|
Name |
Accession |
Description |
Interval |
E-value |
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
1-318 |
0e+00 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 501.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 1 MIRFDNVSKKYNEDKIAVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEKRISDYDIHELRWDIGY 80
Cdd:COG1125 1 MIEFENVTKRYPDGTVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRDLDPVELRRRIGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 81 VLQQIALFPHMTIEENIAIVPELKKWDKDKIHDRITELLDSVGLDPESYRHRKPAELSGGEQQRVGVVRALAADPGIILM 160
Cdd:COG1125 81 VIQQIGLFPHMTVAENIATVPRLLGWDKERIRARVDELLELVGLDPEEYRDRYPHELSGGQQQRVGVARALAADPPILLM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 161 DEPFSALDPISRQRLQQDISALQKKIKKTIVFVTHDMQEALALGDRICVMQDGEIVQVATPQEIIKNPENDFVKDFLASG 240
Cdd:COG1125 161 DEPFGALDPITREQLQDELLRLQRELGKTIVFVTHDIDEALKLGDRIAVMREGRIVQYDTPEEILANPANDFVADFVGAD 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489843944 241 HAFNTPILegsFTVNDLIDADLFYAyqtsdgSLGISLTDPVENLVRRvaEEQSIPVLDEAtGEFVGTITNKHVMQFLA 318
Cdd:COG1125 241 RGLRRLSL---LRVEDLMLPEPPTV------SPDASLREALSLMLER--GVDWLLVVDED-GRPLGWLTLEDLLRALA 306
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
2-243 |
3.27e-138 |
|
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: 391.28 E-value: 3.27e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 2 IRFDNVSKKYNEDKIAVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEKRISDYDIHELRWDIGYV 81
Cdd:cd03295 1 IEFENVTKRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 82 LQQIALFPHMTIEENIAIVPELKKWDKDKIHDRITELLDSVGLDPESYRHRKPAELSGGEQQRVGVVRALAADPGIILMD 161
Cdd:cd03295 81 IQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLDPAEFADRYPHELSGGQQQRVGVARALAADPPLLLMD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 162 EPFSALDPISRQRLQQDISALQKKIKKTIVFVTHDMQEALALGDRICVMQDGEIVQVATPQEIIKNPENDFVKDFLASGH 241
Cdd:cd03295 161 EPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDFVAEFVGADR 240
|
..
gi 489843944 242 AF 243
Cdd:cd03295 241 LL 242
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-237 |
4.81e-110 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 323.97 E-value: 4.81e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 1 MIRFDNVSKKYNeDKIAVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEKRISDYDIHElRwDIGY 80
Cdd:COG3842 5 ALELENVSKRYG-DVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEK-R-NVGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 81 VLQQIALFPHMTIEENIAIVPELKKWDKDKIHDRITELLDSVGLdpESYRHRKPAELSGGEQQRVGVVRALAADPGIILM 160
Cdd:COG3842 82 VFQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGL--EGLADRYPHQLSGGQQQRVALARALAPEPRVLLL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489843944 161 DEPFSALDPISRQRLQQDISALQKKIKKTIVFVTHDMQEALALGDRICVMQDGEIVQVATPQEIIKNPENDFVKDFL 237
Cdd:COG3842 160 DEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEIYERPATRFVADFI 236
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-239 |
1.01e-102 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 305.07 E-value: 1.01e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 1 MIRFDNVSKKYNEDKiAVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEKRISDYDIHElRwDIGY 80
Cdd:COG3839 3 SLELENVSKSYGGVE-ALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKD-R-NIAM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 81 VLQQIALFPHMTIEENIAIVPELKKWDKDKIHDRITELLDSVGLDPesYRHRKPAELSGGEQQRVGVVRALAADPGIILM 160
Cdd:COG3839 80 VFQSYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLED--LLDRKPKQLSGGQRQRVALGRALVREPKVFLL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489843944 161 DEPFSALDPISRQRLQQDISALQKKIKKTIVFVTHDMQEALALGDRICVMQDGEIVQVATPQEIIKNPENDFVKDFLAS 239
Cdd:COG3839 158 DEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGTPEELYDRPANLFVAGFIGS 236
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
15-237 |
9.05e-100 |
|
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Functionally, this transport system is involved in osmoregulation. Under conditions of stress, the organism recruits these transport system to accumulate glycine betaine and other solutes which offer osmo-protection. It has been demonstrated that glycine betaine uptake is accompanied by symport with sodium ions. The locus has been named variously as proU or opuA. A gene library from L.lactis functionally complements an E.coli proU mutant. The comlementing locus is similar to a opuA locus in B.sutlis. This clarifies the differences in nomenclature. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 130254 [Multi-domain] Cd Length: 363 Bit Score: 298.30 E-value: 9.05e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 15 KIAVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEKRISDYDIHELRW----DIGYVLQQIALFPH 90
Cdd:TIGR01186 6 KKGVNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEPTAGQIFIDGENIMKQSPVELREvrrkKIGMVFQQFALFPH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 91 MTIEENIAIVPELKKWDKDKIHDRITELLDSVGLdpESYRHRKPAELSGGEQQRVGVVRALAADPGIILMDEPFSALDPI 170
Cdd:TIGR01186 86 MTILQNTSLGPELLGWPEQERKEKALELLKLVGL--EEYEHRYPDELSGGMQQRVGLARALAAEPDILLMDEAFSALDPL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489843944 171 SRQRLQQDISALQKKIKKTIVFVTHDMQEALALGDRICVMQDGEIVQVATPQEIIKNPENDFVKDFL 237
Cdd:TIGR01186 164 IRDSMQDELKKLQATLQKTIVFITHDLDEAIRIGDRIVIMKAGEIVQVGTPDEILRNPANEYVEEFI 230
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
1-318 |
9.59e-99 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 296.24 E-value: 9.59e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 1 MIRFDNVSK-------------KYNEDK----------IAVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTG 57
Cdd:COG4175 3 KIEVRNLYKifgkrperalkllDQGKSKdeilektgqtVGVNDASFDVEEGEIFVIMGLSGSGKSTLVRCLNRLIEPTAG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 58 TIYINEKRISDYDIHEL----RWDIGYVLQQIALFPHMTIEENIAIVPELKKWDKDKIHDRITELLDSVGLDPesYRHRK 133
Cdd:COG4175 83 EVLIDGEDITKLSKKELrelrRKKMSMVFQHFALLPHRTVLENVAFGLEIQGVPKAERRERAREALELVGLAG--WEDSY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 134 PAELSGGEQQRVGVVRALAADPGIILMDEPFSALDPISRQRLQQDISALQKKIKKTIVFVTHDMQEALALGDRICVMQDG 213
Cdd:COG4175 161 PDELSGGMQQRVGLARALATDPDILLMDEAFSALDPLIRREMQDELLELQAKLKKTIVFITHDLDEALRLGDRIAIMKDG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 214 EIVQVATPQEIIKNPENDFVKDFLA---------------SGHAFNTPILEGSFTVNDLIDADLFYAYQTSDGS--LGI- 275
Cdd:COG4175 241 RIVQIGTPEEILTNPANDYVADFVEdvdrskvltagsvmrPPEAVVSEKDGPRVALRRMREEGISSLYVVDRDRrlLGVv 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 276 --------------------------SLTDPVENLVRRVAE-EQSIPVLDEAtGEFVGTITNKHVMQFLA 318
Cdd:COG4175 321 taddaleavkgekdleeilltdvptvSPDTPLRDLLPLVAEsPYPLAVVDED-GRLLGVISRGSLLAALA 389
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
2-219 |
1.57e-96 |
|
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: 284.41 E-value: 1.57e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 2 IRFDNVSKKYNeDKIAVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEKRISDYDIHelRWDIGYV 81
Cdd:cd03259 1 LELKGLSKTYG-SVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE--RRNIGMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 82 LQQIALFPHMTIEENIAIVPELKKWDKDKIHDRITELLDSVGLDPesYRHRKPAELSGGEQQRVGVVRALAADPGIILMD 161
Cdd:cd03259 78 FQDYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEG--LLNRYPHELSGGQQQRVALARALAREPSLLLLD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489843944 162 EPFSALDPISRQRLQQDISALQKKIKKTIVFVTHDMQEALALGDRICVMQDGEIVQVA 219
Cdd:cd03259 156 EPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
16-236 |
7.72e-95 |
|
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: 282.22 E-value: 7.72e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 16 IAVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEK---RISDYDIHELRW-DIGYVLQQIALFPHM 91
Cdd:cd03294 38 VGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQdiaAMSRKELRELRRkKISMVFQSFALLPHR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 92 TIEENIAIVPELKKWDKDKIHDRITELLDSVGLdpESYRHRKPAELSGGEQQRVGVVRALAADPGIILMDEPFSALDPIS 171
Cdd:cd03294 118 TVLENVAFGLEVQGVPRAEREERAAEALELVGL--EGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLI 195
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489843944 172 RQRLQQDISALQKKIKKTIVFVTHDMQEALALGDRICVMQDGEIVQVATPQEIIKNPENDFVKDF 236
Cdd:cd03294 196 RREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDYVREF 260
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-229 |
3.14e-93 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 277.74 E-value: 3.14e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 1 MIRFDNVSKKY---NEDKIAVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEKRIsdydiHELRWD 77
Cdd:COG1116 7 ALELRGVSKRFptgGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPV-----TGPGPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 78 IGYVLQQIALFPHMTIEENIAIVPELKKWDKDKIHDRITELLDSVGLdpESYRHRKPAELSGGEQQRVGVVRALAADPGI 157
Cdd:COG1116 82 RGVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGL--AGFEDAYPHQLSGGMRQRVAIARALANDPEV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 158 ILMDEPFSALDPISRQRLQQDISALQKKIKKTIVFVTHDMQEALALGDRICVMQDG-----EIVQVATP----QEIIKNP 228
Cdd:COG1116 160 LLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFLADRVVVLSARpgrivEEIDVDLPrprdRELRTSP 239
|
.
gi 489843944 229 E 229
Cdd:COG1116 240 E 240
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
2-237 |
2.30e-92 |
|
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: 274.50 E-value: 2.30e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 2 IRFDNVSKKYNeDKIAVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEKRISDYDIHELRwdIGYV 81
Cdd:cd03300 1 IELENVSKFYG-GFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKRP--VNTV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 82 LQQIALFPHMTIEENIAIVPELKKWDKDKIHDRITELLDSVGLdpESYRHRKPAELSGGEQQRVGVVRALAADPGIILMD 161
Cdd:cd03300 78 FQNYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQL--EGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLD 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489843944 162 EPFSALDPISRQRLQQDISALQKKIKKTIVFVTHDMQEALALGDRICVMQDGEIVQVATPQEIIKNPENDFVKDFL 237
Cdd:cd03300 156 EPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPANRFVADFI 231
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
2-210 |
3.48e-88 |
|
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: 263.56 E-value: 3.48e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 2 IRFDNVSKKY---NEDKIAVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEKRISdydihELRWDI 78
Cdd:cd03293 1 LEVRNVSKTYgggGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVT-----GPGPDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 79 GYVLQQIALFPHMTIEENIAIVPELKKWDKDKIHDRITELLDSVGLdpESYRHRKPAELSGGEQQRVGVVRALAADPGII 158
Cdd:cd03293 76 GYVFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGL--SGFENAYPHQLSGGMRQRVALARALAVDPDVL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 489843944 159 LMDEPFSALDPISRQRLQQDISALQKKIKKTIVFVTHDMQEALALGDRICVM 210
Cdd:cd03293 154 LLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVL 205
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
2-237 |
2.25e-86 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 263.55 E-value: 2.25e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 2 IRFDNVSKKYNEDKiAVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEKrisDYDIH----ELRwd 77
Cdd:COG1118 3 IEVRNISKRFGSFT-LLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGR---DLFTNlpprERR-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 78 IGYVLQQIALFPHMTIEENIAIVPELKKWDKDKIHDRITELLDSVGLdpESYRHRKPAELSGGEQQRVGVVRALAADPGI 157
Cdd:COG1118 77 VGFVFQHYALFPHMTVAENIAFGLRVRPPSKAEIRARVEELLELVQL--EGLADRYPSQLSGGQRQRVALARALAVEPEV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 158 ILMDEPFSALDPISRQRLQQDISALQKKIKKTIVFVTHDMQEALALGDRICVMQDGEIVQVATPQEIIKNPENDFVKDFL 237
Cdd:COG1118 155 LLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDRPATPFVARFL 234
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
5-251 |
5.30e-83 |
|
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ATP-binding protein is found in a number of genomes in operon-like contexts strongly suggesting a substrate specificity for 2-aminoethylphosphonate (2-AEP). The characterized PhnSTUV system is absent in the genomes in which this system is found. These genomes encode systems for the catabolism of 2-AEP, making the need for a 2-AEP-specific transporter likely. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274496 [Multi-domain] Cd Length: 353 Bit Score: 254.96 E-value: 5.30e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 5 DNVSKKYNeDKIAVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEKRISDYDIhELRwDIGYVLQQ 84
Cdd:TIGR03265 8 DNIRKRFG-AFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRLPP-QKR-DYGIVFQS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 85 IALFPHMTIEENIAIVPELKKWDKDKIHDRITELLDSVGLdPESyrHRK-PAELSGGEQQRVGVVRALAADPGIILMDEP 163
Cdd:TIGR03265 85 YALFPNLTVADNIAYGLKNRGMGRAEVAERVAELLDLVGL-PGS--ERKyPGQLSGGQQQRVALARALATSPGLLLLDEP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 164 FSALDPISRQRLQQDISALQKKIKKTIVFVTHDMQEALALGDRICVMQDGEIVQVATPQEIIKNPENDFVKDFLASGHAF 243
Cdd:TIGR03265 162 LSALDARVREHLRTEIRQLQRRLGVTTIMVTHDQEEALSMADRIVVMNHGVIEQVGTPQEIYRHPATPFVADFVGEVNWL 241
|
....*...
gi 489843944 244 NTPILEGS 251
Cdd:TIGR03265 242 PGTRGGGS 249
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-237 |
1.82e-78 |
|
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: 239.50 E-value: 1.82e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 1 MIRFDNVSKKYNeDKIAVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEKRISDYDIHEL---RWD 77
Cdd:COG1127 5 MIEVRNLTKSFG-DRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELyelRRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 78 IGYVLQQIALFPHMTIEENIAiVP--ELKKWDKDKIHDRITELLDSVGLdpESYRHRKPAELSGGEQQRVGVVRALAADP 155
Cdd:COG1127 84 IGMLFQGGALFDSLTVFENVA-FPlrEHTDLSEAEIRELVLEKLELVGL--PGAADKMPSELSGGMRKRVALARALALDP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 156 GIILMDEPFSALDPISRQRLQQDISALQKKIKKTIVFVTHDMQEALALGDRICVMQDGEIVQVATPQEiIKNPENDFVKD 235
Cdd:COG1127 161 EILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEE-LLASDDPWVRQ 239
|
..
gi 489843944 236 FL 237
Cdd:COG1127 240 FL 241
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
2-219 |
4.03e-78 |
|
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: 237.54 E-value: 4.03e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 2 IRFDNVSKKYnEDKIAVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEKRISDYDIHElRwDIGYV 81
Cdd:cd03301 1 VELENVTKRF-GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKD-R-DIAMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 82 LQQIALFPHMTIEENIAIVPELKKWDKDKIHDRITELLDSVGLdpESYRHRKPAELSGGEQQRVGVVRALAADPGIILMD 161
Cdd:cd03301 78 FQNYALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQI--EHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489843944 162 EPFSALDPISRQRLQQDISALQKKIKKTIVFVTHDMQEALALGDRICVMQDGEIVQVA 219
Cdd:cd03301 156 EPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
1-238 |
4.11e-78 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 238.36 E-value: 4.11e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 1 MIRFDNVSKKYNeDKIAVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEKRI--SDYDIHELRWDI 78
Cdd:COG1126 1 MIEIENLHKSFG-DLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLtdSKKDINKLRRKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 79 GYVLQQIALFPHMTIEENIAIVP-ELKKWDKDKIHDRITELLDSVGLdpESYRHRKPAELSGGEQQRVGVVRALAADPGI 157
Cdd:COG1126 80 GMVFQQFNLFPHLTVLENVTLAPiKVKKMSKAEAEERAMELLERVGL--ADKADAYPAQLSGGQQQRVAIARALAMEPKV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 158 ILMDEPFSALDPisrqRLQQDISALQKKIKK---TIVFVTHDMQEALALGDRICVMQDGEIVQVATPQEIIKNPENDFVK 234
Cdd:COG1126 158 MLFDEPTSALDP----ELVGEVLDVMRDLAKegmTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFENPQHERTR 233
|
....
gi 489843944 235 DFLA 238
Cdd:COG1126 234 AFLS 237
|
|
| tungstate_WtpC |
NF040840 |
tungstate ABC transporter ATP-binding protein WtpC; |
1-237 |
7.41e-78 |
|
tungstate ABC transporter ATP-binding protein WtpC;
Pssm-ID: 468779 [Multi-domain] Cd Length: 347 Bit Score: 241.52 E-value: 7.41e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 1 MIRFDNVSKKYNEDKIavNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEKRISDYDIhELRwDIGY 80
Cdd:NF040840 1 MIRIENLSKDWKEFKL--RDISLEVKEGEYFIILGPSGAGKTVLLELIAGIWPPDSGKIYLDGKDITNLPP-EKR-GIAY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 81 VLQQIALFPHMTIEENIAIVPELKKWDKDKIHDRITELLDSVGLdpESYRHRKPAELSGGEQQRVGVVRALAADPGIILM 160
Cdd:NF040840 77 VYQNYMLFPHKTVFENIAFGLKLRKVPKEEIERKVKEIMELLGI--SHLLHRKPRTLSGGEQQRVALARALIIEPKLLLL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489843944 161 DEPFSALDPISRQRLQQDISALQKKIKKTIVFVTHDMQEALALGDRICVMQDGEIVQVATPQEIIKNPENDFVKDFL 237
Cdd:NF040840 155 DEPLSALDVQTRDELIREMKRWHREFGFTAIHVTHNFEEALSLADRVGIMLNGRLSQVGDVREVFRRPKNEFVARFV 231
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
2-229 |
3.74e-76 |
|
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: 232.99 E-value: 3.74e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 2 IRFDNVSKKYNEDKIAVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEKRISDYDIHELRWDIGYV 81
Cdd:COG1122 1 IELENLSFSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 82 LQ----QiaLFpHMTIEENIAIVPELKKWDKDKIHDRITELLDSVGLdpESYRHRKPAELSGGEQQRVGVVRALAADPGI 157
Cdd:COG1122 81 FQnpddQ--LF-APTVEEDVAFGPENLGLPREEIRERVEEALELVGL--EHLADRPPHELSGGQKQRVAIAGVLAMEPEV 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489843944 158 ILMDEPFSALDPISRQRLQQDISALQKKiKKTIVFVTHDMQEALALGDRICVMQDGEIVQVATPQEIIKNPE 229
Cdd:COG1122 156 LVLDEPTAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDYE 226
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
2-226 |
1.21e-74 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 229.57 E-value: 1.21e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 2 IRFDNVSKKYNeDKIAVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEKRISDyDIHELRWDIGYV 81
Cdd:COG1131 1 IEVRGLTKRYG-DKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVAR-DPAEVRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 82 LQQIALFPHMTIEENIAIVPELKKWDKDKIHDRITELLDSVGLDPesYRHRKPAELSGGEQQRVGVVRALAADPGIILMD 161
Cdd:COG1131 79 PQEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTD--AADRKVGTLSGGMKQRLGLALALLHDPELLILD 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489843944 162 EPFSALDPISRQRLQQDISALQKKiKKTIVFVTHDMQEALALGDRICVMQDGEIVQVATPQEIIK 226
Cdd:COG1131 157 EPTSGLDPEARRELWELLRELAAE-GKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKA 220
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
2-237 |
4.69e-74 |
|
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: 227.99 E-value: 4.69e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 2 IRFDNVSKKYNEDKiaVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEKrisdyDIHEL---RWDI 78
Cdd:cd03299 1 LKVENLSKDWKEFK--LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGK-----DITNLppeKRDI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 79 GYVLQQIALFPHMTIEENIAIVPELKKWDKDKIHDRITELLDSVGLDpeSYRHRKPAELSGGEQQRVGVVRALAADPGII 158
Cdd:cd03299 74 SYVPQNYALFPHMTVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGID--HLLNRKPETLSGGEQQRVAIARALVVNPKIL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489843944 159 LMDEPFSALDPISRQRLQQDISALQKKIKKTIVFVTHDMQEALALGDRICVMQDGEIVQVATPQEIIKNPENDFVKDFL 237
Cdd:cd03299 152 LLDEPFSALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPKNEFVAEFL 230
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
2-239 |
1.63e-73 |
|
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: 226.84 E-value: 1.63e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 2 IRFDNVSKKYNeDKIAVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEKRISDYDIHELrwDIGYV 81
Cdd:cd03296 3 IEVRNVSKRFG-DFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQER--NVGFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 82 LQQIALFPHMTIEENIA----IVPELKKWDKDKIHDRITELLDSVGLDpeSYRHRKPAELSGGEQQRVGVVRALAADPGI 157
Cdd:cd03296 80 FQHYALFRHMTVFDNVAfglrVKPRSERPPEAEIRAKVHELLKLVQLD--WLADRYPAQLSGGQRQRVALARALAVEPKV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 158 ILMDEPFSALDPISRQRLQQDISALQKKIKKTIVFVTHDMQEALALGDRICVMQDGEIVQVATPQEIIKNPENDFVKDFL 237
Cdd:cd03296 158 LLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPASPFVYSFL 237
|
..
gi 489843944 238 AS 239
Cdd:cd03296 238 GE 239
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
2-249 |
3.13e-73 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 230.60 E-value: 3.13e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 2 IRFDNVSKKYnEDKIAVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEKRISDYDIhELRwDIGYV 81
Cdd:PRK09452 15 VELRGISKSF-DGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPA-ENR-HVNTV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 82 LQQIALFPHMTIEENIAIVPELKKWDKDKIHDRITELLDSVGLdpESYRHRKPAELSGGEQQRVGVVRALAADPGIILMD 161
Cdd:PRK09452 92 FQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQL--EEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLD 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 162 EPFSALDPISRQRLQQDISALQKKIKKTIVFVTHDMQEALALGDRICVMQDGEIVQVATPQEIIKNPENDFVKDFLASGH 241
Cdd:PRK09452 170 ESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNLFVARFIGEIN 249
|
....*...
gi 489843944 242 AFNTPILE 249
Cdd:PRK09452 250 IFDATVIE 257
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-239 |
8.86e-73 |
|
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: 233.64 E-value: 8.86e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 1 MIRFDNVSKKYN----EDKIAVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEKRISDY---DIHE 73
Cdd:COG1123 260 LLEVRNLSKRYPvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLsrrSLRE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 74 LRWDIGYVLQ--QIALFPHMTIEENIAIVPEL-KKWDKDKIHDRITELLDSVGLDPEsYRHRKPAELSGGEQQRVGVVRA 150
Cdd:COG1123 340 LRRRVQMVFQdpYSSLNPRMTVGDIIAEPLRLhGLLSRAERRERVAELLERVGLPPD-LADRYPHELSGGQRQRVAIARA 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 151 LAADPGIILMDEPFSALDPISRQRLQQDISALQKKIKKTIVFVTHDMQEALALGDRICVMQDGEIVQVATPQEIIKNPEN 230
Cdd:COG1123 419 LALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVFANPQH 498
|
....*....
gi 489843944 231 DFVKDFLAS 239
Cdd:COG1123 499 PYTRALLAA 507
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
2-214 |
1.75e-72 |
|
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: 222.06 E-value: 1.75e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 2 IRFDNVSKKYNEdKIAVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEKRISDYDIH--ELRWDIG 79
Cdd:cd03229 1 LELKNVSKRYGQ-KTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDElpPLRRRIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 80 YVLQQIALFPHMTIEENIAIVpelkkwdkdkihdritelldsvgldpesyrhrkpaeLSGGEQQRVGVVRALAADPGIIL 159
Cdd:cd03229 80 MVFQDFALFPHLTVLENIALG------------------------------------LSGGQQQRVALARALAMDPDVLL 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489843944 160 MDEPFSALDPISRQRLQQDISALQKKIKKTIVFVTHDMQEALALGDRICVMQDGE 214
Cdd:cd03229 124 LDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-216 |
5.48e-71 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 219.91 E-value: 5.48e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 1 MIRFDNVSKKYNEDKI---AVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEKRISDYDIHEL--- 74
Cdd:COG1136 4 LLELRNLTKSYGTGEGevtALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELarl 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 75 -RWDIGYVLQQIALFPHMTIEENIAIVPELKKWDKDKIHDRITELLDSVGLdpESYRHRKPAELSGGEQQRVGVVRALAA 153
Cdd:COG1136 84 rRRHIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGL--GDRLDHRPSQLSGGQQQRVAIARALVN 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489843944 154 DPGIILMDEPFSALDPISRQRLQQDISALQKKIKKTIVFVTHDMqEALALGDRICVMQDGEIV 216
Cdd:COG1136 162 RPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDP-ELAARADRVIRLRDGRIV 223
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
2-224 |
7.05e-71 |
|
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: 219.74 E-value: 7.05e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 2 IRFDNVSKKYNeDKIAVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPL-----TTGTIYINEKRI--SDYDIHEL 74
Cdd:cd03260 1 IELRDLNVYYG-DKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLipgapDEGEVLLDGKDIydLDVDVLEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 75 RWDIGYVLQQIALFPhMTIEENIAIVPEL-KKWDKDKIHDRITELLDSVGLDPESYRHRKPAELSGGEQQRVGVVRALAA 153
Cdd:cd03260 80 RRRVGMVFQKPNPFP-GSIYDNVAYGLRLhGIKLKEELDERVEEALRKAALWDEVKDRLHALGLSGGQQQRLCLARALAN 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489843944 154 DPGIILMDEPFSALDPISRQRLQQDISALQKKIkkTIVFVTHDMQEALALGDRICVMQDGEIVQVATPQEI 224
Cdd:cd03260 159 EPEVLLLDEPTSALDPISTAKIEELIAELKKEY--TIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
2-215 |
3.02e-70 |
|
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: 217.74 E-value: 3.02e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 2 IRFDNVSKKYNEDKI---AVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEKRISDYDIHEL---- 74
Cdd:cd03255 1 IELKNLSKTYGGGGEkvqALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 75 RWDIGYVLQQIALFPHMTIEENIAIVPELKKWDKDKIHDRITELLDSVGLdpESYRHRKPAELSGGEQQRVGVVRALAAD 154
Cdd:cd03255 81 RRHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGL--GDRLNHYPSELSGGQQQRVAIARALAND 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489843944 155 PGIILMDEPFSALDPISRQRLQQDISALQKKIKKTIVFVTHDMQEAlALGDRICVMQDGEI 215
Cdd:cd03255 159 PKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELA-EYADRIIELRDGKI 218
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
2-237 |
4.78e-68 |
|
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 212.74 E-value: 4.78e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 2 IRFDNVSKKYNeDKIAVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEKRISDYDIHelRWDIGYV 81
Cdd:TIGR00968 1 IEIANISKRFG-SFQALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGLEQPDSGRIRLNGQDATRVHAR--DRKIGFV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 82 LQQIALFPHMTIEENIAIVPELKKWDKDKIHDRITELLDSVGLdpESYRHRKPAELSGGEQQRVGVVRALAADPGIILMD 161
Cdd:TIGR00968 78 FQHYALFKHLTVRDNIAFGLEIRKHPKAKIKARVEELLELVQL--EGLGDRYPNQLSGGQRQRVALARALAVEPQVLLLD 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489843944 162 EPFSALDPISRQRLQQDISALQKKIKKTIVFVTHDMQEALALGDRICVMQDGEIVQVATPQEIIKNPENDFVKDFL 237
Cdd:TIGR00968 156 EPFGALDAKVRKELRSWLRKLHDEVHVTTVFVTHDQEEAMEVADRIVVMSNGKIEQIGSPDEVYDHPANPFVMSFL 231
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
2-236 |
5.64e-68 |
|
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: 212.36 E-value: 5.64e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 2 IRFDNVSKKYnEDKIAVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEKRI---SDYDIHELRWDI 78
Cdd:cd03261 1 IELRGLTKSF-GGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDIsglSEAELYRLRRRM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 79 GYVLQQIALFPHMTIEENIAiVP--ELKKWDKDKIHDRITELLDSVGLDPesYRHRKPAELSGGEQQRVGVVRALAADPG 156
Cdd:cd03261 80 GMLFQSGALFDSLTVFENVA-FPlrEHTRLSEEEIREIVLEKLEAVGLRG--AEDLYPAELSGGMKKRVALARALALDPE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 157 IILMDEPFSALDPISRQRLQQDISALQKKIKKTIVFVTHDMQEALALGDRICVMQDGEIVQVATPQEiIKNPENDFVKDF 236
Cdd:cd03261 157 LLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEE-LRASDDPLVRQF 235
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1-216 |
8.06e-68 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 211.45 E-value: 8.06e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 1 MIRFDNVSKKYNEDKIAVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEK---RISDYDIHELRWD 77
Cdd:COG2884 1 MIRFENVSKRYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQdlsRLKRREIPYLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 78 IGYVLQQIALFPHMTIEENIAIVPELKKWDKDKIHDRITELLDSVGLdpESYRHRKPAELSGGEQQRVGVVRALAADPGI 157
Cdd:COG2884 81 IGVVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGL--SDKAKALPHELSGGEQQRVAIARALVNRPEL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489843944 158 ILMDEPFSALDPISRQRLqqdISALQK--KIKKTIVFVTHDMQEALALGDRICVMQDGEIV 216
Cdd:COG2884 159 LLADEPTGNLDPETSWEI---MELLEEinRRGTTVLIATHDLELVDRMPKRVLELEDGRLV 216
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1-246 |
5.37e-67 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 213.40 E-value: 5.37e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 1 MIRFDNVSKKYNEDK---IAVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEKRISDYDIHEL--- 74
Cdd:COG1135 1 MIELENLSKTFPTKGgpvTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELraa 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 75 RWDIGYVLQQIALFPHMTIEENIAIVPELKKWDKDKIHDRITELLDSVGLdpESYRHRKPAELSGGEQQRVGVVRALAAD 154
Cdd:COG1135 81 RRKIGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGL--SDKADAYPSQLSGGQKQRVGIARALANN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 155 PGIILMDEPFSALDPISrqrlQQDISALQKKIKK----TIVFVTHDMQEALALGDRICVMQDGEIVQVATPQEIIKNPEN 230
Cdd:COG1135 159 PKVLLCDEATSALDPET----TRSILDLLKDINRelglTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVLDVFANPQS 234
|
250
....*....|....*.
gi 489843944 231 DFVKDFLASGHAFNTP 246
Cdd:COG1135 235 ELTRRFLPTVLNDELP 250
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-243 |
8.66e-66 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 207.35 E-value: 8.66e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 1 MIRFDNVSKKY---NEDKIAVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEKRISDYDIHELRWD 77
Cdd:COG1124 1 MLEVRNLSVSYgqgGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 78 IGYVLQQI--ALFPHMTIEENIAivpE-LKKWDKDKIHDRITELLDSVGLDPeSYRHRKPAELSGGEQQRVGVVRALAAD 154
Cdd:COG1124 81 VQMVFQDPyaSLHPRHTVDRILA---EpLRIHGLPDREERIAELLEQVGLPP-SFLDRYPHQLSGGQRQRVAIARALILE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 155 PGIILMDEPFSALDPIsrqrLQQDISALQKKIKK----TIVFVTHDMQEALALGDRICVMQDGEIVQVATPQEIIKNPEN 230
Cdd:COG1124 157 PELLLLDEPTSALDVS----VQAEILNLLKDLREerglTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAGPKH 232
|
250
....*....|...
gi 489843944 231 DFVKDFLASGHAF 243
Cdd:COG1124 233 PYTRELLAASLAF 245
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
6-239 |
1.16e-65 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 211.04 E-value: 1.16e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 6 NVSKKYNEDKIAvNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEKRISDydIHELRWDIGYVLQQI 85
Cdd:PRK11000 8 NVTKAYGDVVIS-KDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMND--VPPAERGVGMVFQSY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 86 ALFPHMTIEENIAIVPELKKWDKDKIHDRITELLDSVGLDpesyrH---RKPAELSGGEQQRVGVVRALAADPGIILMDE 162
Cdd:PRK11000 85 ALYPHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLA-----HlldRKPKALSGGQRQRVAIGRTLVAEPSVFLLDE 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489843944 163 PFSALDPISRQRLQQDISALQKKIKKTIVFVTHDMQEALALGDRICVMQDGEIVQVATPQEIIKNPENDFVKDFLAS 239
Cdd:PRK11000 160 PLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPANRFVAGFIGS 236
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
2-237 |
5.93e-65 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 208.78 E-value: 5.93e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 2 IRFDNVSKKYNEDKIaVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEKRISDydIHELRWDIGYV 81
Cdd:PRK10851 3 IEIANIKKSFGRTQV-LNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSR--LHARDRKVGFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 82 LQQIALFPHMTIEENIA----IVPELKKWDKDKIHDRITELLDSVGLdpESYRHRKPAELSGGEQQRVGVVRALAADPGI 157
Cdd:PRK10851 80 FQHYALFRHMTVFDNIAfgltVLPRRERPNAAAIKAKVTQLLEMVQL--AHLADRYPAQLSGGQKQRVALARALAVEPQI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 158 ILMDEPFSALDPISRQRLQQDISALQKKIKKTIVFVTHDMQEALALGDRICVMQDGEIVQVATPQEIIKNPENDFVKDFL 237
Cdd:PRK10851 158 LLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREPATRFVLEFM 237
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
3-214 |
3.00e-64 |
|
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: 201.93 E-value: 3.00e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 3 RFDNVSKKY-NEDKIAVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEKRISDYDIHELRWDIGYV 81
Cdd:cd03225 1 ELKNLSFSYpDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 82 LQ----QIAlfpHMTIEENIAIVPELKKWDKDKIHDRITELLDSVGLdpESYRHRKPAELSGGEQQRVGVVRALAADPGI 157
Cdd:cd03225 81 FQnpddQFF---GPTVEEEVAFGLENLGLPEEEIEERVEEALELVGL--EGLRDRSPFTLSGGQKQRVAIAGVLAMDPDI 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 489843944 158 ILMDEPFSALDPISRQRLQQDISALQKKiKKTIVFVTHDMQEALALGDRICVMQDGE 214
Cdd:cd03225 156 LLLDEPTAGLDPAGRRELLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
34-249 |
9.97e-64 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 204.65 E-value: 9.97e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 34 IGPSGCGKTTTLKMINRLIPLTTGTIYINEKRISDYDIHelRWDIGYVLQQIALFPHMTIEENIAIVPELKKWDKDKIHD 113
Cdd:TIGR01187 2 LGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPH--LRHINMVFQSYALFPHMTVEENVAFGLKMRKVPRAEIKP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 114 RITELLDSVGLdpESYRHRKPAELSGGEQQRVGVVRALAADPGIILMDEPFSALDPISRQRLQQDISALQKKIKKTIVFV 193
Cdd:TIGR01187 80 RVLEALRLVQL--EEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITFVFV 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489843944 194 THDMQEALALGDRICVMQDGEIVQVATPQEIIKNPENDFVKDFLASGHAFNTPILE 249
Cdd:TIGR01187 158 THDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFVARFIGEINVFEATVIE 213
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-239 |
3.10e-63 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 204.31 E-value: 3.10e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 1 MIRFDNVSKKYNEDKIAVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEKRISDYDIHElRwDIGY 80
Cdd:PRK11650 3 GLKLQAVRKSYDGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPAD-R-DIAM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 81 VLQQIALFPHMTIEENIAIVPELKKWDKDKIHDRITELLDSVGLDPesYRHRKPAELSGGEQQRVGVVRALAADPGIILM 160
Cdd:PRK11650 81 VFQNYALYPHMSVRENMAYGLKIRGMPKAEIEERVAEAARILELEP--LLDRKPRELSGGQRQRVAMGRAIVREPAVFLF 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489843944 161 DEPFSALDPISRQRLQQDISALQKKIKKTIVFVTHDMQEALALGDRICVMQDGEIVQVATPQEIIKNPENDFVKDFLAS 239
Cdd:PRK11650 159 DEPLSNLDAKLRVQMRLEIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGGVAEQIGTPVEVYEKPASTFVASFIGS 237
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
2-215 |
3.93e-63 |
|
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: 199.29 E-value: 3.93e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 2 IRFDNVSKKYNeDKIAVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEKRISD--YDIHELRWDIG 79
Cdd:cd03262 1 IEIKNLHKSFG-DFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDdkKNINELRQKVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 80 YVLQQIALFPHMTIEENIAIVP-ELKKWDKDKIHDRITELLDSVGLdpESYRHRKPAELSGGEQQRVGVVRALAADPGII 158
Cdd:cd03262 80 MVFQQFNLFPHLTVLENITLAPiKVKGMSKAEAEERALELLEKVGL--ADKADAYPAQLSGGQQQRVAIARALAMNPKVM 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 489843944 159 LMDEPFSALDPISRQRLQQDISALQKKiKKTIVFVTHDMQEALALGDRICVMQDGEI 215
Cdd:cd03262 158 LFDEPTSALDPELVGEVLDVMKDLAEE-GMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1-237 |
1.02e-62 |
|
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: 199.31 E-value: 1.02e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 1 MIRFDNVSKKYNeDKIAVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEKRISDYDIhELRWDIGY 80
Cdd:COG4555 1 MIEVENLSKKYG-KVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPR-EARRQIGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 81 VLQQIALFPHMTIEENIAIVPELKKWDKDKIHDRITELLDSVGLDPesYRHRKPAELSGGEQQRVGVVRALAADPGIILM 160
Cdd:COG4555 79 LPDERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEE--FLDRRVGELSTGMKKKVALARALVHDPKVLLL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489843944 161 DEPFSALDPISRQRLQQDISALqKKIKKTIVFVTHDMQEALALGDRICVMQDGEIVQVATPQEIIKNPENDFVKDFL 237
Cdd:COG4555 157 DEPTNGLDVMARRLLREILRAL-KKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREEIGEENLEDAF 232
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
2-215 |
1.39e-62 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 197.73 E-value: 1.39e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 2 IRFDNVSKKYNEDKIaVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEKRISDYDIHELRWDIGYV 81
Cdd:COG4619 1 LELEGLSFRVGGKPI-LSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAYV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 82 LQQIALFPhMTIEENIAIVPELKKWDKDKihDRITELLDSVGLdPESYRHRKPAELSGGEQQRVGVVRALAADPGIILMD 161
Cdd:COG4619 80 PQEPALWG-GTVRDNLPFPFQLRERKFDR--ERALELLERLGL-PPDILDKPVERLSGGERQRLALIRALLLQPDVLLLD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 489843944 162 EPFSALDPISRQRLQQDISALQKKIKKTIVFVTHDMQEALALGDRICVMQDGEI 215
Cdd:COG4619 156 EPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1-229 |
5.03e-62 |
|
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: 197.03 E-value: 5.03e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 1 MIRFDNVSKKY---NEDKIAVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEKRISDYDIHEL--- 74
Cdd:cd03258 1 MIELKNVSKVFgdtGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELrka 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 75 RWDIGYVLQQIALFPHMTIEENIAIVPELKKWDKDKIHDRITELLDSVGLdpESYRHRKPAELSGGEQQRVGVVRALAAD 154
Cdd:cd03258 81 RRRIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGL--EDKADAYPAQLSGGQKQRVGIARALANN 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489843944 155 PGIILMDEPFSALDPISRQRLQQDISALQKKIKKTIVFVTHDMQEALALGDRICVMQDGEIVQVATPQEIIKNPE 229
Cdd:cd03258 159 PKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFANPQ 233
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
1-216 |
5.69e-62 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 197.59 E-value: 5.69e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 1 MIRFDNVSKKYNEDKIAVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEKRISDY---DIHELRWD 77
Cdd:COG3638 2 MLELRNLSKRYPGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALrgrALRRLRRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 78 IGYVLQQIALFPHMTIEENI------------AIVPELKKWDKDKIHdritELLDSVGLDPESYRhrKPAELSGGEQQRV 145
Cdd:COG3638 82 IGMIFQQFNLVPRLSVLTNVlagrlgrtstwrSLLGLFPPEDRERAL----EALERVGLADKAYQ--RADQLSGGQQQRV 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489843944 146 GVVRALAADPGIILMDEPFSALDPISRQRLQQDISALQKKIKKTIVFVTHDMQEALALGDRICVMQDGEIV 216
Cdd:COG3638 156 AIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRVV 226
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1-230 |
1.31e-61 |
|
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: 196.80 E-value: 1.31e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 1 MIRFDNVSKKYNeDKIAVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEKRISDYDIHELRWDIGY 80
Cdd:COG1120 1 MLEAENLSVGYG-GRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 81 VLQQIALFPHMTIEENIAI--VPELKKWDKDKIHDR--ITELLDSVGLdpESYRHRKPAELSGGEQQRVGVVRALAADPG 156
Cdd:COG1120 80 VPQEPPAPFGLTVRELVALgrYPHLGLFGRPSAEDReaVEEALERTGL--EHLADRPVDELSGGERQRVLIARALAQEPP 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489843944 157 IILMDEPFSALDPISRQRLQQDISALQKKIKKTIVFVTHDMQEALALGDRICVMQDGEIVQVATPQEIIkNPEN 230
Cdd:COG1120 158 LLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEVL-TPEL 230
|
|
| 3a0107s01c2 |
TIGR00972 |
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein ... |
2-238 |
1.97e-61 |
|
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein of a family of ABC transporters for inorganic phosphate. In the model species Escherichia coli, a constitutive transporter for inorganic phosphate, with low affinity, is also present. The high affinity transporter that includes this polypeptide is induced when extracellular phosphate concentrations are low. The proteins most similar to the members of this family but not included appear to be amino acid transporters. [Transport and binding proteins, Anions]
Pssm-ID: 273372 [Multi-domain] Cd Length: 247 Bit Score: 195.98 E-value: 1.97e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 2 IRFDNVSKKYNEdKIAVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLT-----TGTIYINEKRISDY--DIHEL 74
Cdd:TIGR00972 2 IEIENLNLFYGE-KEALKNINLDIPKNQVTALIGPSGCGKSTLLRSLNRMNDLVpgvriEGKVLFDGQDIYDKkiDVVEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 75 RWDIGYVLQQIALFPhMTIEENIAIVPELKKW-DKDKIHDRITELLDSVGLDPE--SYRHRKPAELSGGEQQRVGVVRAL 151
Cdd:TIGR00972 81 RRRVGMVFQKPNPFP-MSIYDNIAYGPRLHGIkDKKELDEIVEESLKKAALWDEvkDRLHDSALGLSGGQQQRLCIARAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 152 AADPGIILMDEPFSALDPISRQRLQQDISALQKKIkkTIVFVTHDMQEALALGDRICVMQDGEIVQVATPQEIIKNPEND 231
Cdd:TIGR00972 160 AVEPEVLLLDEPTSALDPIATGKIEELIQELKKKY--TIVIVTHNMQQAARISDRTAFFYDGELVEYGPTEQIFTNPKEK 237
|
....*..
gi 489843944 232 FVKDFLA 238
Cdd:TIGR00972 238 RTEDYIS 244
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1-216 |
2.97e-61 |
|
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: 195.03 E-value: 2.97e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 1 MIRFDNVSKKYNEDKI---AVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEKRISDYDIHELRW- 76
Cdd:cd03257 1 LLEVKNLSVSFPTGGGsvkALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 77 --DIGYVLQ--QIALFPHMTIEENIA--IVPELKKWDKDKIHDRITELLDSVGLDPEsYRHRKPAELSGGEQQRVGVVRA 150
Cdd:cd03257 81 rkEIQMVFQdpMSSLNPRMTIGEQIAepLRIHGKLSKKEARKEAVLLLLVGVGLPEE-VLNRYPHELSGGQRQRVAIARA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489843944 151 LAADPGIILMDEPFSALDPISRQRLQQDISALQKKIKKTIVFVTHDMQEALALGDRICVMQDGEIV 216
Cdd:cd03257 160 LALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIV 225
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-229 |
5.57e-61 |
|
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: 202.83 E-value: 5.57e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 1 MIRFDNVSKKY-NEDKIAVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLT---TGTIYINEKRISDYDIHELRW 76
Cdd:COG1123 4 LLEVRDLSVRYpGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRGR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 77 DIGYVLQ--QIALFPhMTIEENIAIVPELKKWDKDKIHDRITELLDSVGLdpESYRHRKPAELSGGEQQRVGVVRALAAD 154
Cdd:COG1123 84 RIGMVFQdpMTQLNP-VTVGDQIAEALENLGLSRAEARARVLELLEAVGL--ERRLDRYPHQLSGGQRQRVAIAMALALD 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489843944 155 PGIILMDEPFSALDPISRQRLQQDISALQKKIKKTIVFVTHDMQEALALGDRICVMQDGEIVQVATPQEIIKNPE 229
Cdd:COG1123 161 PDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAPQ 235
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
16-325 |
6.17e-61 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 199.87 E-value: 6.17e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 16 IAVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINE---KRISDYDIHELRWD-IGYVLQQIALFPHM 91
Cdd:PRK10070 42 LGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGvdiAKISDAELREVRRKkIAMVFQSFALMPHM 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 92 TIEENIAIVPELKKWDKDKIHDRITELLDSVGLdpESYRHRKPAELSGGEQQRVGVVRALAADPGIILMDEPFSALDPIS 171
Cdd:PRK10070 122 TVLDNTAFGMELAGINAEERREKALDALRQVGL--ENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLI 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 172 RQRLQQDISALQKKIKKTIVFVTHDMQEALALGDRICVMQDGEIVQVATPQEIIKNPENDFVKDFL-------------- 237
Cdd:PRK10070 200 RTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFFrgvdisqvfsakdi 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 238 ----ASGHAFNTPILEGSFTVNDLIDADLFYAYQTS-----------------------------DGSLGISLTDPVENL 284
Cdd:PRK10070 280 arrtPNGLIRKTPGFGPRSALKLLQDEDREYGYVIErgnkfvgavsidslktaltqqqgldaaliDAPLAVDAQTPLSEL 359
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 489843944 285 VRRVAEEQ-SIPVLDEATgEFVGTITNKHVMQFLARHLESSG 325
Cdd:PRK10070 360 LSHVGQAPcAVPVVDEDQ-QYVGIISKGMLLRALDREGVNNG 400
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
2-260 |
7.14e-61 |
|
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: 195.75 E-value: 7.14e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 2 IRFDNVSKKYNED----KIAVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEKRISDYD---IHEL 74
Cdd:TIGR04521 1 IKLKNVSYIYQPGtpfeKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKkkkLKDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 75 RWDIGYVLQqialFPHM-----TIEENIAIVPELKKWDKDKIHDRITELLDSVGLDpESYRHRKPAELSGGEQQRVGVVR 149
Cdd:TIGR04521 81 RKKVGLVFQ----FPEHqlfeeTVYKDIAFGPKNLGLSEEEAEERVKEALELVGLD-EEYLERSPFELSGGQMRRVAIAG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 150 ALAADPGIILMDEPFSALDPISRQRLQQDISALQKKIKKTIVFVTHDMQEALALGDRICVMQDGEIVQVATPQEIIKNPE 229
Cdd:TIGR04521 156 VLAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVFSDVD 235
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 489843944 230 N------------DFVKDFLASGHAFNTPIlegsFTVNDLIDA 260
Cdd:TIGR04521 236 ElekigldvpeitELARKLKEKGLPVPKDP----LTVEEAADE 274
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1-237 |
9.08e-61 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 194.16 E-value: 9.08e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 1 MIRFDNVSKKYNEDKIaVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEKRISD--YDIHELRWDI 78
Cdd:PRK09493 1 MIEFKNVSKHFGPTQV-LHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDpkVDERLIRQEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 79 GYVLQQIALFPHMTIEENIAIVP-ELKKWDKDKIHDRITELLDSVGLdpESYRHRKPAELSGGEQQRVGVVRALAADPGI 157
Cdd:PRK09493 80 GMVFQQFYLFPHLTALENVMFGPlRVRGASKEEAEKQARELLAKVGL--AERAHHYPSELSGGQQQRVAIARALAVKPKL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 158 ILMDEPFSALDPISRQRLQQDISALQKKiKKTIVFVTHDMQEALALGDRICVMQDGEIVQVATPQEIIKNPENDFVKDFL 237
Cdd:PRK09493 158 MLFDEPTSALDPELRHEVLKVMQDLAEE-GMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPPSQRLQEFL 236
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
2-224 |
2.94e-60 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 192.33 E-value: 2.94e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 2 IRFDNVSKKYNED-KIAVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEKRIsDYDIHELRWDIGY 80
Cdd:cd03263 1 LQIRNLTKTYKKGtKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSI-RTDRKAARQSLGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 81 VLQQIALFPHMTIEENIAIVPELKKWDKDKIHDRITELLDSVGLdpESYRHRKPAELSGGEQQRVGVVRALAADPGIILM 160
Cdd:cd03263 80 CPQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGL--TDKANKRARTLSGGMKRKLSLAIALIGGPSVLLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489843944 161 DEPFSALDPISRQRLQQDISALQKkiKKTIVFVTHDMQEALALGDRICVMQDGEIVQVATPQEI 224
Cdd:cd03263 158 DEPTSGLDPASRRAIWDLILEVRK--GRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQEL 219
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2-237 |
9.03e-60 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 192.17 E-value: 9.03e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 2 IRFDNVSKKYNeDKIAVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPL-----TTGTIYINEKRI--SDYDIHEL 74
Cdd:COG1117 12 IEVRNLNVYYG-DKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDLipgarVEGEILLDGEDIydPDVDVVEL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 75 RWDIGYVLQQIALFPhMTIEENIAIVPELKKW-DKDKIHDRITELLDSVGL-----DpesyRHRKPA-ELSGGEQQRVGV 147
Cdd:COG1117 91 RRRVGMVFQKPNPFP-KSIYDNVAYGLRLHGIkSKSELDEIVEESLRKAALwdevkD----RLKKSAlGLSGGQQQRLCI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 148 VRALAADPGIILMDEPFSALDPISRQRLQQDISALQKKIkkTIVFVTHDMQEALALGDRICVMQDGEIVQVATPQEIIKN 227
Cdd:COG1117 166 ARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDY--TIVIVTHNMQQAARVSDYTAFFYLGELVEFGPTEQIFTN 243
|
250
....*....|
gi 489843944 228 PENDFVKDFL 237
Cdd:COG1117 244 PKDKRTEDYI 253
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
2-229 |
4.80e-59 |
|
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: 190.72 E-value: 4.80e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 2 IRFDNVSKKY-NEDKIAVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEKRISDYD-IHELRWDIG 79
Cdd:TIGR04520 1 IEVENVSFSYpESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLDEEnLWEIRKKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 80 YVLQ----QialFPHMTIEENIAIVPELKKWDKDKIHDRITELLDSVGLdpESYRHRKPAELSGGEQQRVGVVRALAADP 155
Cdd:TIGR04520 81 MVFQnpdnQ---FVGATVEDDVAFGLENLGVPREEMRKRVDEALKLVGM--EDFRDREPHLLSGGQKQRVAIAGVLAMRP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489843944 156 GIILMDEPFSALDPISRQRLQQDISALQKKIKKTIVFVTHDMQEAlALGDRICVMQDGEIVQVATPQEIIKNPE 229
Cdd:TIGR04520 156 DIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEA-VLADRVIVMNKGKIVAEGTPREIFSQVE 228
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-242 |
2.95e-57 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 185.84 E-value: 2.95e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 1 MIRFDNVSKKY---NEDKIAVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEKRISDYDIhelrwD 77
Cdd:COG4525 3 MLTVRHVSVRYpggGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGA-----D 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 78 IGYVLQQIALFPHMTIEENIAIVPELKKWDKDKIHDRITELLDSVGLdpESYRHRKPAELSGGEQQRVGVVRALAADPGI 157
Cdd:COG4525 78 RGVVFQKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGL--ADFARRRIWQLSGGMRQRVGIARALAADPRF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 158 ILMDEPFSALDPISRQRLQQDISALQKKIKKTIVFVTHDMQEALALGDRICVMQDGeivqvatPQEIIKNPENDFVKDFL 237
Cdd:COG4525 156 LLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHSVEEALFLATRLVVMSPG-------PGRIVERLELDFSRRFL 228
|
....*
gi 489843944 238 ASGHA 242
Cdd:COG4525 229 AGEDA 233
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
2-224 |
1.64e-56 |
|
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: 183.15 E-value: 1.64e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 2 IRFDNVSKKYNEDKIAVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEKRISDY---DIHELRWDI 78
Cdd:cd03256 1 IEVENLSKTYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLkgkALRQLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 79 GYVLQQIALFPHMTIEENI--AIVPELKKW--------DKDKIhdRITELLDSVGLDpeSYRHRKPAELSGGEQQRVGVV 148
Cdd:cd03256 81 GMIFQQFNLIERLSVLENVlsGRLGRRSTWrslfglfpKEEKQ--RALAALERVGLL--DKAYQRADQLSGGQQQRVAIA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489843944 149 RALAADPGIILMDEPFSALDPISRQRLQQDISALQKKIKKTIVFVTHDMQEALALGDRICVMQDGEIVQVATPQEI 224
Cdd:cd03256 157 RALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAEL 232
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
2-215 |
3.57e-56 |
|
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: 179.90 E-value: 3.57e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 2 IRFDNVSKKYNeDKIAVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEKRISDyDIHELRWDIGYV 81
Cdd:cd03230 1 IEVRNLSKRYG-KKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK-EPEEVKRRIGYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 82 LQQIALFPHMTIEENIaivpelkkwdkdkihdritelldsvgldpesyrhrkpaELSGGEQQRVGVVRALAADPGIILMD 161
Cdd:cd03230 79 PEEPSLYENLTVRENL--------------------------------------KLSGGMKQRLALAQALLHDPELLILD 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 489843944 162 EPFSALDPISRQRLQQDISALQKKiKKTIVFVTHDMQEALALGDRICVMQDGEI 215
Cdd:cd03230 121 EPTSGLDPESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
22-217 |
4.36e-56 |
|
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: 181.34 E-value: 4.36e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 22 TLDIK---DGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYIN-------EKRIsDYDIHELRwdIGYVLQQIALFPHM 91
Cdd:cd03297 14 TLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNgtvlfdsRKKI-NLPPQQRK--IGLVFQQYALFPHL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 92 TIEENIAIVpeLKKWDKDKIHDRITELLDSVGLDPESYRHrkPAELSGGEQQRVGVVRALAADPGIILMDEPFSALDPIS 171
Cdd:cd03297 91 NVRENLAFG--LKRKRNREDRISVDELLDLLGLDHLLNRY--PAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRAL 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 489843944 172 RQRLQQDISALQKKIKKTIVFVTHDMQEALALGDRICVMQDGEIVQ 217
Cdd:cd03297 167 RLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQY 212
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
6-243 |
8.93e-56 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 185.81 E-value: 8.93e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 6 NVSKKYnEDKIAVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEKRISDydIHELRWDIGYVLQQI 85
Cdd:PRK11607 24 NLTKSF-DGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSH--VPPYQRPINMMFQSY 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 86 ALFPHMTIEENIAIVPELKKWDKDKIHDRITELLDSVGLdpESYRHRKPAELSGGEQQRVGVVRALAADPGIILMDEPFS 165
Cdd:PRK11607 101 ALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHM--QEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMG 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489843944 166 ALDPISRQRLQQDISALQKKIKKTIVFVTHDMQEALALGDRICVMQDGEIVQVATPQEIIKNPENDFVKDFLASGHAF 243
Cdd:PRK11607 179 ALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAEFIGSVNVF 256
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
6-272 |
1.03e-55 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 184.54 E-value: 1.03e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 6 NVSKKYNEDKIaVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEKRISDYDIHELrwDIGYVLQQI 85
Cdd:PRK11432 11 NITKRFGSNTV-IDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQR--DICMVFQSY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 86 ALFPHMTIEENIAIVPELKKWDKDKIHDRITELLDSVglDPESYRHRKPAELSGGEQQRVGVVRALAADPGIILMDEPFS 165
Cdd:PRK11432 88 ALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELV--DLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLS 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 166 ALDPISRQRLQQDISALQKKIKKTIVFVTHDMQEALALGDRICVMQDGEIVQVATPQEIIKNPENDFVKDFLASGHAFNT 245
Cdd:PRK11432 166 NLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPASRFMASFMGDANIFPA 245
|
250 260
....*....|....*....|....*...
gi 489843944 246 PILEGSFTVND-LIDADLFYAYQTSDGS 272
Cdd:PRK11432 246 TLSGDYVDIYGyRLPRPAAFAFNLPDGE 273
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
2-226 |
6.28e-55 |
|
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: 190.43 E-value: 6.28e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 2 IRFDNVSKKYNEDKIAV-NNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEKRISDYDIHELRWDIGY 80
Cdd:COG2274 474 IELENVSFRYPGDSPPVlDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGV 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 81 VLQQIALFpHMTIEENIAIvpelkkWDKDKIHDRITELLDSVGLDPESYRHrkP-----------AELSGGEQQRVGVVR 149
Cdd:COG2274 554 VLQDVFLF-SGTIRENITL------GDPDATDEEIIEAARLAGLHDFIEAL--PmgydtvvgeggSNLSGGQRQRLAIAR 624
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489843944 150 ALAADPGIILMDEPFSALDPISRQRLQQDISALQKkiKKTIVFVTHDMqEALALGDRICVMQDGEIVQVATPQEIIK 226
Cdd:COG2274 625 ALLRNPRILILDEATSALDAETEAIILENLRRLLK--GRTVIIIAHRL-STIRLADRIIVLDKGRIVEDGTHEELLA 698
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-228 |
1.40e-54 |
|
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: 180.63 E-value: 1.40e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 1 MIRFDNVSKKYNEDKI---AVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIP---LTTGTIYINEKRISDYDIHEL 74
Cdd:COG0444 1 LLEVRNLKVYFPTRRGvvkAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPppgITSGEILFDGEDLLKLSEKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 75 RW----DIGYVLQ--QIALFPHMTIEENIAIVPEL-KKWDKDKIHDRITELLDSVGL-DPESYRHRKPAELSGGEQQRVG 146
Cdd:COG0444 81 RKirgrEIQMIFQdpMTSLNPVMTVGDQIAEPLRIhGGLSKAEARERAIELLERVGLpDPERRLDRYPHELSGGMRQRVM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 147 VVRALAADPGIILMDEPFSALDP-ISRQRLQQdISALQKKIKKTIVFVTHDMQEALALGDRICVMQDGEIVQVATPQEII 225
Cdd:COG0444 161 IARALALEPKLLIADEPTTALDVtIQAQILNL-LKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGPVEELF 239
|
...
gi 489843944 226 KNP 228
Cdd:COG0444 240 ENP 242
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-230 |
2.64e-54 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 177.59 E-value: 2.64e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 1 MIRFDNVSKKYNeDKIAVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIyinekRISDYDIHELRWDIGY 80
Cdd:COG1121 6 AIELENLTVSYG-GRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTV-----RLFGKPPRRARRRIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 81 VLQQIAL---FPhMTIEENIA--IVPELK--KWDKDKIHDRITELLDSVGLdpESYRHRKPAELSGGEQQRVGVVRALAA 153
Cdd:COG1121 80 VPQRAEVdwdFP-ITVRDVVLmgRYGRRGlfRRPSRADREAVDEALERVGL--EDLADRPIGELSGGQQQRVLLARALAQ 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489843944 154 DPGIILMDEPFSALDPISRQRLQQDISALQKKiKKTIVFVTHDMQEALALGDRICVMqDGEIVQVATPQEIIkNPEN 230
Cdd:COG1121 157 DPDLLLLDEPFAGVDAATEEALYELLRELRRE-GKTILVVTHDLGAVREYFDRVLLL-NRGLVAHGPPEEVL-TPEN 230
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1-246 |
3.02e-54 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 180.77 E-value: 3.02e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 1 MIRFDNVSKKYNEDK---IAVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEKRISDYDIHEL--- 74
Cdd:PRK11153 1 MIELKNISKVFPQGGrtiHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELrka 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 75 RWDIGYVLQQIALFPHMTIEENIAIVPELKKWDKDKIHDRITELLDSVGLdpESYRHRKPAELSGGEQQRVGVVRALAAD 154
Cdd:PRK11153 81 RRQIGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGL--SDKADRYPAQLSGGQKQRVAIARALASN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 155 PGIILMDEPFSALDPISRQRLQQDISALQKKIKKTIVFVTHDMQEALALGDRICVMQDGEIVQVATPQEIIKNPENDFVK 234
Cdd:PRK11153 159 PKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHPKHPLTR 238
|
250
....*....|..
gi 489843944 235 DFLASGHAFNTP 246
Cdd:PRK11153 239 EFIQSTLHLDLP 250
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
2-214 |
2.04e-53 |
|
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: 172.95 E-value: 2.04e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 2 IRFDNVSKKY-NEDKIAVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEKRISDYDIHELRWDIGY 80
Cdd:cd03228 1 IEFKNVSFSYpGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 81 VLQQIALFpHMTIEENIaivpelkkwdkdkihdritelldsvgldpesyrhrkpaeLSGGEQQRVGVVRALAADPGIILM 160
Cdd:cd03228 81 VPQDPFLF-SGTIRENI---------------------------------------LSGGQRQRIAIARALLRDPPILIL 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 489843944 161 DEPFSALDPISRQRLQQDISALQKkiKKTIVFVTHDMqEALALGDRICVMQDGE 214
Cdd:cd03228 121 DEATSALDPETEALILEALRALAK--GKTVIVIAHRL-STIRDADRIIVLDDGR 171
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-229 |
2.09e-53 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 175.22 E-value: 2.09e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 1 MIRFDNVSKKYNeDKIAVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEKRISDYDIHE-LRWDIG 79
Cdd:COG1137 3 TLEAENLVKSYG-KRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMHKrARLGIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 80 YVLQQIALFPHMTIEENIAIVPELKKWDKDKIHDRITELLDSVGLdpESYRHRKPAELSGGEQQRVGVVRALAADPGIIL 159
Cdd:COG1137 82 YLPQEASIFRKLTVEDNILAVLELRKLSKKEREERLEELLEEFGI--THLRKSKAYSLSGGERRRVEIARALATNPKFIL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489843944 160 MDEPFSALDPISRQRLQQDISALQkkiKKTI-VFVT-HDMQEALALGDRICVMQDGEIVQVATPQEIIKNPE 229
Cdd:COG1137 160 LDEPFAGVDPIAVADIQKIIRHLK---ERGIgVLITdHNVRETLGICDRAYIISEGKVLAEGTPEEILNNPL 228
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
2-229 |
4.18e-53 |
|
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: 174.27 E-value: 4.18e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 2 IRFDNVSKKYNEDKIaVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEKRISDYDIHE-LRWDIGY 80
Cdd:cd03218 1 LRAENLSKRYGKRKV-VNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKrARLGIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 81 VLQQIALFPHMTIEENIAIVPELKKWDKDKIHDRITELLDSVGLdpESYRHRKPAELSGGEQQRVGVVRALAADPGIILM 160
Cdd:cd03218 80 LPQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHI--THLRKSKASSLSGGERRRVEIARALATNPKFLLL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489843944 161 DEPFSALDPISRQRLQQDISAL-QKKIKktiVFVT-HDMQEALALGDRICVMQDGEIVQVATPQEIIKNPE 229
Cdd:cd03218 158 DEPFAGVDPIAVQDIQKIIKILkDRGIG---VLITdHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANEL 225
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-229 |
5.96e-53 |
|
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: 174.46 E-value: 5.96e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 1 MIRFDNVSKKYNEDKiAVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEKRISDYDIHEL-RWDIG 79
Cdd:COG0411 4 LLEVRGLTKRFGGLV-AVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIaRLGIA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 80 YVLQQIALFPHMTIEENIAI-------------VPELKKWDKD--KIHDRITELLDSVGLDPesYRHRKPAELSGGEQQR 144
Cdd:COG0411 83 RTFQNPRLFPELTVLENVLVaaharlgrgllaaLLRLPRARREerEARERAEELLERVGLAD--RADEPAGNLSYGQQRR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 145 VGVVRALAADPGIILMDEPFSALDPISRQRLQQDISALQKKIKKTIVFVTHDMQEALALGDRICVMQDGEIVQVATPQEI 224
Cdd:COG0411 161 LEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGTPAEV 240
|
....*
gi 489843944 225 IKNPE 229
Cdd:COG0411 241 RADPR 245
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
1-214 |
1.44e-52 |
|
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC transporter ATP-binding protein family. This protein, and its permease partner FtsX, localize to the division site. In a number of species, the ftsEX gene pair is located next to FtsY, the signal recognition particle-docking protein. [Cellular processes, Cell division]
Pssm-ID: 131721 [Multi-domain] Cd Length: 214 Bit Score: 172.05 E-value: 1.44e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 1 MIRFDNVSKKYNEDKIAVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEKRISDYDIHE---LRWD 77
Cdd:TIGR02673 1 MIEFHNVSKAYPGGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLRGRQlplLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 78 IGYVLQQIALFPHMTIEENIAIVPELKKWDKDKIHDRITELLDSVGLdpeSYRHR-KPAELSGGEQQRVGVVRALAADPG 156
Cdd:TIGR02673 81 IGVVFQDFRLLPDRTVYENVALPLEVRGKKEREIQRRVGAALRQVGL---EHKADaFPEQLSGGEQQRVAIARAIVNSPP 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489843944 157 IILMDEPFSALDPisrqRLQQDISALQKKIKK---TIVFVTHDMQEALALGDRICVMQDGE 214
Cdd:TIGR02673 158 LLLADEPTGNLDP----DLSERILDLLKRLNKrgtTVIVATHDLSLVDRVAHRVIILDDGR 214
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-229 |
5.89e-52 |
|
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: 179.96 E-value: 5.89e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 2 IRFDNVSKKY-NEDKIAVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEKRISDYDIHELRWDIGY 80
Cdd:COG4987 334 LELEDVSFRYpGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRRIAV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 81 VLQQIALFpHMTIEENIAIVpelkkwDKDKIHDRITELLDSVGLD------PESY------RHRKpaeLSGGEQQRVGVV 148
Cdd:COG4987 414 VPQRPHLF-DTTLRENLRLA------RPDATDEELWAALERVGLGdwlaalPDGLdtwlgeGGRR---LSGGERRRLALA 483
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 149 RALAADPGIILMDEPFSALDPISRQRLQQDISALQKkiKKTIVFVTHDMQeALALGDRICVMQDGEIVQVATPQEIIKNP 228
Cdd:COG4987 484 RALLRDAPILLLDEPTEGLDAATEQALLADLLEALA--GRTVLLITHRLA-GLERMDRILVLEDGRIVEQGTHEELLAQN 560
|
.
gi 489843944 229 E 229
Cdd:COG4987 561 G 561
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
1-224 |
5.95e-52 |
|
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: 171.71 E-value: 5.95e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 1 MIRFDNVSKKYNEDKIAVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEKRISDY---DIHELRWD 77
Cdd:TIGR02315 1 MLEVENLSKVYPNGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLrgkKLRKLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 78 IGYVLQQIALFPHMTIEENI-----AIVPELKKW-----DKDKIhdRITELLDSVGLDpeSYRHRKPAELSGGEQQRVGV 147
Cdd:TIGR02315 81 IGMIFQHYNLIERLTVLENVlhgrlGYKPTWRSLlgrfsEEDKE--RALSALERVGLA--DKAYQRADQLSGGQQQRVAI 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489843944 148 VRALAADPGIILMDEPFSALDPISRQRLQQDISALQKKIKKTIVFVTHDMQEALALGDRICVMQDGEIVQVATPQEI 224
Cdd:TIGR02315 157 ARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSEL 233
|
|
| ABC_ATP_SaoA |
NF040729 |
ABC transporter ATP-binding protein SaoA; SaoA is the ATP-binding subunit of an ABC ... |
2-217 |
2.61e-51 |
|
ABC transporter ATP-binding protein SaoA; SaoA is the ATP-binding subunit of an ABC transporter in which both the permease subunit SaoP, and the substrate-binding protein SaoB, are nearly always selenoproteins that were unrecognized as such until recently (2022). The SAO system is found in Clostridium difficile and various other anaerobic heterotrophs.
Pssm-ID: 468693 [Multi-domain] Cd Length: 248 Bit Score: 170.31 E-value: 2.61e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 2 IRFDNVSKKYNEDKI---AVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEKRISDYDIhelrwDI 78
Cdd:NF040729 2 LKIQNISKTFINNKKeneVLKDISFDVEEGEFVSLLGPSGCGKTTLLTIIAGFQNATSGEILVNGNEVTKPGP-----DR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 79 GYVLQQIALFPHMTIEENIAIVPELKKWDKDKIHDRITELLDSVGLdpESYRHRKPAELSGGEQQRVGVVRALAADPGII 158
Cdd:NF040729 77 GFVFQNYALFPWMTVKENIEYPMKQQKMPKQEREKRLNELLEMAQL--TGKENLYPHQISGGMKQRTAVIRALACKPEVL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489843944 159 LMDEPFSALDPISRQRLQQDISALQKKIKKTIVFVTHDMQEALALGDRICVM--QDGEIVQ 217
Cdd:NF040729 155 LMDEPLGAVDFQMRQILQEELESIWLKDKTTVLMVTHDVDEAVYLSDRVIVMsrDKGKILE 215
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
5-229 |
3.31e-51 |
|
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: 169.54 E-value: 3.31e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 5 DNVSKKYNEDKiAVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEKRISDYDIHEL-RWDIGYVLQ 83
Cdd:cd03219 4 RGLTKRFGGLV-ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIaRLGIGRTFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 84 QIALFPHMTIEENIAIVPELKK----------WDKDKIHDRITELLDSVGLDPesYRHRKPAELSGGEQQRVGVVRALAA 153
Cdd:cd03219 83 IPRLFPELTVLENVMVAAQARTgsglllararREEREARERAEELLERVGLAD--LADRPAGELSYGQQRRLEIARALAT 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489843944 154 DPGIILMDEPFSALDPisrqRLQQDISALQKKIKK---TIVFVTHDMQEALALGDRICVMQDGEIVQVATPQEIIKNPE 229
Cdd:cd03219 161 DPKLLLLDEPAAGLNP----EETEELAELIRELRErgiTVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRNNPR 235
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1-237 |
5.22e-51 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 168.78 E-value: 5.22e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 1 MIRFDNVSKKYNEDKIavnNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEKRISDYDIHElRwDIGY 80
Cdd:COG3840 1 MLRLDDLTYRYGDFPL---RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAE-R-PVSM 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 81 VLQQIALFPHMTIEENIA--IVPELKKWDKDKihDRITELLDSVGLdpESYRHRKPAELSGGEQQRVGVVRALAADPGII 158
Cdd:COG3840 76 LFQENNLFPHLTVAQNIGlgLRPGLKLTAEQR--AQVEQALERVGL--AGLLDRLPGQLSGGQRQRVALARCLVRKRPIL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489843944 159 LMDEPFSALDPISRQRLQQDISALQKKIKKTIVFVTHDMQEALALGDRICVMQDGEIVQVATPQEIIKNPENDFVKDFL 237
Cdd:COG3840 152 LLDEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPPALAAYL 230
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-224 |
8.00e-51 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 170.29 E-value: 8.00e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 1 MIRFDNVSKKYnEDKIAVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEKRISDYDIHelrwDIGY 80
Cdd:COG4152 1 MLELKGLTKRF-GDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDRR----RIGY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 81 VLQQIALFPHMTIEENIAIVPELKKWDKDKIHDRITELLDSVGLdpESYRHRKPAELSGGEQQRVGVVRALAADPGIILM 160
Cdd:COG4152 76 LPEERGLYPKMKVGEQLVYLARLKGLSKAEAKRRADEWLERLGL--GDRANKKVEELSKGNQQKVQLIAALLHDPELLIL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489843944 161 DEPFSALDPISRQRLQQDISALQKKiKKTIVFVTHDMQEALALGDRICVMQDGEIVQVATPQEI 224
Cdd:COG4152 154 DEPFSGLDPVNVELLKDVIRELAAK-GTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEI 216
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
5-216 |
1.13e-50 |
|
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: 166.07 E-value: 1.13e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 5 DNVSKKYNeDKIAVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEKRISDYDIHELRWDIGYVLQq 84
Cdd:cd03214 3 ENLSVGYG-GRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVPQ- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 85 ialfphmtieeniaivpelkkwdkdkihdriteLLDSVGLdpESYRHRKPAELSGGEQQRVGVVRALAADPGIILMDEPF 164
Cdd:cd03214 81 ---------------------------------ALELLGL--AHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPT 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 489843944 165 SALDPISRQRLQQDISALQKKIKKTIVFVTHDMQEALALGDRICVMQDGEIV 216
Cdd:cd03214 126 SHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIV 177
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1-229 |
1.26e-50 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 169.02 E-value: 1.26e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 1 MIRFDNVSKKYNED-KIAVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEKRISDYDIHELRWDIG 79
Cdd:PRK13632 7 MIKVENVSFSYPNSeNNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 80 YVLQ----QialFPHMTIEENIAIVPELKKWDKDKIHDRITELLDSVGLdpESYRHRKPAELSGGEQQRVGVVRALAADP 155
Cdd:PRK13632 87 IIFQnpdnQ---FIGATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGM--EDYLDKEPQNLSGGQKQRVAIASVLALNP 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489843944 156 GIILMDEPFSALDPISRQRLQQDISALQKKIKKTIVFVTHDMQEALaLGDRICVMQDGEIVQVATPQEIIKNPE 229
Cdd:PRK13632 162 EIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAI-LADKVIVFSEGKLIAQGKPKEILNNKE 234
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-227 |
1.46e-50 |
|
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: 176.10 E-value: 1.46e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 2 IRFDNVSKKYNEDKIAVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEKRISDYDIHELRWDIGYV 81
Cdd:COG4988 337 IELEDVSFSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWV 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 82 LQQIALFpHMTIEENIAivpeLKKWDKDKihDRITELLDSVGLD------PESYRHR---KPAELSGGEQQRVGVVRALA 152
Cdd:COG4988 417 PQNPYLF-AGTIRENLR----LGRPDASD--EELEAALEAAGLDefvaalPDGLDTPlgeGGRGLSGGQAQRLALARALL 489
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489843944 153 ADPGIILMDEPFSALDPISRQRLQQDISALQKkiKKTIVFVTHDMqEALALGDRICVMQDGEIVQVATPQEIIKN 227
Cdd:COG4988 490 RDAPLLLLDEPTAHLDAETEAEILQALRRLAK--GRTVILITHRL-ALLAQADRILVLDDGRIVEQGTHEELLAK 561
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
2-227 |
2.24e-50 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 175.74 E-value: 2.24e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 2 IRFDNVSKKYNEDKIAVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEKRISDYDIHELRWDIGYV 81
Cdd:COG1132 340 IEFENVSFSYPGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESLRRQIGVV 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 82 LQQIALFpHMTIEENIAI-VPELkkwDKDKI---------HDRITELldsvgldPESYRHR---KPAELSGGEQQRVGVV 148
Cdd:COG1132 420 PQDTFLF-SGTIRENIRYgRPDA---TDEEVeeaakaaqaHEFIEAL-------PDGYDTVvgeRGVNLSGGQRQRIAIA 488
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 149 RALAADPGIILMDEPFSALDPISRQRLQQDISALQKkiKKTIVFVTHDM---QEAlalgDRICVMQDGEIVQVATPQEII 225
Cdd:COG1132 489 RALLKDPPILILDEATSALDTETEALIQEALERLMK--GRTTIVIAHRLstiRNA----DRILVLDDGRIVEQGTHEELL 562
|
..
gi 489843944 226 KN 227
Cdd:COG1132 563 AR 564
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
2-229 |
2.65e-50 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 168.69 E-value: 2.65e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 2 IRFDNVSKKYNE----DKIAVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEKRISDYDIH--ELR 75
Cdd:PRK13637 3 IKIENLTHIYMEgtpfEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKlsDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 76 WDIGYVLQ--QIALFPHmTIEENIAIVPELKKWDKDKIHDRITELLDSVGLDPESYRHRKPAELSGGEQQRVGVVRALAA 153
Cdd:PRK13637 83 KKVGLVFQypEYQLFEE-TIEKDIAFGPINLGLSEEEIENRVKRAMNIVGLDYEDYKDKSPFELSGGQKRRVAIAGVVAM 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489843944 154 DPGIILMDEPFSALDPISRQRLQQDISALQKKIKKTIVFVTHDMQEALALGDRICVMQDGEIVQVATPQEIIKNPE 229
Cdd:PRK13637 162 EPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVFKEVE 237
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
3-214 |
2.41e-49 |
|
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: 162.03 E-value: 2.41e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 3 RFDNVSKKYNeDKIAVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEKRISDYDIHELRWDIGYVL 82
Cdd:cd00267 1 EIENLSFRYG-GRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 83 QqialfphmtieeniaivpelkkwdkdkihdritelldsvgldpesyrhrkpaeLSGGEQQRVGVVRALAADPGIILMDE 162
Cdd:cd00267 80 Q-----------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDE 106
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 489843944 163 PFSALDPISRQRLQQDISALQKKiKKTIVFVTHDMQEALALGDRICVMQDGE 214
Cdd:cd00267 107 PTSGLDPASRERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
5-229 |
3.48e-49 |
|
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: 164.37 E-value: 3.48e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 5 DNVSKKYNEDKIaVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEKRISDYDIHE-LRWDIGYVLQ 83
Cdd:TIGR04406 5 ENLIKSYKKRKV-VNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHLPMHErARLGIGYLPQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 84 QIALFPHMTIEENIAIVPEL-KKWDKDKIHDRITELLDSVGLdpESYRHRKPAELSGGEQQRVGVVRALAADPGIILMDE 162
Cdd:TIGR04406 84 EASIFRKLTVEENIMAVLEIrKDLDRAEREERLEALLEEFQI--SHLRDNKAMSLSGGERRRVEIARALATNPKFILLDE 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489843944 163 PFSALDPISRQRLQQDISALqkKIKKTIVFVT-HDMQEALALGDRICVMQDGEIVQVATPQEIIKNPE 229
Cdd:TIGR04406 162 PFAGVDPIAVGDIKKIIKHL--KERGIGVLITdHNVRETLDICDRAYIISDGKVLAEGTPAEIVANEK 227
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
2-224 |
9.05e-49 |
|
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: 162.54 E-value: 9.05e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 2 IRFDNVSKKYNeDKIAVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGtiyinEKRISDYDI----HELRWD 77
Cdd:cd03265 1 IEVENLVKKYG-DFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSG-----RATVAGHDVvrepREVRRR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 78 IGYVLQQIALFPHMTIEENIAIVPELKKWDKDKIHDRITELLDSVGLdpESYRHRKPAELSGGEQQRVGVVRALAADPGI 157
Cdd:cd03265 75 IGIVFQDLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGL--LEAADRLVKTYSGGMRRRLEIARSLVHRPEV 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489843944 158 ILMDEPFSALDPISRQRLQQDISALQKKIKKTIVFVTHDMQEALALGDRICVMQDGEIVQVATPQEI 224
Cdd:cd03265 153 LFLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
17-228 |
3.48e-48 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 164.52 E-value: 3.48e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 17 AVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEKRISDYDIHELRW---DIGYVLQ--QIALFPHM 91
Cdd:COG4608 33 AVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELRPlrrRMQMVFQdpYASLNPRM 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 92 TIEENIAIVPEL-KKWDKDKIHDRITELLDSVGLDPESYrHRKPAELSGGEQQRVGVVRALAADPGIILMDEPFSALDpI 170
Cdd:COG4608 113 TVGDIIAEPLRIhGLASKAERRERVAELLELVGLRPEHA-DRYPHEFSGGQRQRIGIARALALNPKLIVCDEPVSALD-V 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489843944 171 SRQ----RLQQDisaLQKKIKKTIVFVTHDmqeaLA----LGDRICVMQDGEIVQVATPQEIIKNP 228
Cdd:COG4608 191 SIQaqvlNLLED---LQDELGLTYLFISHD----LSvvrhISDRVAVMYLGKIVEIAPRDELYARP 249
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-237 |
2.03e-47 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 160.33 E-value: 2.03e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 1 MIRFDNVSKKYNEDKiAVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINR---LIP--LTTGTIYINEKRI--SDYDIHE 73
Cdd:PRK14239 5 ILQVSDLSVYYNKKK-ALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRmndLNPevTITGSIVYNGHNIysPRTDTVD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 74 LRWDIGYVLQQIALFPhMTIEENI-----------------AIVPELKK---WD--KDKIHDritellDSVGLdpesyrh 131
Cdd:PRK14239 84 LRKEIGMVFQQPNPFP-MSIYENVvyglrlkgikdkqvldeAVEKSLKGasiWDevKDRLHD------SALGL------- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 132 rkpaelSGGEQQRVGVVRALAADPGIILMDEPFSALDPISRQRLQQDISALQKKIkkTIVFVTHDMQEALALGDRICVMQ 211
Cdd:PRK14239 150 ------SGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDY--TMLLVTRSMQQASRISDRTGFFL 221
|
250 260
....*....|....*....|....*.
gi 489843944 212 DGEIVQVATPQEIIKNPENDFVKDFL 237
Cdd:PRK14239 222 DGDLIEYNDTKQMFMNPKHKETEDYI 247
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
2-216 |
5.46e-47 |
|
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: 157.83 E-value: 5.46e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 2 IRFDNVSKKYNeDKIAVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEKRISDYDIHelrwDIGYV 81
Cdd:cd03269 1 LEVENVTKRFG-RVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARN----RIGYL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 82 LQQIALFPHMTIEENIAIVPELKKWDKDKIHDRITELLDSVGLdpESYRHRKPAELSGGEQQRVGVVRALAADPGIILMD 161
Cdd:cd03269 76 PEERGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLEL--SEYANKRVEELSKGNQQKVQFIAAVIHDPELLILD 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489843944 162 EPFSALDPISRQRLQQDISALQKKiKKTIVFVTHDMQEALALGDRICVMQDGEIV 216
Cdd:cd03269 154 EPFSGLDPVNVELLKDVIRELARA-GKTVILSTHQMELVEELCDRVLLLNKGRAV 207
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
2-215 |
1.43e-46 |
|
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: 156.80 E-value: 1.43e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 2 IRFDNVSKKYNEDKIAVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEKRISDYD---IHELRWDI 78
Cdd:cd03292 1 IEFINVTKTYPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRgraIPYLRRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 79 GYVLQQIALFPHMTIEENIAIVPELKKWDKDKIHDRITELLDSVGLdpeSYRHRK-PAELSGGEQQRVGVVRALAADPGI 157
Cdd:cd03292 81 GVVFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGL---SHKHRAlPAELSGGEQQRVAIARAIVNSPTI 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489843944 158 ILMDEPFSALDPISRQRlqqdISALQKKIKK---TIVFVTHDMQEALALGDRICVMQDGEI 215
Cdd:cd03292 158 LIADEPTGNLDPDTTWE----IMNLLKKINKagtTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-237 |
1.41e-45 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 155.29 E-value: 1.41e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 1 MIRFDNVSKKYNeDKIAVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEKRIsDYD---------I 71
Cdd:PRK11264 3 AIEVKNLVKKFH-GQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITI-DTArslsqqkglI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 72 HELRWDIGYVLQQIALFPHMTIEENIAIVPEL-KKWDKDKIHDRITELLDSVGLD--PESYrhrkPAELSGGEQQRVGVV 148
Cdd:PRK11264 81 RQLRQHVGFVFQNFNLFPHRTVLENIIEGPVIvKGEPKEEATARARELLAKVGLAgkETSY----PRRLSGGQQQRVAIA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 149 RALAADPGIILMDEPFSALDPISRQRLQQDISALQKKiKKTIVFVTHDMQEALALGDRICVMQDGEIVQVATPQEIIKNP 228
Cdd:PRK11264 157 RALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADP 235
|
....*....
gi 489843944 229 ENDFVKDFL 237
Cdd:PRK11264 236 QQPRTRQFL 244
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
9-301 |
1.60e-45 |
|
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin resistance ABC transporter, ATP binding subunit in bacteria and archaea. This model is restricted in its scope to preferentially recognize the ATP binding subunit associated with effux of the drug, daunorubicin. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. In eukaryotes proteins of similar function include p-gyco proteins, multidrug resistance protein etc. [Transport and binding proteins, Other]
Pssm-ID: 130256 [Multi-domain] Cd Length: 302 Bit Score: 156.78 E-value: 1.60e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 9 KKYNEDKiAVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIyinekRISDYDI----HELRWDIGYVLQQ 84
Cdd:TIGR01188 1 KVYGDFK-AVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTA-----RVAGYDVvrepRKVRRSIGIVPQY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 85 IALFPHMTIEENIAIVPELKKWDKDKIHDRITELLDSVGLdpeSYRHRKPAE-LSGGEQQRVGVVRALAADPGIILMDEP 163
Cdd:TIGR01188 75 ASVDEDLTGRENLEMMGRLYGLPKDEAEERAEELLELFEL---GEAADRPVGtYSGGMRRRLDIAASLIHQPDVLFLDEP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 164 FSALDPISRQRLQQDISALqKKIKKTIVFVTHDMQEALALGDRICVMQDGEIVQVATPQEIiknpendfvKDFLASGHAF 243
Cdd:TIGR01188 152 TTGLDPRTRRAIWDYIRAL-KEEGVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPEEL---------KRRLGKDTLE 221
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 244 NTPILEGSFTV-NDLIDADLFyayQTSDGSLGISLT-DPVENLVRRvAEEQSIPVLDEAT 301
Cdd:TIGR01188 222 SRPRDIQSLKVeVSMLIAELG---ETGLGLLAVTVDsDRIKILVPD-GDETVPEIVEAAI 277
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
20-229 |
2.08e-45 |
|
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: 157.96 E-value: 2.08e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 20 NVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEKRIsdYDIHELRW------DIGYVLQQIALFPHMTI 93
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVL--QDSARGIFlpphrrRIGYVFQEARLFPHLSV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 94 EENIAIVPELKKWDKDKIH-DRITELLdsvGLDPesYRHRKPAELSGGEQQRVGVVRALAADPGIILMDEPFSALDPISR 172
Cdd:COG4148 95 RGNLLYGRKRAPRAERRISfDEVVELL---GIGH--LLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARK 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 489843944 173 QRLQQDISALQKKIKKTIVFVTHDMQEALALGDRICVMQDGEIVQVATPQEIIKNPE 229
Cdd:COG4148 170 AEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRPD 226
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
3-216 |
2.84e-45 |
|
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: 153.46 E-value: 2.84e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 3 RFDNVSKKYNeDKIAVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIyinekRISDYDIHELRWDIGYVL 82
Cdd:cd03235 1 EVEDLTVSYG-GHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSI-----RVFGKPLEKERKRIGYVP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 83 QQIAL---FPhMTIEENIAIVPELKKW------DKDKihDRITELLDSVGLdpESYRHRKPAELSGGEQQRVGVVRALAA 153
Cdd:cd03235 75 QRRSIdrdFP-ISVRDVVLMGLYGHKGlfrrlsKADK--AKVDEALERVGL--SELADRQIGELSGGQQQRVLLARALVQ 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489843944 154 DPGIILMDEPFSALDPISRQRLQQDISALQKKiKKTIVFVTHDMQEALALGDRIcVMQDGEIV 216
Cdd:cd03235 150 DPDLLLLDEPFAGVDPKTQEDIYELLRELRRE-GMTILVVTHDLGLVLEYFDRV-LLLNRTVV 210
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
18-165 |
3.92e-45 |
|
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: 150.88 E-value: 3.92e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 18 VNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEKRISDYDIHELRWDIGYVLQQIALFPHMTIEENI 97
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 98 AIVPELKKWDKDKIHDRITELLDSVGLDPESYR--HRKPAELSGGEQQRVGVVRALAADPGIILMDEPFS 165
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEALEKLGLGDLADRpvGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
2-229 |
4.44e-44 |
|
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: 151.15 E-value: 4.44e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 2 IRFDNVSKKYNE--DKIAVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEKRISDYDIHELRWDIG 79
Cdd:cd03249 1 IEFKNVSFRYPSrpDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 80 YVLQQIALFPhMTIEENI------AIVPELKKWDKD-KIHDRITELldsvgldPESYRHR---KPAELSGGEQQRVGVVR 149
Cdd:cd03249 81 LVSQEPVLFD-GTIAENIrygkpdATDEEVEEAAKKaNIHDFIMSL-------PDGYDTLvgeRGSQLSGGQKQRIAIAR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 150 ALAADPGIILMDEPFSALDPISRQRLQQdisALQKKIK-KTIVFVTHDM---QEAlalgDRICVMQDGEIVQVATPQEII 225
Cdd:cd03249 153 ALLRNPKILLLDEATSALDAESEKLVQE---ALDRAMKgRTTIVIAHRLstiRNA----DLIAVLQNGQVVEQGTHDELM 225
|
....
gi 489843944 226 KNPE 229
Cdd:cd03249 226 AQKG 229
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1-229 |
7.53e-44 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 151.78 E-value: 7.53e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 1 MIRFDNVSKKY-----NEDKIAVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEKRISDY-DIHEL 74
Cdd:PRK13633 4 MIKCKNVSYKYesneeSTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEeNLWDI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 75 RWDIGYVLQ----QIAlfphMTI-EENIAIVPELKKWDKDKIHDRITELLDSVGLdpESYRHRKPAELSGGEQQRVGVVR 149
Cdd:PRK13633 84 RNKAGMVFQnpdnQIV----ATIvEEDVAFGPENLGIPPEEIRERVDESLKKVGM--YEYRRHAPHLLSGGQKQRVAIAG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 150 ALAADPGIILMDEPFSALDPISRQRLQQDISALQKKIKKTIVFVTHDMQEAlALGDRICVMQDGEIVQVATPQEIIKNPE 229
Cdd:PRK13633 158 ILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEA-VEADRIIVMDSGKVVMEGTPKEIFKEVE 236
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
2-226 |
2.35e-43 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 150.55 E-value: 2.35e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 2 IRFDNVSKKY-NEDKIAVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEKRISDYDIHELRWDIGY 80
Cdd:PRK13635 6 IRVEHISFRYpDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVGM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 81 VLQ----QialFPHMTIEENIAIVPELKKWDKDKIHDRITELLDSVGLdpESYRHRKPAELSGGEQQRVGVVRALAADPG 156
Cdd:PRK13635 86 VFQnpdnQ---FVGATVQDDVAFGLENIGVPREEMVERVDQALRQVGM--EDFLNREPHRLSGGQKQRVAIAGVLALQPD 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 157 IILMDEPFSALDPISRQRLQQDISALQKKIKKTIVFVTHDMQEAlALGDRICVMQDGEIVQVATPQEIIK 226
Cdd:PRK13635 161 IIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEA-AQADRVIVMNKGEILEEGTPEEIFK 229
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
6-207 |
2.73e-43 |
|
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly wide distribution consists of a polypeptide related to the lactococcin 972 (see TIGR01653) and multiple-membrane-spanning putative immunity protein (see TIGR01654). This model represents a small clade within the ABC transporters that regularly are found adjacent to these bacteriocin system gene pairs and are likely serve as export proteins. [Cellular processes, Toxin production and resistance, Transport and binding proteins, Unknown substrate]
Pssm-ID: 188353 [Multi-domain] Cd Length: 206 Bit Score: 148.15 E-value: 2.73e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 6 NVSKKYNeDKIAVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEK---RISDYDIHEL-RWDIGYV 81
Cdd:TIGR03608 3 NISKKFG-DKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQetpPLNSKKASKFrREKLGYL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 82 LQQIALFPHMTIEENIAIVPELKKWDKDKIHDRITELLDSVGLdpESYRHRKPAELSGGEQQRVGVVRALAADPGIILMD 161
Cdd:TIGR03608 82 FQNFALIENETVEENLDLGLKYKKLSKKEKREKKKEALEKVGL--NLKLKQKIYELSGGEQQRVALARAILKPPPLILAD 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 489843944 162 EPFSALDPISRQRLQQDISALQKKiKKTIVFVTHDMqEALALGDRI 207
Cdd:TIGR03608 160 EPTGSLDPKNRDEVLDLLLELNDE-GKTIIIVTHDP-EVAKQADRV 203
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
2-225 |
3.15e-43 |
|
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: 148.92 E-value: 3.15e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 2 IRFDNVSKKYNEDKIAVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEKRISDYDIHELRWDIGYV 81
Cdd:cd03253 1 IEFENVTFAYDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 82 LQQIALFpHMTIEENIAI---------VPELKKwdKDKIHDRITELldsvgldPESYRHR---KPAELSGGEQQRVGVVR 149
Cdd:cd03253 81 PQDTVLF-NDTIGYNIRYgrpdatdeeVIEAAK--AAQIHDKIMRF-------PDGYDTIvgeRGLKLSGGEKQRVAIAR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489843944 150 ALAADPGIILMDEPFSALDPISRQRLQQDISALQKkiKKTIVFVTHDMQEaLALGDRICVMQDGEIVQVATPQEII 225
Cdd:cd03253 151 AILKNPPILLLDEATSALDTHTEREIQAALRDVSK--GRTTIVIAHRLST-IVNADKIIVLKDGRIVERGTHEELL 223
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
17-246 |
4.20e-43 |
|
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: 155.61 E-value: 4.20e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 17 AVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPlTTGTIYINEKRISDYDIHE---LRWDIgyvlqQI-------A 86
Cdd:COG4172 301 AVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIP-SEGEIRFDGQDLDGLSRRAlrpLRRRM-----QVvfqdpfgS 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 87 LFPHMTIEEniaIVPE-LK----KWDKDKIHDRITELLDSVGLDPESyRHRKPAELSGGEQQRVGVVRALAADPGIILMD 161
Cdd:COG4172 375 LSPRMTVGQ---IIAEgLRvhgpGLSAAERRARVAEALEEVGLDPAA-RHRYPHEFSGGQRQRIAIARALILEPKLLVLD 450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 162 EPFSALDpisrQRLQQDI----SALQKKIKKTIVFVTHDMQEALALGDRICVMQDGEIVQVATPQEIIKNPENDFVKDFL 237
Cdd:COG4172 451 EPTSALD----VSVQAQIldllRDLQREHGLAYLFISHDLAVVRALAHRVMVMKDGKVVEQGPTEQVFDAPQHPYTRALL 526
|
....*....
gi 489843944 238 ASghAFNTP 246
Cdd:COG4172 527 AA--APLLE 533
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-229 |
5.05e-43 |
|
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: 148.21 E-value: 5.05e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 1 MIRFDNVSKKYNeDKIAVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEKRISDYDIHEL-RWDIG 79
Cdd:COG0410 3 MLEVENLHAGYG-GIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIaRLGIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 80 YVLQQIALFPHMTIEENIAIVPELKKwDKDKIHDRITELLDsvgLDP--ESYRHRKPAELSGGEQQRVGVVRALAADPGI 157
Cdd:COG0410 82 YVPEGRRIFPSLTVEENLLLGAYARR-DRAEVRADLERVYE---LFPrlKERRRQRAGTLSGGEQQMLAIGRALMSRPKL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489843944 158 ILMDEPFSALDPIsrqrLQQDISALQKKIKK---TIVFVTHDMQEALALGDRICVMQDGEIVQVATPQEIIKNPE 229
Cdd:COG0410 158 LLLDEPSLGLAPL----IVEEIFEIIRRLNRegvTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLADPE 228
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-230 |
7.13e-43 |
|
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: 148.31 E-value: 7.13e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 1 MIRFDNVSKKYNeDKIAVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTG-TIYINEKRISDYDIHELRWDIG 79
Cdd:COG1119 3 LLELRNVTVRRG-GKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRGGEDVWELRKRIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 80 YV---LQQiALFPHMTIEE--------NIAIVPELKKWDKDKIHdritELLDSVGLdpESYRHRKPAELSGGEQQRVGVV 148
Cdd:COG1119 82 LVspaLQL-RFPRDETVLDvvlsgffdSIGLYREPTDEQRERAR----ELLELLGL--AHLADRPFGTLSQGEQRRVLIA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 149 RALAADPGIILMDEPFSALDPISRQRLQQDISALQKKIKKTIVFVTHDMQEALALGDRICVMQDGEIVQvATPQEIIKNP 228
Cdd:COG1119 155 RALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRVVA-AGPKEEVLTS 233
|
..
gi 489843944 229 EN 230
Cdd:COG1119 234 EN 235
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
18-228 |
8.69e-43 |
|
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: 147.61 E-value: 8.69e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 18 VNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEKRISdydihELRWDIGYVLQQIALFPHMTIEENI 97
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQIT-----EPGPDRMVVFQNYSLLPWLTVRENI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 98 A-----IVPELKKWDKDKIhdrITELLDSVGLDPESyrHRKPAELSGGEQQRVGVVRALAADPGIILMDEPFSALDPISR 172
Cdd:TIGR01184 76 AlavdrVLPDLSKSERRAI---VEEHIALVGLTEAA--DKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTR 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489843944 173 QRLQQDISALQKKIKKTIVFVTHDMQEALALGDRICVMQD------GEIVQVATPQ-----EIIKNP 228
Cdd:TIGR01184 151 GNLQEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNgpaaniGQILEVPFPRprdrlEVVEDP 217
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1-238 |
1.34e-42 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 147.92 E-value: 1.34e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 1 MIRFDNVSKKYnEDKIAVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEKRISDYDIHElrwdiGY 80
Cdd:PRK11248 1 MLQISHLYADY-GGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAER-----GV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 81 VLQQIALFPHMTIEENIAIVPELKKWDKDKIHDRITELLDSVGLdpESYRHRKPAELSGGEQQRVGVVRALAADPGIILM 160
Cdd:PRK11248 75 VFQNEGLLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGL--EGAEKRYIWQLSGGQRQRVGIARALAANPQLLLL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489843944 161 DEPFSALDPISRQRLQQDISALQKKIKKTIVFVTHDMQEALALGDRICVMQDGeivqvatPQEIIKNPENDFVKDFLA 238
Cdd:PRK11248 153 DEPFGALDAFTREQMQTLLLKLWQETGKQVLLITHDIEEAVFMATELVLLSPG-------PGRVVERLPLNFARRFVA 223
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
1-223 |
1.81e-42 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 146.09 E-value: 1.81e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 1 MIRFDNVSKKYNeDKIAVNNVTLDIKDGEFFVFIGPSGCGKTTTLK-MINRLIPL--TTGTIYINEKRISDYDIHELRwd 77
Cdd:COG4136 1 MLSLENLTITLG-GRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAaIAGTLSPAfsASGEVLLNGRRLTALPAEQRR-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 78 IGYVLQQIALFPHMTIEENI--AIVPELKKWDKdkiHDRITELLDSVGLDpeSYRHRKPAELSGGEQQRVGVVRALAADP 155
Cdd:COG4136 78 IGILFQDDLLFPHLSVGENLafALPPTIGRAQR---RARVEQALEEAGLA--GFADRDPATLSGGQRARVALLRALLAEP 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489843944 156 GIILMDEPFSALDPISRQRL---------QQDISALQkkikktivfVTHDMQEALAlgdricvmqDGEIVQVATPQE 223
Cdd:COG4136 153 RALLLDEPFSKLDAALRAQFrefvfeqirQRGIPALL---------VTHDEEDAPA---------AGRVLDLGNWQH 211
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1-216 |
2.66e-42 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 145.97 E-value: 2.66e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 1 MIRFDNVSKKYNEDK---IAVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIyinekRISDYDIH----E 73
Cdd:cd03266 1 MITADALTKRFRDVKktvQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFA-----TVDGFDVVkepaE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 74 LRWDIGYVLQQIALFPHMTIEENIAIVPELKKWDKDKIHDRITELLDSvgLDPESYRHRKPAELSGGEQQRVGVVRALAA 153
Cdd:cd03266 76 ARRRLGFVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADR--LGMEELLDRRVGGFSTGMRQKVAIARALVH 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489843944 154 DPGIILMDEPFSALDPISRQRLQQDISALqKKIKKTIVFVTHDMQEALALGDRICVMQDGEIV 216
Cdd:cd03266 154 DPPVLLLDEPTTGLDVMATRALREFIRQL-RALGKCILFSTHIMQEVERLCDRVVVLHRGRVV 215
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-196 |
3.01e-42 |
|
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: 145.31 E-value: 3.01e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 1 MIRFDNVSKKYNEDKIaVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEKRISDyDIHELRWDIGY 80
Cdd:COG4133 2 MLEAENLSCRRGERLL-FSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRD-AREDYRRRLAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 81 VLQQIALFPHMTIEENIAIVPELKKWDKDkiHDRITELLDSVGLDPesYRHRKPAELSGGEQQRVGVVRALAADPGIILM 160
Cdd:COG4133 80 LGHADGLKPELTVRENLRFWAALYGLRAD--REAIDEALEAVGLAG--LADLPVRQLSAGQKRRVALARLLLSPAPLWLL 155
|
170 180 190
....*....|....*....|....*....|....*.
gi 489843944 161 DEPFSALDPISRQRLQQDISALQKKiKKTIVFVTHD 196
Cdd:COG4133 156 DEPFTALDAAGVALLAELIAAHLAR-GGAVLLTTHQ 190
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-224 |
5.82e-42 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 146.80 E-value: 5.82e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 1 MIRFDNVSKKYNED--KIAVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEKRISDYDIHELRWDI 78
Cdd:PRK13650 4 IIEVKNLTFKYKEDqeKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 79 GYVLQQI-ALFPHMTIEENIAIVPELKKWDKDKIHDRITELLDSVGLdpESYRHRKPAELSGGEQQRVGVVRALAADPGI 157
Cdd:PRK13650 84 GMVFQNPdNQFVGATVEDDVAFGLENKGIPHEEMKERVNEALELVGM--QDFKEREPARLSGGQKQRVAIAGAVAMRPKI 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489843944 158 ILMDEPFSALDPISRQRLQQDISALQKKIKKTIVFVTHDMQEaLALGDRICVMQDGEIVQVATPQEI 224
Cdd:PRK13650 162 IILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDE-VALSDRVLVMKNGQVESTSTPREL 227
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
2-229 |
6.86e-42 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 147.09 E-value: 6.86e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 2 IRFDNVSKKYNE----DKIAVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEKRIS----DYDIHE 73
Cdd:PRK13634 3 ITFQKVEHRYQYktpfERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITagkkNKKLKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 74 LRWDIGYVLQqialFP-HM----TIEENIAIVPELKKWDKDKIHDRITELLDSVGLdPESYRHRKPAELSGGEQQRVGVV 148
Cdd:PRK13634 83 LRKKVGIVFQ----FPeHQlfeeTVEKDICFGPMNFGVSEEDAKQKAREMIELVGL-PEELLARSPFELSGGQMRRVAIA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 149 RALAADPGIILMDEPFSALDPISRQRLQQDISALQKKIKKTIVFVTHDMQEALALGDRICVMQDGEIVQVATPQEIIKNP 228
Cdd:PRK13634 158 GVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADP 237
|
.
gi 489843944 229 E 229
Cdd:PRK13634 238 D 238
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
2-226 |
8.15e-42 |
|
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: 145.06 E-value: 8.15e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 2 IRFDNVSKKYNEDKIAVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEKRISDYDIHELRWDIGYV 81
Cdd:cd03254 3 IEFENVNFSYDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMIGVV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 82 LQQIALFPHmTIEENIAIVPELKKWDKDKIHDRITELLDSVGLDPESYRH---RKPAELSGGEQQRVGVVRALAADPGII 158
Cdd:cd03254 83 LQDTFLFSG-TIMENIRLGRPNATDEEVIEAAKEAGAHDFIMKLPNGYDTvlgENGGNLSQGERQLLAIARAMLRDPKIL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489843944 159 LMDEPFSALDPISRQRLQQDISALQKkiKKTIVFVTHDM---QEAlalgDRICVMQDGEIVQVATPQEIIK 226
Cdd:cd03254 162 ILDEATSNIDTETEKLIQEALEKLMK--GRTSIIIAHRLstiKNA----DKILVLDDGKIIEEGTHDELLA 226
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
17-227 |
1.00e-41 |
|
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: 144.50 E-value: 1.00e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 17 AVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEKRISDYDIHE-LRWDIGYVLQQIALFPHMTIEE 95
Cdd:cd03224 15 ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHErARAGIGYVPEGRRIFPELTVEE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 96 NI-----AIVPELKKWDKDKIHDRITELLDSvgldpesyRHRKPAELSGGEQQRVGVVRALAADPGIILMDEPFSALDPI 170
Cdd:cd03224 95 NLllgayARRRAKRKARLERVYELFPRLKER--------RKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLAPK 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 171 srqrLQQDISALQKKIKK---TIVFVTHDMQEALALGDRICVMQDGEIVQVATPQEIIKN 227
Cdd:cd03224 167 ----IVEEIFEAIRELRDegvTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELLAD 222
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
2-216 |
1.37e-41 |
|
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: 143.88 E-value: 1.37e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 2 IRFDNVSKKYNEDKI-AVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEKRISDYDIHELRWDIGY 80
Cdd:cd03245 3 IEFRNVSFSYPNQEIpALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 81 VLQQIALFpHMTIEENIAIvpelkkwdKDKIHD--RITELLDSVGLDPESYRHRKP---------AELSGGEQQRVGVVR 149
Cdd:cd03245 83 VPQDVTLF-YGTLRDNITL--------GAPLADdeRILRAAELAGVTDFVNKHPNGldlqigergRGLSGGQRQAVALAR 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489843944 150 ALAADPGIILMDEPFSALDPISRQRLqqdISALQKKIK-KTIVFVTHDMQeALALGDRICVMQDGEIV 216
Cdd:cd03245 154 ALLNDPPILLLDEPTSAMDMNSEERL---KERLRQLLGdKTLIIITHRPS-LLDLVDRIIVMDSGRIV 217
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
2-238 |
1.67e-41 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 144.39 E-value: 1.67e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 2 IRFDNVSKKYNEDKiAVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINE------KRISDYDIHELR 75
Cdd:COG4161 3 IQLKNINCFYGSHQ-ALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGhqfdfsQKPSEKAIRLLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 76 WDIGYVLQQIALFPHMTIEENIAIVP-ELKKWDKDKIHDRITELLDSVGLDPesYRHRKPAELSGGEQQRVGVVRALAAD 154
Cdd:COG4161 82 QKVGMVFQQYNLWPHLTVMENLIEAPcKVLGLSKEQAREKAMKLLARLRLTD--KADRFPLHLSGGQQQRVAIARALMME 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 155 PGIILMDEPFSALDP-ISRQrlqqdISALQKKIKKT-I--VFVTHDMQEALALGDRICVMQDGEIVQVATpQEIIKNPEN 230
Cdd:COG4161 160 PQVLLFDEPTAALDPeITAQ-----VVEIIRELSQTgItqVIVTHEVEFARKVASQVVYMEKGRIIEQGD-ASHFTQPQT 233
|
....*...
gi 489843944 231 DFVKDFLA 238
Cdd:COG4161 234 EAFAHYLS 241
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
2-217 |
3.73e-41 |
|
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: 142.72 E-value: 3.73e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 2 IRFDNVSKKYNeDKIAVNNVTLDIKDGeFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEKRISDyDIHELRWDIGYV 81
Cdd:cd03264 1 LQLENLTKRYG-KKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLK-QPQKLRRRIGYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 82 LQQIALFPHMTIEENIAIVPELKKWDKDKIHDRITELLDSVGLdpESYRHRKPAELSGGEQQRVGVVRALAADPGIILMD 161
Cdd:cd03264 78 PQEFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNL--GDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489843944 162 EPFSALDPISRQRLQQDISALQKkiKKTIVFVTHDMQEALALGDRICVMQDGEIVQ 217
Cdd:cd03264 156 EPTAGLDPEERIRFRNLLSELGE--DRIVILSTHIVEDVESLCNQVAVLNKGKLVF 209
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
11-237 |
1.80e-40 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 142.49 E-value: 1.80e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 11 YNEDKIAVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEK------RISDYDIHELRWDIGYVLQQ 84
Cdd:PRK14246 19 YINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKvlyfgkDIFQIDAIKLRKEVGMVFQQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 85 IALFPHMTIEENIAIvpELKKW---DKDKIHDRITELLDSVGLDPESY-RHRKPA-ELSGGEQQRVGVVRALAADPGIIL 159
Cdd:PRK14246 99 PNPFPHLSIYDNIAY--PLKSHgikEKREIKKIVEECLRKVGLWKEVYdRLNSPAsQLSGGQQQRLTIARALALKPKVLL 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489843944 160 MDEPFSALDPISRQRLQQDISALQKKIkkTIVFVTHDMQEALALGDRICVMQDGEIVQVATPQEIIKNPENDFVKDFL 237
Cdd:PRK14246 177 MDEPTSMIDIVNSQAIEKLITELKNEI--AIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNELTEKYV 252
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
35-228 |
2.19e-40 |
|
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: 144.87 E-value: 2.19e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 35 GPSGCGKTTTLKMINRLIPLTTGTIYIN-------EKRIsDYDIHELRwdIGYVLQQIALFPHMTIEENIaiVPELKKWD 107
Cdd:TIGR02142 30 GRSGSGKTTLIRLIAGLTRPDEGEIVLNgrtlfdsRKGI-FLPPEKRR--IGYVFQEARLFPHLSVRGNL--RYGMKRAR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 108 KDKIH---DRITELLdsvGLDPesYRHRKPAELSGGEQQRVGVVRALAADPGIILMDEPFSALDPISRQRLQQDISALQK 184
Cdd:TIGR02142 105 PSERRisfERVIELL---GIGH--LLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILPYLERLHA 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 489843944 185 KIKKTIVFVTHDMQEALALGDRICVMQDGEIVQVATPQEIIKNP 228
Cdd:TIGR02142 180 EFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASP 223
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-226 |
5.32e-40 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 146.32 E-value: 5.32e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 1 MIRFDNVSKKYNEDKiAVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEKRISDYDIHE-LRWDIG 79
Cdd:COG1129 4 LLEMRGISKSFGGVK-ALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDaQAAGIA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 80 YVLQQIALFPHMTIEENIAIVPELKKW---DKDKIHDRITELLDSVGL--DPesyrHRKPAELSGGEQQRVGVVRALAAD 154
Cdd:COG1129 83 IIHQELNLVPNLSVAENIFLGREPRRGgliDWRAMRRRARELLARLGLdiDP----DTPVGDLSVAQQQLVEIARALSRD 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489843944 155 PGIILMDEPFSALDPISRQRLQQDISALQKKiKKTIVFVTHDMQEALALGDRICVMQDGEIVQVA-----TPQEIIK 226
Cdd:COG1129 159 ARVLILDEPTASLTEREVERLFRIIRRLKAQ-GVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGpvaelTEDELVR 234
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
2-215 |
7.60e-40 |
|
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: 138.12 E-value: 7.60e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 2 IRFDNVSKKY-NEDKIAVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEKRISDYDIHELRWDIGY 80
Cdd:cd03246 1 LEVENVSFRYpGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 81 VLQQIALFPHmTIEENIaivpelkkwdkdkihdritelldsvgldpesyrhrkpaeLSGGEQQRVGVVRALAADPGIILM 160
Cdd:cd03246 81 LPQDDELFSG-SIAENI---------------------------------------LSGGQRQRLGLARALYGNPRILVL 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489843944 161 DEPFSALDPISRQRLQQDISALQKKiKKTIVFVTHDMqEALALGDRICVMQDGEI 215
Cdd:cd03246 121 DEPNSHLDVEGERALNQAIAALKAA-GATRIVIAHRP-ETLASADRILVLEDGRV 173
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
2-226 |
9.62e-40 |
|
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: 139.67 E-value: 9.62e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 2 IRFDNVSKKYNEDKIAV-NNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEKRISDYDIHELRWDIGY 80
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVlRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 81 VLQQIALFpHMTIEENIAI-VPELkkwDKDKI---------HDRITELldsvgldPESYRHR---KPAELSGGEQQRVGV 147
Cdd:cd03251 81 VSQDVFLF-NDTVAENIAYgRPGA---TREEVeeaaraanaHEFIMEL-------PEGYDTVigeRGVKLSGGQRQRIAI 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489843944 148 VRALAADPGIILMDEPFSALDPISRQRLQQDISALQKkiKKTIVFVTHDMQeALALGDRICVMQDGEIVQVATPQEIIK 226
Cdd:cd03251 150 ARALLKDPPILILDEATSALDTESERLVQAALERLMK--NRTTFVIAHRLS-TIENADRIVVLEDGKIVERGTHEELLA 225
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
2-229 |
1.81e-39 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 140.53 E-value: 1.81e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 2 IRFDNVSKKYNEDKI----AVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEKRISD-----YDIH 72
Cdd:PRK13645 7 IILDNVSYTYAKKTPfefkALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPAnlkkiKEVK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 73 ELRWDIGYVLQ--QIALFPHmTIEENIAIVPELKKWDKDKIHDRITELLDSVGLdPESYRHRKPAELSGGEQQRVGVVRA 150
Cdd:PRK13645 87 RLRKEIGLVFQfpEYQLFQE-TIEKDIAFGPVNLGENKQEAYKKVPELLKLVQL-PEDYVKRSPFELSGGQKRRVALAGI 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489843944 151 LAADPGIILMDEPFSALDPISRQRLQQDISALQKKIKKTIVFVTHDMQEALALGDRICVMQDGEIVQVATPQEIIKNPE 229
Cdd:PRK13645 165 IAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFSNQE 243
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
2-238 |
7.29e-39 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 138.38 E-value: 7.29e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 2 IRFDNVSKKYNeDKIAVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINR---LIP--LTTGTIYINEKRISDYDIH--EL 74
Cdd:PRK14243 11 LRTENLNVYYG-SFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRlndLIPgfRVEGKVTFHGKNLYAPDVDpvEV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 75 RWDIGYVLQQIALFPHmTIEENIAIVPELK--KWDKDKIHDRitELLDSVGLDPESYRHRKPA-ELSGGEQQRVGVVRAL 151
Cdd:PRK14243 90 RRRIGMVFQKPNPFPK-SIYDNIAYGARINgyKGDMDELVER--SLRQAALWDEVKDKLKQSGlSLSGGQQQRLCIARAI 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 152 AADPGIILMDEPFSALDPISRQRLQQDISALQKKIkkTIVFVTHDMQEALALGDRICVM---------QDGEIVQVATPQ 222
Cdd:PRK14243 167 AVQPEVILMDEPCSALDPISTLRIEELMHELKEQY--TIIIVTHNMQQAARVSDMTAFFnveltegggRYGYLVEFDRTE 244
|
250
....*....|....*.
gi 489843944 223 EIIKNPENDFVKDFLA 238
Cdd:PRK14243 245 KIFNSPQQQATRDYVS 260
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
2-226 |
1.13e-38 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 138.37 E-value: 1.13e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 2 IRFDNVSKKYNE----DKIAVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEKRIS----DYDIHE 73
Cdd:PRK13646 3 IRFDNVSYTYQKgtpyEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIThktkDKYIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 74 LRWDIGYVLQqialFPHM-----TIEENIAIVPELKKWDKDKIHDRITELLDSVGLdPESYRHRKPAELSGGEQQRVGVV 148
Cdd:PRK13646 83 VRKRIGMVFQ----FPESqlfedTVEREIIFGPKNFKMNLDEVKNYAHRLLMDLGF-SRDVMSQSPFQMSGGQMRKIAIV 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489843944 149 RALAADPGIILMDEPFSALDPISRQRLQQDISALQKKIKKTIVFVTHDMQEALALGDRICVMQDGEIVQVATPQEIIK 226
Cdd:PRK13646 158 SILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFK 235
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
2-216 |
1.14e-38 |
|
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: 136.08 E-value: 1.14e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 2 IRFDNVSKKYNEdkiavNNVTLD--IKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEKRISDYDIHELrwDIG 79
Cdd:cd03298 1 VRLDKIRFSYGE-----QPMHFDltFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADR--PVS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 80 YVLQQIALFPHMTIEENIAI--VPELKKWDKDKihDRITELLDSVGLDpeSYRHRKPAELSGGEQQRVGVVRALAADPGI 157
Cdd:cd03298 74 MLFQENNLFAHLTVEQNVGLglSPGLKLTAEDR--QAIEVALARVGLA--GLEKRLPGELSGGERQRVALARVLVRDKPV 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489843944 158 ILMDEPFSALDPISRQRLQQDISALQKKIKKTIVFVTHDMQEALALGDRICVMQDGEIV 216
Cdd:cd03298 150 LLLDEPFAALDPALRAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIA 208
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
21-237 |
1.22e-38 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 137.35 E-value: 1.22e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 21 VTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPL-----TTGTIYINEKRISDYDIHELRWDIGYVLQQIALFPHMTIEE 95
Cdd:PRK14247 22 VNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELypearVSGEVYLDGQDIFKMDVIELRRRVQMVFQIPNPIPNLSIFE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 96 NIAIVPELKKWDKDK--IHDRITELLDSVGL-DPESYRHRKPA-ELSGGEQQRVGVVRALAADPGIILMDEPFSALDPIS 171
Cdd:PRK14247 102 NVALGLKLNRLVKSKkeLQERVRWALEKAQLwDEVKDRLDAPAgKLSGGQQQRLCIARALAFQPEVLLADEPTANLDPEN 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489843944 172 RQRLQQDISALQKKIkkTIVFVTHDMQEALALGDRICVMQDGEIVQVATPQEIIKNPENDFVKDFL 237
Cdd:PRK14247 182 TAKIESLFLELKKDM--TIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTNPRHELTEKYV 245
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
2-238 |
1.37e-38 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 137.07 E-value: 1.37e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 2 IRFDNVSKKYNEDKiAVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYIN------EKRISDYDIHELR 75
Cdd:PRK11124 3 IQLNGINCFYGAHQ-ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAgnhfdfSKTPSDKAIRELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 76 WDIGYVLQQIALFPHMTIEENIAIVP-ELKKWDKDKIHDRITELLDSVGLDPesYRHRKPAELSGGEQQRVGVVRALAAD 154
Cdd:PRK11124 82 RNVGMVFQQYNLWPHLTVQQNLIEAPcRVLGLSKDQALARAEKLLERLRLKP--YADRFPLHLSGGQQQRVAIARALMME 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 155 PGIILMDEPFSALDP-ISRQrLQQDISALQK-KIkkTIVFVTHDMQEALALGDRICVMQDGEIVQVATpQEIIKNPENDF 232
Cdd:PRK11124 160 PQVLLFDEPTAALDPeITAQ-IVSIIRELAEtGI--TQVIVTHEVEVARKTASRVVYMENGHIVEQGD-ASCFTQPQTEA 235
|
....*.
gi 489843944 233 VKDFLA 238
Cdd:PRK11124 236 FKNYLS 241
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1-225 |
1.44e-38 |
|
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: 143.02 E-value: 1.44e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 1 MIRFDNVSKKY-NEDK---IAVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYInekRISD--YDIHEL 74
Cdd:TIGR03269 279 IIKVRNVSKRYiSVDRgvvKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNV---RVGDewVDMTKP 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 75 RWD--------IGYVLQQIALFPHMTIEENI--AIVPELKKwdkDKIHDRITELLDSVGLDPESYRH---RKPAELSGGE 141
Cdd:TIGR03269 356 GPDgrgrakryIGILHQEYDLYPHRTVLDNLteAIGLELPD---ELARMKAVITLKMVGFDEEKAEEildKYPDELSEGE 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 142 QQRVGVVRALAADPGIILMDEPFSALDPISRQRLQQDISALQKKIKKTIVFVTHDMQEALALGDRICVMQDGEIVQVATP 221
Cdd:TIGR03269 433 RHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDP 512
|
....
gi 489843944 222 QEII 225
Cdd:TIGR03269 513 EEIV 516
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-223 |
1.44e-37 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 133.71 E-value: 1.44e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 1 MIRFDNVSKKYNEDKIAVN---NVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEKRISDYDihE---- 73
Cdd:COG4181 8 IIELRGLTKTVGTGAGELTilkGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALD--Edara 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 74 -LRWD-IGYVLQQIALFPHMTIEENIAIVPELKKwDKDKiHDRITELLDSVGLDpESYRHRkPAELSGGEQQRVGVVRAL 151
Cdd:COG4181 86 rLRARhVGFVFQSFQLLPTLTALENVMLPLELAG-RRDA-RARARALLERVGLG-HRLDHY-PAQLSGGEQQRVALARAF 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489843944 152 AADPGIILMDEPFSALDPISRQRLQQDISALQKKIKKTIVFVTHDMQEAlALGDRICVMQDGEIVQVATPQE 223
Cdd:COG4181 162 ATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALA-ARCDRVLRLRAGRLVEDTAATA 232
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
11-237 |
2.05e-37 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 134.20 E-value: 2.05e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 11 YNEDKIAVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEKRISDYDIH-------ELRWDIGYVLQ 83
Cdd:PRK14267 13 YYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNEEARVEGEVRLFGRNIYspdvdpiEVRREVGMVFQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 84 QIALFPHMTIEENIAIVPELKKW--DKDKIHDRITELLDSVGLDPEsYRHR---KPAELSGGEQQRVGVVRALAADPGII 158
Cdd:PRK14267 93 YPNPFPHLTIYDNVAIGVKLNGLvkSKKELDERVEWALKKAALWDE-VKDRlndYPSNLSGGQRQRLVIARALAMKPKIL 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489843944 159 LMDEPFSALDPISRQRLQQDISALQKKIkkTIVFVTHDMQEALALGDRICVMQDGEIVQVATPQEIIKNPENDFVKDFL 237
Cdd:PRK14267 172 LMDEPTANIDPVGTAKIEELLFELKKEY--TIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENPEHELTEKYV 248
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1-225 |
3.20e-37 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 133.67 E-value: 3.20e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 1 MIRFDNVSKKYNEDKIaVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEKRISDYDIHELRWDIGy 80
Cdd:COG4604 1 MIEIKNVSKRYGGKVV-LDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLA- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 81 VLQQ---IAL------------FPH----MTIEeniaivpelkkwDKDKIhdriTELLDSVGLDPesYRHRKPAELSGGE 141
Cdd:COG4604 79 ILRQenhINSrltvrelvafgrFPYskgrLTAE------------DREII----DEAIAYLDLED--LADRYLDELSGGQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 142 QQRVGVVRALAADPGIILMDEPFSALDPI-SRQRLQQdISALQKKIKKTIVFVTHDMQEALALGDRICVMQDGEIVQVAT 220
Cdd:COG4604 141 RQRAFIAMVLAQDTDYVLLDEPLNNLDMKhSVQMMKL-LRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGT 219
|
....*
gi 489843944 221 PQEII 225
Cdd:COG4604 220 PEEII 224
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
5-229 |
7.88e-37 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 132.32 E-value: 7.88e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 5 DNVSKKYNEDKIaVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEKRISDYDIHE-LRWDIGYVLQ 83
Cdd:PRK10895 7 KNLAKAYKGRRV-VEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHArARRGIGYLPQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 84 QIALFPHMTIEENIAIVPELKK-WDKDKIHDRITELLDSVGLdpESYRHRKPAELSGGEQQRVGVVRALAADPGIILMDE 162
Cdd:PRK10895 86 EASIFRRLSVYDNLMAVLQIRDdLSAEQREDRANELMEEFHI--EHLRDSMGQSLSGGERRRVEIARALAANPKFILLDE 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489843944 163 PFSALDPISRQRLQQDISALQKKiKKTIVFVTHDMQEALALGDRICVMQDGEIVQVATPQEIIKNPE 229
Cdd:PRK10895 164 PFAGVDPISVIDIKRIIEHLRDS-GLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDEH 229
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
2-226 |
8.24e-37 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 138.73 E-value: 8.24e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 2 IRFDNVSKKY-NEDKIAVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEKRISDYDIHELRWDIGY 80
Cdd:COG4618 331 LSVENLTVVPpGSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRHIGY 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 81 VLQQIALFPHmTIEENIAIVPELkkwDKDKI---------HDRITELldsvgldPESYRHRKPAE---LSGGEQQRVGVV 148
Cdd:COG4618 411 LPQDVELFDG-TIAENIARFGDA---DPEKVvaaaklagvHEMILRL-------PDGYDTRIGEGgarLSGGQRQRIGLA 479
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489843944 149 RALAADPGIILMDEPFSALDPISRQRLQQDISALqKKIKKTIVFVTHDMQeALALGDRICVMQDGEIVQVATPQEIIK 226
Cdd:COG4618 480 RALYGDPRLVVLDEPNSNLDDEGEAALAAAIRAL-KARGATVVVITHRPS-LLAAVDKLLVLRDGRVQAFGPRDEVLA 555
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1-228 |
1.15e-36 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 132.80 E-value: 1.15e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 1 MIRFDNVSKKYNEDKIAVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEKRISDYD-IHELRWDIG 79
Cdd:PRK13644 1 MIRLENVSYSYPDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSkLQGIRKLVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 80 YVLQQIAL-FPHMTIEENIAIVPELKKWDKDKIHDRITELLDSVGLdpESYRHRKPAELSGGEQQRVGVVRALAADPGII 158
Cdd:PRK13644 81 IVFQNPETqFVGRTVEEDLAFGPENLCLPPIEIRKRVDRALAEIGL--EKYRHRSPKTLSGGQGQCVALAGILTMEPECL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 159 LMDEPFSALDPISRQRLQQDISALQKKiKKTIVFVTHDMQEaLALGDRICVMQDGEIVQVATPQEIIKNP 228
Cdd:PRK13644 159 IFDEVTSMLDPDSGIAVLERIKKLHEK-GKTIVYITHNLEE-LHDADRIIVMDRGKIVLEGEPENVLSDV 226
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
2-218 |
2.00e-36 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 130.37 E-value: 2.00e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 2 IRFDNVSKKYNEDKIAVNnvtLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEK---RISDYdihelRWDI 78
Cdd:TIGR01277 1 LALDKVRYEYEHLPMEFD---LNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQshtGLAPY-----QRPV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 79 GYVLQQIALFPHMTIEENIA--IVPELK--KWDKDKIHDriteLLDSVGLDpeSYRHRKPAELSGGEQQRVGVVRALAAD 154
Cdd:TIGR01277 73 SMLFQENNLFAHLTVRQNIGlgLHPGLKlnAEQQEKVVD----AAQQVGIA--DYLDRLPEQLSGGQRQRVALARCLVRP 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489843944 155 PGIILMDEPFSALDPISRQRLQQDISALQKKIKKTIVFVTHDMQEALALGDRICVMQDGEIVQV 218
Cdd:TIGR01277 147 NPILLLDEPFSALDPLLREEMLALVKQLCSERQRTLLMVTHHLSDARAIASQIAVVSQGKIKVV 210
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
9-238 |
2.16e-36 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 131.63 E-value: 2.16e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 9 KKYNEDKIaVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEKRIS---DYD----------IHELR 75
Cdd:PRK10619 13 KRYGEHEV-LKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrDKDgqlkvadknqLRLLR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 76 WDIGYVLQQIALFPHMTIEENIAIVP-ELKKWDKDKIHDRITELLDSVGLDpESYRHRKPAELSGGEQQRVGVVRALAAD 154
Cdd:PRK10619 92 TRLTMVFQHFNLWSHMTVLENVMEAPiQVLGLSKQEARERAVKYLAKVGID-ERAQGKYPVHLSGGQQQRVSIARALAME 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 155 PGIILMDEPFSALDPisrqRLQQDISALQKKIK---KTIVFVTHDMQEALALGDRICVMQDGEIVQVATPQEIIKNPEND 231
Cdd:PRK10619 171 PEVLLFDEPTSALDP----ELVGEVLRIMQQLAeegKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGNPQSP 246
|
....*..
gi 489843944 232 FVKDFLA 238
Cdd:PRK10619 247 RLQQFLK 253
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
21-242 |
2.70e-36 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 131.46 E-value: 2.70e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 21 VTLDIKDGEFFVFIGPSGCGKTTTLKMINRL-IPlTTGTIYIN------------EKRISDYD-IHELRWDIGYVLQQIA 86
Cdd:COG4598 27 VSLTARKGDVISIIGSSGSGKSTFLRCINLLeTP-DSGEIRVGgeeirlkpdrdgELVPADRRqLQRIRTRLGMVFQSFN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 87 LFPHMTIEENIAIVP-ELKKWDKDKIHDRITELLDSVGLdpESYRHRKPAELSGGEQQRVGVVRALAADPGIILMDEPFS 165
Cdd:COG4598 106 LWSHMTVLENVIEAPvHVLGRPKAEAIERAEALLAKVGL--ADKRDAYPAHLSGGQQQRAAIARALAMEPEVMLFDEPTS 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 166 ALDPisrqRLQQDISALQKKIK---KTIVFVTHDMQEALALGDRICVMQDGEIVQVATPQEIIKNPENDFVKDFLASGHA 242
Cdd:COG4598 184 ALDP----ELVGEVLKVMRDLAeegRTMLVVTHEMGFARDVSSHVVFLHQGRIEEQGPPAEVFGNPKSERLRQFLSSSLK 259
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
2-216 |
4.30e-36 |
|
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: 129.26 E-value: 4.30e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 2 IRFDNVSKKYNEdKIAVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEKriSDYDIHELRWDIGYV 81
Cdd:cd03268 1 LKTNDLTKTYGK-KRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGK--SYQKNIEALRRIGAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 82 LQQIALFPHMTIEENIAIVPELkkwdKDKIHDRITELLDSVGLDpeSYRHRKPAELSGGEQQRVGVVRALAADPGIILMD 161
Cdd:cd03268 78 IEAPGFYPNLTARENLRLLARL----LGIRKKRIDEVLDVVGLK--DSAKKKVKGFSLGMKQRLGIALALLGNPDLLILD 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489843944 162 EPFSALDPISRQRLQQDISALQKKiKKTIVFVTHDMQEALALGDRICVMQDGEIV 216
Cdd:cd03268 152 EPTNGLDPDGIKELRELILSLRDQ-GITVLISSHLLSEIQKVADRIGIINKGKLI 205
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
17-234 |
5.33e-36 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 132.52 E-value: 5.33e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 17 AVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEK---RISDYDIHELRWDIGYVLQQ--IALFPHM 91
Cdd:PRK15079 36 AVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKdllGMKDDEWRAVRSDIQMIFQDplASLNPRM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 92 TIEENIA-----IVPELKKwdkDKIHDRITELLDSVGLDPESYrHRKPAELSGGEQQRVGVVRALAADPGIILMDEPFSA 166
Cdd:PRK15079 116 TIGEIIAeplrtYHPKLSR---QEVKDRVKAMMLKVGLLPNLI-NRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSA 191
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489843944 167 LDpISRQR-----LQQdisaLQKKIKKTIVFVTHDMQEALALGDRICVMQDGEIVQVATPQEIIKNPENDFVK 234
Cdd:PRK15079 192 LD-VSIQAqvvnlLQQ----LQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNPLHPYTK 259
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-239 |
5.75e-36 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 130.54 E-value: 5.75e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 2 IRFDNVSKKYNEDKIaVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTT-----GTI-----YINEKRIsdyDI 71
Cdd:PRK14258 8 IKVNNLSFYYDTQKI-LEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVeffnqNIYERRV---NL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 72 HELRWDIGYVLQQIALFPhMTIEENIAIVPELKKWD-KDKIHDRITELLDSVGLDPESYR--HRKPAELSGGEQQRVGVV 148
Cdd:PRK14258 84 NRLRRQVSMVHPKPNLFP-MSVYDNVAYGVKIVGWRpKLEIDDIVESALKDADLWDEIKHkiHKSALDLSGGQQQRLCIA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 149 RALAADPGIILMDEPFSALDPISRQRLQQDISALQKKIKKTIVFVTHDMQEALALGDRICVMQD-----GEIVQVATPQE 223
Cdd:PRK14258 163 RALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGnenriGQLVEFGLTKK 242
|
250
....*....|....*.
gi 489843944 224 IIKNPENDFVKDFLAS 239
Cdd:PRK14258 243 IFNSPHDSRTREYVLS 258
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
17-239 |
8.84e-36 |
|
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: 135.58 E-value: 8.84e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 17 AVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIP----LTTGTIYINEKRISDYDIHELRW----DIGYVLQQ--IA 86
Cdd:COG4172 25 AVKGVSFDIAAGETLALVGESGSGKSVTALSILRLLPdpaaHPSGSILFDGQDLLGLSERELRRirgnRIAMIFQEpmTS 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 87 LFPHMTIEENIAIVPEL-KKWDKDKIHDRITELLDSVGL-DPESYRHRKPAELSGGEQQRVGVVRALAADPGIILMDEPF 164
Cdd:COG4172 105 LNPLHTIGKQIAEVLRLhRGLSGAAARARALELLERVGIpDPERRLDAYPHQLSGGQRQRVMIAMALANEPDLLIADEPT 184
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489843944 165 SALDP-ISRQRLQQdISALQKKIKKTIVFVTHDMQEALALGDRICVMQDGEIVQVATPQEIIKNPENDFVKDFLAS 239
Cdd:COG4172 185 TALDVtVQAQILDL-LKDLQRELGMALLLITHDLGVVRRFADRVAVMRQGEIVEQGPTAELFAAPQHPYTRKLLAA 259
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
5-215 |
9.76e-36 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 129.80 E-value: 9.76e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 5 DNVSKKYNEDKIaVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGtiyinEKRISDYDIHELRWDIGYVLQQ 84
Cdd:PRK11247 16 NAVSKRYGERTV-LNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAG-----ELLAGTAPLAEAREDTRLMFQD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 85 IALFPHMTIEENIAIvpELK-KWdkdkiHDRITELLDSVGLdpESYRHRKPAELSGGEQQRVGVVRALAADPGIILMDEP 163
Cdd:PRK11247 90 ARLLPWKKVIDNVGL--GLKgQW-----RDAALQALAAVGL--ADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 489843944 164 FSALDPISRQRLQQDISALQKKIKKTIVFVTHDMQEALALGDRICVMQDGEI 215
Cdd:PRK11247 161 LGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
2-210 |
2.47e-35 |
|
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: 134.34 E-value: 2.47e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 2 IRFDNVSKKYNEDKIAVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEKRISDYDIHELRWDIGYV 81
Cdd:TIGR02857 322 LEFSGVSVAYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWV 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 82 LQQIALFPHmTIEENIAIvpelkkWDKDKIHDRITELLDSVGLD------PESYRHR---KPAELSGGEQQRVGVVRALA 152
Cdd:TIGR02857 402 PQHPFLFAG-TIAENIRL------ARPDASDAEIREALERAGLDefvaalPQGLDTPigeGGAGLSGGQAQRLALARAFL 474
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489843944 153 ADPGIILMDEPFSALDPISRQRLQQDISALQKkiKKTIVFVTHDMqEALALGDRICVM 210
Cdd:TIGR02857 475 RDAPLLLLDEPTAHLDAETEAEVLEALRALAQ--GRTVLLVTHRL-ALAALADRIVVL 529
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1-229 |
2.76e-35 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 129.10 E-value: 2.76e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 1 MIRFDNVSKKYNEDK-IAVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEKRISDYDIHELRWDIG 79
Cdd:PRK13648 7 IIVFKNVSFQYQSDAsFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 80 YVLQQIA-LFPHMTIEENIAIVPELKKWDKDKIHDRITELLDSVGLdpESYRHRKPAELSGGEQQRVGVVRALAADPGII 158
Cdd:PRK13648 87 IVFQNPDnQFVGSIVKYDVAFGLENHAVPYDEMHRRVSEALKQVDM--LERADYEPNALSGGQKQRVAIAGVLALNPSVI 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489843944 159 LMDEPFSALDPISRQRLQQDISALQKKIKKTIVFVTHDMQEALAlGDRICVMQDGEIVQVATPQEIIKNPE 229
Cdd:PRK13648 165 ILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIFDHAE 234
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-216 |
6.91e-35 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 127.89 E-value: 6.91e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 1 MIRFDNVSKKYN----EDKIAVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEKRISDYDIHELRW 76
Cdd:COG1101 1 MLELKNLSKTFNpgtvNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 77 DIGYVLQ--QIALFPHMTIEENIAI----------VPELKKWDKDKIHDRITEL-------LDS-VGLdpesyrhrkpae 136
Cdd:COG1101 81 YIGRVFQdpMMGTAPSMTIEENLALayrrgkrrglRRGLTKKRRELFRELLATLglglenrLDTkVGL------------ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 137 LSGGEQQRVGVVRALAADPGIILMDEPFSALDPisrqRLQQDISALQKKI----KKTIVFVTHDMQEALALGDRICVMQD 212
Cdd:COG1101 149 LSGGQRQALSLLMATLTKPKLLLLDEHTAALDP----KTAALVLELTEKIveenNLTTLMVTHNMEQALDYGNRLIMMHE 224
|
....
gi 489843944 213 GEIV 216
Cdd:COG1101 225 GRII 228
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
2-235 |
1.41e-34 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 127.89 E-value: 1.41e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 2 IRFDNVSKKYN-----EDKiAVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTI---YINEK------RIS 67
Cdd:PRK13651 3 IKVKNIVKIFNkklptELK-ALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewiFKDEKnkkktkEKE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 68 DY---------------DIHELRWDIGYVLQ--QIALFpHMTIEENIAIVPELKKWDKDKIHDRITELLDSVGLdPESYR 130
Cdd:PRK13651 82 KVleklviqktrfkkikKIKEIRRRVGVVFQfaEYQLF-EQTIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGL-DESYL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 131 HRKPAELSGGEQQRVGVVRALAADPGIILMDEPFSALDPISRQRLQQDISALQKKiKKTIVFVTHDMQEALALGDRICVM 210
Cdd:PRK13651 160 QRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQ-GKTIILVTHDLDNVLEWTKRTIFF 238
|
250 260
....*....|....*....|....*
gi 489843944 211 QDGEIVQVATPQEIIKNpeNDFVKD 235
Cdd:PRK13651 239 KDGKIIKDGDTYDILSD--NKFLIE 261
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-225 |
1.89e-34 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 127.61 E-value: 1.89e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 2 IRFDNVSKKYNeDKIAVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEKRISDYdIHELRWDIGYV 81
Cdd:PRK13537 8 IDFRNVEKRYG-DKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSR-ARHARQRVGVV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 82 LQQIALFPHMTIEENIAIVPELKKWDKDKIHDRITELLDSVGLdpESYRHRKPAELSGGEQQRVGVVRALAADPGIILMD 161
Cdd:PRK13537 86 PQFDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKL--ENKADAKVGELSGGMKRRLTLARALVNDPDVLVLD 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489843944 162 EPFSALDPISRQRLQQDISALQKKiKKTIVFVTHDMQEALALGDRICVMQDGEIVQVATPQEII 225
Cdd:PRK13537 164 EPTTGLDPQARHLMWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALI 226
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1-229 |
2.12e-34 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 126.73 E-value: 2.12e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 1 MIRFDNVSKKYNEDKIAVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEKRIsDYD---IHELRWD 77
Cdd:PRK13639 1 ILETRDLKYSYPDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPI-KYDkksLLEVRKT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 78 IGYVLQQI--ALFPHmTIEENIAIVPELKKWDKDKIHDRITELLDSVGLdpESYRHRKPAELSGGEQQRVGVVRALAADP 155
Cdd:PRK13639 80 VGIVFQNPddQLFAP-TVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGM--EGFENKPPHHLSGGQKKRVAIAGILAMKP 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489843944 156 GIILMDEPFSALDPISRQRLQQDISALQKKiKKTIVFVTHDMQEALALGDRICVMQDGEIVQVATPQEIIKNPE 229
Cdd:PRK13639 157 EIIVLDEPTSGLDPMGASQIMKLLYDLNKE-GITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDIE 229
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-223 |
9.06e-34 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 129.38 E-value: 9.06e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 1 MIRFDNVSKKYNeDKIAVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEKRIsdyDIHE----LRW 76
Cdd:COG3845 5 ALELRGITKRFG-GVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPV---RIRSprdaIAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 77 DIGYVLQQIALFPHMTIEENIAI-VPELKKW--DKDKIHDRITELLDSVGL--DPesyrHRKPAELSGGEQQRVGVVRAL 151
Cdd:COG3845 81 GIGMVHQHFMLVPNLTVAENIVLgLEPTKGGrlDRKAARARIRELSERYGLdvDP----DAKVEDLSVGEQQRVEILKAL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489843944 152 AADPGIILMDEPFSALDPISRQRLQQDISALQKKiKKTIVFVTHDMQEALALGDRICVMQDGEIVQVATPQE 223
Cdd:COG3845 157 YRGARILILDEPTAVLTPQEADELFEILRRLAAE-GKSIIFITHKLREVMAIADRVTVLRRGKVVGTVDTAE 227
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-227 |
1.30e-33 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 129.94 E-value: 1.30e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 2 IRFDNVSKKY-NEDKIAVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEKRISDYDIHELRWDIGY 80
Cdd:PRK11160 339 LTLNNVSFTYpDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQAISV 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 81 VLQQIALFPHmTIEENIAIVpelkkwdKDKIHD-RITELLDSVGLDP-------------ESYRhrkpaELSGGEQQRVG 146
Cdd:PRK11160 419 VSQRVHLFSA-TLRDNLLLA-------APNASDeALIEVLQQVGLEKlleddkglnawlgEGGR-----QLSGGEQRRLG 485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 147 VVRALAADPGIILMDEPFSALDpisRQRLQQDISALQKKIK-KTIVFVTHDMQeALALGDRICVMQDGEIVQVATPQEII 225
Cdd:PRK11160 486 IARALLHDAPLLLLDEPTEGLD---AETERQILELLAEHAQnKTVLMITHRLT-GLEQFDRICVMDNGQIIEQGTHQELL 561
|
..
gi 489843944 226 KN 227
Cdd:PRK11160 562 AQ 563
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1-230 |
1.61e-33 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 124.43 E-value: 1.61e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 1 MIRFDNVSKKYNE--DKIAVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEKRISDYDIHELRWDI 78
Cdd:PRK13642 4 ILEVENLVFKYEKesDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 79 GYVLQQI-ALFPHMTIEENIAIVPELKKWDKDKIHDRITELLDSVGLdpESYRHRKPAELSGGEQQRVGVVRALAADPGI 157
Cdd:PRK13642 84 GMVFQNPdNQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNM--LDFKTREPARLSGGQKQRVAVAGIIALRPEI 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489843944 158 ILMDEPFSALDPISRQRLQQDISALQKKIKKTIVFVTHDMQEAlALGDRICVMQDGEIVQVATPQEIIKNPEN 230
Cdd:PRK13642 162 IILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEA-ASSDRILVMKAGEIIKEAAPSELFATSED 233
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1-272 |
1.72e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 124.53 E-value: 1.72e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 1 MIRFDNVSKKYNEDKIAVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEKRISDYDIHELRWDIGY 80
Cdd:PRK13652 3 LIETRDLCYSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 81 VLQ----QIAlfpHMTIEENIAIVPELKKWDKDKIHDRITELLDSVGLdpESYRHRKPAELSGGEQQRVGVVRALAADPG 156
Cdd:PRK13652 83 VFQnpddQIF---SPTVEQDIAFGPINLGLDEETVAHRVSSALHMLGL--EELRDRVPHHLSGGEKKRVAIAGVIAMEPQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 157 IILMDEPFSALDPISRQRLQQDISALQKKIKKTIVFVTHDMQEALALGDRICVMQDGEIVQVATPQEIIKNPendfvkDF 236
Cdd:PRK13652 158 VLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP------DL 231
|
250 260 270
....*....|....*....|....*....|....*...
gi 489843944 237 LASGHaFNTPILEG--SFTVNDLIDADLFYAYQTSDGS 272
Cdd:PRK13652 232 LARVH-LDLPSLPKliRSLQAQGIAIDMAYTYQEAEDA 268
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1-225 |
1.78e-33 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 123.97 E-value: 1.78e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 1 MIRFDNVSKKYNEDKIaVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEKRISDYDIHELRwdigy 80
Cdd:PRK11231 2 TLRTENLTVGYGTKRI-LNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLA----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 81 vlQQIALFP-HMTIEENIAI--------VPELKKWDK--DKIHDRITELLDSVGLDpeSYRHRKPAELSGGEQQRVGVVR 149
Cdd:PRK11231 76 --RRLALLPqHHLTPEGITVrelvaygrSPWLSLWGRlsAEDNARVNQAMEQTRIN--HLADRRLTDLSGGQRQRAFLAM 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489843944 150 ALAADPGIILMDEPFSALDpISRQ-RLQQDISALQKKiKKTIVFVTHDMQEALALGDRICVMQDGEIVQVATPQEII 225
Cdd:PRK11231 152 VLAQDTPVVLLDEPTTYLD-INHQvELMRLMRELNTQ-GKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVM 226
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
1-264 |
4.04e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 124.58 E-value: 4.04e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 1 MIRFDNVSKKYNEDK----IAVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYI--------------- 61
Cdd:PRK13631 21 ILRVKNLYCVFDEKQenelVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVgdiyigdkknnheli 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 62 ---NEKRISDYDihELRWDIGYVLQqialFPHM-----TIEENIAIVPELKKWDKDKIHDRITELLDSVGLDpESYRHRK 133
Cdd:PRK13631 101 tnpYSKKIKNFK--ELRRRVSMVFQ----FPEYqlfkdTIEKDIMFGPVALGVKKSEAKKLAKFYLNKMGLD-DSYLERS 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 134 PAELSGGEQQRVGVVRALAADPGIILMDEPFSALDPISRQRLQQDISAlQKKIKKTIVFVTHDMQEALALGDRICVMQDG 213
Cdd:PRK13631 174 PFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILD-AKANNKTVFVITHTMEHVLEVADEVIVMDKG 252
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 489843944 214 EIVQVATPQEIIKNPendfvkDFLASGHAFNTPILEgsfTVNDLIDADLFY 264
Cdd:PRK13631 253 KILKTGTPYEIFTDQ------HIINSTSIQVPRVIQ---VINDLIKKDPKY 294
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
17-239 |
5.97e-33 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 128.43 E-value: 5.97e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 17 AVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEKRI---SDYDIHELRWDIGYVLQQ--IALFPHM 91
Cdd:PRK10261 339 AVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIdtlSPGKLQALRRDIQFIFQDpyASLDPRQ 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 92 TIeeNIAIVPELKK---WDKDKIHDRITELLDSVGLDPEsYRHRKPAELSGGEQQRVGVVRALAADPGIILMDEPFSALD 168
Cdd:PRK10261 419 TV--GDSIMEPLRVhglLPGKAAAARVAWLLERVGLLPE-HAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALD 495
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489843944 169 PISRQRLQQDISALQKKIKKTIVFVTHDMQEALALGDRICVMQDGEIVQVATPQEIIKNPENDFVKDFLAS 239
Cdd:PRK10261 496 VSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENPQHPYTRKLMAA 566
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-226 |
7.69e-33 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 124.17 E-value: 7.69e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 2 IRFDNVSKKYNeDKIAVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEKRISDyDIHELRWDIGYV 81
Cdd:PRK13536 42 IDLAGVSKSYG-DKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPA-RARLARARIGVV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 82 LQQIALFPHMTIEENIAIVPELKKWDKDKIHDRITELLDSVGLdpESYRHRKPAELSGGEQQRVGVVRALAADPGIILMD 161
Cdd:PRK13536 120 PQFDNLDLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARL--ESKADARVSDLSGGMKRRLTLARALINDPQLLILD 197
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489843944 162 EPFSALDPISRQRLQQDISALQKKiKKTIVFVTHDMQEALALGDRICVMQDGEIVQVATPQEIIK 226
Cdd:PRK13536 198 EPTTGLDPHARHLIWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHALID 261
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-230 |
7.95e-33 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 122.15 E-value: 7.95e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 1 MIRFDNVSKKYNeDKIAVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEKRISDYDIHEL---Rwd 77
Cdd:COG4559 1 MLEAENLSVRLG-GRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELarrR-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 78 igYVL-QQIAL-FPhMTIEENIAI--VPelkkWDKDKIHDR--ITELLDSVGLDPesYRHRKPAELSGGEQQRVGVVRAL 151
Cdd:COG4559 78 --AVLpQHSSLaFP-FTVEEVVALgrAP----HGSSAAQDRqiVREALALVGLAH--LAGRSYQTLSGGEQQRVQLARVL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 152 A-------ADPGIILMDEPFSALDPisrqRLQQDISALQKKIKK---TIVFVTHDMQEALALGDRICVMQDGEIVQVATP 221
Cdd:COG4559 149 AqlwepvdGGPRWLFLDEPTSALDL----AHQHAVLRLARQLARrggGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTP 224
|
....*....
gi 489843944 222 QEIIkNPEN 230
Cdd:COG4559 225 EEVL-TDEL 232
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
2-216 |
9.55e-33 |
|
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: 119.07 E-value: 9.55e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 2 IRFDNVSKKYNeDKIAVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEKRISDYDIHE-LRWDIGY 80
Cdd:cd03216 1 LELRGITKRFG-GVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDaRRAGIAM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 81 VLQqialfphmtieeniaivpelkkwdkdkihdritelldsvgldpesyrhrkpaeLSGGEQQRVGVVRALAADPGIILM 160
Cdd:cd03216 80 VYQ-----------------------------------------------------LSVGERQMVEIARALARNARLLIL 106
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489843944 161 DEPFSALDPISRQRLQQDISALQKKiKKTIVFVTHDMQEALALGDRICVMQDGEIV 216
Cdd:cd03216 107 DEPTAALTPAEVERLFKVIRRLRAQ-GVAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
2-225 |
2.31e-32 |
|
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: 120.28 E-value: 2.31e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 2 IRFDNVSKKYNED-KIAVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEKRISDYDIHELRWDIGY 80
Cdd:cd03252 1 ITFEHVRFRYKPDgPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 81 VLQQIALFpHMTIEENIAIVPElkKWDKDKI---------HDRITELldsvgldPESYRH---RKPAELSGGEQQRVGVV 148
Cdd:cd03252 81 VLQENVLF-NRSIRDNIALADP--GMSMERVieaaklagaHDFISEL-------PEGYDTivgEQGAGLSGGQRQRIAIA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489843944 149 RALAADPGIILMDEPFSALDPISRQRLQQDISALQKkiKKTIVFVTHDMQeALALGDRICVMQDGEIVQVATPQEII 225
Cdd:cd03252 151 RALIHNPRILIFDEATSALDYESEHAIMRNMHDICA--GRTVIIIAHRLS-TVKNADRIIVMEKGRIVEQGSHDELL 224
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
2-260 |
2.75e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 121.47 E-value: 2.75e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 2 IRFDNVSKKYNE----DKIAVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEKRI----SDYDIHE 73
Cdd:PRK13641 3 IKFENVDYIYSPgtpmEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHItpetGNKNLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 74 LRWDIGYVLQ--QIALFPHmTIEENIAIVPELKKWDKDKIHDRITELLDSVGLdPESYRHRKPAELSGGEQQRVGVVRAL 151
Cdd:PRK13641 83 LRKKVSLVFQfpEAQLFEN-TVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGL-SEDLISKSPFELSGGQMRRVAIAGVM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 152 AADPGIILMDEPFSALDPISRQRLQQDISALQKKiKKTIVFVTHDMQEALALGDRICVMQDGEIVQVATPQEIIKNPE-- 229
Cdd:PRK13641 161 AYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKA-GHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDKEwl 239
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 489843944 230 ----------NDFVKDFLASGHAFntpiLEGSFTVNDLIDA 260
Cdd:PRK13641 240 kkhyldepatSRFASKLEKGGFKF----SEMPLTIDELVDG 276
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1-230 |
5.29e-32 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 119.88 E-value: 5.29e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 1 MIRFDNVSKKYNeDKIAVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEKRISDYDIHEL---Rwd 77
Cdd:PRK13548 2 MLEARNLSVRLG-GRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELarrR-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 78 igYVL-QQIAL-FPhMTIEENIAI--VPelkkWDKDKIHDR--ITELLDSVGLDPesYRHRKPAELSGGEQQRVGVVRAL 151
Cdd:PRK13548 79 --AVLpQHSSLsFP-FTVEEVVAMgrAP----HGLSRAEDDalVAAALAQVDLAH--LAGRDYPQLSGGEQQRVQLARVL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 152 A------ADPGIILMDEPFSALDPISRQRLQQDISALQKKIKKTIVFVTHDMQEALALGDRICVMQDGEIVQVATPQEII 225
Cdd:PRK13548 150 AqlwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAEVL 229
|
....*
gi 489843944 226 kNPEN 230
Cdd:PRK13548 230 -TPET 233
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1-216 |
5.53e-32 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 119.30 E-value: 5.53e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 1 MIRFDNVSKKYNEDKIavnNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEKrisDY-DIHELRWDIG 79
Cdd:PRK10771 1 MLKLTDITWLYHHLPM---RFDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQ---DHtTTPPSRRPVS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 80 YVLQQIALFPHMTIEENIA--IVPELKKWDKDKihDRITELLDSVGLdpESYRHRKPAELSGGEQQRVGVVRALAADPGI 157
Cdd:PRK10771 75 MLFQENNLFSHLTVAQNIGlgLNPGLKLNAAQR--EKLHAIARQMGI--EDLLARLPGQLSGGQRQRVALARCLVREQPI 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489843944 158 ILMDEPFSALDPISRQ---RLQQDISAlQKKIkkTIVFVTHDMQEALALGDRICVMQDGEIV 216
Cdd:PRK10771 151 LLLDEPFSALDPALRQemlTLVSQVCQ-ERQL--TLLMVSHSLEDAARIAPRSLVVADGRIA 209
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
14-237 |
1.85e-31 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 118.71 E-value: 1.85e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 14 DKIAVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEKRI---SDYDIHELRWDIGYVLQQIALFPH 90
Cdd:PRK11831 19 NRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIpamSRSRLYTVRKRMSMLFQSGALFTD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 91 MTIEENIAI-VPELKKWDKDKIHDRITELLDSVGLDPESyrHRKPAELSGGEQQRVGVVRALAADPGIILMDEPFSALDP 169
Cdd:PRK11831 99 MNVFDNVAYpLREHTQLPAPLLHSTVMMKLEAVGLRGAA--KLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDP 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489843944 170 ISRQRLQQDISALQKKIKKTIVFVTHDMQEALALGDRICVMQDGEIVQVATPQEIIKNPENDfVKDFL 237
Cdd:PRK11831 177 ITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQANPDPR-VRQFL 243
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
2-216 |
3.11e-31 |
|
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: 115.49 E-value: 3.11e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 2 IRFDNVSKKY-NEDKIAVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEKRISDYDiHELRWDIGY 80
Cdd:cd03247 1 LSINNVSFSYpEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 81 VLQQIALFPhmtieeniaivpelkkwdkdkihdriTELLDSVGldpesyrhrkpAELSGGEQQRVGVVRALAADPGIILM 160
Cdd:cd03247 80 LNQRPYLFD--------------------------TTLRNNLG-----------RRFSGGERQRLALARILLQDAPIVLL 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 489843944 161 DEPFSALDPIS-RQRLQQDISALQkkiKKTIVFVTHDMQeALALGDRICVMQDGEIV 216
Cdd:cd03247 123 DEPTVGLDPITeRQLLSLIFEVLK---DKTLIWITHHLT-GIEHMDKILFLENGKII 175
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
17-238 |
6.35e-31 |
|
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. NikD and NikE are homologous. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131817 [Multi-domain] Cd Length: 230 Bit Score: 116.31 E-value: 6.35e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 17 AVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIP----LTTGTIYINEKRISDYDIHELrwDIGYVLQ--QIALFPH 90
Cdd:TIGR02770 1 LVQDLNLSLKRGEVLALVGESGSGKSLTCLAILGLLPpgltQTSGEILLDGRPLLPLSIRGR--HIATIMQnpRTAFNPL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 91 MTIE----ENIAIVPELKKwdkdKIHDRITELLDSVGL-DPESYRHRKPAELSGGEQQRVGVVRALAADPGIILMDEPFS 165
Cdd:TIGR02770 79 FTMGnhaiETLRSLGKLSK----QARALILEALEAVGLpDPEEVLKKYPFQLSGGMLQRVMIALALLLEPPFLIADEPTT 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489843944 166 ALDPISRQRLQQDISALQKKIKKTIVFVTHDMQEALALGDRICVMQDGEIVQVATPQEIIKNPENDFVKDFLA 238
Cdd:TIGR02770 155 DLDVVNQARVLKLLRELRQLFGTGILLITHDLGVVARIADEVAVMDDGRIVERGTVKEIFYNPKHETTRKLLS 227
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
2-224 |
6.37e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 117.54 E-value: 6.37e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 2 IRFDNVSKKYNE----DKIAVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEKRIS----DYDIHE 73
Cdd:PRK13649 3 INLQNVSYTYQAgtpfEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITstskNKDIKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 74 LRWDIGYVLQqialFPHM-----TIEENIAIVPELKKWDKDKIHDRITELLDSVGLDpESYRHRKPAELSGGEQQRVGVV 148
Cdd:PRK13649 83 IRKKVGLVFQ----FPESqlfeeTVLKDVAFGPQNFGVSQEEAEALAREKLALVGIS-ESLFEKNPFELSGGQMRRVAIA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489843944 149 RALAADPGIILMDEPFSALDPISRQRLQQDISALQKKiKKTIVFVTHDMQEALALGDRICVMQDGEIVQVATPQEI 224
Cdd:PRK13649 158 GILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQS-GMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDI 232
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
3-216 |
6.50e-31 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 115.43 E-value: 6.50e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 3 RFDNVSKKYNEDKIAVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEKRISDydiHELRWDIGYVL 82
Cdd:cd03226 1 RIENISFSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKA---KERRKSIGYVM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 83 Q--QIALFPHmTIEENIAIVPElkkwDKDKIHDRITELLDSvgLDPESYRHRKPAELSGGEQQRVGVVRALAADPGIILM 160
Cdd:cd03226 78 QdvDYQLFTD-SVREELLLGLK----ELDAGNEQAETVLKD--LDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIF 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489843944 161 DEPFSALDPISRQRLQQDISALQKKiKKTIVFVTHDMQEALALGDRICVMQDGEIV 216
Cdd:cd03226 151 DEPTSGLDYKNMERVGELIRELAAQ-GKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
16-237 |
6.54e-31 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 117.01 E-value: 6.54e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 16 IAVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEKRISDYDIHEL-RWDIGYVLQQIALFPHMTIE 94
Cdd:PRK11300 19 LAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIaRMGVVRTFQHVRLFREMTVI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 95 ENIAI----------------VPELKKWDKDKIhDRITELLDSVGLDPesYRHRKPAELSGGEQQRVGVVRALAADPGII 158
Cdd:PRK11300 99 ENLLVaqhqqlktglfsgllkTPAFRRAESEAL-DRAATWLERVGLLE--HANRQAGNLAYGQQRRLEIARCMVTQPEIL 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489843944 159 LMDEPFSALDPISRQRLQQDISALQKKIKKTIVFVTHDMQEALALGDRICVMQDGEIVQVATPQEIIKNPenDFVKDFL 237
Cdd:PRK11300 176 MLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEIRNNP--DVIKAYL 252
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
5-220 |
1.62e-30 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 115.30 E-value: 1.62e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 5 DNVSKKYNEDKI---AVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEK---RISDYDIHELR-WD 77
Cdd:PRK11629 9 DNLCKRYQEGSVqtdVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQpmsKLSSAAKAELRnQK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 78 IGYVLQQIALFPHMTIEENIAIVPELKKWDKDKIHDRITELLDSVGLDPESYrHRkPAELSGGEQQRVGVVRALAADPGI 157
Cdd:PRK11629 89 LGFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRAN-HR-PSELSGGERQRVAIARALVNNPRL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489843944 158 ILMDEPFSALDPISRQRLQQDISALQKKIKKTIVFVTHDMQEALALgDRICVMQDGEIVQVAT 220
Cdd:PRK11629 167 VLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRM-SRQLEMRDGRLTAELS 228
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
6-215 |
2.79e-30 |
|
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: 114.42 E-value: 2.79e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 6 NVSKKYNEdKIAVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEKRISDYDIHelrwDIGYVLQQI 85
Cdd:TIGR03740 5 NLSKRFGK-QTAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGHPWTRKDLH----KIGSLIESP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 86 ALFPHMTIEENIAIVPELKKWDKDkihdRITELLDSVGLdpESYRHRKPAELSGGEQQRVGVVRALAADPGIILMDEPFS 165
Cdd:TIGR03740 80 PLYENLTARENLKVHTTLLGLPDS----RIDEVLNIVDL--TNTGKKKAKQFSLGMKQRLGIAIALLNHPKLLILDEPTN 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 489843944 166 ALDPISRQRLQQDISALQKKiKKTIVFVTHDMQEALALGDRICVMQDGEI 215
Cdd:TIGR03740 154 GLDPIGIQELRELIRSFPEQ-GITVILSSHILSEVQQLADHIGIISEGVL 202
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
35-216 |
3.60e-30 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 117.28 E-value: 3.60e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 35 GPSGCGKTTTLKMINRLIPLTTGTIYINEKRISDYD--IH---ELRwDIGYVLQQIALFPHMTIEENIAIvpELKKWDKD 109
Cdd:PRK11144 31 GRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEkgIClppEKR-RIGYVFQDARLFPHYKVRGNLRY--GMAKSMVA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 110 KIhDRITELLdsvGLDPESYRHrkPAELSGGEQQRVGVVRALAADPGIILMDEPFSALDpISRQR-LQQDISALQKKIKK 188
Cdd:PRK11144 108 QF-DKIVALL---GIEPLLDRY--PGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLD-LPRKReLLPYLERLAREINI 180
|
170 180
....*....|....*....|....*...
gi 489843944 189 TIVFVTHDMQEALALGDRICVMQDGEIV 216
Cdd:PRK11144 181 PILYVSHSLDEILRLADRVVVLEQGKVK 208
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
15-238 |
9.44e-30 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 118.65 E-value: 9.44e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 15 KIAVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPlTTGTIYINEKRISDYDIHEL---RWDIGYVLQ--QIALFP 89
Cdd:PRK15134 299 NVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLIN-SQGEIWFDGQPLHNLNRRQLlpvRHRIQVVFQdpNSSLNP 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 90 HMTIEENIAI-----VPELKKWDKDkihDRITELLDSVGLDPESyRHRKPAELSGGEQQRVGVVRALAADPGIILMDEPF 164
Cdd:PRK15134 378 RLNVLQIIEEglrvhQPTLSAAQRE---QQVIAVMEEVGLDPET-RHRYPAEFSGGQRQRIAIARALILKPSLIILDEPT 453
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489843944 165 SALDPISRQRLQQDISALQKKIKKTIVFVTHDMQEALALGDRICVMQDGEIVQVATPQEIIKNPENDFVKDFLA 238
Cdd:PRK15134 454 SSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERVFAAPQQEYTRQLLA 527
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
9-216 |
1.16e-29 |
|
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: 112.75 E-value: 1.16e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 9 KKYNEDKIAVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIP---LTTGTIYINEKRISdydIHELRWDIGYVLQQI 85
Cdd:cd03234 14 KNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEgggTTSGQILFNGQPRK---PDQFQKCVAYVRQDD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 86 ALFPHMTIEENIAIVPELK--KWDKDKIHDRITELLDSVGLDPESYRHRKPAELSGGEQQRVGVVRALAADPGIILMDEP 163
Cdd:cd03234 91 ILLPGLTVRETLTYTAILRlpRKSSDAIRKKRVEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEP 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489843944 164 FSALDPISRQRLQQDISALQKKIKKTIVFVTHDMQEALALGDRICVMQDGEIV 216
Cdd:cd03234 171 TSGLDSFTALNLVSTLSQLARRNRIVILTIHQPRSDLFRLFDRILLLSSGEIV 223
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
2-216 |
1.20e-29 |
|
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: 111.87 E-value: 1.20e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 2 IRFDNV-----SKKYNEDKIAVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMI-NRLIPL-TTGTIYINEKRIsdyDIHEL 74
Cdd:cd03213 4 LSFRNLtvtvkSSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALaGRRTGLgVSGEVLINGRPL---DKRSF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 75 RWDIGYVLQQIALFPHMTIEENIAIVPELKKwdkdkihdritelldsvgldpesyrhrkpaeLSGGEQQRVGVVRALAAD 154
Cdd:cd03213 81 RKIIGYVPQDDILHPTLTVRETLMFAAKLRG-------------------------------LSGGERKRVSIALELVSN 129
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489843944 155 PGIILMDEPFSALDPISRQRLqqdISALQK--KIKKTIVFVTHD-MQEALALGDRICVMQDGEIV 216
Cdd:cd03213 130 PSLLFLDEPTSGLDSSSALQV---MSLLRRlaDTGRTIICSIHQpSSEIFELFDKLLLLSQGRVI 191
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-213 |
1.21e-29 |
|
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: 112.91 E-value: 1.21e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 1 MIRFDNVSKK---YNEDKI---AVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEK-------RIS 67
Cdd:COG4778 4 LLEVENLSKTftlHLQGGKrlpVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDggwvdlaQAS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 68 DYDIHELRWD-IGYVLQQIALFPHMTIEEnIAIVPELKK-WDKDKIHDRITELLDSVGLdPESYRHRKPAELSGGEQQRV 145
Cdd:COG4778 84 PREILALRRRtIGYVSQFLRVIPRVSALD-VVAEPLLERgVDREEARARARELLARLNL-PERLWDLPPATFSGGEQQRV 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 146 GVVRALAADPGIILMDEPFSALDPISRQRLQQDISALqKKIKKTIVFVTHDM--QEALAlgDRICVMQDG 213
Cdd:COG4778 162 NIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEA-KARGTAIIGIFHDEevREAVA--DRVVDVTPF 228
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
17-221 |
1.73e-29 |
|
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: 119.35 E-value: 1.73e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 17 AVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEKRIsDYDIHELRWDIGYVLQQIALFPHMTIEEN 96
Cdd:TIGR01257 945 AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI-ETNLDAVRQSLGMCPQHNILFHHLTVAEH 1023
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 97 IAIVPELKKWDKDKIHDRITELLDSVGLDPEsyRHRKPAELSGGEQQRVGVVRALAADPGIILMDEPFSALDPISRQRLQ 176
Cdd:TIGR01257 1024 ILFYAQLKGRSWEEAQLEMEAMLEDTGLHHK--RNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIW 1101
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 489843944 177 QDIsaLQKKIKKTIVFVTHDMQEALALGDRICVMQDGEIVQVATP 221
Cdd:TIGR01257 1102 DLL--LKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTP 1144
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-227 |
4.52e-29 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 111.51 E-value: 4.52e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 1 MIRFDNVSKKYNEDKiAVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEKRISDYDIHE-LRWDIG 79
Cdd:PRK11614 5 MLSFDKVSAHYGKIQ-ALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKiMREAVA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 80 YVLQQIALFPHMTIEENIAIVPELKkwDKDKIHDRITELLDsvgLDPESY--RHRKPAELSGGEQQRVGVVRALAADPGI 157
Cdd:PRK11614 84 IVPEGRRVFSRMTVEENLAMGGFFA--ERDQFQERIKWVYE---LFPRLHerRIQRAGTMSGGEQQMLAIGRALMSQPRL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 158 ILMDEPFSALDPISRQRLQQDISALQKKiKKTIVFVTHDMQEALALGDRICVMQDGEIVQVATPQEIIKN 227
Cdd:PRK11614 159 LLLDEPSLGLAPIIIQQIFDTIEQLREQ-GMTIFLVEQNANQALKLADRGYVLENGHVVLEDTGDALLAN 227
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
2-196 |
5.78e-29 |
|
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: 116.31 E-value: 5.78e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 2 IRFDNVSKKYNEDKIAVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEKRISDYDIHELRWDIGYV 81
Cdd:TIGR02868 335 LELRDLSAGYPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVC 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 82 LQQIALFpHMTIEENIAIVpelkkwDKDKIHDRITELLDSVGLdpESYRHRKP-----------AELSGGEQQRVGVVRA 150
Cdd:TIGR02868 415 AQDAHLF-DTTVRENLRLA------RPDATDEELWAALERVGL--ADWLRALPdgldtvlgeggARLSGGERQRLALARA 485
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 489843944 151 LAADPGIILMDEPFSALDPISRQRLQQDI-SALQkkiKKTIVFVTHD 196
Cdd:TIGR02868 486 LLADAPILLLDEPTEHLDAETADELLEDLlAALS---GRTVVLITHH 529
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
2-229 |
5.92e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 112.14 E-value: 5.92e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 2 IRFDNVSKKYNEDKIAVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEKRISDYDIHELRWDIGYV 81
Cdd:PRK13647 5 IEVEDLHFRYKDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGLV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 82 LQQI--ALFPhMTIEENIAIVPELKKWDKDKIHDRITELLDSVGLdpESYRHRKPAELSGGEQQRVGVVRALAADPGIIL 159
Cdd:PRK13647 85 FQDPddQVFS-STVWDDVAFGPVNMGLDKDEVERRVEEALKAVRM--WDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIV 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 160 MDEPFSALDPISRQRLQQDISALQKKiKKTIVFVTHDMQEALALGDRICVMQDGEIVQVATPqEIIKNPE 229
Cdd:PRK13647 162 LDEPMAYLDPRGQETLMEILDRLHNQ-GKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDK-SLLTDED 229
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
1-234 |
6.58e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 112.52 E-value: 6.58e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 1 MIRFDNVSKKYNEDKI----AVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEKRISDY----DIH 72
Cdd:PRK13643 1 MIKFEKVNYTYQPNSPfasrALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTskqkEIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 73 ELRWDIGYVLQ--QIALFPHmTIEENIAIVPELKKWDKDKIHDRITELLDSVGLDPEsYRHRKPAELSGGEQQRVGVVRA 150
Cdd:PRK13643 81 PVRKKVGVVFQfpESQLFEE-TVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLADE-FWEKSPFELSGGQMRRVAIAGI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 151 LAADPGIILMDEPFSALDPISRQRLQQDISALQKKiKKTIVFVTHDMQEALALGDRICVMQDGEIVQVATPQEIIKnpEN 230
Cdd:PRK13643 159 LAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQS-GQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQ--EV 235
|
....
gi 489843944 231 DFVK 234
Cdd:PRK13643 236 DFLK 239
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
2-229 |
1.22e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 111.82 E-value: 1.22e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 2 IRFDNVSKKYNEDKI-AVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLI--------PLTTGTIYINEKRISDydih 72
Cdd:PRK13640 6 VEFKHVSFTYPDSKKpALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLlpddnpnsKITVDGITLTAKTVWD---- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 73 eLRWDIGYVLQQI-ALFPHMTIEENIAIVPELKKWDKDKIHDRITELLDSVGLdpESYRHRKPAELSGGEQQRVGVVRAL 151
Cdd:PRK13640 82 -IREKVGIVFQNPdNQFVGATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGM--LDYIDSEPANLSGGQKQRVAIAGIL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489843944 152 AADPGIILMDEPFSALDPISRQRLQQDISALQKKIKKTIVFVTHDMQEAlALGDRICVMQDGEIVQVATPQEIIKNPE 229
Cdd:PRK13640 159 AVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEA-NMADQVLVLDDGKLLAQGSPVEIFSKVE 235
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1-216 |
2.27e-28 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 109.58 E-value: 2.27e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 1 MIRFDNVSKKYNEDKIAVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYI---NEKRISDYDIHELRWD 77
Cdd:PRK10908 1 MIRFEHVSKAYLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFsghDITRLKNREVPFLRRQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 78 IGYVLQQIALFPHMTIEENIAIVPELKKWDKDKIHDRITELLDSVGLDPESYRHrkPAELSGGEQQRVGVVRALAADPGI 157
Cdd:PRK10908 81 IGMIFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNF--PIQLSGGEQQRVGIARAVVNKPAV 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489843944 158 ILMDEPFSALDpisrQRLQQDISALQKKIKK---TIVFVTHDMQEALALGDRICVMQDGEIV 216
Cdd:PRK10908 159 LLADEPTGNLD----DALSEGILRLFEEFNRvgvTVLMATHDIGLISRRSYRMLTLSDGHLH 216
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
17-202 |
2.92e-28 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 108.09 E-value: 2.92e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 17 AVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEKRisdydihelrwDIGYVLQQIAL---FPhMTI 93
Cdd:NF040873 7 VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGA-----------RVAYVPQRSEVpdsLP-LTV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 94 EENIAI--VPELKKWDKDKIHDR--ITELLDSVGLdpESYRHRKPAELSGGEQQRVGVVRALAADPGIILMDEPFSALDP 169
Cdd:NF040873 75 RDLVAMgrWARRGLWRRLTRDDRaaVDDALERVGL--ADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDA 152
|
170 180 190
....*....|....*....|....*....|...
gi 489843944 170 ISRQRLQQDISALQKKiKKTIVFVTHDMQEALA 202
Cdd:NF040873 153 ESRERIIALLAEEHAR-GATVVVVTHDLELVRR 184
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1-199 |
3.46e-28 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 109.03 E-value: 3.46e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 1 MIRFDNVSKKYNEDKIaVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEKRISDYDIHELRWDIGY 80
Cdd:PRK10247 7 LLQLQNVGYLAGDAKI-LNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 81 VLQQIALFPHmTIEENIAIVPELKKWDKDKihDRITELLDSVGLdPESYRHRKPAELSGGEQQRVGVVRALAADPGIILM 160
Cdd:PRK10247 86 CAQTPTLFGD-TVYDNLIFPWQIRNQQPDP--AIFLDDLERFAL-PDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLL 161
|
170 180 190
....*....|....*....|....*....|....*....
gi 489843944 161 DEPFSALDPISRQRLQQDISALQKKIKKTIVFVTHDMQE 199
Cdd:PRK10247 162 DEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDE 200
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
2-215 |
3.76e-28 |
|
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: 109.10 E-value: 3.76e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 2 IRFDNVSKKY--NEDKIAVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEKRISDYDIHELRWDIG 79
Cdd:cd03248 12 VKFQNVTFAYptRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSKVS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 80 YVLQQIALFPHmTIEENIAI---------VPELKkwDKDKIHDRITELLDsvGLDPESyrHRKPAELSGGEQQRVGVVRA 150
Cdd:cd03248 92 LVGQEPVLFAR-SLQDNIAYglqscsfecVKEAA--QKAHAHSFISELAS--GYDTEV--GEKGSQLSGGQKQRVAIARA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489843944 151 LAADPGIILMDEPFSALDPISRQRLQQDISalQKKIKKTIVFVTHDMQeALALGDRICVMQDGEI 215
Cdd:cd03248 165 LIRNPQVLILDEATSALDAESEQQVQQALY--DWPERRTVLVIAHRLS-TVERADQILVLDGGRI 226
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
2-225 |
6.56e-28 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 109.31 E-value: 6.56e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 2 IRFDNVSKKYNEDKIAvNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEKRISDYDIHELRWDIGYV 81
Cdd:PRK10253 8 LRGEQLTLGYGKYTVA-ENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 82 LQQIALFPHMTIEENIAI-----VPELKKWDKDKiHDRITELLDSVGLdpESYRHRKPAELSGGEQQRVGVVRALAADPG 156
Cdd:PRK10253 87 AQNATTPGDITVQELVARgryphQPLFTRWRKED-EEAVTKAMQATGI--THLADQSVDTLSGGQRQRAWIAMVLAQETA 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 157 IILMDEPFSALDpISRQ-RLQQDISALQKKIKKTIVFVTHDMQEALALGDRICVMQDGEIVQVATPQEII 225
Cdd:PRK10253 164 IMLLDEPTTWLD-ISHQiDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIV 232
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
14-226 |
9.82e-28 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 113.68 E-value: 9.82e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 14 DKIAVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEKRISDYDIhELRWDIGYVLQQIALFPHMTI 93
Cdd:NF033858 278 DFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDAGDI-ATRRRVGYMSQAFSLYGELTV 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 94 EENIAI------VPElkkwdkDKIHDRITELLDSVGLdpESYRHRKPAELSGGEQQR----VGVVRAlaadPGIILMDEP 163
Cdd:NF033858 357 RQNLELharlfhLPA------AEIAARVAEMLERFDL--ADVADALPDSLPLGIRQRlslaVAVIHK----PELLILDEP 424
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489843944 164 FSALDPISRQRLQQDISALQKKIKKTIvFV-THDMQEAlALGDRICVMQDGEIVQVATPQEIIK 226
Cdd:NF033858 425 TSGVDPVARDMFWRLLIELSREDGVTI-FIsTHFMNEA-ERCDRISLMHAGRVLASDTPAALVA 486
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
6-223 |
2.68e-27 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 112.12 E-value: 2.68e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 6 NVSKKY--NEDKIAV-NNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEKRISDYDIHEL----RWDI 78
Cdd:PRK10535 9 DIRRSYpsGEEQVEVlKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALaqlrREHF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 79 GYVLQQIALFPHMTIEENIAIVPELKKWDKDKIHDRITELLDSVGL-DPESYRhrkPAELSGGEQQRVGVVRALAADPGI 157
Cdd:PRK10535 89 GFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLeDRVEYQ---PSQLSGGQQQRVSIARALMNGGQV 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489843944 158 ILMDEPFSALDPISRQRLQQDISALQKKiKKTIVFVTHDMQEAlALGDRICVMQDGEIVQVATPQE 223
Cdd:PRK10535 166 ILADEPTGALDSHSGEEVMAILHQLRDR-GHTVIIVTHDPQVA-AQAERVIEIRDGEIVRNPPAQE 229
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1-215 |
2.75e-27 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 107.41 E-value: 2.75e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 1 MIRFDNVSKKYNEDKiAVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTT---------GTIYINEKRISDyDI 71
Cdd:PRK09984 4 IIRVEKLAKTFNQHQ-ALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKsagshiellGRTVQREGRLAR-DI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 72 HELRWDIGYVLQQIALFPHMTIEENIAI-----VPELK---KWDKDKIHDRITELLDSVGLdpESYRHRKPAELSGGEQQ 143
Cdd:PRK09984 82 RKSRANTGYIFQQFNLVNRLSVLENVLIgalgsTPFWRtcfSWFTREQKQRALQALTRVGM--VHFAHQRVSTLSGGQQQ 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489843944 144 RVGVVRALAADPGIILMDEPFSALDPISRQRLQQDISALQKKIKKTIVFVTHDMQEALALGDRICVMQDGEI 215
Cdd:PRK09984 160 RVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHV 231
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
11-196 |
3.09e-27 |
|
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: 105.58 E-value: 3.09e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 11 YNEDKIAVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEKRIsDYD---IHELRWDIGYVLQ---- 83
Cdd:TIGR01166 1 YPGGPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPL-DYSrkgLLERRQRVGLVFQdpdd 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 84 QIaLFPhmTIEENIAIVPELKKWDKDKIHDRITELLDSVGLDpeSYRHRKPAELSGGEQQRVGVVRALAADPGIILMDEP 163
Cdd:TIGR01166 80 QL-FAA--DVDQDVAFGPLNLGLSEAEVERRVREALTAVGAS--GLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEP 154
|
170 180 190
....*....|....*....|....*....|...
gi 489843944 164 FSALDPISRQRLQQDISALQKKiKKTIVFVTHD 196
Cdd:TIGR01166 155 TAGLDPAGREQMLAILRRLRAE-GMTVVISTHD 186
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
2-216 |
7.26e-27 |
|
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: 105.31 E-value: 7.26e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 2 IRFDNVSKKY---------------------NEDKIAVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIY 60
Cdd:cd03220 1 IELENVSKSYptykggssslkklgilgrkgeVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 61 INEKrisdydiheLRWDIGYvlqQIALFPHMTIEENIAIVPELKKWDKDKIHDRITELLDSVGLdpESYRHRKPAELSGG 140
Cdd:cd03220 81 VRGR---------VSSLLGL---GGGFNPELTGRENIYLNGRLLGLSRKEIDEKIDEIIEFSEL--GDFIDLPVKTYSSG 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489843944 141 EQQRVGVVRALAADPGIILMDEPFSALDPISRQRLQQDISALQKKiKKTIVFVTHDMQEALALGDRICVMQDGEIV 216
Cdd:cd03220 147 MKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQ-GKTVILVSHDPSSIKRLCDRALVLEKGKIR 221
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
2-221 |
1.23e-26 |
|
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: 104.50 E-value: 1.23e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 2 IRFDNVSKKYNED-KIAVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEKRISDYDIHELRWDIGY 80
Cdd:cd03244 3 IEFKNVSLRYRPNlPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRISI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 81 VLQQIALFPHmTIEENIAIvpeLKKWDKDKIHD-----RITELLDSVGLDPESYRHRKPAELSGGEQQRVGVVRALAADP 155
Cdd:cd03244 83 IPQDPVLFSG-TIRSNLDP---FGEYSDEELWQalervGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKS 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489843944 156 GIILMDEPFSALDPISRQRLQQdisALQKKIK-KTIVFVTHDMqEALALGDRICVMQDGEIVQVATP 221
Cdd:cd03244 159 KILVLDEATASVDPETDALIQK---TIREAFKdCTVLTIAHRL-DTIIDSDRILVLDKGRVVEFDSP 221
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
15-215 |
1.42e-26 |
|
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: 103.28 E-value: 1.42e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 15 KIAVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEKRISDYDIHE-LRWDIGYVL---QQIALFPH 90
Cdd:cd03215 13 KGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDaIRAGIAYVPedrKREGLVLD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 91 MTIEENIAIvpelkkwdkdkihdritelldsvgldpesyrhrkPAELSGGEQQRVGVVRALAADPGIILMDEPFSALDPI 170
Cdd:cd03215 93 LSVAENIAL----------------------------------SSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVG 138
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 489843944 171 SRQRLQQDISALQKKiKKTIVFVTHDMQEALALGDRICVMQDGEI 215
Cdd:cd03215 139 AKAEIYRLIRELADA-GKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
5-220 |
1.69e-26 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 105.54 E-value: 1.69e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 5 DNVSKKY--------NEDKIAVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEKRISDYD---IHE 73
Cdd:PRK10419 7 SGLSHHYahgglsgkHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNraqRKA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 74 LRWDIGYVLQQI--ALFPHMTIEEniaIVPE----LKKWDKDKIHDRITELLDSVGLDPEsYRHRKPAELSGGEQQRVGV 147
Cdd:PRK10419 87 FRRDIQMVFQDSisAVNPRKTVRE---IIREplrhLLSLDKAERLARASEMLRAVDLDDS-VLDKRPPQLSGGQLQRVCL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489843944 148 VRALAADPGIILMDEPFSALDPISRQRLQQDISALQKKIKKTIVFVTHDmqeaLALGDRIC----VMQDGEIVQVAT 220
Cdd:PRK10419 163 ARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHD----LRLVERFCqrvmVMDNGQIVETQP 235
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-226 |
1.76e-26 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 109.10 E-value: 1.76e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 1 MIRFDNVSKKYNEDKiAVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEKRISDYDiHELRWD--I 78
Cdd:PRK09700 5 YISMAGIGKSFGPVH-ALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLD-HKLAAQlgI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 79 GYVLQQIALFPHMTIEENIAI--VPELKKW-----DKDKIHDRITELLDSVGL--DPESyrhrKPAELSGGEQQRVGVVR 149
Cdd:PRK09700 83 GIIYQELSVIDELTVLENLYIgrHLTKKVCgvniiDWREMRVRAAMMLLRVGLkvDLDE----KVANLSISHKQMLEIAK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 150 ALAADPGIILMDEPFSALDPISRQRLQQDISALQKKiKKTIVFVTHDMQEALALGDRICVMQDGE-----IVQVATPQEI 224
Cdd:PRK09700 159 TLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKE-GTAIVYISHKLAEIRRICDRYTVMKDGSsvcsgMVSDVSNDDI 237
|
..
gi 489843944 225 IK 226
Cdd:PRK09700 238 VR 239
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-226 |
1.80e-26 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 104.78 E-value: 1.80e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 1 MIRFDNVSKKYN---------------------EDKIAVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTI 59
Cdd:COG1134 4 MIEVENVSKSYRlyhepsrslkelllrrrrtrrEEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 60 YINEkRISdydihelrwdigyvlqqiALF-------PHMTIEENIAIVPELKKWDKDKIHDRITELLDSVGLdpESYRHR 132
Cdd:COG1134 84 EVNG-RVS------------------ALLelgagfhPELTGRENIYLNGRLLGLSRKEIDEKFDEIVEFAEL--GDFIDQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 133 KPAELSGGEQQRVGVVRALAADPGIILMDEPFSALDPISRQRLQQDISALQKKiKKTIVFVTHDMQEALALGDRICVMQD 212
Cdd:COG1134 143 PVKTYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRES-GRTVIFVSHSMGAVRRLCDRAIWLEK 221
|
250
....*....|....
gi 489843944 213 GEIVQVATPQEIIK 226
Cdd:COG1134 222 GRLVMDGDPEEVIA 235
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
2-228 |
1.60e-25 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 107.12 E-value: 1.60e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 2 IRFDNVSKKY--NEDKIAVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEKRISDYDIHELRWDIG 79
Cdd:TIGR00958 479 IEFQDVSFSYpnRPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVA 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 80 YVLQQIALFPHmTIEENIAIvpELKKWDKDKI---------HDRITELLDsvGLDPESyrHRKPAELSGGEQQRVGVVRA 150
Cdd:TIGR00958 559 LVGQEPVLFSG-SVRENIAY--GLTDTPDEEImaaakaanaHDFIMEFPN--GYDTEV--GEKGSQLSGGQKQRIAIARA 631
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 151 LAADPGIILMDEPFSALDPISRQRLQQDisalQKKIKKTIVFVTHDM---QEAlalgDRICVMQDGEIVQVATPQEIIKN 227
Cdd:TIGR00958 632 LVRKPRVLILDEATSALDAECEQLLQES----RSRASRTVLLIAHRLstvERA----DQILVLKKGSVVEMGTHKQLMED 703
|
.
gi 489843944 228 P 228
Cdd:TIGR00958 704 Q 704
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
2-225 |
2.19e-25 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 106.58 E-value: 2.19e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 2 IRFDNVSKKYNEDKIAVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEKRISDYDIHELRWDIGYV 81
Cdd:PRK13657 335 VEFDDVSFSYDNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAVV 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 82 LQQIALFpHMTIEENIAIvpelKKWD--KDKIHD--RITELLDSVGLDPESY------RHRKpaeLSGGEQQRVGVVRAL 151
Cdd:PRK13657 415 FQDAGLF-NRSIEDNIRV----GRPDatDEEMRAaaERAQAHDFIERKPDGYdtvvgeRGRQ---LSGGERQRLAIARAL 486
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489843944 152 AADPGIILMDEPFSALDPISRQRLQQDISALQKkiKKTIVFVTHDM---QEAlalgDRICVMQDGEIVQVATPQEII 225
Cdd:PRK13657 487 LKDPPILILDEATSALDVETEAKVKAALDELMK--GRTTFIIAHRLstvRNA----DRILVFDNGRVVESGSFDELV 557
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
15-238 |
3.18e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 102.48 E-value: 3.18e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 15 KIAVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIY-----INEKRISDY-DIHELRWDIGYVLQQIALF 88
Cdd:PRK14271 34 KTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYsgdvlLGGRSIFNYrDVLEFRRRVGMLFQRPNPF 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 89 PhMTIEENI-------AIVPelKKWDKDKIHDRITE--LLDSVgldpESYRHRKPAELSGGEQQRVGVVRALAADPGIIL 159
Cdd:PRK14271 114 P-MSIMDNVlagvrahKLVP--RKEFRGVAQARLTEvgLWDAV----KDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLL 186
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489843944 160 MDEPFSALDPISRQRLQQDISALQKKIkkTIVFVTHDMQEALALGDRICVMQDGEIVQVATPQEIIKNPENDFVKDFLA 238
Cdd:PRK14271 187 LDEPTSALDPTTTEKIEEFIRSLADRL--TVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKHAETARYVA 263
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
2-216 |
4.44e-25 |
|
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: 105.67 E-value: 4.44e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 2 IRFDNVSKKYNEDKIAVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEKRISDYDIHELRWDIGYV 81
Cdd:COG5265 358 VRFENVSFGYDPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIV 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 82 LQQIALFpHMTIEENIAivpeLKKWDKDK-----------IHDRITELldsvgldPESY------RHRKpaeLSGGEQQR 144
Cdd:COG5265 438 PQDTVLF-NDTIAYNIA----YGRPDASEeeveaaaraaqIHDFIESL-------PDGYdtrvgeRGLK---LSGGEKQR 502
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489843944 145 VGVVRALAADPGIILMDEPFSALDPISRQRLQQDISALQKKiKKTIVfVTHDM---QEAlalgDRICVMQDGEIV 216
Cdd:COG5265 503 VAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARG-RTTLV-IAHRLstiVDA----DEILVLEAGRIV 571
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
17-239 |
5.02e-25 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 105.32 E-value: 5.02e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 17 AVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIY-------------INEKRISDYDIHELRW-DIGYVL 82
Cdd:PRK10261 31 AVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQcdkmllrrrsrqvIELSEQSAAQMRHVRGaDMAMIF 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 83 QQ--IALFPHMTIEENIAIVPELKK-WDKDKIHDRITELLDSVGL-DPESYRHRKPAELSGGEQQRVGVVRALAADPGII 158
Cdd:PRK10261 111 QEpmTSLNPVFTVGEQIAESIRLHQgASREEAMVEAKRMLDQVRIpEAQTILSRYPHQLSGGMRQRVMIAMALSCRPAVL 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 159 LMDEPFSALDPISRQRLQQDISALQKKIKKTIVFVTHDMQEALALGDRICVMQDGEIVQVATPQEIIKNPENDFVKDFLA 238
Cdd:PRK10261 191 IADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQIFHAPQHPYTRALLA 270
|
.
gi 489843944 239 S 239
Cdd:PRK10261 271 A 271
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-290 |
1.48e-24 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 102.61 E-value: 1.48e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 1 MIRFDNVSKKYNEDKIaVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEKRISDYDIHELRWDIGY 80
Cdd:PRK09536 3 MIDVSDLSVEFGDTTV-LDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVAS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 81 VLQQIALFPHMTIEENIAI--VPELKKWDKDKIHDR--ITELLDSVGLDpeSYRHRKPAELSGGEQQRVGVVRALAADPG 156
Cdd:PRK09536 82 VPQDTSLSFEFDVRQVVEMgrTPHRSRFDTWTETDRaaVERAMERTGVA--QFADRPVTSLSGGERQRVLLARALAQATP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 157 IILMDEPFSALDpISRQ--------RLQQDisalqkkiKKTIVFVTHDMQEALALGDRICVMQDGEIVQVATPQEIIKNP 228
Cdd:PRK09536 160 VLLLDEPTASLD-INHQvrtlelvrRLVDD--------GKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVLTAD 230
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489843944 229 EndfVKDFLASGHAFNTPILEGSFTVNDLIDADlfyAYQTSDGSL--GISLTDPVENLVRRVAE 290
Cdd:PRK09536 231 T---LRAAFDARTAVGTDPATGAPTVTPLPDPD---RTEAAADTRvhVVGGGQPAARAVSRLVA 288
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
17-248 |
1.69e-24 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 101.19 E-value: 1.69e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 17 AVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEKRISDYD---IHELRWDIGYVLQQ--IALFPHM 91
Cdd:PRK11308 30 ALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADpeaQKLLRQKIQIVFQNpyGSLNPRK 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 92 TI----EENIAIVPELKKWDKdkiHDRITELLDSVGLDPESYrHRKPAELSGGEQQRVGVVRALAADPGIILMDEPFSAL 167
Cdd:PRK11308 110 KVgqilEEPLLINTSLSAAER---REKALAMMAKVGLRPEHY-DRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSAL 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 168 DpISRQ----RLQQDisaLQKKIKKTIVFVTHDMQEALALGDRICVMQDGEIVQVATPQEIIKNPENDFVKDFLASghaf 243
Cdd:PRK11308 186 D-VSVQaqvlNLMMD---LQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFNNPRHPYTQALLSA---- 257
|
....*
gi 489843944 244 nTPIL 248
Cdd:PRK11308 258 -TPRL 261
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
2-216 |
3.82e-24 |
|
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: 98.56 E-value: 3.82e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 2 IRFDNVSKKYN--------------------EDKIAVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYI 61
Cdd:cd03267 1 IEVSNLSKSYRvyskepgligslkslfkrkyREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 62 NEKRISDYDIHELRwDIGYVL-QQIALFPHMTIEENIAIVPELKKWDKDKIHDRITELLDSVGLDPESYrhrKPA-ELSG 139
Cdd:cd03267 81 AGLVPWKRRKKFLR-RIGVVFgQKTQLWWDLPVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLD---TPVrQLSL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489843944 140 GEQQRVGVVRALAADPGIILMDEPFSALDPISRQRLQQDISALQKKIKKTIVFVTHDMQEALALGDRICVMQDGEIV 216
Cdd:cd03267 157 GQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLL 233
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1-229 |
4.16e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 99.54 E-value: 4.16e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 1 MIRFDNVSKKYNEDKIAVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEKRIsDYD---IHELRWD 77
Cdd:PRK13636 5 ILKVEELNYNYSDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPI-DYSrkgLMKLRES 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 78 IGYVLQQI--ALFPhMTIEENIAIVPELKKWDKDKIHDRITELLDSVGLDPesYRHRKPAELSGGEQQRVGVVRALAADP 155
Cdd:PRK13636 84 VGMVFQDPdnQLFS-ASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEH--LKDKPTHCLSFGQKKRVAIAGVLVMEP 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489843944 156 GIILMDEPFSALDPISRQRLQQDISALQKKIKKTIVFVTHDMQEALALGDRICVMQDGEIVQVATPQEIIKNPE 229
Cdd:PRK13636 161 KVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFAEKE 234
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
21-219 |
1.01e-23 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 97.16 E-value: 1.01e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 21 VTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEKRISDYDIH---ELR-WDIGYVLQQIALFPHMTIEEN 96
Cdd:PRK10584 29 VELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEaraKLRaKHVGFVFQSFMLIPTLNALEN 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 97 IAIVPELKKWDKDKIHDRITELLDSVGLDpESYRHRkPAELSGGEQQRVGVVRALAADPGIILMDEPFSALDPISRQRLQ 176
Cdd:PRK10584 109 VELPALLRGESSRQSRNGAKALLEQLGLG-KRLDHL-PAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIA 186
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 489843944 177 QDISALQKKIKKTIVFVTHDMQEAlALGDRICVMQDGEIVQVA 219
Cdd:PRK10584 187 DLLFSLNREHGTTLILVTHDLQLA-ARCDRRLRLVNGQLQEEA 228
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
2-214 |
1.14e-23 |
|
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: 96.38 E-value: 1.14e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 2 IRFDNVSKKYNEDKIAVN----NVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEKrisdydihelrwd 77
Cdd:cd03250 1 ISVEDASFTWDSGEQETSftlkDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 78 IGYVLQQIALFPhMTIEENIAIvpeLKKWDkdkiHDRITELLDSVGLDP---------ESYRHRKPAELSGGEQQRVGVV 148
Cdd:cd03250 68 IAYVSQEPWIQN-GTIRENILF---GKPFD----EERYEKVIKACALEPdleilpdgdLTEIGEKGINLSGGQKQRISLA 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489843944 149 RALAADPGIILMDEPFSALDPISRQRLQQDisALQKKIK--KTIVFVTHDMQeALALGDRICVMQDGE 214
Cdd:cd03250 140 RAVYSDADIYLLDDPLSAVDAHVGRHIFEN--CILGLLLnnKTRILVTHQLQ-LLPHADQIVVLDNGR 204
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
2-225 |
1.84e-23 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 100.86 E-value: 1.84e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 2 IRFDNVSKKYNE-DKIAVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEKRISDYDIHELRWDIGY 80
Cdd:PRK11176 342 IEFRNVTFTYPGkEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVAL 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 81 VLQQIALFpHMTIEENIAIVPElKKWDKDKIH---------DRITELLDsvGLDpeSYRHRKPAELSGGEQQRVGVVRAL 151
Cdd:PRK11176 422 VSQNVHLF-NDTIANNIAYART-EQYSREQIEeaarmayamDFINKMDN--GLD--TVIGENGVLLSGGQRQRIAIARAL 495
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489843944 152 AADPGIILMDEPFSALDPISRQRLQQDISALQKkiKKTIVFVTHDMQeALALGDRICVMQDGEIVQVATPQEII 225
Cdd:PRK11176 496 LRDSPILILDEATSALDTESERAIQAALDELQK--NRTSLVIAHRLS-TIEKADEILVVEDGEIVERGTHAELL 566
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
17-215 |
2.15e-23 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 96.72 E-value: 2.15e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 17 AVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEKRISDYDIHEL-RWDIGYVLQQIALFPHMTIEE 95
Cdd:COG4674 25 ALNDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTRPDSGSVLFGGTDLTGLDEHEIaRLGIGRKFQKPTVFEELTVFE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 96 NIAI--------VPELKKWDKDKIHDRITELLDSVGLDPEsyRHRKPAELSGGEQQR--VGVVraLAADPGIILMDEPFS 165
Cdd:COG4674 105 NLELalkgdrgvFASLFARLTAEERDRIEEVLETIGLTDK--ADRLAGLLSHGQKQWleIGML--LAQDPKLLLLDEPVA 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 489843944 166 ALDPISRQRLQQDISALQKkiKKTIVFVTHDMQEALALGDRICVMQDGEI 215
Cdd:COG4674 181 GMTDAETERTAELLKSLAG--KHSVVVVEHDMEFVRQIARKVTVLHQGSV 228
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
34-228 |
4.78e-23 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 96.01 E-value: 4.78e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 34 IGPSGCGKTTTLKMINRLIPLTTGTIYINEKRISDYDIHELRWDIGYVLQQIALFPHMTIEENIAI--------VPELKK 105
Cdd:PRK10575 43 IGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLPQQLPAAEGMTVRELVAIgrypwhgaLGRFGA 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 106 WDKDKIHDRITelldSVGLDPesYRHRKPAELSGGEQQRVGVVRALAADPGIILMDEPFSALDpISRqrlQQDISALQKK 185
Cdd:PRK10575 123 ADREKVEEAIS----LVGLKP--LAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALD-IAH---QVDVLALVHR 192
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 489843944 186 IKK----TIVFVTHDMQEALALGDRICVMQDGEIVQVATPQEIIKNP 228
Cdd:PRK10575 193 LSQerglTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRGE 239
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
17-224 |
1.16e-22 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 98.17 E-value: 1.16e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 17 AVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEKRISDYDIHE-LRWDIGYV----LQQiALFPHM 91
Cdd:COG1129 267 VVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDaIRAGIAYVpedrKGE-GLVLDL 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 92 TIEENIAIV--PELKKW---DKDKIHDRITELLDSVGLDPESyRHRKPAELSGGEQQRVGVVRALAADPGIILMDEPFSA 166
Cdd:COG1129 346 SIRENITLAslDRLSRGgllDRRRERALAEEYIKRLRIKTPS-PEQPVGNLSGGNQQKVVLAKWLATDPKVLILDEPTRG 424
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489843944 167 LDPISRQRLQQDISALQKKiKKTIVFVTHDMQEALALGDRICVMQDGEIVQVATPQEI 224
Cdd:COG1129 425 IDVGAKAEIYRLIRELAAE-GKAVIVISSELPELLGLSDRILVMREGRIVGELDREEA 481
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
28-216 |
1.18e-22 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 98.20 E-value: 1.18e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 28 GEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEK---RISDYDIHELrwDIGYVLQQIALFPHMTIEENIAIvpELK 104
Cdd:PRK15439 37 GEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNpcaRLTPAKAHQL--GIYLVPQEPLLFPNLSVKENILF--GLP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 105 KWDKDKihDRITELLDSVG--LDPESyrhrKPAELSGGEQQRVGVVRALAADPGIILMDEPFSALDPISRQRLQQDISAL 182
Cdd:PRK15439 113 KRQASM--QKMKQLLAALGcqLDLDS----SAGSLEVADRQIVEILRGLMRDSRILILDEPTASLTPAETERLFSRIREL 186
|
170 180 190
....*....|....*....|....*....|....
gi 489843944 183 QKKiKKTIVFVTHDMQEALALGDRICVMQDGEIV 216
Cdd:PRK15439 187 LAQ-GVGIVFISHKLPEIRQLADRISVMRDGTIA 219
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
17-239 |
2.17e-22 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 94.47 E-value: 2.17e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 17 AVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEKRIS--DYDIHELRwdIGYVLQ--QIALFPHMT 92
Cdd:PRK15112 28 AVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHfgDYSYRSQR--IRMIFQdpSTSLNPRQR 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 93 IEEnIAIVP-----ELKKWDKDKihdRITELLDSVGLDPE--SYRhrkPAELSGGEQQRVGVVRALAADPGIILMDEPFS 165
Cdd:PRK15112 106 ISQ-ILDFPlrlntDLEPEQREK---QIIETLRQVGLLPDhaSYY---PHMLAPGQKQRLGLARALILRPKVIIADEALA 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489843944 166 ALDPISRQRLQQDISALQKKIKKTIVFVTHDMQEALALGDRICVMQDGEIVQVATPQEIIKNPENDFVKDFLAS 239
Cdd:PRK15112 179 SLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVLASPLHELTKRLIAG 252
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1-216 |
2.37e-22 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 97.44 E-value: 2.37e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 1 MIRFDNVSKKYNEDKIaVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEKrisdydiheLRwdIGY 80
Cdd:COG0488 315 VLELEGLSKSYGDKTL-LDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGET---------VK--IGY 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 81 VLQ-QIALFPHMTIEENIAivpELKKwDKDKIHdrITELLDSVGLDPEsyRHRKPAE-LSGGEQQRVGVVRALAADPGII 158
Cdd:COG0488 383 FDQhQEELDPDKTVLDELR---DGAP-GGTEQE--VRGYLGRFLFSGD--DAFKPVGvLSGGEKARLALAKLLLSPPNVL 454
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 159 LMDEPFSALDPISRQRLQQdisALQkKIKKTIVFVTHDMQ--EALAlgDRICVMQDGEIV 216
Cdd:COG0488 455 LLDEPTNHLDIETLEALEE---ALD-DFPGTVLLVSHDRYflDRVA--TRILEFEDGGVR 508
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
1-239 |
6.02e-22 |
|
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated complex. This protein (PhnK) and the adjacent-encoded PhnL resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this complex rather than part of a transporter per se. [Central intermediary metabolism, Phosphorus compounds]
Pssm-ID: 188208 [Multi-domain] Cd Length: 253 Bit Score: 92.97 E-value: 6.02e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 1 MIRFDNVSKKYNeDKIAVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEKRISDYDIHEL------ 74
Cdd:TIGR02323 3 LLQVSGLSKSYG-GGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMRSGAELELYQLseaerr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 75 ---RWDIGYVLQQIALFPHMTIEENIAIVPELKKWDK---DKIHDRITELLDSVGLDPESYRHrKPAELSGGEQQRVGVV 148
Cdd:TIGR02323 82 rlmRTEWGFVHQNPRDGLRMRVSAGANIGERLMAIGArhyGNIRATAQDWLEEVEIDPTRIDD-LPRAFSGGMQQRLQIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 149 RALAADPGIILMDEPFSALDPISRQRLQQDISALQKKIKKTIVFVTHDMQEALALGDRICVMQDGEIVQVATPQEIIKNP 228
Cdd:TIGR02323 161 RNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRVVESGLTDQVLDDP 240
|
250
....*....|.
gi 489843944 229 ENDFVKDFLAS 239
Cdd:TIGR02323 241 QHPYTQLLVSS 251
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
13-228 |
6.90e-22 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 96.07 E-value: 6.90e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 13 EDKIAVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTtGTIYINEKRISDYDIHELRWDIGYVLQQIALFpHMT 92
Cdd:PRK11174 361 DGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPYQ-GSLKINGIELRELDPESWRKHLSWVGQNPQLP-HGT 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 93 IEENIAIV-PELkkwDKDKIHD-----RITELLDSV--GLDPESYRHRkpAELSGGEQQRVGVVRALAADPGIILMDEPF 164
Cdd:PRK11174 439 LRDNVLLGnPDA---SDEQLQQalenaWVSEFLPLLpqGLDTPIGDQA--AGLSVGQAQRLALARALLQPCQLLLLDEPT 513
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489843944 165 SALDPISRQRLQQdisALQKKIK-KTIVFVTHDMqEALALGDRICVMQDGEIVQVATPQEIIKNP 228
Cdd:PRK11174 514 ASLDAHSEQLVMQ---ALNAASRrQTTLMVTHQL-EDLAQWDQIWVMQDGQIVQQGDYAELSQAG 574
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
13-239 |
8.81e-22 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 95.54 E-value: 8.81e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 13 EDKIAVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIP-----LTTGTIYINEKRISDYDIHELRW----DIGYVLQ 83
Cdd:PRK15134 20 TVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPsppvvYPSGDIRFHGESLLHASEQTLRGvrgnKIAMIFQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 84 Q--IALFPHMTIEENIAIVPELKK-WDKDKIHDRITELLDSVGLDPESYRHRK-PAELSGGEQQRVGVVRALAADPGIIL 159
Cdd:PRK15134 100 EpmVSLNPLHTLEKQLYEVLSLHRgMRREAARGEILNCLDRVGIRQAAKRLTDyPHQLSGGERQRVMIAMALLTRPELLI 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 160 MDEPFSALDPISRQRLQQDISALQKKIKKTIVFVTHDMQEALALGDRICVMQDGEIVQVATPQEIIKNPENDFVKDFLAS 239
Cdd:PRK15134 180 ADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAATLFSAPTHPYTQKLLNS 259
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-196 |
2.27e-21 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 94.36 E-value: 2.27e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 4 FDNVSKKYNEDKIaVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEkrisdydihelRWDIGYVLQ 83
Cdd:COG0488 1 LENLSKSFGGRPL-LDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK-----------GLRIGYLPQ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 84 QIALFPHMTIEENI---------------AIVPELKKWDKD-----KIHD------------RITELLDSVGLdPESYRH 131
Cdd:COG0488 69 EPPLDDDLTVLDTVldgdaelraleaeleELEAKLAEPDEDlerlaELQEefealggweaeaRAEEILSGLGF-PEEDLD 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489843944 132 RKPAELSGGEQQRVGVVRALAADPGIILMDEPFSALDPISRQRLQQDIsalqKKIKKTIVFVTHD 196
Cdd:COG0488 148 RPVSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFL----KNYPGTVLVVSHD 208
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-216 |
1.06e-20 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 90.53 E-value: 1.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 1 MIRFDNVSKKYN--------------------EDKIAVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIY 60
Cdd:COG4586 1 IIEVENLSKTYRvyekepglkgalkglfrreyREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 61 IN-----EKRIsdydihELRWDIGYVL---QQiaLFPHMTIEENIAIVPELKKWDKDKIHDRITELLDSVGLDPESyrhR 132
Cdd:COG4586 81 VLgyvpfKRRK------EFARRIGVVFgqrSQ--LWWDLPAIDSFRLLKAIYRIPDAEYKKRLDELVELLDLGELL---D 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 133 KPA-ELSGGEQQRVGVVRALAADPGIILMDEPFSALDPISRQRLQQDISALQKKIKKTIVFVTHDMQEALALGDRICVMQ 211
Cdd:COG4586 150 TPVrQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEALCDRVIVID 229
|
....*
gi 489843944 212 DGEIV 216
Cdd:COG4586 230 HGRII 234
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1-236 |
1.45e-20 |
|
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: 92.77 E-value: 1.45e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 1 MIRFDNVSKKYN-EDKIAVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEKRISDyDIHELRWDIG 79
Cdd:TIGR01257 1937 ILRLNELTKVYSgTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT-NISDVHQNMG 2015
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 80 YVLQQIALFPHMTIEENIAIVPELKKWDKDKIHDRITELLDSVGLdpESYRHRKPAELSGGEQQRVGVVRALAADPGIIL 159
Cdd:TIGR01257 2016 YCPQFDAIDDLLTGREHLYLYARLRGVPAEEIEKVANWSIQSLGL--SLYADRLAGTYSGGNKRKLSTAIALIGCPPLVL 2093
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 160 MDEPFSALDPISRQRLQQDISALQKKiKKTIVFVTHDMQEALALGDRICVMQDGEIVQVATPQEI-------------IK 226
Cdd:TIGR01257 2094 LDEPTTGMDPQARRMLWNTIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGTIQHLkskfgdgyivtmkIK 2172
|
250
....*....|
gi 489843944 227 NPENDFVKDF 236
Cdd:TIGR01257 2173 SPKDDLLPDL 2182
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
18-213 |
1.63e-20 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 88.16 E-value: 1.63e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 18 VNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEKRISDYDIHEL----RWDIGYVLQQIALFpHMTI 93
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATrsrnRYSVAYAAQKPWLL-NATV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 94 EENIAIVPELKKwdkdkihDRITELLDSVGLDP---------ESYRHRKPAELSGGEQQRVGVVRALAADPGIILMDEPF 164
Cdd:cd03290 96 EENITFGSPFNK-------QRYKAVTDACSLQPdidllpfgdQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPF 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 489843944 165 SALD-PISRQRLQQDISALQKKIKKTIVFVTHDMQeALALGDRICVMQDG 213
Cdd:cd03290 169 SALDiHLSDHLMQEGILKFLQDDKRTLVLVTHKLQ-YLPHADWIIAMKDG 217
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
2-195 |
1.71e-20 |
|
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: 86.44 E-value: 1.71e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 2 IRFDNVSKKYNEDKIAVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEKRisdydihelrwDIGYV 81
Cdd:cd03223 1 IELENLSLATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEGE-----------DLLFL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 82 LQQiALFPHMTIEENIaIVPelkkWDKdkihdritelldsvgldpesyrhrkpaELSGGEQQRVGVVRALAADPGIILMD 161
Cdd:cd03223 70 PQR-PYLPLGTLREQL-IYP----WDD---------------------------VLSGGEQQRLAFARLLLHKPKFVFLD 116
|
170 180 190
....*....|....*....|....*....|....
gi 489843944 162 EPFSALDPISRQRLQQdisALQKKiKKTIVFVTH 195
Cdd:cd03223 117 EATSALDEESEDRLYQ---LLKEL-GITVISVGH 146
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
15-238 |
1.02e-19 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 89.72 E-value: 1.02e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 15 KIAVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIP---LTTGTIYINEKRIsdyDIHELRWDIGYVLQQIALFPHM 91
Cdd:TIGR00955 38 KHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPkgvKGSGSVLLNGMPI---DAKEMRAISAYVQQDDLFIPTL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 92 TIEENIAIVPELK---KWDKDKIHDRITELLDSVGLDP-------ESYRHRKpaeLSGGEQQRVGVVRALAADPGIILMD 161
Cdd:TIGR00955 115 TVREHLMFQAHLRmprRVTKKEKRERVDEVLQALGLRKcantrigVPGRVKG---LSGGERKRLAFASELLTDPPLLFCD 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 162 EPFSALDPISRQRLQQDISALQKKiKKTIVFVTHD-MQEALALGDRICVMQDGEIVQVATPQEIIK--------NPEN-- 230
Cdd:TIGR00955 192 EPTSGLDSFMAYSVVQVLKGLAQK-GKTIICTIHQpSSELFELFDKIILMAEGRVAYLGSPDQAVPffsdlghpCPENyn 270
|
250
....*....|
gi 489843944 231 --DFVKDFLA 238
Cdd:TIGR00955 271 paDFYVQVLA 280
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
2-225 |
1.25e-19 |
|
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: 89.48 E-value: 1.25e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 2 IRFDNVSKKYnEDKIAVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRL--IPLTTGTIYINEKR-------------- 65
Cdd:TIGR03269 1 IEVKNLTKKF-DGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIYHVALcekcgyverpskvg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 66 -------------------ISDYDIHELRWDIGYVLQQ-IALFPHMTIEENIAIVPELKKWDKDKIHDRITELLDSVGLd 125
Cdd:TIGR03269 80 epcpvcggtlepeevdfwnLSDKLRRRIRKRIAIMLQRtFALYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEMVQL- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 126 peSYRHRKPA-ELSGGEQQRVGVVRALAADPGIILMDEPFSALDPISRQRLQQDISALQKKIKKTIVFVTHDMQEALALG 204
Cdd:TIGR03269 159 --SHRITHIArDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDLS 236
|
250 260
....*....|....*....|.
gi 489843944 205 DRICVMQDGEIVQVATPQEII 225
Cdd:TIGR03269 237 DKAIWLENGEIKEEGTPDEVV 257
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
5-217 |
1.49e-19 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 86.52 E-value: 1.49e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 5 DNVSKKYNeDKIAVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEKRISDYDIHEL---------R 75
Cdd:PRK11701 10 RGLTKLYG-PRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYALseaerrrllR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 76 WDIGYVLQQIA--LFPHMTIEENIAIVPELKKWDK-DKIHDRITELLDSVGLDPEsyrhR---KPAELSGGEQQRVGVVR 149
Cdd:PRK11701 89 TEWGFVHQHPRdgLRMQVSAGGNIGERLMAVGARHyGDIRATAGDWLERVEIDAA----RiddLPTTFSGGMQQRLQIAR 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489843944 150 ALAADPGIILMDEPFSALDpISRQ-RLQQDISALQKKIKKTIVFVTHDMQEALALGDRICVMQDGEIVQ 217
Cdd:PRK11701 165 NLVTHPRLVFMDEPTGGLD-VSVQaRLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVVE 232
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
6-214 |
2.42e-19 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 88.45 E-value: 2.42e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 6 NVSKKYNEDKiAVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTT--GTIYINEKRISDYDIHEL-RWDIGYVL 82
Cdd:PRK13549 10 NITKTFGGVK-ALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGTyeGEIIFEGEELQASNIRDTeRAGIAIIH 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 83 QQIALFPHMTIEENIAIVPELKKW---DKDKIHDRITELLDSVGLDPESYRhrKPAELSGGEQQRVGVVRALAADPGIIL 159
Cdd:PRK13549 89 QELALVKELSVLENIFLGNEITPGgimDYDAMYLRAQKLLAQLKLDINPAT--PVGNLGLGQQQLVEIAKALNKQARLLI 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489843944 160 MDEPFSALDPISRQRLQQDISALQKKiKKTIVFVTHDMQEALALGDRICVMQDGE 214
Cdd:PRK13549 167 LDEPTASLTESETAVLLDIIRDLKAH-GIACIYISHKLNEVKAISDTICVIRDGR 220
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
14-247 |
2.74e-19 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 85.28 E-value: 2.74e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 14 DKIAVNN----VTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPlTTGTIYINEKRISDYDIHELRWDIGYVLQQIALFP 89
Cdd:COG4138 4 NDVAVAGrlgpISAQVNAGELIHLIGPNGAGKSTLLARMAGLLP-GQGEILLNGRPLSDWSAAELARHRAYLSQQQSPPF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 90 HMTIEENIAI-VPelKKWDKDKIHDRITELLDSVGLDPesYRHRKPAELSGGEQQRVGVVRAL-----AADPG--IILMD 161
Cdd:COG4138 83 AMPVFQYLALhQP--AGASSEAVEQLLAQLAEALGLED--KLSRPLTQLSGGEWQRVRLAAVLlqvwpTINPEgqLLLLD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 162 EPFSALDpISRQrlqqdiSALQKKIKK------TIVFVTHDMQEALALGDRICVMQDGEIVQVATPQEIIKnPENdfvkd 235
Cdd:COG4138 159 EPMNSLD-VAQQ------AALDRLLRElcqqgiTVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEVMT-PEN----- 225
|
250
....*....|..
gi 489843944 236 fLAsgHAFNTPI 247
Cdd:COG4138 226 -LS--EVFGVKF 234
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
19-201 |
3.14e-19 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 84.62 E-value: 3.14e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 19 NNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYInekrisdyDIHELRWDigyvlqqialfPHMTIEENIA 98
Cdd:COG2401 47 RDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCV--------DVPDNQFG-----------REASLIDAIG 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 99 IVPELKkwdkDKIhdritELLDSVGL-DPESYRhRKPAELSGGEQQRVGVVRALAADPGIILMDEPFSALDPISRQRLQQ 177
Cdd:COG2401 108 RKGDFK----DAV-----ELLNAVGLsDAVLWL-RRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVAR 177
|
170 180
....*....|....*....|....*.
gi 489843944 178 DISALQKKIKKTIVFVTH--DMQEAL 201
Cdd:COG2401 178 NLQKLARRAGITLVVATHhyDVIDDL 203
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
6-226 |
3.47e-19 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 87.92 E-value: 3.47e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 6 NVSKKyneDKIAVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEKRI---SDYDihELRWDIGYVL 82
Cdd:PRK09700 270 NVTSR---DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDIsprSPLD--AVKKGMAYIT 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 83 Q---QIALFPHMTIEENIAIVPELKK------W------DKDKIHDRITELLDsvgLDPESYrHRKPAELSGGEQQRVGV 147
Cdd:PRK09700 345 EsrrDNGFFPNFSIAQNMAISRSLKDggykgaMglfhevDEQRTAENQRELLA---LKCHSV-NQNITELSGGNQQKVLI 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 148 VRALAADPGIILMDEPFSALDPISRqrlqQDISALQKKIK---KTIVFVTHDMQEALALGDRICVMQDGEIVQV------ 218
Cdd:PRK09700 421 SKWLCCCPEVIIFDEPTRGIDVGAK----AEIYKVMRQLAddgKVILMVSSELPEIITVCDRIAVFCEGRLTQIltnrdd 496
|
....*...
gi 489843944 219 ATPQEIIK 226
Cdd:PRK09700 497 MSEEEIMA 504
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
2-221 |
4.30e-19 |
|
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: 84.00 E-value: 4.30e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 2 IRFDNVSKKYNEDKIAV-NNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEKRISDYDIHELRWDIGY 80
Cdd:cd03369 7 IEVENLSVRYAPDLPPVlKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSSLTI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 81 VLQQIALFPHmTIEENIAIVPElkkWDKDKIHD--RITElldsVGLDpesyrhrkpaeLSGGEQQRVGVVRALAADPGII 158
Cdd:cd03369 87 IPQDPTLFSG-TIRSNLDPFDE---YSDEEIYGalRVSE----GGLN-----------LSQGQRQLLCLARALLKRPRVL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489843944 159 LMDEPFSALDPISRQRLQQDISALQKKIkkTIVFVTHDMQeALALGDRICVMQDGEIVQVATP 221
Cdd:cd03369 148 VLDEATASIDYATDALIQKTIREEFTNS--TILTIAHRLR-TIIDYDKILVMDAGEVKEYDHP 207
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
14-181 |
9.71e-19 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 83.00 E-value: 9.71e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 14 DKIAVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEKrisDYDIHELRWDIGYVLQQIALFPHMTI 93
Cdd:PRK13539 14 GRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGG---DIDDPDVAEACHYLGHRNAMKPALTV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 94 EENIAIVPELKKWDKDKIHdritELLDSVGLDPESyrHRKPAELSGGEQQRVGVVRALAADPGIILMDEPFSALDPISRQ 173
Cdd:PRK13539 91 AENLEFWAAFLGGEELDIA----AALEAVGLAPLA--HLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVA 164
|
....*...
gi 489843944 174 RLQQDISA 181
Cdd:PRK13539 165 LFAELIRA 172
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
14-228 |
2.13e-18 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 85.92 E-value: 2.13e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 14 DKIAVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEKRISDYDIHELRWDIGYVLQQIALFPHmTI 93
Cdd:PRK10789 327 DHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFLFSD-TV 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 94 EENIAI-VPELKKWDKDK------IHDRITELldsvgldPESYRHR---KPAELSGGEQQRVGVVRALAADPGIILMDEP 163
Cdd:PRK10789 406 ANNIALgRPDATQQEIEHvarlasVHDDILRL-------PQGYDTEvgeRGVMLSGGQKQRISIARALLLNAEILILDDA 478
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489843944 164 FSALDPISRQRLQQDISalQKKIKKTIVFVTHDMQeALALGDRICVMQDGEIVQVATPQEIIKNP 228
Cdd:PRK10789 479 LSAVDGRTEHQILHNLR--QWGEGRTVIISAHRLS-ALTEASEILVMQHGHIAQRGNHDQLAQQS 540
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
5-224 |
2.43e-18 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 85.46 E-value: 2.43e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 5 DNVSKKYNEDKIAVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEKRISDYDIHELR-WDIGYVL- 82
Cdd:COG3845 261 ENLSVRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRrLGVAYIPe 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 83 --QQIALFPHMTIEENIAI----VPELKKW---DKDKIHDRITELLdsvgldpESYRHRKPAE------LSGGEQQRVGV 147
Cdd:COG3845 341 drLGRGLVPDMSVAENLILgryrRPPFSRGgflDRKAIRAFAEELI-------EEFDVRTPGPdtparsLSGGNQQKVIL 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 148 VRALAADPGIILMDEPFSALDPISRQRLQQDISALQKKiKKTIVFVTHDMQEALALGDRICVMQDGEIVQV-----ATPQ 222
Cdd:COG3845 414 ARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDA-GAAVLLISEDLDEILALSDRIAVMYEGRIVGEvpaaeATRE 492
|
..
gi 489843944 223 EI 224
Cdd:COG3845 493 EI 494
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
17-214 |
2.49e-18 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 85.44 E-value: 2.49e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 17 AVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTI-YINEKRISDYDIHELRWDIGYVLQQIALFPHMTIEE 95
Cdd:PRK10762 19 ALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSIlYLGKEVTFNGPKSSQEAGIGIIHQELNLIPQLTIAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 96 NI----AIVPELKKWDKDKIHDRITELLDSVGLDPESyrHRKPAELSGGEQQRVGVVRALAADPGIILMDEPFSALDPIS 171
Cdd:PRK10762 99 NIflgrEFVNRFGRIDWKKMYAEADKLLARLNLRFSS--DKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDALTDTE 176
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 489843944 172 RQRLQQDISALQKKiKKTIVFVTHDMQEALALGDRICVMQDGE 214
Cdd:PRK10762 177 TESLFRVIRELKSQ-GRGIVYISHRLKEIFEICDDVTVFRDGQ 218
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1-220 |
2.57e-18 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 85.26 E-value: 2.57e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 1 MIRFDNVSKKYNEDKiAVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTT--GTIYINEKRISDYDIHEL-RWD 77
Cdd:TIGR02633 1 LLEMKGIVKTFGGVK-ALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTwdGEIYWSGSPLKASNIRDTeRAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 78 IGYVLQQIALFPHMTIEENIAIVPEL----KKWDKDKIHDRITELLDSVGLDpESYRHRKPAELSGGEQQRVGVVRALAA 153
Cdd:TIGR02633 80 IVIIHQELTLVPELSVAENIFLGNEItlpgGRMAYNAMYLRAKNLLRELQLD-ADNVTRPVGDYGGGQQQLVEIAKALNK 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489843944 154 DPGIILMDEPFSALDPISRQRLQQDISALQKKiKKTIVFVTHDMQEALALGDRICVMQDGEivQVAT 220
Cdd:TIGR02633 159 QARLLILDEPSSSLTEKETEILLDIIRDLKAH-GVACVYISHKLNEVKAVCDTICVIRDGQ--HVAT 222
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
1-195 |
4.19e-18 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 84.86 E-value: 4.19e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 1 MIRFDNVSKKYNEDKIAVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYinekRISDYDIhelrwdigY 80
Cdd:COG4178 362 ALALEDLTLRTPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIA----RPAGARV--------L 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 81 VLQQIALFPHMTIEENIAiVPELKKWDKDkihDRITELLDSVGLDPESYRHRKPA----ELSGGEQQRVGVVRALAADPG 156
Cdd:COG4178 430 FLPQRPYLPLGTLREALL-YPATAEAFSD---AELREALEAVGLGHLAERLDEEAdwdqVLSLGEQQRLAFARLLLHKPD 505
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 489843944 157 IILMDEPFSALDPISRQRLQQdisALQKKIKK-TIVFVTH 195
Cdd:COG4178 506 WLFLDEATSALDEENEAALYQ---LLREELPGtTVISVGH 542
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
3-217 |
6.25e-18 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 84.19 E-value: 6.25e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 3 RFDNVSKKYNEDKiAVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEKRISDYDIHE-LRWDIGYV 81
Cdd:PRK11288 6 SFDGIGKTFPGVK-ALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAaLAAGVAII 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 82 LQQIALFPHMTIEENIAI--VPELKKW-DKDKIHDRITELLDSVG--LDPESyrhrKPAELSGGEQQRVGVVRALAADPG 156
Cdd:PRK11288 85 YQELHLVPEMTVAENLYLgqLPHKGGIvNRRLLNYEAREQLEHLGvdIDPDT----PLKYLSIGQRQMVEIAKALARNAR 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489843944 157 IILMDEPFSALDPISRQRLQQDISALQKKiKKTIVFVTHDMQEALALGDRICVMQDGEIVQ 217
Cdd:PRK11288 161 VIAFDEPTSSLSAREIEQLFRVIRELRAE-GRVILYVSHRMEEIFALCDAITVFKDGRYVA 220
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
2-214 |
6.66e-18 |
|
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: 79.03 E-value: 6.66e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 2 IRFDNVSKKYnEDKIAVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIyineKRISDYDIhelrwdiGYV 81
Cdd:cd03221 1 IELENLSKTY-GGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIV----TWGSTVKI-------GYF 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 82 LQqialfphmtieeniaivpelkkwdkdkihdritelldsvgldpesyrhrkpaeLSGGEQQRVGVVRALAADPGIILMD 161
Cdd:cd03221 69 EQ-----------------------------------------------------LSGGEKMRLALAKLLLENPNLLLLD 95
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 489843944 162 EPFSALDPISRQRLQQDIsalqKKIKKTIVFVTHDmQEAL-ALGDRICVMQDGE 214
Cdd:cd03221 96 EPTNHLDLESIEALEEAL----KEYPGTVILVSHD-RYFLdQVATKIIELEDGK 144
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
17-247 |
1.24e-17 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 82.26 E-value: 1.24e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 17 AVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPlTTGTIYINEKRISDYDIHEL---------RWDIGYVLQ--QI 85
Cdd:COG4170 22 AVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITK-DNWHVTADRFRWNGIDLLKLsprerrkiiGREIAMIFQepSS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 86 ALFPHMTIEENIAIV---PELK----KWDKDKiHDRITELLDSVGL-DPESYRHRKPAELSGGEQQRVGVVRALAADPGI 157
Cdd:COG4170 101 CLDPSAKIGDQLIEAipsWTFKgkwwQRFKWR-KKRAIELLHRVGIkDHKDIMNSYPHELTEGECQKVMIAMAIANQPRL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 158 ILMDEPFSALDPISRQRLQQDISALQKKIKKTIVFVTHDMQEALALGDRICVMQDGEIVQVATPQEIIKNPENDFVKDFL 237
Cdd:COG4170 180 LIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYCGQTVESGPTEQILKSPHHPYTKALL 259
|
250
....*....|
gi 489843944 238 ASGHAFNTPI 247
Cdd:COG4170 260 RSMPDFRQPL 269
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
20-169 |
1.58e-17 |
|
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: 79.32 E-value: 1.58e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 20 NVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEKRISDYDIHELRwDIGYVLQQIALFPHMTIEENiai 99
Cdd:TIGR01189 18 GLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHE-NILYLGHLPGLKPELSALEN--- 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489843944 100 vpeLKKWDKD-KIHDR-ITELLDSVGLDpeSYRHRKPAELSGGEQQRVGVVRALAADPGIILMDEPFSALDP 169
Cdd:TIGR01189 94 ---LHFWAAIhGGAQRtIEDALAAVGLT--GFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDK 160
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
2-224 |
1.90e-17 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 83.25 E-value: 1.90e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 2 IRFDNVSKKYNeDKIAVNNVTLDIKDGEFFVFIGPSGCGKTTtlkminrLIPLTTGTiyineKRISDYDIHELRWDIG-- 79
Cdd:NF033858 2 ARLEGVSHRYG-KTVALDDVSLDIPAGCMVGLIGPDGVGKSS-------LLSLIAGA-----RKIQQGRVEVLGGDMAda 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 80 ----YVLQQIA---------LFPHMTIEENIAIVPELKKWDKDKIHDRITELLDSVGLDPesYRHRKPAELSGGEQQRVG 146
Cdd:NF033858 69 rhrrAVCPRIAympqglgknLYPTLSVFENLDFFGRLFGQDAAERRRRIDELLRATGLAP--FADRPAGKLSGGMKQKLG 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489843944 147 VVRALAADPGIILMDEPFSALDPISRQRLQQDISALQKKIKKTIVFV-THDMQEAlALGDRICVMQDGEIVQVATPQEI 224
Cdd:NF033858 147 LCCALIHDPDLLILDEPTTGVDPLSRRQFWELIDRIRAERPGMSVLVaTAYMEEA-ERFDWLVAMDAGRVLATGTPAEL 224
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
17-228 |
2.51e-17 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 81.39 E-value: 2.51e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 17 AVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMInrlIPLTTGTIYINEKRISDYDIHELRWD-------IGYVLQQIALFP 89
Cdd:PRK15093 22 AVDRVSMTLTEGEIRGLVGESGSGKSLIAKAI---CGVTKDNWRVTADRMRFDDIDLLRLSprerrklVGHNVSMIFQEP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 90 HMTIEENIAIVPELKK-----------WDKDKI-HDRITELLDSVGL-DPESYRHRKPAELSGGEQQRVGVVRALAADPG 156
Cdd:PRK15093 99 QSCLDPSERVGRQLMQnipgwtykgrwWQRFGWrKRRAIELLHRVGIkDHKDAMRSFPYELTEGECQKVMIAIALANQPR 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489843944 157 IILMDEPFSALDPISRQRLQQDISALQKKIKKTIVFVTHDMQEALALGDRICVMQDGEIVQVATPQEIIKNP 228
Cdd:PRK15093 179 LLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTVETAPSKELVTTP 250
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-229 |
2.53e-17 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 80.16 E-value: 2.53e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 1 MIRFDNVSKKYNEDKIaVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIyinekrisdydIHELRWDIGY 80
Cdd:PRK09544 4 LVSLENVSVSFGQRRV-LSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI-----------KRNGKLRIGY 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 81 VLQQIALFPHM--TIEENIAIVPELKKWDkdkihdrITELLDSVgldPESYRHRKPAE-LSGGEQQRVGVVRALAADPGI 157
Cdd:PRK09544 72 VPQKLYLDTTLplTVNRFLRLRPGTKKED-------ILPALKRV---QAGHLIDAPMQkLSGGETQRVLLARALLNRPQL 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489843944 158 ILMDEPFSALDPISRQRLQQDISALQKKIKKTIVFVTHDMQEALALGDRI-CVMQdgEIVQVATPQEIIKNPE 229
Cdd:PRK09544 142 LVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVlCLNH--HICCSGTPEVVSLHPE 212
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
14-228 |
3.31e-17 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 80.92 E-value: 3.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 14 DKIAVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIP---LTTGTIYINEKRI---SDYDIHELRWD-IGYVLQQ-- 84
Cdd:PRK09473 28 DVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAangRIGGSATFNGREIlnlPEKELNKLRAEqISMIFQDpm 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 85 IALFPHMTIEENIAIVPEL-KKWDKDKIHDRITELLDSVGLdPESYRHRK--PAELSGGEQQRVGVVRALAADPGIILMD 161
Cdd:PRK09473 108 TSLNPYMRVGEQLMEVLMLhKGMSKAEAFEESVRMLDAVKM-PEARKRMKmyPHEFSGGMRQRVMIAMALLCRPKLLIAD 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489843944 162 EPFSALDPISRQRLQQDISALQKKIKKTIVFVTHDMQEALALGDRICVMQDGEIVQVATPQEIIKNP 228
Cdd:PRK09473 187 EPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARDVFYQP 253
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
14-239 |
3.40e-17 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 79.74 E-value: 3.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 14 DKIAVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIP----LTTGTIYINEKRISDYDiheLRW-DIGYVLQ--QIA 86
Cdd:PRK10418 15 AQPLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPagvrQTAGRVLLDGKPVAPCA---LRGrKIATIMQnpRSA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 87 LFPHMTIEENIaiVPELKKWDKDKIHDRITELLDSVGL-DPESYRHRKPAELSGGEQQRVGVVRALAADPGIILMDEPFS 165
Cdd:PRK10418 92 FNPLHTMHTHA--RETCLALGKPADDATLTAALEAVGLeNAARVLKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTT 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489843944 166 ALDPISRQRLQQDISALQKKIKKTIVFVTHDMQEALALGDRICVMQDGEIVQVATPQEIIKNPENDFVKDFLAS 239
Cdd:PRK10418 170 DLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPKHAVTRSLVSA 243
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
5-239 |
8.91e-17 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 79.79 E-value: 8.91e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 5 DNVSKKYNEDKI---AVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIP----LTTGTIYINEKRISDYDIHELRWD 77
Cdd:PRK11022 7 DKLSVHFGDESApfrAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDypgrVMAEKLEFNGQDLQRISEKERRNL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 78 IGYVLQQI------ALFPHMTIeeNIAIVPELK---KWDKDKIHDRITELLDSVGL-DPESYRHRKPAELSGGEQQRVGV 147
Cdd:PRK11022 87 VGAEVAMIfqdpmtSLNPCYTV--GFQIMEAIKvhqGGNKKTRRQRAIDLLNQVGIpDPASRLDVYPHQLSGGMSQRVMI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 148 VRALAADPGIILMDEPFSALDPISRQRLQQDISALQKKIKKTIVFVTHDMQEALALGDRICVMQDGEIVQVATPQEIIKN 227
Cdd:PRK11022 165 AMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDIFRA 244
|
250
....*....|..
gi 489843944 228 PENDFVKDFLAS 239
Cdd:PRK11022 245 PRHPYTQALLRA 256
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
13-195 |
1.30e-16 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 80.69 E-value: 1.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 13 EDKIAVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLT--TGTIYINEKRISDYDIHElrwdIGYVLQQIALFPH 90
Cdd:PLN03211 79 QERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNnfTGTILANNRKPTKQILKR----TGFVTQDDILYPH 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 91 MTIEENIAIVPELK------KWDKDKIHDRITELLDSVGLDPESYRHRKPAELSGGEQQRVGVVRALAADPGIILMDEPF 164
Cdd:PLN03211 155 LTVRETLVFCSLLRlpksltKQEKILVAESVISELGLTKCENTIIGNSFIRGISGGERKRVSIAHEMLINPSLLILDEPT 234
|
170 180 190
....*....|....*....|....*....|.
gi 489843944 165 SALDPISRQRLQQDISALQKKiKKTIVFVTH 195
Cdd:PLN03211 235 SGLDATAAYRLVLTLGSLAQK-GKTIVTSMH 264
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
24-222 |
1.39e-16 |
|
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: 77.83 E-value: 1.39e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 24 DIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGtiyinekrisdyDIHELRWDIGYVLQQIALFPHMTIEEniaivpEL 103
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEG------------DIEIELDTVSYKPQYIKADYEGTVRD------LL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 104 KKWDKDKIHDR--ITELLDSVGLdpESYRHRKPAELSGGEQQRVGVVRALAADPGIILMDEPFSALDPISRQRLQQDISA 181
Cdd:cd03237 83 SSITKDFYTHPyfKTEIAKPLQI--EQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRR 160
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 489843944 182 LQKKIKKTIVFVTHDMQEALALGDRICVM--QDGEIVQVATPQ 222
Cdd:cd03237 161 FAENNEKTAFVVEHDIIMIDYLADRLIVFegEPSVNGVANPPQ 203
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
2-231 |
1.84e-16 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 80.46 E-value: 1.84e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 2 IRFDNVSKKYN--EDKIAVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEKR-ISDYDIHELRWDI 78
Cdd:PTZ00265 383 IQFKNVRFHYDtrKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDSHnLKDINLKWWRSKI 462
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 79 GYVLQQIALFPHmTIEENI-----------AIVPELKK------WDKDK------------------------------- 110
Cdd:PTZ00265 463 GVVSQDPLLFSN-SIKNNIkyslyslkdleALSNYYNEdgndsqENKNKrnscrakcagdlndmsnttdsneliemrkny 541
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 111 ----------------IHDRITELLDSVgldpESYRHRKPAELSGGEQQRVGVVRALAADPGIILMDEPFSALDPISRQR 174
Cdd:PTZ00265 542 qtikdsevvdvskkvlIHDFVSALPDKY----ETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYL 617
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 489843944 175 LQQDISALQKKIKKTIVFVTHDMQeALALGDRICVMQDGEIVQVATPQEIIKNPEND 231
Cdd:PTZ00265 618 VQKTINNLKGNENRITIIIAHRLS-TIRYANTIFVLSNRERGSTVDVDIIGEDPTKD 673
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
21-247 |
4.20e-16 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 76.51 E-value: 4.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 21 VTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPlTTGTIYINEKRISDYDIHELRWDIGYVLQQIALFPHMTIEENIAI- 99
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLLP-GSGSIQFAGQPLEAWSAAELARHRAYLSQQQTPPFAMPVFQYLTLh 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 100 VPElkKWDKDKIHDRITELLDSVGLDPEsyRHRKPAELSGGEQQRV---GVVraLAADPGI------ILMDEPFSALDpI 170
Cdd:PRK03695 94 QPD--KTRTEAVASALNEVAEALGLDDK--LGRSVNQLSGGEWQRVrlaAVV--LQVWPDInpagqlLLLDEPMNSLD-V 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489843944 171 SRQR-LQQDISAL-QKKIkkTIVFVTHDMQEALALGDRICVMQDGEIVQVATPQEIIKnPENdfvkdfLASghAFNTPI 247
Cdd:PRK03695 167 AQQAaLDRLLSELcQQGI--AVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVLT-PEN------LAQ--VFGVNF 234
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
21-181 |
1.44e-15 |
|
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: 74.07 E-value: 1.44e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 21 VTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEkRISDYDIHELRWDIGYVLQQIALFPHMTIEENiaiv 100
Cdd:cd03231 19 LSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNG-GPLDFQRDSIARGLLYLGHAPGIKTTLSVLEN---- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 101 peLKKWDKDKIHDRITELLDSVGLDpeSYRHRKPAELSGGEQQRVGVVRALAADPGIILMDEPFSALDPISRQRLQQDIS 180
Cdd:cd03231 94 --LRFWHADHSDEQVEEALARVGLN--GFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEAMA 169
|
.
gi 489843944 181 A 181
Cdd:cd03231 170 G 170
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
2-215 |
1.64e-15 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 76.93 E-value: 1.64e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 2 IRFDNVSKKYNEDKIAVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEKRISDYDIHELRWDIGYV 81
Cdd:PRK10522 323 LELRNVTFAYQDNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFSAV 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 82 LQQIALFPHMTIEENIAIVPEL-KKW-------DKDKIHD-RITELldsvgldpesyrhrkpaELSGGEQQRVGVVRALA 152
Cdd:PRK10522 403 FTDFHLFDQLLGPEGKPANPALvEKWlerlkmaHKLELEDgRISNL-----------------KLSKGQKKRLALLLALA 465
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489843944 153 ADPGIILMDEPFSALDPISRQRLQQDISALQKKIKKTIVFVTHDmQEALALGDRICVMQDGEI 215
Cdd:PRK10522 466 EERDILLLDEWAADQDPHFRREFYQVLLPLLQEMGKTIFAISHD-DHYFIHADRLLEMRNGQL 527
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
13-226 |
1.32e-14 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 72.02 E-value: 1.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 13 EDKIAVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMI--NRLIPLTTGTIYINEKRISDYDIHE-LRWDIGYVLQQIALFP 89
Cdd:COG0396 11 EGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLmgHPKYEVTSGSILLDGEDILELSPDErARAGIFLAFQYPVEIP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 90 HMTIEE--NIAI-VPELKKWDKDKIHDRITELLDSVGLDPEsYRHRKPAE-LSGGEQQRVGVVRALAADPGIILMDEPFS 165
Cdd:COG0396 91 GVSVSNflRTALnARRGEELSAREFLKLLKEKMKELGLDED-FLDRYVNEgFSGGEKKRNEILQMLLLEPKLAILDETDS 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489843944 166 ALDPISRQRLQQDISALQKKiKKTIVFVTH-----DMQEAlalgDRICVMQDGEIVQVATPqEIIK 226
Cdd:COG0396 170 GLDIDALRIVAEGVNKLRSP-DRGILIITHyqrilDYIKP----DFVHVLVDGRIVKSGGK-ELAL 229
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
2-225 |
3.80e-14 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 72.83 E-value: 3.80e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 2 IRFDNVSKKYNEDKIAVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEKRISDYDIHELRWDIGYV 81
Cdd:PRK10790 341 IDIDNVSFAYRDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMV 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 82 LQQ---IA--LFPHMTIEENIAivpELKKWD--------------KDKIHDRITElldsvgldpesyrhrKPAELSGGEQ 142
Cdd:PRK10790 421 QQDpvvLAdtFLANVTLGRDIS---EEQVWQaletvqlaelarslPDGLYTPLGE---------------QGNNLSVGQK 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 143 QRVGVVRALAADPGIILMDEPFSALDPISRQRLQQDISALQKkiKKTIVFVTHDMQ---EAlalgDRICVMQDGEIVQVA 219
Cdd:PRK10790 483 QLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVRE--HTTLVVIAHRLStivEA----DTILVLHRGQAVEQG 556
|
....*.
gi 489843944 220 TPQEII 225
Cdd:PRK10790 557 THQQLL 562
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
19-225 |
6.26e-14 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 72.75 E-value: 6.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 19 NNVTLDIKDGEFFVFIGPSGCGKTTTLKMinrliplTTGTIYINEKRISDYDIHELRWDIGYVLQQIALFpHMTIEENI- 97
Cdd:PTZ00265 1246 EEQNVGMKNVNEFSLTKEGGSGEDSTVFK-------NSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLF-NMSIYENIk 1317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 98 -----AIVPELKKWDKDKIHDRITELLdsvgldPESY-RHRKP--AELSGGEQQRVGVVRALAADPGIILMDEPFSALDP 169
Cdd:PTZ00265 1318 fgkedATREDVKRACKFAAIDEFIESL------PNKYdTNVGPygKSLSGGQKQRIAIARALLREPKILLLDEATSSLDS 1391
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489843944 170 ISRQRLQQDISALQKKIKKTIVFVTHDMQeALALGDRICVMQD----GEIVQV-ATPQEII 225
Cdd:PTZ00265 1392 NSEKLIEKTIVDIKDKADKTIITIAHRIA-SIKRSDKIVVFNNpdrtGSFVQAhGTHEELL 1451
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
13-216 |
9.19e-14 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 72.12 E-value: 9.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 13 EDKIAVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMInrliplttgtiyinekrISDYDIHELR-W---DIGYVLQQiALF 88
Cdd:PTZ00243 671 EPKVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSL-----------------LSQFEISEGRvWaerSIAYVPQQ-AWI 732
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 89 PHMTIEENIAIVPELkkwDKDKIHD--RITEL---LDSVGLDPESYRHRKPAELSGGEQQRVGVVRALAADPGIILMDEP 163
Cdd:PTZ00243 733 MNATVRGNILFFDEE---DAARLADavRVSQLeadLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDP 809
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489843944 164 FSALDPISRQRLQQDIsALQKKIKKTIVFVTHDMQeALALGDRICVMQDGEIV 216
Cdd:PTZ00243 810 LSALDAHVGERVVEEC-FLGALAGKTRVLATHQVH-VVPRADYVVALGDGRVE 860
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
2-197 |
9.42e-14 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 70.30 E-value: 9.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 2 IRFDNVSKKYNEDKIAVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEKRISDYDIHELrwdIGYV 81
Cdd:PRK15056 7 IVVNDVTVTWRNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNL---VAYV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 82 LQQIAL---FPhmTIEENIAIVPE---LKKWDKDKIHDR--ITELLDSVglDPESYRHRKPAELSGGEQQRVGVVRALAA 153
Cdd:PRK15056 84 PQSEEVdwsFP--VLVEDVVMMGRyghMGWLRRAKKRDRqiVTAALARV--DMVEFRHRQIGELSGGQKKRVFLARAIAQ 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 489843944 154 DPGIILMDEPFSALDPISRQRlqqdISALQKKIK---KTIVFVTHDM 197
Cdd:PRK15056 160 QGQVILLDEPFTGVDVKTEAR----IISLLRELRdegKTMLVSTHNL 202
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
13-229 |
1.01e-13 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 70.04 E-value: 1.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 13 EDKIAVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEKRIsDYD---IHELRWDIGYVLQ----QI 85
Cdd:PRK13638 12 QDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPL-DYSkrgLLALRQQVATVFQdpeqQI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 86 AlfpHMTIEENIAI------VPElkkwdkDKIHDRITELLDSVglDPESYRHRKPAELSGGEQQRVGVVRALAADPGIIL 159
Cdd:PRK13638 91 F---YTDIDSDIAFslrnlgVPE------AEITRRVDEALTLV--DAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489843944 160 MDEPFSALDPISRQRLqqdISALQKKIKK--TIVFVTHDMQEALALGDRICVMQDGEIVQVATPQEIIKNPE 229
Cdd:PRK13638 160 LDEPTAGLDPAGRTQM---IAIIRRIVAQgnHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVFACTE 228
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
21-226 |
2.23e-13 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 70.33 E-value: 2.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 21 VTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEKRIsdyDIHELRWDI--GYVL-----QQIALFPHMTI 93
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPI---DIRSPRDAIraGIMLcpedrKAEGIIPVHSV 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 94 EENIAIVPELK----------KWDKDKIHDRITELldsvGLDPESyRHRKPAELSGGEQQRVGVVRALAADPGIILMDEP 163
Cdd:PRK11288 349 ADNINISARRHhlragclinnRWEAENADRFIRSL----NIKTPS-REQLIMNLSGGNQQKAILGRWLSEDMKVILLDEP 423
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489843944 164 FSALDPISRQRLQQDISALQKKiKKTIVFVTHDMQEALALGDRICVMQDGEIV-----QVATPQEIIK 226
Cdd:PRK11288 424 TRGIDVGAKHEIYNVIYELAAQ-GVAVLFVSSDLPEVLGVADRIVVMREGRIAgelarEQATERQALS 490
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
18-225 |
3.93e-13 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 70.36 E-value: 3.93e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 18 VNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYInekrisdydihelRWDIGYVLQQiALFPHMTIEENI 97
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHM-------------KGSVAYVPQQ-AWIQNDSLRENI 719
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 98 AIVPELKkwdkDKIHDRITE---LLDSVGLDPESYRHR---KPAELSGGEQQRVGVVRALAADPGIILMDEPFSALDP-I 170
Cdd:TIGR00957 720 LFGKALN----EKYYQQVLEacaLLPDLEILPSGDRTEigeKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAhV 795
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489843944 171 SRQRLQQDISALQKKIKKTIVFVTHDMQeALALGDRICVMQDGEIVQVATPQEII 225
Cdd:TIGR00957 796 GKHIFEHVIGPEGVLKNKTRILVTHGIS-YLPQVDVIIVMSGGKISEMGSYQELL 849
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
18-226 |
6.13e-13 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 67.93 E-value: 6.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 18 VNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIP--------LTTGTIYINEKRISDYDIHELRwDIGYVLQQIA--L 87
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTgggaprgaRVTGDVTLNGEPLAAIDAPRLA-RLRAVLPQAAqpA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 88 FPhMTIEENIAI--VPELKKWDKDKIHDR--ITELLDSVGLDPesYRHRKPAELSGGEQQRVGVVRALA---------AD 154
Cdd:PRK13547 96 FA-FSAREIVLLgrYPHARRAGALTHRDGeiAWQALALAGATA--LVGRDVTTLSGGELARVQFARVLAqlwpphdaaQP 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489843944 155 PGIILMDEPFSALDPISRQRLQQDISALQKKIKKTIVFVTHDMQEALALGDRICVMQDGEIVQVATPQEIIK 226
Cdd:PRK13547 173 PRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPADVLT 244
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
17-217 |
9.51e-13 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 68.66 E-value: 9.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 17 AVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTT--GTIYINEKRISDYDIHELRwDIGYVL--QQIALFPHMT 92
Cdd:NF040905 16 ALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGSyeGEILFDGEVCRFKDIRDSE-ALGIVIihQELALIPYLS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 93 IEENIAIVPELKKW---DKDKIHDRITELLDSVGLDpESyrhrkPAELSG----GEQQRVGVVRALAADPGIILMDEPFS 165
Cdd:NF040905 95 IAENIFLGNERAKRgviDWNETNRRARELLAKVGLD-ES-----PDTLVTdigvGKQQLVEIAKALSKDVKLLILDEPTA 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489843944 166 ALDPISRQRLQQDISALQKK-IkkTIVFVTHDMQEALALGDRICVMQDGEIVQ 217
Cdd:NF040905 169 ALNEEDSAALLDLLLELKAQgI--TSIIISHKLNEIRRVADSITVLRDGRTIE 219
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
18-215 |
1.10e-12 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 68.49 E-value: 1.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 18 VNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEKRI---SDYD--------IHELRWDIGYVLQqia 86
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVvtrSPQDglangivyISEDRKRDGLVLG--- 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 87 lfphMTIEENIAIvPELKKWDKDKIHDRITELLDSVGLDPESYRHRKPA------ELSGGEQQRVGVVRALAADPGIILM 160
Cdd:PRK10762 345 ----MSVKENMSL-TALRYFSRAGGSLKHADEQQAVSDFIRLFNIKTPSmeqaigLLSGGNQQKVAIARGLMTRPKVLIL 419
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489843944 161 DEPFSALDPISRQRLQQDISALqKKIKKTIVFVTHDMQEALALGDRICVMQDGEI 215
Cdd:PRK10762 420 DEPTRGVDVGAKKEIYQLINQF-KAEGLSIILVSSEMPEVLGMSDRILVMHEGRI 473
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
20-224 |
1.21e-12 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 68.15 E-value: 1.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 20 NVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEKRISDYDIHElRWDIGYVL-----QQIALFPHMTIE 94
Cdd:PRK15439 281 NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQ-RLARGLVYlpedrQSSGLYLDAPLA 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 95 ENIA--IVPELKKWDKDKIHDRITElldsvgldpeSYRH---------RKPAE-LSGGEQQRVGVVRALAADPGIILMDE 162
Cdd:PRK15439 360 WNVCalTHNRRGFWIKPARENAVLE----------RYRRalnikfnhaEQAARtLSGGNQQKVLIAKCLEASPQLLIVDE 429
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489843944 163 PFSALDPISRqrlqQDISALQKKIKK---TIVFVTHDMQEALALGDRICVMQDGEIVQVATPQEI 224
Cdd:PRK15439 430 PTRGVDVSAR----NDIYQLIRSIAAqnvAVLFISSDLEEIEQMADRVLVMHQGEISGALTGAAI 490
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
20-196 |
1.61e-12 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 68.05 E-value: 1.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 20 NVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYIN----------------EKRISDY------DIHELRWD 77
Cdd:PRK11147 21 NAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEqdlivarlqqdpprnvEGTVYDFvaegieEQAEYLKR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 78 IGYVLQQIALFPHmtiEENIAIVPELKK-------WDKDkihDRITELLDSVGLDPESyrhrKPAELSGGEQQRVGVVRA 150
Cdd:PRK11147 101 YHDISHLVETDPS---EKNLNELAKLQEqldhhnlWQLE---NRINEVLAQLGLDPDA----ALSSLSGGWLRKAALGRA 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 489843944 151 LAADPGIILMDEPFSALDPISRQRLQQdisaLQKKIKKTIVFVTHD 196
Cdd:PRK11147 171 LVSNPDVLLLDEPTNHLDIETIEWLEG----FLKTFQGSIIFISHD 212
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
5-216 |
1.65e-12 |
|
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: 65.36 E-value: 1.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 5 DNVSKKYNEDKIaVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPlttGTIYINEK-RISDYDIHEL----RWDIG 79
Cdd:cd03233 11 FTTGKGRSKIPI-LKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTE---GNVSVEGDiHYNGIPYKEFaekyPGEII 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 80 YVLQQIALFPHMTIEENIAIVPELKKwdkdkiHDRItelldsvgldpesyrhRKpaeLSGGEQQRVGVVRALAADPGIIL 159
Cdd:cd03233 87 YVSEEDVHFPTLTVRETLDFALRCKG------NEFV----------------RG---ISGGERKRVSIAEALVSRASVLC 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489843944 160 MDEPFSALDPISRQRLQQDISALQKKIKKTIVF-VTHDMQEALALGDRICVMQDGEIV 216
Cdd:cd03233 142 WDNSTRGLDSSTALEILKCIRTMADVLKTTTFVsLYQASDEIYDLFDKVLVLYEGRQI 199
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
6-216 |
2.04e-12 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 67.45 E-value: 2.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 6 NVSKKYNEDKiAVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEKRISDYDIHE-LRWDIGYVLQQ 84
Cdd:PRK10982 3 NISKSFPGVK-ALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEaLENGISMVHQE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 85 IALFPHMTIEENIAIVPELKKW---DKDKIHDRITELLDSVGLDPESyrHRKPAELSGGEQQRVGVVRALAADPGIILMD 161
Cdd:PRK10982 82 LNLVLQRSVMDNMWLGRYPTKGmfvDQDKMYRDTKAIFDELDIDIDP--RAKVATLSVSQMQMIEIAKAFSYNAKIVIMD 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489843944 162 EPFSALDpisrqrlQQDISALQKKIKK------TIVFVTHDMQEALALGDRICVMQDGEIV 216
Cdd:PRK10982 160 EPTSSLT-------EKEVNHLFTIIRKlkergcGIVYISHKMEEIFQLCDEITILRDGQWI 213
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
17-225 |
4.47e-12 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 66.68 E-value: 4.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 17 AVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEKRISDYDIHElRWDIGYVL-----QQIALFPHM 91
Cdd:PRK10982 263 SIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANE-AINHGFALvteerRSTGIYAYL 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 92 TIEENiAIVPELKKW-------DKDKIHDRITELLDSVGLDPESYrHRKPAELSGGEQQRVGVVRALAADPGIILMDEPF 164
Cdd:PRK10982 342 DIGFN-SLISNIRNYknkvgllDNSRMKSDTQWVIDSMRVKTPGH-RTQIGSLSGGNQQKVIIGRWLLTQPEILMLDEPT 419
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489843944 165 SALDPISRQRLQQDISALQKKiKKTIVFVTHDMQEALALGDRICVMQDGE---IVQVA-TPQEII 225
Cdd:PRK10982 420 RGIDVGAKFEIYQLIAELAKK-DKGIIIISSEMPELLGITDRILVMSNGLvagIVDTKtTTQNEI 483
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
2-200 |
5.89e-12 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 66.19 E-value: 5.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 2 IRFDNVSKKYNEDKIaVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMInrlipltTG---TIYINE------KRISDYDIH 72
Cdd:PRK10938 261 IVLNNGVVSYNDRPI-LHNLSWQVNPGEHWQIVGPNGAGKSTLLSLI-------TGdhpQGYSNDltlfgrRRGSGETIW 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 73 ELRWDIGYVLQQIalfpHMTIEENIAIvpelkkwdKDKIhdrITELLDSVGL-DPESYRHRKPAE--------------- 136
Cdd:PRK10938 333 DIKKHIGYVSSSL----HLDYRVSTSV--------RNVI---LSGFFDSIGIyQAVSDRQQKLAQqwldilgidkrtada 397
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489843944 137 ----LSGGEQQRVGVVRALAADPGIILMDEPFSALDPISRQRLQQDISALQKKIKKTIVFVTHDMQEA 200
Cdd:PRK10938 398 pfhsLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISEGETQLLFVSHHAEDA 465
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
14-227 |
6.46e-12 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 66.69 E-value: 6.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 14 DKIAVNNVTLDIKDGEFFVFIGPSGCGKTTTLK-MINRLIPLTTGTIYInekrisdydihelRWDIGYVLQQIALFpHMT 92
Cdd:PLN03130 629 ERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISaMLGELPPRSDASVVI-------------RGTVAYVPQVSWIF-NAT 694
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 93 IEENIAIVPElkkWDKDKIHD--RITEL---LDSV-GLDPESYRHRKpAELSGGEQQRVGVVRALAADPGIILMDEPFSA 166
Cdd:PLN03130 695 VRDNILFGSP---FDPERYERaiDVTALqhdLDLLpGGDLTEIGERG-VNISGGQKQRVSMARAVYSNSDVYIFDDPLSA 770
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489843944 167 LDP-ISRQRLQQDI-SALQkkiKKTIVFVTHDMQeALALGDRICVMQDGEIVQVATPQEIIKN 227
Cdd:PLN03130 771 LDAhVGRQVFDKCIkDELR---GKTRVLVTNQLH-FLSQVDRIILVHEGMIKEEGTYEELSNN 829
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
13-168 |
6.73e-12 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 63.67 E-value: 6.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 13 EDKIAVNNVTLDIKDGEFfVFI-GPSGCGKTTTLKMINRLIPLTTGTIYINEKRISDYDiHELRWDIGYVLQQIALFPHM 91
Cdd:PRK13538 12 DERILFSGLSFTLNAGEL-VQIeGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQR-DEYHQDLLYLGHQPGIKTEL 89
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489843944 92 TIEENIAIVPELKKWDKDkihDRITELLDSVGLdpeSYRHRKPAE-LSGGEQQRVGVVRALAADPGIILMDEPFSALD 168
Cdd:PRK13538 90 TALENLRFYQRLHGPGDD---EALWEALAQVGL---AGFEDVPVRqLSAGQQRRVALARLWLTRAPLWILDEPFTAID 161
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
2-229 |
9.13e-12 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 66.15 E-value: 9.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 2 IRFDNVSKKYNEDKIAVNNVTLDIKDGEFFVFIGPSGCGKTTTLK-MINRLIPLTTGTIYInekrisdydihelRWDIGY 80
Cdd:PLN03232 617 IKNGYFSWDSKTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISaMLGELSHAETSSVVI-------------RGSVAY 683
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 81 VLQQIALFpHMTIEENIAIVPELKKWDKDKIHDrITELLDSVGLDPESYRHR---KPAELSGGEQQRVGVVRALAADPGI 157
Cdd:PLN03232 684 VPQVSWIF-NATVRENILFGSDFESERYWRAID-VTALQHDLDLLPGRDLTEigeRGVNISGGQKQRVSMARAVYSNSDI 761
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489843944 158 ILMDEPFSALDP-ISRQRLQqdiSALQKKIK-KTIVFVTHDMQeALALGDRICVMQDGEIVQVATPQEIIKNPE 229
Cdd:PLN03232 762 YIFDDPLSALDAhVAHQVFD---SCMKDELKgKTRVLVTNQLH-FLPLMDRIILVSEGMIKEEGTFAELSKSGS 831
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
1-214 |
1.07e-11 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 65.60 E-value: 1.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 1 MIRFDNVSKKYNEDKIAVNNVTldIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEKrisdydihelrwdIGY 80
Cdd:PRK13409 340 LVEYPDLTKKLGDFSLEVEGGE--IYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELK-------------ISY 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 81 VLQQIALFPHMTIEENIAIVpelkkwdKDKIHDRI--TELLDSVGLDP--EsyrhRKPAELSGGEQQRVGVVRALAADPG 156
Cdd:PRK13409 405 KPQYIKPDYDGTVEDLLRSI-------TDDLGSSYykSEIIKPLQLERllD----KNVKDLSGGELQRVAIAACLSRDAD 473
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489843944 157 IILMDEPFSALDpiSRQRLQ--QDISALQKKIKKTIVFVTHD--MQEALAlgDRICVMqDGE 214
Cdd:PRK13409 474 LYLLDEPSAHLD--VEQRLAvaKAIRRIAEEREATALVVDHDiyMIDYIS--DRLMVF-EGE 530
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
1-242 |
1.61e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 65.38 E-value: 1.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 1 MIRFDNVSKKYNEDKIAV-NNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEKRISDYDIHELRWDIG 79
Cdd:PLN03232 1234 SIKFEDVHLRYRPGLPPVlHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLS 1313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 80 YVLQQIALFPHmTIEENIAIVPE------LKKWDKDKIHDRITEllDSVGLDPESYRHRKpaELSGGEQQRVGVVRALAA 153
Cdd:PLN03232 1314 IIPQSPVLFSG-TVRFNIDPFSEhndadlWEALERAHIKDVIDR--NPFGLDAEVSEGGE--NFSVGQRQLLSLARALLR 1388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 154 DPGIILMDEPFSALDpisrqrLQQDiSALQKKIKK-----TIVFVTHDMQEALALgDRICVMQDGEIVQVATPQEIIKNP 228
Cdd:PLN03232 1389 RSKILVLDEATASVD------VRTD-SLIQRTIREefkscTMLVIAHRLNTIIDC-DKILVLSSGQVLEYDSPQELLSRD 1460
|
250
....*....|....
gi 489843944 229 ENDFVKDFLASGHA 242
Cdd:PLN03232 1461 TSAFFRMVHSTGPA 1474
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
1-195 |
1.84e-11 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 64.77 E-value: 1.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 1 MIRFDNVSKKYNEDKIAVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEKRisdydihelrwDIGY 80
Cdd:TIGR00954 451 GIKFENIPLVTPNGDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPAKG-----------KLFY 519
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 81 VLQQialfPHM---TIEENIaIVPELKKWDKDK-IHDR-ITELLDSVGLDP--------ESYRHRKPaELSGGEQQRVGV 147
Cdd:TIGR00954 520 VPQR----PYMtlgTLRDQI-IYPDSSEDMKRRgLSDKdLEQILDNVQLTHilereggwSAVQDWMD-VLSGGEKQRIAM 593
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 489843944 148 VRALAADPGIILMDEPFSALDPISRQRLQQdisaLQKKIKKTIVFVTH 195
Cdd:TIGR00954 594 ARLFYHKPQFAILDECTSAVSVDVEGYMYR----LCREFGITLFSVSH 637
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
2-214 |
4.27e-11 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 63.65 E-value: 4.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 2 IRFDNVSKKYNEDKIAVNNVTldIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEKrisdydihelrwdIGYV 81
Cdd:COG1245 342 VEYPDLTKSYGGFSLEVEGGE--IREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLK-------------ISYK 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 82 LQQIALFPHMTIEENiaivpeLKKWDKDKIHDRI--TELLDSVGLDPesYRHRKPAELSGGEQQRVGVVRALAADPGIIL 159
Cdd:COG1245 407 PQYISPDYDGTVEEF------LRSANTDDFGSSYykTEIIKPLGLEK--LLDKNVKDLSGGELQRVAIAACLSRDADLYL 478
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489843944 160 MDEPFSALDpiSRQRLQ--QDISALQKKIKKTIVFVTHD--MQEALAlgDRICVMqDGE 214
Cdd:COG1245 479 LDEPSAHLD--VEQRLAvaKAIRRFAENRGKTAMVVDHDiyLIDYIS--DRLMVF-EGE 532
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
2-242 |
1.08e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 62.83 E-value: 1.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 2 IRFDNVSKKYNEDKIAV-NNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEKRISDYDIHELRWDIGY 80
Cdd:PLN03130 1238 IKFEDVVLRYRPELPPVlHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGI 1317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 81 VLQQIALFPHmTIEENIAIVPELKK---WDK-DKIHDRITELLDSVGLDPESyrhrkpAE----LSGGEQQRVGVVRALA 152
Cdd:PLN03130 1318 IPQAPVLFSG-TVRFNLDPFNEHNDadlWESlERAHLKDVIRRNSLGLDAEV------SEagenFSVGQRQLLSLARALL 1390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 153 ADPGIILMDEPFSALDpisrqrLQQDiSALQKKIKK-----TIVFVTHDMQEALALgDRICVMQDGEIVQVATPQEIIKN 227
Cdd:PLN03130 1391 RRSKILVLDEATAAVD------VRTD-ALIQKTIREefkscTMLIIAHRLNTIIDC-DRILVLDAGRVVEFDTPENLLSN 1462
|
250
....*....|....*
gi 489843944 228 PENDFVKDFLASGHA 242
Cdd:PLN03130 1463 EGSAFSKMVQSTGAA 1477
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
24-237 |
1.34e-10 |
|
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: 59.51 E-value: 1.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 24 DIKDGEFFVFIGPSGCGKTTTLKMInrlipltTGTIYINEKRISdydihelrwdigyvlqqialfphmtieeniaivpel 103
Cdd:cd03222 21 VVKEGEVIGIVGPNGTGKTTAVKIL-------AGQLIPNGDNDE------------------------------------ 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 104 kkWDKDKIhdritelldsvgldpeSYRHRKpAELSGGEQQRVGVVRALAADPGIILMDEPFSALDpiSRQRLQ--QDISA 181
Cdd:cd03222 58 --WDGITP----------------VYKPQY-IDLSGGELQRVAIAAALLRNATFYLFDEPSAYLD--IEQRLNaaRAIRR 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489843944 182 LQKKIKKTIVFVTHDMQEALALGDRICVMQdGE--IVQVATPQEIIKNPENDFVKDFL 237
Cdd:cd03222 117 LSEEGKKTALVVEHDLAVLDYLSDRIHVFE-GEpgVYGIASQPKGTREGINRFLRGYL 173
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
4-232 |
2.19e-10 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 61.72 E-value: 2.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 4 FDNVSKKYNED-KIAVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEKRISDYDIHELRWDIGYVL 82
Cdd:PTZ00243 1311 FEGVQMRYREGlPLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFSMIP 1390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 83 QQIALFPHmTIEENIAivPELKKWDKDkihdrITELLDSVGLdpesyRHRKPAE--------LSGGEQQRVG------VV 148
Cdd:PTZ00243 1391 QDPVLFDG-TVRQNVD--PFLEASSAE-----VWAALELVGL-----RERVASEsegidsrvLEGGSNYSVGqrqlmcMA 1457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 149 RA-LAADPGIILMDEPFSALDP-ISRQRLQQDISALQkkiKKTIVFVTHDMQeALALGDRICVMQDGEIVQVATPQEIIK 226
Cdd:PTZ00243 1458 RAlLKKGSGFILMDEATANIDPaLDRQIQATVMSAFS---AYTVITIAHRLH-TVAQYDKIIVMDHGAVAEMGSPRELVM 1533
|
....*.
gi 489843944 227 NPENDF 232
Cdd:PTZ00243 1534 NRQSIF 1539
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
12-216 |
3.88e-10 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 59.27 E-value: 3.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 12 NEDKIaVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMI--NRLIPLTTGTIYINEKRISDYDiHELRWDIGYVL--QQIAL 87
Cdd:CHL00131 18 NENEI-LKGLNLSINKGEIHAIMGPNGSGKSTLSKVIagHPAYKILEGDILFKGESILDLE-PEERAHLGIFLafQYPIE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 88 FPHMTIEE--NIAIVPELKKWDKDKIH-----DRITELLDSVGLDPeSYRHRKPAE-LSGGEQQRVGVVRALAADPGIIL 159
Cdd:CHL00131 96 IPGVSNADflRLAYNSKRKFQGLPELDpleflEIINEKLKLVGMDP-SFLSRNVNEgFSGGEKKRNEILQMALLDSELAI 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489843944 160 MDEPFSALDPISRQRLQQDISALQKKiKKTIVFVTHdMQEAL--ALGDRICVMQDGEIV 216
Cdd:CHL00131 175 LDETDSGLDIDALKIIAEGINKLMTS-ENSIILITH-YQRLLdyIKPDYVHVMQNGKII 231
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
2-216 |
4.51e-10 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 60.29 E-value: 4.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 2 IRFD-------------NVSKKYnEDKIAVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEKRisd 68
Cdd:PRK15064 307 IRFEqdkklhrnaleveNLTKGF-DNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSENA--- 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 69 ydihelrwDIGYVLQQIAL-FPH-MTIEENIAivpelkKWDKDKiHD----RIT--ELL---DSVgldpesyrhRKPAE- 136
Cdd:PRK15064 383 --------NIGYYAQDHAYdFENdLTLFDWMS------QWRQEG-DDeqavRGTlgRLLfsqDDI---------KKSVKv 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 137 LSGGEQQRVGVVRALAADPGIILMDEPFSALDPISRQRLQqdiSALqKKIKKTIVFVTHDMQEALALGDRICVMQDGEIV 216
Cdd:PRK15064 439 LSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDMESIESLN---MAL-EKYEGTLIFVSHDREFVSSLATRIIEITPDGVV 514
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
28-209 |
6.23e-10 |
|
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: 57.00 E-value: 6.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 28 GEFFVFIGPSGCGKTTTLKMI-NRLIPLTTGTIYINEKRISDYDIHELRwdigyvlqqialfphmtieeniaivpelkkw 106
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALaRELGPPGGGVIYIDGEDILEEVLDQLL------------------------------- 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 107 dkdkihdritelldsvgldpESYRHRKPAELSGGEQQRVGVVRALAADPGIILMDEPFSALDPISRQRLQQDISALQKKI 186
Cdd:smart00382 51 --------------------LIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLLLL 110
|
170 180
....*....|....*....|....*...
gi 489843944 187 KK-----TIVFVTHDMQEALALGDRICV 209
Cdd:smart00382 111 LKseknlTVILTTNDEKDLGPALLRRRF 138
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
13-216 |
7.55e-10 |
|
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: 57.54 E-value: 7.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 13 EDKIAVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMI--NRLIPLTTGTIYINEKRISDYDIHElRWDIGyvlqqiaLFph 90
Cdd:cd03217 11 GGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTImgHPKYEVTEGEILFKGEDITDLPPEE-RARLG-------IF-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 91 MTIEENIAIvPELKkwdkdkihdrITELLDSVGldpesyrhrkpAELSGGEQQRVGVVRALAADPGIILMDEPFSALDPI 170
Cdd:cd03217 81 LAFQYPPEI-PGVK----------NADFLRYVN-----------EGFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDID 138
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 489843944 171 SRQRLQQDISALQKKiKKTIVFVTHdMQEALAL--GDRICVMQDGEIV 216
Cdd:cd03217 139 ALRLVAEVINKLREE-GKSVLIITH-YQRLLDYikPDRVHVLYDGRIV 184
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
5-196 |
9.13e-10 |
|
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: 59.56 E-value: 9.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 5 DNVSKKYNEDKIAVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLiplttGTIYINEKRISDyDIhelrwDIGYVLQQ 84
Cdd:TIGR03719 8 NRVSKVVPPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGV-----DKDFNGEARPQP-GI-----KVGYLPQE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 85 IALFPHMTIEENI-AIVPELKK----------------WDKDKIHDRITEL---LDSVGL-DPESYRH------RKP--- 134
Cdd:TIGR03719 77 PQLDPTKTVRENVeEGVAEIKDaldrfneisakyaepdADFDKLAAEQAELqeiIDAADAwDLDSQLEiamdalRCPpwd 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489843944 135 ---AELSGGEQQRVGVVRALAADPGIILMDEPFSALDPISRQRLQQDIsalqKKIKKTIVFVTHD 196
Cdd:TIGR03719 157 advTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHL----QEYPGTVVAVTHD 217
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
2-222 |
9.21e-10 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 59.43 E-value: 9.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 2 IRFDNVSKKYNEDKI----AVNNVTLDIKDGEFfVFI-GPSGCGKTTTLKMINRLIPLTTGTIYINEKRISDYDIHELRw 76
Cdd:COG4615 328 LELRGVTYRYPGEDGdegfTLGPIDLTIRRGEL-VFIvGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAYR- 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 77 digyvlQQIA-------LFPHMtIEENIAIVPElkkwdkdkihdRITELLDSVGLDpesyrhRKPA---------ELSGG 140
Cdd:COG4615 406 ------QLFSavfsdfhLFDRL-LGLDGEADPA-----------RARELLERLELD------HKVSvedgrfsttDLSQG 461
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 141 EQQRVGVVRALAADPGIILMDEPFSALDPISRQRLQQDISALQKKIKKTIVFVTHDMQeALALGDRICVMQDGEIVQVAT 220
Cdd:COG4615 462 QRKRLALLVALLEDRPILVFDEWAADQDPEFRRVFYTELLPELKARGKTVIAISHDDR-YFDLADRVLKMDYGKLVELTG 540
|
..
gi 489843944 221 PQ 222
Cdd:COG4615 541 PA 542
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
2-226 |
1.87e-09 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 59.19 E-value: 1.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 2 IRFDNVSKKYNED-KIAVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEKRISDYDIHELRWDIGY 80
Cdd:TIGR00957 1285 VEFRNYCLRYREDlDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITI 1364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 81 VLQQIALFP---HMTI-------EENIAIVPELKkwdkdKIHDRITELLDsvGLDPESYRHRKpaELSGGEQQRVGVVRA 150
Cdd:TIGR00957 1365 IPQDPVLFSgslRMNLdpfsqysDEEVWWALELA-----HLKTFVSALPD--KLDHECAEGGE--NLSVGQRQLVCLARA 1435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 151 LAADPGIILMDEPFSALDpisrqrLQQDiSALQKKIKK-----TIVFVTHDMQEALALgDRICVMQDGEIVQVATPQEII 225
Cdd:TIGR00957 1436 LLRKTKILVLDEATAAVD------LETD-NLIQSTIRTqfedcTVLTIAHRLNTIMDY-TRVIVLDKGEVAEFGAPSNLL 1507
|
.
gi 489843944 226 K 226
Cdd:TIGR00957 1508 Q 1508
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
13-185 |
1.97e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 56.50 E-value: 1.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 13 EDKIAVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEKRIsDYDIHELRWDIGYVLQQIALFPHMT 92
Cdd:PRK13540 12 HDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSI-KKDLCTYQKQLCFVGHRSGINPYLT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 93 IEENIAIvpelkkwdkdKIHDR-----ITELLDSVGLdpESYRHRKPAELSGGEQQRVGVVRALAADPGIILMDEPFSAL 167
Cdd:PRK13540 91 LRENCLY----------DIHFSpgavgITELCRLFSL--EHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVAL 158
|
170
....*....|....*...
gi 489843944 168 DPISRQRLQQDISALQKK 185
Cdd:PRK13540 159 DELSLLTIITKIQEHRAK 176
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
19-168 |
2.07e-09 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 56.48 E-value: 2.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 19 NNVTLDIKDGEFFVFIGPSGCGKTTTLKMI--NRLIPLTTGTIYINEKRISDydihELRWDIGYVLQQIALFPHMTIEEN 96
Cdd:cd03232 24 NNISGYVKPGTLTALMGESGAGKTTLLDVLagRKTAGVITGEILINGRPLDK----NFQRSTGYVEQQDVHSPNLTVREA 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489843944 97 IaivpelkkwdkdkihdRITELLDsvGLDPEsyrHRKpaelsggeqqRVGVVRALAADPGIILMDEPFSALD 168
Cdd:cd03232 100 L----------------RFSALLR--GLSVE---QRK----------RLTIGVELAAKPSILFLDEPTSGLD 140
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
20-241 |
4.55e-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: 58.00 E-value: 4.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 20 NVTLDIKDGEFFVFIGPSGCGKTTTLKMI-NRLIPlTTGTI-------------YINEKRISDYDIHELRWDigyVLQQI 85
Cdd:TIGR01271 444 NISFKLEKGQLLAVAGSTGSGKSSLLMMImGELEP-SEGKIkhsgrisfspqtsWIMPGTIKDNIIFGLSYD---EYRYT 519
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 86 ALFPHMTIEENIAIVPElkkwdKDKIhdriteLLDSVGLdpesyrhrkpaELSGGEQQRVGVVRALAADPGIILMDEPFS 165
Cdd:TIGR01271 520 SVIKACQLEEDIALFPE-----KDKT------VLGEGGI-----------TLSGGQRARISLARAVYKDADLYLLDSPFT 577
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489843944 166 ALDPISRQRLQQdiSALQKKI-KKTIVFVTHDMqEALALGDRICVMQDGEIVQVATPQEiIKNPENDFVKDFLASGH 241
Cdd:TIGR01271 578 HLDVVTEKEIFE--SCLCKLMsNKTRILVTSKL-EHLKKADKILLLHEGVCYFYGTFSE-LQAKRPDFSSLLLGLEA 650
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
18-215 |
5.20e-09 |
|
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: 57.14 E-value: 5.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 18 VNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIP-LTTGTIYINEKRIsdydihELRWDIGYVLQQIALFPH------ 90
Cdd:TIGR02633 276 VDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPgKFEGNVFINGKPV------DIRNPAQAIRAGIAMVPEdrkrhg 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 91 ----MTIEENIAIvPELKKWDKDKIHDRITELlDSV--GLDPESYRHRKP----AELSGGEQQRVGVVRALAADPGIILM 160
Cdd:TIGR02633 350 ivpiLGVGKNITL-SVLKSFCFKMRIDAAAEL-QIIgsAIQRLKVKTASPflpiGRLSGGNQQKAVLAKMLLTNPRVLIL 427
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489843944 161 DEPFSALDPISRQRLQQDISAL-QKKIkkTIVFVTHDMQEALALGDRICVMQDGEI 215
Cdd:TIGR02633 428 DEPTRGVDVGAKYEIYKLINQLaQEGV--AIIVVSSELAEVLGLSDRVLVIGEGKL 481
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
18-215 |
6.84e-09 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 56.86 E-value: 6.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 18 VNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIP-LTTGTIYINEKRISDYDIHE-LRWDIGYVLQ---QIALFPHMT 92
Cdd:PRK13549 278 VDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPgRWEGEIFIDGKPVKIRNPQQaIAQGIAMVPEdrkRDGIVPVMG 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 93 IEENIAIvPELKKWDKDKIHDRITELlDSVGLDPESYRHRKP------AELSGGEQQRVGVVRALAADPGIILMDEPFSA 166
Cdd:PRK13549 358 VGKNITL-AALDRFTGGSRIDDAAEL-KTILESIQRLKVKTAspelaiARLSGGNQQKAVLAKCLLLNPKILILDEPTRG 435
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 489843944 167 LDPISRQRLQQDISALQKKiKKTIVFVTHDMQEALALGDRICVMQDGEI 215
Cdd:PRK13549 436 IDVGAKYEIYKLINQLVQQ-GVAIIVISSELPEVLGLSDRVLVMHEGKL 483
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
2-198 |
1.26e-08 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 56.11 E-value: 1.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 2 IRFD--NVSkkYN-EDKIAVNNVTLDIKDGEFFVFIGPSGCGKTTTLK-MINRLIPlTTGTIYINEKrisdydihelrWD 77
Cdd:PRK11147 318 IVFEmeNVN--YQiDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKlMLGQLQA-DSGRIHCGTK-----------LE 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 78 IGYVLQ-QIALFPHMTIEENIAivpELKKwdKDKIHDRITELLdsvgldpeSY---------RHRKPAE-LSGGEQQRVG 146
Cdd:PRK11147 384 VAYFDQhRAELDPEKTVMDNLA---EGKQ--EVMVNGRPRHVL--------GYlqdflfhpkRAMTPVKaLSGGERNRLL 450
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 489843944 147 VVRALAADPGIILMDEPFSALDPISRQRLQQDISALQkkikKTIVFVTHDMQ 198
Cdd:PRK11147 451 LARLFLKPSNLLILDEPTNDLDVETLELLEELLDSYQ----GTVLLVSHDRQ 498
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
25-216 |
2.06e-08 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 55.89 E-value: 2.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 25 IKDGEFFVFIGPSGCGKTTTLKMInrlipltTGTIY----INEKRISdYDIHEL-------RWDIGYVLQQIALFPHMTI 93
Cdd:TIGR00956 84 IKPGELTVVLGRPGSGCSTLLKTI-------ASNTDgfhiGVEGVIT-YDGITPeeikkhyRGDVVYNAETDVHFPHLTV 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 94 EENIAIVPELKK-------WDKDKIHDRITEL-LDSVGLDpesyrHRKPAE--------LSGGEQQRVGVVRALAADPGI 157
Cdd:TIGR00956 156 GETLDFAARCKTpqnrpdgVSREEYAKHIADVyMATYGLS-----HTRNTKvgndfvrgVSGGERKRVSIAEASLGGAKI 230
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489843944 158 ILMDEPFSALDpiSRQRLQQdISALQK--KIKKTIVFVT--HDMQEALALGDRICVMQDGEIV 216
Cdd:TIGR00956 231 QCWDNATRGLD--SATALEF-IRALKTsaNILDTTPLVAiyQCSQDAYELFDKVIVLYEGYQI 290
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
2-168 |
2.55e-08 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 54.94 E-value: 2.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 2 IRFDNVSKKYNeDKIAVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEKRisdydihelrwDIGYV 81
Cdd:TIGR03719 323 IEAENLTKAFG-DKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETV-----------KLAYV 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 82 LQQ-IALFPHMTIEENIAIVPELKKWDKDKIHDR-ITELLDSVGLDPEsyrhRKPAELSGGEQQRVGVVRALAADPGIIL 159
Cdd:TIGR03719 391 DQSrDALDPNKTVWEEISGGLDIIKLGKREIPSRaYVGRFNFKGSDQQ----KKVGQLSGGERNRVHLAKTLKSGGNVLL 466
|
....*....
gi 489843944 160 MDEPFSALD 168
Cdd:TIGR03719 467 LDEPTNDLD 475
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
6-225 |
2.83e-08 |
|
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: 54.09 E-value: 2.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 6 NVSKKYNEDKIAV-NNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPlTTGTIYINEKRISDYDIHELRWDIGYVLQQ 84
Cdd:cd03289 7 DLTAKYTEGGNAVlENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQKWRKAFGVIPQK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 85 IALFPHmTIEENIaivPELKKWDKDKIhdriTELLDSVGLdpESYRHRKPAEL-----------SGGEQQRVGVVRALAA 153
Cdd:cd03289 86 VFIFSG-TFRKNL---DPYGKWSDEEI----WKVAEEVGL--KSVIEQFPGQLdfvlvdggcvlSHGHKQLMCLARSVLS 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489843944 154 DPGIILMDEPFSALDPISRQRLQQDISalQKKIKKTIVFVTHDMqEALALGDRICVMQDGEIVQVATPQEII 225
Cdd:cd03289 156 KAKILLLDEPSAHLDPITYQVIRKTLK--QAFADCTVILSEHRI-EAMLECQRFLVIEENKVRQYDSIQKLL 224
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
26-237 |
4.66e-08 |
|
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: 53.14 E-value: 4.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 26 KDGEFFVFIGPSGCGKTTTLKMI-NRLIPlttgtiyiNEKRIS---DYD--IHELRwdiGYVLQQiaLFPHMTIEENIAI 99
Cdd:cd03236 24 REGQVLGLVGPNGIGKSTALKILaGKLKP--------NLGKFDdppDWDeiLDEFR---GSELQN--YFTKLLEGDVKVI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 100 -----VPELKKWDKDKIHDRIT---------ELLDSVGLDPesYRHRKPAELSGGEQQRVGVVRALAADPGIILMDEPFS 165
Cdd:cd03236 91 vkpqyVDLIPKAVKGKVGELLKkkdergkldELVDQLELRH--VLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSS 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489843944 166 ALDpiSRQRLQ--QDISALQKKiKKTIVFVTHDMQEALALGDRICVMQdGE--IVQVATPQEIIKNPENDFVKDFL 237
Cdd:cd03236 169 YLD--IKQRLNaaRLIRELAED-DNYVLVVEHDLAVLDYLSDYIHCLY-GEpgAYGVVTLPKSVREGINEFLDGYL 240
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
20-207 |
1.13e-07 |
|
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: 51.87 E-value: 1.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 20 NVTLDIKDGEFFVFIGPSGCGKTTtlkminrlipLTTGTIYINEKR-----ISDYdiheLRWDIG-----YVLQQIALFP 89
Cdd:cd03270 13 NVDVDIPRNKLVVITGVSGSGKSS----------LAFDTIYAEGQRryvesLSAY----ARQFLGqmdkpDVDSIEGLSP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 90 HMTIEEN---------IAIVPELKK-----WDKDKIHDRITELLDsVGLDPESYrHRKPAELSGGEQQRVGVVRALAAD- 154
Cdd:cd03270 79 AIAIDQKttsrnprstVGTVTEIYDylrllFARVGIRERLGFLVD-VGLGYLTL-SRSAPTLSGGEAQRIRLATQIGSGl 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489843944 155 PGII-LMDEPFSALDPISRQRLqqdISALQ--KKIKKTIVFVTHDmQEALALGDRI 207
Cdd:cd03270 157 TGVLyVLDEPSIGLHPRDNDRL---IETLKrlRDLGNTVLVVEHD-EDTIRAADHV 208
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
7-236 |
1.22e-07 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 52.13 E-value: 1.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 7 VSKKYNEDKIAVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIyinekrisdydihELRWDIGYVLQQIA 86
Cdd:PRK13546 29 IPKHKNKTFFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKV-------------DRNGEVSVIAISAG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 87 LFPHMTIEENIAIVPELKKWDKDKIHDRITELLDSVGLDPESYRHRKpaELSGGEQQRVGVVRALAADPGIILMDEPFSA 166
Cdd:PRK13546 96 LSGQLTGIENIEFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVK--KYSSGMRAKLGFSINITVNPDILVIDEALSV 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 167 LDPISRQRLQQDISALqKKIKKTIVFVTHDMQEALALGDRICVMQDGEIVQVATPQEIIKNPEnDFVKDF 236
Cdd:PRK13546 174 GDQTFAQKCLDKIYEF-KEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDVLPKYE-AFLNDF 241
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
95-216 |
1.27e-07 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 52.43 E-value: 1.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 95 ENIAIVPELKKWDKDKIHDRITELLDSVGLDPESyrHRKPAELSGGEQQRVGVVRALAADPGIILMDEPFSALDPISRQR 174
Cdd:NF000106 105 ENLYMIGR*LDLSRKDARARADELLERFSLTEAA--GRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNE 182
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 489843944 175 LQQDISALQKKiKKTIVFVTHDMQEALALGDRICVMQDGEIV 216
Cdd:NF000106 183 VWDEVRSMVRD-GATVLLTTQYMEEAEQLAHELTVIDRGRVI 223
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
103-197 |
1.58e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 52.50 E-value: 1.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 103 LKKWDKDKIHDritELLDSVGLDPesYRHRKPAELSGGEQQRVGVVRALAADPGIILMDEPFSALDPISRQRLQQDISAL 182
Cdd:PRK13409 184 LKKVDERGKLD---EVVERLGLEN--ILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRQRLNVARLIREL 258
|
90
....*....|....*
gi 489843944 183 QKkiKKTIVFVTHDM 197
Cdd:PRK13409 259 AE--GKYVLVVEHDL 271
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
34-197 |
1.68e-07 |
|
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: 52.48 E-value: 1.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 34 IGPSGCGKTTTLKMIN-RLIPlttgtiyiNekrISDYDiHELRWDigYVLQQIA---LFPHMT--IEENIAIV------- 100
Cdd:COG1245 105 LGPNGIGKSTALKILSgELKP--------N---LGDYD-EEPSWD--EVLKRFRgteLQDYFKklANGEIKVAhkpqyvd 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 101 --PE---------LKKWDKDKIHDRITELLdsvGLDPesYRHRKPAELSGGEQQRVGVVRALAADPGIILMDEPFSALDP 169
Cdd:COG1245 171 liPKvfkgtvrelLEKVDERGKLDELAEKL---GLEN--ILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDI 245
|
170 180
....*....|....*....|....*...
gi 489843944 170 ISRQRLQQDISALQKKIKKTIVfVTHDM 197
Cdd:COG1245 246 YQRLNVARLIRELAEEGKYVLV-VEHDL 272
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
85-229 |
1.91e-07 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 52.71 E-value: 1.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 85 IALFPHMTIEENIAIVPELKKWDKDK---------IHDRITELLDsVGLDPESYrHRKPAELSGGEQQRVgvvrALAADP 155
Cdd:TIGR00630 430 IADVSELSIREAHEFFNQLTLTPEEKkiaeevlkeIRERLGFLID-VGLDYLSL-SRAAGTLSGGEAQRI----RLATQI 503
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 156 G------IILMDEPFSALDPISRQRLQQDISALQKKiKKTIVFVTHDmQEALALGDRICVM------QDGEIVQVATPQE 223
Cdd:TIGR00630 504 GsgltgvLYVLDEPSIGLHQRDNRRLINTLKRLRDL-GNTLIVVEHD-EDTIRAADYVIDIgpgageHGGEVVASGTPEE 581
|
....*.
gi 489843944 224 IIKNPE 229
Cdd:TIGR00630 582 ILANPD 587
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
115-224 |
2.08e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 52.32 E-value: 2.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 115 ITELLDsvgldpesyrhRKPAELSGGEQQRVGVVRALAADPGIILMDEPFSALDPISRQRLQQDISALQKKiKKTIVFVT 194
Cdd:PRK10938 125 ITALLD-----------RRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQS-GITLVLVL 192
|
90 100 110
....*....|....*....|....*....|
gi 489843944 195 HDMQEALALGDRICVMQDGEIVQVATPQEI 224
Cdd:PRK10938 193 NRFDEIPDFVQFAGVLADCTLAETGEREEI 222
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
2-232 |
2.67e-07 |
|
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: 51.06 E-value: 2.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 2 IRFDNVSKKY-NEDKIAVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEKRISDYDIHELRWDIGY 80
Cdd:cd03288 20 IKIHDLCVRYeNNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 81 VLQQIALFPHmTIEENIAivPELKKWDkdkihDRITELLDSVGLdpESYRHRKPAEL-----SGGEQQRVG------VVR 149
Cdd:cd03288 100 ILQDPILFSG-SIRFNLD--PECKCTD-----DRLWEALEIAQL--KNMVKSLPGGLdavvtEGGENFSVGqrqlfcLAR 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 150 ALAADPGIILMDEPFSALDPISRQRLQQDIsaLQKKIKKTIVFVTHDMQEALAlGDRICVMQDGEIVQVATPQEIIKNPE 229
Cdd:cd03288 170 AFVRKSSILIMDEATASIDMATENILQKVV--MTAFADRTVVTIAHRVSTILD-ADLVLVLSRGILVECDTPENLLAQED 246
|
...
gi 489843944 230 NDF 232
Cdd:cd03288 247 GVF 249
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
14-216 |
2.84e-07 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 51.71 E-value: 2.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 14 DKIAVNNVTLDIKDGEFFVFIGPSGCGKTTtLKM------INRLIpltTGTIYINEKRISDYDIHE-LRWDIGYVLQ--- 83
Cdd:NF040905 272 ERKVVDDVSLNVRRGEIVGIAGLMGAGRTE-LAMsvfgrsYGRNI---SGTVFKDGKEVDVSTVSDaIDAGLAYVTEdrk 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 84 QIALFPHMTIEENIAIvPELKKWDKDKIHDRITELLDSvgldpESYRHR----------KPAELSGGEQQRVGVVRALAA 153
Cdd:NF040905 348 GYGLNLIDDIKRNITL-ANLGKVSRRGVIDENEEIKVA-----EEYRKKmniktpsvfqKVGNLSGGNQQKVVLSKWLFT 421
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489843944 154 DPGIILMDEPFSALDPISRQRLQQDISALQKKiKKTIVFVTHDMQEALALGDRICVMQDGEIV 216
Cdd:NF040905 422 DPDVLILDEPTRGIDVGAKYEIYTIINELAAE-GKGVIVISSELPELLGMCDRIYVMNEGRIT 483
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
35-175 |
4.21e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 49.48 E-value: 4.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 35 GPSGCGKTTTLKMINRLIPLTTGTIYINEKRISdyDIHELRwdIGYVLQQIALFPHMTIEENiaivpeLKKWdkDKIHD- 113
Cdd:PRK13541 33 GANGCGKSSLLRMIAGIMQPSSGNIYYKNCNIN--NIAKPY--CTYIGHNLGLKLEMTVFEN------LKFW--SEIYNs 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489843944 114 -----------RITELLDsvgldpesyrhRKPAELSGGEQQRVGVVRALAADPGIILMDEPFSALDPISRQRL 175
Cdd:PRK13541 101 aetlyaaihyfKLHDLLD-----------EKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLL 162
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
20-214 |
9.29e-07 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 49.47 E-value: 9.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 20 NVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTI-------------YINEKRISDYDIHELRWDigyVLQQIA 86
Cdd:cd03291 55 NINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIkhsgrisfssqfsWIMPGTIKENIIFGVSYD---EYRYKS 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 87 LFPHMTIEENIAIVPElkkwdKDKIhdriteLLDSVGLDpesyrhrkpaeLSGGEQQRVGVVRALAADPGIILMDEPFSA 166
Cdd:cd03291 132 VVKACQLEEDITKFPE-----KDNT------VLGEGGIT-----------LSGGQRARISLARAVYKDADLYLLDSPFGY 189
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 489843944 167 LDPISRQRLQQdiSALQKKI-KKTIVFVTHDMqEALALGDRICVMQDGE 214
Cdd:cd03291 190 LDVFTEKEIFE--SCVCKLMaNKTRILVTSKM-EHLKKADKILILHEGS 235
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
124-227 |
1.49e-06 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 49.83 E-value: 1.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 124 LDPEsyrhRKPAELSGGEQQRVGVVRALAAD-PGII-LMDEPFSALDPISRQRLQQDISALQKKiKKTIVFVTHDMQeAL 201
Cdd:PRK00635 468 LTPE----RALATLSGGEQERTALAKHLGAElIGITyILDEPSIGLHPQDTHKLINVIKKLRDQ-GNTVLLVEHDEQ-MI 541
|
90 100 110
....*....|....*....|....*....|..
gi 489843944 202 ALGDRICVMQ------DGEIVQVATPQEIIKN 227
Cdd:PRK00635 542 SLADRIIDIGpgagifGGEVLFNGSPREFLAK 573
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
6-177 |
1.58e-06 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 49.91 E-value: 1.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 6 NVSKKYNEDKIAV-NNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPlTTGTIYINEKRISDYDIHELRWDIGYVLQQ 84
Cdd:TIGR01271 1222 GLTAKYTEAGRAVlQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVSWNSVTLQTWRKAFGVIPQK 1300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 85 IALFPHmTIEENIaivPELKKWDKDKIHdRITElldSVGLdpESYRHRKPAEL-----------SGGEQQRVGVVRALAA 153
Cdd:TIGR01271 1301 VFIFSG-TFRKNL---DPYEQWSDEEIW-KVAE---EVGL--KSVIEQFPDKLdfvlvdggyvlSNGHKQLMCLARSILS 1370
|
170 180
....*....|....*....|....
gi 489843944 154 DPGIILMDEPFSALDPISRQRLQQ 177
Cdd:TIGR01271 1371 KAKILLLDEPSAHLDPVTLQIIRK 1394
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
1-196 |
4.64e-06 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 48.19 E-value: 4.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 1 MIRfdnVSKKYNEDKIAVNNVTLdikdgEFF------VfIGPSGCGKTTTLKMINRLiplttGTIYINEKRISD-YDIhe 73
Cdd:PRK11819 9 MNR---VSKVVPPKKQILKDISL-----SFFpgakigV-LGLNGAGKSTLLRIMAGV-----DKEFEGEARPAPgIKV-- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 74 lrwdiGYVLQQIALFPHMTIEENIAI-VPELKKW----------------DKDKIHDRITEL---LDSVGL-DPESYRHR 132
Cdd:PRK11819 73 -----GYLPQEPQLDPEKTVRENVEEgVAEVKAAldrfneiyaayaepdaDFDALAAEQGELqeiIDAADAwDLDSQLEI 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489843944 133 ------------KPAELSGGEQQRVGVVRALAADPGIILMDEPFSALDPISRQRLQQDIsalqKKIKKTIVFVTHD 196
Cdd:PRK11819 148 amdalrcppwdaKVTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLEQFL----HDYPGTVVAVTHD 219
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
1-215 |
5.34e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 47.93 E-value: 5.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 1 MIRFDNVSKKYNEDKIAVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEK-RISDYDIHE---LRW 76
Cdd:PLN03073 508 IISFSDASFGYPGGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSAKvRMAVFSQHHvdgLDL 587
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 77 DIGYVLQQIALFPHmtieeniaiVPElkkwDKDKIHDRITELLDSVGLDPESyrhrkpaELSGGEQQRVGVVRALAADPG 156
Cdd:PLN03073 588 SSNPLLYMMRCFPG---------VPE----QKLRAHLGSFGVTGNLALQPMY-------TLSGGQKSRVAFAKITFKKPH 647
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489843944 157 IILMDEPFSALDPISRQRLQQDISALQKKikktIVFVTHDmqEALALG--DRICVMQDGEI 215
Cdd:PLN03073 648 ILLLDEPSNHLDLDAVEALIQGLVLFQGG----VLMVSHD--EHLISGsvDELWVVSEGKV 702
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
2-236 |
1.17e-05 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 46.81 E-value: 1.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 2 IRFDNVSKKYN-----EDKI--------------AVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIyin 62
Cdd:PRK13545 5 VKFEHVTKKYKmynkpFDKLkdlffrskdgeyhyALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTV--- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 63 ekrisdydihelrwDIGYVLQQIA----LFPHMTIEENIAIVPELKKWDKDKIHDRITELLDSVglDPESYRHRKPAELS 138
Cdd:PRK13545 82 --------------DIKGSAALIAissgLNGQLTGIENIELKGLMMGLTKEKIKEIIPEIIEFA--DIGKFIYQPVKTYS 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 139 GGEQQRVGVVRALAADPGIILMDEPFSALDPISRQRLQQDISALQKKiKKTIVFVTHDMQEALALGDRICVMQDGEIVQV 218
Cdd:PRK13545 146 SGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKCLDKMNEFKEQ-GKTIFFISHSLSQVKSFCTKALWLHYGQVKEY 224
|
250
....*....|....*...
gi 489843944 219 ATPQEIIKNpENDFVKDF 236
Cdd:PRK13545 225 GDIKEVVDH-YDEFLKKY 241
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
2-168 |
1.60e-05 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 46.27 E-value: 1.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 2 IRFDNVSKKYNeDKIAVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEKRisdydihelrwDIGYV 81
Cdd:PRK11819 325 IEAENLSKSFG-DRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGETV-----------KLAYV 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 82 LQQ-IALFPHMTIEENIAIVPELKKWDKDKIHDRitelldsvgldpeSYRHR---------KPA-ELSGGEQQRVGVVRA 150
Cdd:PRK11819 393 DQSrDALDPNKTVWEEISGGLDIIKVGNREIPSR-------------AYVGRfnfkggdqqKKVgVLSGGERNRLHLAKT 459
|
170
....*....|....*...
gi 489843944 151 LAADPGIILMDEPFSALD 168
Cdd:PRK11819 460 LKQGGNVLLLDEPTNDLD 477
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
13-168 |
2.68e-05 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 45.87 E-value: 2.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 13 EDKIAVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRliPLTTGTIYINEKRISDYDIHE-LRWDIGYVLQQIALFPHM 91
Cdd:TIGR00956 774 EKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAE--RVTTGVITGGDRLVNGRPLDSsFQRSIGYVQQQDLHLPTS 851
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 92 TIEENIAIVPELK------KWDKDKIHDRITELLDSvgldpESYRHR---KPAE-LSGGEQQRVGVVRALAADPGIIL-M 160
Cdd:TIGR00956 852 TVRESLRFSAYLRqpksvsKSEKMEYVEEVIKLLEM-----ESYADAvvgVPGEgLNVEQRKRLTIGVELVAKPKLLLfL 926
|
....*...
gi 489843944 161 DEPFSALD 168
Cdd:TIGR00956 927 DEPTSGLD 934
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
132-196 |
3.36e-05 |
|
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: 43.85 E-value: 3.36e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489843944 132 RKPAELSGGEQQRVGVVRALAADPG--IILMDEPFSALDPISRQRLQQDISALQKKiKKTIVFVTHD 196
Cdd:cd03238 83 QKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGLIDL-GNTVILIEHN 148
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
25-169 |
4.26e-05 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 44.07 E-value: 4.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 25 IKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEKRISDYDihELRWdIGYVLQQIALFPHMTIEENIAIVPELK 104
Cdd:PRK13543 34 VDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGD--RSRF-MAYLGHLPGLKADLSTLENLHFLCGLH 110
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489843944 105 KWDKDKIHdriTELLDSVGLdpESYRHRKPAELSGGEQQRVGVVRALAADPGIILMDEPFSALDP 169
Cdd:PRK13543 111 GRRAKQMP---GSALAIVGL--AGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDL 170
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
13-168 |
5.76e-05 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 44.84 E-value: 5.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 13 EDKIAV-NNVTLDIKDGEFFVFIGPSGCGKTTtlkMINRLIPLTTGTIYINEKRISDY-DIHELRWDI-GYVLQQIALFP 89
Cdd:PLN03140 890 EDRLQLlREVTGAFRPGVLTALMGVSGAGKTT---LMDVLAGRKTGGYIEGDIRISGFpKKQETFARIsGYCEQNDIHSP 966
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 90 HMTIEENIA------IVPELKKWDKDKIHDRITELLDSVGLDPESYRHRKPAELSGGEQQRVGVVRALAADPGIILMDEP 163
Cdd:PLN03140 967 QVTVRESLIysaflrLPKEVSKEEKMMFVDEVMELVELDNLKDAIVGLPGVTGLSTEQRKRLTIAVELVANPSIIFMDEP 1046
|
....*
gi 489843944 164 FSALD 168
Cdd:PLN03140 1047 TSGLD 1051
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
4-196 |
1.69e-04 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 42.96 E-value: 1.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 4 FDNVSKKYNEdkiavnnvtldikdGEFFVFIGPSGCGKTTTLKMI-NRLIPlTTGTIYI--NEK--------------RI 66
Cdd:PRK15064 17 FENISVKFGG--------------GNRYGLIGANGCGKSTFMKILgGDLEP-SAGNVSLdpNERlgklrqdqfafeefTV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 67 SDYDI--HELRWDIGYVLQQIALFPHMTIEENIAiVPELK----KWDKDKIHDRITELLDSVGLDPEsyRHRKP-AELSG 139
Cdd:PRK15064 82 LDTVImgHTELWEVKQERDRIYALPEMSEEDGMK-VADLEvkfaEMDGYTAEARAGELLLGVGIPEE--QHYGLmSEVAP 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 489843944 140 GEQQRVGVVRALAADPGIILMDEPFSALDpISRQRLQQDIsaLQKKiKKTIVFVTHD 196
Cdd:PRK15064 159 GWKLRVLLAQALFSNPDILLLDEPTNNLD-INTIRWLEDV--LNER-NSTMIIISHD 211
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
65-229 |
2.79e-04 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 42.71 E-value: 2.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 65 RISDYDIHELRwdigyvlqqialfpHMTIEENIAIVPELKKWDKDK---------IHDRITELLDsVGLDpesY--RHRK 133
Cdd:COG0178 421 KIGGKNIAELT--------------ALSIDEALEFFENLELTEREAeiaerilkeIRSRLGFLVD-VGLD---YltLDRS 482
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 134 PAELSGGEQQR-----------VGVVralaadpgIILmDEPFSALDPISRQRLqqdISALQK--KIKKTIVFVTHD---M 197
Cdd:COG0178 483 AGTLSGGEAQRirlatqigsglVGVL--------YVL-DEPSIGLHQRDNDRL---IETLKRlrDLGNTVIVVEHDedtI 550
|
170 180 190
....*....|....*....|....*....|....*...
gi 489843944 198 QEAlalgDRICVM------QDGEIVQVATPQEIIKNPE 229
Cdd:COG0178 551 RAA----DYIIDIgpgageHGGEVVAQGTPEEILKNPD 584
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
91-229 |
4.19e-04 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 41.98 E-value: 4.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 91 MTIEENIAIVPELKKWDKDK---------IHDRITELLDsVGLDpesY--RHRKPAELSGGEQQR-----------VGVV 148
Cdd:PRK00349 437 LSIGEALEFFENLKLSEQEAkiaepilkeIRERLKFLVD-VGLD---YltLSRSAGTLSGGEAQRirlatqigsglTGVL 512
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 149 RALaadpgiilmDEPFSALDPISRQRLqqdISALQK--KIKKTIVFVTHDmQEALALGDRICVM------QDGEIVQVAT 220
Cdd:PRK00349 513 YVL---------DEPSIGLHQRDNDRL---IETLKHlrDLGNTLIVVEHD-EDTIRAADYIVDIgpgagvHGGEVVASGT 579
|
....*....
gi 489843944 221 PQEIIKNPE 229
Cdd:PRK00349 580 PEEIMKNPN 588
|
|
| SbcC_Walker_B |
pfam13558 |
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from ... |
125-175 |
5.59e-04 |
|
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from eukaryotes and the prokaryotic homolog SbcCD complex subunit C. RAD50-ATPase forms a complex with Mre11-nuclease that detects and processes diverse and obstructed DNA ends. This domain is separated of the Walker A domain by a long coiled-coil domain and forms the nucleotide-binding domain (NBD) when the coiled coils fold back on themselves and bring together Walker A and B domains. Two RAD50-NBDs forms heterotetramers with a Mre11 nuclease dimer that assemble as catalytic head module that binds and cleaves DNA in an ATP-dependent reaction. Through secondary structural analysis, it has been suggested that there is a wide structural conservation in the Rad50/SMC protein family as seen in structural similarities between RAD50's hook and ABC-ATPase MukB's elbow region.
Pssm-ID: 463921 [Multi-domain] Cd Length: 90 Bit Score: 38.37 E-value: 5.59e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489843944 125 DPESYRHRKPAELSGGEQQRVGVVrALAA--------------DPGIILMDEPFSALDPISRQRL 175
Cdd:pfam13558 21 GSEVETYRRSGGLSGGEKQLLAYL-PLAAalaaqygsaegrppAPRLVFLDEAFAKLDEENIRTA 84
|
|
| COG4938 |
COG4938 |
Predicted ATPase [General function prediction only]; |
17-182 |
9.20e-04 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443965 [Multi-domain] Cd Length: 277 Bit Score: 40.34 E-value: 9.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 17 AVNNVTLDIKDgeFFVFIGPSGCGKTTTLKMInrLIPLTTGTIYINEKRIS-----DYDIHELRwDIG----YVLQQIAL 87
Cdd:COG4938 11 PFKEAELELKP--LTLLIGPNGSGKSTLIQAL--LLLLQSNFIYLPAERSGparlyPSLVRELS-DLGsrgeYTADFLAE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 88 FPHMTIEENIA------IVPELKKWDKDKIHDRITELLDSVGLDPESYRHR-KPAELSGGEQQRVGVVRAL--AADPG-I 157
Cdd:COG4938 86 LENLEILDDKSkelleqVEEWLEKIFPGKVEVDASSDLVRLVFRPSGNGKRiPLSNVGSGVSELLPILLALlsAAKPGsL 165
|
170 180
....*....|....*....|....*
gi 489843944 158 ILMDEPFSALDPisrqRLQQDISAL 182
Cdd:COG4938 166 LIIEEPEAHLHP----KAQSALAEL 186
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
99-168 |
3.30e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 39.07 E-value: 3.30e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489843944 99 IVPELKKWDKDKIHDRITELLDSVGLDPEsYRHRKPAELSGGEQQRVGVVRALAADPGIILMDEPFSALD 168
Cdd:PLN03073 308 IYKRLELIDAYTAEARAASILAGLSFTPE-MQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLD 376
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
137-196 |
9.12e-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: 9.12e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489843944 137 LSGGEQQRVGVVRALA----ADPGIILMDEPFSALDPISRQRLQQDISALQKKIKKTIvFVTHD 196
Cdd:cd03227 78 LSGGEKELSALALILAlaslKPRPLYILDEIDRGLDPRDGQALAEAILEHLVKGAQVI-VITHL 140
|
|
| |
