGVSKN----RVDEVLDIVKLaKEANRPVKGF----SLGMKQRLGIASALLGNP 151
Cdd:COG4172 103 tSL--NP----LHTIGKQIaEVLRLHRGLSGAaaraRALELLERVGI-PDPERRLDAYphqlSGGQRQRVMIAMALANEP 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1265835877 152 RLLILDEPTNGLDpAGIQ-EIRSLIKEMPGKNGVTVLISSHLLYEIDHLATQVGIITKGKMLFNGSIESLRKKAKH 226
Cdd:COG4172 176 DLLIADEPTTALD-VTVQaQILDLLKDLQRELGMALLLITHDLGVVRRFADRVAVMRQGEIVEQGPTAELFAAPQH 250
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
21-219 |
1.54e-15 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 76.07 E-value: 1.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 21 EVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELFGERIKNHRQHIQ---ALKKIGSLVESPSYYAHLTARE 97
Cdd:PRK11144 16 TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEKGIClppEKRRIGYVFQDARLFPHYKVRG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 98 NLEvlrkiLGVSKNRVDEVLDIVK-LAKEA--NRPVKGFSLGMKQRLGIASALLGNPRLLILDEPTNGLDPAGIQEIRSL 174
Cdd:PRK11144 96 NLR-----YGMAKSMVAQFDKIVAlLGIEPllDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPY 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1265835877 175 IKEMPGKNGVTVLISSHLLYEIDHLATQVGIITKGKMLFNGSIES 219
Cdd:PRK11144 171 LERLAREINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEE 215
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
10-191 |
1.64e-15 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 74.84 E-value: 1.64e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 10 IKVFKGaeavneVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELFGERIK------------NHRQhIQAL 77
Cdd:COG4598 21 LEVLKG------VSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIRlkpdrdgelvpaDRRQ-LQRI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 78 K-KIGSLVESPSYYAHLTARENL-EVLRKILGVSKN----RVDEVLDIVKLAKEANRPVKGFSLGMKQRLGIASALLGNP 151
Cdd:COG4598 94 RtRLGMVFQSFNLWSHMTVLENViEAPVHVLGRPKAeaieRAEALLAKVGLADKRDAYPAHLSGGQQQRAAIARALAMEP 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1265835877 152 RLLILDEPTNGLDPAGIQE----IRSLIKEmpgknGVTVLISSH 191
Cdd:COG4598 174 EVMLFDEPTSALDPELVGEvlkvMRDLAEE-----GRTMLVVTH 212
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
2-227 |
1.75e-15 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 74.43 E-value: 1.75e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 2 EIVKTTQLIKVFKGAEAVNEVNLSIKEGEIYGFLGPNGAGKTTTIRML--LGLMKP---TSGKIELFGERIKNHRQH-IQ 75
Cdd:PRK14239 4 PILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDLNPevtITGSIVYNGHNIYSPRTDtVD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 76 ALKKIGSLVESPSYYAhLTARENLEVLRKILGV-SKNRVDEVLDivKLAKEAN--RPVK--------GFSLGMKQRLGIA 144
Cdd:PRK14239 84 LRKEIGMVFQQPNPFP-MSIYENVVYGLRLKGIkDKQVLDEAVE--KSLKGASiwDEVKdrlhdsalGLSGGQQQRVCIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 145 SALLGNPRLLILDEPTNGLDPAGIQEIRSLIKEMpgKNGVTVLISSHLLYEIDHLATQVGIITKGKMLFNGSIESLRKKA 224
Cdd:PRK14239 161 RVLATSPKIILLDEPTSALDPISAGKIEETLLGL--KDDYTMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQMFMNP 238
|
...
gi 1265835877 225 KHQ 227
Cdd:PRK14239 239 KHK 241
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
16-212 |
3.23e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 74.48 E-value: 3.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 16 AEAVNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELFGERI--KNHRQHIQALKKIGSLV-ESPSyyAH 92
Cdd:PRK13641 20 KKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHItpETGNKNLKKLRKKVSLVfQFPE--AQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 93 L---TARENLEVLRKILGVS----KNRVDEVLDIVKLAKE-ANRPVKGFSLGMKQRLGIASALLGNPRLLILDEPTNGLD 164
Cdd:PRK13641 98 LfenTVLKDVEFGPKNFGFSedeaKEKALKWLKKVGLSEDlISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLD 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1265835877 165 PAGIQEIRSLIKEMPgKNGVTVLISSHLLYEIDHLATQVGIITKGKML 212
Cdd:PRK13641 178 PEGRKEMMQLFKDYQ-KAGHTVILVTHNMDDVAEYADDVLVLEHGKLI 224
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
18-223 |
3.24e-15 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 74.08 E-value: 3.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 18 AVNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELFGEriknhrqhiqalkkIGSLVESPSYYAHLTARE 97
Cdd:PRK13546 39 ALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGE--------------VSVIAISAGLSGQLTGIE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 98 NLEVLRKILGVSKNRVD----EVLDIVKLAKEANRPVKGFSLGMKQRLGIASALLGNPRLLILDEPTNGLDPAGIQEIRS 173
Cdd:PRK13546 105 NIEFKMLCMGFKRKEIKamtpKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKCLD 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1265835877 174 LIKEMPGKNGvTVLISSHLLYEIDHLATQVGIITKGKMLFNGSIESLRKK 223
Cdd:PRK13546 185 KIYEFKEQNK-TIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDVLPK 233
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
17-191 |
3.53e-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: 3.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 17 EAVNEVNLSIKEGEIYGFLGPNGAGKTT---TI-RM--LLGLMKpTSGKIELFGERIKNHRQHIQAL-KKIGSLVESP-- 87
Cdd:COG1117 25 QALKDINLDIPENKVTALIGPSGCGKSTllrCLnRMndLIPGAR-VEGEILLDGEDIYDPDVDVVELrRRVGMVFQKPnp 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 88 ---SYYahltarENLEVLRKILGV-SKNRVDEvldIVKLA-KEA----------NRPVKGFSLGMKQRLGIASALLGNPR 152
Cdd:COG1117 104 fpkSIY------DNVAYGLRLHGIkSKSELDE---IVEESlRKAalwdevkdrlKKSALGLSGGQQQRLCIARALAVEPE 174
|
170 180 190
....*....|....*....|....*....|....*....
gi 1265835877 153 LLILDEPTNGLDPAGIQEIRSLIKEMpgKNGVTVLISSH 191
Cdd:COG1117 175 VLLMDEPTSALDPISTAKIEELILEL--KKDYTIVIVTH 211
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
27-210 |
5.71e-15 |
|
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: 75.21 E-value: 5.71e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 27 KEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGK----------IELF-GERIKNHRQHIQAlKKIgSLVESPSY------ 89
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKILSGELKPNLGDydeepswdevLKRFrGTELQDYFKKLAN-GEI-KVAHKPQYvdlipk 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 90 YAHLTARenlEVLRKIlgVSKNRVDEVLDIVKLAKEANRPVKGFSLGMKQRLGIASALLGNPRLLILDEPTNGLDpagI- 168
Cdd:COG1245 175 VFKGTVR---ELLEKV--DERGKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLD---Iy 246
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1265835877 169 QEIR--SLIKEMpGKNGVTVLISSHLLYEIDHLATQV----------GIITKGK 210
Cdd:COG1245 247 QRLNvaRLIREL-AEEGKYVLVVEHDLAILDYLADYVhilygepgvyGVVSKPK 299
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
11-212 |
6.54e-15 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 74.89 E-value: 6.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 11 KVFKGAEAVNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELFGERIKN-HRQHIQALKK-IGSLVESPs 88
Cdd:PRK10261 332 RVTREVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTlSPGKLQALRRdIQFIFQDP- 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 89 yYAHLTAR--------ENLEVLRKILG-VSKNRVDEVLDIVKLAKE-ANRPVKGFSLGMKQRLGIASALLGNPRLLILDE 158
Cdd:PRK10261 411 -YASLDPRqtvgdsimEPLRVHGLLPGkAAAARVAWLLERVGLLPEhAWRYPHEFSGGQRQRICIARALALNPKVIIADE 489
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1265835877 159 PTNGLDPAGIQEIRSLIKEMPGKNGVTVLISSHLLYEIDHLATQVGIITKGKML 212
Cdd:PRK10261 490 AVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIV 543
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
18-226 |
6.73e-15 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 73.79 E-value: 6.73e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 18 AVNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTS---------GKIELFGERIKNHR-----------QHIQA- 76
Cdd:COG4170 22 AVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDNWhvtadrfrwNGIDLLKLSPRERRkiigreiamifQEPSSc 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 77 ---LKKIGS-LVES---PSYYAHLTARenlevlrkiLGVSKNRVDEVLDIVKLaKEANRPVKGF----SLGMKQRLGIAS 145
Cdd:COG4170 102 ldpSAKIGDqLIEAipsWTFKGKWWQR---------FKWRKKRAIELLHRVGI-KDHKDIMNSYphelTEGECQKVMIAM 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 146 ALLGNPRLLILDEPTNGLDPAGIQEIRSLIKEMPGKNGVTVLISSHLLYEIDHLATQVGIITKGKMLFNGSIESLRKKAK 225
Cdd:COG4170 172 AIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYCGQTVESGPTEQILKSPH 251
|
.
gi 1265835877 226 H 226
Cdd:COG4170 252 H 252
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
19-191 |
8.45e-15 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 74.60 E-value: 8.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 19 VNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIelfgeriknhrqhiqalkKIGSLVESP---SYYAHL-- 93
Cdd:PRK11147 335 VKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRI------------------HCGTKLEVAyfdQHRAELdp 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 94 --TARENL-----EVLrkILGVSKNRVDEVLDIVKLAKEANRPVKGFSLGMKQRLGIASALLGNPRLLILDEPTNGLDPA 166
Cdd:PRK11147 397 ekTVMDNLaegkqEVM--VNGRPRHVLGYLQDFLFHPKRAMTPVKALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVE 474
|
170 180
....*....|....*....|....*
gi 1265835877 167 GIQEIRSLIKEMPGkngvTVLISSH 191
Cdd:PRK11147 475 TLELLEELLDSYQG----TVLLVSH 495
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
18-226 |
1.43e-14 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 73.07 E-value: 1.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 18 AVNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELFG--------ERIKNHRQHIQAL-----------K 78
Cdd:PRK11308 30 ALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGqdllkadpEAQKLLRQKIQIVfqnpygslnprK 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 79 KIGSLVESP-SYYAHLTARENLEvlrkilgvsknRVDEVLDIVKLAKE-ANRPVKGFSLGMKQRLGIASALLGNPRLLIL 156
Cdd:PRK11308 110 KVGQILEEPlLINTSLSAAERRE-----------KALAMMAKVGLRPEhYDRYPHMFSGGQRQRIAIARALMLDPDVVVA 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1265835877 157 DEPTNGLDpAGIQ-EIRSLIKEMPGKNGVTVLISSHLLYEIDHLATQVGIITKGKMLFNGSIESLRKKAKH 226
Cdd:PRK11308 179 DEPVSALD-VSVQaQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFNNPRH 248
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-164 |
2.19e-14 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 72.57 E-value: 2.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 1 MEIVKTTQLIKVFKG-AEAVNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELFGERIkNHRQhiQALKK 79
Cdd:PRK11650 1 MAGLKLQAVRKSYDGkTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVV-NELE--PADRD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 80 IGSLVESPSYYAHLTARENLEVLRKILGVSK----NRVDEVLDIVKLAKEANRPVKGFSLGMKQRLGIASALLGNPRLLI 155
Cdd:PRK11650 78 IAMVFQNYALYPHMSVRENMAYGLKIRGMPKaeieERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFL 157
|
....*....
gi 1265835877 156 LDEPTNGLD 164
Cdd:PRK11650 158 FDEPLSNLD 166
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
20-191 |
2.69e-14 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 73.13 E-value: 2.69e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 20 NEVNLSIKEGEIYGFLGPNGAGKTTtirmLLGLM-----KPTSGKIELFGER---------IKNHrqhiqalkkIGSLVE 85
Cdd:PRK10938 277 HNLSWQVNPGEHWQIVGPNGAGKST----LLSLItgdhpQGYSNDLTLFGRRrgsgetiwdIKKH---------IGYVSS 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 86 SpsyyAHLTARENLEVLRKIL-----------GVS---KNRVDEVLDIVKLAKE-ANRPVKGFSLGmKQRLG-IASALLG 149
Cdd:PRK10938 344 S----LHLDYRVSTSVRNVILsgffdsigiyqAVSdrqQKLAQQWLDILGIDKRtADAPFHSLSWG-QQRLAlIVRALVK 418
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1265835877 150 NPRLLILDEPTNGLDPAGIQEIRSLIKEMPGKNGVTVLISSH 191
Cdd:PRK10938 419 HPTLLILDEPLQGLDPLNRQLVRRFVDVLISEGETQLLFVSH 460
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
17-191 |
3.30e-14 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 72.83 E-value: 3.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 17 EAVNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELFGERIKN-HRQHIQALKK--IGSLVESPSYYAHL 93
Cdd:PRK10535 22 EVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATlDADALAQLRRehFGFIFQRYHLLSHL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 94 TARENLEVLRKILGVSKN----RVDEVLDIVKLAKEANRPVKGFSLGMKQRLGIASALLGNPRLLILDEPTNGLDPAGIQ 169
Cdd:PRK10535 102 TAAQNVEVPAVYAGLERKqrllRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDSHSGE 181
|
170 180
....*....|....*....|..
gi 1265835877 170 EIRSLIKEMPGKnGVTVLISSH 191
Cdd:PRK10535 182 EVMAILHQLRDR-GHTVIIVTH 202
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
18-191 |
3.61e-14 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 70.89 E-value: 3.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 18 AVNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELFGERIKNHRQHIQAlKKIGSLVESPSY--YAHLTA 95
Cdd:COG1101 21 ALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRA-KYIGRVFQDPMMgtAPSMTI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 96 RENLEV---------LRkiLGVSKNRVD---EVLDIVKLAKEaNR---PVKGFSLGMKQRLGIASALLGNPRLLILDEPT 160
Cdd:COG1101 100 EENLALayrrgkrrgLR--RGLTKKRRElfrELLATLGLGLE-NRldtKVGLLSGGQRQALSLLMATLTKPKLLLLDEHT 176
|
170 180 190
....*....|....*....|....*....|.
gi 1265835877 161 NGLDPAGIQEIRSLIKEMPGKNGVTVLISSH 191
Cdd:COG1101 177 AALDPKTAALVLELTEKIVEENNLTTLMVTH 207
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
15-222 |
3.64e-14 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 72.57 E-value: 3.64e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 15 GAEAVNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMkPTSGKIELFGERIKN-----HRQHIQALKKIGSLVespsy 89
Cdd:PRK11174 362 GKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELREldpesWRKHLSWVGQNPQLP----- 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 90 yaHLTARENLevlrkILG---VSKNRVDEVLD-------IVKLAKEANRPVK----GFSLGMKQRLGIASALLGNPRLLI 155
Cdd:PRK11174 436 --HGTLRDNV-----LLGnpdASDEQLQQALEnawvsefLPLLPQGLDTPIGdqaaGLSVGQAQRLALARALLQPCQLLL 508
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1265835877 156 LDEPTNGLDPAGIQEI-RSLIKEMPGKngvTVLISSHLLYEIDHLaTQVGIITKGKMLFNGSIESLRK 222
Cdd:PRK11174 509 LDEPTASLDAHSEQLVmQALNAASRRQ---TTLMVTHQLEDLAQW-DQIWVMQDGQIVQQGDYAELSQ 572
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
19-211 |
4.06e-14 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 72.51 E-value: 4.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 19 VNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELFGERIKNhRQHIQALKK-IGSLVES---PSYYAHLT 94
Cdd:PRK09700 279 VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISP-RSPLDAVKKgMAYITESrrdNGFFPNFS 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 95 ARENLEVLRKI----LGVSKNRVDEVlDIVKLAKEA-----------NRPVKGFSLGMKQRLGIASALLGNPRLLILDEP 159
Cdd:PRK09700 358 IAQNMAISRSLkdggYKGAMGLFHEV-DEQRTAENQrellalkchsvNQNITELSGGNQQKVLISKWLCCCPEVIIFDEP 436
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1265835877 160 TNGLDPAGIQEIRSLIKEMpGKNGVTVLISSHLLYEIDHLATQVGIITKGKM 211
Cdd:PRK09700 437 TRGIDVGAKAEIYKVMRQL-ADDGKVILMVSSELPEIITVCDRIAVFCEGRL 487
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
16-220 |
4.55e-14 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 72.30 E-value: 4.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 16 AEAVNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELFGERIKNhrQHIQALKK-IGSLVESPSYYAHlT 94
Cdd:PRK13657 348 RQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRT--VTRASLRRnIAVVFQDAGLFNR-S 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 95 ARENLEVlrkilGVSKNRVDEVLDIVKLAKEAN---RPVKGF-----------SLGMKQRLGIASALLGNPRLLILDEPT 160
Cdd:PRK13657 425 IEDNIRV-----GRPDATDEEMRAAAERAQAHDfieRKPDGYdtvvgergrqlSGGERQRLAIARALLKDPPILILDEAT 499
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 161 NGLDPAGIQEIRSLIKEMpgKNGVTVLISSHLLYEIDHlATQVGIITKGKMLFNGSIESL 220
Cdd:PRK13657 500 SALDVETEAKVKAALDEL--MKGRTTFIIAHRLSTVRN-ADRILVFDNGRVVESGSFDEL 556
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
18-196 |
4.75e-14 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 69.83 E-value: 4.75e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 18 AVNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELFGERIKnhRQHIQAL-KKIGSLVESPsyyaHL--- 93
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDIS--KIGLHDLrSRISIIPQDP----VLfsg 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 94 TARENLEVLRKilgVSKNRVDEVLDIVKLAKEANRPVKG-----------FSLGMKQRLGIASALLGNPRLLILDEPTNG 162
Cdd:cd03244 93 TIRSNLDPFGE---YSDEELWQALERVGLKEFVESLPGGldtvveeggenLSVGQRQLLCLARALLRKSKILVLDEATAS 169
|
170 180 190
....*....|....*....|....*....|....
gi 1265835877 163 LDPAGIQEIRSLIKEMpgKNGVTVLISSHLLYEI 196
Cdd:cd03244 170 VDPETDALIQKTIREA--FKDCTVLTIAHRLDTI 201
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
4-187 |
7.75e-14 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 69.73 E-value: 7.75e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 4 VKTTQLIKVFKGAEAVNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELFGERIKNHRQHIQAlKKIGSL 83
Cdd:COG4604 2 IEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELA-KRLAIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 84 VESPSYYAHLTAREnLevlrkilgV-------SKNR--------VDEVLDIVKLAKEANRPVKGFSLGMKQRLGIASALL 148
Cdd:COG4604 81 RQENHINSRLTVRE-L--------VafgrfpySKGRltaedreiIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLA 151
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1265835877 149 GNPRLLILDEPTNGLDPAGIQEI----RSLIKEMpGKNGVTVL 187
Cdd:COG4604 152 QDTDYVLLDEPLNNLDMKHSVQMmkllRRLADEL-GKTVVIVL 193
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
17-216 |
9.12e-14 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 69.82 E-value: 9.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 17 EAVNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIEL------FG------ERIK----------NHRQhi 74
Cdd:PRK15112 27 EAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIddhplhFGdysyrsQRIRmifqdpstslNPRQ-- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 75 qalkKIGSLVESPsyyahLTARENLEVLRKilgvsKNRVDEVLDIVKLAKE-ANRPVKGFSLGMKQRLGIASALLGNPRL 153
Cdd:PRK15112 105 ----RISQILDFP-----LRLNTDLEPEQR-----EKQIIETLRQVGLLPDhASYYPHMLAPGQKQRLGLARALILRPKV 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1265835877 154 LILDEPTNGLDPAGIQEIRSLIKEMPGKNGVTVLISSHLLYEIDHLATQVGIITKGKMLFNGS 216
Cdd:PRK15112 171 IIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGS 233
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
19-211 |
1.13e-13 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 71.01 E-value: 1.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 19 VNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPT-SGKIELFGER--IKNHRQHIQAlkKIGSLVESPSYYA---H 92
Cdd:TIGR02633 276 VDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKPvdIRNPAQAIRA--GIAMVPEDRKRHGivpI 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 93 LTAREN--LEVLRKILGVSknRVDEVLDIVKLAKEANR----------PVKGFSLGMKQRLGIASALLGNPRLLILDEPT 160
Cdd:TIGR02633 354 LGVGKNitLSVLKSFCFKM--RIDAAAELQIIGSAIQRlkvktaspflPIGRLSGGNQQKAVLAKMLLTNPRVLILDEPT 431
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1265835877 161 NGLDPAGIQEIRSLIKEMpGKNGVTVLISSHLLYEIDHLATQVGIITKGKM 211
Cdd:TIGR02633 432 RGVDVGAKYEIYKLINQL-AQEGVAIIVVSSELAEVLGLSDRVLVIGEGKL 481
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
26-210 |
1.51e-13 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 70.99 E-value: 1.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 26 IKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGK----------IELF-GERIKNHRQHIQAlKKIgSLVESPSYYAHL- 93
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILSGELIPNLGDyeeepswdevLKRFrGTELQNYFKKLYN-GEI-KVVHKPQYVDLIp 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 94 -----TAREnleVLRKIlgVSKNRVDEVLDIVKLAKEANRPVKGFSLGMKQRLGIASALLGNPRLLILDEPTNGLDpagI 168
Cdd:PRK13409 174 kvfkgKVRE---LLKKV--DERGKLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLD---I 245
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1265835877 169 -QEIR--SLIKEMpgKNGVTVLISSHLLYEIDHLATQV----------GIITKGK 210
Cdd:PRK13409 246 rQRLNvaRLIREL--AEGKYVLVVEHDLAVLDYLADNVhiaygepgayGVVSKPK 298
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
22-218 |
1.89e-13 |
|
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six proteins and believed to act in Fe-S cluster formation during oxidative stress. SufC forms a complex with SufB and SufD. SufC belongs to the ATP-binding cassette transporter family (pfam00005) but is no longer thought to be part of a transporter. The complex is reported as cytosolic () or associated with the membrane (). The SUF system also includes a cysteine desulfurase (SufS, enhanced by SufE) and a probable iron-sulfur cluster assembly scaffold protein, SufA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 273907 [Multi-domain] Cd Length: 243 Bit Score: 68.83 E-value: 1.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 22 VNLSIKEGEIYGFLGPNGAGKTTTIRMLLGlmKP----TSGKIELFGERIKNHRQHIQALKKIGSLVESPSYYAHLTare 97
Cdd:TIGR01978 19 VNLTVKKGEIHAIMGPNGSGKSTLSKTIAG--HPsyevTSGTILFKGQDLLELEPDERARAGLFLAFQYPEEIPGVS--- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 98 NLEVLRKIL-GVSKNRVDEVLDI---VKLAKE-----------ANRPVK-GFSLGMKQRLGIASALLGNPRLLILDEPTN 161
Cdd:TIGR01978 94 NLEFLRSALnARRSARGEEPLDLldfEKLLKEklalldmdeefLNRSVNeGFSGGEKKRNEILQMALLEPKLAILDEIDS 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1265835877 162 GLDPAGIQEIRSLIKEMPGKNGVTVLIsSHLLYEIDHLA-TQVGIITKGKMLFNGSIE 218
Cdd:TIGR01978 174 GLDIDALKIVAEGINRLREPDRSFLII-THYQRLLNYIKpDYVHVLLDGRIVKSGDVE 230
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
20-199 |
2.04e-13 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 70.91 E-value: 2.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 20 NEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGlmKPTSGKIELfGERIKNHRQHIQALKKIGSLVESPSYY-AHLTAREN 98
Cdd:TIGR00956 780 NNVDGWVKPGTLTALMGASGAGKTTLLNVLAE--RVTTGVITG-GDRLVNGRPLDSSFQRSIGYVQQQDLHlPTSTVRES 856
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 99 LEV---LRKILGVS---KNR-VDEVLDIVKLA--KEANRPVKGFSLGMKQR--LGIASALLGNPRLLI-LDEPTNGLDPA 166
Cdd:TIGR00956 857 LRFsayLRQPKSVSkseKMEyVEEVIKLLEMEsyADAVVGVPGEGLNVEQRkrLTIGVELVAKPKLLLfLDEPTSGLDSQ 936
|
170 180 190
....*....|....*....|....*....|....*...
gi 1265835877 167 GIQEIRSLIKEMpGKNGVTVLISSH-----LLYEIDHL 199
Cdd:TIGR00956 937 TAWSICKLMRKL-ADHGQAILCTIHqpsaiLFEEFDRL 973
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
19-191 |
2.85e-13 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 69.84 E-value: 2.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 19 VNEVNLSIKEGEiyGFL--GPNGAGKTTTIRMLLGLMKPTSGKIELfgeriknhrqhiQALKKI-----------GSLVE 85
Cdd:COG4178 379 LEDLSLSLKPGE--RLLitGPSGSGKSTLLRAIAGLWPYGSGRIAR------------PAGARVlflpqrpylplGTLRE 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 86 SPSYYAHLTAREN---LEVLRKI-LGVSKNRVDEVLDIVKLakeanrpvkgFSLGMKQRLGIASALLGNPRLLILDEPTN 161
Cdd:COG4178 445 ALLYPATAEAFSDaelREALEAVgLGHLAERLDEEADWDQV----------LSLGEQQRLAFARLLLHKPDWLFLDEATS 514
|
170 180 190
....*....|....*....|....*....|..
gi 1265835877 162 GLDPAGIQEIRSLIK-EMPGkngvTVLIS-SH 191
Cdd:COG4178 515 ALDEENEAALYQLLReELPG----TTVISvGH 542
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
19-201 |
3.66e-13 |
|
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: 69.58 E-value: 3.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 19 VNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELfGERIknhrqhiqalkKIGSLVESpsyyahltaREN 98
Cdd:TIGR03719 338 IDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETV-----------KLAYVDQS---------RDA 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 99 LEvlrkilgVSKNRVDEV---LDIVKLAK-EAN----------------RPVKGFSLGMKQRLGIASALLGNPRLLILDE 158
Cdd:TIGR03719 397 LD-------PNKTVWEEIsggLDIIKLGKrEIPsrayvgrfnfkgsdqqKKVGQLSGGERNRVHLAKTLKSGGNVLLLDE 469
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1265835877 159 PTNGLDpagIQEIRSL---IKEMPGkngvTVLISSHLLYEIDHLAT 201
Cdd:TIGR03719 470 PTNDLD---VETLRALeeaLLNFAG----CAVVISHDRWFLDRIAT 508
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
19-164 |
7.05e-13 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 69.04 E-value: 7.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 19 VNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELF-GERIKNHRQH-IQALKKigslVESP-SYYAHLTA 95
Cdd:PRK10636 328 LDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAkGIKLGYFAQHqLEFLRA----DESPlQHLARLAP 403
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1265835877 96 RENLEVLRKILGVSKNRVDEVLDivklakeanrPVKGFSLGMKQRLGIASALLGNPRLLILDEPTNGLD 164
Cdd:PRK10636 404 QELEQKLRDYLGGFGFQGDKVTE----------ETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLD 462
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
15-231 |
7.13e-13 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 67.60 E-value: 7.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 15 GAEAVNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELFGERIKnhrqhiQALKK--------------- 79
Cdd:PRK15056 19 GHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTR------QALQKnlvayvpqseevdws 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 80 IGSLVESP---SYYAHLTarenleVLRKILGVSKNRVDEVLDIVKLAKEANRPVKGFSLGMKQRLGIASALLGNPRLLIL 156
Cdd:PRK15056 93 FPVLVEDVvmmGRYGHMG------WLRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILL 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1265835877 157 DEPTNGLDPAGIQEIRSLIKEMPGKnGVTVLISSHLLYEIDHLATQVgIITKGKMLFNGSIESLRKKAKHQVAFT 231
Cdd:PRK15056 167 DEPFTGVDVKTEARIISLLRELRDE-GKTMLVSTHNLGSVTEFCDYT-VMVKGTVLASGPTETTFTAENLELAFS 239
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
19-211 |
1.62e-12 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 67.65 E-value: 1.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 19 VNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMK-PTSGKIELFGE--RIKNHRQHIQA--------LKKIGsLVESP 87
Cdd:PRK13549 278 VDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPgRWEGEIFIDGKpvKIRNPQQAIAQgiamvpedRKRDG-IVPVM 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 88 SYYAHLTarenLEVLRKILGVSknRVDEVLDIVKLAKEANR----------PVKGFSLGMKQRLGIASALLGNPRLLILD 157
Cdd:PRK13549 357 GVGKNIT----LAALDRFTGGS--RIDDAAELKTILESIQRlkvktaspelAIARLSGGNQQKAVLAKCLLLNPKILILD 430
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1265835877 158 EPTNGLDPAGIQEIRSLIKEMpGKNGVTVLISSHLLYEIDHLATQVGIITKGKM 211
Cdd:PRK13549 431 EPTRGIDVGAKYEIYKLINQL-VQQGVAIIVISSELPEVLGLSDRVLVMHEGKL 483
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
2-191 |
2.01e-12 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 65.96 E-value: 2.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 2 EIVKTTQLIKVFKGAE-AVNEVNLSIKEGEIYGFLGPNGAGKTTTIRML--LGLMKPT---SGKIELFGERIknHRQHIQ 75
Cdd:PRK14243 8 ETVLRTENLNVYYGSFlAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFnrLNDLIPGfrvEGKVTFHGKNL--YAPDVD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 76 AL---KKIGSLVESPSYYAHlTARENLEVLRKILGVsKNRVDEV----LDIVKLAKEANRPVK--GFSL--GMKQRLGIA 144
Cdd:PRK14243 86 PVevrRRIGMVFQKPNPFPK-SIYDNIAYGARINGY-KGDMDELversLRQAALWDEVKDKLKqsGLSLsgGQQQRLCIA 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1265835877 145 SALLGNPRLLILDEPTNGLDPAGIQEIRSLIKEMpgKNGVTVLISSH 191
Cdd:PRK14243 164 RAIAVQPEVILMDEPCSALDPISTLRIEELMHEL--KEQYTIIIVTH 208
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
9-224 |
4.48e-12 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 66.45 E-value: 4.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 9 LIKVFKGAEAVNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIElFGE--RIKNHRQ-HIQALKKIGSLVE 85
Cdd:PRK15064 325 LTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVK-WSEnaNIGYYAQdHAYDFENDLTLFD 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 86 SPSYYAhlTARENLEVLRKILGvsknrvdevldivKL---AKEANRPVKGFSLGMKQRLGIASALLGNPRLLILDEPTNG 162
Cdd:PRK15064 404 WMSQWR--QEGDDEQAVRGTLG-------------RLlfsQDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLVMDEPTNH 468
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1265835877 163 LDPAGIQEIRSLIKEMPGkngvTVLISSHLLYEIDHLATQVGIITKGKML-FNGSIES-LRKKA 224
Cdd:PRK15064 469 MDMESIESLNMALEKYEG----TLIFVSHDREFVSSLATRIIEITPDGVVdFSGTYEEyLRSQG 528
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
17-226 |
4.90e-12 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 65.59 E-value: 4.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 17 EAVNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKP----TSGK-----IELFGERIKNHRQHIQalKKIGSLVESP 87
Cdd:PRK15093 21 KAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDnwrvTADRmrfddIDLLRLSPRERRKLVG--HNVSMIFQEP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 88 SYYAHLTARENLEVLRKILGVS------------KNRVDEVLDIVKLaKEANRPVKGFSL----GMKQRLGIASALLGNP 151
Cdd:PRK15093 99 QSCLDPSERVGRQLMQNIPGWTykgrwwqrfgwrKRRAIELLHRVGI-KDHKDAMRSFPYelteGECQKVMIAIALANQP 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1265835877 152 RLLILDEPTNGLDPAGIQEIRSLIKEMPGKNGVTVLISSHLLYEIDHLATQVGIITKGKMLFNGSIESLRKKAKH 226
Cdd:PRK15093 178 RLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTVETAPSKELVTTPHH 252
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
21-200 |
5.40e-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: 66.11 E-value: 5.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 21 EVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELfgeriknhrqhiQALKKIGSLVESPSYYAHLTARENLE 100
Cdd:TIGR03719 23 DISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARP------------QPGIKVGYLPQEPQLDPTKTVRENVE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 101 --------VLRKILGVSKNRVDEVLDIVKLAKEANR-------------------------------PVKGFSLGMKQRL 141
Cdd:TIGR03719 91 egvaeikdALDRFNEISAKYAEPDADFDKLAAEQAElqeiidaadawdldsqleiamdalrcppwdaDVTKLSGGERRRV 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1265835877 142 GIASALLGNPRLLILDEPTNGLDPAGIQEIRSLIKEMPGkngvTVLISSHLLYEIDHLA 200
Cdd:TIGR03719 171 ALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPG----TVVAVTHDRYFLDNVA 225
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
17-196 |
5.72e-12 |
|
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: 63.97 E-value: 5.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 17 EAVNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELFGERIKnhrqHI--QALK-KIGSLVESPSYYAHl 93
Cdd:cd03369 22 PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDIS----TIplEDLRsSLTIIPQDPTLFSG- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 94 TARENLEVLRKilgVSKNRVDEVLDIvklaKEANrpvKGFSLGMKQRLGIASALLGNPRLLILDEPTNGLDPAGIQEIRS 173
Cdd:cd03369 97 TIRSNLDPFDE---YSDEEIYGALRV----SEGG---LNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDALIQK 166
|
170 180
....*....|....*....|...
gi 1265835877 174 LIKEMpgKNGVTVLISSHLLYEI 196
Cdd:cd03369 167 TIREE--FTNSTILTIAHRLRTI 187
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
22-191 |
5.88e-12 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 64.03 E-value: 5.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 22 VNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELFGERIKNHRQHIQAL---KKIGSLVESPSYYAHLTAREN 98
Cdd:PRK10584 29 VELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKlraKHVGFVFQSFMLIPTLNALEN 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 99 LEVLRKILGV----SKNRVDEVLDIVKLAKEANRPVKGFSLGMKQRLGIASALLGNPRLLILDEPTNGLDPAGIQEIRSL 174
Cdd:PRK10584 109 VELPALLRGEssrqSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADL 188
|
170
....*....|....*..
gi 1265835877 175 IKEMPGKNGVTVLISSH 191
Cdd:PRK10584 189 LFSLNREHGTTLILVTH 205
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
26-206 |
1.54e-11 |
|
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: 61.82 E-value: 1.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 26 IKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELFGERIKNHRQHIQalkkigslvespsyyahltarenlevlrki 105
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITPVYKPQYID------------------------------ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 106 lgvsknrvdevldivklakeanrpvkgFSLGMKQRLGIASALLGNPRLLILDEPTNGLDPAGIQEIRSLIKEMPGKNGVT 185
Cdd:cd03222 72 ---------------------------LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKT 124
|
170 180
....*....|....*....|.
gi 1265835877 186 VLISSHLLYEIDHLATQVGII 206
Cdd:cd03222 125 ALVVEHDLAVLDYLSDRIHVF 145
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
3-218 |
1.82e-11 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 63.12 E-value: 1.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 3 IVKTTQLIKVFKGAEAVNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLG--LMKPTSGKIELFGERIKNHRQHIQALKKI 80
Cdd:CHL00131 7 ILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGhpAYKILEGDILFKGESILDLEPEERAHLGI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 81 GSLVESPSYYAHLTARENLEVL----RKILGVSK-------NRVDEVLDIVKL-AKEANRPV-KGFSLGMKQRLGIASAL 147
Cdd:CHL00131 87 FLAFQYPIEIPGVSNADFLRLAynskRKFQGLPEldpleflEIINEKLKLVGMdPSFLSRNVnEGFSGGEKKRNEILQMA 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1265835877 148 LGNPRLLILDEPTNGLDPAGIQEIRSLIKEMPGKNGVTVLIsSHLLYEIDHLATQ-VGIITKGKMLFNGSIE 218
Cdd:CHL00131 167 LLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIILI-THYQRLLDYIKPDyVHVMQNGKIIKTGDAE 237
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
23-201 |
2.32e-11 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 64.37 E-value: 2.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 23 NLSIK--EGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELfGERIknhrqhiqalkKIGSLVESpsyyahltaRENLE 100
Cdd:PRK11819 342 DLSFSlpPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GETV-----------KLAYVDQS---------RDALD 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 101 vlrkilgVSKNRVDEV---LDIVKLAK-EAN----------------RPVKGFSLGMKQRLGIASALL--GNprLLILDE 158
Cdd:PRK11819 401 -------PNKTVWEEIsggLDIIKVGNrEIPsrayvgrfnfkggdqqKKVGVLSGGERNRLHLAKTLKqgGN--VLLLDE 471
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1265835877 159 PTNGLDpagIQEIRSL---IKEMPGkngvTVLISSHLLYEIDHLAT 201
Cdd:PRK11819 472 PTNDLD---VETLRALeeaLLEFPG----CAVVISHDRWFLDRIAT 510
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
7-210 |
2.51e-11 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 63.98 E-value: 2.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 7 TQLIKVFKGAEAVNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELFGERIkNHRQHIQALKKIGSLV-E 85
Cdd:PRK10982 2 SNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEI-DFKSSKEALENGISMVhQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 86 SPSYYAHLTARENLEVLR-----------KILGVSKNRVDEvLDIVKLAKEAnrpVKGFSLGMKQRLGIASALLGNPRLL 154
Cdd:PRK10982 81 ELNLVLQRSVMDNMWLGRyptkgmfvdqdKMYRDTKAIFDE-LDIDIDPRAK---VATLSVSQMQMIEIAKAFSYNAKIV 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1265835877 155 ILDEPTNGLDPAGIQEIRSLIKEMPGKnGVTVLISSHLLYEIDHLATQVGIITKGK 210
Cdd:PRK10982 157 IMDEPTSSLTEKEVNHLFTIIRKLKER-GCGIVYISHKMEEIFQLCDEITILRDGQ 211
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
18-192 |
2.54e-11 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 63.98 E-value: 2.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 18 AVNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELFGERIKNHRQHiQALKKIGSLV----ESPSYYAHL 93
Cdd:PRK10982 263 SIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNAN-EAINHGFALVteerRSTGIYAYL 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 94 TAR-----ENLEVLRKILGVSKNR-----VDEVLDIVKLAKEANRPVKG-FSLGMKQRLGIASALLGNPRLLILDEPTNG 162
Cdd:PRK10982 342 DIGfnsliSNIRNYKNKVGLLDNSrmksdTQWVIDSMRVKTPGHRTQIGsLSGGNQQKVIIGRWLLTQPEILMLDEPTRG 421
|
170 180 190
....*....|....*....|....*....|
gi 1265835877 163 LDPAGIQEIRSLIKEMPGKNGVTVLISSHL 192
Cdd:PRK10982 422 IDVGAKFEIYQLIAELAKKDKGIIIISSEM 451
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
27-221 |
3.05e-11 |
|
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: 62.38 E-value: 3.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 27 KEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIEL---FGERIKNHR-----QHIQALKKIG-SLVESPSYYAHL---- 93
Cdd:cd03236 24 REGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFDDppdWDEILDEFRgselqNYFTKLLEGDvKVIVKPQYVDLIpkav 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 94 --TARENLEVLRKilgvsKNRVDEVLDIVKLAKEANRPVKGFSLGMKQRLGIASALLGNPRLLILDEPTNGLDpagIQE- 170
Cdd:cd03236 104 kgKVGELLKKKDE-----RGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLD---IKQr 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1265835877 171 ------IRSLIKEmpgknGVTVLISSHLLYEIDHLATQV----------GIITKGKMLFNGSIESLR 221
Cdd:cd03236 176 lnaarlIRELAED-----DNYVLVVEHDLAVLDYLSDYIhclygepgayGVVTLPKSVREGINEFLD 237
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
21-164 |
4.37e-11 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 63.71 E-value: 4.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 21 EVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGlmKPTSGKIElfGE-RIKNHRQHIQALKKIGSLVESPSYYA-HLTAREN 98
Cdd:PLN03140 898 EVTGAFRPGVLTALMGVSGAGKTTLMDVLAG--RKTGGYIE--GDiRISGFPKKQETFARISGYCEQNDIHSpQVTVRES 973
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1265835877 99 L---EVLRKILGVSKNR----VDEVLDIVKLA--KEA--NRP-VKGFSLGMKQRLGIASALLGNPRLLILDEPTNGLD 164
Cdd:PLN03140 974 LiysAFLRLPKEVSKEEkmmfVDEVMELVELDnlKDAivGLPgVTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLD 1051
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
19-198 |
8.31e-11 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 60.88 E-value: 8.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 19 VNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELFGERI-----KNHRQhiqalkKIGSLVESPSYYAHl 93
Cdd:PRK10247 23 LNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDIstlkpEIYRQ------QVSYCAQTPTLFGD- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 94 TARENLEVLRKILG--VSKNRVDEVLDIVKLAKEA-NRPVKGFSLGMKQRLGIASALLGNPRLLILDEPTNGLDPAGIQE 170
Cdd:PRK10247 96 TVYDNLIFPWQIRNqqPDPAIFLDDLERFALPDTIlTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDESNKHN 175
|
170 180
....*....|....*....|....*...
gi 1265835877 171 IRSLIKEMPGKNGVTVLISSHLLYEIDH 198
Cdd:PRK10247 176 VNEIIHRYVREQNIAVLWVTHDKDEINH 203
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
23-206 |
1.53e-10 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 61.57 E-value: 1.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 23 NLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGkielfgERIkNHRQHIQAL--KKIGSLVE-----------SPSy 89
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSG------ERQ-SQFSHITRLsfEQLQKLVSdewqrnntdmlSPG- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 90 yAHLTARENLEVLRkiLGVSKN-RVDEVLDIVKLAKEANRPVKGFSLGMKQRLGIASALLGNPRLLILDEPTNGLDPAGI 168
Cdd:PRK10938 95 -EDDTGRTTAEIIQ--DEVKDPaRCEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASR 171
|
170 180 190
....*....|....*....|....*....|....*...
gi 1265835877 169 QEIRSLIKEMPGKNGVTVLISSHlLYEIDHLATQVGII 206
Cdd:PRK10938 172 QQLAELLASLHQSGITLVLVLNR-FDEIPDFVQFAGVL 208
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
14-192 |
1.73e-10 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 61.97 E-value: 1.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 14 KGAEAVNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKI---------------------------ELFGER 66
Cdd:PTZ00265 396 KDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIiindshnlkdinlkwwrskigvvsqdpLLFSNS 475
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 67 IKNHRQH-IQALKKIGSL--------------------------------VESPSYYAHLTARENLEVLR--KILGVSKN 111
Cdd:PTZ00265 476 IKNNIKYsLYSLKDLEALsnyynedgndsqenknkrnscrakcagdlndmSNTTDSNELIEMRKNYQTIKdsEVVDVSKK 555
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 112 RVdeVLDIVKLAKEANRPVKG-----FSLGMKQRLGIASALLGNPRLLILDEPTNGLDPAGIQEIRSLIKEMPG-KNGVT 185
Cdd:PTZ00265 556 VL--IHDFVSALPDKYETLVGsnaskLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGnENRIT 633
|
....*..
gi 1265835877 186 VLISSHL 192
Cdd:PTZ00265 634 IIIAHRL 640
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
18-226 |
1.73e-10 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 61.80 E-value: 1.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 18 AVNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIEL--------------FGERIKNHRQHIQAlKKIGSL 83
Cdd:PRK10261 31 AVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCdkmllrrrsrqvieLSEQSAAQMRHVRG-ADMAMI 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 84 VESP--SYYAHLTARENL-EVLRKILGVSKNR----VDEVLDIVKLAKEA---NRPVKGFSLGMKQRLGIASALLGNPRL 153
Cdd:PRK10261 110 FQEPmtSLNPVFTVGEQIaESIRLHQGASREEamveAKRMLDQVRIPEAQtilSRYPHQLSGGMRQRVMIAMALSCRPAV 189
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1265835877 154 LILDEPTNGLDPAGIQEIRSLIKEMPGKNGVTVLISSHLLYEIDHLATQVGIITKGKMLFNGSIESLRKKAKH 226
Cdd:PRK10261 190 LIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQIFHAPQH 262
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
17-226 |
1.86e-10 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 61.26 E-value: 1.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 17 EAVNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMkPT------SGKIELFGERI-KNHRQHIQALK--KIGSLVESP 87
Cdd:PRK15134 23 TVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLL-PSppvvypSGDIRFHGESLlHASEQTLRGVRgnKIAMIFQEP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 88 SYYA---HLTARENLEVLRKILGVSKN--RVDEV--LDIVKLAKEANRpVKGF----SLGMKQRLGIASALLGNPRLLIL 156
Cdd:PRK15134 102 MVSLnplHTLEKQLYEVLSLHRGMRREaaRGEILncLDRVGIRQAAKR-LTDYphqlSGGERQRVMIAMALLTRPELLIA 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 157 DEPTNGLDPAGIQEIRSLIKEMPGKNGVTVLISSHLLYEIDHLATQVGIITKGKMLFNGSIESLRKKAKH 226
Cdd:PRK15134 181 DEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAATLFSAPTH 250
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
22-210 |
2.01e-10 |
|
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: 59.41 E-value: 2.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 22 VNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELFGeRIknhrqhiqalkkigSLVESPSYYAHLTARENlev 101
Cdd:cd03250 24 INLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG-SI--------------AYVSQEPWIQNGTIREN--- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 102 lrkILG---VSKNRVDEVL-------DIVKLAKEANRPV--KGFSL--GMKQRLGIASALLGNPRLLILDEPTNGLDPA- 166
Cdd:cd03250 86 ---ILFgkpFDEERYEKVIkacalepDLEILPDGDLTEIgeKGINLsgGQKQRISLARAVYSDADIYLLDDPLSAVDAHv 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1265835877 167 GIQEIRSLIKEMpGKNGVTVLISSHLLYEIDHlATQVGIITKGK 210
Cdd:cd03250 163 GRHIFENCILGL-LLNNKTRILVTHQLQLLPH-ADQIVVLDNGR 204
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
20-191 |
2.42e-10 |
|
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: 58.79 E-value: 2.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 20 NEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGlmKPTSGKIElfGERIKNHRQHIQALKKIGSLVEspSYYAH---LTAR 96
Cdd:cd03232 24 NNISGYVKPGTLTALMGESGAGKTTLLDVLAG--RKTAGVIT--GEILINGRPLDKNFQRSTGYVE--QQDVHspnLTVR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 97 ENLE---VLRkilgvsknrvdevldivklakeanrpvkGFSLGMKQRLGIASALLGNPRLLILDEPTNGLDPAGIQEIRS 173
Cdd:cd03232 98 EALRfsaLLR----------------------------GLSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVR 149
|
170
....*....|....*...
gi 1265835877 174 LIKEMpGKNGVTVLISSH 191
Cdd:cd03232 150 FLKKL-ADSGQAILCTIH 166
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
21-196 |
2.99e-10 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 60.89 E-value: 2.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 21 EVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELFGERIK--NH---RQHIqALKKIGSLVESPSYYAHLTa 95
Cdd:PRK10790 359 NINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSslSHsvlRQGV-AMVQQDPVVLADTFLANVT- 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 96 renlevlrkiLG--VSKNRVDEVLDIVKLAKEANRPVKG-----------FSLGMKQRLGIASALLGNPRLLILDEPTNG 162
Cdd:PRK10790 437 ----------LGrdISEEQVWQALETVQLAELARSLPDGlytplgeqgnnLSVGQKQLLALARVLVQTPQILILDEATAN 506
|
170 180 190
....*....|....*....|....*....|....*..
gi 1265835877 163 LDPA---GIQEIRSLIKEMpgkngVTVLISSHLLYEI 196
Cdd:PRK10790 507 IDSGteqAIQQALAAVREH-----TTLVVIAHRLSTI 538
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
18-226 |
3.54e-10 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 60.14 E-value: 3.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 18 AVNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKpTSGKIelFGERIKNHRQHIQALKK------IGSLVE------ 85
Cdd:PRK11022 22 AVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLID-YPGRV--MAEKLEFNGQDLQRISEkerrnlVGAEVAmifqdp 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 86 ----SPSYYAHLTARENLEVLRkilGVSK----NRVDEVLDIVKLAKEANR----PVKgFSLGMKQRLGIASALLGNPRL 153
Cdd:PRK11022 99 mtslNPCYTVGFQIMEAIKVHQ---GGNKktrrQRAIDLLNQVGIPDPASRldvyPHQ-LSGGMSQRVMIAMAIACRPKL 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1265835877 154 LILDEPTNGLDPAGIQEIRSLIKEMPGKNGVTVLISSHLLYEIDHLATQVGIITKGKMLFNGSIESLRKKAKH 226
Cdd:PRK11022 175 LIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDIFRAPRH 247
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
9-193 |
4.07e-10 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 59.17 E-value: 4.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 9 LIKVFKGAEAVNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIElfgeriknHRQHIQALKKIGSLVESPS 88
Cdd:PRK11701 12 LTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVH--------YRMRDGQLRDLYALSEAER 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 89 Y--------YAHLTARENLE--------VLRKILGVSKNRVDEV-------LDIVKLAkeANR----PvKGFSLGMKQRL 141
Cdd:PRK11701 84 RrllrtewgFVHQHPRDGLRmqvsaggnIGERLMAVGARHYGDIratagdwLERVEID--AARiddlP-TTFSGGMQQRL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1265835877 142 GIASALLGNPRLLILDEPTNGLDpAGIQE-----IRSLIKEMpgknGVTVLISSHLL 193
Cdd:PRK11701 161 QIARNLVTHPRLVFMDEPTGGLD-VSVQArlldlLRGLVREL----GLAVVIVTHDL 212
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
26-225 |
6.09e-10 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 60.12 E-value: 6.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 26 IKEGEIYGFLGPNGAGKTTtirmllgLMKPTSGKIELF--------------GERIKNHrqhiqalkKIGSLV---ESPS 88
Cdd:TIGR00956 84 IKPGELTVVLGRPGSGCST-------LLKTIASNTDGFhigvegvitydgitPEEIKKH--------YRGDVVynaETDV 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 89 YYAHLTARENLEVLRKILGVsKNRVDEV------------------LDIVKLAKEANRPVKGFSLGMKQRLGIASALLGN 150
Cdd:TIGR00956 149 HFPHLTVGETLDFAARCKTP-QNRPDGVsreeyakhiadvymatygLSHTRNTKVGNDFVRGVSGGERKRVSIAEASLGG 227
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1265835877 151 PRLLILDEPTNGLDPAGIQEIRSLIKEMPGKNGVTVLIS----SHLLYEidhLATQVGIITKGKMLFNGSieslRKKAK 225
Cdd:TIGR00956 228 AKIQCWDNATRGLDSATALEFIRALKTSANILDTTPLVAiyqcSQDAYE---LFDKVIVLYEGYQIYFGP----ADKAK 299
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
11-210 |
6.10e-10 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 59.63 E-value: 6.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 11 KVFKGAEAVNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELFGERI--KNHRQHIQAlkKIGSLVESPS 88
Cdd:PRK10762 12 KAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVtfNGPKSSQEA--GIGIIHQELN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 89 YYAHLTARENL----EVLRKILGVSKNRV----DEVLDIVKLAKEANRPVKGFSLGMKQRLGIASALLGNPRLLILDEPT 160
Cdd:PRK10762 90 LIPQLTIAENIflgrEFVNRFGRIDWKKMyaeaDKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPT 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1265835877 161 NGLDPAGIQEIRSLIKEMPGKNGVTVLIsSHLLYEIDHLATQVGIITKGK 210
Cdd:PRK10762 170 DALTDTETESLFRVIRELKSQGRGIVYI-SHRLKEIFEICDDVTVFRDGQ 218
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
19-191 |
8.69e-10 |
|
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: 56.78 E-value: 8.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 19 VNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIEL-FGERIKNHRQHiqalkkigslvespSYYAHLTARE 97
Cdd:cd03223 17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMpEGEDLLFLPQR--------------PYLPLGTLRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 98 NL-----EVLrkilgvsknrvdevldivklakeanrpvkgfSLGMKQRLGIASALLGNPRLLILDEPTNGLDPAGIQEIR 172
Cdd:cd03223 83 QLiypwdDVL-------------------------------SGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLY 131
|
170
....*....|....*....
gi 1265835877 173 SLIKEMpgknGVTVLISSH 191
Cdd:cd03223 132 QLLKEL----GITVISVGH 146
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
15-221 |
2.20e-09 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 57.17 E-value: 2.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 15 GAEAVNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELFGeRIknhrqhiqalkkigSLVESPSYYAHLT 94
Cdd:cd03291 49 GAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG-RI--------------SFSSQFSWIMPGT 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 95 ARENLevlrkILGVSKN--RVDEVL-------DIVKLAKEANRPVK--GFSL--GMKQRLGIASALLGNPRLLILDEPTN 161
Cdd:cd03291 114 IKENI-----IFGVSYDeyRYKSVVkacqleeDITKFPEKDNTVLGegGITLsgGQRARISLARAVYKDADLYLLDSPFG 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1265835877 162 GLDPAGIQEI--RSLIKEMPGKNgvTVLISShllyEIDHL--ATQVGIITKGKMLFNGSIESLR 221
Cdd:cd03291 189 YLDVFTEKEIfeSCVCKLMANKT--RILVTS----KMEHLkkADKILILHEGSSYFYGTFSELQ 246
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
18-220 |
2.49e-09 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 58.11 E-value: 2.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 18 AVNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELFGERIKNHRqhIQALKKIGSLVespSYYAHLTare 97
Cdd:PRK11176 358 ALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYT--LASLRNQVALV---SQNVHLF--- 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 98 NLEVLRKILGVSKNRVDEVlDIVKLAKEA------NRPVKGF-----------SLGMKQRLGIASALLGNPRLLILDEPT 160
Cdd:PRK11176 430 NDTIANNIAYARTEQYSRE-QIEEAARMAyamdfiNKMDNGLdtvigengvllSGGQRQRIAIARALLRDSPILILDEAT 508
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 161 NGLDPAGIQEIRSLIKEMPgKNGvTVLISSHLLYEIDHlATQVGIITKGKMLFNGSIESL 220
Cdd:PRK11176 509 SALDTESERAIQAALDELQ-KNR-TSLVIAHRLSTIEK-ADEILVVEDGEIVERGTHAEL 565
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
22-193 |
2.52e-09 |
|
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: 57.91 E-value: 2.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 22 VNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELFGERIKNHRQHiqalkkigslvespSyyahltarenlev 101
Cdd:COG5265 377 VSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQA--------------S------------- 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 102 LRKILGVsknrV--DEVL-------------------DIVKLAKEAN------------------RPVKgFSLGMKQRLG 142
Cdd:COG5265 430 LRAAIGI----VpqDTVLfndtiayniaygrpdaseeEVEAAARAAQihdfieslpdgydtrvgeRGLK-LSGGEKQRVA 504
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1265835877 143 IASALLGNPRLLILDEPTNGLDPAGIQEIRSLIKEMpgKNGVTVLISSHLL 193
Cdd:COG5265 505 IARTLLKNPPILIFDEATSALDSRTERAIQAALREV--ARGRTTLVIAHRL 553
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
15-191 |
2.69e-09 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 57.98 E-value: 2.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 15 GAEAVNEvNLSIK--EGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIEL-FGERIKNHRQ-----------------HI 74
Cdd:PRK15064 12 GAKPLFE-NISVKfgGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLdPNERLGKLRQdqfafeeftvldtvimgHT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 75 Q--ALKKigslvESPSYYAHLTARE-------NLEVLRKILG--VSKNRVDEVLDIVKLAKEA-NRPVKGFSLGMKQRLG 142
Cdd:PRK15064 91 ElwEVKQ-----ERDRIYALPEMSEedgmkvaDLEVKFAEMDgyTAEARAGELLLGVGIPEEQhYGLMSEVAPGWKLRVL 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1265835877 143 IASALLGNPRLLILDEPTNGLDpagIQEIRSLIKEMPGKNGvTVLISSH 191
Cdd:PRK15064 166 LAQALFSNPDILLLDEPTNNLD---INTIRWLEDVLNERNS-TMIIISH 210
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
22-211 |
2.77e-09 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 57.61 E-value: 2.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 22 VNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELFGER--IKNHRQHIQA--------LKKIGSL-VESPSYY 90
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPidIRSPRDAIRAgimlcpedRKAEGIIpVHSVADN 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 91 AHLTARENLEVLRKILGVSKNRVDEVLDIVKLA-KEANR--PVKGFSLGMKQRLGIASALLGNPRLLILDEPTNGLDPAG 167
Cdd:PRK11288 352 INISARRHHLRAGCLINNRWEAENADRFIRSLNiKTPSReqLIMNLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGA 431
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1265835877 168 IQEIRSLIKEMpGKNGVTVLISSHLLYEIDHLATQVGIITKGKM 211
Cdd:PRK11288 432 KHEIYNVIYEL-AAQGVAVLFVSSDLPEVLGVADRIVVMREGRI 474
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
15-223 |
4.94e-09 |
|
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: 57.61 E-value: 4.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 15 GAEAVNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELFGeRIknhrqhiqalkkigSLVESPSYYAHLT 94
Cdd:TIGR01271 438 VTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG-RI--------------SFSPQTSWIMPGT 502
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 95 ARENLevlrkILGVSKN--RVDEVL-------DIVKLAKEANRPVK--GFSL--GMKQRLGIASALLGNPRLLILDEPTN 161
Cdd:TIGR01271 503 IKDNI-----IFGLSYDeyRYTSVIkacqleeDIALFPEKDKTVLGegGITLsgGQRARISLARAVYKDADLYLLDSPFT 577
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1265835877 162 GLDPAGIQEI--RSLIKEMPGKngVTVLISSHLlyeiDHL--ATQVGIITKGKMLFNGSIESLRKK 223
Cdd:TIGR01271 578 HLDVVTEKEIfeSCLCKLMSNK--TRILVTSKL----EHLkkADKILLLHEGVCYFYGTFSELQAK 637
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
18-191 |
5.58e-09 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 56.90 E-value: 5.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 18 AVNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELFGERIknHRQHIQALKKIGSLVESPSY-YAHLTAR 96
Cdd:PRK10522 338 SVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPV--TAEQPEDYRKLFSAVFTDFHlFDQLLGP 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 97 ENLEVLRKIlgvsknrVDEVLDIV----KLAKEANRPVK-GFSLGMKQRLGIASALLGNPRLLILDEPTNGLDPA----G 167
Cdd:PRK10522 416 EGKPANPAL-------VEKWLERLkmahKLELEDGRISNlKLSKGQKKRLALLLALAEERDILLLDEWAADQDPHfrreF 488
|
170 180
....*....|....*....|....
gi 1265835877 168 IQEIRSLIKEMpgknGVTVLISSH 191
Cdd:PRK10522 489 YQVLLPLLQEM----GKTIFAISH 508
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
24-211 |
1.90e-08 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 55.34 E-value: 1.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 24 LSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELFGERIKNHRQ-----HIQ---------ALKKIGSLVESPSY 89
Cdd:PRK11147 24 LHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLIVARLQqdpprNVEgtvydfvaeGIEEQAEYLKRYHD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 90 YAHLTARE----NLEVLRKILGV--------SKNRVDEVLDIVKLakEANRPVKGFSLGMKQRLGIASALLGNPRLLILD 157
Cdd:PRK11147 104 ISHLVETDpsekNLNELAKLQEQldhhnlwqLENRINEVLAQLGL--DPDAALSSLSGGWLRKAALGRALVSNPDVLLLD 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1265835877 158 EPTNGLDPAGIQEIRSLIKEMpgkNGVTVLIsSHLLYEIDHLATQVGIITKGKM 211
Cdd:PRK11147 182 EPTNHLDIETIEWLEGFLKTF---QGSIIFI-SHDRSFIRNMATRIVDLDRGKL 231
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
15-191 |
3.07e-08 |
|
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: 54.92 E-value: 3.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 15 GAEAVNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKpTSGKIELFGerIKNHRQHIQALKKIGSLVESPSYYAHLT 94
Cdd:TIGR01271 1231 GRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDG--VSWNSVTLQTWRKAFGVIPQKVFIFSGT 1307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 95 ARENLEVLRKIlgvSKNRVDEVLDIVKLAKEANR-PVK--------GFSL--GMKQRLGIASALLGNPRLLILDEPTNGL 163
Cdd:TIGR01271 1308 FRKNLDPYEQW---SDEEIWKVAEEVGLKSVIEQfPDKldfvlvdgGYVLsnGHKQLMCLARSILSKAKILLLDEPSAHL 1384
|
170 180
....*....|....*....|....*...
gi 1265835877 164 DPAGIQEIRSLIKEmpGKNGVTVLISSH 191
Cdd:TIGR01271 1385 DPVTLQIIRKTLKQ--SFSNCTVILSEH 1410
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
33-200 |
5.91e-08 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 53.58 E-value: 5.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 33 GFLGPNGAGKTTTIRMLLGLMKPTSGKIELfgeriknhrqhiQALKKIGSLVESPSYYAHLTARENLEvlrkiLGVS--- 109
Cdd:PRK11819 37 GVLGLNGAGKSTLLRIMAGVDKEFEGEARP------------APGIKVGYLPQEPQLDPEKTVRENVE-----EGVAevk 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 110 --KNRVDEV--------LDIVKLAKE-------------------------ANR------PVKGFSLGMKQRLGIASALL 148
Cdd:PRK11819 100 aaLDRFNEIyaayaepdADFDALAAEqgelqeiidaadawdldsqleiamdALRcppwdaKVTKLSGGERRRVALCRLLL 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1265835877 149 GNPRLLILDEPTNGLDPAGIQEIRSLIKEMPGkngvTVLISSHLLYEIDHLA 200
Cdd:PRK11819 180 EKPDMLLLDEPTNHLDAESVAWLEQFLHDYPG----TVVAVTHDRYFLDNVA 227
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
29-201 |
8.71e-08 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 50.83 E-value: 8.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 29 GEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELfgeriknhrqhiqalkkigslvespsyyahltarenlevlrkilgV 108
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIY---------------------------------------------I 36
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 109 SKNRVDEVLDIVKLAKEANRPVKGFSLGMKQRLGIASALLGNPRLLILDEPTNGLDPAGIQEIRSLI-----KEMPGKNG 183
Cdd:smart00382 37 DGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEelrllLLLKSEKN 116
|
170
....*....|....*...
gi 1265835877 184 VTVLISSHLLYEIDHLAT 201
Cdd:smart00382 117 LTVILTTNDEKDLGPALL 134
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
18-193 |
9.02e-08 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 53.18 E-value: 9.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 18 AVNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELFGERIknHRQHIQALKKIGSLVESPSYYAHLTARE 97
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPL--TKLQLDSWRSRLAVVSQTPFLFSDTVAN 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 98 NLEVLRKilGVSKNRVDEVL-------DIVKLAKEANRPV--KGFSL--GMKQRLGIASALLGNPRLLILDEPTNGLDPA 166
Cdd:PRK10789 408 NIALGRP--DATQQEIEHVArlasvhdDILRLPQGYDTEVgeRGVMLsgGQKQRISIARALLLNAEILILDDALSAVDGR 485
|
170 180
....*....|....*....|....*..
gi 1265835877 167 GIQEIRSLIKEMpgKNGVTVLISSHLL 193
Cdd:PRK10789 486 TEHQILHNLRQW--GEGRTVIISAHRL 510
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
2-193 |
7.18e-07 |
|
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: 49.85 E-value: 7.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 2 EIVKTTQLIKVFKGAEAVNE-VNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKpTSGKIELFGerIKNHRQHIQALKKI 80
Cdd:cd03289 2 QMTVKDLTAKYTEGGNAVLEnISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDG--VSWNSVPLQKWRKA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 81 GSLVESPSYYAHLTARENLEVLRK-----ILGVS-----KNRVDEVLDIVKLAKEANRPVkgFSLGMKQRLGIASALLGN 150
Cdd:cd03289 79 FGVIPQKVFIFSGTFRKNLDPYGKwsdeeIWKVAeevglKSVIEQFPGQLDFVLVDGGCV--LSHGHKQLMCLARSVLSK 156
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1265835877 151 PRLLILDEPTNGLDPAGIQEIRSLIKEmpGKNGVTVLISSHLL 193
Cdd:cd03289 157 AKILLLDEPSAHLDPITYQVIRKTLKQ--AFADCTVILSEHRI 197
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
127-197 |
1.01e-06 |
|
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: 49.31 E-value: 1.01e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1265835877 127 NRPVKGFSLGMKQRLGIASALL---GNPRLLILDEPTNGLDPAGIQEIRSLIKEMPgKNGVTVLISSHLLYEID 197
Cdd:pfam13304 231 ELPAFELSDGTKRLLALLAALLsalPKGGLLLIDEPESGLHPKLLRRLLELLKELS-RNGAQLILTTHSPLLLD 303
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
13-196 |
1.32e-06 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 50.03 E-value: 1.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 13 FKGAEAVNEVNLSIKEGEIYGFLGPNGAGKTTTIRmllglmkPTSGKIELFGERIKNHrqHIQALKKIGSLVESPSYYAH 92
Cdd:PTZ00265 1239 EQDYQGDEEQNVGMKNVNEFSLTKEGGSGEDSTVF-------KNSGKILLDGVDICDY--NLKDLRNLFSIVSQEPMLFN 1309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 93 LTARENLE------VLRKILGVSK-NRVDEVLDIVKLAKEANRPVKGFSL--GMKQRLGIASALLGNPRLLILDEPTNGL 163
Cdd:PTZ00265 1310 MSIYENIKfgkedaTREDVKRACKfAAIDEFIESLPNKYDTNVGPYGKSLsgGQKQRIAIARALLREPKILLLDEATSSL 1389
|
170 180 190
....*....|....*....|....*....|...
gi 1265835877 164 DPAGIQEIRSLIKEMPGKNGVTVLISSHLLYEI 196
Cdd:PTZ00265 1390 DSNSEKLIEKTIVDIKDKADKTIITIAHRIASI 1422
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
36-192 |
1.69e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 47.94 E-value: 1.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 36 GPNGAGKTTTIRMLLGLMKPTSGKIELfgeriknHRQHIQALKK--IGSLVESPSYYAHLTARENLEVLRKILGvSKNRV 113
Cdd:PRK13541 33 GANGCGKSSLLRMIAGIMQPSSGNIYY-------KNCNINNIAKpyCTYIGHNLGLKLEMTVFENLKFWSEIYN-SAETL 104
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1265835877 114 DEVLDIVKLAKEANRPVKGFSLGMKQRLGIASALLGNPRLLILDEPTNGLDPAGIQEIRSLIKeMPGKNGVTVLISSHL 192
Cdd:PRK13541 105 YAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNNLIV-MKANSGGIVLLSSHL 182
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
36-191 |
2.60e-06 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 47.22 E-value: 2.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 36 GPNGAGKTTTIRMLlglmkptsgKIELFGERIKNHRQHIQALKKIGSlvESPSYYAHL----------TARENLEVLRKI 105
Cdd:cd03240 29 GQNGAGKTTIIEAL---------KYALTGELPPNSKGGAHDPKLIRE--GEVRAQVKLafenangkkyTITRSLAILENV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 106 LGVsknRVDEVLDIvkLAKEANRPVKG--FSLGMKQRLGIASALLGNPRLLILDEPTNGLDPAGIQE-IRSLIKEMPGKN 182
Cdd:cd03240 98 IFC---HQGESNWP--LLDMRGRCSGGekVLASLIIRLALAETFGSNCGILALDEPTTNLDEENIEEsLAEIIEERKSQK 172
|
....*....
gi 1265835877 183 GVTVLISSH 191
Cdd:cd03240 173 NFQLIVITH 181
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
128-191 |
2.65e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 48.63 E-value: 2.65e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1265835877 128 RPVKGFSLGMKQRLGIASALLGNPRLLILDEPTNGLDPAGIQEIRSLIKEMPGkngvTVLISSH 191
Cdd:PRK10636 145 RPVSDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLDLDAVIWLEKWLKSYQG----TLILISH 204
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
35-222 |
2.90e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 48.70 E-value: 2.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 35 LGPNGAGKTTTIRMLLGLMKPTSG--------KIELFGEriknhrQHIQALkkigSLVESPSYYahltarenleVLRKIL 106
Cdd:PLN03073 541 VGPNGIGKSTILKLISGELQPSSGtvfrsakvRMAVFSQ------HHVDGL----DLSSNPLLY----------MMRCFP 600
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 107 GVSKNRVDEVLDIVKLAKE-ANRPVKGFSLGMKQRLGIASALLGNPRLLILDEPTNGLDpagIQEIRSLIKEMPGKNGvT 185
Cdd:PLN03073 601 GVPEQKLRAHLGSFGVTGNlALQPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLD---LDAVEALIQGLVLFQG-G 676
|
170 180 190
....*....|....*....|....*....|....*...
gi 1265835877 186 VLISSHLLYEIDHLATQVGIITKGKML-FNGSIESLRK 222
Cdd:PLN03073 677 VLMVSHDEHLISGSVDELWVVSEGKVTpFHGTFHDYKK 714
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
127-215 |
2.97e-06 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 46.55 E-value: 2.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 127 NRPVKGFSLGMKQRLGIASALLGNPR--LLILDEPTNGLDPAGIQEIRSLIKEMpGKNGVTVLISSHLLYEIDHLATQVG 204
Cdd:cd03238 82 GQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGL-IDLGNTVILIEHNLDVLSSADWIID 160
|
90
....*....|....*.
gi 1265835877 205 I-----ITKGKMLFNG 215
Cdd:cd03238 161 FgpgsgKSGGKVVFSG 176
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
19-222 |
4.62e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 48.05 E-value: 4.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 19 VNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPtsgkIELFGERIKnhrqhiqalkkiGSLVESP--SYYAHLTAR 96
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSH----AETSSVVIR------------GSVAYVPqvSWIFNATVR 696
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 97 ENL------EVLRKILGVSKNRVDEVLDIV---KLAKEANRPVKgFSLGMKQRLGIASALLGNPRLLILDEPTNGLDP-A 166
Cdd:PLN03232 697 ENIlfgsdfESERYWRAIDVTALQHDLDLLpgrDLTEIGERGVN-ISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAhV 775
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1265835877 167 GIQEIRSLIK-EMPGKNGVTVLISSHLLYEIDhlatQVGIITKGKMLFNGSIESLRK 222
Cdd:PLN03232 776 AHQVFDSCMKdELKGKTRVLVTNQLHFLPLMD----RIILVSEGMIKEEGTFAELSK 828
|
|
| COG4938 |
COG4938 |
Predicted ATPase [General function prediction only]; |
34-191 |
9.23e-06 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443965 [Multi-domain] Cd Length: 277 Bit Score: 46.50 E-value: 9.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 34 FLGPNGAGKTTTIRMLLGLMkptSGKIELFG-ERIKNHRQHIQALKKIGSLVESPSYYAH-LTARENLEVLRKILGVSKN 111
Cdd:COG4938 25 LIGPNGSGKSTLIQALLLLL---QSNFIYLPaERSGPARLYPSLVRELSDLGSRGEYTADfLAELENLEILDDKSKELLE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 112 RVDEVL-----------------DIVKLAKEANRPVK----GFslGMKQRLGIASALL---GNPRLLILDEPTNGLDPAG 167
Cdd:COG4938 102 QVEEWLekifpgkvevdassdlvRLVFRPSGNGKRIPlsnvGS--GVSELLPILLALLsaaKPGSLLIIEEPEAHLHPKA 179
|
170 180
....*....|....*....|....
gi 1265835877 168 IQEIRSLIKEMpGKNGVTVLISSH 191
Cdd:COG4938 180 QSALAELLAEL-ANSGVQVIIETH 202
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
15-191 |
1.13e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 46.78 E-value: 1.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 15 GAEAVNEVNLSIKEGEIYGFLGPNGAGKTTTIR-MLLGLMK--PTSGKI-----ELFG--------------ERIKNHRQ 72
Cdd:PLN03073 189 GRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRyMAMHAIDgiPKNCQIlhveqEVVGddttalqcvlntdiERTQLLEE 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 73 HIQALKKIGSLvESPSYYAHLTAREN-----------LEVLRKILGV-----SKNRVDEVLDIVKLAKEAN-RPVKGFSL 135
Cdd:PLN03073 269 EAQLVAQQREL-EFETETGKGKGANKdgvdkdavsqrLEEIYKRLELidaytAEARAASILAGLSFTPEMQvKATKTFSG 347
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1265835877 136 GMKQRLGIASALLGNPRLLILDEPTNGLDPAGIQEIRSLIKEMPGkngvTVLISSH 191
Cdd:PLN03073 348 GWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPK----TFIVVSH 399
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
19-164 |
1.99e-05 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 46.09 E-value: 1.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 19 VNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELFGERIKNHRQH-IQ--ALKK---IGSLVESPSYYAH 92
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSVAYVPQQAwIQndSLREnilFGKALNEKYYQQV 733
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1265835877 93 LTARENLEVLRKILGVSKNRVDEvldivklakeanrpvKGFSL--GMKQRLGIASALLGNPRLLILDEPTNGLD 164
Cdd:TIGR00957 734 LEACALLPDLEILPSGDRTEIGE---------------KGVNLsgGQKQRVSLARAVYSNADIYLFDDPLSAVD 792
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
87-191 |
2.53e-05 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 45.31 E-value: 2.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 87 PSYYAHLtARENLEVLRKILGVSKNRVDEVLDIVKLAKEANRpvkgFSLGMKQR------------------LGIASALL 148
Cdd:COG4637 200 AAVLATL-RETHPERFERILEALRDAFPGFEDIEVEPDEDGR----VLLEFREKgldrpfparelsdgtlrfLALLAALL 274
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1265835877 149 GN--PRLLILDEPTNGLDPAGIQEIRSLIKEMPGKngVTVLISSH 191
Cdd:COG4637 275 SPrpPPLLCIEEPENGLHPDLLPALAELLREASER--TQVIVTTH 317
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
14-164 |
3.92e-05 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 44.40 E-value: 3.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 14 KGAEAVNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGL--MKPTSGKIELFGERIKNHRQHIQALKKI----GSLVESP 87
Cdd:PRK09580 12 EDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKDLLELSPEDRAGEGIfmafQYPVEIP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 88 SYYAHLTARENLEVLRKILGVS-------KNRVDEVLDIVKLAKE-ANRPVK-GFSLGMKQRLGIASALLGNPRLLILDE 158
Cdd:PRK09580 92 GVSNQFFLQTALNAVRSYRGQEpldrfdfQDLMEEKIALLKMPEDlLTRSVNvGFSGGEKKRNDILQMAVLEPELCILDE 171
|
....*.
gi 1265835877 159 PTNGLD 164
Cdd:PRK09580 172 SDSGLD 177
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
19-191 |
4.07e-05 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 45.12 E-value: 4.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 19 VNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMkPTSGkielfGERIKNHRQhiqalkKIGSLVESPsYYAHLTAREN 98
Cdd:TIGR00954 468 IESLSFEVPSGNNLLICGPNGCGKSSLFRILGELW-PVYG-----GRLTKPAKG------KLFYVPQRP-YMTLGTLRDQ 534
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 99 L-------EVLRKilGVSKNRVDEVLDIVKLAKEANRPVkGF----------SLGMKQRLGIASALLGNPRLLILDEPTN 161
Cdd:TIGR00954 535 IiypdsseDMKRR--GLSDKDLEQILDNVQLTHILEREG-GWsavqdwmdvlSGGEKQRIAMARLFYHKPQFAILDECTS 611
|
170 180 190
....*....|....*....|....*....|
gi 1265835877 162 GLDPAGIQEIRSLIKEMpgknGVTVLISSH 191
Cdd:TIGR00954 612 AVSVDVEGYMYRLCREF----GITLFSVSH 637
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
22-305 |
5.79e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 44.73 E-value: 5.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 22 VNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELFGERIknhrqhiqalkkigSLVESPSYYAHLTARENL-- 99
Cdd:PLN03130 636 INLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDASVVIRGTV--------------AYVPQVSWIFNATVRDNIlf 701
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 100 ------EVLRKILGVSKNRVDevLDIV---KLAKEANRPVKgFSLGMKQRLGIASALLGNPRLLILDEPTNGLDP-AGIQ 169
Cdd:PLN03130 702 gspfdpERYERAIDVTALQHD--LDLLpggDLTEIGERGVN-ISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAhVGRQ 778
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 170 EIRSLIK-EMPGKNGVTVLISSHLLYEIDHLAtqvgIITKGKMLFNGSIESLRKKAK--HQVAFTTGEIEKSKTillang 246
Cdd:PLN03130 779 VFDKCIKdELRGKTRVLVTNQLHFLSQVDRII----LVHEGMIKEEGTYEELSNNGPlfQKLMENAGKMEEYVE------ 848
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1265835877 247 fvptiDKNSLLLDYIDHEQVAHLVYQLVQENVSIYRVEEKSKSledIFLKLTSEENGYV 305
Cdd:PLN03130 849 -----ENGEEEDDQTSSKPVANGNANNLKKDSSSKKKSKEGKS---VLIKQEERETGVV 899
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
6-166 |
6.29e-05 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 43.66 E-value: 6.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 6 TTQLIKVFKGAEAV-NEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLG-LMKP-------TSGKIELFGE---RIKNHRqh 73
Cdd:PRK13547 3 TADHLHVARRHRAIlRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGdLTGGgaprgarVTGDVTLNGEplaAIDAPR-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 74 IQALKKIGSLVESPSY------------YAHltARENLEVLRKILGVsknrVDEVLDIVKLAKEANRPVKGFSLGMKQRL 141
Cdd:PRK13547 81 LARLRAVLPQAAQPAFafsareivllgrYPH--ARRAGALTHRDGEI----AWQALALAGATALVGRDVTTLSGGELARV 154
|
170 180 190
....*....|....*....|....*....|....
gi 1265835877 142 GIASAL---------LGNPRLLILDEPTNGLDPA 166
Cdd:PRK13547 155 QFARVLaqlwpphdaAQPPRYLLLDEPTAALDLA 188
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
22-196 |
6.90e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 44.73 E-value: 6.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 22 VNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELFGERIKnhRQHIQALKKIGSLV-ESPSYYAHlTARENLE 100
Cdd:PLN03130 1258 LSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDIS--KFGLMDLRKVLGIIpQAPVLFSG-TVRFNLD 1334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 101 VLRKilgvsKNRVD--EVL------DIVK-----LAKEANRPVKGFSLGMKQRLGIASALLGNPRLLILDEPTNGLD--- 164
Cdd:PLN03130 1335 PFNE-----HNDADlwESLerahlkDVIRrnslgLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDvrt 1409
|
170 180 190
....*....|....*....|....*....|...
gi 1265835877 165 PAGIQE-IRSLIKempgknGVTVLISSHLLYEI 196
Cdd:PLN03130 1410 DALIQKtIREEFK------SCTMLIIAHRLNTI 1436
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
19-192 |
7.51e-05 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 44.01 E-value: 7.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 19 VNEVNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLM--KPTSGKIELFGE--RIKNHRQHIQAlkKIGSLVES-PSYYAHL 93
Cdd:NF040905 276 VDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFGRSygRNISGTVFKDGKevDVSTVSDAIDA--GLAYVTEDrKGYGLNL 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 94 --TARENLeVLRKILGVSKNRVdevLDIVKLAKEANR--------------PVKGFSLGMKQRLGIASALLGNPRLLILD 157
Cdd:NF040905 354 idDIKRNI-TLANLGKVSRRGV---IDENEEIKVAEEyrkkmniktpsvfqKVGNLSGGNQQKVVLSKWLFTDPDVLILD 429
|
170 180 190
....*....|....*....|....*....|....*..
gi 1265835877 158 EPTNGLDPAGIQEIRSLIKEMP--GKnGVtVLISSHL 192
Cdd:NF040905 430 EPTRGIDVGAKYEIYTIINELAaeGK-GV-IVISSEL 464
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
14-191 |
4.33e-04 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 40.70 E-value: 4.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 14 KGAEAVN--EVNLSIKEGEIYGFLGPNGAGKTT----TI----------------RMLLGLM-KPTSGKIELFGERI--- 67
Cdd:cd03270 4 RGAREHNlkNVDVDIPRNKLVVITGVSGSGKSSlafdTIyaegqrryveslsayaRQFLGQMdKPDVDSIEGLSPAIaid 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 68 -KNHRQHIQAlkKIGSLVESPSYYAHLTARENLevlrkilgvsKNRVDEVLDI----VKLAKEANRpvkgFSLGMKQRLG 142
Cdd:cd03270 84 qKTTSRNPRS--TVGTVTEIYDYLRLLFARVGI----------RERLGFLVDVglgyLTLSRSAPT----LSGGEAQRIR 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1265835877 143 IA----SALLGnpRLLILDEPTNGLDPAGIQEIRSLIKEMPGKnGVTVLISSH 191
Cdd:cd03270 148 LAtqigSGLTG--VLYVLDEPSIGLHPRDNDRLIETLKRLRDL-GNTVLVVEH 197
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
30-196 |
5.12e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 41.89 E-value: 5.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 30 EIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELFGERIKnhRQHIQALKKIGSLV-ESPSYYAHlTARENLEVLRKilgv 108
Cdd:PLN03232 1263 EKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVA--KFGLTDLRRVLSIIpQSPVLFSG-TVRFNIDPFSE---- 1335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 109 sKNRVD--------EVLDIVK-----LAKEANRPVKGFSLGMKQRLGIASALLGNPRLLILDEPTNGLDPAGIQEIRSLI 175
Cdd:PLN03232 1336 -HNDADlwealeraHIKDVIDrnpfgLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTI 1414
|
170 180
....*....|....*....|.
gi 1265835877 176 KEMpgKNGVTVLISSHLLYEI 196
Cdd:PLN03232 1415 REE--FKSCTMLVIAHRLNTI 1433
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
10-191 |
1.33e-03 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 39.99 E-value: 1.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 10 IKVFKGaeaVNEVNLSIKEGeIYGFLGPNGAGKTTT---IRMLLGLMKPTSGKIELF--GERIKNHRQHIQA-----LKK 79
Cdd:COG3593 8 IKNFRS---IKDLSIELSDD-LTVLVGENNSGKSSIleaLRLLLGPSSSRKFDEEDFylGDDPDLPEIEIELtfgslLSR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 80 IGSLVESPSYYAHLTA---------RENLEVLRKIL---------------GVSKNRVDEVLDIVKL--AKEANRPVKGF 133
Cdd:COG3593 84 LLRLLLKEEDKEELEEaleelneelKEALKALNELLseylkelldgldlelELSLDELEDLLKSLSLriEDGKELPLDRL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1265835877 134 SLGMKQRLGIA--SALL-----GNPRLLILDEPTNGLDPAGIQEIRSLIKEMPGKNgVTVLISSH 191
Cdd:COG3593 164 GSGFQRLILLAllSALAelkraPANPILLIEEPEAHLHPQAQRRLLKLLKELSEKP-NQVIITTH 227
|
|
| DUF4162 |
pfam13732 |
Domain of unknown function (DUF4162); This domain is found at the C-terminus of bacterial ABC ... |
215-298 |
1.43e-03 |
|
Domain of unknown function (DUF4162); This domain is found at the C-terminus of bacterial ABC transporter proteins. The function is not known.
Pssm-ID: 463971 [Multi-domain] Cd Length: 82 Bit Score: 36.80 E-value: 1.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 215 GSIESLRKK-AKHQVAFTTGEIEKSKTILlanGFVPTIDKNSLLLDYIDHEQVAHLVYQLVQENVSIYRVEEKSKSLEDI 293
Cdd:pfam13732 1 GTLEEIKRSyGRNRIEVETADAEELLELP---GVEEVEEEGGGLELKLEDEEAANELLAALLSGGEIRSFEEEEPSLNDI 77
|
....*
gi 1265835877 294 FLKLT 298
Cdd:pfam13732 78 FIEKV 82
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
22-220 |
1.70e-03 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 39.12 E-value: 1.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 22 VNLSIKEGEIYGFLGPNGAGKTTTIRMLLGLMKPTSGKIELFGerIKNHRQHIQALK-KIGSLVESPSYYAHlTARENLE 100
Cdd:cd03288 40 VKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDG--IDISKLPLHTLRsRLSIILQDPILFSG-SIRFNLD 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 101 VLRKilgVSKNRVDEVLDIVKLaKEANRPVKG------------FSLGMKQRLGIASALLGNPRLLILDEPTNGLDPAGI 168
Cdd:cd03288 117 PECK---CTDDRLWEALEIAQL-KNMVKSLPGgldavvteggenFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATE 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1265835877 169 QEIRSLIkeMPGKNGVTVLISSHLLYEIDHlATQVGIITKGKMLFNGSIESL 220
Cdd:cd03288 193 NILQKVV--MTAFADRTVVTIAHRVSTILD-ADLVLVLSRGILVECDTPENL 241
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
128-191 |
4.46e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 38.66 E-value: 4.46e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1265835877 128 RPVKGFSLGMKQRLGIASALLG---NPRLLILDEPTNGLDP----AGIQEIRSLIKEmpgknGVTVLISSH 191
Cdd:PRK00635 805 RPLSSLSGGEIQRLKLAYELLApskKPTLYVLDEPTTGLHThdikALIYVLQSLTHQ-----GHTVVIIEH 870
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
36-193 |
9.24e-03 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 36.18 E-value: 9.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 36 GPNGAGKTTTIRMLLglmkptsgkielFGERIKNHRQHIQALKKIGSLVESPSYYAHLTarenlevlrkilgvsknrvde 115
Cdd:cd03227 28 GPNGSGKSTILDAIG------------LALGGAQSATRRRSGVKAGCIVAAVSAELIFT--------------------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265835877 116 vldivklakeanrpVKGFSLGMKQRLGIASAL---LGNPR-LLILDEPTNGLDPAGIQEIRSLIKEMpGKNGVTVLISSH 191
Cdd:cd03227 75 --------------RLQLSGGEKELSALALILalaSLKPRpLYILDEIDRGLDPRDGQALAEAILEH-LVKGAQVIVITH 139
|
..
gi 1265835877 192 LL 193
Cdd:cd03227 140 LP 141
|
|
| |
