|
Name |
Accession |
Description |
Interval |
E-value |
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
1-309 |
1.83e-169 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 472.27 E-value: 1.83e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 1 MIEIERAGKRFGDI-VAVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGVDTATVAPEQLRRGIGY 79
Cdd:COG1125 1 MIEFENVTKRYPDGtVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRDLDPVELRRRIGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 80 AIQGHGLFPHWSVARNIATVPRLLGWPADRIDARVNELLDLFHLAPAEFADKLPHELSGGQQQRVGVARALAAEPAMLLM 159
Cdd:COG1125 81 VIQQIGLFPHMTVAENIATVPRLLGWDKERIRARVDELLELVGLDPEEYRDRYPHELSGGQQQRVGVARALAADPPILLM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 160 DEPFGALDPIIRNKAQDDLFALQRRLGITVVIVTHDIEEALKLGDTIAVMDAGRLLQVASPAEILGKPAAGVVEQLVaGV 239
Cdd:COG1125 161 DEPFGALDPITREQLQDELLRLQRELGKTIVFVTHDIDEALKLGDRIAVMREGRIVQYDTPEEILANPANDFVADFV-GA 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 240 DRPLRLLALTPIDAVAEPghaDGEPIAATRTLRDAVSELLWRGVDVLPVGDGDGHNTRRITLDAIRAHAR 309
Cdd:COG1125 240 DRGLRRLSLLRVEDLMLP---EPPTVSPDASLREALSLMLERGVDWLLVVDEDGRPLGWLTLEDLLRALA 306
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
2-241 |
1.19e-122 |
|
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: 351.22 E-value: 1.19e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 2 IEIERAGKRFGDI-VAVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGVDTATVAPEQLRRGIGYA 80
Cdd:cd03295 1 IEFENVTKRYGGGkKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 81 IQGHGLFPHWSVARNIATVPRLLGWPADRIDARVNELLDLFHLAPAEFADKLPHELSGGQQQRVGVARALAAEPAMLLMD 160
Cdd:cd03295 81 IQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLDPAEFADRYPHELSGGQQQRVGVARALAADPPLLLMD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 161 EPFGALDPIIRNKAQDDLFALQRRLGITVVIVTHDIEEALKLGDTIAVMDAGRLLQVASPAEILGKPAAGVVEQLVaGVD 240
Cdd:cd03295 161 EPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDFVAEFV-GAD 239
|
.
gi 1861108599 241 R 241
Cdd:cd03295 240 R 240
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-228 |
5.40e-100 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 297.78 E-value: 5.40e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 1 MIEIERAGKRFGDIVAVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGVDTATVAPEqlRRGIGYA 80
Cdd:COG3842 5 ALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPE--KRNVGMV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 81 IQGHGLFPHWSVARNIATVPRLLGWPADRIDARVNELLDLFHLApaEFADKLPHELSGGQQQRVGVARALAAEPAMLLMD 160
Cdd:COG3842 83 FQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLE--GLADRYPHQLSGGQQQRVALARALAPEPRVLLLD 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1861108599 161 EPFGALDPIIRNKAQDDLFALQRRLGITVVIVTHDIEEALKLGDTIAVMDAGRLLQVASPAEILGKPA 228
Cdd:COG3842 161 EPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEIYERPA 228
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
9-311 |
4.82e-93 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 281.22 E-value: 4.82e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 9 KRFGDIVAVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGVDTATVAPEQL----RRGIGYAIQGH 84
Cdd:COG4175 35 EKTGQTVGVNDASFDVEEGEIFVIMGLSGSGKSTLVRCLNRLIEPTAGEVLIDGEDITKLSKKELrelrRKKMSMVFQHF 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 85 GLFPHWSVARN------IATVPRllgwpADRIdARVNELLDLFHLApaEFADKLPHELSGGQQQRVGVARALAAEPAMLL 158
Cdd:COG4175 115 ALLPHRTVLENvafgleIQGVPK-----AERR-ERAREALELVGLA--GWEDSYPDELSGGMQQRVGLARALATDPDILL 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 159 MDEPFGALDPIIRNKAQDDLFALQRRLGITVVIVTHDIEEALKLGDTIAVMDAGRLLQVASPAEILGKPAAGVVEQLVAG 238
Cdd:COG4175 187 MDEAFSALDPLIRREMQDELLELQAKLKKTIVFITHDLDEALRLGDRIAIMKDGRIVQIGTPEEILTNPANDYVADFVED 266
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1861108599 239 VDRpLRLLALtpiDAVAEPGHADgepIAATRTLRDAVSELLWRGVDVLPVGDGDGHNTRRITLDAIRAHARKP 311
Cdd:COG4175 267 VDR-SKVLTA---GSVMRPPEAV---VSEKDGPRVALRRMREEGISSLYVVDRDRRLLGVVTADDALEAVKGE 332
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
2-218 |
8.87e-89 |
|
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: 264.00 E-value: 8.87e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 2 IEIERAGKRFGDIVAVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGVDTATVAPEqlRRGIGYAI 81
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE--RRNIGMVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 82 QGHGLFPHWSVARNIATVPRLLGWPADRIDARVNELLDLFHLApaEFADKLPHELSGGQQQRVGVARALAAEPAMLLMDE 161
Cdd:cd03259 79 QDYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLE--GLLNRYPHELSGGQQQRVALARALAREPSLLLLDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1861108599 162 PFGALDPIIRNKAQDDLFALQRRLGITVVIVTHDIEEALKLGDTIAVMDAGRLLQVA 218
Cdd:cd03259 157 PLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
2-307 |
1.34e-88 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 268.55 E-value: 1.34e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 2 IEIERAGKRFGDIVAVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGVDTATVAPEQlRRGIGYAI 81
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFTNLPPR-ERRVGFVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 82 QGHGLFPHWSVARNIATVPRLLGWPADRIDARVNELLDLFHLApaEFADKLPHELSGGQQQRVGVARALAAEPAMLLMDE 161
Cdd:COG1118 82 QHYALFPHMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLE--GLADRYPSQLSGGQRQRVALARALAVEPEVLLLDE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 162 PFGALDPIIRNKAQDDLFALQRRLGITVVIVTHDIEEALKLGDTIAVMDAGRLLQVASPAEILGKPAAGVVEQLVAGVDR 241
Cdd:COG1118 160 PFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDRPATPFVARFLGCVNV 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1861108599 242 plrllalTPIDAVAEPGHADGEPIAATRTLRDAVSELLWRGVDVLPVGDGDGHNTRRITLDAIRAH 307
Cdd:COG1118 240 -------LRGRVIGGQLEADGLTLPVAEPLPDGPAVAGVRPHDIEVSREPEGENTFPATVARVSEL 298
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-228 |
6.04e-86 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 261.93 E-value: 6.04e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 1 MIEIERAGKRFGDIVAVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGVDTATVAPEqlRRGIGYA 80
Cdd:COG3839 3 SLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPK--DRNIAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 81 IQGHGLFPHWSVARNIATVPRLLGWPADRIDARVNELLDLFHLAPaeFADKLPHELSGGQQQRVGVARALAAEPAMLLMD 160
Cdd:COG3839 81 FQSYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLED--LLDRKPKQLSGGQRQRVALGRALVREPKVFLLD 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1861108599 161 EPFGALDPIIRNKAQDDLFALQRRLGITVVIVTHDIEEALKLGDTIAVMDAGRLLQVASPAEILGKPA 228
Cdd:COG3839 159 EPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGTPEELYDRPA 226
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-212 |
2.29e-85 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 256.94 E-value: 2.29e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 1 MIEIERAGKRF----GDIVAVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGVdtatvAPEQLRRG 76
Cdd:COG1116 7 ALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGK-----PVTGPGPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 77 IGYAIQGHGLFPHWSVARNIATVPRLLGWPADRIDARVNELLDLFHLApaEFADKLPHELSGGQQQRVGVARALAAEPAM 156
Cdd:COG1116 82 RGVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLA--GFEDAYPHQLSGGMRQRVAIARALANDPEV 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1861108599 157 LLMDEPFGALDPIIRNKAQDDLFALQRRLGITVVIVTHDIEEALKLGDTIAVMDAG 212
Cdd:COG1116 160 LLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFLADRVVVLSAR 215
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
9-241 |
4.51e-85 |
|
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: 256.80 E-value: 4.51e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 9 KRFGDIVAVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGVDTATVAPEQL----RRGIGYAIQGH 84
Cdd:cd03294 32 KKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELrelrRKKISMVFQSF 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 85 GLFPHWSVARNIATVPRLLGWPADRIDARVNELLDLFHLAPaeFADKLPHELSGGQQQRVGVARALAAEPAMLLMDEPFG 164
Cdd:cd03294 112 ALLPHRTVLENVAFGLEVQGVPRAEREERAAEALELVGLEG--WEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFS 189
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1861108599 165 ALDPIIRNKAQDDLFALQRRLGITVVIVTHDIEEALKLGDTIAVMDAGRLLQVASPAEILGKPAAGVVEQLVAGVDR 241
Cdd:cd03294 190 ALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDYVREFFRGVDR 266
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
9-290 |
3.25e-84 |
|
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: 257.86 E-value: 3.25e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 9 KRFGDIVAVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGVDTATVAPEQL----RRGIGYAIQGH 84
Cdd:TIGR01186 1 KKTGGKKGVNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEPTAGQIFIDGENIMKQSPVELrevrRKKIGMVFQQF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 85 GLFPHWSVARNIATVPRLLGWPADRIDARVNELLDLFHLApaEFADKLPHELSGGQQQRVGVARALAAEPAMLLMDEPFG 164
Cdd:TIGR01186 81 ALFPHMTILQNTSLGPELLGWPEQERKEKALELLKLVGLE--EYEHRYPDELSGGMQQRVGLARALAAEPDILLMDEAFS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 165 ALDPIIRNKAQDDLFALQRRLGITVVIVTHDIEEALKLGDTIAVMDAGRLLQVASPAEILGKPAAGVVEQLVAGVDrplr 244
Cdd:TIGR01186 159 ALDPLIRDSMQDELKKLQATLQKTIVFITHDLDEAIRIGDRIVIMKAGEIVQVGTPDEILRNPANEYVEEFIGKVD---- 234
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1861108599 245 LLALTPIDAVAEPGHADGEPIAATRTLRDAVSELLWRGVDVLPVGD 290
Cdd:TIGR01186 235 LSQVFDAERIAQRMNTGPITKTADKGPRSALQLMRDERVDSLYVVD 280
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
2-228 |
1.15e-82 |
|
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: 249.46 E-value: 1.15e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 2 IEIERAGKRFGDIVAVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGVDTATVAPEqlRRGIGYAI 81
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPH--KRPVNTVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 82 QGHGLFPHWSVARNIATVPRLLGWPADRIDARVNELLDLFHLApaEFADKLPHELSGGQQQRVGVARALAAEPAMLLMDE 161
Cdd:cd03300 79 QNYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLE--GYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDE 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1861108599 162 PFGALDPIIRNKAQDDLFALQRRLGITVVIVTHDIEEALKLGDTIAVMDAGRLLQVASPAEILGKPA 228
Cdd:cd03300 157 PLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPA 223
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
2-217 |
1.59e-78 |
|
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: 238.14 E-value: 1.59e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 2 IEIERAGKRFGD----IVAVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGVdtatvAPEQLRRGI 77
Cdd:cd03293 1 LEVRNVSKTYGGgggaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGE-----PVTGPGPDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 78 GYAIQGHGLFPHWSVARNIATVPRLLGWPADRIDARVNELLDLFHLApaEFADKLPHELSGGQQQRVGVARALAAEPAML 157
Cdd:cd03293 76 GYVFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLS--GFENAYPHQLSGGMRQRVALARALAVDPDVL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1861108599 158 LMDEPFGALDPIIRNKAQDDLFALQRRLGITVVIVTHDIEEALKLGDTIAVMDA--GRLLQV 217
Cdd:cd03293 154 LLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLSArpGRIVAE 215
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
2-232 |
1.41e-74 |
|
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: 228.76 E-value: 1.41e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 2 IEIERAGKRFGDIVAVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGVDTATVAPEQlrRGIGYAI 81
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQE--RNVGFVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 82 QGHGLFPHWSVARNIA----TVPRLLGWPADRIDARVNELLDLFHLApaEFADKLPHELSGGQQQRVGVARALAAEPAML 157
Cdd:cd03296 81 QHYALFRHMTVFDNVAfglrVKPRSERPPEAEIRAKVHELLKLVQLD--WLADRYPAQLSGGQRQRVALARALAVEPKVL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1861108599 158 LMDEPFGALDPIIRNKAQDDLFALQRRLGITVVIVTHDIEEALKLGDTIAVMDAGRLLQVASPAEILGKPAAGVV 232
Cdd:cd03296 159 LLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPASPFV 233
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1-242 |
3.45e-74 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 231.12 E-value: 3.45e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 1 MIEIERAGKRF----GDIVAVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGVDTATVAPEQL--- 73
Cdd:COG1135 1 MIELENLSKTFptkgGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELraa 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 74 RRGIGYAIQGHGLFPHWSVARNIATVPRLLGWPADRIDARVNELLDLFHLapAEFADKLPHELSGGQQQRVGVARALAAE 153
Cdd:COG1135 81 RRKIGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGL--SDKADAYPSQLSGGQKQRVGIARALANN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 154 PAMLLMDEPFGALDP-----IIrnkaqdDLFA-LQRRLGITVVIVTHDIEEALKLGDTIAVMDAGRLLQVASPAEILGKP 227
Cdd:COG1135 159 PKVLLCDEATSALDPettrsIL------DLLKdINRELGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVLDVFANP 232
|
250
....*....|....*
gi 1861108599 228 AAGVVEQLVAGVDRP 242
Cdd:COG1135 233 QSELTRRFLPTVLND 247
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
1-227 |
4.74e-74 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 227.57 E-value: 4.74e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 1 MIEIERAGKRFGDIVAVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDG--VDTATVAPEQLRRGIG 78
Cdd:COG1126 1 MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGedLTDSKKDINKLRRKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 79 YAIQGHGLFPHWSVARNIATVPR-LLGWPADRIDARVNELLDLFHLApaEFADKLPHELSGGQQQRVGVARALAAEPAML 157
Cdd:COG1126 81 MVFQQFNLFPHLTVLENVTLAPIkVKKMSKAEAEERAMELLERVGLA--DKADAYPAQLSGGQQQRVAIARALAMEPKVM 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1861108599 158 LMDEPFGALDP--------IIRNKAQDdlfalqrrlGITVVIVTHDIEEALKLGDTIAVMDAGRLLQVASPAEILGKP 227
Cdd:COG1126 159 LFDEPTSALDPelvgevldVMRDLAKE---------GMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFENP 227
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
2-226 |
6.55e-74 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 226.87 E-value: 6.55e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 2 IEIERAGKRFGDIVAVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGVDTATvAPEQLRRGIGYAI 81
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVAR-DPAEVRRRIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 82 QGHGLFPHWSVARNIATVPRLLGWPADRIDARVNELLDLFHLapAEFADKLPHELSGGQQQRVGVARALAAEPAMLLMDE 161
Cdd:COG1131 80 QEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGL--TDAADRKVGTLSGGMKQRLGLALALLHDPELLILDE 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1861108599 162 PFGALDPIIRNKAQDDLFALQRRlGITVVIVTHDIEEALKLGDTIAVMDAGRLLQVASPAEILGK 226
Cdd:COG1131 158 PTSGLDPEARRELWELLRELAAE-GKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKAR 221
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
2-241 |
1.68e-72 |
|
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 223.52 E-value: 1.68e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 2 IEIERAGKRFGDIVAVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGVDTATVAPEqlRRGIGYAI 81
Cdd:TIGR00968 1 IEIANISKRFGSFQALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGLEQPDSGRIRLNGQDATRVHAR--DRKIGFVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 82 QGHGLFPHWSVARNIATVPRLLGWPADRIDARVNELLDLFHLApaEFADKLPHELSGGQQQRVGVARALAAEPAMLLMDE 161
Cdd:TIGR00968 79 QHYALFKHLTVRDNIAFGLEIRKHPKAKIKARVEELLELVQLE--GLGDRYPNQLSGGQRQRVALARALAVEPQVLLLDE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 162 PFGALDPIIRNKAQDDLFALQRRLGITVVIVTHDIEEALKLGDTIAVMDAGRLLQVASPAEILGKPAAGVVEQLVAGVDR 241
Cdd:TIGR00968 157 PFGALDAKVRKELRSWLRKLHDEVHVTTVFVTHDQEEAMEVADRIVVMSNGKIEQIGSPDEVYDHPANPFVMSFLGEVNV 236
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-224 |
8.68e-72 |
|
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: 221.78 E-value: 8.68e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 1 MIEIERAGKRFGDIVAVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGVDTATVAPEQL---RRGI 77
Cdd:COG1127 5 MIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELyelRRRI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 78 GYAIQGHGLFPHWSVARNIAtVP--RLLGWPADRIDARVNELLDLFHLAPAefADKLPHELSGGQQQRVGVARALAAEPA 155
Cdd:COG1127 85 GMLFQGGALFDSLTVFENVA-FPlrEHTDLSEAEIRELVLEKLELVGLPGA--ADKMPSELSGGMRKRVALARALALDPE 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 156 MLLMDEPFGALDPIIRNKAqDDLFA-LQRRLGITVVIVTHDIEEALKLGDTIAVMDAGRLLQVASPAEIL 224
Cdd:COG1127 162 ILLYDEPTAGLDPITSAVI-DELIReLRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELL 230
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-237 |
3.44e-71 |
|
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: 228.63 E-value: 3.44e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 1 MIEIERAGKRF-----GDIVAVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGVDTATVAPE---Q 72
Cdd:COG1123 260 LLEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRslrE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 73 LRRGIGYAIQG--HGLFPHWSVARNIATVPRLLGW-PADRIDARVNELLDLFHLaPAEFADKLPHELSGGQQQRVGVARA 149
Cdd:COG1123 340 LRRRVQMVFQDpySSLNPRMTVGDIIAEPLRLHGLlSRAERRERVAELLERVGL-PPDLADRYPHELSGGQRQRVAIARA 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 150 LAAEPAMLLMDEPFGALDPIIRNKAQDDLFALQRRLGITVVIVTHDIEEALKLGDTIAVMDAGRLLQVASPAEILGKPAA 229
Cdd:COG1123 419 LALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVFANPQH 498
|
....*...
gi 1861108599 230 GVVEQLVA 237
Cdd:COG1123 499 PYTRALLA 506
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1-227 |
5.96e-70 |
|
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: 217.06 E-value: 5.96e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 1 MIEIERAGKRFGD----IVAVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGVDTATVAPEQL--- 73
Cdd:cd03258 1 MIELKNVSKVFGDtggkVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELrka 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 74 RRGIGYAIQGHGLFPHWSVARNIATVPRLLGWPADRIDARVNELLDLFHLapAEFADKLPHELSGGQQQRVGVARALAAE 153
Cdd:cd03258 81 RRRIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGL--EDKADAYPAQLSGGQKQRVGIARALANN 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1861108599 154 PAMLLMDEPFGALDPIIRNKAQDDLFALQRRLGITVVIVTHDIEEALKLGDTIAVMDAGRLLQVASPAEILGKP 227
Cdd:cd03258 159 PKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFANP 232
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
2-236 |
4.88e-69 |
|
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: 218.75 E-value: 4.88e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 2 IEIERAGKRFGDIVAVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGVDTATVAPEQlrRGIGYAI 81
Cdd:TIGR03265 5 LSIDNIRKRFGAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRLPPQK--RDYGIVF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 82 QGHGLFPHWSVARNIA--TVPRllGWPADRIDARVNELLDLFHLAPAEfaDKLPHELSGGQQQRVGVARALAAEPAMLLM 159
Cdd:TIGR03265 83 QSYALFPNLTVADNIAygLKNR--GMGRAEVAERVAELLDLVGLPGSE--RKYPGQLSGGQQQRVALARALATSPGLLLL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1861108599 160 DEPFGALDPIIRNKAQDDLFALQRRLGITVVIVTHDIEEALKLGDTIAVMDAGRLLQVASPAEILGKPAAGVVEQLV 236
Cdd:TIGR03265 159 DEPLSALDARVREHLRTEIRQLQRRLGVTTIMVTHDQEEALSMADRIVVMNHGVIEQVGTPQEIYRHPATPFVADFV 235
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1-240 |
5.28e-69 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 219.32 E-value: 5.28e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 1 MIEIERAGKRFGDIVAVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGVDTATVAPEQlrRGIGYA 80
Cdd:PRK11607 19 LLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQ--RPINMM 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 81 IQGHGLFPHWSVARNIATVPRLLGWPADRIDARVNELLDLFHLApaEFADKLPHELSGGQQQRVGVARALAAEPAMLLMD 160
Cdd:PRK11607 97 FQSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQ--EFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLD 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 161 EPFGALDPIIRNKAQDDLFALQRRLGITVVIVTHDIEEALKLGDTIAVMDAGRLLQVASPAEILGKPAAGVVEQLVAGVD 240
Cdd:PRK11607 175 EPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAEFIGSVN 254
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
2-218 |
1.01e-68 |
|
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: 212.89 E-value: 1.01e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 2 IEIERAGKRFGDIVAVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGVDTATVAPEQlrRGIGYAI 81
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKD--RDIAMVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 82 QGHGLFPHWSVARNIATVPRLLGWPADRIDARVNELLDLFHLApaEFADKLPHELSGGQQQRVGVARALAAEPAMLLMDE 161
Cdd:cd03301 79 QNYALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIE--HLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1861108599 162 PFGALDPIIRNKAQDDLFALQRRLGITVVIVTHDIEEALKLGDTIAVMDAGRLLQVA 218
Cdd:cd03301 157 PLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
2-228 |
1.22e-67 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 215.58 E-value: 1.22e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 2 IEIERAGKRFGDIVAVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGVDTATVAPEQlrRGIGYAI 81
Cdd:PRK09452 15 VELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAEN--RHVNTVF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 82 QGHGLFPHWSVARNIATVPRLLGWPADRIDARVNELLDLFHLApaEFADKLPHELSGGQQQRVGVARALAAEPAMLLMDE 161
Cdd:PRK09452 93 QSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLE--EFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDE 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1861108599 162 PFGALDPIIRNKAQDDLFALQRRLGITVVIVTHDIEEALKLGDTIAVMDAGRLLQVASPAEILGKPA 228
Cdd:PRK09452 171 SLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPK 237
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-214 |
1.51e-67 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 210.28 E-value: 1.51e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 1 MIEIERAGKRFGD----IVAVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGVDTATVAPEQL--- 73
Cdd:COG1136 4 LLELRNLTKSYGTgegeVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELarl 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 74 -RRGIGYAIQGHGLFPHWSVARNIATVPRLLGWPADRIDARVNELLDLFHLApaEFADKLPHELSGGQQQRVGVARALAA 152
Cdd:COG1136 84 rRRHIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLG--DRLDHRPSQLSGGQQQRVAIARALVN 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1861108599 153 EPAMLLMDEPFGALDPiiRNKAQ--DDLFALQRRLGITVVIVTHDiEEALKLGDTIAVMDAGRL 214
Cdd:COG1136 162 RPKLILADEPTGNLDS--KTGEEvlELLRELNRELGTTIVMVTHD-PELAARADRVIRLRDGRI 222
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
32-228 |
3.38e-67 |
|
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: 213.12 E-value: 3.38e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 32 LVGASGSGKSTLLRMINRLIAPTSGTIRIDGVDTATVAPEqlRRGIGYAIQGHGLFPHWSVARNIATVPRLLGWPADRID 111
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPH--LRHINMVFQSYALFPHMTVEENVAFGLKMRKVPRAEIK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 112 ARVNELLDLFHLApaEFADKLPHELSGGQQQRVGVARALAAEPAMLLMDEPFGALDPIIRNKAQDDLFALQRRLGITVVI 191
Cdd:TIGR01187 79 PRVLEALRLVQLE--EFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITFVF 156
|
170 180 190
....*....|....*....|....*....|....*..
gi 1861108599 192 VTHDIEEALKLGDTIAVMDAGRLLQVASPAEILGKPA 228
Cdd:TIGR01187 157 VTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPA 193
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
2-213 |
5.12e-67 |
|
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: 207.42 E-value: 5.12e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 2 IEIERAGKRFGDIVAVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGVDTATVA--PEQLRRGIGY 79
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEdeLPPLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 80 AIQGHGLFPHWSVARNIAtvprllgwpadridarvnelldlfhlapaefadklpHELSGGQQQRVGVARALAAEPAMLLM 159
Cdd:cd03229 81 VFQDFALFPHLTVLENIA------------------------------------LGLSGGQQQRVALARALAMDPDVLLL 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1861108599 160 DEPFGALDPIIRNKAQDDLFALQRRLGITVVIVTHDIEEALKLGDTIAVMDAGR 213
Cdd:cd03229 125 DEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1-222 |
2.91e-66 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 207.21 E-value: 2.91e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 1 MIEIERAGKRF-GDIVAVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGVDTATVAPEQ---LRRG 76
Cdd:COG2884 1 MIRFENVSKRYpGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREipyLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 77 IGYAIQGHGLFPHWSVARNIATVPRLLGWPADRIDARVNELLDLFHLApaEFADKLPHELSGGQQQRVGVARALAAEPAM 156
Cdd:COG2884 81 IGVVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLS--DKAKALPHELSGGEQQRVAIARALVNRPEL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1861108599 157 LLMDEPFGALDP-----IIRnkaqddLFALQRRLGITVVIVTHDIEEALKLGDTIAVMDAGRLLQVASPAE 222
Cdd:COG2884 159 LLADEPTGNLDPetsweIME------LLEEINRRGTTVLIATHDLELVDRMPKRVLELEDGRLVRDEARGV 223
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
12-227 |
3.43e-66 |
|
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: 207.18 E-value: 3.43e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 12 GDIVAVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGVDTATVAPEQLRRGIGYAIQ--GHGLF-P 88
Cdd:COG1122 12 GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGLVFQnpDDQLFaP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 89 hwSVARNIATVPRLLGWPADRIDARVNELLDLFHLapAEFADKLPHELSGGQQQRVGVARALAAEPAMLLMDEPFGALDP 168
Cdd:COG1122 92 --TVEEDVAFGPENLGLPREEIRERVEEALELVGL--EHLADRPPHELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDP 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1861108599 169 iirnKAQDDLFALQRRL---GITVVIVTHDIEEALKLGDTIAVMDAGRLLQVASPAEILGKP 227
Cdd:COG1122 168 ----RGRRELLELLKRLnkeGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDY 225
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
2-223 |
3.17e-65 |
|
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: 204.72 E-value: 3.17e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 2 IEIERAGKRFGDIVAVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLI-----APTSGTIRIDGVD--TATVAPEQLR 74
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNdlipgAPDEGEVLLDGKDiyDLDVDVLELR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 75 RGIGYAIQGHGLFPHwSVARNIATVPRLLG-WPADRIDARVNELLDLFHLaPAEFADKL-PHELSGGQQQRVGVARALAA 152
Cdd:cd03260 81 RRVGMVFQKPNPFPG-SIYDNVAYGLRLHGiKLKEELDERVEEALRKAAL-WDEVKDRLhALGLSGGQQQRLCLARALAN 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1861108599 153 EPAMLLMDEPFGALDPIIRNKAQDDLFALQRRlgITVVIVTHDIEEALKLGDTIAVMDAGRLLQVASPAEI 223
Cdd:cd03260 159 EPEVLLLDEPTSALDPISTAKIEELIAELKKE--YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
1-214 |
6.24e-64 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 201.82 E-value: 6.24e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 1 MIEIERAGKRF-GDIVAVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGVDTATVAPEQL---RRG 76
Cdd:COG3638 2 MLELRNLSKRYpGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALrrlRRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 77 IGYAIQGHGLFPHWSVARNI--------ATVPRLLGW--PADRIDARvnELLDLFHLApaEFADKLPHELSGGQQQRVGV 146
Cdd:COG3638 82 IGMIFQQFNLVPRLSVLTNVlagrlgrtSTWRSLLGLfpPEDRERAL--EALERVGLA--DKAYQRADQLSGGQQQRVAI 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1861108599 147 ARALAAEPAMLLMDEPFGALDPIIRNKAQDDLFALQRRLGITVVIVTHDIEEALKLGDTIAVMDAGRL 214
Cdd:COG3638 158 ARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRV 225
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1-224 |
7.42e-64 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 201.62 E-value: 7.42e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 1 MIEIERAGKRFGDIVAVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGVDTATvAPEQLRRGIGYA 80
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRK-EPREARRQIGVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 81 IQGHGLFPHWSVARNIATVPRLLGWPADRIDARVNELLDLFHLapAEFADKLPHELSGGQQQRVGVARALAAEPAMLLMD 160
Cdd:COG4555 80 PDERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGL--EEFLDRRVGELSTGMKKKVALARALVHDPKVLLLD 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1861108599 161 EPFGALDPIIRNKAQDDLFALqRRLGITVVIVTHDIEEALKLGDTIAVMDAGRLLQVASPAEIL 224
Cdd:COG4555 158 EPTNGLDVMARRLLREILRAL-KKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELR 220
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
2-223 |
4.02e-63 |
|
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: 199.65 E-value: 4.02e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 2 IEIERAGKRFGDIVAVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGVDTATVAPEQL---RRGIG 78
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELyrlRRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 79 YAIQGHGLFPHWSVARNIAtVP-----RLlgwPADRIDARVNELLDLFHLAPAEfaDKLPHELSGGQQQRVGVARALAAE 153
Cdd:cd03261 81 MLFQSGALFDSLTVFENVA-FPlrehtRL---SEEEIREIVLEKLEAVGLRGAE--DLYPAELSGGMKKRVALARALALD 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 154 PAMLLMDEPFGALDPIIRNKAQDDLFALQRRLGITVVIVTHDIEEALKLGDTIAVMDAGRLLQVASPAEI 223
Cdd:cd03261 155 PELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEEL 224
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1-214 |
8.83e-63 |
|
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: 198.50 E-value: 8.83e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 1 MIEIERAGKRF----GDIVAVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGVDTATVAPEQL--- 73
Cdd:cd03257 1 LLEVKNLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRkir 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 74 RRGIGYAIQ--GHGLFPHWSVARNIATVPRLLG--WPADRIDARVNELLDLFHLaPAEFADKLPHELSGGQQQRVGVARA 149
Cdd:cd03257 81 RKEIQMVFQdpMSSLNPRMTIGEQIAEPLRIHGklSKKEARKEAVLLLLVGVGL-PEEVLNRYPHELSGGQRQRVAIARA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1861108599 150 LAAEPAMLLMDEPFGALDPIIRNKAQDDLFALQRRLGITVVIVTHDIEEALKLGDTIAVMDAGRL 214
Cdd:cd03257 160 LALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKI 224
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
2-236 |
1.04e-62 |
|
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: 198.33 E-value: 1.04e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 2 IEIERAGKRFGDIVaVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGVDTATVAPEqlRRGIGYAI 81
Cdd:cd03299 1 LKVENLSKDWKEFK-LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE--KRDISYVP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 82 QGHGLFPHWSVARNIATVPRLLGWPADRIDARVNELLDLFHLApaEFADKLPHELSGGQQQRVGVARALAAEPAMLLMDE 161
Cdd:cd03299 78 QNYALFPHMTVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGID--HLLNRKPETLSGGEQQRVAIARALVVNPKILLLDE 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1861108599 162 PFGALDPIIRNKAQDDLFALQRRLGITVVIVTHDIEEALKLGDTIAVMDAGRLLQVASPAEILGKPAAGVVEQLV 236
Cdd:cd03299 156 PFSALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPKNEFVAEFL 230
|
|
| tungstate_WtpC |
NF040840 |
tungstate ABC transporter ATP-binding protein WtpC; |
1-236 |
1.53e-62 |
|
tungstate ABC transporter ATP-binding protein WtpC;
Pssm-ID: 468779 [Multi-domain] Cd Length: 347 Bit Score: 201.84 E-value: 1.53e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 1 MIEIERAGKRFGDIvAVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGVDTATVAPEQlrRGIGYA 80
Cdd:NF040840 1 MIRIENLSKDWKEF-KLRDISLEVKEGEYFIILGPSGAGKTVLLELIAGIWPPDSGKIYLDGKDITNLPPEK--RGIAYV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 81 IQGHGLFPHWSVARNIATVPRLLGWPADRIDARVNELLDLF---HLApaefaDKLPHELSGGQQQRVGVARALAAEPAML 157
Cdd:NF040840 78 YQNYMLFPHKTVFENIAFGLKLRKVPKEEIERKVKEIMELLgisHLL-----HRKPRTLSGGEQQRVALARALIIEPKLL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1861108599 158 LMDEPFGALDPIIRNKAQDDLFALQRRLGITVVIVTHDIEEALKLGDTIAVMDAGRLLQVASPAEILGKPAAGVVEQLV 236
Cdd:NF040840 153 LLDEPLSALDVQTRDELIREMKRWHREFGFTAIHVTHNFEEALSLADRVGIMLNGRLSQVGDVREVFRRPKNEFVARFV 231
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
2-214 |
2.10e-62 |
|
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: 196.94 E-value: 2.10e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 2 IEIERAGKRFGD----IVAVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGVDTATVAPEQL---- 73
Cdd:cd03255 1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 74 RRGIGYAIQGHGLFPHWSVARNIATVPRLLGWPADRIDARVNELLDLFHLApaEFADKLPHELSGGQQQRVGVARALAAE 153
Cdd:cd03255 81 RRHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLG--DRLNHYPSELSGGQQQRVAIARALAND 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1861108599 154 PAMLLMDEPFGALDPIIRNKAQDDLFALQRRLGITVVIVTHDIEEAlKLGDTIAVMDAGRL 214
Cdd:cd03255 159 PKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELA-EYADRIIELRDGKI 218
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1-265 |
7.73e-62 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 199.64 E-value: 7.73e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 1 MIEIERAGKRF----GDIVAVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGVDTATVAPEQL--- 73
Cdd:PRK11153 1 MIELKNISKVFpqggRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELrka 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 74 RRGIGYAIQGHGLFPHWSVARNIATVPRLLGWPADRIDARVNELLDLFHLapAEFADKLPHELSGGQQQRVGVARALAAE 153
Cdd:PRK11153 81 RRQIGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGL--SDKADRYPAQLSGGQKQRVAIARALASN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 154 PAMLLMDEPFGALDPIIRNKAQDDLFALQRRLGITVVIVTHDIEEALKLGDTIAVMDAGRLLQVASPAEILGKPAAGVVE 233
Cdd:PRK11153 159 PKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHPKHPLTR 238
|
250 260 270
....*....|....*....|....*....|....*
gi 1861108599 234 QLVA---GVDRPLRLLaltpiDAVAEPGHADGEPI 265
Cdd:PRK11153 239 EFIQstlHLDLPEDYL-----ARLQAEPTTGSGPL 268
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-239 |
3.37e-61 |
|
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: 195.02 E-value: 3.37e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 1 MIEIERAGKRFG----DIVAVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGVDTATVAPEQLRRG 76
Cdd:COG1124 1 MLEVRNLSVSYGqggrRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 77 IGYAIQ-GHG-LFPHWSVARNIATVPRLLGWPadRIDARVNELLDLFHLaPAEFADKLPHELSGGQQQRVGVARALAAEP 154
Cdd:COG1124 81 VQMVFQdPYAsLHPRHTVDRILAEPLRIHGLP--DREERIAELLEQVGL-PPSFLDRYPHQLSGGQRQRVAIARALILEP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 155 AMLLMDEPFGALDPIIRNKAQDDLFALQRRLGITVVIVTHDIEEALKLGDTIAVMDAGRLLQVASPAEILGKPAAGVVEQ 234
Cdd:COG1124 158 ELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAGPKHPYTRE 237
|
....*
gi 1861108599 235 LVAGV 239
Cdd:COG1124 238 LLAAS 242
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
12-213 |
1.88e-60 |
|
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: 191.91 E-value: 1.88e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 12 GDIVAVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGVDTATVAPEQLRRGIGYAIQG--HGLFPH 89
Cdd:cd03225 12 GARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLVFQNpdDQFFGP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 90 wSVARNIATVPRLLGWPADRIDARVNELLDLFHLapAEFADKLPHELSGGQQQRVGVARALAAEPAMLLMDEPFGALDPi 169
Cdd:cd03225 92 -TVEEEVAFGLENLGLPEEEIEERVEEALELVGL--EGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDP- 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1861108599 170 irnKAQDDLFALQRRL---GITVVIVTHDIEEALKLGDTIAVMDAGR 213
Cdd:cd03225 168 ---AGRRELLELLKKLkaeGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
2-214 |
4.28e-60 |
|
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: 190.82 E-value: 4.28e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 2 IEIERAGKRFGDIVAVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDG--VDTATVAPEQLRRGIGY 79
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGlkLTDDKKNINELRQKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 80 AIQGHGLFPHWSVARNIATVPR-LLGWPADRIDARVNELLDLFHLapAEFADKLPHELSGGQQQRVGVARALAAEPAMLL 158
Cdd:cd03262 81 VFQQFNLFPHLTVLENITLAPIkVKGMSKAEAEERALELLEKVGL--ADKADAYPAQLSGGQQQRVAIARALAMNPKVML 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1861108599 159 MDEPFGALDP--------IIRNKAQDdlfalqrrlGITVVIVTHDIEEALKLGDTIAVMDAGRL 214
Cdd:cd03262 159 FDEPTSALDPelvgevldVMKDLAEE---------GMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
9-229 |
1.43e-59 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 194.17 E-value: 1.43e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 9 KRFGDIVAVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGVDTATVAPEQlrRGIGYAIQGHGLFP 88
Cdd:PRK11432 14 KRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQ--RDICMVFQSYALFP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 89 HWSVARNIATVPRLLGWPADRIDARVNELLDLFHLApaEFADKLPHELSGGQQQRVGVARALAAEPAMLLMDEPFGALDP 168
Cdd:PRK11432 92 HMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLA--GFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDA 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1861108599 169 IIRNKAQDDLFALQRRLGITVVIVTHDIEEALKLGDTIAVMDAGRLLQVASPAEILGKPAA 229
Cdd:PRK11432 170 NLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPAS 230
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
2-241 |
1.41e-58 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 191.45 E-value: 1.41e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 2 IEIERAGKRFGDIVAVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGVDTATVAPEQlrRGIGYAI 81
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARD--RKVGFVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 82 QGHGLFPHWSVARNIA---TV-PRLLGWPADRIDARVNELLDLFHLApaEFADKLPHELSGGQQQRVGVARALAAEPAML 157
Cdd:PRK10851 81 QHYALFRHMTVFDNIAfglTVlPRRERPNAAAIKAKVTQLLEMVQLA--HLADRYPAQLSGGQKQRVALARALAVEPQIL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 158 LMDEPFGALDPIIRNKAQDDLFALQRRLGITVVIVTHDIEEALKLGDTIAVMDAGRLLQVASPAEILGKPAAGVVEQLVA 237
Cdd:PRK10851 159 LLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREPATRFVLEFMG 238
|
....
gi 1861108599 238 GVDR 241
Cdd:PRK10851 239 EVNR 242
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
16-227 |
1.76e-58 |
|
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: 188.81 E-value: 1.76e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 16 AVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGVDTAT---VAPEQLRRGIGYAIQ--GHGLFPHw 90
Cdd:TIGR04521 20 ALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAkkkKKLKDLRKKVGLVFQfpEHQLFEE- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 91 SVARNIATVPRLLGWPADRIDARVNELLDLFHLaPAEFADKLPHELSGGQQQRVGVARALAAEPAMLLMDEPFGALDPii 170
Cdd:TIGR04521 99 TVYKDIAFGPKNLGLSEEEAEERVKEALELVGL-DEEYLERSPFELSGGQMRRVAIAGVLAMEPEVLILDEPTAGLDP-- 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1861108599 171 rnKAQDDLFA----LQRRLGITVVIVTHDIEEALKLGDTIAVMDAGRLLQVASPAEILGKP 227
Cdd:TIGR04521 176 --KGRKEILDlfkrLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVFSDV 234
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
27-216 |
1.29e-57 |
|
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: 184.81 E-value: 1.29e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 27 GTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGV---DT--ATVAPEQlRRGIGYAIQGHGLFPHWSVARNIATVPR 101
Cdd:cd03297 23 EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTvlfDSrkKINLPPQ-QRKIGLVFQQYALFPHLNVRENLAFGLK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 102 LLGWPADRIdaRVNELLDLFHLAPAEFADklPHELSGGQQQRVGVARALAAEPAMLLMDEPFGALDPIIRNKAQDDLFAL 181
Cdd:cd03297 102 RKRNREDRI--SVDELLDLLGLDHLLNRY--PAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELKQI 177
|
170 180 190
....*....|....*....|....*....|....*
gi 1861108599 182 QRRLGITVVIVTHDIEEALKLGDTIAVMDAGRLLQ 216
Cdd:cd03297 178 KKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQY 212
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1-224 |
5.65e-57 |
|
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: 184.48 E-value: 5.65e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 1 MIEIERAGKRFGDIVAVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGVDTATVAPEQLRRGIGYA 80
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 81 IQGHGLFPHWSVARNIAT--VP--RLLGWPADRIDARVNELLDLFHLapAEFADKLPHELSGGQQQRVGVARALAAEPAM 156
Cdd:COG1120 81 PQEPPAPFGLTVRELVALgrYPhlGLFGRPSAEDREAVEEALERTGL--EHLADRPVDELSGGERQRVLIARALAQEPPL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1861108599 157 LLMDEPFGALDPiirnKAQDDLFALQRRL----GITVVIVTHDIEEALKLGDTIAVMDAGRLLQVASPAEIL 224
Cdd:COG1120 159 LLLDEPTSHLDL----AHQLEVLELLRRLarerGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEVL 226
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-233 |
7.12e-57 |
|
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: 184.09 E-value: 7.12e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 1 MIEIERAGKRFGDIVAVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGVDTATVAPEQL-RRGIGY 79
Cdd:COG0411 4 LLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIaRLGIAR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 80 AIQGHGLFPHWSVARNIAT----------VPRLLGWPADR-----IDARVNELLDLFHLapAEFADKLPHELSGGQQQRV 144
Cdd:COG0411 84 TFQNPRLFPELTVLENVLVaaharlgrglLAALLRLPRARreereARERAEELLERVGL--ADRADEPAGNLSYGQQRRL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 145 GVARALAAEPAMLLMDEPFGALDPIIRNKAQDDLFALQRRLGITVVIVTHDIEEALKLGDTIAVMDAGRLLQVASPAEIL 224
Cdd:COG0411 162 EIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGTPAEVR 241
|
....*....
gi 1861108599 225 GKPAagVVE 233
Cdd:COG0411 242 ADPR--VIE 248
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
2-223 |
1.11e-55 |
|
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: 180.46 E-value: 1.11e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 2 IEIERAGKRFGDIV-AVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGVDTATVAPE---QLRRGI 77
Cdd:cd03256 1 IEVENLSKTYPNGKkALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKalrQLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 78 GYAIQGHGLFPHWSVARNI--------ATVPRLLGW--PADRIDARvnELLDLFHLApaEFADKLPHELSGGQQQRVGVA 147
Cdd:cd03256 81 GMIFQQFNLIERLSVLENVlsgrlgrrSTWRSLFGLfpKEEKQRAL--AALERVGLL--DKAYQRADQLSGGQQQRVAIA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1861108599 148 RALAAEPAMLLMDEPFGALDPIIRNKAQDDLFALQRRLGITVVIVTHDIEEALKLGDTIAVMDAGRLLQVASPAEI 223
Cdd:cd03256 157 RALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAEL 232
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-229 |
1.56e-55 |
|
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: 187.80 E-value: 1.56e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 1 MIEIERAGKRF--GDIVAVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPT---SGTIRIDGVDTATVAPEQLRR 75
Cdd:COG1123 4 LLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRGR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 76 GIGYAIQ--GHGLFPhWSVARNIATVPRLLGWPADRIDARVNELLDLFHLApaEFADKLPHELSGGQQQRVGVARALAAE 153
Cdd:COG1123 84 RIGMVFQdpMTQLNP-VTVGDQIAEALENLGLSRAEARARVLELLEAVGLE--RRLDRYPHQLSGGQRQRVAIAMALALD 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1861108599 154 PAMLLMDEPFGALDPIIRNKAQDDLFALQRRLGITVVIVTHDIEEALKLGDTIAVMDAGRLLQVASPAEILGKPAA 229
Cdd:COG1123 161 PDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAPQA 236
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-228 |
2.24e-55 |
|
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: 182.18 E-value: 2.24e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 1 MIEIERAGKRF----GDIVAVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAP---TSGTIRIDGVDTATVAPEQL 73
Cdd:COG0444 1 LLEVRNLKVYFptrrGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 74 R----RGIGYAIQG--HGLFPHWSVARNIATVPRL-LGWPADRIDARVNELLDLFHL-APAEFADKLPHELSGGQQQRVG 145
Cdd:COG0444 81 RkirgREIQMIFQDpmTSLNPVMTVGDQIAEPLRIhGGLSKAEARERAIELLERVGLpDPERRLDRYPHELSGGMRQRVM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 146 VARALAAEPAMLLMDEPFGALDPIIRnkAQ--DDLFALQRRLGITVVIVTHDIEEALKLGDTIAVMDAGRLLQVASPAEI 223
Cdd:COG0444 161 IARALALEPKLLIADEPTTALDVTIQ--AQilNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGPVEEL 238
|
....*
gi 1861108599 224 LGKPA 228
Cdd:COG0444 239 FENPR 243
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-212 |
1.27e-54 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 178.52 E-value: 1.27e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 1 MIEIERAGKRFG----DIVAVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGVDTATVAPEqlrRG 76
Cdd:COG4525 3 MLTVRHVSVRYPgggqPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGAD---RG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 77 IGYaiQGHGLFPHWSVARNIATVPRLLGWPADRIDARVNELLDLFHLApaEFADKLPHELSGGQQQRVGVARALAAEPAM 156
Cdd:COG4525 80 VVF--QKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLA--DFARRRIWQLSGGMRQRVGIARALAADPRF 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1861108599 157 LLMDEPFGALDPIIRNKAQDDLFALQRRLGITVVIVTHDIEEALKLGDTIAVMDAG 212
Cdd:COG4525 156 LLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHSVEEALFLATRLVVMSPG 211
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
2-228 |
2.52e-54 |
|
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: 176.86 E-value: 2.52e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 2 IEIERAGKRFGDIVAVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGVDTATVAPEQL-RRGIGYA 80
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIaRLGIGRT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 81 IQGHGLFPHWSVARNI------ATVPRLLGWPA----DRIDARVNELLDLFHLapAEFADKLPHELSGGQQQRVGVARAL 150
Cdd:cd03219 81 FQIPRLFPELTVLENVmvaaqaRTGSGLLLARArreeREARERAEELLERVGL--ADLADRPAGELSYGQQRRLEIARAL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 151 AAEPAMLLMDEPFGALDPiirnKAQDDLFALQRRL---GITVVIVTHDIEEALKLGDTIAVMDAGRLLQVASPAEILGKP 227
Cdd:cd03219 159 ATDPKLLLLDEPAAGLNP----EETEELAELIRELrerGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRNNP 234
|
.
gi 1861108599 228 A 228
Cdd:cd03219 235 R 235
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
2-214 |
4.88e-54 |
|
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: 174.12 E-value: 4.88e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 2 IEIERAGKRFGDIVAVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGVDTATvAPEQLRRGIGYAI 81
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK-EPEEVKRRIGYLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 82 QGHGLFPHWSVARNIatvprllgwpadridarvnelldlfhlapaefadklphELSGGQQQRVGVARALAAEPAMLLMDE 161
Cdd:cd03230 80 EEPSLYENLTVRENL--------------------------------------KLSGGMKQRLALAQALLHDPELLILDE 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1861108599 162 PFGALDPIIRNKAQDDLFALQRRlGITVVIVTHDIEEALKLGDTIAVMDAGRL 214
Cdd:cd03230 122 PTSGLDPESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
15-240 |
1.34e-53 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 180.23 E-value: 1.34e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 15 VAVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGVDTATVAPEQLR----RGIGYAIQGHGLFPHW 90
Cdd:PRK10070 42 LGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELRevrrKKIAMVFQSFALMPHM 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 91 SVARNIATVPRLLGWPADriDARVNELLDLFHLAPAEFADKLPHELSGGQQQRVGVARALAAEPAMLLMDEPFGALDPII 170
Cdd:PRK10070 122 TVLDNTAFGMELAGINAE--ERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLI 199
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 171 RNKAQDDLFALQRRLGITVVIVTHDIEEALKLGDTIAVMDAGRLLQVASPAEILGKPAAGVVEQLVAGVD 240
Cdd:PRK10070 200 RTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFFRGVD 269
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
2-214 |
3.38e-53 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 173.08 E-value: 3.38e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 2 IEIERAGKRFGDIVAVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGVDTATVAPEQLRRGIGYAI 81
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 82 QGHGLFPHwSVARNIATVPRLLGWPADRidARVNELLDLFHLaPAEFADKLPHELSGGQQQRVGVARALAAEPAMLLMDE 161
Cdd:COG4619 81 QEPALWGG-TVRDNLPFPFQLRERKFDR--ERALELLERLGL-PPDILDKPVERLSGGERQRLALIRALLLQPDVLLLDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1861108599 162 PFGALDPIIRNKAQDDLFALQRRLGITVVIVTHDIEEALKLGDTIAVMDAGRL 214
Cdd:COG4619 157 PTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
1-223 |
4.53e-53 |
|
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: 174.02 E-value: 4.53e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 1 MIEIERAGKRFG-DIVAVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGVDTATVAPE---QLRRG 76
Cdd:TIGR02315 1 MLEVENLSKVYPnGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKklrKLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 77 IGYAIQGHGLFPHWSVARNI--------ATVPRLLGW--PADRIDARvnELLDLFHLApaEFADKLPHELSGGQQQRVGV 146
Cdd:TIGR02315 81 IGMIFQHYNLIERLTVLENVlhgrlgykPTWRSLLGRfsEEDKERAL--SALERVGLA--DKAYQRADQLSGGQQQRVAI 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1861108599 147 ARALAAEPAMLLMDEPFGALDPIIRNKAQDDLFALQRRLGITVVIVTHDIEEALKLGDTIAVMDAGRLLQVASPAEI 223
Cdd:TIGR02315 157 ARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSEL 233
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1-227 |
5.82e-53 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 173.74 E-value: 5.82e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 1 MIEIERAGKRFGDIVAVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDG--VDTATVAPEQLRRGIG 78
Cdd:PRK09493 1 MIEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGlkVNDPKVDERLIRQEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 79 YAIQGHGLFPHWSVARNIATVP-RLLGwpADRIDAR--VNELLDLFHLapAEFADKLPHELSGGQQQRVGVARALAAEPA 155
Cdd:PRK09493 81 MVFQQFYLFPHLTALENVMFGPlRVRG--ASKEEAEkqARELLAKVGL--AERAHHYPSELSGGQQQRVAIARALAVKPK 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1861108599 156 MLLMDEPFGALDPIIRNkaqdDLFALQRRL---GITVVIVTHDIEEALKLGDTIAVMDAGRLLQVASPAEILGKP 227
Cdd:PRK09493 157 LMLFDEPTSALDPELRH----EVLKVMQDLaeeGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNP 227
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1-228 |
1.06e-52 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 172.63 E-value: 1.06e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 1 MIEIERAGKRFGDIVAvdDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGVDTATVAPEQlrRGIGYA 80
Cdd:COG3840 1 MLRLDDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAE--RPVSML 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 81 IQGHGLFPHWSVARNIAtvprlLGW-------PADRidARVNELLDLFHLApaEFADKLPHELSGGQQQRVGVARALAAE 153
Cdd:COG3840 77 FQENNLFPHLTVAQNIG-----LGLrpglkltAEQR--AQVEQALERVGLA--GLLDRLPGQLSGGQRQRVALARCLVRK 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1861108599 154 PAMLLMDEPFGALDPIIRNKAQDDLFALQRRLGITVVIVTHDIEEALKLGDTIAVMDAGRLLQVASPAEILGKPA 228
Cdd:COG3840 148 RPILLLDEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEP 222
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
2-223 |
2.62e-52 |
|
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: 171.40 E-value: 2.62e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 2 IEIERAGKRFGDIVAVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGVDtATVAPEQLRRGIGYAI 81
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHD-VVREPREVRRRIGIVF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 82 QGHGLFPHWSVARNIATVPRLLGWPADRIDARVNELLDLFHLApaEFADKLPHELSGGQQQRVGVARALAAEPAMLLMDE 161
Cdd:cd03265 80 QDLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLL--EAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDE 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1861108599 162 PFGALDPIIRNKAQDDLFALQRRLGITVVIVTHDIEEALKLGDTIAVMDAGRLLQVASPAEI 223
Cdd:cd03265 158 PTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-224 |
3.07e-52 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 171.81 E-value: 3.07e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 1 MIEIERAGKRFGDIVAVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGVDtatvaPEQLRRGIGYA 80
Cdd:COG1121 6 AIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKP-----PRRARRRIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 81 IQGHGL---FPhwsvarniATV-----------PRLLGWPADRIDARVNELLDLFHLapAEFADKLPHELSGGQQQRVGV 146
Cdd:COG1121 81 PQRAEVdwdFP--------ITVrdvvlmgrygrRGLFRRPSRADREAVDEALERVGL--EDLADRPIGELSGGQQQRVLL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 147 ARALAAEPAMLLMDEPFGALDPiirnKAQDDLFALQRRL---GITVVIVTHDIEEALKLGDTIAVMDaGRLLQVASPAEI 223
Cdd:COG1121 151 ARALAQDPDLLLLDEPFAGVDA----ATEEALYELLRELrreGKTILVVTHDLGAVREYFDRVLLLN-RGLVAHGPPEEV 225
|
.
gi 1861108599 224 L 224
Cdd:COG1121 226 L 226
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2-227 |
4.64e-52 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 171.76 E-value: 4.64e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 2 IEIERAGKRFGDIVAVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLI-----APTSGTIRIDGVD--TATVAPEQLR 74
Cdd:COG1117 12 IEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNdlipgARVEGEILLDGEDiyDPDVDVVELR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 75 RGIGYAIQGHGLFPHwSVARNIATVPRLLGW-PADRIDARVNELL------DlfhlapaEFADKL---PHELSGGQQQRV 144
Cdd:COG1117 92 RRVGMVFQKPNPFPK-SIYDNVAYGLRLHGIkSKSELDEIVEESLrkaalwD-------EVKDRLkksALGLSGGQQQRL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 145 GVARALAAEPAMLLMDEPFGALDPIIRNKAQDDLFALQRRLgiTVVIVTHDIEEALKLGDTIAVMDAGRLLQVASPAEIL 224
Cdd:COG1117 164 CIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDY--TIVIVTHNMQQAARVSDYTAFFYLGELVEFGPTEQIF 241
|
...
gi 1861108599 225 GKP 227
Cdd:COG1117 242 TNP 244
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
1-228 |
9.64e-52 |
|
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: 174.13 E-value: 9.64e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 1 MIEIeRAGKRFGDIVAvdDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDG---VDTAT---VAPEqlR 74
Cdd:COG4148 2 MLEV-DFRLRRGGFTL--DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGevlQDSARgifLPPH--R 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 75 RGIGYAIQGHGLFPHWSVARNIATVPRLLGWPADRID-ARVNELLDLFHLApaefaDKLPHELSGGQQQRVGVARALAAE 153
Cdd:COG4148 77 RRIGYVFQEARLFPHLSVRGNLLYGRKRAPRAERRISfDEVVELLGIGHLL-----DRRPATLSGGERQRVAIGRALLSS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 154 PAMLLMDEPFGALD--------PIIRnkaqddlfALQRRLGITVVIVTHDIEEALKLGDTIAVMDAGRLLQVASPAEILG 225
Cdd:COG4148 152 PRLLLMDEPLAALDlarkaeilPYLE--------RLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLS 223
|
...
gi 1861108599 226 KPA 228
Cdd:COG4148 224 RPD 226
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
8-228 |
1.39e-51 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 172.61 E-value: 1.39e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 8 GKRFGDIVAVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGVDTATVAPEQL---RRGIG------ 78
Cdd:COG4608 25 GRTVGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELrplRRRMQmvfqdp 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 79 YAiqghGLFPHWSVARNIATVPRLLG-WPADRIDARVNELLDLFHLAPaEFADKLPHELSGGQQQRVGVARALAAEPAML 157
Cdd:COG4608 105 YA----SLNPRMTVGDIIAEPLRIHGlASKAERRERVAELLELVGLRP-EHADRYPHEFSGGQRQRIGIARALALNPKLI 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1861108599 158 LMDEPFGALDPIIRnkAQD-DLFA-LQRRLGITVVIVTHDieealkLG------DTIAVMDAGRLLQVASPAEILGKPA 228
Cdd:COG4608 180 VCDEPVSALDVSIQ--AQVlNLLEdLQDELGLTYLFISHD------LSvvrhisDRVAVMYLGKIVEIAPRDELYARPL 250
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-213 |
2.64e-51 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 171.06 E-value: 2.64e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 1 MIEIERAGKRFGDIVAVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGvdtATVAPEQLRRgIGYA 80
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDG---EPLDPEDRRR-IGYL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 81 IQGHGLFPHWSVARNIATVPRLLGWPADRIDARVNELLDLFHLapAEFADKLPHELSGGQQQRVGVARALAAEPAMLLMD 160
Cdd:COG4152 77 PEERGLYPKMKVGEQLVYLARLKGLSKAEAKRRADEWLERLGL--GDRANKKVEELSKGNQQKVQLIAALLHDPELLILD 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1861108599 161 EPFGALDPIIRNKAQDDLFALQRRlGITVVIVTHDIEEALKLGDTIAVMDAGR 213
Cdd:COG4152 155 EPFSGLDPVNVELLKDVIRELAAK-GTTVIFSSHQMELVEELCDRIVIINKGR 206
|
|
| 3a0107s01c2 |
TIGR00972 |
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein ... |
2-239 |
7.49e-51 |
|
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: 168.24 E-value: 7.49e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 2 IEIERAGKRFGDIVAVDDVSLTMQRGTITALVGASGSGKSTLLRMINRL-----IAPTSGTIRIDGVD--TATVAPEQLR 74
Cdd:TIGR00972 2 IEIENLNLFYGEKEALKNINLDIPKNQVTALIGPSGCGKSTLLRSLNRMndlvpGVRIEGKVLFDGQDiyDKKIDVVELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 75 RGIGYAIQGHGLFPHwSVARNIATVPRLLGW-PADRIDARVNELLDLFHLaPAEFADKL---PHELSGGQQQRVGVARAL 150
Cdd:TIGR00972 82 RRVGMVFQKPNPFPM-SIYDNIAYGPRLHGIkDKKELDEIVEESLKKAAL-WDEVKDRLhdsALGLSGGQQQRLCIARAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 151 AAEPAMLLMDEPFGALDPIIRNKAQDDLFALQRRLgiTVVIVTHDIEEALKLGDTIAVMDAGRLLQVASPAEILGKPAAG 230
Cdd:TIGR00972 160 AVEPEVLLLDEPTSALDPIATGKIEELIQELKKKY--TIVIVTHNMQQAARISDRTAFFYDGELVEYGPTEQIFTNPKEK 237
|
....*....
gi 1861108599 231 VVEQLVAGV 239
Cdd:TIGR00972 238 RTEDYISGR 246
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
9-238 |
3.42e-50 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 170.21 E-value: 3.42e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 9 KRFGDIVAVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGVDTATVAPEQlrRGIGYAIQGHGLFP 88
Cdd:PRK11000 11 KAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAE--RGVGMVFQSYALYP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 89 HWSVARNIATVPRLLGWPADRIDARVN---ELLDLFHLApaefaDKLPHELSGGQQQRVGVARALAAEPAMLLMDEPFGA 165
Cdd:PRK11000 89 HLSVAENMSFGLKLAGAKKEEINQRVNqvaEVLQLAHLL-----DRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSN 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1861108599 166 LDPIIRNKAQDDLFALQRRLGITVVIVTHDIEEALKLGDTIAVMDAGRLLQVASPAEILGKPAagvvEQLVAG 238
Cdd:PRK11000 164 LDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPA----NRFVAG 232
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
12-228 |
5.60e-49 |
|
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: 163.23 E-value: 5.60e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 12 GDIVAVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGVDTATVAPEQL-RRGIGYAIQGHGLFPHW 90
Cdd:COG0410 14 GGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIaRLGIGYVPEGRRIFPSL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 91 SVARNIATVPRLLGwPADRIDARVNELLDLFhlaP--AEFADKLPHELSGGQQQRVGVARALAAEPAMLLMDEPFGALDP 168
Cdd:COG0410 94 TVEENLLLGAYARR-DRAEVRADLERVYELF---PrlKERRRQRAGTLSGGEQQMLAIGRALMSRPKLLLLDEPSLGLAP 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1861108599 169 IIRnkaqDDLFALQRRL---GITVVIVTHDIEEALKLGDTIAVMDAGRLLQVASPAEILGKPA 228
Cdd:COG0410 170 LIV----EEIFEIIRRLnreGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLADPE 228
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
12-224 |
5.77e-49 |
|
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: 162.60 E-value: 5.77e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 12 GDIVAVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGVDTATVAPEQ-LRRGIGYAIQGHGLFPHW 90
Cdd:cd03224 11 GKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHErARAGIGYVPEGRRIFPEL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 91 SVARNIatvprLLGW---PADRIDARVNELLDLFhlaP--AEFADKLPHELSGGQQQRVGVARALAAEPAMLLMDEPFGA 165
Cdd:cd03224 91 TVEENL-----LLGAyarRRAKRKARLERVYELF---PrlKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEG 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1861108599 166 LDPIIRnkaqDDLFALQRRL---GITVVIVTHDIEEALKLGDTIAVMDAGRLLQVASPAEIL 224
Cdd:cd03224 163 LAPKIV----EEIFEAIRELrdeGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELL 220
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
3-215 |
6.06e-49 |
|
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: 161.06 E-value: 6.06e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 3 EIERAGKRFGDIVAVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGVDTATVAPEQLrrgigyaiq 82
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKEL--------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 83 ghglfphwsvARNIATVPRLLgwpadridarvnELLDLFHLapaefADKLPHELSGGQQQRVGVARALAAEPAMLLMDEP 162
Cdd:cd03214 72 ----------ARKIAYVPQAL------------ELLGLAHL-----ADRPFNELSGGERQRVLLARALAQEPPILLLDEP 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1861108599 163 FGALDPiirnKAQDDLFALQRRL----GITVVIVTHDIEEALKLGDTIAVMDAGRLL 215
Cdd:cd03214 125 TSHLDI----AHQIELLELLRRLarerGKTVVMVLHDLNLAARYADRVILLKDGRIV 177
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
2-223 |
1.13e-48 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 161.90 E-value: 1.13e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 2 IEIERAGKRFGDI--VAVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGVDTATvAPEQLRRGIGY 79
Cdd:cd03263 1 LQIRNLTKTYKKGtkPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT-DRKAARQSLGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 80 AIQGHGLFPHWSVARNIATVPRLLGWPADRIDARVNELLDLFHLAPaeFADKLPHELSGGQQQRVGVARALAAEPAMLLM 159
Cdd:cd03263 80 CPQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTD--KANKRARTLSGGMKRKLSLAIALIGGPSVLLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1861108599 160 DEPFGALDPIIRNKAQDDLFALQRRLgiTVVIVTHDIEEALKLGDTIAVMDAGRLLQVASPAEI 223
Cdd:cd03263 158 DEPTSGLDPASRRAIWDLILEVRKGR--SIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQEL 219
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
9-302 |
3.18e-48 |
|
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: 163.33 E-value: 3.18e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 9 KRFGDIVAVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGVDTaTVAPEQLRRGIGYAIQGHGLFP 88
Cdd:TIGR01188 1 KVYGDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDV-VREPRKVRRSIGIVPQYASVDE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 89 HWSVARNIATVPRLLGWPADRIDARVNELLDLFHLApaEFADKLPHELSGGQQQRVGVARALAAEPAMLLMDEPFGALDP 168
Cdd:TIGR01188 80 DLTGRENLEMMGRLYGLPKDEAEERAEELLELFELG--EAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 169 IIRNKAQDDLFALqRRLGITVVIVTHDIEEALKLGDTIAVMDAGRLLQVASPAEI---LGKPAAGVVEQLVAGVDRPLRL 245
Cdd:TIGR01188 158 RTRRAIWDYIRAL-KEEGVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPEELkrrLGKDTLESRPRDIQSLKVEVSM 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1861108599 246 LA--LTPIDAVAEPGHADGEPIA-----ATRTLRDAVSELLWRGVDVLPVgdgdghNTRRITLD 302
Cdd:TIGR01188 237 LIaeLGETGLGLLAVTVDSDRIKilvpdGDETVPEIVEAAIRNGIRIRSI------STERPSLD 294
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
2-216 |
6.20e-48 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 160.56 E-value: 6.20e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 2 IEIERAGKRFGDIVAVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDG------VDTATVAPEQLRR 75
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGnhfdfsKTPSDKAIRELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 76 GIGYAIQGHGLFPHWSVARNIATVP-RLLGWPADRIDARVNELLDLFHLApaEFADKLPHELSGGQQQRVGVARALAAEP 154
Cdd:PRK11124 83 NVGMVFQQYNLWPHLTVQQNLIEAPcRVLGLSKDQALARAEKLLERLRLK--PYADRFPLHLSGGQQQRVAIARALMMEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1861108599 155 AMLLMDEPFGALDPIIRNKAQDDLFALQrRLGITVVIVTHDIEEALKLGDTIAVMDAGRLLQ 216
Cdd:PRK11124 161 QVLLFDEPTAALDPEITAQIVSIIRELA-ETGITQVIVTHEVEVARKTASRVVYMENGHIVE 221
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
2-242 |
8.08e-48 |
|
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: 161.06 E-value: 8.08e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 2 IEIERAGKRF--GDIVAVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGVDTATvaPEQL---RRG 76
Cdd:TIGR04520 1 IEVENVSFSYpeSEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLD--EENLweiRKK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 77 IGYAIQ-------GHglfphwSVARNIATVPRLLGWPADRIDARVNELLDLFHLApaEFADKLPHELSGGQQQRVGVARA 149
Cdd:TIGR04520 79 VGMVFQnpdnqfvGA------TVEDDVAFGLENLGVPREEMRKRVDEALKLVGME--DFRDREPHLLSGGQKQRVAIAGV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 150 LAAEPAMLLMDEPFGALDPIIRNKAQDDLFALQRRLGITVVIVTHDIEEALkLGDTIAVMDAGRLLQVASPAEILGKpaa 229
Cdd:TIGR04520 151 LAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEAV-LADRVIVMNKGKIVAEGTPREIFSQ--- 226
|
250
....*....|....
gi 1861108599 230 gvVEQLVA-GVDRP 242
Cdd:TIGR04520 227 --VELLKEiGLDVP 238
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
16-228 |
9.41e-48 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 161.73 E-value: 9.41e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 16 AVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRI-DGVDTATVAPEQLRR-----GIGYAIQGHGLFPH 89
Cdd:PRK13634 22 ALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIgERVITAGKKNKKLKPlrkkvGIVFQFPEHQLFEE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 90 wSVARNIATVPRLLGWPADRIDARVNELLDLFHLaPAEFADKLPHELSGGQQQRVGVARALAAEPAMLLMDEPFGALDPI 169
Cdd:PRK13634 102 -TVEKDICFGPMNFGVSEEDAKQKAREMIELVGL-PEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPK 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1861108599 170 IRNKAQDDLFALQRRLGITVVIVTHDIEEALKLGDTIAVMDAGRLLQVASPAEILGKPA 228
Cdd:PRK13634 180 GRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADPD 238
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
2-216 |
1.27e-47 |
|
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: 158.90 E-value: 1.27e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 2 IEIERAGKRFGDIVAVDDVSLTMQRGtITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGVDtATVAPEQLRRGIGYAI 81
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQD-VLKQPQKLRRRIGYLP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 82 QGHGLFPHWSVARNIATVPRLLGWPADRIDARVNELLDLFHLapAEFADKLPHELSGGQQQRVGVARALAAEPAMLLMDE 161
Cdd:cd03264 79 QEFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNL--GDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1861108599 162 PFGALDPIIRNKAQDdlfaLQRRLG--ITVVIVTHDIEEALKLGDTIAVMDAGRLLQ 216
Cdd:cd03264 157 PTAGLDPEERIRFRN----LLSELGedRIVILSTHIVEDVESLCNQVAVLNKGKLVF 209
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
3-213 |
2.62e-47 |
|
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: 156.25 E-value: 2.62e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 3 EIERAGKRFGDIVAVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGVDTATVAPEQLRRGIGYAIQ 82
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 83 ghglfphwsvarniatvprllgwpadridarvnelldlfhlapaefadklpheLSGGQQQRVGVARALAAEPAMLLMDEP 162
Cdd:cd00267 81 -----------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEP 107
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1861108599 163 FGALDPIIRNKAQDDLFALQRRlGITVVIVTHDIEEALKLGDTIAVMDAGR 213
Cdd:cd00267 108 TSGLDPASRERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
15-223 |
3.88e-47 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 160.21 E-value: 3.88e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 15 VAVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGVDTA--TVAPEQLRRGIGYAIQ--GHGLFPHw 90
Cdd:PRK13637 21 KALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITdkKVKLSDIRKKVGLVFQypEYQLFEE- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 91 SVARNIATVPRLLGWPADRIDARVNELLDLFHLAPAEFADKLPHELSGGQQQRVGVARALAAEPAMLLMDEPFGALDPii 170
Cdd:PRK13637 100 TIEKDIAFGPINLGLSEEEIENRVKRAMNIVGLDYEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDP-- 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1861108599 171 rnKAQDDLFA----LQRRLGITVVIVTHDIEEALKLGDTIAVMDAGRLLQVASPAEI 223
Cdd:PRK13637 178 --KGRDEILNkikeLHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREV 232
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
12-228 |
1.61e-46 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 160.39 E-value: 1.61e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 12 GDIVAVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGVDTATVAPEQlrRGIGYAIQGHGLFPHWS 91
Cdd:PRK11650 15 GKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPAD--RDIAMVFQNYALYPHMS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 92 VARNIATVPRLLGWPADRIDARVNELLDLFHLAPaeFADKLPHELSGGQQQRVGVARALAAEPAMLLMDEPFGALDPIIR 171
Cdd:PRK11650 93 VRENMAYGLKIRGMPKAEIEERVAEAARILELEP--LLDRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDAKLR 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1861108599 172 NKAQDDLFALQRRLGITVVIVTHDIEEALKLGDTIAVMDAGRLLQVASPAEILGKPA 228
Cdd:PRK11650 171 VQMRLEIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGGVAEQIGTPVEVYEKPA 227
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-229 |
2.87e-46 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 156.34 E-value: 2.87e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 1 MIEIERAGKRFGDIVAVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGVDtATVAP--EQLRRGIG 78
Cdd:COG1137 3 TLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGED-ITHLPmhKRARLGIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 79 YAIQGHGLFPHWSVARNIATVPRLLGWPADRIDARVNELLDLFHLApaEFADKLPHELSGGQQQRVGVARALAAEPAMLL 158
Cdd:COG1137 82 YLPQEASIFRKLTVEDNILAVLELRKLSKKEREERLEELLEEFGIT--HLRKSKAYSLSGGERRRVEIARALATNPKFIL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1861108599 159 MDEPFGALDPIIRNKAQDDLFALQRRlGITVVIVTHDIEEALKLGDTIAVMDAGRLLQVASPAEILGKPAA 229
Cdd:COG1137 160 LDEPFAGVDPIAVADIQKIIRHLKER-GIGVLITDHNVRETLGICDRAYIISEGKVLAEGTPEEILNNPLV 229
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
1-213 |
2.94e-46 |
|
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: 155.48 E-value: 2.94e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 1 MIEIERAGKRF-GDIVAVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGVDTATVAPEQ---LRRG 76
Cdd:TIGR02673 1 MIEFHNVSKAYpGGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLRGRQlplLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 77 IGYAIQGHGLFPHWSVARNIATVPRLLGWPADRIDARVNELLDLFHLAPAefADKLPHELSGGQQQRVGVARALAAEPAM 156
Cdd:TIGR02673 81 IGVVFQDFRLLPDRTVYENVALPLEVRGKKEREIQRRVGAALRQVGLEHK--ADAFPEQLSGGEQQRVAIARAIVNSPPL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1861108599 157 LLMDEPFGALDPiiRNKAQD-DLFALQRRLGITVVIVTHDIEEALKLGDTIAVMDAGR 213
Cdd:TIGR02673 159 LLADEPTGNLDP--DLSERIlDLLKRLNKRGTTVIVATHDLSLVDRVAHRVIILDDGR 214
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
2-216 |
3.76e-46 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 155.94 E-value: 3.76e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 2 IEIERAGKRFGDIVAVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGVD---TATVAPEQ---LRR 75
Cdd:COG4161 3 IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQfdfSQKPSEKAirlLRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 76 GIGYAIQGHGLFPHWSVARNIATVP-RLLGWPADRIDARVNELLDLFHLApaEFADKLPHELSGGQQQRVGVARALAAEP 154
Cdd:COG4161 83 KVGMVFQQYNLWPHLTVMENLIEAPcKVLGLSKEQAREKAMKLLARLRLT--DKADRFPLHLSGGQQQRVAIARALMMEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1861108599 155 AMLLMDEPFGALDPIIRNKAQDDLFALQrRLGITVVIVTHDIEEALKLGDTIAVMDAGRLLQ 216
Cdd:COG4161 161 QVLLFDEPTAALDPEITAQVVEIIRELS-QTGITQVIVTHEVEFARKVASQVVYMEKGRIIE 221
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
2-226 |
4.23e-46 |
|
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: 165.39 E-value: 4.23e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 2 IEIERAGKRFGD--IVAVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGVDTATVAPEQLRRGIGY 79
Cdd:COG2274 474 IELENVSFRYPGdsPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGV 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 80 AIQGHGLFpHWSVARNIAtvprllGWPADRIDARVNELLDLFHLapAEFADKLPH-----------ELSGGQQQRVGVAR 148
Cdd:COG2274 554 VLQDVFLF-SGTIRENIT------LGDPDATDEEIIEAARLAGL--HDFIEALPMgydtvvgeggsNLSGGQRQRLAIAR 624
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1861108599 149 ALAAEPAMLLMDEPFGALDPIIRNKAQDDLFALQRrlGITVVIVTHDiEEALKLGDTIAVMDAGRLLQVASPAEILGK 226
Cdd:COG2274 625 ALLRNPRILILDEATSALDAETEAIILENLRRLLK--GRTVIIIAHR-LSTIRLADRIIVLDKGRIVEDGTHEELLAR 699
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
17-163 |
6.84e-46 |
|
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: 152.42 E-value: 6.84e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 17 VDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGVDTATVAPEQLRRGIGYAIQGHGLFPHWSVARNI 96
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1861108599 97 ATVPRLLGWPADRIDARVNELLDLF--HLAPAEFADKLPHELSGGQQQRVGVARALAAEPAMLLMDEPF 163
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEALEKLglGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
2-213 |
4.68e-45 |
|
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: 152.05 E-value: 4.68e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 2 IEIERAGKRFGDIVAVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDG--VDTATvapeqlRRGIGY 79
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGkpLDIAA------RNRIGY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 80 AIQGHGLFPHWSVARNIATVPRLLGWPADRIDARVNELLDLFHLapAEFADKLPHELSGGQQQRVGVARALAAEPAMLLM 159
Cdd:cd03269 75 LPEERGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLEL--SEYANKRVEELSKGNQQKVQFIAAVIHDPELLIL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1861108599 160 DEPFGALDPIIRNKAQDDLFALQRRlGITVVIVTHDIEEALKLGDTIAVMDAGR 213
Cdd:cd03269 153 DEPFSGLDPVNVELLKDVIRELARA-GKTVILSTHQMELVEELCDRVLLLNKGR 205
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
1-222 |
4.91e-45 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 152.25 E-value: 4.91e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 1 MIEIERAGKRFGDIVAVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAP---TSGTIRIDGVDTATVAPEQlrRGI 77
Cdd:COG4136 1 MLSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLTALPAEQ--RRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 78 GYAIQGHGLFPHWSVARNIA-TVPRLLGWPADRidARVNELLDlfHLAPAEFADKLPHELSGGQQQRVGVARALAAEPAM 156
Cdd:COG4136 79 GILFQDDLLFPHLSVGENLAfALPPTIGRAQRR--ARVEQALE--EAGLAGFADRDPATLSGGQRARVALLRALLAEPRA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1861108599 157 LLMDEPFGALDPIIRNKAQDDLFALQRRLGITVVIVTHDIEEALklgdtiavmDAGRLLQVASPAE 222
Cdd:COG4136 155 LLLDEPFSKLDAALRAQFREFVFEQIRQRGIPALLVTHDEEDAP---------AAGRVLDLGNWQH 211
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
16-213 |
1.02e-44 |
|
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: 149.84 E-value: 1.02e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 16 AVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGVDTATVAPEQLRRGIGYAIQGHGLFpHWSVARN 95
Cdd:cd03228 17 VLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAYVPQDPFLF-SGTIREN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 96 IatvprllgwpadridarvnelldlfhlapaefadklpheLSGGQQQRVGVARALAAEPAMLLMDEPFGALDPIIRNKAQ 175
Cdd:cd03228 96 I---------------------------------------LSGGQRQRIAIARALLRDPPILILDEATSALDPETEALIL 136
|
170 180 190
....*....|....*....|....*....|....*...
gi 1861108599 176 DDLFALQRrlGITVVIVTHDIeEALKLGDTIAVMDAGR 213
Cdd:cd03228 137 EALRALAK--GKTVIVIAHRL-STIRDADRIIVLDDGR 171
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
2-215 |
1.76e-44 |
|
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: 150.83 E-value: 1.76e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 2 IEIERAGKRFGDIVAVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGVDTaTVAPEQLRRgIGYAI 81
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSY-QKNIEALRR-IGALI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 82 QGHGLFPHWSVARNIATVPRLLGWPadriDARVNELLDLFHLapAEFADKLPHELSGGQQQRVGVARALAAEPAMLLMDE 161
Cdd:cd03268 79 EAPGFYPNLTARENLRLLARLLGIR----KKRIDEVLDVVGL--KDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDE 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1861108599 162 PFGALDPI----IRnkaqdDLFALQRRLGITVVIVTHDIEEALKLGDTIAVMDAGRLL 215
Cdd:cd03268 153 PTNGLDPDgikeLR-----ELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKLI 205
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1-224 |
2.61e-44 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 151.39 E-value: 2.61e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 1 MIEIERAGKRFGDIVAVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGVDTATVAPEQLrrgigya 80
Cdd:COG4604 1 MIEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSREL------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 81 iqghglfphwsvARNIA------------TVPRLLG---WP--------ADRidARVNELLDLFHLAPaeFADKLPHELS 137
Cdd:COG4604 74 ------------AKRLAilrqenhinsrlTVRELVAfgrFPyskgrltaEDR--EIIDEAIAYLDLED--LADRYLDELS 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 138 GGQQQRVGVARALAAEPAMLLMDEPFGALDPiirnKAQDDLFALQRRL----GITVVIVTHDIEEALKLGDTIAVMDAGR 213
Cdd:COG4604 138 GGQRQRAFIAMVLAQDTDYVLLDEPLNNLDM----KHSVQMMKLLRRLadelGKTVVIVLHDINFASCYADHIVAMKDGR 213
|
250
....*....|.
gi 1861108599 214 LLQVASPAEIL 224
Cdd:COG4604 214 VVAQGTPEEII 224
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
19-214 |
2.71e-44 |
|
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: 150.34 E-value: 2.71e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 19 DVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGVDTATVAPEqlRRGIGYAIQGHGLFPHWSVARNI-- 96
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPA--DRPVSMLFQENNLFAHLTVEQNVgl 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 97 ATVPRLLGWPADRidARVNELLDLFHLApaEFADKLPHELSGGQQQRVGVARALAAEPAMLLMDEPFGALDPIIRNKAQD 176
Cdd:cd03298 94 GLSPGLKLTAEDR--QAIEVALARVGLA--GLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLD 169
|
170 180 190
....*....|....*....|....*....|....*...
gi 1861108599 177 DLFALQRRLGITVVIVTHDIEEALKLGDTIAVMDAGRL 214
Cdd:cd03298 170 LVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRI 207
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
16-223 |
2.78e-44 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 152.48 E-value: 2.78e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 16 AVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGV--DTATVApeQLRRGIGYAIQG-HGLFPHWSV 92
Cdd:PRK13635 22 ALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMvlSEETVW--DVRRQVGMVFQNpDNQFVGATV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 93 ARNIATVPRLLGWPADRIDARVNELLDLFHLApaEFADKLPHELSGGQQQRVGVARALAAEPAMLLMDEPFGALDPIIRN 172
Cdd:PRK13635 100 QDDVAFGLENIGVPREEMVERVDQALRQVGME--DFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRR 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1861108599 173 KAQDDLFALQRRLGITVVIVTHDIEEALKlGDTIAVMDAGRLLQVASPAEI 223
Cdd:PRK13635 178 EVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEI 227
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
2-197 |
3.68e-44 |
|
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: 149.87 E-value: 3.68e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 2 IEIERAGKRF-GDIVAVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGVDTATV---APEQLRRGI 77
Cdd:cd03292 1 IEFINVTKTYpNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLrgrAIPYLRRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 78 GYAIQGHGLFPHWSVARNIATVPRLLGWPADRIDARVNELLDLFHLAPAEfaDKLPHELSGGQQQRVGVARALAAEPAML 157
Cdd:cd03292 81 GVVFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKH--RALPAELSGGEQQRVAIARAIVNSPTIL 158
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1861108599 158 LMDEPFGALDPIIRNKAQdDLFALQRRLGITVVIVTHDIE 197
Cdd:cd03292 159 IADEPTGNLDPDTTWEIM-NLLKKINKAGTTVVVATHAKE 197
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
10-210 |
7.64e-44 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 149.22 E-value: 7.64e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 10 RFGDIVAVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGVDtatvaPEQLRRGIGYAIQGH----- 84
Cdd:cd03235 8 SYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKP-----LEKERKRIGYVPQRRsidrd 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 85 -----------GLFPHWsvarniatvpRLLGWPADRIDARVNELLDLFHLApaEFADKLPHELSGGQQQRVGVARALAAE 153
Cdd:cd03235 83 fpisvrdvvlmGLYGHK----------GLFRRLSKADKAKVDEALERVGLS--ELADRQIGELSGGQQQRVLLARALVQD 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 154 PAMLLMDEPFGALDPiirnKAQDDLFAL---QRRLGITVVIVTHDIEEALKLGDTIAVMD 210
Cdd:cd03235 151 PDLLLLDEPFAGVDP----KTQEDIYELlreLRREGMTILVVTHDLGLVLEYFDRVLLLN 206
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
9-229 |
2.25e-43 |
|
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: 148.46 E-value: 2.25e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 9 KRFGDIVAVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGVDTATVAP-EQLRRGIGYAIQGHGLF 87
Cdd:cd03218 8 KRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMhKRARLGIGYLPQEASIF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 88 PHWSVARNIATVPRLLGWPADRIDARVNELLDLFHLAPaeFADKLPHELSGGQQQRVGVARALAAEPAMLLMDEPFGALD 167
Cdd:cd03218 88 RKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITH--LRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVD 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1861108599 168 PIirnkAQDDLFALQRRL---GITVVIVTHDIEEALKLGDTIAVMDAGRLLQVASPAEILGKPAA 229
Cdd:cd03218 166 PI----AVQDIQKIIKILkdrGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANELV 226
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
17-242 |
4.12e-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: 148.00 E-value: 4.12e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 17 VDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGVDTATVAPEQLrrgigYAIQGHGLFPHWSVARNI 96
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRM-----VVFQNYSLLPWLTVRENI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 97 A-TVPRLL-GWPADRIDARVNELLDLFHLAPAefADKLPHELSGGQQQRVGVARALAAEPAMLLMDEPFGALDPIIRNKA 174
Cdd:TIGR01184 76 AlAVDRVLpDLSKSERRAIVEEHIALVGLTEA--ADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1861108599 175 QDDLFALQRRLGITVVIVTHDIEEALKLGDTIAVMDAGrllqvaspaeilgkPAAGVVEQLVAGVDRP 242
Cdd:TIGR01184 154 QEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNG--------------PAANIGQILEVPFPRP 207
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1-215 |
4.52e-43 |
|
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: 147.51 E-value: 4.52e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 1 MIEIERAGKRFGD----IVAVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGVDTATvAPEQLRRG 76
Cdd:cd03266 1 MITADALTKRFRDvkktVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVK-EPAEARRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 77 IGYAIQGHGLFPHWSVARNIATVPRLLGWPADRIDARVNELLDLFHLapAEFADKLPHELSGGQQQRVGVARALAAEPAM 156
Cdd:cd03266 80 LGFVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGM--EELLDRRVGGFSTGMRQKVAIARALVHDPPV 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1861108599 157 LLMDEPFGALDpIIRNKAQDDLFALQRRLGITVVIVTHDIEEALKLGDTIAVMDAGRLL 215
Cdd:cd03266 158 LLLDEPTTGLD-VMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVV 215
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-227 |
6.05e-43 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 147.97 E-value: 6.05e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 1 MIEIERAGKRFGDIVAVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGVDTATVAP--------EQ 72
Cdd:PRK11264 3 AIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTARSlsqqkgliRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 73 LRRGIGYAIQGHGLFPHWSVARNIATVPRLL-GWPADRIDARVNELLDLFHLAPAEfaDKLPHELSGGQQQRVGVARALA 151
Cdd:PRK11264 83 LRQHVGFVFQNFNLFPHRTVLENIIEGPVIVkGEPKEEATARARELLAKVGLAGKE--TSYPRRLSGGQQQRVAIARALA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 152 AEPAMLLMDEPFGALDP--------IIRNKAQddlfalQRRlgiTVVIVTHDIEEALKLGDTIAVMDAGRLLQVASPAEI 223
Cdd:PRK11264 161 MRPEVILFDEPTSALDPelvgevlnTIRQLAQ------EKR---TMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKAL 231
|
....
gi 1861108599 224 LGKP 227
Cdd:PRK11264 232 FADP 235
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
6-255 |
6.95e-43 |
|
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: 150.65 E-value: 6.95e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 6 RAGKRFGDIVAvdDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGVDTATVA------PEqlRRGIGY 79
Cdd:TIGR02142 4 RFSKRLGDFSL--DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRkgiflpPE--KRRIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 80 AIQGHGLFPHWSVARNIA-TVPRLLGWPADRIDARVNELLDLFHLApaefaDKLPHELSGGQQQRVGVARALAAEPAMLL 158
Cdd:TIGR02142 80 VFQEARLFPHLSVRGNLRyGMKRARPSERRISFERVIELLGIGHLL-----GRLPGRLSGGEKQRVAIGRALLSSPRLLL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 159 MDEPFGALDPIIRNKAQDDLFALQRRLGITVVIVTHDIEEALKLGDTIAVMDAGRLLQVASPAEILGKPAAGVVEQLVAG 238
Cdd:TIGR02142 155 MDEPLAALDDPRKYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPDLPWLAREDQG 234
|
250
....*....|....*..
gi 1861108599 239 VDRPLRLLALTPIDAVA 255
Cdd:TIGR02142 235 SLIEGVVAEHDQHYGLT 251
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1-216 |
1.20e-42 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 147.54 E-value: 1.20e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 1 MIEIERAGKRFGDIVAVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGVDTATVAPEQlrrgiGYA 80
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAER-----GVV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 81 IQGHGLFPHWSVARNIATVPRLLGWPADRIDARVNELLDLFHLAPAEfaDKLPHELSGGQQQRVGVARALAAEPAMLLMD 160
Cdd:PRK11248 76 FQNEGLLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAE--KRYIWQLSGGQRQRVGIARALAANPQLLLLD 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1861108599 161 EPFGALDPIIRNKAQDDLFALQRRLGITVVIVTHDIEEALKLGDTIAVM--DAGRLLQ 216
Cdd:PRK11248 154 EPFGALDAFTREQMQTLLLKLWQETGKQVLLITHDIEEAVFMATELVLLspGPGRVVE 211
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-195 |
1.48e-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: 145.70 E-value: 1.48e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 1 MIEIERAGKRFGDIVAVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGVDTATvAPEQLRRGIGYA 80
Cdd:COG4133 2 MLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRD-AREDYRRRLAYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 81 IQGHGLFPHWSVARNIATVPRLLGWPADRidARVNELLDLFHLAPaeFADKLPHELSGGQQQRVGVARALAAEPAMLLMD 160
Cdd:COG4133 81 GHADGLKPELTVRENLRFWAALYGLRADR--EAIDEALEAVGLAG--LADLPVRQLSAGQKRRVALARLLLSPAPLWLLD 156
|
170 180 190
....*....|....*....|....*....|....*...
gi 1861108599 161 EPFGALDPiirnKAQD---DLFALQRRLGITVVIVTHD 195
Cdd:COG4133 157 EPFTALDA----AGVAllaELIAAHLARGGAVLLTTHQ 190
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
1-238 |
1.76e-42 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 146.87 E-value: 1.76e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 1 MIEIERAGKRFGDIVAVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDG---------------VDT 65
Cdd:COG4598 8 ALEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGeeirlkpdrdgelvpADR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 66 ATVapEQLRRGIGYAIQGHGLFPHWSVARNIATVP-RLLGWPADRIDARVNELLDLFHLApaEFADKLPHELSGGQQQRV 144
Cdd:COG4598 88 RQL--QRIRTRLGMVFQSFNLWSHMTVLENVIEAPvHVLGRPKAEAIERAEALLAKVGLA--DKRDAYPAHLSGGQQQRA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 145 GVARALAAEPAMLLMDEPFGALDP--------IIRNKAQDdlfalqrrlGITVVIVTHDIEEALKLGDTIAVMDAGRLLQ 216
Cdd:COG4598 164 AIARALAMEPEVMLFDEPTSALDPelvgevlkVMRDLAEE---------GRTMLVVTHEMGFARDVSSHVVFLHQGRIEE 234
|
250 260
....*....|....*....|..
gi 1861108599 217 VASPAEILGKPAAGVVEQLVAG 238
Cdd:COG4598 235 QGPPAEVFGNPKSERLRQFLSS 256
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
9-229 |
9.58e-42 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 144.72 E-value: 9.58e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 9 KRFGDIVAVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGVDTaTVAP--EQLRRGIGYAIQGHGL 86
Cdd:TIGR04406 9 KSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDI-THLPmhERARLGIGYLPQEASI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 87 FPHWSVARNIATVPRLLG-WPADRIDARVNELLDLFHLApaEFADKLPHELSGGQQQRVGVARALAAEPAMLLMDEPFGA 165
Cdd:TIGR04406 88 FRKLTVEENIMAVLEIRKdLDRAEREERLEALLEEFQIS--HLRDNKAMSLSGGERRRVEIARALATNPKFILLDEPFAG 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1861108599 166 LDPIIRNKAQDDLFALQRRlGITVVIVTHDIEEALKLGDTIAVMDAGRLLQVASPAEILGKPAA 229
Cdd:TIGR04406 166 VDPIAVGDIKKIIKHLKER-GIGVLITDHNVRETLDICDRAYIISDGKVLAEGTPAEIVANEKV 228
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
12-224 |
1.34e-41 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 151.47 E-value: 1.34e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 12 GDIVAVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGVDTATVAPEQLRRGIGYAIQGHGLFpHWS 91
Cdd:COG1132 351 GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESLRRQIGVVPQDTFLF-SGT 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 92 VARNIAtvprlLGWPaDRIDARVNELLDLFHLapAEFADKLPH-----------ELSGGQQQRVGVARALAAEPAMLLMD 160
Cdd:COG1132 430 IRENIR-----YGRP-DATDEEVEEAAKAAQA--HEFIEALPDgydtvvgergvNLSGGQRQRIAIARALLKDPPILILD 501
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1861108599 161 EPFGALDPIIRNKAQDDLFALQRrlGITVVIVTHD---IEEAlklgDTIAVMDAGRLLQVASPAEIL 224
Cdd:COG1132 502 EATSALDTETEALIQEALERLMK--GRTTIVIAHRlstIRNA----DRILVLDDGRIVEQGTHEELL 562
|
|
| ABC_ATP_SaoA |
NF040729 |
ABC transporter ATP-binding protein SaoA; SaoA is the ATP-binding subunit of an ABC ... |
17-216 |
1.82e-41 |
|
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: 144.11 E-value: 1.82e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 17 VDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGVDTATVAPEQlrrgiGYAIQGHGLFPHWSVARNI 96
Cdd:NF040729 21 LKDISFDVEEGEFVSLLGPSGCGKTTLLTIIAGFQNATSGEILVNGNEVTKPGPDR-----GFVFQNYALFPWMTVKENI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 97 ATVPRLLGWPADRIDARVNELLDLFHLAPAEfaDKLPHELSGGQQQRVGVARALAAEPAMLLMDEPFGALDPIIRNKAQD 176
Cdd:NF040729 96 EYPMKQQKMPKQEREKRLNELLEMAQLTGKE--NLYPHQISGGMKQRTAVIRALACKPEVLLMDEPLGAVDFQMRQILQE 173
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1861108599 177 DLFALQRRLGITVVIVTHDIEEALKLGDTIAVM--DAGRLLQ 216
Cdd:NF040729 174 ELESIWLKDKTTVLMVTHDVDEAVYLSDRVIVMsrDKGKILE 215
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
12-226 |
5.97e-40 |
|
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: 146.83 E-value: 5.97e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 12 GDIVAVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGVDTATVAPEQLRRGIGYAIQgHGLFPHWS 91
Cdd:COG4988 348 GGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQ-NPYLFAGT 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 92 VARNIatvprLLGWPaDRIDARVNELLDLFHLapAEFADKLPHE-----------LSGGQQQRVGVARALAAEPAMLLMD 160
Cdd:COG4988 427 IRENL-----RLGRP-DASDEELEAALEAAGL--DEFVAALPDGldtplgeggrgLSGGQAQRLALARALLRDAPLLLLD 498
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1861108599 161 EPFGALDPiirnKAQDDLFALQRRL--GITVVIVTHDIeEALKLGDTIAVMDAGRLLQVASPAEILGK 226
Cdd:COG4988 499 EPTAHLDA----ETEAEILQALRRLakGRTVILITHRL-ALLAQADRILVLDDGRIVEQGTHEELLAK 561
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-222 |
1.90e-39 |
|
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: 138.34 E-value: 1.90e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 1 MIEIERAGKRFGD----IVAVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGVDTATVAPEQL--- 73
Cdd:COG4181 8 IIELRGLTKTVGTgageLTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDARarl 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 74 -RRGIGYAIQGHGLFPHWSVARNIATVPRLLGWPADRidARVNELLDLFHLapAEFADKLPHELSGGQQQRVGVARALAA 152
Cdd:COG4181 88 rARHVGFVFQSFQLLPTLTALENVMLPLELAGRRDAR--ARARALLERVGL--GHRLDHYPAQLSGGEQQRVALARAFAT 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 153 EPAMLLMDEPFGALDPIIRNKAQDDLFALQRRLGITVVIVTHDIEEALKLGDTIAvMDAGRLLQVASPAE 222
Cdd:COG4181 164 EPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAARCDRVLR-LRAGRLVEDTAATA 232
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
2-214 |
1.90e-39 |
|
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: 136.02 E-value: 1.90e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 2 IEIERAGKRFGDIVAVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGVDTATVAPEQLRRgigyai 81
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDARR------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 82 qgHGlfphwsvarnIATVprllgwpadridarvnelldlfhlapaefadklpHELSGGQQQRVGVARALAAEPAMLLMDE 161
Cdd:cd03216 75 --AG----------IAMV----------------------------------YQLSVGERQMVEIARALARNARLLILDE 108
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1861108599 162 PFGALDPiirnKAQDDLFALQRRL---GITVVIVTHDIEEALKLGDTIAVMDAGRL 214
Cdd:cd03216 109 PTAALTP----AEVERLFKVIRRLraqGVAVIFISHRLDEVFEIADRVTVLRDGRV 160
|
|
| ABC_ATP_DarD |
NF038007 |
darobactin export ABC transporter ATP-binding protein; |
1-214 |
3.00e-39 |
|
darobactin export ABC transporter ATP-binding protein;
Pssm-ID: 411600 [Multi-domain] Cd Length: 218 Bit Score: 137.54 E-value: 3.00e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 1 MIEIERAGK----RFGDIVAVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGVDTATVAPEQ---L 73
Cdd:NF038007 1 MLNMQNAEKcyitKTIKTKVLNHLNFSVEKGDFVSIMGPSGSGKSTLLNIIGMFDSLDSGSLTLAGKEVTNLSYSQkiiL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 74 RRG-IGYAIQGHGLFPHWSVARNIATVPRLLGWP-ADRIdARVNELLDLFHLAPAefADKLPHELSGGQQQRVGVARALA 151
Cdd:NF038007 81 RRElIGYIFQSFNLIPHLSIFDNVALPLKYRGVAkKERI-ERVNQVLNLFGIDNR--RNHKPMQLSGGQQQRVAIARAMV 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1861108599 152 AEPAMLLMDEPFGALDpiiRNKAQDDLFALQR--RLGITVVIVTHDiEEALKLGDTIAVMDAGRL 214
Cdd:NF038007 158 SNPALLLADEPTGNLD---SKNARAVLQQLKYinQKGTTIIMVTHS-DEASTYGNRIINMKDGKL 218
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
4-197 |
7.38e-39 |
|
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: 135.82 E-value: 7.38e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 4 IERAGKRFGDIVAVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGVDTATVAPEQ----LRRGIGY 79
Cdd:TIGR03608 1 LKNISKKFGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLNSKKaskfRREKLGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 80 AIQGHGLFPHWSVARNIatvprLLGWPADRIDARVNELLDLFHLAPAEFADKL---PHELSGGQQQRVGVARALAAEPAM 156
Cdd:TIGR03608 81 LFQNFALIENETVEENL-----DLGLKYKKLSKKEKREKKKEALEKVGLNLKLkqkIYELSGGEQQRVALARAILKPPPL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1861108599 157 LLMDEPFGALDPIIRNKAQDDLFALQRRlGITVVIVTHDIE 197
Cdd:TIGR03608 156 ILADEPTGSLDPKNRDEVLDLLLELNDE-GKTIIIVTHDPE 195
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
15-223 |
1.23e-38 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 137.53 E-value: 1.23e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 15 VAVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGVDTATVAPE-QLRRGIGYAIQGhglfPHWS-- 91
Cdd:PRK13633 24 LALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLwDIRNKAGMVFQN----PDNQiv 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 92 ---VARNIATVPRLLGWPADRIDARVNELLDLFHLApaEFADKLPHELSGGQQQRVGVARALAAEPAMLLMDEPFGALDP 168
Cdd:PRK13633 100 atiVEEDVAFGPENLGIPPEEIRERVDESLKKVGMY--EYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDP 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1861108599 169 IIRNKAQDDLFALQRRLGITVVIVTHDIEEALKlGDTIAVMDAGRLLQVASPAEI 223
Cdd:PRK13633 178 SGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEI 231
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-265 |
1.66e-38 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 142.08 E-value: 1.66e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 1 MIEIERAGKRFGDIVAVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGVDTATVAPEQ-LRRGIGY 79
Cdd:COG1129 4 LLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDaQAAGIAI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 80 AIQGHGLFPHWSVARNIA-----TVPRLLGWPADRIDARvnELLDLFHL-----APAEfadklphELSGGQQQRVGVARA 149
Cdd:COG1129 84 IHQELNLVPNLSVAENIFlgrepRRGGLIDWRAMRRRAR--ELLARLGLdidpdTPVG-------DLSVAQQQLVEIARA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 150 LAAEPAMLLMDEPFGALDPiirnKAQDDLFALQRRL---GITVVIVTHDIEEALKLGDTIAVMDAGRLlqVASpaeilgK 226
Cdd:COG1129 155 LSRDARVLILDEPTASLTE----REVERLFRIIRRLkaqGVAIIYISHRLDEVFEIADRVTVLRDGRL--VGT------G 222
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1861108599 227 PAAGV-VEQLVAG-VDRPLRllaltpiDAVAEPGHADGEPI 265
Cdd:COG1129 223 PVAELtEDELVRLmVGRELE-------DLFPKRAAAPGEVV 256
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
1-214 |
2.51e-38 |
|
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ABC transporter family (pfam00005). LolD is involved in localization of lipoproteins in some bacteria. It works with a transmembrane protein LolC, which in some species is a paralogous pair LolC and LolE. Depending on whether the residue immediately following the new, modified N-terminal Cys residue, the nascent lipoprotein may be carried further by LolA and LolB to the outer membrane, or remain at the inner membrane. The top scoring proteins excluded by this model include homologs from the archaeal genus Methanosarcina. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 131266 [Multi-domain] Cd Length: 221 Bit Score: 135.17 E-value: 2.51e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 1 MIEIERAGKRFGD----IVAVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGVDTATVAPEQ---L 73
Cdd:TIGR02211 1 LLKCENLGKRYQEgkldTRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSSNErakL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 74 R-RGIGYAIQGHGLFPHWSVARNIAtVPRLLGwPADRIDA--RVNELLDLFHLApaEFADKLPHELSGGQQQRVGVARAL 150
Cdd:TIGR02211 81 RnKKLGFIYQFHHLLPDFTALENVA-MPLLIG-KKSVKEAkeRAYEMLEKVGLE--HRINHRPSELSGGERQRVAIARAL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1861108599 151 AAEPAMLLMDEPFGALDPIIRNKAQDDLFALQRRLGITVVIVTHDIEEALKLgDTIAVMDAGRL 214
Cdd:TIGR02211 157 VNQPSLVLADEPTGNLDNNNAKIIFDLMLELNRELNTSFLVVTHDLELAKKL-DRVLEMKDGQL 219
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-238 |
2.73e-38 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 135.81 E-value: 2.73e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 2 IEIERAGKRFGDIVAVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLI-----APTSGTIRIDGVDTATVAPEQLRRG 76
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIelypeARVSGEVYLDGQDIFKMDVIELRRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 77 IGYAIQGHGLFPHWSVARNIATVPRL--LGWPADRIDARVNELLDLFHLApAEFADKL---PHELSGGQQQRVGVARALA 151
Cdd:PRK14247 84 VQMVFQIPNPIPNLSIFENVALGLKLnrLVKSKKELQERVRWALEKAQLW-DEVKDRLdapAGKLSGGQQQRLCIARALA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 152 AEPAMLLMDEPFGALDPIirNKAQDDLFALQRRLGITVVIVTHDIEEALKLGDTIAVMDAGRLLQVASPAEILGKPAAGV 231
Cdd:PRK14247 163 FQPEVLLADEPTANLDPE--NTAKIESLFLELKKDMTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTNPRHEL 240
|
....*..
gi 1861108599 232 VEQLVAG 238
Cdd:PRK14247 241 TEKYVTG 247
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
11-214 |
2.87e-38 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 135.35 E-value: 2.87e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 11 FGDIVAVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGVDTATVAPEQL-RRGIGYAIQGHGLFPH 89
Cdd:TIGR03410 10 YGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERaRAGIAYVPQGREIFPR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 90 WSVARNIATVPRLLGWPADRIDArvnELLDLFhlaPA--EFADKLPHELSGGQQQRVGVARALAAEPAMLLMDEPFGALD 167
Cdd:TIGR03410 90 LTVEENLLTGLAALPRRSRKIPD---EIYELF---PVlkEMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDEPTEGIQ 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1861108599 168 PIIRNKAQDDLFALQRRLGITVVIVTHDIEEALKLGDTIAVMDAGRL 214
Cdd:TIGR03410 164 PSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRV 210
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
8-227 |
1.01e-37 |
|
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: 140.20 E-value: 1.01e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 8 GKRFGDIVAVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIaPTSGTIRIDGVDTATVAPEQ---LRRGIG------ 78
Cdd:COG4172 293 RRTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLI-PSEGEIRFDGQDLDGLSRRAlrpLRRRMQvvfqdp 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 79 YAiqghGLFPHWSVARNIATVPRLLGWPADR--IDARVNELLDLFHLaPAEFADKLPHELSGGQQQRVGVARALAAEPAM 156
Cdd:COG4172 372 FG----SLSPRMTVGQIIAEGLRVHGPGLSAaeRRARVAEALEEVGL-DPAARHRYPHEFSGGQRQRIAIARALILEPKL 446
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1861108599 157 LLMDEPFGALDPIIRnkAQ--DDLFALQRRLGITVVIVTHDieeaLK----LGDTIAVMDAGRLLQVASPAEILGKP 227
Cdd:COG4172 447 LVLDEPTSALDVSVQ--AQilDLLRDLQREHGLAYLFISHD----LAvvraLAHRVMVMKDGKVVEQGPTEQVFDAP 517
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
12-228 |
1.08e-37 |
|
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: 140.20 E-value: 1.08e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 12 GDIVAVDDVSLTMQRGTITALVGASGSGKS----TLLRMINRLIAPTSGTIRIDGVDTATVAPEQLR--RG--IGYAIQ- 82
Cdd:COG4172 21 GTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERELRriRGnrIAMIFQe 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 83 -GHGLFPHWSVARNIATVPRL-LGWPADRIDARVNELLDLFHLAPAEF-ADKLPHELSGGQQQRVGVARALAAEPAMLLM 159
Cdd:COG4172 101 pMTSLNPLHTIGKQIAEVLRLhRGLSGAAARARALELLERVGIPDPERrLDAYPHQLSGGQRQRVMIAMALANEPDLLIA 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1861108599 160 DEPFGALDPIIRnkAQ--DDLFALQRRLGITVVIVTHDIEEALKLGDTIAVMDAGRLLQVASPAEILGKPA 228
Cdd:COG4172 181 DEPTTALDVTVQ--AQilDLLKDLQRELGMALLLITHDLGVVRRFADRVAVMRQGEIVEQGPTAELFAAPQ 249
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
21-217 |
2.07e-37 |
|
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: 132.68 E-value: 2.07e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 21 SLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGVDTATVAPEQlrRGIGYAIQGHGLFPHWSVARNIAtvp 100
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPYQ--RPVSMLFQENNLFAHLTVRQNIG--- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 101 rlLGW-PADRIDARVNELLDLF--HLAPAEFADKLPHELSGGQQQRVGVARALAAEPAMLLMDEPFGALDPIIRNKAQDD 177
Cdd:TIGR01277 93 --LGLhPGLKLNAEQQEKVVDAaqQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLAL 170
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1861108599 178 LFALQRRLGITVVIVTHDIEEALKLGDTIAVMDAGRLLQV 217
Cdd:TIGR01277 171 VKQLCSERQRTLLMVTHHLSDARAIASQIAVVSQGKIKVV 210
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-239 |
2.66e-37 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 133.43 E-value: 2.66e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 2 IEIERAGKRFGDIVAVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLI-----APTSGTIRIDGVD--TATVAPEQLR 74
Cdd:PRK14267 5 IETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLelneeARVEGEVRLFGRNiySPDVDPIEVR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 75 RGIGYAIQGHGLFPHWSVARNIATVPRL--LGWPADRIDARVNELLDLFHLAPaEFADKL---PHELSGGQQQRVGVARA 149
Cdd:PRK14267 85 REVGMVFQYPNPFPHLTIYDNVAIGVKLngLVKSKKELDERVEWALKKAALWD-EVKDRLndyPSNLSGGQRQRLVIARA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 150 LAAEPAMLLMDEPFGALDPIIRNKAQDDLFALQRRLgiTVVIVTHDIEEALKLGDTIAVMDAGRLLQVASPAEILGKPAA 229
Cdd:PRK14267 164 LAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEY--TIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENPEH 241
|
250
....*....|
gi 1861108599 230 GVVEQLVAGV 239
Cdd:PRK14267 242 ELTEKYVTGA 251
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
11-238 |
3.28e-37 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 132.98 E-value: 3.28e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 11 FGDIVAVDDVSLTMQRGTITALVGASGSGKSTLLRMINRL--IAP---TSGTIRIDGVD-----TATVapeQLRRGIGYA 80
Cdd:PRK14239 15 YNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndLNPevtITGSIVYNGHNiysprTDTV---DLRKEIGMV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 81 IQGHGLFPhWSVARNIATVPRLLGWP-ADRIDARVNELLDLFHLAPaEFADKLpHE----LSGGQQQRVGVARALAAEPA 155
Cdd:PRK14239 92 FQQPNPFP-MSIYENVVYGLRLKGIKdKQVLDEAVEKSLKGASIWD-EVKDRL-HDsalgLSGGQQQRVCIARVLATSPK 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 156 MLLMDEPFGALDPIIRNKAQDDLFALQRRLgiTVVIVTHDIEEALKLGDTIAVMDAGRLLQVASPAEILGKPAAGVVEQL 235
Cdd:PRK14239 169 IILLDEPTSALDPISAGKIEETLLGLKDDY--TMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQMFMNPKHKETEDY 246
|
...
gi 1861108599 236 VAG 238
Cdd:PRK14239 247 ISG 249
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
13-214 |
5.72e-37 |
|
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: 131.56 E-value: 5.72e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 13 DIVAVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGVDTATVAPEQLRRGIGYAIQGHGLFpHWSV 92
Cdd:cd03245 16 EIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNIGYVPQDVTLF-YGTL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 93 ARNIAtvprlLGWP-ADriDARVNELLDLFHLapAEFADKLPH-----------ELSGGQQQRVGVARALAAEPAMLLMD 160
Cdd:cd03245 95 RDNIT-----LGAPlAD--DERILRAAELAGV--TDFVNKHPNgldlqigergrGLSGGQRQAVALARALLNDPPILLLD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1861108599 161 EPFGALDpiirNKAQDDLF-ALQRRL-GITVVIVTHDIeEALKLGDTIAVMDAGRL 214
Cdd:cd03245 166 EPTSAMD----MNSEERLKeRLRQLLgDKTLIIITHRP-SLLDLVDRIIVMDSGRI 216
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
11-238 |
6.25e-37 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 132.60 E-value: 6.25e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 11 FGDIVAVDDVSLTMQRGTITALVGASGSGKSTLLRMINRL--IAPTSgtiRIDG--------VDTATVAPEQLRRGIGYA 80
Cdd:PRK14243 20 YGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLndLIPGF---RVEGkvtfhgknLYAPDVDPVEVRRRIGMV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 81 IQGHGLFPHwSVARNIATVPRLLGWPADrIDARVNELLDLFHLAPaEFADKLPHE---LSGGQQQRVGVARALAAEPAML 157
Cdd:PRK14243 97 FQKPNPFPK-SIYDNIAYGARINGYKGD-MDELVERSLRQAALWD-EVKDKLKQSglsLSGGQQQRLCIARAIAVQPEVI 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 158 LMDEPFGALDPIIRNKAQDDLFALQRRLgiTVVIVTHDIEEALKLGDTIAVMDA---------GRLLQVASPAEILGKPA 228
Cdd:PRK14243 174 LMDEPCSALDPISTLRIEELMHELKEQY--TIIIVTHNMQQAARVSDMTAFFNVeltegggryGYLVEFDRTEKIFNSPQ 251
|
250
....*....|
gi 1861108599 229 AGVVEQLVAG 238
Cdd:PRK14243 252 QQATRDYVSG 261
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1-224 |
1.13e-36 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 131.67 E-value: 1.13e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 1 MIEIERAGKRFGDIVAVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGVDTATVAPEQLRRGIGYA 80
Cdd:PRK11231 2 TLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 81 IQGHgLFPHWSVARNIATVPR-----LLGWPADRIDARVNELLDLFHLapAEFADKLPHELSGGQQQRVGVARALAAEPA 155
Cdd:PRK11231 82 PQHH-LTPEGITVRELVAYGRspwlsLWGRLSAEDNARVNQAMEQTRI--NHLADRRLTDLSGGQRQRAFLAMVLAQDTP 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1861108599 156 MLLMDEPFGALDpIIRnkaQDDLFALQRRL---GITVVIVTHDIEEALKLGDTIAVMDAGRLLQVASPAEIL 224
Cdd:PRK11231 159 VVLLDEPTTYLD-INH---QVELMRLMRELntqGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVM 226
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-224 |
1.20e-36 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 131.78 E-value: 1.20e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 1 MIEIERAGKRFGDIVAVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGVDTATVAPEQL--RRgig 78
Cdd:COG4559 1 MLEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELarRR--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 79 yAI--QGHGL-FPhWSVArniaTVPRL----LGWPADRIDARVNELLDLFHLAPaeFADKLPHELSGGQQQRVGVARALA 151
Cdd:COG4559 78 -AVlpQHSSLaFP-FTVE----EVVALgrapHGSSAAQDRQIVREALALVGLAH--LAGRSYQTLSGGEQQRVQLARVLA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 152 -------AEPAMLLMDEPFGALDPiirnKAQDDLFALQRRL---GITVVIVTHDIEEALKLGDTIAVMDAGRLLQVASPA 221
Cdd:COG4559 150 qlwepvdGGPRWLFLDEPTSALDL----AHQHAVLRLARQLarrGGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPE 225
|
...
gi 1861108599 222 EIL 224
Cdd:COG4559 226 EVL 228
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
16-224 |
1.32e-36 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 132.82 E-value: 1.32e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 16 AVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSG-TIRIDGVDTATVAP----EQLRRGIGYAIQghglFPHW 90
Cdd:PRK13645 26 ALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGqTIVGDYAIPANLKKikevKRLRKEIGLVFQ----FPEY 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 91 -----SVARNIATVPRLLGWPADRIDARVNELLDLFHLaPAEFADKLPHELSGGQQQRVGVARALAAEPAMLLMDEPFGA 165
Cdd:PRK13645 102 qlfqeTIEKDIAFGPVNLGENKQEAYKKVPELLKLVQL-PEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGG 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1861108599 166 LDPiirnKAQDDLFALQRRL----GITVVIVTHDIEEALKLGDTIAVMDAGRLLQVASPAEIL 224
Cdd:PRK13645 181 LDP----KGEEDFINLFERLnkeyKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIF 239
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
16-229 |
2.36e-36 |
|
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: 136.82 E-value: 2.36e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 16 AVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGVDTATVAPEQLRRGIGYAIQGHGLFpHWSVARN 95
Cdd:COG4987 350 VLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRRIAVVPQRPHLF-DTTLREN 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 96 IatvprLLGWP-ADriDARVNELLDLFHLAPaeFADKLPH-----------ELSGGQQQRVGVARALAAEPAMLLMDEPF 163
Cdd:COG4987 429 L-----RLARPdAT--DEELWAALERVGLGD--WLAALPDgldtwlgeggrRLSGGERRRLALARALLRDAPILLLDEPT 499
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1861108599 164 GALDPIIRNKAQDDLFALQRrlGITVVIVTHDiEEALKLGDTIAVMDAGRLLQVASPAEILGKPAA 229
Cdd:COG4987 500 EGLDAATEQALLADLLEALA--GRTVLLITHR-LAGLERMDRILVLEDGRIVEQGTHEELLAQNGR 562
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
9-223 |
3.80e-36 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 137.95 E-value: 3.80e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 9 KRFGDIVAVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIR-----IDGVDTATvapeqlRRGIGYAIQG 83
Cdd:NF033858 274 MRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWlfgqpVDAGDIAT------RRRVGYMSQA 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 84 HGLFPHWSVARNIATVPRLLGWPADRIDARVNELLDLFHLapAEFADKLPHELSGGQQQRVGVARALAAEPAMLLMDEPF 163
Cdd:NF033858 348 FSLYGELTVRQNLELHARLFHLPAAEIAARVAEMLERFDL--ADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPT 425
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 164 GALDPIIRNKAQDDLFALQRRLGITVVIVTHDIEEALKLgDTIAVMDAGRLLQVASPAEI 223
Cdd:NF033858 426 SGVDPVARDMFWRLLIELSREDGVTIFISTHFMNEAERC-DRISLMHAGRVLASDTPAAL 484
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-222 |
4.47e-36 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 135.54 E-value: 4.47e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 1 MIEIERAGKRFGDIVAVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGVDTATVAPEQ-LRRGIGY 79
Cdd:COG3845 5 ALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRDaIALGIGM 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 80 AIQGHGLFPHWSVARNIA--TVPRLLGWPA-DRIDARVNELLDLFHLA--PaefaDKLPHELSGGQQQRVGVARALAAEP 154
Cdd:COG3845 85 VHQHFMLVPNLTVAENIVlgLEPTKGGRLDrKAARARIRELSERYGLDvdP----DAKVEDLSVGEQQRVEILKALYRGA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1861108599 155 AMLLMDEPFGALDPiirnKAQDDLFALQRRL---GITVVIVTHDIEEALKLGDTIAVMDAGRLLQVASPAE 222
Cdd:COG3845 161 RILILDEPTAVLTP----QEADELFEILRRLaaeGKSIIFITHKLREVMAIADRVTVLRRGKVVGTVDTAE 227
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
17-227 |
5.85e-36 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 130.72 E-value: 5.85e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 17 VDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDG----VDTATVAPEQLRRGIGYAIQghglFPHW-- 90
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGyhitPETGNKNLKKLRKKVSLVFQ----FPEAql 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 91 ---SVARNIATVPRLLGWPADRIDARVNELLDLFHLaPAEFADKLPHELSGGQQQRVGVARALAAEPAMLLMDEPFGALD 167
Cdd:PRK13641 99 fenTVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGL-SEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLD 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 168 PIIRnKAQDDLFALQRRLGITVVIVTHDIEEALKLGDTIAVMDAGRLLQVASPAEILGKP 227
Cdd:PRK13641 178 PEGR-KEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDK 236
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
21-224 |
1.20e-35 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 128.55 E-value: 1.20e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 21 SLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGVDTATVAPEQlrRGIGYAIQGHGLFPHWSVARNIAtvp 100
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSR--RPVSMLFQENNLFSHLTVAQNIG--- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 101 rlLGW-PADRIDARVNELLDLF--HLAPAEFADKLPHELSGGQQQRVGVARALAAEPAMLLMDEPFGALDPIIRNKAQDD 177
Cdd:PRK10771 94 --LGLnPGLKLNAAQREKLHAIarQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTL 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1861108599 178 LFALQRRLGITVVIVTHDIEEALKLGDTIAVMDAGRLLQVASPAEIL 224
Cdd:PRK10771 172 VSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELL 218
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
16-223 |
1.71e-35 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 129.48 E-value: 1.71e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 16 AVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGVD-TATVAPE---QLRRGIGYAIQghglFPH-- 89
Cdd:PRK13649 22 ALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLiTSTSKNKdikQIRKKVGLVFQ----FPEsq 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 90 ---WSVARNIATVPRLLGWPADRIDARVNELLDLFHLApAEFADKLPHELSGGQQQRVGVARALAAEPAMLLMDEPFGAL 166
Cdd:PRK13649 98 lfeETVLKDVAFGPQNFGVSQEEAEALAREKLALVGIS-ESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGL 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1861108599 167 DPIIRnKAQDDLFALQRRLGITVVIVTHDIEEALKLGDTIAVMDAGRLLQVASPAEI 223
Cdd:PRK13649 177 DPKGR-KELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDI 232
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
13-236 |
1.95e-35 |
|
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: 128.04 E-value: 1.95e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 13 DIVAVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGVDTATVAPEQLRRGIGYAIQGHGLFPHwSV 92
Cdd:cd03249 15 DVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIGLVSQEPVLFDG-TI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 93 ARNIAtvprlLGwpadRIDARVNELLDLFHLAPA-EFADKLPH-----------ELSGGQQQRVGVARALAAEPAMLLMD 160
Cdd:cd03249 94 AENIR-----YG----KPDATDEEVEEAAKKANIhDFIMSLPDgydtlvgergsQLSGGQKQRIAIARALLRNPKILLLD 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1861108599 161 EPFGALDPIIRNKAQDdlfALQR-RLGITVVIVTHDIeEALKLGDTIAVMDAGRLLQVASPAEILGKPaaGVVEQLV 236
Cdd:cd03249 165 EATSALDAESEKLVQE---ALDRaMKGRTTIVIAHRL-STIRNADLIAVLQNGQVVEQGTHDELMAQK--GVYAKLV 235
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
17-212 |
3.68e-35 |
|
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: 126.22 E-value: 3.68e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 17 VDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGVDtatVAPEQLRRGIGYAIQ--GHGLFPHwSVAR 94
Cdd:cd03226 16 LDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKP---IKAKERRKSIGYVMQdvDYQLFTD-SVRE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 95 NIatvprLLGWP-ADRIDARVNELLDLFHLApaEFADKLPHELSGGQQQRVGVARALAAEPAMLLMDEPFGALDPiiRNK 173
Cdd:cd03226 92 EL-----LLGLKeLDAGNEQAETVLKDLDLY--ALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDY--KNM 162
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1861108599 174 AQ-DDLFALQRRLGITVVIVTHDIEEALKLGDTIAVMDAG 212
Cdd:cd03226 163 ERvGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANG 202
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
17-247 |
4.85e-35 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 127.88 E-value: 4.85e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 17 VDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGVDTATVAPEQ---LRRGIGYAIQGH--GLFPHWS 91
Cdd:PRK10419 28 LNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQrkaFRRDIQMVFQDSisAVNPRKT 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 92 VARNIATVPR-LLGWPADRIDARVNELLDLFHLAPaEFADKLPHELSGGQQQRVGVARALAAEPAMLLMDEPFGALDPII 170
Cdd:PRK10419 108 VREIIREPLRhLLSLDKAERLARASEMLRAVDLDD-SVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVL 186
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1861108599 171 RNKAQDDLFALQRRLGITVVIVTHDIEEALKLGDTIAVMDAGRLL--QVASPAEILGKPAAGVVEQLVAGVdRPLRLLA 247
Cdd:PRK10419 187 QAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVetQPVGDKLTFSSPAGRVLQNAVLPA-FPVRRRT 264
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
13-224 |
5.04e-35 |
|
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274550 [Multi-domain] Cd Length: 694 Bit Score: 134.22 E-value: 5.04e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 13 DIVAVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGVDTATVAPEQLRRGIGYAIQGHGLFpHWSV 92
Cdd:TIGR03375 477 ETPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQIDPADLRRNIGYVPQDPRLF-YGTL 555
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 93 ARNIAtvprlLGWPADRiDARVNELLDLFHLApaEFADKLPH-----------ELSGGQQQRVGVARALAAEPAMLLMDE 161
Cdd:TIGR03375 556 RDNIA-----LGAPYAD-DEEILRAAELAGVT--EFVRRHPDgldmqigergrSLSGGQRQAVALARALLRDPPILLLDE 627
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1861108599 162 PFGALDpiirNKAQDDLF-ALQRRL-GITVVIVTHDIeEALKLGDTIAVMDAGRLLQVASPAEIL 224
Cdd:TIGR03375 628 PTSAMD----NRSEERFKdRLKRWLaGKTLVLVTHRT-SLLDLVDRIIVMDNGRIVADGPKDQVL 687
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1-224 |
5.28e-35 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 127.80 E-value: 5.28e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 1 MIEIERAGKRFGDIV--AVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGVDTATVAPEQLRRGIG 78
Cdd:PRK13632 7 MIKVENVSFSYPNSEnnALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 79 YAIQG-HGLFPHWSVARNIA------TVPRllgwpaDRIDARVNELLDLFHLApaEFADKLPHELSGGQQQRVGVARALA 151
Cdd:PRK13632 87 IIFQNpDNQFIGATVEDDIAfglenkKVPP------KKMKDIIDDLAKKVGME--DYLDKEPQNLSGGQKQRVAIASVLA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1861108599 152 AEPAMLLMDEPFGALDPIIRNKAQDDLFALQRRLGITVVIVTHDIEEALkLGDTIAVMDAGRLLQVASPAEIL 224
Cdd:PRK13632 159 LNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAI-LADKVIVFSEGKLIAQGKPKEIL 230
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-224 |
5.37e-35 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 128.77 E-value: 5.37e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 2 IEIERAGKRFGDIVAVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGVDTATVAPeQLRRGIGYAI 81
Cdd:PRK13537 8 IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRAR-HARQRVGVVP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 82 QGHGLFPHWSVARNIATVPRLLGWPADRIDARVNELLDLFHLAPAefADKLPHELSGGQQQRVGVARALAAEPAMLLMDE 161
Cdd:PRK13537 87 QFDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENK--ADAKVGELSGGMKRRLTLARALVNDPDVLVLDE 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1861108599 162 PFGALDPIIRNKAQDDLFALQRRlGITVVIVTHDIEEALKLGDTIAVMDAGRLLQVASPAEIL 224
Cdd:PRK13537 165 PTTGLDPQARHLMWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALI 226
|
|
| heterocyst_DevA |
TIGR02982 |
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly ... |
19-215 |
5.82e-35 |
|
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly in the Cyanobacteria, but also in the Planctomycetes. Cyanobacterial examples are involved in heterocyst formation, by which some fraction of members of the colony undergo a developmental change and become capable of nitrogen fixation. The DevBCA proteins are thought export of either heterocyst-specific glycolipids or an enzyme essential for formation of the laminated layer found in heterocysts.
Pssm-ID: 274374 [Multi-domain] Cd Length: 220 Bit Score: 126.29 E-value: 5.82e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 19 DVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGVDTATVAPE---QLRRGIGYAIQGHGLFPHWSVARN 95
Cdd:TIGR02982 23 DINLEINPGEIVILTGPSGSGKTTLLTLIGGLRSVQEGSLKVLGQELHGASKKqlvQLRRRIGYIFQAHNLLGFLTARQN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 96 IATVPRLL-GWPADRIDARVNELLDLFHLApaEFADKLPHELSGGQQQRVGVARALAAEPAMLLMDEPFGALDpiirNKA 174
Cdd:TIGR02982 103 VQMALELQpNLSYQEARERARAMLEAVGLG--DHLNYYPHNLSGGQKQRVAIARALVHHPKLVLADEPTAALD----SKS 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1861108599 175 QDDLFALQRRL----GITVVIVTHDiEEALKLGDTIAVMDAGRLL 215
Cdd:TIGR02982 177 GRDVVELMQKLakeqGCTILMVTHD-NRILDVADRILQMEDGKLL 220
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-213 |
6.36e-35 |
|
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: 126.39 E-value: 6.36e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 1 MIEIERAGKRF-----GD--IVAVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRID----GVDTATVA 69
Cdd:COG4778 4 LLEVENLSKTFtlhlqGGkrLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRhdggWVDLAQAS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 70 PEQL----RRGIGYAIQghglF----PHWSvARNIATVP-RLLGWPADRIDARVNELLD-------LFHLAPAEFadklp 133
Cdd:COG4778 84 PREIlalrRRTIGYVSQ----FlrviPRVS-ALDVVAEPlLERGVDREEARARARELLArlnlperLWDLPPATF----- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 134 helSGGQQQRVGVARALAAEPAMLLMDEPFGALDPIIRNKAQDDLFALQRRlGITVVIVTHDIEEALKLGDTIAVMDAGR 213
Cdd:COG4778 154 ---SGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKAR-GTAIIGIFHDEEVREAVADRVVDVTPFS 229
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
16-224 |
6.63e-35 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 128.31 E-value: 6.63e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 16 AVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRI-DGVDTAT-----VAPEQLRRGIGYAIQGHGLFPH 89
Cdd:PRK13643 21 ALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVgDIVVSSTskqkeIKPVRKKVGVVFQFPESQLFEE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 90 wSVARNIATVPRLLGWPADRIDARVNELLDLFHLApAEFADKLPHELSGGQQQRVGVARALAAEPAMLLMDEPFGALDPI 169
Cdd:PRK13643 101 -TVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLA-DEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPK 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1861108599 170 IRNKAQdDLFALQRRLGITVVIVTHDIEEALKLGDTIAVMDAGRLLQVASPAEIL 224
Cdd:PRK13643 179 ARIEMM-QLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVF 232
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
2-225 |
1.12e-34 |
|
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: 131.85 E-value: 1.12e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 2 IEIERagkrfGDIVAVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRI----DGVDTATVAPE---QLR 74
Cdd:TIGR03269 290 ISVDR-----GVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdEWVDMTKPGPDgrgRAK 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 75 RGIGYAIQGHGLFPHWSVARNIAtvprllgwpadriDARVNELLDLFHLAPA---------------EFADKLPHELSGG 139
Cdd:TIGR03269 365 RYIGILHQEYDLYPHRTVLDNLT-------------EAIGLELPDELARMKAvitlkmvgfdeekaeEILDKYPDELSEG 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 140 QQQRVGVARALAAEPAMLLMDEPFGALDPIIRNKAQDDLFALQRRLGITVVIVTHDIEEALKLGDTIAVMDAGRLLQVAS 219
Cdd:TIGR03269 432 ERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGD 511
|
....*.
gi 1861108599 220 PAEILG 225
Cdd:TIGR03269 512 PEEIVE 517
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
9-238 |
1.19e-34 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 126.62 E-value: 1.19e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 9 KRFGDIVAVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGVDTATVAPEQ-------------LRR 75
Cdd:PRK10619 13 KRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKDgqlkvadknqlrlLRT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 76 GIGYAIQGHGLFPHWSVARNIATVP-RLLGwpADRIDARVNELLDLFHLAPAEFA-DKLPHELSGGQQQRVGVARALAAE 153
Cdd:PRK10619 93 RLTMVFQHFNLWSHMTVLENVMEAPiQVLG--LSKQEARERAVKYLAKVGIDERAqGKYPVHLSGGQQQRVSIARALAME 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 154 PAMLLMDEPFGALDPIIRNKAQDDLFALQRRlGITVVIVTHDIEEALKLGDTIAVMDAGRLLQVASPAEILGKPAAGVVE 233
Cdd:PRK10619 171 PEVLLFDEPTSALDPELVGEVLRIMQQLAEE-GKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGNPQSPRLQ 249
|
....*
gi 1861108599 234 QLVAG 238
Cdd:PRK10619 250 QFLKG 254
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
16-237 |
1.67e-34 |
|
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: 125.56 E-value: 1.67e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 16 AVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAP----TSGTIRIDGVDtatVAPEQLR-RGIGYAIQG--HGLFP 88
Cdd:TIGR02770 1 LVQDLNLSLKRGEVLALVGESGSGKSLTCLAILGLLPPgltqTSGEILLDGRP---LLPLSIRgRHIATIMQNprTAFNP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 89 HWSVARNIATVPRLLGWPADRIDARVNELLDLFHLA-PAEFADKLPHELSGGQQQRVGVARALAAEPAMLLMDEPFGALD 167
Cdd:TIGR02770 78 LFTMGNHAIETLRSLGKLSKQARALILEALEAVGLPdPEEVLKKYPFQLSGGMLQRVMIALALLLEPPFLIADEPTTDLD 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 168 PIIRNKAQDDLFALQRRLGITVVIVTHDIEEALKLGDTIAVMDAGRLLQVASPAEILGKPAAGVVEQLVA 237
Cdd:TIGR02770 158 VVNQARVLKLLRELRQLFGTGILLITHDLGVVARIADEVAVMDDGRIVERGTVKEIFYNPKHETTRKLLS 227
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
2-236 |
2.55e-34 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 125.72 E-value: 2.55e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 2 IEIERAGKRF---------GDIVAVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGV-----DTAT 67
Cdd:COG4167 5 LEVRNLSKTFkyrtglfrrQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHkleygDYKY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 68 VApeQLRRGIgyaIQ--GHGLFPHWSVARnIATVPRLL--GWPADRIDARVNELLDLFHLAPaEFADKLPHELSGGQQQR 143
Cdd:COG4167 85 RC--KHIRMI---FQdpNTSLNPRLNIGQ-ILEEPLRLntDLTAEEREERIFATLRLVGLLP-EHANFYPHMLSSGQKQR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 144 VGVARALAAEPAMLLMDEPFGALDPIIRNKAQDDLFALQRRLGITVVIVTHDIEEALKLGDTIAVMDAGRLLQVASPAEI 223
Cdd:COG4167 158 VALARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKHISDKVLVMHQGEVVEYGKTAEV 237
|
250
....*....|...
gi 1861108599 224 LGKPAAGVVEQLV 236
Cdd:COG4167 238 FANPQHEVTKRLI 250
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
1-228 |
2.87e-34 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 127.68 E-value: 2.87e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 1 MIEIERAgKRFGDIVAvdDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDG---VDTAT---VAPEQlr 74
Cdd:PRK11144 1 MLELNFK-QQLGDLCL--TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGrvlFDAEKgicLPPEK-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 75 RGIGYAIQGHGLFPHWSVARNiatvprlLGWPADRIDA----RVNELLDLFHLApaefaDKLPHELSGGQQQRVGVARAL 150
Cdd:PRK11144 76 RRIGYVFQDARLFPHYKVRGN-------LRYGMAKSMVaqfdKIVALLGIEPLL-----DRYPGSLSGGEKQRVAIGRAL 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1861108599 151 AAEPAMLLMDEPFGALDPIIRNKAQDDLFALQRRLGITVVIVTHDIEEALKLGDTIAVMDAGRLLQVASPAEILGKPA 228
Cdd:PRK11144 144 LTAPELLLMDEPLASLDLPRKRELLPYLERLAREINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVWASSA 221
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
2-226 |
3.59e-34 |
|
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: 124.91 E-value: 3.59e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 2 IEIERAGKRFG--DIVAVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGVDTATVAPEQLRRGIGY 79
Cdd:cd03252 1 ITFEHVRFRYKpdGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 80 AIQGHGLFPHwSVARNIAtvprlLGWPAdridARVNELLDLFHLAPA-EFADKLPH-----------ELSGGQQQRVGVA 147
Cdd:cd03252 81 VLQENVLFNR-SIRDNIA-----LADPG----MSMERVIEAAKLAGAhDFISELPEgydtivgeqgaGLSGGQRQRIAIA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 148 RALAAEPAMLLMDEPFGALD-----PIIRNkaQDDLFAlqrrlGITVVIVTHDIeEALKLGDTIAVMDAGRLLQVASPAE 222
Cdd:cd03252 151 RALIHNPRILIFDEATSALDyesehAIMRN--MHDICA-----GRTVIIIAHRL-STVKNADRIIVMEKGRIVEQGSHDE 222
|
....
gi 1861108599 223 ILGK 226
Cdd:cd03252 223 LLAE 226
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-224 |
9.33e-34 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 123.65 E-value: 9.33e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 1 MIEIERAGKRF----------------------GDIVAVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTI 58
Cdd:COG1134 4 MIEVENVSKSYrlyhepsrslkelllrrrrtrrEEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 59 RIDGvdtaTVAPeqLrrgIGYaiqGHGLFPHWSVARNIATVPRLLGWPADRIDARVNELldlfhlapAEFAD-----KLP 133
Cdd:COG1134 84 EVNG----RVSA--L---LEL---GAGFHPELTGRENIYLNGRLLGLSRKEIDEKFDEI--------VEFAElgdfiDQP 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 134 -HELSGGQQQRVGVARALAAEPAMLLMDEPFGALDPIIRNKAQDDLFALQRRlGITVVIVTHDIEEALKLGDTIAVMDAG 212
Cdd:COG1134 144 vKTYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRES-GRTVIFVSHSMGAVRRLCDRAIWLEKG 222
|
250
....*....|..
gi 1861108599 213 RLLQVASPAEIL 224
Cdd:COG1134 223 RLVMDGDPEEVI 234
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
4-214 |
1.07e-33 |
|
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: 123.03 E-value: 1.07e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 4 IERAGKRFGDIVAVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGVDTATVAPeqlrrgigyaiqG 83
Cdd:cd03220 25 ILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSLLGL------------G 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 84 HGLFPHWSVARNIATVPRLLGWPADRIDARVNELLDLFHLapAEFADKLPHELSGGQQQRVGVARALAAEPAMLLMDEPF 163
Cdd:cd03220 93 GGFNPELTGRENIYLNGRLLGLSRKEIDEKIDEIIEFSEL--GDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVL 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1861108599 164 GALDPIIRNKAQDDLFALQRRlGITVVIVTHDIEEALKLGDTIAVMDAGRL 214
Cdd:cd03220 171 AVGDAAFQEKCQRRLRELLKQ-GKTVILVSHDPSSIKRLCDRALVLEKGKI 220
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1-226 |
1.35e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 124.57 E-value: 1.35e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 1 MIEIERAGKRFGD-IVAVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDG--VDTATVAPEQLRRGI 77
Cdd:PRK13636 5 ILKVEELNYNYSDgTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGkpIDYSRKGLMKLRESV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 78 GYAIQG--HGLFPHwSVARNIATVPRLLGWPADRIDARVNELLDLFHLAPaeFADKLPHELSGGQQQRVGVARALAAEPA 155
Cdd:PRK13636 85 GMVFQDpdNQLFSA-SVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEH--LKDKPTHCLSFGQKKRVAIAGVLVMEPK 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1861108599 156 MLLMDEPFGALDPIIRNKAQDDLFALQRRLGITVVIVTHDIEEALKLGDTIAVMDAGRLLQVASPAEILGK 226
Cdd:PRK13636 162 VLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFAE 232
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
16-227 |
2.03e-33 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 125.08 E-value: 2.03e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 16 AVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGVDTATVAPE---QLRRGIGYAIQG--HGLFPHW 90
Cdd:PRK11308 30 ALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEaqkLLRQKIQIVFQNpyGSLNPRK 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 91 SVaRNIATVPRLLGWPADRID--ARVNELLDLFHLAPaEFADKLPHELSGGQQQRVGVARALAAEPAMLLMDEPFGALDP 168
Cdd:PRK11308 110 KV-GQILEEPLLINTSLSAAErrEKALAMMAKVGLRP-EHYDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALDV 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1861108599 169 IIRnkAQD-DLFA-LQRRLGITVVIVTHDIEEALKLGDTIAVMDAGRLLQVASPAEILGKP 227
Cdd:PRK11308 188 SVQ--AQVlNLMMdLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFNNP 246
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
16-243 |
2.39e-33 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 123.76 E-value: 2.39e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 16 AVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTS---GTIRIDGVDTATVAPEQLRRGIGYAIQG-HGLFPHWS 91
Cdd:PRK13640 22 ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDnpnSKITVDGITLTAKTVWDIREKVGIVFQNpDNQFVGAT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 92 VARNIATVPRLLGWPADRIDARVNELLDlfHLAPAEFADKLPHELSGGQQQRVGVARALAAEPAMLLMDEPFGALDPIIR 171
Cdd:PRK13640 102 VGDDVAFGLENRAVPRPEMIKIVRDVLA--DVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGK 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1861108599 172 NKAQDDLFALQRRLGITVVIVTHDIEEAlKLGDTIAVMDAGRLLQVASPAEILGKPAagVVEQlvAGVDRPL 243
Cdd:PRK13640 180 EQILKLIRKLKKKNNLTVISITHDIDEA-NMADQVLVLDDGKLLAQGSPVEIFSKVE--MLKE--IGLDIPF 246
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
15-226 |
4.11e-33 |
|
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: 127.94 E-value: 4.11e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 15 VAVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGVDTATVAPEQLRRGIGYAIQGHGLFPHwSVAR 94
Cdd:COG4618 346 PILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRHIGYLPQDVELFDG-TIAE 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 95 NIAtvpRLlgwpADRIDARVnelldlfhLAPAEFAD------KLP-----------HELSGGQQQRVGVARALAAEPAML 157
Cdd:COG4618 425 NIA---RF----GDADPEKV--------VAAAKLAGvhemilRLPdgydtrigeggARLSGGQRQRIGLARALYGDPRLV 489
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1861108599 158 LMDEPFGALDPIIRnKAQDDLFALQRRLGITVVIVTHDIeEALKLGDTIAVMDAGRLLQVASPAEILGK 226
Cdd:COG4618 490 VLDEPNSNLDDEGE-AALAAAIRALKARGATVVVITHRP-SLLAAVDKLLVLRDGRVQAFGPRDEVLAR 556
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
12-227 |
5.42e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 122.60 E-value: 5.42e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 12 GDIVAVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGVDTATVAPEQLRRGIGYAIQG--HGLFPH 89
Cdd:PRK13652 15 GSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLVFQNpdDQIFSP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 90 wSVARNIATVPRLLGWPADRIDARVNELLDLFHLApaEFADKLPHELSGGQQQRVGVARALAAEPAMLLMDEPFGALDPI 169
Cdd:PRK13652 95 -TVEQDIAFGPINLGLDEETVAHRVSSALHMLGLE--ELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQ 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1861108599 170 IRNKAQDDLFALQRRLGITVVIVTHDIEEALKLGDTIAVMDAGRLLQVASPAEILGKP 227
Cdd:PRK13652 172 GVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
13-228 |
5.52e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 123.81 E-value: 5.52e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 13 DIVAVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRID--------GVDTATVAPEQ--------LRRG 76
Cdd:PRK13631 38 ELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGdiyigdkkNNHELITNPYSkkiknfkeLRRR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 77 IGYAIQghglFPHW-----SVARNIATVPRLLGWPADRIDARVNELLDLFHLApAEFADKLPHELSGGQQQRVGVARALA 151
Cdd:PRK13631 118 VSMVFQ----FPEYqlfkdTIEKDIMFGPVALGVKKSEAKKLAKFYLNKMGLD-DSYLERSPFGLSGGQKRRVAIAGILA 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 152 AEPAMLLMDEPFGALDP---------IIRNKAQddlfalqrrlGITVVIVTHDIEEALKLGDTIAVMDAGRLLQVASPAE 222
Cdd:PRK13631 193 IQPEILIFDEPTAGLDPkgehemmqlILDAKAN----------NKTVFVITHTMEHVLEVADEVIVMDKGKILKTGTPYE 262
|
....*.
gi 1861108599 223 ILGKPA 228
Cdd:PRK13631 263 IFTDQH 268
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1-224 |
5.69e-33 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 122.19 E-value: 5.69e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 1 MIEIERAGKRFGDIVAVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGVDTATVAPEQLRRGIGYA 80
Cdd:PRK13548 2 MLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 81 IQGHGL-FPhWSVARNIA--TVPRLLGW-PADRIDARVNELLDLfhlapAEFADKLPHELSGGQQQRVGVARALA----- 151
Cdd:PRK13548 82 PQHSSLsFP-FTVEEVVAmgRAPHGLSRaEDDALVAAALAQVDL-----AHLAGRDYPQLSGGEQQRVQLARVLAqlwep 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1861108599 152 -AEPAMLLMDEPFGALDPiirnKAQDDLFALQRRL----GITVVIVTHDIEEALKLGDTIAVMDAGRLLQVASPAEIL 224
Cdd:PRK13548 156 dGPPRWLLLDEPTSALDL----AHQHHVLRLARQLaherGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAEVL 229
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
12-199 |
1.19e-32 |
|
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: 119.45 E-value: 1.19e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 12 GDIVAVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDG--VDTATVAPEQLRRGIGYAIQG--HGLF 87
Cdd:TIGR01166 3 GGPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGepLDYSRKGLLERRQRVGLVFQDpdDQLF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 88 PHwSVARNIATVPRLLGWPADRIDARVNELLDLfhLAPAEFADKLPHELSGGQQQRVGVARALAAEPAMLLMDEPFGALD 167
Cdd:TIGR01166 83 AA-DVDQDVAFGPLNLGLSEAEVERRVREALTA--VGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAGLD 159
|
170 180 190
....*....|....*....|....*....|....*
gi 1861108599 168 PiirnKAQDDLFALQRRL---GITVVIVTHDIEEA 199
Cdd:TIGR01166 160 P----AGREQMLAILRRLraeGMTVVISTHDVDLA 190
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
15-226 |
1.27e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 121.81 E-value: 1.27e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 15 VAVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGVD----TATVAPEQLRRGIGYAIQghglFPHW 90
Cdd:PRK13646 21 QAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITithkTKDKYIRPVRKRIGMVFQ----FPES 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 91 -----SVARNIATVPRLLGWPADRIDARVNELLDLFHLaPAEFADKLPHELSGGQQQRVGVARALAAEPAMLLMDEPFGA 165
Cdd:PRK13646 97 qlfedTVEREIIFGPKNFKMNLDEVKNYAHRLLMDLGF-SRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAG 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1861108599 166 LDPIIRNKAQDDLFALQRRLGITVVIVTHDIEEALKLGDTIAVMDAGRLLQVASPAEILGK 226
Cdd:PRK13646 176 LDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFKD 236
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-224 |
1.71e-32 |
|
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: 120.57 E-value: 1.71e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 1 MIEIERAGKRFGDIVAVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSG-TIRIDGVDTATVAPEQLRRGIGY 79
Cdd:COG1119 3 LLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRGGEDVWELRKRIGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 80 AIQG-HGLFPHWSVARNI------ATVpRLLGWPADRIDARVNELLDLFHLApaEFADKLPHELSGGQQQRVGVARALAA 152
Cdd:COG1119 83 VSPAlQLRFPRDETVLDVvlsgffDSI-GLYREPTDEQRERARELLELLGLA--HLADRPFGTLSQGEQRRVLIARALVK 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1861108599 153 EPAMLLMDEPFGALDPiirnKAQDDLFALQRRL----GITVVIVTHDIEEALKLGDTIAVMDAGRLLQVASPAEIL 224
Cdd:COG1119 160 DPELLILDEPTAGLDL----GARELLLALLDKLaaegAPTLVLVTHHVEEIPPGITHVLLLKDGRVVAAGPKEEVL 231
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
16-226 |
1.88e-32 |
|
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: 120.03 E-value: 1.88e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 16 AVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGVDTATVAPEQLRRGIGYAIQGHGLFpHWSVARN 95
Cdd:cd03251 17 VLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGLVSQDVFLF-NDTVAEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 96 IATvprllgwpaDRIDARVNELLDLFHLAPA-EFADKLPH-----------ELSGGQQQRVGVARALAAEPAMLLMDEPF 163
Cdd:cd03251 96 IAY---------GRPGATREEVEEAARAANAhEFIMELPEgydtvigergvKLSGGQRQRIAIARALLKDPPILILDEAT 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1861108599 164 GALDPIIRNKAQDDLFALQRrlGITVVIVTH---DIEEAlklgDTIAVMDAGRLLQVASPAEILGK 226
Cdd:cd03251 167 SALDTESERLVQAALERLMK--NRTTFVIAHrlsTIENA----DRIVVLEDGKIVERGTHEELLAQ 226
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
2-243 |
1.94e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 121.00 E-value: 1.94e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 2 IEIERAGKRFGD-IVAVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGVDTATVAPEQLRRGIGYA 80
Cdd:PRK13647 5 IEVEDLHFRYKDgTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGLV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 81 IQG--HGLFPHwSVARNIATVPRLLGWPADRIDARVNELLDLFHLApaEFADKLPHELSGGQQQRVGVARALAAEPAMLL 158
Cdd:PRK13647 85 FQDpdDQVFSS-TVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMW--DFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 159 MDEPFGALDPiirnKAQDDLFALQRRL---GITVVIVTHDIEEALKLGDTIAVMDAGRLLQVASPaEILGKPAagVVEQl 235
Cdd:PRK13647 162 LDEPMAYLDP----RGQETLMEILDRLhnqGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDK-SLLTDED--IVEQ- 233
|
....*...
gi 1861108599 236 vAGVDRPL 243
Cdd:PRK13647 234 -AGLRLPL 240
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
17-227 |
2.54e-32 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 120.53 E-value: 2.54e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 17 VDDVSLTMQRGTITALVGASGSGKSTLLRMINRLiAPTSGTIRIDG--------VDTATVAPEQLRRGIGYAIQGHGLFP 88
Cdd:PRK14258 23 LEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRM-NELESEVRVEGrveffnqnIYERRVNLNRLRRQVSMVHPKPNLFP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 89 hWSVARNIATVPRLLGW-PADRIDARVNELLDlfhlaPAEFADKLPH-------ELSGGQQQRVGVARALAAEPAMLLMD 160
Cdd:PRK14258 102 -MSVYDNVAYGVKIVGWrPKLEIDDIVESALK-----DADLWDEIKHkihksalDLSGGQQQRLCIARALAVKPKVLLMD 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1861108599 161 EPFGALDPIIRNKAQDDLFALQRRLGITVVIVTHDIEEALKLGDTIAVMDA-----GRLLQVASPAEILGKP 227
Cdd:PRK14258 176 EPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGnenriGQLVEFGLTKKIFNSP 247
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-246 |
6.15e-32 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 121.48 E-value: 6.15e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 1 MIEIERAG--KRFGDIVAVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGVDTATVApEQLRRGIG 78
Cdd:PRK13536 39 TVAIDLAGvsKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARA-RLARARIG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 79 YAIQGHGLFPHWSVARNIATVPRLLGWPADRIDARVNELLDLFHLAPAefADKLPHELSGGQQQRVGVARALAAEPAMLL 158
Cdd:PRK13536 118 VVPQFDNLDLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESK--ADARVSDLSGGMKRRLTLARALINDPQLLI 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 159 MDEPFGALDPIIRNKAQDDLFALQRRlGITVVIVTHDIEEALKLGDTIAVMDAGRLLQVASPAEILGKPAAGVVEQLVAG 238
Cdd:PRK13536 196 LDEPTTGLDPHARHLIWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHALIDEHIGCQVIEIYGG 274
|
....*...
gi 1861108599 239 VDRPLRLL 246
Cdd:PRK13536 275 DPHELSSL 282
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
16-226 |
6.61e-32 |
|
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: 118.48 E-value: 6.61e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 16 AVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGVDTATVAPEQLRRGIGYAIQGHGLFPHwSVARN 95
Cdd:cd03254 18 VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMIGVVLQDTFLFSG-TIMEN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 96 IatvprLLGWPADRiDARVNELLDLFHLapAEFADKLP-----------HELSGGQQQRVGVARALAAEPAMLLMDEPFG 164
Cdd:cd03254 97 I-----RLGRPNAT-DEEVIEAAKEAGA--HDFIMKLPngydtvlgengGNLSQGERQLLAIARAMLRDPKILILDEATS 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1861108599 165 ALDPIIRNKAQDDLFALQRrlGITVVIVTH---DIEEAlklgDTIAVMDAGRLLQVASPAEILGK 226
Cdd:cd03254 169 NIDTETEKLIQEALEKLMK--GRTSIIIAHrlsTIKNA----DKILVLDDGKIIEEGTHDELLAK 227
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
17-214 |
9.36e-32 |
|
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: 116.55 E-value: 9.36e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 17 VDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGVDTATVAPEQLRRGIGYAIQGHGLFPHwSVARNI 96
Cdd:cd03246 18 LRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGYLPQDDELFSG-SIAENI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 97 atvprllgwpadridarvnelldlfhlapaefadklpheLSGGQQQRVGVARALAAEPAMLLMDEPFGALDPIIRNKAQD 176
Cdd:cd03246 97 ---------------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQ 137
|
170 180 190
....*....|....*....|....*....|....*...
gi 1861108599 177 DLFALQRRlGITVVIVTHDIeEALKLGDTIAVMDAGRL 214
Cdd:cd03246 138 AIAALKAA-GATRIVIAHRP-ETLASADRILVLEDGRV 173
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
16-214 |
1.16e-31 |
|
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: 116.38 E-value: 1.16e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 16 AVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGVDTATVAPEQ-LRRGIGYAI---QGHGLFPHWS 91
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDaIRAGIAYVPedrKREGLVLDLS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 92 VARNIAtvprllgwpadridarvnelldlfhlapaefadkLPHELSGGQQQRVGVARALAAEPAMLLMDEPFGALDPiir 171
Cdd:cd03215 95 VAENIA----------------------------------LSSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDV--- 137
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1861108599 172 nKAQDDLFALQRRL---GITVVIVTHDIEEALKLGDTIAVMDAGRL 214
Cdd:cd03215 138 -GAKAEIYRLIRELadaGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
13-238 |
1.21e-31 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 118.61 E-value: 1.21e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 13 DIVAVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGV------DTATVAPEQLRRGIGYAIQGHGL 86
Cdd:PRK14246 22 DKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKvlyfgkDIFQIDAIKLRKEVGMVFQQPNP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 87 FPHWSVARNIATVPRLLGWPADR-IDARVNELLDLFHLApAEFADKL---PHELSGGQQQRVGVARALAAEPAMLLMDEP 162
Cdd:PRK14246 102 FPHLSIYDNIAYPLKSHGIKEKReIKKIVEECLRKVGLW-KEVYDRLnspASQLSGGQQQRLTIARALALKPKVLLMDEP 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1861108599 163 FGALDpIIRNKAQDDLFAlQRRLGITVVIVTHDIEEALKLGDTIAVMDAGRLLQVASPAEILGKPAAGVVEQLVAG 238
Cdd:PRK14246 181 TSMID-IVNSQAIEKLIT-ELKNEIAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNELTEKYVIG 254
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
12-236 |
1.30e-31 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 124.07 E-value: 1.30e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 12 GDIVAVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGVDTATVAPEQL----RRGIGYAIQGHGLF 87
Cdd:PRK10535 19 EQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALaqlrREHFGFIFQRYHLL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 88 PHWSVARNIATVPRLLGWPADRIDARVNELLDlfHLAPAEFADKLPHELSGGQQQRVGVARALAAEPAMLLMDEPFGALD 167
Cdd:PRK10535 99 SHLTAAQNVEVPAVYAGLERKQRLLRAQELLQ--RLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALD 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1861108599 168 PIIRNKAQDDLFALQRRlGITVVIVTHDIEEALKLGDTIAVMDaGRLlqVASPAEILGKPAAGVVEQLV 236
Cdd:PRK10535 177 SHSGEEVMAILHQLRDR-GHTVIIVTHDPQVAAQAERVIEIRD-GEI--VRNPPAQEKVNVAGGTEPVV 241
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
5-224 |
1.76e-31 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 117.69 E-value: 1.76e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 5 ERAGKRFGDIVAVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGVDTATVA-PEQLRRGIGYAIQG 83
Cdd:PRK10895 7 KNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPlHARARRGIGYLPQE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 84 HGLFPHWSVARNIATVPRLL-GWPADRIDARVNELLDLFHLApaEFADKLPHELSGGQQQRVGVARALAAEPAMLLMDEP 162
Cdd:PRK10895 87 ASIFRRLSVYDNLMAVLQIRdDLSAEQREDRANELMEEFHIE--HLRDSMGQSLSGGERRRVEIARALAANPKFILLDEP 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1861108599 163 FGALDPIIRNKAQDDLFALqRRLGITVVIVTHDIEEALKLGDTIAVMDAGRLLQVASPAEIL 224
Cdd:PRK10895 165 FAGVDPISVIDIKRIIEHL-RDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEIL 225
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
2-214 |
2.45e-31 |
|
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: 116.73 E-value: 2.45e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 2 IEIERAGKRFGDIVAVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGVDTAtvapEQLRRGIGYAI 81
Cdd:TIGR03740 1 LETKNLSKRFGKQTAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGHPWT----RKDLHKIGSLI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 82 QGHGLFPHWSVARNIATVPRLLGWPadriDARVNELLDLFHLAPAEfaDKLPHELSGGQQQRVGVARALAAEPAMLLMDE 161
Cdd:TIGR03740 77 ESPPLYENLTARENLKVHTTLLGLP----DSRIDEVLNIVDLTNTG--KKKAKQFSLGMKQRLGIAIALLNHPKLLILDE 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1861108599 162 PFGALDPIirnkAQDDLFALQRRL---GITVVIVTHDIEEALKLGDTIAVMDAGRL 214
Cdd:TIGR03740 151 PTNGLDPI----GIQELRELIRSFpeqGITVILSSHILSEVQQLADHIGIISEGVL 202
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
19-216 |
3.26e-31 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 116.84 E-value: 3.26e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 19 DVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGVDTATV---APEQLR-RGIGYAIQGHGLFPHWSVAR 94
Cdd:PRK11629 27 NVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLssaAKAELRnQKLGFIYQFHHLLPDFTALE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 95 NIAtVPRLLGW-PADRIDARVNELLDLFHLApaEFADKLPHELSGGQQQRVGVARALAAEPAMLLMDEPFGALDpiIRNK 173
Cdd:PRK11629 107 NVA-MPLLIGKkKPAEINSRALEMLAAVGLE--HRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLD--ARNA 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1861108599 174 aqDDLFA----LQRRLGITVVIVTHDIEEALKLGDTIAVMDaGRLLQ 216
Cdd:PRK11629 182 --DSIFQllgeLNRLQGTAFLVVTHDLQLAKRMSRQLEMRD-GRLTA 225
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-311 |
1.78e-30 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 118.79 E-value: 1.78e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 1 MIEIERAGKRFGDIVAVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGVDTATVAPEQLRRGIGYA 80
Cdd:PRK09536 3 MIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 81 IQGHGLFPHWSVARNIAT-----VPRLLGW-PADRidARVNELLDlfHLAPAEFADKLPHELSGGQQQRVGVARALAAEP 154
Cdd:PRK09536 83 PQDTSLSFEFDVRQVVEMgrtphRSRFDTWtETDR--AAVERAME--RTGVAQFADRPVTSLSGGERQRVLLARALAQAT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 155 AMLLMDEPFGALDpiIRNKAQDdlFALQRRL---GITVVIVTHDIEEALKLGDTIAVMDAGRLLQVASPAEILGKPA--- 228
Cdd:PRK09536 159 PVLLLDEPTASLD--INHQVRT--LELVRRLvddGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVLTADTlra 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 229 -----AGVVEQLVAGVDRPLRLLALTPIDAVAEPG-HADGEPIAATRTLRDAVSELLWRGVDVLPVGDGDGHNTRRITLD 302
Cdd:PRK09536 235 afdarTAVGTDPATGAPTVTPLPDPDRTEAAADTRvHVVGGGQPAARAVSRLVAAGASVSVGPVPEGDTAAETAARVGCE 314
|
....*....
gi 1861108599 303 AIRAHARKP 311
Cdd:PRK09536 315 AVTVPPFKP 323
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
18-226 |
2.09e-30 |
|
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: 114.63 E-value: 2.09e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 18 DDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGVDTATVAPEQLRRGIGYAIQGHGLFpHWSVARNIA 97
Cdd:cd03253 18 KDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGVVPQDTVLF-NDTIGYNIR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 98 tvprlLGWP------------ADRIDARVNELLDLFHLAPAEFADKlpheLSGGQQQRVGVARALAAEPAMLLMDEPFGA 165
Cdd:cd03253 97 -----YGRPdatdeevieaakAAQIHDKIMRFPDGYDTIVGERGLK----LSGGEKQRVAIARAILKNPPILLLDEATSA 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1861108599 166 LDPIIRNKAQDDLFALQRrlGITVVIVTHDIEEALKlGDTIAVMDAGRLLQVASPAEILGK 226
Cdd:cd03253 168 LDTHTEREIQAALRDVSK--GRTTIVIAHRLSTIVN-ADKIIVLKDGRIVERGTHEELLAK 225
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
8-239 |
2.44e-30 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 115.02 E-value: 2.44e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 8 GKRFGDIVAVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGVDTATV----APEQLRRGI-----G 78
Cdd:PRK11701 13 TKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRdlyaLSEAERRRLlrtewG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 79 YAIQG--HGLFPHWSVARNIATVPRLLGWPA-DRIDARVNELLDLFHLAPAEFaDKLPHELSGGQQQRVGVARALAAEPA 155
Cdd:PRK11701 93 FVHQHprDGLRMQVSAGGNIGERLMAVGARHyGDIRATAGDWLERVEIDAARI-DDLPTTFSGGMQQRLQIARNLVTHPR 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 156 MLLMDEPFGALDPIIRNKAQDDLFALQRRLGITVVIVTHDIEEALKLGDTIAVMDAGRLLQVASPAEILGKPAAGVVEQL 235
Cdd:PRK11701 172 LVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVVESGLTDQVLDDPQHPYTQLL 251
|
....
gi 1861108599 236 VAGV 239
Cdd:PRK11701 252 VSSV 255
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1-198 |
2.63e-30 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 114.04 E-value: 2.63e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 1 MIEIERAGKRFGDIVAVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGVDTATVAPEQLRRGIGYA 80
Cdd:PRK10247 7 LLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYC 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 81 IQGHGLFPHwSVARNIATVPRLLGWPADRidARVNELLDLFHLaPAEFADKLPHELSGGQQQRVGVARALAAEPAMLLMD 160
Cdd:PRK10247 87 AQTPTLFGD-TVYDNLIFPWQIRNQQPDP--AIFLDDLERFAL-PDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLD 162
|
170 180 190
....*....|....*....|....*....|....*...
gi 1861108599 161 EPFGALDPIIRNKAQDDLFALQRRLGITVVIVTHDIEE 198
Cdd:PRK10247 163 EITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDE 200
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
4-214 |
3.23e-30 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 114.77 E-value: 3.23e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 4 IERAGKRFGDIVAVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRidgvdtATVAP-EQLRRGIGYAIQ 82
Cdd:PRK11247 15 LNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELL------AGTAPlAEAREDTRLMFQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 83 GHGLFPHWSVARNIAtvprlLGWPAD-RIDARvnELLDLFHLApaEFADKLPHELSGGQQQRVGVARALAAEPAMLLMDE 161
Cdd:PRK11247 89 DARLLPWKKVIDNVG-----LGLKGQwRDAAL--QALAAVGLA--DRANEWPAALSGGQKQRVALARALIHRPGLLLLDE 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1861108599 162 PFGALDPIIRNKAQDDLFALQRRLGITVVIVTHDIEEALKLGDTIAVMDAGRL 214
Cdd:PRK11247 160 PLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
13-227 |
4.81e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 114.79 E-value: 4.81e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 13 DIVAVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDG--VDTATVAPEQLRRGIGYAIQG--HGLFP 88
Cdd:PRK13639 14 GTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGepIKYDKKSLLEVRKTVGIVFQNpdDQLFA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 89 HwSVARNIATVPRLLGWPADRIDARVNELLDLFHLApaEFADKLPHELSGGQQQRVGVARALAAEPAMLLMDEPFGALDP 168
Cdd:PRK13639 94 P-TVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGME--GFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDP 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1861108599 169 IIRNKAQDDLFALQRRlGITVVIVTHDIEEALKLGDTIAVMDAGRLLQVASPAEILGKP 227
Cdd:PRK13639 171 MGASQIMKLLYDLNKE-GITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDI 228
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
17-279 |
1.65e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 113.67 E-value: 1.65e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 17 VDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGVDTATVAPEQLRRGIGYAIQG-HGLFPHWSVARN 95
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIGMVFQNpDNQFVGATVEDD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 96 IATVPRLLGWPADRIDARVNELLDLFHLApaEFADKLPHELSGGQQQRVGVARALAAEPAMLLMDEPFGALDPIIRNKAQ 175
Cdd:PRK13650 103 VAFGLENKGIPHEEMKERVNEALELVGMQ--DFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELI 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 176 DDLFALQRRLGITVVIVTHDIEEaLKLGDTIAVMDAGRLLQVASPAEILGKPaagvvEQLVA-GVDRPlrlLALTPIDAV 254
Cdd:PRK13650 181 KTIKGIRDDYQMTVISITHDLDE-VALSDRVLVMKNGQVESTSTPRELFSRG-----NDLLQlGLDIP---FTTSLVQSL 251
|
250 260
....*....|....*....|....*
gi 1861108599 255 AEPGHADGEPIAATRTLRDAVSELL 279
Cdd:PRK13650 252 RQNGYDLPEGYLTEKELEEQLWELI 276
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1-223 |
2.87e-29 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 112.55 E-value: 2.87e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 1 MIEIERAGKRFGDIVAVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGVDTATVAPEQL---RRGI 77
Cdd:PRK11831 7 LVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLytvRKRM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 78 GYAIQGHGLFPHWSVARNIATVPR-LLGWPADRIDARVNELLDLFHLAPAefADKLPHELSGGQQQRVGVARALAAEPAM 156
Cdd:PRK11831 87 SMLFQSGALFTDMNVFDNVAYPLReHTQLPAPLLHSTVMMKLEAVGLRGA--AKLMPSELSGGMARRAALARAIALEPDL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1861108599 157 LLMDEPFGALDPIIRNKAQDDLFALQRRLGITVVIVTHDIEEALKLGDTIAVMDAGRLLQVASPAEI 223
Cdd:PRK11831 165 IMFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQAL 231
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
17-226 |
4.53e-29 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 116.29 E-value: 4.53e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 17 VDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGVDTATVAPEQLRRGIGYAIQGHGLFPHwSVARNI 96
Cdd:TIGR01842 334 LRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGKHIGYLPQDVELFPG-TVAENI 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 97 ATVprllgwpADRIDARvnELLDLFHLAPA-EFADKLPH-----------ELSGGQQQRVGVARALAAEPAMLLMDEPFG 164
Cdd:TIGR01842 413 ARF-------GENADPE--KIIEAAKLAGVhELILRLPDgydtvigpggaTLSGGQRQRIALARALYGDPKLVVLDEPNS 483
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1861108599 165 ALDPIIRNKAQDDLFALQRRlGITVVIVTHDIeEALKLGDTIAVMDAGRLLQVASPAEILGK 226
Cdd:TIGR01842 484 NLDEEGEQALANAIKALKAR-GITVVVITHRP-SLLGCVDKILVLQDGRIARFGERDEVLAK 543
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
16-227 |
7.03e-29 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 112.88 E-value: 7.03e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 16 AVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGVDTATVAPEQL---RRGIGYAIQG--HGLFPHW 90
Cdd:PRK15079 36 AVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWravRSDIQMIFQDplASLNPRM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 91 SVARNIAT-----VPRLlgwPADRIDARVNELLDLFHLAPaEFADKLPHELSGGQQQRVGVARALAAEPAMLLMDEPFGA 165
Cdd:PRK15079 116 TIGEIIAEplrtyHPKL---SRQEVKDRVKAMMLKVGLLP-NLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSA 191
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1861108599 166 LDPIIRNKAQDDLFALQRRLGITVVIVTHDIEEALKLGDTIAVMDAGRLLQVASPAEILGKP 227
Cdd:PRK15079 192 LDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNP 253
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
16-265 |
9.26e-29 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 116.11 E-value: 9.26e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 16 AVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGVDTATVAPEQL---RRGIGYAIQG--HGLFPHW 90
Cdd:PRK10261 339 AVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLqalRRDIQFIFQDpyASLDPRQ 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 91 SVARNIATVPRLLGW-PADRIDARVNELLDLFHLAPaEFADKLPHELSGGQQQRVGVARALAAEPAMLLMDEPFGALDPI 169
Cdd:PRK10261 419 TVGDSIMEPLRVHGLlPGKAAAARVAWLLERVGLLP-EHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVS 497
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 170 IRNKAQDDLFALQRRLGITVVIVTHDIEEALKLGDTIAVMDAGRLLQVASPAEILGKPAAGVVEQLVAGVdrplrllalt 249
Cdd:PRK10261 498 IRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENPQHPYTRKLMAAV---------- 567
|
250
....*....|....*.
gi 1861108599 250 pidAVAEPGHADGEPI 265
Cdd:PRK10261 568 ---PVADPSRQRPQRV 580
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
9-215 |
1.42e-28 |
|
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: 109.73 E-value: 1.42e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 9 KRFGDIVAVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGVDTATVAPEQLRRgIGYAI-QGHGLF 87
Cdd:cd03267 29 RKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLRR-IGVVFgQKTQLW 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 88 PHWSVARNIATVPRLLGWPADRIDARVNELLDLFHLAPaeFADKLPHELSGGQQQRVGVARALAAEPAMLLMDEPFGALD 167
Cdd:cd03267 108 WDLPVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEE--LLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLD 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1861108599 168 PIIRNKAQDDLFALQRRLGITVVIVTHDIEEALKLGDTIAVMDAGRLL 215
Cdd:cd03267 186 VVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLL 233
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
15-209 |
2.39e-28 |
|
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: 114.31 E-value: 2.39e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 15 VAVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGVDTATVAPEQLRRGIGYAIQGHGLFPHwSVAR 94
Cdd:TIGR02857 336 PALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAG-TIAE 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 95 NIAtvprlLGWPadriDARVNELLDLFHLAPA-EFADKLP-----------HELSGGQQQRVGVARALAAEPAMLLMDEP 162
Cdd:TIGR02857 415 NIR-----LARP----DASDAEIREALERAGLdEFVAALPqgldtpigeggAGLSGGQAQRLALARAFLRDAPLLLLDEP 485
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1861108599 163 FGALDPIIRNKAQDDLFALQRrlGITVVIVTHDIEEALkLGDTIAVM 209
Cdd:TIGR02857 486 TAHLDAETEAEVLEALRALAQ--GRTVLLVTHRLALAA-LADRIVVL 529
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1-214 |
3.54e-28 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 108.42 E-value: 3.54e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 1 MIEIERAGKRF-GDIVAVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGVDTATVAPEQ---LRRG 76
Cdd:PRK10908 1 MIRFEHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREvpfLRRQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 77 IGYAIQGHGLFPHWSVARNIATVPRLLGWPADRIDARVNELLDLFHLApaEFADKLPHELSGGQQQRVGVARALAAEPAM 156
Cdd:PRK10908 81 IGMIFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLL--DKAKNFPIQLSGGEQQRVGIARAVVNKPAV 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1861108599 157 LLMDEPFGALDP-----IIRnkaqddLFALQRRLGITVVIVTHDIEEALKLGDTIAVMDAGRL 214
Cdd:PRK10908 159 LLADEPTGNLDDalsegILR------LFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
13-237 |
5.78e-28 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 108.63 E-value: 5.78e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 13 DIVAVDDVSLTMQRGTITALVGASGSGKS----TLLRMINRLIAPTSGTIRIDGVdtaTVAPEQLR-RGIGYAIQG--HG 85
Cdd:PRK10418 15 AQPLVHGVSLTLQRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGRVLLDGK---PVAPCALRgRKIATIMQNprSA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 86 LFPHWSVARNIATVPRLLGWPADriDARVNELLDLFHLA-PAEFADKLPHELSGGQQQRVGVARALAAEPAMLLMDEPFG 164
Cdd:PRK10418 92 FNPLHTMHTHARETCLALGKPAD--DATLTAALEAVGLEnAARVLKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTT 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1861108599 165 ALDPIIRNKAQDDLFALQRRLGITVVIVTHDIEEALKLGDTIAVMDAGRLLQVASPAEILGKPAAGVVEQLVA 237
Cdd:PRK10418 170 DLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPKHAVTRSLVS 242
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
16-220 |
7.81e-28 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 113.96 E-value: 7.81e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 16 AVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGVDTATvAPEQLRRGIGYAIQGHGLFPHWSVARN 95
Cdd:TIGR01257 945 AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIET-NLDAVRQSLGMCPQHNILFHHLTVAEH 1023
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 96 IATVPRLLGWPADRIDARVNELLD---LFHLAPAEFADklpheLSGGQQQRVGVARALAAEPAMLLMDEPFGALDPIIRN 172
Cdd:TIGR01257 1024 ILFYAQLKGRSWEEAQLEMEAMLEdtgLHHKRNEEAQD-----LSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRR 1098
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1861108599 173 KAQDDLfaLQRRLGITVVIVTHDIEEALKLGDTIAVMDAGRLLQVASP 220
Cdd:TIGR01257 1099 SIWDLL--LKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTP 1144
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
9-239 |
8.68e-28 |
|
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: 108.38 E-value: 8.68e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 9 KRFGDIVAVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGVDTATVA----PEQLRR-------GI 77
Cdd:TIGR02323 11 KSYGGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMRSGAELElyqlSEAERRrlmrtewGF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 78 GYAIQGHGLFPHWSVARNIATVPRLLGWPA-DRIDARVNELLDLFHLAPAEFaDKLPHELSGGQQQRVGVARALAAEPAM 156
Cdd:TIGR02323 91 VHQNPRDGLRMRVSAGANIGERLMAIGARHyGNIRATAQDWLEEVEIDPTRI-DDLPRAFSGGMQQRLQIARNLVTRPRL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 157 LLMDEPFGALDPIIRNKAQDDLFALQRRLGITVVIVTHDIEEALKLGDTIAVMDAGRLLQVASPAEILGKPAAGVVEQLV 236
Cdd:TIGR02323 170 VFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRVVESGLTDQVLDDPQHPYTQLLV 249
|
...
gi 1861108599 237 AGV 239
Cdd:TIGR02323 250 SSI 252
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
13-225 |
9.25e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 109.03 E-value: 9.25e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 13 DIVAVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGVDTATVAPEQLRRGIGYAIQG-HGLFPHWS 91
Cdd:PRK13642 19 DVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIGMVFQNpDNQFVGAT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 92 VARNIATVPRLLGWPADRIDARVNELLDLFHLApaEFADKLPHELSGGQQQRVGVARALAAEPAMLLMDEPFGALDPIIR 171
Cdd:PRK13642 99 VEDDVAFGMENQGIPREEMIKRVDEALLAVNML--DFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGR 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1861108599 172 NKAQDDLFALQRRLGITVVIVTHDIEEALKlGDTIAVMDAGRLLQVASPAEILG 225
Cdd:PRK13642 177 QEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELFA 229
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
1-218 |
2.44e-27 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 106.40 E-value: 2.44e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 1 MIEIERAGKRFGD----IVAVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGVDTATVAPEQ---L 73
Cdd:PRK10584 6 IVEVHHLKKSVGQgeheLSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEArakL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 74 R-RGIGYAIQGHGLFPHWSVARNIaTVPRLLGWPADRiDARVNELLDLFHLAPAEFADKLPHELSGGQQQRVGVARALAA 152
Cdd:PRK10584 86 RaKHVGFVFQSFMLIPTLNALENV-ELPALLRGESSR-QSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNG 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1861108599 153 EPAMLLMDEPFGALDPIIRNKAQDDLFALQRRLGITVVIVTHDIEEALKLGDTIAVMDaGRLLQVA 218
Cdd:PRK10584 164 RPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLAARCDRRLRLVN-GQLQEEA 228
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
16-224 |
2.77e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 108.25 E-value: 2.77e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 16 AVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRI----DGVDTATVAPE-------------------- 71
Cdd:PRK13651 22 ALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWifkdEKNKKKTKEKEkvleklviqktrfkkikkik 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 72 QLRRGIGYAIQ--GHGLFPHwSVARNIATVPRLLGWPADRIDARVNELLDLFHLaPAEFADKLPHELSGGQQQRVGVARA 149
Cdd:PRK13651 102 EIRRRVGVVFQfaEYQLFEQ-TIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGL-DESYLQRSPFELSGGQKRRVALAGI 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1861108599 150 LAAEPAMLLMDEPFGALDPIIRNKAQDDLFALQRRlGITVVIVTHDIEEALKLGDTIAVMDAGRLLQVASPAEIL 224
Cdd:PRK13651 180 LAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQ-GKTIILVTHDLDNVLEWTKRTIFFKDGKIIKDGDTYDIL 253
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
16-264 |
3.11e-27 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 111.21 E-value: 3.11e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 16 AVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGVDTATVAPEQLRRGIGYAIQGHGLFPHwSVARN 95
Cdd:PRK13657 350 GVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAVVFQDAGLFNR-SIEDN 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 96 IatvprLLGWPadriDARVNELLDLFHLAPA-EFADKLPH-----------ELSGGQQQRVGVARALAAEPAMLLMDEPF 163
Cdd:PRK13657 429 I-----RVGRP----DATDEEMRAAAERAQAhDFIERKPDgydtvvgergrQLSGGERQRLAIARALLKDPPILILDEAT 499
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 164 GALDPIIRNKAQDDLFALQRrlGITVVIVTH---DIEEAlklgDTIAVMDAGRLLQvaspaeilgkpaAGVVEQLVAGVD 240
Cdd:PRK13657 500 SALDVETEAKVKAALDELMK--GRTTFIIAHrlsTVRNA----DRILVFDNGRVVE------------SGSFDELVARGG 561
|
250 260
....*....|....*....|....*..
gi 1861108599 241 RPLRLLA---LTPIDAVAEPGHADGEP 264
Cdd:PRK13657 562 RFAALLRaqgMLQEDERRKQPAAEGAN 588
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
10-200 |
4.40e-27 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 104.62 E-value: 4.40e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 10 RFGDIVAVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGVDTATVAPEQLRRGIGYAIQ-----GH 84
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQRSEVPDSLPLTvrdlvAM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 85 GLFPHwsvarniatvPRLLGWPADRIDARVNELLDLFHLapAEFADKLPHELSGGQQQRVGVARALAAEPAMLLMDEPFG 164
Cdd:NF040873 81 GRWAR----------RGLWRRLTRDDRAAVDDALERVGL--ADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTT 148
|
170 180 190
....*....|....*....|....*....|....*....
gi 1861108599 165 ALDPiirnKAQDDLFALQRRL---GITVVIVTHDIEEAL 200
Cdd:NF040873 149 GLDA----ESRERIIALLAEEharGATVVVVTHDLELVR 183
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
16-214 |
5.87e-27 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 110.11 E-value: 5.87e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 16 AVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGVDTATVAPEQ-LRRGIGYAI---QGHGLFPHWS 91
Cdd:COG1129 267 VVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDaIRAGIAYVPedrKGEGLVLDLS 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 92 VARNI--ATVPRLLGWP---ADRIDARVNELLDLFHLAPAEfADKLPHELSGGQQQRVGVARALAAEPAMLLMDEPFGAL 166
Cdd:COG1129 347 IRENItlASLDRLSRGGlldRRRERALAEEYIKRLRIKTPS-PEQPVGNLSGGNQQKVVLAKWLATDPKVLILDEPTRGI 425
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1861108599 167 DpiIRNKAqdDLFALQRRL---GITVVIVTHDIEEALKLGDTIAVMDAGRL 214
Cdd:COG1129 426 D--VGAKA--EIYRLIRELaaeGKAVIVISSELPELLGLSDRILVMREGRI 472
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
16-238 |
8.76e-27 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 106.03 E-value: 8.76e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 16 AVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGvdtatvapEQLRRG-IGYAIQG-HGLFPHWSVA 93
Cdd:PRK15112 28 AVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDD--------HPLHFGdYSYRSQRiRMIFQDPSTS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 94 RN-------IATVPRLLGW---PADRiDARVNELLDLFHLAPaEFADKLPHELSGGQQQRVGVARALAAEPAMLLMDEPF 163
Cdd:PRK15112 100 LNprqrisqILDFPLRLNTdlePEQR-EKQIIETLRQVGLLP-DHASYYPHMLAPGQKQRLGLARALILRPKVIIADEAL 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1861108599 164 GALDPIIRNKAQDDLFALQRRLGITVVIVTHDIEEALKLGDTIAVMDAGRLLQVASPAEILGKPAAGVVEQLVAG 238
Cdd:PRK15112 178 ASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVLASPLHELTKRLIAG 252
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1-250 |
1.19e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 105.84 E-value: 1.19e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 1 MIEIERAGKRFGD-IVAVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGVDTATVAPEQ-LRRGIG 78
Cdd:PRK13644 1 MIRLENVSYSYPDgTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKLQgIRKLVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 79 YAIQG-HGLFPHWSVARNIATVPRLLGWPADRIDARVNELLDLFHLapAEFADKLPHELSGGQQQRVGVARALAAEPAML 157
Cdd:PRK13644 81 IVFQNpETQFVGRTVEEDLAFGPENLCLPPIEIRKRVDRALAEIGL--EKYRHRSPKTLSGGQGQCVALAGILTMEPECL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 158 LMDEPFGALDPIIRNKAQDDLFALQRRlGITVVIVTHDIEEaLKLGDTIAVMDAGRLLQVASPAEILGKPAagvveqlva 237
Cdd:PRK13644 159 IFDEVTSMLDPDSGIAVLERIKKLHEK-GKTIVYITHNLEE-LHDADRIIVMDRGKIVLEGEPENVLSDVS--------- 227
|
250
....*....|...
gi 1861108599 238 gvdrpLRLLALTP 250
Cdd:PRK13644 228 -----LQTLGLTP 235
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
17-237 |
1.41e-26 |
|
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes a multidomain ABC transporter subunit that is one of three protein families associated with some regularity with a distinctive family of putative bacteriocins. It includes a bacteriocin-processing peptidase domain at the N-terminus. Model TIGR03793 describes a conserved propeptide region for this bacteriocin family, unusual because it shows obvious homology a region of the enzyme nitrile hydratase up to the classic Gly-Gly cleavage motif. This family is therefore predicted to be a subunit of a bacteriocin processing and export system characteristic to this system that we designate NHLM, Nitrile Hydratase Leader Microcin. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274788 [Multi-domain] Cd Length: 710 Bit Score: 109.65 E-value: 1.41e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 17 VDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGVDTATVAPEQLRRGIGYAIQGHGLFpHWSVARNI 96
Cdd:TIGR03796 495 IENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIPREEIPREVLANSVAMVDQDIFLF-EGTVRDNL 573
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 97 A----TVPRllgwpADRIDA-RVNELLDLFHLAPAEFADKLPH---ELSGGQQQRVGVARALAAEPAMLLMDEPFGALDP 168
Cdd:TIGR03796 574 TlwdpTIPD-----ADLVRAcKDAAIHDVITSRPGGYDAELAEggaNLSGGQRQRLEIARALVRNPSILILDEATSALDP 648
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1861108599 169 IIRNKAQDDLfalqRRLGITVVIVTH---DIEEAlklgDTIAVMDAGRLLQVASPAEILGKPaaGVVEQLVA 237
Cdd:TIGR03796 649 ETEKIIDDNL----RRRGCTCIIVAHrlsTIRDC----DEIIVLERGKVVQRGTHEELWAVG--GAYARLIR 710
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-213 |
1.66e-26 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 105.17 E-value: 1.66e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 1 MIEIERAGKRFG-----DIVAVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGVDTATVAPEQLRR 75
Cdd:COG1101 1 MLELKNLSKTFNpgtvnEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 76 GIGYAIQG--HGLFPHWSVARNIA-----TVPRLLGW---PADRidARVNELLDLFHL-------APAEFadklpheLSG 138
Cdd:COG1101 81 YIGRVFQDpmMGTAPSMTIEENLAlayrrGKRRGLRRgltKKRR--ELFRELLATLGLglenrldTKVGL-------LSG 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1861108599 139 GQQQRVGVARALAAEPAMLLMDEPFGALDPiirnKAQDDLFALQRRL----GITVVIVTHDIEEALKLGDTIAVMDAGR 213
Cdd:COG1101 152 GQRQALSLLMATLTKPKLLLLDEHTAALDP----KTAALVLELTEKIveenNLTTLMVTHNMEQALDYGNRLIMMHEGR 226
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
16-242 |
1.83e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 105.22 E-value: 1.83e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 16 AVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGVDTATVAPEQLRRGIGYAIQG-HGLFPHWSVAR 94
Cdd:PRK13648 24 TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGIVFQNpDNQFVGSIVKY 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 95 NIATVPRLLGWPADRIDARVNELLDLFHLApaEFADKLPHELSGGQQQRVGVARALAAEPAMLLMDEPFGALDPiirnKA 174
Cdd:PRK13648 104 DVAFGLENHAVPYDEMHRRVSEALKQVDML--ERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDP----DA 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1861108599 175 QDDLFALQRRL----GITVVIVTHDIEEALKlGDTIAVMDAGRLLQVASPAEILgKPAAGVVEqlvAGVDRP 242
Cdd:PRK13648 178 RQNLLDLVRKVksehNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIF-DHAEELTR---IGLDLP 244
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
2-234 |
3.81e-26 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 108.67 E-value: 3.81e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 2 IEIERAGKRFGDIVAVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGVDTA------TVAPEqlrr 75
Cdd:NF033858 2 ARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMAdarhrrAVCPR---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 76 gIGYAIQGHG--LFPHWSVARNIATVPRLLGWPADRIDARVNELLDLFHLAPaeFADKLPHELSGGQQQRVGVARALAAE 153
Cdd:NF033858 78 -IAYMPQGLGknLYPTLSVFENLDFFGRLFGQDAAERRRRIDELLRATGLAP--FADRPAGKLSGGMKQKLGLCCALIHD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 154 PAMLLMDEPFGALDPIIRnkAQ-----DDLFAlqRRLGITVVIVTHDIEEALKLgDTIAVMDAGRLLQVASPAEILGKPA 228
Cdd:NF033858 155 PDLLILDEPTTGVDPLSR--RQfweliDRIRA--ERPGMSVLVATAYMEEAERF-DWLVAMDAGRVLATGTPAELLARTG 229
|
....*.
gi 1861108599 229 AGVVEQ 234
Cdd:NF033858 230 ADTLEA 235
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-228 |
2.87e-25 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 101.11 E-value: 2.87e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 1 MIEIERAGKRFGDIVAVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGVD-TATVAPEQLRRGIGY 79
Cdd:PRK11614 5 MLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDiTDWQTAKIMREAVAI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 80 AIQGHGLFPHWSVARNIAtvprLLGWPADR--IDARVNELLDLFhlaPAEFADKLPHE--LSGGQQQRVGVARALAAEPA 155
Cdd:PRK11614 85 VPEGRRVFSRMTVEENLA----MGGFFAERdqFQERIKWVYELF---PRLHERRIQRAgtMSGGEQQMLAIGRALMSQPR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1861108599 156 MLLMDEPFGALDPIIRNKAQDDLFALqRRLGITVVIVTHDIEEALKLGDTIAVMDAGRLLQVASPAEILGKPA 228
Cdd:PRK11614 158 LLLLDEPSLGLAPIIIQQIFDTIEQL-REQGMTIFLVEQNANQALKLADRGYVLENGHVVLEDTGDALLANEA 229
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
15-216 |
4.42e-25 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 104.93 E-value: 4.42e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 15 VAVDDVSLTMQRGTITALVGASGSGKSTLLrmiNRLI--APTSGTIRIDGVDTATVAPEQLRRGIGYAIQGHGLFpHWSV 92
Cdd:PRK11174 364 TLAGPLNFTLPAGQRIALVGPSGAGKTSLL---NALLgfLPYQGSLKINGIELRELDPESWRKHLSWVGQNPQLP-HGTL 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 93 ARNIatvprLLGWPaDRIDARVNELLDLFHLApaEFADKLPH-----------ELSGGQQQRVGVARALAAEPAMLLMDE 161
Cdd:PRK11174 440 RDNV-----LLGNP-DASDEQLQQALENAWVS--EFLPLLPQgldtpigdqaaGLSVGQAQRLALARALLQPCQLLLLDE 511
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1861108599 162 PFGALDpiiRNKAQDDLFALQR-RLGITVVIVTHDIEEaLKLGDTIAVMDAGRLLQ 216
Cdd:PRK11174 512 PTASLD---AHSEQLVMQALNAaSRRQTTLMVTHQLED-LAQWDQIWVMQDGQIVQ 563
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
2-227 |
9.68e-25 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 101.52 E-value: 9.68e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 2 IEIERAGkrfGDIVAVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAP----TSGTIRIDGVDTATVAPEQLRRGI 77
Cdd:COG4170 11 IEIDTPQ---GRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDnwhvTADRFRWNGIDLLKLSPRERRKII 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 78 GYAI-------QGHgLFPHWSVARNIATV---PRLLGWPADRIDARVNELLDLFHLA----PAEFADKLPHELSGGQQQR 143
Cdd:COG4170 88 GREIamifqepSSC-LDPSAKIGDQLIEAipsWTFKGKWWQRFKWRKKRAIELLHRVgikdHKDIMNSYPHELTEGECQK 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 144 VGVARALAAEPAMLLMDEPFGALDPIirNKAQddLFALQRRL----GITVVIVTHDIEEALKLGDTIAVMDAGRLLQVAS 219
Cdd:COG4170 167 VMIAMAIANQPRLLIADEPTNAMEST--TQAQ--IFRLLARLnqlqGTSILLISHDLESISQWADTITVLYCGQTVESGP 242
|
....*...
gi 1861108599 220 PAEILGKP 227
Cdd:COG4170 243 TEQILKSP 250
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
11-239 |
1.47e-24 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 100.17 E-value: 1.47e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 11 FGDIVAVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSG-----TIRIDGVDTATVAPE-QLRRGIGYAIQGH 84
Cdd:PRK14271 31 FAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIFNYRDVlEFRRRVGMLFQRP 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 85 GLFPhWSVARNIatvprLLGWPADRI----------DARVNELlDLFHLAPAEFADKlPHELSGGQQQRVGVARALAAEP 154
Cdd:PRK14271 111 NPFP-MSIMDNV-----LAGVRAHKLvprkefrgvaQARLTEV-GLWDAVKDRLSDS-PFRLSGGQQQLLCLARTLAVNP 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 155 AMLLMDEPFGALDPIIRNKAQDDLFALQRRLgiTVVIVTHDIEEALKLGDTIAVMDAGRLLQVASPAEILGKPAAGVVEQ 234
Cdd:PRK14271 183 EVLLLDEPTSALDPTTTEKIEEFIRSLADRL--TVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKHAETAR 260
|
....*
gi 1861108599 235 LVAGV 239
Cdd:PRK14271 261 YVAGL 265
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
15-223 |
1.67e-24 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 103.18 E-value: 1.67e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 15 VAVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGVDTATVAPEQLRR-GIGYaI----QGHGLFPH 89
Cdd:COG3845 272 PALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRlGVAY-IpedrLGRGLVPD 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 90 WSVARNIA----TVPRLLGWP---ADRIDARVNELLDLFHLAPAEfADKLPHELSGGQQQRVGVARALAAEPAMLLMDEP 162
Cdd:COG3845 351 MSVAENLIlgryRRPPFSRGGfldRKAIRAFAEELIEEFDVRTPG-PDTPARSLSGGNQQKVILARELSRDPKLLIAAQP 429
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1861108599 163 FGALDP----IIRNKaqddLFALqRRLGITVVIVTHDIEEALKLGDTIAVMDAGRLLQVASPAEI 223
Cdd:COG3845 430 TRGLDVgaieFIHQR----LLEL-RDAGAAVLLISEDLDEILALSDRIAVMYEGRIVGEVPAAEA 489
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1-215 |
8.76e-24 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 97.78 E-value: 8.76e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 1 MIEIERAGKRFGDIVAVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIA--PTSGTiRIDGVDTATVAPEQLRRGI- 77
Cdd:PRK09984 4 IIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITgdKSAGS-HIELLGRTVQREGRLARDIr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 78 ------GYAIQGHGLFPHWSVARNI-----ATVP---RLLGW--PADRIDArvneLLDLFHLAPAEFADKLPHELSGGQQ 141
Cdd:PRK09984 83 ksrantGYIFQQFNLVNRLSVLENVligalGSTPfwrTCFSWftREQKQRA----LQALTRVGMVHFAHQRVSTLSGGQQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1861108599 142 QRVGVARALAAEPAMLLMDEPFGALDPIIRNKAQDDLFALQRRLGITVVIVTHDIEEALKLGDTIAVMDAGRLL 215
Cdd:PRK09984 159 QRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVF 232
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
18-213 |
9.51e-24 |
|
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: 101.44 E-value: 9.51e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 18 DDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGVDTATVAPEQLRRGIGYAIQGHGLFPHwSVARNIA 97
Cdd:COG5265 375 KGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFND-TIAYNIA 453
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 98 tvprlLGWPaDRIDARVNELLDLFHLapAEFADKLPH-----------ELSGGQQQRVGVARALAAEPAMLLMDEPFGAL 166
Cdd:COG5265 454 -----YGRP-DASEEEVEAAARAAQI--HDFIESLPDgydtrvgerglKLSGGEKQRVAIARTLLKNPPILIFDEATSAL 525
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1861108599 167 DPIIRNKAQDDLFALQRrlGITVVIVTH---DIEEAlklgDTIAVMDAGR 213
Cdd:COG5265 526 DSRTERAIQAALREVAR--GRTTLVIAHrlsTIVDA----DEILVLEAGR 569
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
14-271 |
9.89e-24 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 101.47 E-value: 9.89e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 14 IVAVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDG----------VDTATVAPEQLRRGIGYAIQG 83
Cdd:PRK10261 29 IAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKmllrrrsrqvIELSEQSAAQMRHVRGADMAM 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 84 ------HGLFPHWSVARNIATVPRL-LGWPADRIDARVNELLDLFHLAPAE-FADKLPHELSGGQQQRVGVARALAAEPA 155
Cdd:PRK10261 109 ifqepmTSLNPVFTVGEQIAESIRLhQGASREEAMVEAKRMLDQVRIPEAQtILSRYPHQLSGGMRQRVMIAMALSCRPA 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 156 MLLMDEPFGALDPIIRNKAQDDLFALQRRLGITVVIVTHDIEEALKLGDTIAVMDAGRLLQVASPAEILGKPAAGVVEQL 235
Cdd:PRK10261 189 VLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQIFHAPQHPYTRAL 268
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1861108599 236 VAGVDR---------PLRLlaltPIDAVAEPGH----------ADGEPIAATRTL 271
Cdd:PRK10261 269 LAAVPQlgamkgldyPRRF----PLISLEHPAKqeppieqdtvVDGEPILQVRNL 319
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
10-227 |
1.10e-23 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 97.37 E-value: 1.10e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 10 RFGDIVAVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGVDTATVAPEQL-RRGIGYAIQGHGLFP 88
Cdd:PRK11300 14 RFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIaRMGVVRTFQHVRLFR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 89 HWSVARNI----------ATVPRLLGWPADRIDARvnELLD-----LFHLAPAEFADKLPHELSGGQQQRVGVARALAAE 153
Cdd:PRK11300 94 EMTVIENLlvaqhqqlktGLFSGLLKTPAFRRAES--EALDraatwLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQ 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1861108599 154 PAMLLMDEPFGALDPiirnKAQDDLFALQRRL----GITVVIVTHDIEEALKLGDTIAVMDAGRLLQVASPAEILGKP 227
Cdd:PRK11300 172 PEILMLDEPAAGLNP----KETKELDELIAELrnehNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEIRNNP 245
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
20-224 |
1.81e-23 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 96.78 E-value: 1.81e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 20 VSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGVDTAT---------VA--PEQLRRGIGYAIQ---GHG 85
Cdd:PRK10575 30 LSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESwsskafarkVAylPQQLPAAEGMTVRelvAIG 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 86 LFP-HWSVARNIAtvprllgwpADRidARVNELLDLFHLAPaeFADKLPHELSGGQQQRVGVARALAAEPAMLLMDEPFG 164
Cdd:PRK10575 110 RYPwHGALGRFGA---------ADR--EKVEEAISLVGLKP--LAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTS 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1861108599 165 ALDPiirnKAQDDLFALQRRL----GITVVIVTHDIEEALKLGDTIAVMDAGRLLQVASPAEIL 224
Cdd:PRK10575 177 ALDI----AHQVDVLALVHRLsqerGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELM 236
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
16-220 |
1.98e-23 |
|
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: 95.64 E-value: 1.98e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 16 AVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGVDTATVAPEQLRRGIGYAIQGHGLFPHwSVARN 95
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRISIIPQDPVLFSG-TIRSN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 96 IAtvprllgwPADRI-DARVNELLDLFHLAP--AEFADKLPHE-------LSGGQQQRVGVARALAAEPAMLLMDEPFGA 165
Cdd:cd03244 98 LD--------PFGEYsDEELWQALERVGLKEfvESLPGGLDTVveeggenLSVGQRQLLCLARALLRKSKILVLDEATAS 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1861108599 166 LDPIIRNKAQDdlfALQRRL-GITVVIVTHDIEEALKLgDTIAVMDAGRLLQVASP 220
Cdd:cd03244 170 VDPETDALIQK---TIREAFkDCTVLTIAHRLDTIIDS-DRILVLDKGRVVEFDSP 221
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-195 |
3.34e-23 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 99.37 E-value: 3.34e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 4 IERAGKRFGDIVAVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIdgvdtatvaPEQLRrgIGYAIQG 83
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSI---------PKGLR--IGYLPQE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 84 HGLFPHWSVARNIAT-VPRLL----------------------------------GWpadRIDARVNELLDLFHLAPAEF 128
Cdd:COG0488 70 PPLDDDLTVLDTVLDgDAELRaleaeleeleaklaepdedlerlaelqeefealgGW---EAEARAEEILSGLGFPEEDL 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1861108599 129 aDKLPHELSGGQQQRVGVARALAAEPAMLLMDEPFGALdpiirnkaqdDLFA-------LQRRLGiTVVIVTHD 195
Cdd:COG0488 147 -DRPVSELSGGWRRRVALARALLSEPDLLLLDEPTNHL----------DLESiewleefLKNYPG-TVLVVSHD 208
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-242 |
4.12e-23 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 96.23 E-value: 4.12e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 1 MIEIERAGKRFGDIVAVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDG--VDTATVAPEQLRRGIG 78
Cdd:PRK13638 1 MLATSDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGkpLDYSKRGLLALRQQVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 79 YAIQG--HGLFpHWSVARNIATVPRLLGWPADRIDARVNELLDLfhLAPAEFADKLPHELSGGQQQRVGVARALAAEPAM 156
Cdd:PRK13638 81 TVFQDpeQQIF-YTDIDSDIAFSLRNLGVPEAEITRRVDEALTL--VDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 157 LLMDEPFGALDPiiRNKAQddLFALQRRL---GITVVIVTHDIEEALKLGDTIAVMDAGRLLQVASPAEILGKpaAGVVE 233
Cdd:PRK13638 158 LLLDEPTAGLDP--AGRTQ--MIAIIRRIvaqGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVFAC--TEAME 231
|
....*....
gi 1861108599 234 QlvAGVDRP 242
Cdd:PRK13638 232 Q--AGLTQP 238
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
2-226 |
5.44e-23 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 98.72 E-value: 5.44e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 2 IEIERAGKRFGDIVAVDDVSLTMQRGTITALVGASGSGKSTLLRMINRL--IAPTSGTI--------------------- 58
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIiyhvalcekcgyverpskvge 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 59 ------------RIDGVDTATVAPEQLRRGIGYAIQ-GHGLFPHWSVARNIATVPRLLGWPADRIDARVNELLDLFHLAp 125
Cdd:TIGR03269 81 pcpvcggtlepeEVDFWNLSDKLRRRIRKRIAIMLQrTFALYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEMVQLS- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 126 aefaDKLPH---ELSGGQQQRVGVARALAAEPAMLLMDEPFGALDPIIRNKAQDDLFALQRRLGITVVIVTHDIEEALKL 202
Cdd:TIGR03269 160 ----HRITHiarDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDL 235
|
250 260
....*....|....*....|....
gi 1861108599 203 GDTIAVMDAGRLLQVASPAEILGK 226
Cdd:TIGR03269 236 SDKAIWLENGEIKEEGTPDEVVAV 259
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
17-215 |
6.01e-23 |
|
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: 93.77 E-value: 6.01e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 17 VDDVSLTMQRGTITALVGASGSGKSTLLRMI-NRLIAP-TSGTIRIDGVDtatVAPEQLRRGIGYAIQGHGLFPHWSVAR 94
Cdd:cd03213 25 LKNVSGKAKPGELTAIMGPSGAGKSTLLNALaGRRTGLgVSGEVLINGRP---LDKRSFRKIIGYVPQDDILHPTLTVRE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 95 NIatvprllgwpadridarvnelldlfhlapaEFADKLpHELSGGQQQRVGVARALAAEPAMLLMDEPFGALDPIirnKA 174
Cdd:cd03213 102 TL------------------------------MFAAKL-RGLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSS---SA 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1861108599 175 QDDLFALQR--RLGITVVIVTHDI-EEALKLGDTIAVMDAGRLL 215
Cdd:cd03213 148 LQVMSLLRRlaDTGRTIICSIHQPsSEIFELFDKLLLLSQGRVI 191
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
13-214 |
1.71e-22 |
|
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: 93.30 E-value: 1.71e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 13 DIVAVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGVDTATVAPEQLRRGIGYAIQGHGLFPHwSV 92
Cdd:cd03248 26 DTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSKVSLVGQEPVLFAR-SL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 93 ARNIATvpRLLGWPADRI-----DARVNELLDLFHLAPAEFADKLPHELSGGQQQRVGVARALAAEPAMLLMDEPFGALD 167
Cdd:cd03248 105 QDNIAY--GLQSCSFECVkeaaqKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALD 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1861108599 168 PIIRNKAQDDLF-ALQRRlgiTVVIVTHDIeEALKLGDTIAVMDAGRL 214
Cdd:cd03248 183 AESEQQVQQALYdWPERR---TVLVIAHRL-STVERADQILVLDGGRI 226
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-212 |
1.91e-22 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 97.16 E-value: 1.91e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 1 MIEIERAGKRFGDIVAVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGVDTATVAPE-QLRRGIGY 79
Cdd:PRK09700 5 YISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKlAAQLGIGI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 80 AIQGHGLFPHWSVARNIaTVPRLLG---WPADRID-----ARVNELLDL--FHLAPAEFADklphELSGGQQQRVGVARA 149
Cdd:PRK09700 85 IYQELSVIDELTVLENL-YIGRHLTkkvCGVNIIDwremrVRAAMMLLRvgLKVDLDEKVA----NLSISHKQMLEIAKT 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1861108599 150 LAAEPAMLLMDEPFGALDpiirNKAQDDLFALQRRL---GITVVIVTHDIEEALKLGDTIAVMDAG 212
Cdd:PRK09700 160 LMLDAKVIIMDEPTSSLT----NKEVDYLFLIMNQLrkeGTAIVYISHKLAEIRRICDRYTVMKDG 221
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
12-227 |
1.94e-22 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 95.25 E-value: 1.94e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 12 GDIVAVDDVSLTMQRGTITALVGASGSGKSTLLRMI----NRLIAPTSGTIRIDGVDTATVAPEQLRRGIGYAIQ----- 82
Cdd:PRK15093 18 GWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAIcgvtKDNWRVTADRMRFDDIDLLRLSPRERRKLVGHNVSmifqe 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 83 -GHGLFPHWSVARN-IATVPrllGWPA-----DRIDARVNELLDLFHLA----PAEFADKLPHELSGGQQQRVGVARALA 151
Cdd:PRK15093 98 pQSCLDPSERVGRQlMQNIP---GWTYkgrwwQRFGWRKRRAIELLHRVgikdHKDAMRSFPYELTEGECQKVMIAIALA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 152 AEPAMLLMDEPFGALDPiirnKAQDDLFALQRRL----GITVVIVTHDIEEALKLGDTIAVMDAGRLLQVASPAEILGKP 227
Cdd:PRK15093 175 NQPRLLIADEPTNAMEP----TTQAQIFRLLTRLnqnnNTTILLISHDLQMLSQWADKINVLYCGQTVETAPSKELVTTP 250
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
15-224 |
3.04e-22 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 93.37 E-value: 3.04e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 15 VAVDD----VSLTMQRGTITALVGASGSGKSTLLRMINRLIaPTSGTIRIDGVDTATVAPEQLRRGIGYAIQghglfphw 90
Cdd:COG4138 6 VAVAGrlgpISAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGRPLSDWSAAELARHRAYLSQ-------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 91 svarNIATVPRLLGW-----------PADRIDARVNELLDLFHLApaefaDKLP---HELSGGQQQRVGVARALA----- 151
Cdd:COG4138 77 ----QQSPPFAMPVFqylalhqpagaSSEAVEQLLAQLAEALGLE-----DKLSrplTQLSGGEWQRVRLAAVLLqvwpt 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1861108599 152 --AEPAMLLMDEPFGALDpIIRNKAQDDLFALQRRLGITVVIVTHDIEEALKLGDTIAVMDAGRLLQVASPAEIL 224
Cdd:COG4138 148 inPEGQLLLLDEPMNSLD-VAQQAALDRLLRELCQQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEVM 221
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
16-235 |
3.23e-22 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 96.63 E-value: 3.23e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 16 AVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGVDTATVAPEQLRRGIGYAIQGHGLFPHwSVARN 95
Cdd:PRK11176 358 ALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFND-TIANN 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 96 IAtvprllgWPADRIDARvNELLDLFHLAPA-EFADKLPH-----------ELSGGQQQRVGVARALAAEPAMLLMDEPF 163
Cdd:PRK11176 437 IA-------YARTEQYSR-EQIEEAARMAYAmDFINKMDNgldtvigengvLLSGGQRQRIAIARALLRDSPILILDEAT 508
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1861108599 164 GALDPIIRNKAQDDLFALQRRLgiTVVIVTH---DIEEAlklgDTIAVMDAGRLLQVASPAEILGKpaAGVVEQL 235
Cdd:PRK11176 509 SALDTESERAIQAALDELQKNR--TSLVIAHrlsTIEKA----DEILVVEDGEIVERGTHAELLAQ--NGVYAQL 575
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
17-237 |
8.50e-22 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 95.54 E-value: 8.50e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 17 VDDVSLTMQRGTITALVGASGSGKS-TLLRMINRLIAP----TSGTIRIDGvDTATVAPEQLRRGIgyaiQGH------- 84
Cdd:PRK15134 25 VNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPpvvyPSGDIRFHG-ESLLHASEQTLRGV----RGNkiamifq 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 85 ----GLFPHWSVARNIATVprLLGWPADRIDARVNELLDLF-----HLAPAEFADkLPHELSGGQQQRVGVARALAAEPA 155
Cdd:PRK15134 100 epmvSLNPLHTLEKQLYEV--LSLHRGMRREAARGEILNCLdrvgiRQAAKRLTD-YPHQLSGGERQRVMIAMALLTRPE 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 156 MLLMDEPFGALDPIIRNKAQDDLFALQRRLGITVVIVTHDIEEALKLGDTIAVMDAGRLLQVASPAEILGKPAAGVVEQL 235
Cdd:PRK15134 177 LLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAATLFSAPTHPYTQKL 256
|
..
gi 1861108599 236 VA 237
Cdd:PRK15134 257 LN 258
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
14-215 |
1.58e-21 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 92.84 E-value: 1.58e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 14 IVAVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGVDtatvaPEQLRRgigyaiqghglfphwSVA 93
Cdd:COG4586 35 VEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYV-----PFKRRK---------------EFA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 94 RNIATV-----------P-----RLL----GWPADRIDARVNELLDLFHLapAEFADKLPHELSGGQQQRVGVARALAAE 153
Cdd:COG4586 95 RRIGVVfgqrsqlwwdlPaidsfRLLkaiyRIPDAEYKKRLDELVELLDL--GELLDTPVRQLSLGQRMRCELAAALLHR 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1861108599 154 PAMLLMDEPFGALDPIIRNKAQDDLFALQRRLGITVVIVTHDIEEALKLGDTIAVMDAGRLL 215
Cdd:COG4586 173 PKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEALCDRVIVIDHGRII 234
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
15-214 |
1.69e-21 |
|
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: 89.29 E-value: 1.69e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 15 VAVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGVDTATVApEQLRRGIGYaiqghglfphwsvar 94
Cdd:cd03247 16 QVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLISV--------------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 95 niatvprllgwpadrIDARVnelldlfHLAPAEFADKLPHELSGGQQQRVGVARALAAEPAMLLMDEPFGALDPIIRNKA 174
Cdd:cd03247 80 ---------------LNQRP-------YLFDTTLRNNLGRRFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQL 137
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1861108599 175 QDDLFALQRrlGITVVIVTHDIeEALKLGDTIAVMDAGRL 214
Cdd:cd03247 138 LSLIFEVLK--DKTLIWITHHL-TGIEHMDKILFLENGKI 174
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
2-285 |
2.49e-21 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 92.49 E-value: 2.49e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 2 IEIERAGKRFGDIVAVDDVSLTMQRGTITALVGASGSGKSTLlRMINRLIAPTSGTiRIDGVDTATVAPEQLRRGIG-YA 80
Cdd:NF000106 14 VEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RG-ALPAHV*GPDAGR-RPWRF*TWCANRRALRRTIG*HR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 81 IQGHGLFPHWSVARNIATVPRLLGWPADRIDARVNELLDLFHLAPAefADKLPHELSGGQQQRVGVARALAAEPAMLLMD 160
Cdd:NF000106 92 PVR*GRRESFSGRENLYMIGR*LDLSRKDARARADELLERFSLTEA--AGRAAAKYSGGMRRRLDLAASMIGRPAVLYLD 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 161 EPFGALDPIIRNKAQDDLFALQRRlGITVVIVTHDIEEALKLGDTIAVMDAGRLLQVASPAEILGKpAAGVVEQL----V 236
Cdd:NF000106 170 EPTTGLDPRTRNEVWDEVRSMVRD-GATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDELKTK-VGGRTLQIrpahA 247
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1861108599 237 AGVDRPLRLLALTPIDAV--AEPGHADG---EPIAATRTLRDAVSELLWRGVDV 285
Cdd:NF000106 248 AELDRMVGAIAQAGLDGIagATADHEDGvvnVPIVSDEQLSAVVGMLGERGFTI 301
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
19-236 |
2.54e-21 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 94.40 E-value: 2.54e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 19 DVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGVDTATVAPEQLRRGIGYAIQGHGLFPHwSVARNIAT 98
Cdd:TIGR00958 499 GLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSG-SVRENIAY 577
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 99 vpRLLGWPADRIDARVNElldlfhlAPA-EFADKLPH-----------ELSGGQQQRVGVARALAAEPAMLLMDEPFGAL 166
Cdd:TIGR00958 578 --GLTDTPDEEIMAAAKA-------ANAhDFIMEFPNgydtevgekgsQLSGGQKQRIAIARALVRKPRVLILDEATSAL 648
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1861108599 167 DPIIRNKAQDDlfalQRRLGITVVIVTHD---IEEALKlgdtIAVMDAGRLLQVASPAEILGKPaaGVVEQLV 236
Cdd:TIGR00958 649 DAECEQLLQES----RSRASRTVLLIAHRlstVERADQ----ILVLKKGSVVEMGTHKQLMEDQ--GCYKHLV 711
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
17-217 |
2.95e-21 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 93.70 E-value: 2.95e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 17 VDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGVDTATVAP-EQLRRGIGYAIQG---HGLFPHWSV 92
Cdd:PRK09700 279 VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPlDAVKKGMAYITESrrdNGFFPNFSI 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 93 ARNIATVPRLLgwpadriDARVNELLDLFH----LAPAEFADKLPH-----------ELSGGQQQRVGVARALAAEPAML 157
Cdd:PRK09700 359 AQNMAISRSLK-------DGGYKGAMGLFHevdeQRTAENQRELLAlkchsvnqnitELSGGNQQKVLISKWLCCCPEVI 431
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1861108599 158 LMDEPFGALDpiIRNKAQddLFALQRRL---GITVVIVTHDIEEALKLGDTIAVMDAGRLLQV 217
Cdd:PRK09700 432 IFDEPTRGID--VGAKAE--IYKVMRQLaddGKVILMVSSELPEIITVCDRIAVFCEGRLTQI 490
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1-227 |
3.13e-21 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 92.11 E-value: 3.13e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 1 MIEIERAGKRFGD----IVAVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLI----APTSGTIRIDGVDTATVAPEQ 72
Cdd:PRK11022 3 LLNVDKLSVHFGDesapFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIdypgRVMAEKLEFNGQDLQRISEKE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 73 LRRGIGYAIQG------HGLFPHWSVARNIATVPRLL--GWPADRIDaRVNELLDLFHL-APAEFADKLPHELSGGQQQR 143
Cdd:PRK11022 83 RRNLVGAEVAMifqdpmTSLNPCYTVGFQIMEAIKVHqgGNKKTRRQ-RAIDLLNQVGIpDPASRLDVYPHQLSGGMSQR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 144 VGVARALAAEPAMLLMDEPFGALDPIIRNKAQDDLFALQRRLGITVVIVTHDIEEALKLGDTIAVMDAGRLLQVASPAEI 223
Cdd:PRK11022 162 VMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDI 241
|
....
gi 1861108599 224 LGKP 227
Cdd:PRK11022 242 FRAP 245
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1-195 |
3.24e-21 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 93.59 E-value: 3.24e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 1 MIEIERAGKRFGDIVAVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRI-DGVDTATVAPEQlrrgigy 79
Cdd:COG0488 315 VLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLgETVKIGYFDQHQ------- 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 80 aiqgHGLFPHWSVARNIAtvprllGWPADRIDARVNELLDLFhLAPAEFADKLPHELSGGQQQRVGVARALAAEPAMLLM 159
Cdd:COG0488 388 ----EELDPDKTVLDELR------DGAPGGTEQEVRGYLGRF-LFSGDDAFKPVGVLSGGEKARLALAKLLLSPPNVLLL 456
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1861108599 160 DEPFGALDPIIRNkaqddlfALQRRL----GiTVVIVTHD 195
Cdd:COG0488 457 DEPTNHLDIETLE-------ALEEALddfpG-TVLLVSHD 488
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
12-208 |
3.37e-21 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 89.55 E-value: 3.37e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 12 GDIVAVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGVD-TATVAPEQlrrgIGYAiqGH--GLFP 88
Cdd:PRK13539 13 GGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDiDDPDVAEA----CHYL--GHrnAMKP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 89 HWSVARNIATVPRLLGWPADRIDARVnELLDLFHLAPAEFADklpheLSGGQQQRVGVARALAAEPAMLLMDEPFGALDp 168
Cdd:PRK13539 87 ALTVAENLEFWAAFLGGEELDIAAAL-EAVGLAPLAHLPFGY-----LSAGQKRRVALARLLVSNRPIWILDEPTAALD- 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1861108599 169 iirnKAQDDLFA--LQRRL--GITVVIVTH---DIEEA--LKLGDTIAV 208
Cdd:PRK13539 160 ----AAAVALFAelIRAHLaqGGIVIAATHiplGLPGAreLDLGPFAAE 204
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
17-194 |
5.32e-21 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 92.95 E-value: 5.32e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 17 VDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGVDTATVAPEQ-------LRRGIGYaiqghglfPH 89
Cdd:COG4178 379 LEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARPAGARVLFLPQRpylplgtLREALLY--------PA 450
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 90 wsvarniatvprllgwPADRI-DARVNELLDLFHLApaEFADKL------PHELSGGQQQRVGVARALAAEPAMLLMDEP 162
Cdd:COG4178 451 ----------------TAEAFsDAELREALEAVGLG--HLAERLdeeadwDQVLSLGEQQRLAFARLLLHKPDWLFLDEA 512
|
170 180 190
....*....|....*....|....*....|....
gi 1861108599 163 FGALDPiirnKAQDDLFA-LQRRL-GITVVIVTH 194
Cdd:COG4178 513 TSALDE----ENEAALYQlLREELpGTTVISVGH 542
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
19-213 |
7.59e-21 |
|
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: 88.30 E-value: 7.59e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 19 DVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGvdtatvapeqlrrGIGYAIQghglFPhW----SVAR 94
Cdd:cd03250 23 DINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG-------------SIAYVSQ----EP-WiqngTIRE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 95 NIatvprLLGWPADriDARVNELLDLFHLAP--AEFADKLPHE-------LSGGQQQRVGVARALAAEPAMLLMDEPFGA 165
Cdd:cd03250 85 NI-----LFGKPFD--EERYEKVIKACALEPdlEILPDGDLTEigekginLSGGQKQRISLARAVYSDADIYLLDDPLSA 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1861108599 166 LDPIIRNKAQDDLFALQRRLGITVVIVTHDIeEALKLGDTIAVMDAGR 213
Cdd:cd03250 158 VDAHVGRHIFENCILGLLLNNKTRILVTHQL-QLLPHADQIVVLDNGR 204
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
11-235 |
9.03e-21 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 89.66 E-value: 9.03e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 11 FGDIVAVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGVDTATVAPEQLRRGIGYAIQ-------- 82
Cdd:PRK10253 17 YGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQnattpgdi 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 83 ------GHGLFPHWsvarniatvPRLLGWPADRIDArVNELLDLFHLapAEFADKLPHELSGGQQQRVGVARALAAEPAM 156
Cdd:PRK10253 97 tvqelvARGRYPHQ---------PLFTRWRKEDEEA-VTKAMQATGI--THLADQSVDTLSGGQRQRAWIAMVLAQETAI 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1861108599 157 LLMDEPFGALDPIIRNKAQDDLFALQRRLGITVVIVTHDIEEALKLGDTIAVMDAGRLLQVASPAEILgkpAAGVVEQL 235
Cdd:PRK10253 165 MLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIV---TAELIERI 240
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
19-215 |
2.09e-20 |
|
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: 87.71 E-value: 2.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 19 DVSLTMQRGTITALVGASGSGKSTLLRMINRLI---APTSGTIRIDGVDtatVAPEQLRRGIGYAIQGHGLFPHWSVARN 95
Cdd:cd03234 25 DVSLHVESGQVMAILGSSGSGKTTLLDAISGRVeggGTTSGQILFNGQP---RKPDQFQKCVAYVRQDDILLPGLTVRET 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 96 IATVPRLLGwP---ADRIDARVNELLDLFHLAPAEFADKLPHELSGGQQQRVGVARALAAEPAMLLMDEPFGALDPIIRN 172
Cdd:cd03234 102 LTYTAILRL-PrksSDAIRKKRVEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFTAL 180
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1861108599 173 KAQDDLFALQRRLGITVVIVTHDIEEALKLGDTIAVMDAGRLL 215
Cdd:cd03234 181 NLVSTLSQLARRNRIVILTIHQPRSDLFRLFDRILLLSSGEIV 223
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
12-195 |
2.19e-20 |
|
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: 91.27 E-value: 2.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 12 GDIVAVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGVDTATVAPEQLRRGIGYAIQGHGLFpHWS 91
Cdd:TIGR02868 346 GAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLF-DTT 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 92 VARNIatvprLLGWPaDRIDARVNELLDLFHLapAEFADKLPH-----------ELSGGQQQRVGVARALAAEPAMLLMD 160
Cdd:TIGR02868 425 VRENL-----RLARP-DATDEELWAALERVGL--ADWLRALPDgldtvlgeggaRLSGGERQRLALARALLADAPILLLD 496
|
170 180 190
....*....|....*....|....*....|....*
gi 1861108599 161 EPFGALDPIIRNKAQDDLFALQRrlGITVVIVTHD 195
Cdd:TIGR02868 497 EPTEHLDAETADELLEDLLAALS--GRTVVLITHH 529
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
12-194 |
1.03e-19 |
|
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: 85.10 E-value: 1.03e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 12 GDIVAVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGVDTATVAPEqLRRGIGYAIQGHGLFPHWS 91
Cdd:TIGR01189 11 GERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDE-PHENILYLGHLPGLKPELS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 92 VARNIATVPRLLGwPADRidaRVNELLDLFHLapAEFADKLPHELSGGQQQRVGVARALAAEPAMLLMDEPFGALDpiir 171
Cdd:TIGR01189 90 ALENLHFWAAIHG-GAQR---TIEDALAAVGL--TGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALD---- 159
|
170 180
....*....|....*....|....*....
gi 1861108599 172 nKAQDDLFA------LQRrlGITVVIVTH 194
Cdd:TIGR01189 160 -KAGVALLAgllrahLAR--GGIVLLTTH 185
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
8-216 |
1.06e-19 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 89.20 E-value: 1.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 8 GKRFGDIVAVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGVDTA-TVAPEQLRRGIGYAIQGHGL 86
Cdd:PRK11288 11 GKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRfASTTAALAAGVAIIYQELHL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 87 FPHWSVARNI--ATVPRLLGWpADRIDARVNELLDLFHLA----PAEfadKLPHeLSGGQQQRVGVARALAAEPAMLLMD 160
Cdd:PRK11288 91 VPEMTVAENLylGQLPHKGGI-VNRRLLNYEAREQLEHLGvdidPDT---PLKY-LSIGQRQMVEIAKALARNARVIAFD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1861108599 161 EPFGALDpiirNKAQDDLFALQRRL---GITVVIVTHDIEEALKLGDTIAVMDAGRLLQ 216
Cdd:PRK11288 166 EPTSSLS----AREIEQLFRVIRELraeGRVILYVSHRMEEIFALCDAITVFKDGRYVA 220
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
16-220 |
2.26e-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: 84.39 E-value: 2.26e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 16 AVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGVDTATVAPEQLRRGIGYAIQGHGLFphwsvarn 95
Cdd:cd03369 23 VLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSSLTIIPQDPTLF-------- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 96 IATVprllgwpadridaRVNelLDLFHlapaEFADKLPHE----------LSGGQQQRVGVARALAAEPAMLLMDEPFGA 165
Cdd:cd03369 95 SGTI-------------RSN--LDPFD----EYSDEEIYGalrvsegglnLSQGQRQLLCLARALLKRPRVLVLDEATAS 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1861108599 166 LDPIIRNKAQD---DLFAlqrrlGITVVIVTHDIEEALKLgDTIAVMDAGRLLQVASP 220
Cdd:cd03369 156 IDYATDALIQKtirEEFT-----NSTILTIAHRLRTIIDY-DKILVMDAGEVKEYDHP 207
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1-212 |
3.36e-19 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 87.80 E-value: 3.36e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 1 MIEIERAGKRFGDIVAVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGVDTATVAPEQLRR-GIGY 79
Cdd:PRK15439 11 LLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQlGIYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 80 AIQGHGLFPHWSVARNIatvprLLGWPADRID-ARVNELLDLF--HLAPAEFADKLphELSggQQQRVGVARALAAEPAM 156
Cdd:PRK15439 91 VPQEPLLFPNLSVKENI-----LFGLPKRQASmQKMKQLLAALgcQLDLDSSAGSL--EVA--DRQIVEILRGLMRDSRI 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1861108599 157 LLMDEPFGALDPIirnkAQDDLFALQRRL---GITVVIVTHDIEEALKLGDTIAVMDAG 212
Cdd:PRK15439 162 LILDEPTASLTPA----ETERLFSRIRELlaqGVGIVFISHKLPEIRQLADRISVMRDG 216
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-196 |
5.99e-19 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 84.40 E-value: 5.99e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 1 MIEIERAGKRFGDIVAVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRidgvdtatvAPEQLRrgIGYA 80
Cdd:PRK09544 4 LVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK---------RNGKLR--IGYV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 81 IQGHGLFPHWSVarniaTVPRLLGW-PADRidaRVNELLDLFHLAPAEFADKLPHELSGGQQQRVGVARALAAEPAMLLM 159
Cdd:PRK09544 73 PQKLYLDTTLPL-----TVNRFLRLrPGTK---KEDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVL 144
|
170 180 190
....*....|....*....|....*....|....*..
gi 1861108599 160 DEPFGALDPIIRNKAQDDLFALQRRLGITVVIVTHDI 196
Cdd:PRK09544 145 DEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDL 181
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
9-213 |
8.84e-19 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 86.52 E-value: 8.84e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 9 KRFGDIVAVDDVSLTMQRGTITALVGASGSGKSTLLRMINRlIAPT---SGTIRIDGVD-TATVAPEQLRRGIGYAIQGH 84
Cdd:PRK13549 13 KTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSG-VYPHgtyEGEIIFEGEElQASNIRDTERAGIAIIHQEL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 85 GLFPHWSVARNIatvprLLG---WPADRID-----ARVNELLDLFHLA--PAefadkLP-HELSGGQQQRVGVARALAAE 153
Cdd:PRK13549 92 ALVKELSVLENI-----FLGneiTPGGIMDydamyLRAQKLLAQLKLDinPA-----TPvGNLGLGQQQLVEIAKALNKQ 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1861108599 154 PAMLLMDEPFGALDP--------IIRnkaqdDLfalqRRLGITVVIVTHDIEEALKLGDTIAVMDAGR 213
Cdd:PRK13549 162 ARLLILDEPTASLTEsetavlldIIR-----DL----KAHGIACIYISHKLNEVKAISDTICVIRDGR 220
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
17-214 |
1.20e-18 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 85.83 E-value: 1.20e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 17 VDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGVDTATVAPEQ-LRRGIGYAIQ---GHGLFPHWSV 92
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDgLANGIVYISEdrkRDGLVLGMSV 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 93 ARNIA-TVPRLLGWPADRIDAR-----VNELLDLFHL-APAefADKLPHELSGGQQQRVGVARALAAEPAMLLMDEPFGA 165
Cdd:PRK10762 348 KENMSlTALRYFSRAGGSLKHAdeqqaVSDFIRLFNIkTPS--MEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRG 425
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1861108599 166 LDPiirnKAQDDLFALQRRL---GITVVIVTHDIEEALKLGDTIAVMDAGRL 214
Cdd:PRK10762 426 VDV----GAKKEIYQLINQFkaeGLSIILVSSEMPEVLGMSDRILVMHEGRI 473
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
12-241 |
1.34e-18 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 84.78 E-value: 1.34e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 12 GDIVAVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAP---TSGTIRIDGVDTATVAPEQLRR----GIGYAIQG- 83
Cdd:PRK09473 27 GDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAAngrIGGSATFNGREILNLPEKELNKlraeQISMIFQDp 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 84 -HGLFPHWSVARNIATVPRL---LGwPADRIDARVnELLDLFHLAPAEFADKL-PHELSGGQQQRVGVARALAAEPAMLL 158
Cdd:PRK09473 107 mTSLNPYMRVGEQLMEVLMLhkgMS-KAEAFEESV-RMLDAVKMPEARKRMKMyPHEFSGGMRQRVMIAMALLCRPKLLI 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 159 MDEPFGALDPIIRNKAQDDLFALQRRLGITVVIVTHDIEEALKLGDTIAVMDAGRLLQVASPAEILGKPAAGVVEQLVAG 238
Cdd:PRK09473 185 ADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARDVFYQPSHPYSIGLLNA 264
|
...
gi 1861108599 239 VDR 241
Cdd:PRK09473 265 VPR 267
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
15-237 |
2.34e-18 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 85.14 E-value: 2.34e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 15 VAVDDVSLTMQRGTITALVGASGSGKST----LLRMINrliapTSGTIRIDGVDTATVAPEQL---RRGIGYAIQ--GHG 85
Cdd:PRK15134 300 VVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLIN-----SQGEIWFDGQPLHNLNRRQLlpvRHRIQVVFQdpNSS 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 86 LFPHWSVARNIAT-----VPRLlgwPADRIDARVNELLDLFHLAPaEFADKLPHELSGGQQQRVGVARALAAEPAMLLMD 160
Cdd:PRK15134 375 LNPRLNVLQIIEEglrvhQPTL---SAAQREQQVIAVMEEVGLDP-ETRHRYPAEFSGGQRQRIAIARALILKPSLIILD 450
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1861108599 161 EPFGALDPIIRNKAQDDLFALQRRLGITVVIVTHDIEEALKLGDTIAVMDAGRLLQVASPAEILGKPAAGVVEQLVA 237
Cdd:PRK15134 451 EPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERVFAAPQQEYTRQLLA 527
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
16-226 |
1.30e-17 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 82.95 E-value: 1.30e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 16 AVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGVDTATVAPEQLRRGIGYAIQGHGLFPHwSVARN 95
Cdd:PRK11160 355 VLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLFSA-TLRDN 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 96 IatvprLLGWPaDRIDARVNELLDLFHLapaefaDKLPHE--------------LSGGQQQRVGVARALAAEPAMLLMDE 161
Cdd:PRK11160 434 L-----LLAAP-NASDEALIEVLQQVGL------EKLLEDdkglnawlgeggrqLSGGEQRRLGIARALLHDAPLLLLDE 501
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1861108599 162 PFGALDPIIRNKAQDDLFALQRrlGITVVIVTHDIeEALKLGDTIAVMDAGRLLQVASPAEILGK 226
Cdd:PRK11160 502 PTEGLDAETERQILELLAEHAQ--NKTVLMITHRL-TGLEQFDRICVMDNGQIIEQGTHQELLAQ 563
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
18-200 |
1.75e-17 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 79.62 E-value: 1.75e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 18 DDVSLTMQRGTITALVGASGSGKSTLLRMINRLI--APTSGTIRIDGVDtatvapeqlrrgigyaiqghglFPhwsvaRN 95
Cdd:COG2401 47 RDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDVPDNQ----------------------FG-----RE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 96 IATVPRLlgWPADRIDARVnELLDLFHLAPAEFADKLPHELSGGQQQRVGVARALAAEPAMLLMDEPFGALDpiiRNKAQ 175
Cdd:COG2401 100 ASLIDAI--GRKGDFKDAV-ELLNAVGLSDAVLWLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLD---RQTAK 173
|
170 180 190
....*....|....*....|....*....|
gi 1861108599 176 DDLFALQ---RRLGITVVIVTH--DIEEAL 200
Cdd:COG2401 174 RVARNLQklaRRAGITLVVATHhyDVIDDL 203
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
2-195 |
1.89e-17 |
|
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: 77.49 E-value: 1.89e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 2 IEIERAGKRFGDIVAVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGVDTatvapeqlrrgIGYai 81
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVK-----------IGY-- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 82 qghglFPHwsvarniatvprllgwpadridarvnelldlfhlapaefadklpheLSGGQQQRVGVARALAAEPAMLLMDE 161
Cdd:cd03221 68 -----FEQ----------------------------------------------LSGGEKMRLALAKLLLENPNLLLLDE 96
|
170 180 190
....*....|....*....|....*....|....
gi 1861108599 162 PFGALDPIIRNKAQDDLFALQRrlgiTVVIVTHD 195
Cdd:cd03221 97 PTNHLDLESIEALEEALKEYPG----TVILVSHD 126
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
20-194 |
2.13e-16 |
|
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: 75.99 E-value: 2.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 20 VSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGVDTATVAPEqLRRGIGYAIQGHGLFPHWSVARNiatv 99
Cdd:cd03231 19 LSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDS-IARGLLYLGHAPGIKTTLSVLEN---- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 100 prLLGWPADRIDARVNELLDLFHLAPaeFADKLPHELSGGQQQRVGVARALAAEPAMLLMDEPFGALDpiirnKAQDDLF 179
Cdd:cd03231 94 --LRFWHADHSDEQVEEALARVGLNG--FEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALD-----KAGVARF 164
|
170
....*....|....*....
gi 1861108599 180 ALQRR----LGITVVIVTH 194
Cdd:cd03231 165 AEAMAghcaRGGMVVLTTH 183
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
16-212 |
2.74e-16 |
|
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: 79.67 E-value: 2.74e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 16 AVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTiridgvdtATVAPEQLRRGIGYAIQGHGLFPHWSVARN 95
Cdd:TIGR01257 1954 AVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGD--------ATVAGKSILTNISDVHQNMGYCPQFDAIDD 2025
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 96 IAT-------VPRLLGWPADRIDARVNelLDLFHLAPAEFADKLPHELSGGQQQRVGVARALAAEPAMLLMDEPFGALDP 168
Cdd:TIGR01257 2026 LLTgrehlylYARLRGVPAEEIEKVAN--WSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDP 2103
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1861108599 169 IIRNKAQDDLFALQRRlGITVVIVTHDIEEALKLGDTIAVMDAG 212
Cdd:TIGR01257 2104 QARRMLWNTIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKG 2146
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
19-214 |
3.18e-16 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 78.94 E-value: 3.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 19 DVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGVDTATVAPEQ-LRRGIGYAI---QGHGLFPHWSVAR 94
Cdd:PRK15439 281 NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQrLARGLVYLPedrQSSGLYLDAPLAW 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 95 NI-ATVPRLLGWPADRidARVNELLDLFHLA---PAEFADKLPHELSGGQQQRVGVARALAAEPAMLLMDEPFGALDPII 170
Cdd:PRK15439 361 NVcALTHNRRGFWIKP--ARENAVLERYRRAlniKFNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSA 438
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1861108599 171 RNkaqdDLFALQRRL---GITVVIVTHDIEEALKLGDTIAVMDAGRL 214
Cdd:PRK15439 439 RN----DIYQLIRSIaaqNVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1-213 |
6.70e-16 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 77.94 E-value: 6.70e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 1 MIEIERAGKRFGDIVAVDDVSLTMQRGTITALVGASGSGKSTLLRMINRlIAPT---SGTIRIDGVD-TATVAPEQLRRG 76
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSG-VYPHgtwDGEIYWSGSPlKASNIRDTERAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 77 IGYAIQGHGLFPHWSVARNI-----ATVP-RLLGWPAdrIDARVNELLDLFHLaPAEFADKLPHELSGGQQQRVGVARAL 150
Cdd:TIGR02633 80 IVIIHQELTLVPELSVAENIflgneITLPgGRMAYNA--MYLRAKNLLRELQL-DADNVTRPVGDYGGGQQQLVEIAKAL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1861108599 151 AAEPAMLLMDEPFGALDPIIRNKAQDDLFALQRRlGITVVIVTHDIEEALKLGDTIAVMDAGR 213
Cdd:TIGR02633 157 NKQARLLILDEPSSSLTEKETEILLDIIRDLKAH-GVACVYISHKLNEVKAVCDTICVIRDGQ 218
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
15-224 |
7.48e-16 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 75.74 E-value: 7.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 15 VAVDD----VSLTMQRGTITALVGASGSGKSTLLRMINRLIaPTSGTIRIDGVDTATVAPEQLRRGIGYAIQG------- 83
Cdd:PRK03695 6 VAVSTrlgpLSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAWSAAELARHRAYLSQQqtppfam 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 84 ---HGLFPHWSVARNIATVPRLLgwpadridarvNELLDLFHLapaefADKLP---HELSGGQQQRVGVA-------RAL 150
Cdd:PRK03695 85 pvfQYLTLHQPDKTRTEAVASAL-----------NEVAEALGL-----DDKLGrsvNQLSGGEWQRVRLAavvlqvwPDI 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1861108599 151 AAEPAMLLMDEPFGALDpIIRNKAQDDLFALQRRLGITVVIVTHDIEEALKLGDTIAVMDAGRLLQVASPAEIL 224
Cdd:PRK03695 149 NPAGQLLLLDEPMNSLD-VAQQAALDRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVL 221
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
16-214 |
4.23e-15 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 75.39 E-value: 4.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 16 AVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGVDTATVAPEQLRRGIGYAIQGHGLFPHwsvarn 95
Cdd:PRK10522 338 SVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFSAVFTDFHLFDQ------ 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 96 iatvprLL---GWPADriDARVNELLDlfHLapaEFADKLPHE--------LSGGQQQRVGVARALAAEPAMLLMDEPFG 164
Cdd:PRK10522 412 ------LLgpeGKPAN--PALVEKWLE--RL---KMAHKLELEdgrisnlkLSKGQKKRLALLLALAEERDILLLDEWAA 478
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1861108599 165 ALDPIIRNKAQDDLFALQRRLGITVVIVTHDiEEALKLGDTIAVMDAGRL 214
Cdd:PRK10522 479 DQDPHFRREFYQVLLPLLQEMGKTIFAISHD-DHYFIHADRLLEMRNGQL 527
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
13-226 |
6.56e-15 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 73.31 E-value: 6.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 13 DIVAVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGvDTATVAPEQlrrgigyaiqghGLFPHWSV 92
Cdd:PRK13546 36 TFFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG-EVSVIAISA------------GLSGQLTG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 93 ARNIATVPRLLGWPADRIDARVNELLDLFHLapAEFADKLPHELSGGQQQRVGVARALAAEPAMLLMDEPFGALDPIIRN 172
Cdd:PRK13546 103 IENIEFKMLCMGFKRKEIKAMTPKIIEFSEL--GEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQ 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1861108599 173 KAQDDLFALQRRlGITVVIVTHDIEEALKLGDTIAVMDAGRLLQVASPAEILGK 226
Cdd:PRK13546 181 KCLDKIYEFKEQ-NKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDVLPK 233
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
20-214 |
6.63e-15 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 74.95 E-value: 6.63e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 20 VSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGVDTATVAP-EQLRRGIGYAIQ---GHGLFPHWSVARN 95
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPrDAIRAGIMLCPEdrkAEGIIPVHSVADN 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 96 IATVPR--------LL--GWPADRIDARVNELldlfhlapaefADKLPH------ELSGGQQQRVGVARALAAEPAMLLM 159
Cdd:PRK11288 352 INISARrhhlragcLInnRWEAENADRFIRSL-----------NIKTPSreqlimNLSGGNQQKAILGRWLSEDMKVILL 420
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1861108599 160 DEPFGALDPIIRNKAQDDLFALQRRlGITVVIVTHDIEEALKLGDTIAVMDAGRL 214
Cdd:PRK11288 421 DEPTRGIDVGAKHEIYNVIYELAAQ-GVAVLFVSSDLPEVLGVADRIVVMREGRI 474
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
16-215 |
8.56e-15 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 72.99 E-value: 8.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 16 AVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGVDTATVAPEQLrrgIGYAIQGHGLfpHWS---V 92
Cdd:PRK15056 22 ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNL---VAYVPQSEEV--DWSfpvL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 93 ARNIATVPRL--LGW---PADRIDARVNELLDLFHLApaEFADKLPHELSGGQQQRVGVARALAAEPAMLLMDEPFGALD 167
Cdd:PRK15056 97 VEDVVMMGRYghMGWlrrAKKRDRQIVTAALARVDMV--EFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVD 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1861108599 168 PiirnKAQDDLFALQRRL---GITVVIVTHDIEEALKLGDtIAVMDAGRLL 215
Cdd:PRK15056 175 V----KTEARIISLLRELrdeGKTMLVSTHNLGSVTEFCD-YTVMVKGTVL 220
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
16-216 |
1.50e-14 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 73.98 E-value: 1.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 16 AVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGVDTATVAPEQLRRGIGYAIQGHGLFPHwSVARN 95
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFLFSD-TVANN 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 96 IAtvprlLGWPadriDARVNELLDLFHLAPA-EFADKLPH-----------ELSGGQQQRVGVARALAAEPAMLLMDEPF 163
Cdd:PRK10789 409 IA-----LGRP----DATQQEIEHVARLASVhDDILRLPQgydtevgergvMLSGGQKQRISIARALLLNAEILILDDAL 479
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1861108599 164 GALD-----PIIRNKAQddlFALQRrlgiTVVIVTHDIeEALKLGDTIAVMDAGRLLQ 216
Cdd:PRK10789 480 SAVDgrtehQILHNLRQ---WGEGR----TVIISAHRL-SALTEASEILVMQHGHIAQ 529
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
20-221 |
1.66e-14 |
|
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: 73.68 E-value: 1.66e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 20 VSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGVdtaTVAPEQLRRgigYaiqghglfphwsvaRN-IAT 98
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQ---PVTADNREA---Y--------------RQlFSA 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 99 V-------PRLLGWPADRIDARVNELLDLFHLapaefADKLPHE--------LSGGQQQRVGVARALAAEPAMLLMDEpF 163
Cdd:COG4615 411 VfsdfhlfDRLLGLDGEADPARARELLERLEL-----DHKVSVEdgrfsttdLSQGQRKRLALLVALLEDRPILVFDE-W 484
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1861108599 164 GA-LDPIIRNKAQDDLFALQRRLGITVVIVTHDiEEALKLGDTIAVMDAGRLLQVASPA 221
Cdd:COG4615 485 AAdQDPEFRRVFYTELLPELKARGKTVIAISHD-DRYFDLADRVLKMDYGKLVELTGPA 542
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
9-213 |
2.80e-14 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 72.90 E-value: 2.80e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 9 KRFGDIVAVDDVSLTMQRGTITALVGASGSGKSTLLRMINRlIAPT---SGTIRIDGvdtatvAPEQLR-------RGIG 78
Cdd:NF040905 9 KTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSG-VYPHgsyEGEILFDG------EVCRFKdirdseaLGIV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 79 YAIQGHGLFPHWSVARNIatvprLLG----------WPADRIDARvnELLDLFHLapAEFADKLPHELSGGQQQRVGVAR 148
Cdd:NF040905 82 IIHQELALIPYLSIAENI-----FLGnerakrgvidWNETNRRAR--ELLAKVGL--DESPDTLVTDIGVGKQQLVEIAK 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1861108599 149 ALAAEPAMLLMDEPFGALDPIIRNKAQDDLFALQRRlGITVVIVTHDIEEALKLGDTIAVMDAGR 213
Cdd:NF040905 153 ALSKDVKLLILDEPTAALNEEDSAALLDLLLELKAQ-GITSIIISHKLNEIRRVADSITVLRDGR 216
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1-212 |
3.21e-14 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 72.73 E-value: 3.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 1 MIEIERAGKRFGDIVAVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGVDTATVAPEQLRR-GIGY 79
Cdd:PRK10762 4 LLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQEaGIGI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 80 AIQGHGLFPHWSVARNIatvprLLG-----------WP-----ADRIDARVNelldLFHlapaeFADKLPHELSGGQQQR 143
Cdd:PRK10762 84 IHQELNLIPQLTIAENI-----FLGrefvnrfgridWKkmyaeADKLLARLN----LRF-----SSDKLVGELSIGEQQM 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1861108599 144 VGVARALAAEPAMLLMDEPFGALDpiirNKAQDDLFALQRRL---GITVVIVTHDIEEALKLGDTIAVMDAG 212
Cdd:PRK10762 150 VEIAKVLSFESKVIIMDEPTDALT----DTETESLFRVIRELksqGRGIVYISHRLKEIFEICDDVTVFRDG 217
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
13-212 |
3.80e-14 |
|
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: 70.44 E-value: 3.80e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 13 DIVAVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTI----RIDGVDTATVAPEQLRRGIGYAIQGHGLFp 88
Cdd:cd03290 13 GLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhwsnKNESEPSFEATRSRNRYSVAYAAQKPWLL- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 89 HWSVARNIAtvprlLGWPADRidARVNELLDLFHLAPAefADKLPH-----------ELSGGQQQRVGVARALAAEPAML 157
Cdd:cd03290 92 NATVEENIT-----FGSPFNK--QRYKAVTDACSLQPD--IDLLPFgdqteigergiNLSGGQRQRICVARALYQNTNIV 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1861108599 158 LMDEPFGALDPIIRNK-AQDDLFALQRRLGITVVIVTHDIeEALKLGDTIAVMDAG 212
Cdd:cd03290 163 FLDDPFSALDIHLSDHlMQEGILKFLQDDKRTLVLVTHKL-QYLPHADWIIAMKDG 217
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
2-195 |
5.70e-14 |
|
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: 72.28 E-value: 5.70e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 2 IEIERAGKRFGDIVAVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRI-DGVDTATVapEQLRrgigya 80
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIgETVKLAYV--DQSR------ 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 81 iqgHGLFPHWSVarniatvprllgWPAdridarVNELLDLFHLAPAEF-------------AD--KLPHELSGGQQQRVG 145
Cdd:TIGR03719 395 ---DALDPNKTV------------WEE------ISGGLDIIKLGKREIpsrayvgrfnfkgSDqqKKVGQLSGGERNRVH 453
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1861108599 146 VARALAAEPAMLLMDEPFGALDpiirnkaQDDLFALQRRL----GITVVIvTHD 195
Cdd:TIGR03719 454 LAKTLKSGGNVLLLDEPTNDLD-------VETLRALEEALlnfaGCAVVI-SHD 499
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
4-213 |
6.02e-14 |
|
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: 69.21 E-value: 6.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 4 IERAGKRFGDIVAVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPT---SGTIRIDGVDtATVAPEQLRRGIGYA 80
Cdd:cd03233 10 SFTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIP-YKEFAEKYPGEIIYV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 81 IQGHGLFPHWSVARNIATVPRLLGwpadridarvNELLdlfhlapaefadklpHELSGGQQQRVGVARALAAEPAMLLMD 160
Cdd:cd03233 89 SEEDVHFPTLTVRETLDFALRCKG----------NEFV---------------RGISGGERKRVSIAEALVSRASVLCWD 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1861108599 161 EPFGALDPI--------IRNKAQddlfALQrrlGITVVIVTHDIEEALKLGDTIAVMDAGR 213
Cdd:cd03233 144 NSTRGLDSStaleilkcIRTMAD----VLK---TTTFVSLYQASDEIYDLFDKVLVLYEGR 197
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
17-214 |
3.15e-13 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 69.85 E-value: 3.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 17 VDDVSLTMQRGTITALVGASGSGKSTLLRMI-NRLIAPTSGTIRIDGVDTATVAPEQ-LRRGIGYAIQG---HGLFPHWS 91
Cdd:TIGR02633 276 VDDVSFSLRRGEILGVAGLVGAGRTELVQALfGAYPGKFEGNVFINGKPVDIRNPAQaIRAGIAMVPEDrkrHGIVPILG 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 92 VARNI--ATVPRLLGwpADRIDARVNE---LLDLFHLAPAEFADKLP-HELSGGQQQRVGVARALAAEPAMLLMDEPFGA 165
Cdd:TIGR02633 356 VGKNItlSVLKSFCF--KMRIDAAAELqiiGSAIQRLKVKTASPFLPiGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRG 433
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1861108599 166 LDPIIRNKAQDDLFALQRRlGITVVIVTHDIEEALKLGDTIAVMDAGRL 214
Cdd:TIGR02633 434 VDVGAKYEIYKLINQLAQE-GVAIIVVSSELAEVLGLSDRVLVIGEGKL 481
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
18-194 |
3.34e-13 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 67.14 E-value: 3.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 18 DDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGVDTATVaPEQLRRGIGYAiqGH--GLFPHWSVARN 95
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQ-RDEYHQDLLYL--GHqpGIKTELTALEN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 96 IATVPRLLGwPADriDARVNELLDLFHLApaEFADKLPHELSGGQQQRVGVARALAAEPAMLLMDEPFGALDpiirNKAQ 175
Cdd:PRK13538 95 LRFYQRLHG-PGD--DEALWEALAQVGLA--GFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAID----KQGV 165
|
170 180
....*....|....*....|..
gi 1861108599 176 DDL---FALQRRLGITVVIVTH 194
Cdd:PRK13538 166 ARLealLAQHAEQGGMVILTTH 187
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
17-201 |
1.29e-12 |
|
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: 68.40 E-value: 1.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 17 VDDVSLTMQRGTITALVGASGSGKSTLLRMINRLiAPTSGTIRIDGVDTATVAPEQLRRGIGYAIQGHGLFPHwSVARNI 96
Cdd:TIGR01271 1235 LQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRL-LSTEGEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSG-TFRKNL 1312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 97 ATVPRllgWPADRIdARVNELLDLFHLApAEFADKLPHE-------LSGGQQQRVGVARALAAEPAMLLMDEPFGALDPI 169
Cdd:TIGR01271 1313 DPYEQ---WSDEEI-WKVAEEVGLKSVI-EQFPDKLDFVlvdggyvLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPV 1387
|
170 180 190
....*....|....*....|....*....|....*
gi 1861108599 170 ---IRNKAQDDLFAlqrrlGITVVIVTHDIEEALK 201
Cdd:TIGR01271 1388 tlqIIRKTLKQSFS-----NCTVILSEHRVEALLE 1417
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
11-167 |
1.33e-12 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 68.05 E-value: 1.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 11 FGDIVAVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGvdTATVA-----PEQLRRGI-------G 78
Cdd:PRK11147 13 FSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQ--DLIVArlqqdPPRNVEGTvydfvaeG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 79 YAIQGHGLFPHWSVARNIATVP--RLL--------------GWpadRIDARVNELLDLFHLAPaefaDKLPHELSGGQQQ 142
Cdd:PRK11147 91 IEEQAEYLKRYHDISHLVETDPseKNLnelaklqeqldhhnLW---QLENRINEVLAQLGLDP----DAALSSLSGGWLR 163
|
170 180
....*....|....*....|....*
gi 1861108599 143 RVGVARALAAEPAMLLMDEPFGALD 167
Cdd:PRK11147 164 KAALGRALVSNPDVLLLDEPTNHLD 188
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
19-226 |
1.46e-12 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 67.82 E-value: 1.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 19 DVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGVDTATVAPEQLRRGIGYAIQ-----GHGLFPHWSVA 93
Cdd:PRK10790 359 NINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMVQQdpvvlADTFLANVTLG 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 94 RNIAtvprllgwpadriDARVNELLDLFHLapAEFADKLP-----------HELSGGQQQRVGVARALAAEPAMLLMDEP 162
Cdd:PRK10790 439 RDIS-------------EEQVWQALETVQL--AELARSLPdglytplgeqgNNLSVGQKQLLALARVLVQTPQILILDEA 503
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1861108599 163 FGALDPIIRNKAQDDLFALQRRlgITVVIVTH---DIEEAlklgDTIAVMDAGRLLQVASPAEILGK 226
Cdd:PRK10790 504 TANIDSGTEQAIQQALAAVREH--TTLVVIAHrlsTIVEA----DTILVLHRGQAVEQGTHQQLLAA 564
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
17-214 |
1.56e-12 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 67.65 E-value: 1.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 17 VDDVSLTMQRGTITALVGASGSGKSTLLRMI-----NRliapTSGTIRIDGVDTATVAPEQ-LRRGIGYAIQG---HGLF 87
Cdd:PRK13549 278 VDDVSFSLRRGEILGIAGLVGAGRTELVQCLfgaypGR----WEGEIFIDGKPVKIRNPQQaIAQGIAMVPEDrkrDGIV 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 88 PHWSVARNI--ATVPRLLGWpaDRIDArvNELLDLFHLAPAEFADKLPH------ELSGGQQQRVGVARALAAEPAMLLM 159
Cdd:PRK13549 354 PVMGVGKNItlAALDRFTGG--SRIDD--AAELKTILESIQRLKVKTASpelaiaRLSGGNQQKAVLAKCLLLNPKILIL 429
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1861108599 160 DEPFGALDPIIRNKAQDDLFALQRRlGITVVIVTHDIEEALKLGDTIAVMDAGRL 214
Cdd:PRK13549 430 DEPTRGIDVGAKYEIYKLINQLVQQ-GVAIIVISSELPEVLGLSDRVLVMHEGKL 483
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
9-213 |
1.86e-12 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 67.45 E-value: 1.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 9 KRFGDIVAVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGVDTA-TVAPEQLRRGIGYAIQGHGLF 87
Cdd:PRK10982 6 KSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfKSSKEALENGISMVHQELNLV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 88 PHWSVARNI--ATVPrLLGWPADRiDARVNELLDLFhlapaefaDKL-----PHE----LSGGQQQRVGVARALAAEPAM 156
Cdd:PRK10982 86 LQRSVMDNMwlGRYP-TKGMFVDQ-DKMYRDTKAIF--------DELdididPRAkvatLSVSQMQMIEIAKAFSYNAKI 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 157 LLMDEPFGALDpiirNKAQDDLFALQRRL---GITVVIVTHDIEEALKLGDTIAVMDAGR 213
Cdd:PRK10982 156 VIMDEPTSSLT----EKEVNHLFTIIRKLkerGCGIVYISHKMEEIFQLCDEITILRDGQ 211
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
19-224 |
2.29e-12 |
|
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: 67.66 E-value: 2.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 19 DVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGVDTATVAPEQLRRGIGYAIQGHGLFPHwSVARNIAT 98
Cdd:TIGR00957 1304 HINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSG-SLRMNLDP 1382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 99 VprllgwpADRIDARVNELLDLFHLAP--AEFADKLPHE-------LSGGQQQRVGVARALAAEPAMLLMDEPFGALDpi 169
Cdd:TIGR00957 1383 F-------SQYSDEEVWWALELAHLKTfvSALPDKLDHEcaeggenLSVGQRQLVCLARALLRKTKILVLDEATAAVD-- 1453
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1861108599 170 irnKAQDDLFALQRRLGI---TVVIVTHDIEEALKLGDTIaVMDAGRLLQVASPAEIL 224
Cdd:TIGR00957 1454 ---LETDNLIQSTIRTQFedcTVLTIAHRLNTIMDYTRVI-VLDKGEVAEFGAPSNLL 1507
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
17-194 |
2.80e-12 |
|
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: 63.71 E-value: 2.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 17 VDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIdgvdtatvaPEqlRRGIGYAIQgHGLFPhwsvarnI 96
Cdd:cd03223 17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGM---------PE--GEDLLFLPQ-RPYLP-------L 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 97 ATVPRLLGWPADRIdarvnelldlfhlapaefadklpheLSGGQQQRVGVARALAAEPAMLLMDEPFGALDPiirnKAQD 176
Cdd:cd03223 78 GTLREQLIYPWDDV-------------------------LSGGEQQRLAFARLLLHKPKFVFLDEATSALDE----ESED 128
|
170
....*....|....*...
gi 1861108599 177 DLFALQRRLGITVVIVTH 194
Cdd:cd03223 129 RLYQLLKELGITVISVGH 146
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
17-246 |
5.75e-12 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 64.88 E-value: 5.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 17 VDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIApTSGTIRIDGVDTATVAPEQLRRGIGYAIQGHGLFPHwSVARNI 96
Cdd:cd03289 20 LENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQKWRKAFGVIPQKVFIFSG-TFRKNL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 97 ATVPRllgWPADRIdARVNELLDLfHLAPAEFADKLPHE-------LSGGQQQRVGVARALAAEPAMLLMDEPFGALDPI 169
Cdd:cd03289 98 DPYGK---WSDEEI-WKVAEEVGL-KSVIEQFPGQLDFVlvdggcvLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPI 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 170 ---IRNKAQDDLFAlqrrlGITVVIVTHDIEEALKLgDTIAVMDAGRLLQVASPAEILGKPAagVVEQLVAGVDRpLRLL 246
Cdd:cd03289 173 tyqVIRKTLKQAFA-----DCTVILSEHRIEAMLEC-QRFLVIEENKVRQYDSIQKLLNEKS--HFKQAISPSDR-LKLF 243
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
2-195 |
2.22e-11 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 64.37 E-value: 2.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 2 IEIERAGKRFGDIVAVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRI-DGVDTATVapEQLRRGIGya 80
Cdd:PRK11819 325 IEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIgETVKLAYV--DQSRDALD-- 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 81 iqghglfphwsvarNIATVprllgWPAdridarVNELLDLFHLAPAEF-------------AD--KLPHELSGGQQQRVG 145
Cdd:PRK11819 401 --------------PNKTV-----WEE------ISGGLDIIKVGNREIpsrayvgrfnfkgGDqqKKVGVLSGGERNRLH 455
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1861108599 146 VARALAAEPAMLLMDEPFGALDpiirnkaQDDLFALQRRL----GITVVIvTHD 195
Cdd:PRK11819 456 LAKTLKQGGNVLLLDEPTNDLD-------VETLRALEEALlefpGCAVVI-SHD 501
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
18-167 |
2.47e-11 |
|
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: 61.88 E-value: 2.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 18 DDVSLTMQRGTITALVGASGSGKSTLLRMI-NRLIAPT-SGTIRIDGVDTatvaPEQLRRGIGYAIQGHGLFPhwsvarn 95
Cdd:cd03232 24 NNISGYVKPGTLTALMGESGAGKTTLLDVLaGRKTAGViTGEILINGRPL----DKNFQRSTGYVEQQDVHSP------- 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1861108599 96 iatvprllgwpadriDARVNELLdlfhlapaEFADKLpHELSGGQQQRVGVARALAAEPAMLLMDEPFGALD 167
Cdd:cd03232 93 ---------------NLTVREAL--------RFSALL-RGLSVEQRKRLTIGVELAAKPSILFLDEPTSGLD 140
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
15-224 |
2.48e-11 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 62.92 E-value: 2.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 15 VAVDDVSLTMQRGTITALVGASGSGKSTLLRMI-NRLIAPT-------SGTIRIDGVDTA-----------TVAPEQLRR 75
Cdd:PRK13547 15 AILRDLSLRIEPGRVTALLGRNGAGKSTLLKALaGDLTGGGaprgarvTGDVTLNGEPLAaidaprlarlrAVLPQAAQP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 76 GIGYA---IQGHGLFPHwsvARNIATVPRLLGWPADRIDARVNelldlfhlaPAEFADKLPHELSGGQQQRVGVARALA- 151
Cdd:PRK13547 95 AFAFSareIVLLGRYPH---ARRAGALTHRDGEIAWQALALAG---------ATALVGRDVTTLSGGELARVQFARVLAq 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 152 --------AEPAMLLMDEPFGALDPIIRNKAQDDLFALQRRLGITVVIVTHDIEEALKLGDTIAVMDAGRLLQVASPAEI 223
Cdd:PRK13547 163 lwpphdaaQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPADV 242
|
.
gi 1861108599 224 L 224
Cdd:PRK13547 243 L 243
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
18-249 |
3.44e-11 |
|
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: 62.04 E-value: 3.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 18 DDVSLTMQRGTIT-----ALVGASGSGKSTLLRMINRLIAPTSGTIRIDGVDTA----------TVAPEQLRRGIgyaIQ 82
Cdd:cd03237 11 GEFTLEVEGGSISeseviGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSykpqyikadyEGTVRDLLSSI---TK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 83 GHGLFPHWSvarniatvprllgwpadridarvNELLDLFHLAPaeFADKLPHELSGGQQQRVGVARALAAEPAMLLMDEP 162
Cdd:cd03237 88 DFYTHPYFK-----------------------TEIAKPLQIEQ--ILDREVPELSGGELQRVAIAACLSKDADIYLLDEP 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 163 FGALD--------PIIRNkaqddlFALQRRLgiTVVIVTHDIEEALKLGDTIAVMDagrllqvaspaeilGKPA----AG 230
Cdd:cd03237 143 SAYLDveqrlmasKVIRR------FAENNEK--TAFVVEHDIIMIDYLADRLIVFE--------------GEPSvngvAN 200
|
250
....*....|....*....
gi 1861108599 231 VVEQLVAGVDRPLRLLALT 249
Cdd:cd03237 201 PPQSLRSGMNRFLKNLDIT 219
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
19-212 |
6.79e-11 |
|
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: 63.39 E-value: 6.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 19 DVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGvdtatvapeqlrrGIGYAIQGHGLFPHwSVARNIat 98
Cdd:TIGR01271 444 NISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG-------------RISFSPQTSWIMPG-TIKDNI-- 507
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 99 vprLLGWPAD--RIDARVN--ELLDLFHLAPAEfaDKLPH-----ELSGGQQQRVGVARALAAEPAMLLMDEPFGALDpI 169
Cdd:TIGR01271 508 ---IFGLSYDeyRYTSVIKacQLEEDIALFPEK--DKTVLgeggiTLSGGQRARISLARAVYKDADLYLLDSPFTHLD-V 581
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1861108599 170 IRNKAQDDLFALQRRLGITVVIVTHDIEEaLKLGDTIAVMDAG 212
Cdd:TIGR01271 582 VTEKEIFESCLCKLMSNKTRILVTSKLEH-LKKADKILLLHEG 623
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
15-194 |
9.38e-11 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 60.85 E-value: 9.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 15 VAVDD------VSLTMQRGTITALVGASGSGKSTLLRminrLIA------PTSGTIRIDGVDTATVAPEQ-LRRGIGYAI 81
Cdd:COG0396 8 VSVEGkeilkgVNLTIKPGEVHAIMGPNGSGKSTLAK----VLMghpkyeVTSGSILLDGEDILELSPDErARAGIFLAF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 82 QGHGLFPHWSVA---RNIATVPRLLGWPADRIDARVNELLDLFHLAPaEFADKLPHE-LSGGQQQRVGVARALAAEPAML 157
Cdd:COG0396 84 QYPVEIPGVSVSnflRTALNARRGEELSAREFLKLLKEKMKELGLDE-DFLDRYVNEgFSGGEKKRNEILQMLLLEPKLA 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1861108599 158 LMDEPfgaldpiirnkaqD---DLFALQ---------RRLGITVVIVTH 194
Cdd:COG0396 163 ILDET-------------DsglDIDALRivaegvnklRSPDRGILIITH 198
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
19-214 |
9.39e-11 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 62.87 E-value: 9.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 19 DVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIridgvdtatvapeqlrrgigyaiqghglfphWSvARNIAT 98
Cdd:PTZ00243 678 DVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV-------------------------------WA-ERSIAY 725
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 99 VPRLlGW-----------------PADRIDA-RVNEL-LDLFHLA---PAEFADKLPHeLSGGQQQRVGVARALAAEPAM 156
Cdd:PTZ00243 726 VPQQ-AWimnatvrgnilffdeedAARLADAvRVSQLeADLAQLGgglETEIGEKGVN-LSGGQKARVSLARAVYANRDV 803
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1861108599 157 LLMDEPFGALDPIIRNKAQDDLFaLQRRLGITVVIVTHDIeEALKLGDTIAVMDAGRL 214
Cdd:PTZ00243 804 YLLDDPLSALDAHVGERVVEECF-LGALAGKTRVLATHQV-HVVPRADYVVALGDGRV 859
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
32-226 |
1.04e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 62.83 E-value: 1.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 32 LVGASGSGKSTLLRMINRLIAPTSGTIRIDGVDTATVAPEQLRRGIGYAIQGHGLFPhwsvarniATVPRLLGWPADRID 111
Cdd:PLN03130 1270 IVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFS--------GTVRFNLDPFNEHND 1341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 112 ARVNELLDLFHLA----------PAEFADKlPHELSGGQQQRVGVARALAAEPAMLLMDEPFGALDpiIRNKAqddlfAL 181
Cdd:PLN03130 1342 ADLWESLERAHLKdvirrnslglDAEVSEA-GENFSVGQRQLLSLARALLRRSKILVLDEATAAVD--VRTDA-----LI 1413
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1861108599 182 QRRL-----GITVVIVTHDIEEALKLgDTIAVMDAGRLLQVASPAEILGK 226
Cdd:PLN03130 1414 QKTIreefkSCTMLIIAHRLNTIIDC-DRILVLDAGRVVEFDTPENLLSN 1462
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
2-215 |
1.47e-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: 59.46 E-value: 1.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 2 IEIERAGKRFGDIVAVDDVSLTMQRGTITALVGASGSGKSTLLRMI--NRLIAPTSGTIRIDGVDTATVAP-EQLRRGIG 78
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTImgHPKYEVTEGEILFKGEDITDLPPeERARLGIF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 79 YAIQGHGLFPHWSVA---RNiatvprllgwpadridarVNElldlfhlapaefadklphELSGGQQQRVGVARALAAEPA 155
Cdd:cd03217 81 LAFQYPPEIPGVKNAdflRY------------------VNE------------------GFSGGEKKRNEILQLLLLEPD 124
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1861108599 156 MLLMDEPFGALDpIIRNKAQDDLFALQRRLGITVVIVTH--DIEEALKlGDTIAVMDAGRLL 215
Cdd:cd03217 125 LAILDEPDSGLD-IDALRLVAEVINKLREEGKSVLIITHyqRLLDYIK-PDRVHVLYDGRIV 184
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
13-209 |
1.51e-10 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 61.97 E-value: 1.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 13 DIVAVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRI-DGVDTATVAPEQLRRGIGYAIQGHGLFPHwS 91
Cdd:PTZ00265 397 DVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDINLKWWRSKIGVVSQDPLLFSN-S 475
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 92 VARNI--------------------------------ATVPRLLGWPADRIDAR-VNELLD------------------- 119
Cdd:PTZ00265 476 IKNNIkyslyslkdlealsnyynedgndsqenknkrnSCRAKCAGDLNDMSNTTdSNELIEmrknyqtikdsevvdvskk 555
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 120 -LFHlapaEFADKLP-----------HELSGGQQQRVGVARALAAEPAMLLMDEPFGALDPIIRNKAQDDLFALQRRLGI 187
Cdd:PTZ00265 556 vLIH----DFVSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENR 631
|
250 260
....*....|....*....|..
gi 1861108599 188 TVVIVTHDIeEALKLGDTIAVM 209
Cdd:PTZ00265 632 ITIIIAHRL-STIRYANTIFVL 652
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
32-226 |
3.71e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 61.15 E-value: 3.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 32 LVGASGSGKSTLLRMINRLIAPTSGTIRIDGVDTATVAPEQLRRGIGYAIQGHGLFPHwSVARNIATVprllgwpADRID 111
Cdd:PLN03232 1267 VVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSG-TVRFNIDPF-------SEHND 1338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 112 ARVNELLDLFHLAPAefADKLPHEL-----------SGGQQQRVGVARALAAEPAMLLMDEPFGALDpiIRNKAqddlfA 180
Cdd:PLN03232 1339 ADLWEALERAHIKDV--IDRNPFGLdaevseggenfSVGQRQLLSLARALLRRSKILVLDEATASVD--VRTDS-----L 1409
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1861108599 181 LQRRL-----GITVVIVTHDIEEALKLgDTIAVMDAGRLLQVASPAEILGK 226
Cdd:PLN03232 1410 IQRTIreefkSCTMLVIAHRLNTIIDC-DKILVLSSGQVLEYDSPQELLSR 1459
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
19-222 |
3.76e-10 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 60.45 E-value: 3.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 19 DVSLTMQRGTITALVGASGSGKSTLLRMINRLIAP---TSGTIRIDGVdtaTVAPEQLRRGIGYAIQGHGLFPHWSVARN 95
Cdd:TIGR00955 43 NVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKgvkGSGSVLLNGM---PIDAKEMRAISAYVQQDDLFIPTLTVREH 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 96 I---ATV--PRLLgwPADRIDARVNELLDLFHLAPAefADKL------PHELSGGQQQRVGVARALAAEPAMLLMDEPFG 164
Cdd:TIGR00955 120 LmfqAHLrmPRRV--TKKEKRERVDEVLQALGLRKC--ANTRigvpgrVKGLSGGERKRLAFASELLTDPPLLFCDEPTS 195
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1861108599 165 ALDP--------IIRNKAQDdlfalqrrlGITVVIVTHD-IEEALKLGDTIAVMDAGRLLQVASPAE 222
Cdd:TIGR00955 196 GLDSfmaysvvqVLKGLAQK---------GKTIICTIHQpSSELFELFDKIILMAEGRVAYLGSPDQ 253
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
20-229 |
4.59e-10 |
|
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: 60.73 E-value: 4.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 20 VSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGvdTATVAPEQ-------LRRGIGYaiqGHGLFPHW-- 90
Cdd:TIGR00957 657 ITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKG--SVAYVPQQawiqndsLRENILF---GKALNEKYyq 731
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 91 SVARNIATVPRLLGWPA-DRidarvnelldlfhlapAEFADKLPHeLSGGQQQRVGVARALAAEPAMLLMDEPFGALDPI 169
Cdd:TIGR00957 732 QVLEACALLPDLEILPSgDR----------------TEIGEKGVN-LSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAH 794
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1861108599 170 IRNKAQDDLFALQRRL-GITVVIVTHDIeEALKLGDTIAVMDAGRLLQVASPAEILGKPAA 229
Cdd:TIGR00957 795 VGKHIFEHVIGPEGVLkNKTRILVTHGI-SYLPQVDVIIVMSGGKISEMGSYQELLQRDGA 854
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
27-215 |
4.78e-10 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 60.28 E-value: 4.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 27 GTITALVGASGSGKSTLLRMINRLIAPTS--GTIRIDGVDTAtvapEQLRRGIGYAIQGHGLFPHWSVaRNIATVPRLLG 104
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRKPT----KQILKRTGFVTQDDILYPHLTV-RETLVFCSLLR 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 105 WPAD-------RIDARVNELLDLFHLAPAEFADKLPHELSGGQQQRVGVARALAAEPAMLLMDEPFGALDPIIRNKAQDD 177
Cdd:PLN03211 169 LPKSltkqekiLVAESVISELGLTKCENTIIGNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLT 248
|
170 180 190
....*....|....*....|....*....|....*....
gi 1861108599 178 LFALQRRlGITVVIVTHD-IEEALKLGDTIAVMDAGRLL 215
Cdd:PLN03211 249 LGSLAQK-GKTIVTSMHQpSSRVYQMFDSVLVLSEGRCL 286
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
19-212 |
7.14e-10 |
|
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: 58.71 E-value: 7.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 19 DVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGvdtatvapeqlrrGIGYAIQGHGLFPHwSVARNIat 98
Cdd:cd03291 55 NINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG-------------RISFSSQFSWIMPG-TIKENI-- 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 99 vprLLGWPADriDARVNELLDLFHLApaEFADKLPHE-----------LSGGQQQRVGVARALAAEPAMLLMDEPFGALD 167
Cdd:cd03291 119 ---IFGVSYD--EYRYKSVVKACQLE--EDITKFPEKdntvlgeggitLSGGQRARISLARAVYKDADLYLLDSPFGYLD 191
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1861108599 168 pIIRNKAQDDLFALQRRLGITVVIVTHDIEEaLKLGDTIAVMDAG 212
Cdd:cd03291 192 -VFTEKEIFESCVCKLMANKTRILVTSKMEH-LKKADKILILHEG 234
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
11-194 |
1.10e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 57.27 E-value: 1.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 11 FGDIVAVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDG--VDTATVAPEQLRRGIGYAiqgHGLFP 88
Cdd:PRK13540 11 YHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERqsIKKDLCTYQKQLCFVGHR---SGINP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 89 HWSVARN----IATVPRLLGwpadridarVNELLDLFHLapAEFADKLPHELSGGQQQRVGVARALAAEPAMLLMDEPFG 164
Cdd:PRK13540 88 YLTLRENclydIHFSPGAVG---------ITELCRLFSL--EHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLV 156
|
170 180 190
....*....|....*....|....*....|....
gi 1861108599 165 ALDP----IIRNKAQDdlfalQRRLGITVVIVTH 194
Cdd:PRK13540 157 ALDElsllTIITKIQE-----HRAKGGAVLLTSH 185
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
34-168 |
2.27e-09 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 56.40 E-value: 2.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 34 GASGSGKSTLLRMINRLIAPTSGTIRIDGVDTATVapeQLRRGIGYAIQGHGLFPHWSVARNIATVPRLLGWPADRIDAR 113
Cdd:PRK13543 44 GDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRG---DRSRFMAYLGHLPGLKADLSTLENLHFLCGLHGRRAKQMPGS 120
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1861108599 114 VNELLDLfhlapAEFADKLPHELSGGQQQRVGVARALAAEPAMLLMDEPFGALDP 168
Cdd:PRK13543 121 ALAIVGL-----AGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDL 170
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
10-171 |
2.39e-09 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 58.10 E-value: 2.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 10 RFGDIVAVDDVSLTMQRGTITALVGASGSGKSTLLRMI---------NRLIaptsgtiridgvdtatvapeqL---RRGI 77
Cdd:PRK10938 269 SYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLItgdhpqgysNDLT---------------------LfgrRRGS 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 78 GYAIqghglfphWSVARNIATVPRLL----------------GW---------PADRIDARVNELLDLFHLApAEFADKL 132
Cdd:PRK10938 328 GETI--------WDIKKHIGYVSSSLhldyrvstsvrnvilsGFfdsigiyqaVSDRQQKLAQQWLDILGID-KRTADAP 398
|
170 180 190
....*....|....*....|....*....|....*....
gi 1861108599 133 PHELSGGQQQRVGVARALAAEPAMLLMDEPFGALDPIIR 171
Cdd:PRK10938 399 FHSLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNR 437
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
19-236 |
2.45e-09 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 58.50 E-value: 2.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 19 DVSLTMQRGTITALVGASGSGKSTLLRMINRL------------------------------------------------ 50
Cdd:PTZ00265 1186 DLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFydlkndhhivfknehtndmtneqdyqgdeeqnvgmknvnefsltkegg 1265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 51 ------IAPTSGTIRIDGVDTATVAPEQLRRGIGYAIQGHGLFpHWSVARNIATvprllgwpaDRIDARVNELLDLFHLA 124
Cdd:PTZ00265 1266 sgedstVFKNSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLF-NMSIYENIKF---------GKEDATREDVKRACKFA 1335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 125 PA-EFADKLPHE-----------LSGGQQQRVGVARALAAEPAMLLMDEPFGALDPIIRNKAQDDLFALQRRLGITVVIV 192
Cdd:PTZ00265 1336 AIdEFIESLPNKydtnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITI 1415
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1861108599 193 THDIeEALKLGDTIAVMD----AGRLLQVASPAEILGKPAAGVVEQLV 236
Cdd:PTZ00265 1416 AHRI-ASIKRSDKIVVFNnpdrTGSFVQAHGTHEELLSVQDGVYKKYV 1462
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
19-161 |
3.68e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 55.65 E-value: 3.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 19 DVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGVDTATVAPEQLrrgiGYAIQGHGLFPHWSVARNIAT 98
Cdd:PRK13541 18 DLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKPYC----TYIGHNLGLKLEMTVFENLKF 93
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1861108599 99 VPRLLGwPADRIDARVNelldLFHLapAEFADKLPHELSGGQQQRVGVARALAAEPAMLLMDE 161
Cdd:PRK13541 94 WSEIYN-SAETLYAAIH----YFKL--HDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDE 149
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
19-206 |
1.79e-08 |
|
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: 53.10 E-value: 1.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 19 DVSLTMQRGTITALVGASGSGKSTLLrmiNRLIApTSGTIRIDGV-----DTATVAPEQLRR----GIGYAiqghglfph 89
Cdd:cd03238 13 NLDVSIPLNVLVVVTGVSGSGKSTLV---NEGLY-ASGKARLISFlpkfsRNKLIFIDQLQFlidvGLGYL--------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 90 wSVARNIATvprllgwpadridarvnelldlfhlapaefadklpheLSGGQQQRVGVARALAAEP--AMLLMDEPFGALD 167
Cdd:cd03238 80 -TLGQKLST-------------------------------------LSGGELQRVKLASELFSEPpgTLFILDEPSTGLH 121
|
170 180 190
....*....|....*....|....*....|....*....
gi 1861108599 168 PIIRNKAQDDLFALqRRLGITVVIVTHDiEEALKLGDTI 206
Cdd:cd03238 122 QQDINQLLEVIKGL-IDLGNTVILIEHN-LDVLSSADWI 158
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
16-198 |
1.81e-08 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 55.28 E-value: 1.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 16 AVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGvdTATVApeqlrrgigyAIqGHGLFPHWSVARN 95
Cdd:PRK13545 39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKG--SAALI----------AI-SSGLNGQLTGIEN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 96 IATVPRLLGWPADRIDARVNELLdlfhlapaEFAD--KLPHE----LSGGQQQRVGVARALAAEPAMLLMDEPFGALDPI 169
Cdd:PRK13545 106 IELKGLMMGLTKEKIKEIIPEII--------EFADigKFIYQpvktYSSGMKSRLGFAISVHINPDILVIDEALSVGDQT 177
|
170 180
....*....|....*....|....*....
gi 1861108599 170 IRNKAQDDLFALQRRlGITVVIVTHDIEE 198
Cdd:PRK13545 178 FTKKCLDKMNEFKEQ-GKTIFFISHSLSQ 205
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
18-195 |
2.09e-08 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 55.33 E-value: 2.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 18 DDVSLTMQRGTITALVGASGSGKSTLLRMINrliaptsgtiridGVDTATVAPEQLRRGI--GYAIQGHGLFPHWSVARN 95
Cdd:TIGR03719 22 KDISLSFFPGAKIGVLGLNGAGKSTLLRIMA-------------GVDKDFNGEARPQPGIkvGYLPQEPQLDPTKTVREN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 96 I----ATVPRLLgwpadridARVNELLDLFHLAPAEFaDKLPHE------------------------------------ 135
Cdd:TIGR03719 89 VeegvAEIKDAL--------DRFNEISAKYAEPDADF-DKLAAEqaelqeiidaadawdldsqleiamdalrcppwdadv 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1861108599 136 --LSGGQQQRVGVARALAAEPAMLLMDEPFGALDpiirnkaQDDLFALQRRL----GiTVVIVTHD 195
Cdd:TIGR03719 160 tkLSGGERRRVALCRLLLSKPDMLLLDEPTNHLD-------AESVAWLERHLqeypG-TVVAVTHD 217
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
19-223 |
2.37e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 55.37 E-value: 2.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 19 DVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPtsgtiridgVDTATVApeqLRRGIGYAIQGHGLFpHWSVARNIat 98
Cdd:PLN03232 635 DINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSH---------AETSSVV---IRGSVAYVPQVSWIF-NATVRENI-- 699
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 99 vprLLG--------WPADRIDARVNELlDLFHLAPAEFADKLPHELSGGQQQRVGVARALAAEPAMLLMDEPFGALDPII 170
Cdd:PLN03232 700 ---LFGsdfeseryWRAIDVTALQHDL-DLLPGRDLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHV 775
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1861108599 171 RNKAQDDLFALQRRlGITVVIVTHDIeEALKLGDTIAVMDAGRLLQVASPAEI 223
Cdd:PLN03232 776 AHQVFDSCMKDELK-GKTRVLVTNQL-HFLPLMDRIILVSEGMIKEEGTFAEL 826
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
21-235 |
5.04e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 53.87 E-value: 5.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 21 SLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGVDTATVAPEQLRRGIGYAIQghglfphwsvaRN----I 96
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLSFEQLQKLVSDEWQ-----------RNntdmL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 97 ATVPRLLGWPADRI-------DARVNELLDLFHLAPaeFADKLPHELSGGQQQRVGVARALAAEPAMLLMDEPFGALDPI 169
Cdd:PRK10938 92 SPGEDDTGRTTAEIiqdevkdPARCEQLAQQFGITA--LLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVA 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1861108599 170 IRNKAQDDLFALQRRlGITVVIVTHDIEEALKLGDTIAVMDAGRLLQVASPAEILgkpAAGVVEQL 235
Cdd:PRK10938 170 SRQQLAELLASLHQS-GITLVLVLNRFDEIPDFVQFAGVLADCTLAETGEREEIL---QQALVAQL 231
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
3-213 |
6.30e-08 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 53.96 E-value: 6.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 3 EIERAGKRFGDIVAVD---DVSLTMQRGTITALVGASGSGKSTLLRMI----NRLIAPTSGTIRIDGVDTATVAPeQLRR 75
Cdd:TIGR00956 60 RGFRKLKKFRDTKTFDilkPMDGLIKPGELTVVLGRPGSGCSTLLKTIasntDGFHIGVEGVITYDGITPEEIKK-HYRG 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 76 GIGYAIQGHGLFPHWSVARNIATVPRLLGwPADRID-----ARVNELLDLF-------HLAPAEFADKLPHELSGGQQQR 143
Cdd:TIGR00956 139 DVVYNAETDVHFPHLTVGETLDFAARCKT-PQNRPDgvsreEYAKHIADVYmatyglsHTRNTKVGNDFVRGVSGGERKR 217
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1861108599 144 VGVARALAAEPAMLLMDEPFGALDP-----IIRnkaqddlfALQRRLGITVVIVTHDI----EEALKLGDTIAVMDAGR 213
Cdd:TIGR00956 218 VSIAEASLGGAKIQCWDNATRGLDSataleFIR--------ALKTSANILDTTPLVAIyqcsQDAYELFDKVIVLYEGY 288
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
17-214 |
6.88e-08 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 53.64 E-value: 6.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 17 VDDVSLTMQRGTITALVGASGSGKSTLLRMI-----NRLIaptSGTIRIDG--VDTATVaPEQLRRGIGYAIQ---GHGL 86
Cdd:NF040905 276 VDDVSLNVRRGEIVGIAGLMGAGRTELAMSVfgrsyGRNI---SGTVFKDGkeVDVSTV-SDAIDAGLAYVTEdrkGYGL 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 87 FPHWSVARNI--ATVPRL--LGWPADRIDARVNElldlfhlapaEFADKL----PH------ELSGGQQQRVGVARALAA 152
Cdd:NF040905 352 NLIDDIKRNItlANLGKVsrRGVIDENEEIKVAE----------EYRKKMniktPSvfqkvgNLSGGNQQKVVLSKWLFT 421
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 153 EPAMLLMDEPFGALD--------PIIRNKAQDdlfalqrrlGITVVIVTHDIEEALKLGDTIAVMDAGRL 214
Cdd:NF040905 422 DPDVLILDEPTRGIDvgakyeiyTIINELAAE---------GKGVIVISSELPELLGMCDRIYVMNEGRI 482
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
32-223 |
1.08e-07 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 53.24 E-value: 1.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 32 LVGASGSGKSTLLRMINRLIAPTSGTIRIDGVDTATVAPEQLRRGIGYAIQGHGLFPHwSVARNIAtvPRLLGWPADrid 111
Cdd:PTZ00243 1341 IVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFSMIPQDPVLFDG-TVRQNVD--PFLEASSAE--- 1414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 112 arVNELLDLFHL-----APAEFADKLPHE----LSGGQQQRVGVARALAAE-PAMLLMDEPFGALDPIIRNKAQDDL--- 178
Cdd:PTZ00243 1415 --VWAALELVGLrervaSESEGIDSRVLEggsnYSVGQRQLMCMARALLKKgSGFILMDEATANIDPALDRQIQATVmsa 1492
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1861108599 179 FAlqrrlGITVVIVTHDIEEALKLgDTIAVMDAGRLLQVASPAEI 223
Cdd:PTZ00243 1493 FS-----AYTVITIAHRLHTVAQY-DKIIVMDHGAVAEMGSPREL 1531
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
19-167 |
1.45e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 52.82 E-value: 1.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 19 DVSLTMQRGTITALVGASGSGKSTLLR-MINRLIAPTSGTIRIDGvdtaTVApeqlrrgigYAIQGHGLFpHWSVARNIa 97
Cdd:PLN03130 635 NINLDVPVGSLVAIVGSTGEGKTSLISaMLGELPPRSDASVVIRG----TVA---------YVPQVSWIF-NATVRDNI- 699
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 98 tvprLLGWPADRidARVNELLDLFHLApaEFADKLP-HEL----------SGGQQQRVGVARALAAEPAMLLMDEPFGAL 166
Cdd:PLN03130 700 ----LFGSPFDP--ERYERAIDVTALQ--HDLDLLPgGDLteigergvniSGGQKQRVSMARAVYSNSDVYIFDDPLSAL 771
|
.
gi 1861108599 167 D 167
Cdd:PLN03130 772 D 772
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
3-59 |
2.15e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 52.26 E-value: 2.15e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1861108599 3 EIERAGKRFGDIVAVDDVSLTMQRGTITALVGASGSGKSTLLR-MINRLiAPTSGTIR 59
Cdd:PRK11147 321 EMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKlMLGQL-QADSGRIH 377
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
26-202 |
3.90e-07 |
|
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: 48.91 E-value: 3.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 26 RGTITALVGASGSGKSTLLRMINRLIAPTSGT-IRIDGVDTATVAPEQLRRGIGYAIqghglfphwsvarniatvprllg 104
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGvIYIDGEDILEEVLDQLLLIIVGGK----------------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 105 wpadridarvnelldlfhlapaefadklPHELSGGQQQRVGVARALAAEPAMLLMDEPFGALDP-----IIRNKAQDDLF 179
Cdd:smart00382 58 ----------------------------KASGSGELRLRLALALARKLKPDVLILDEITSLLDAeqealLLLLEELRLLL 109
|
170 180
....*....|....*....|...
gi 1861108599 180 ALQRRLGITVVIVTHDIEEALKL 202
Cdd:smart00382 110 LLKSEKNLTVILTTNDEKDLGPA 132
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
6-195 |
6.02e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 50.50 E-value: 6.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 6 RAGKRFG-DIVAVDDVSLTMQRGTITALVGASGSGKSTLLRMINrliaptsgtiridGVDT-----ATVAPeqlrrG--I 77
Cdd:PRK11819 11 RVSKVVPpKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMA-------------GVDKefegeARPAP-----GikV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 78 GYAIQGHGLFPHWSVARNI----ATVPRLLgwpadridARVNELLDLFHLAPAEFaDKLPHE------------------ 135
Cdd:PRK11819 73 GYLPQEPQLDPEKTVRENVeegvAEVKAAL--------DRFNEIYAAYAEPDADF-DALAAEqgelqeiidaadawdlds 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 136 --------------------LSGGQQQRVGVARALAAEPAMLLMDEPFGALDpiirnkaqddlfA---------LQRRLG 186
Cdd:PRK11819 144 qleiamdalrcppwdakvtkLSGGERRRVALCRLLLEKPDMLLLDEPTNHLD------------AesvawleqfLHDYPG 211
|
....*....
gi 1861108599 187 iTVVIVTHD 195
Cdd:PRK11819 212 -TVVAVTHD 219
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
2-197 |
7.16e-07 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 50.28 E-value: 7.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 2 IEIERAGKRFGDIVAVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDgvDTATvapeqlrrgIGYAI 81
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWS--ENAN---------IGYYA 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 82 QGHglfphwsvARNIATVPRLLGWPADRIDARVNELLD-------LFhlaPAEFADKLPHELSGGQQQRVGVARALAAEP 154
Cdd:PRK15064 389 QDH--------AYDFENDLTLFDWMSQWRQEGDDEQAVrgtlgrlLF---SQDDIKKSVKVLSGGEKGRMLFGKLMMQKP 457
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1861108599 155 AMLLMDEPFGALDpiirNKAQDDL-FALQRRLGiTVVIVTHDIE 197
Cdd:PRK15064 458 NVLVMDEPTNHMD----MESIESLnMALEKYEG-TLIFVSHDRE 496
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
27-226 |
1.17e-06 |
|
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: 48.75 E-value: 1.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 27 GTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGVDTATVAPEQLRRGIGYAIQGHGLFPHwSVARNIATVPRLlgwp 106
Cdd:cd03288 47 GQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPILFSG-SIRFNLDPECKC---- 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 107 adrIDARVNELLDLFHLapAEFADKLPHEL-----------SGGQQQRVGVARALAAEPAMLLMDEPFGALDPIIRNKAQ 175
Cdd:cd03288 122 ---TDDRLWEALEIAQL--KNMVKSLPGGLdavvteggenfSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENILQ 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1861108599 176 DDLF-ALQRRlgiTVVIVTHDIEEALKlGDTIAVMDAGRLLQVASPAEILGK 226
Cdd:cd03288 197 KVVMtAFADR---TVVTIAHRVSTILD-ADLVLVLSRGILVECDTPENLLAQ 244
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
19-233 |
1.74e-06 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 49.46 E-value: 1.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 19 DVSLTMQRGTITALVGASGSGKSTLLRMI--NRLIAPTSGTIRIDGVdtaTVAPEQLRRGIGYAIQGHGLFPHWSVaRNI 96
Cdd:PLN03140 898 EVTGAFRPGVLTALMGVSGAGKTTLMDVLagRKTGGYIEGDIRISGF---PKKQETFARISGYCEQNDIHSPQVTV-RES 973
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 97 ATVPRLLGWPAD-------RIDARVNELLDLFHLAPAEFAdkLP--HELSGGQQQRVGVARALAAEPAMLLMDEPFGALD 167
Cdd:PLN03140 974 LIYSAFLRLPKEvskeekmMFVDEVMELVELDNLKDAIVG--LPgvTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLD 1051
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1861108599 168 P--------IIRNKAQDdlfalqrrlGITVVIVTH----DIEEALklgDTIAVMDAGRLLQVASPaeiLGKPAAGVVE 233
Cdd:PLN03140 1052 AraaaivmrTVRNTVDT---------GRTVVCTIHqpsiDIFEAF---DELLLMKRGGQVIYSGP---LGRNSHKIIE 1114
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
19-206 |
2.11e-06 |
|
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: 48.02 E-value: 2.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 19 DVSLTMQRGTITALVGASGSGKSTL----------LRMINRLIA---------PTSGTIRIDGVdTATVAPEQLRrgigy 79
Cdd:cd03270 13 NVDVDIPRNKLVVITGVSGSGKSSLafdtiyaegqRRYVESLSAyarqflgqmDKPDVDSIEGL-SPAIAIDQKT----- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 80 aIQGHglfPHWSVAR--NIATVPRLLgWPADRIDARVNELLD--LFHLAPAEFADKLphelSGGQQQRVGVARALAAEPA 155
Cdd:cd03270 87 -TSRN---PRSTVGTvtEIYDYLRLL-FARVGIRERLGFLVDvgLGYLTLSRSAPTL----SGGEAQRIRLATQIGSGLT 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1861108599 156 MLL--MDEPFGALDPIIRNKAQDDLFALqRRLGITVVIVTHDiEEALKLGDTI 206
Cdd:cd03270 158 GVLyvLDEPSIGLHPRDNDRLIETLKRL-RDLGNTVLVVEHD-EDTIRAADHV 208
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
23-196 |
4.28e-06 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 47.86 E-value: 4.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 23 TMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRID----------GVDT-ATVApEQLRRGIGYAIQGHGLFPHws 91
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDlkisykpqyiSPDYdGTVE-EFLRSANTDDFGSSYYKTE-- 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 92 VARniatvpRLlgwpadridaRVNELLDlfhlapaefadKLPHELSGGQQQRVGVARALAAEPAMLLMDEPFGALD---- 167
Cdd:COG1245 439 IIK------PL----------GLEKLLD-----------KNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDveqr 491
|
170 180 190
....*....|....*....|....*....|...
gi 1861108599 168 ----PIIRNkaqddlFALQRrlGITVVIVTHDI 196
Cdd:COG1245 492 lavaKAIRR------FAENR--GKTAMVVDHDI 516
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
12-167 |
5.85e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 47.80 E-value: 5.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 12 GDIVAVDDVSLTMQRGTITALVGASGSGKSTLL-----RMINRLIapTSGTIRIDG--VDtatvapEQLRRGIGYAIQGH 84
Cdd:TIGR00956 774 EKRVILNNVDGWVKPGTLTALMGASGAGKTTLLnvlaeRVTTGVI--TGGDRLVNGrpLD------SSFQRSIGYVQQQD 845
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 85 GLFPHWSVA---------RNIATVPRllgwpaDRIDARVNELLDLFHLapAEFADKL---PHE-LSGGQQQRVGVARALA 151
Cdd:TIGR00956 846 LHLPTSTVReslrfsaylRQPKSVSK------SEKMEYVEEVIKLLEM--ESYADAVvgvPGEgLNVEQRKRLTIGVELV 917
|
170
....*....|....*..
gi 1861108599 152 AEPAMLL-MDEPFGALD 167
Cdd:TIGR00956 918 AKPKLLLfLDEPTSGLD 934
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
31-167 |
8.33e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 47.16 E-value: 8.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 31 ALVGASGSGKSTLLRMINRLIAPTSGTI-RIDGVDTATVApeqlrrgigyaiQGHglfphwsvarniatvprllgwpADR 109
Cdd:PLN03073 539 AMVGPNGIGKSTILKLISGELQPSSGTVfRSAKVRMAVFS------------QHH----------------------VDG 584
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1861108599 110 IDARVNELLDLFHLAPAEFADKLP-----------------HELSGGQQQRVGVARALAAEPAMLLMDEPFGALD 167
Cdd:PLN03073 585 LDLSSNPLLYMMRCFPGVPEQKLRahlgsfgvtgnlalqpmYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLD 659
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1-195 |
1.07e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 46.70 E-value: 1.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 1 MIEIERAGKRFGDIVAVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIridgvdtatvapeQLRRGI--G 78
Cdd:PRK10636 312 LLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEI-------------GLAKGIklG 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 79 YAIQgHGLfphwsvarniatvprllgwpaDRIDARVNELLDLFHLAPAEFADKLPHEL-----------------SGGQQ 141
Cdd:PRK10636 379 YFAQ-HQL---------------------EFLRADESPLQHLARLAPQELEQKLRDYLggfgfqgdkvteetrrfSGGEK 436
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1861108599 142 QRVGVARALAAEPAMLLMDEPFGALDPIIRNKAQDDLFALQRRLgitvVIVTHD 195
Cdd:PRK10636 437 ARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIDFEGAL----VVVSHD 486
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
26-196 |
1.52e-05 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 46.34 E-value: 1.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 26 RGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDgvdtatvapeqLRrgIGYAiqghglfPHWSVARNIATVPRLLGW 105
Cdd:PRK13409 364 EGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE-----------LK--ISYK-------PQYIKPDYDGTVEDLLRS 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 106 PADRIDARV--NELLDLFHLAPaeFADKLPHELSGGQQQRVGVARALAAEPAMLLMDEPFGALD--------PIIRNkaq 175
Cdd:PRK13409 424 ITDDLGSSYykSEIIKPLQLER--LLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDveqrlavaKAIRR--- 498
|
170 180
....*....|....*....|.
gi 1861108599 176 ddlFALQRrlGITVVIVTHDI 196
Cdd:PRK13409 499 ---IAEER--EATALVVDHDI 514
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
25-232 |
2.81e-05 |
|
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: 45.55 E-value: 2.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 25 QRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRiDGVDTATVapeqLRRgigyaIQGHGLFPHWS--------VAR-- 94
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKILSGELKPNLGDYD-EEPSWDEV----LKR-----FRGTELQDYFKklangeikVAHkp 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 95 -NIATVPR--------LLgwpaDRIDAR--VNELLDLFHLAPaeFADKLPHELSGGQQQRVGVARALAAEPAMLLMDEPF 163
Cdd:COG1245 167 qYVDLIPKvfkgtvreLL----EKVDERgkLDELAEKLGLEN--ILDRDISELSGGELQRVAIAAALLRDADFYFFDEPS 240
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1861108599 164 GALD--------PIIRNKAQDdlfalqrrlGITVVIVTHDieealklgdtIAVMDAgrllqVASPAEIL-GKPAA-GVV 232
Cdd:COG1245 241 SYLDiyqrlnvaRLIRELAEE---------GKYVLVVEHD----------LAILDY-----LADYVHILyGEPGVyGVV 295
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
136-206 |
5.86e-05 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 43.36 E-value: 5.86e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1861108599 136 LSGGQQQ------RVGVARALAAEPAMLLMDEPFGALDPIIRNKAQDDLFALQRRLGI-TVVIVTHDiEEALKLGDTI 206
Cdd:cd03240 116 CSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENIEESLAEIIEERKSQKNfQLIVITHD-EELVDAADHI 192
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
12-194 |
6.97e-05 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 44.35 E-value: 6.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 12 GDIVaVDDVSLTMQRGTITALVGASGSGKSTLLRMIN--------RLIAP--------------TSGTIRiDGVDTATVA 69
Cdd:TIGR00954 464 GDVL-IESLSFEVPSGNNLLICGPNGCGKSSLFRILGelwpvyggRLTKPakgklfyvpqrpymTLGTLR-DQIIYPDSS 541
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 70 PEQLRRGIGyaiqghglfphwsvarniatvprllgwpadriDARVNELLDLFHL-----------APAEFADklphELSG 138
Cdd:TIGR00954 542 EDMKRRGLS--------------------------------DKDLEQILDNVQLthilereggwsAVQDWMD----VLSG 585
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1861108599 139 GQQQRVGVARALAAEPAMLLMDEPFGALDPiirnKAQDDLFALQRRLGITVVIVTH 194
Cdd:TIGR00954 586 GEKQRIAMARLFYHKPQFAILDECTSAVSV----DVEGYMYRLCREFGITLFSVSH 637
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
10-195 |
8.47e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 44.01 E-value: 8.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 10 RFGDIVAVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDG------VDTATVAPEQlrRGIGYAIQG 83
Cdd:PRK10636 10 RRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGnwqlawVNQETPALPQ--PALEYVIDG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 84 HGLFP------HWSVARN----IATVPRLLgwpaDRIDA-----RVNELLDLFHLAPAEFADKLpHELSGGQQQRVGVAR 148
Cdd:PRK10636 88 DREYRqleaqlHDANERNdghaIATIHGKL----DAIDAwtirsRAASLLHGLGFSNEQLERPV-SDFSGGWRMRLNLAQ 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1861108599 149 ALAAEPAMLLMDEPFGALDpiirnkaQDDLFALQRRLGI---TVVIVTHD 195
Cdd:PRK10636 163 ALICRSDLLLLDEPTNHLD-------LDAVIWLEKWLKSyqgTLILISHD 205
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
136-222 |
1.32e-04 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 43.18 E-value: 1.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 136 LSGGQQQRVGVARALAAEPAMLLMDEPFGALDPiirnKAQDDLFALQRRL---GITVVIVTHDIEEALKLGDTIAVMDAG 212
Cdd:PRK10982 392 LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDV----GAKFEIYQLIAELakkDKGIIIISSEMPELLGITDRILVMSNG 467
|
90
....*....|
gi 1861108599 213 RLLQVASPAE 222
Cdd:PRK10982 468 LVAGIVDTKT 477
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
18-55 |
2.02e-04 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 38.74 E-value: 2.02e-04
10 20 30
....*....|....*....|....*....|....*...
gi 1861108599 18 DDVSLTMQRGTITALVGASGSGKSTLLRMINRLIAPTS 55
Cdd:pfam13555 13 DGHTIPIDPRGNTLLTGPSGSGKSTLLDAIQTLLVPAK 50
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
136-226 |
3.32e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 42.51 E-value: 3.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 136 LSGGQQQRVGVARALAAEPA--MLLMDEPFGALDPiirnKAQDDLFALQRRL---GITVVIVTHDiEEALKLGDTI---- 206
Cdd:PRK00635 477 LSGGEQERTALAKHLGAELIgiTYILDEPSIGLHP----QDTHKLINVIKKLrdqGNTVLLVEHD-EQMISLADRIidig 551
|
90 100
....*....|....*....|..
gi 1861108599 207 --AVMDAGRLLQVASPAEILGK 226
Cdd:PRK00635 552 pgAGIFGGEVLFNGSPREFLAK 573
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
5-208 |
5.59e-04 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 40.25 E-value: 5.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 5 ERAGKRFGDI---VAVDDVSltmqRGTITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGVdTATVAPEQLrrgigyai 81
Cdd:cd03222 4 PDCVKRYGVFfllVELGVVK----EGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGI-TPVYKPQYI-------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 82 qghglfphwsvarniatvprllgwpadridarvnelldlfhlapaefadklphELSGGQQQRVGVARALAAEPAMLLMDE 161
Cdd:cd03222 71 -----------------------------------------------------DLSGGELQRVAIAAALLRNATFYLFDE 97
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1861108599 162 PFGALDPIIRNKAQDDLFALQRRLGITVVIVTHDIEEALKLGDTIAV 208
Cdd:cd03222 98 PSAYLDIEQRLNAARAIRRLSEEGKKTALVVEHDLAVLDYLSDRIHV 144
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
23-234 |
5.75e-04 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 41.33 E-value: 5.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 23 TMQRGTITALVGASGSGKSTLLRMINRLIAPTSGtiridGVDTATVAPEQLRRGIGYAIQGHglFPHWS-----VARNI- 96
Cdd:PRK13409 95 IPKEGKVTGILGPNGIGKTTAVKILSGELIPNLG-----DYEEEPSWDEVLKRFRGTELQNY--FKKLYngeikVVHKPq 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 97 ----------ATVPRLLgwpaDRIDAR--VNELLDLFHLAPaeFADKLPHELSGGQQQRVGVARALAAEPAMLLMDEPFG 164
Cdd:PRK13409 168 yvdlipkvfkGKVRELL----KKVDERgkLDEVVERLGLEN--ILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTS 241
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1861108599 165 ALDPIIRNKAQDdlfaLQRRL--GITVVIVTHDieealklgdtIAVMDAgrllqVASPAEIL-GKPAA-GVVEQ 234
Cdd:PRK13409 242 YLDIRQRLNVAR----LIRELaeGKYVLVVEHD----------LAVLDY-----LADNVHIAyGEPGAyGVVSK 296
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1-82 |
5.83e-04 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 40.78 E-value: 5.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 1 MIEIERAGKRFGDIVAVDDVSLTMQRGTITALVGASGSGKSTLLRMINRLIA--PTSGTIRIDGVDTATVAPEQL-RRGI 77
Cdd:CHL00131 7 ILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPAykILEGDILFKGESILDLEPEERaHLGI 86
|
....*
gi 1861108599 78 GYAIQ 82
Cdd:CHL00131 87 FLAFQ 91
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
20-167 |
7.10e-04 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 40.54 E-value: 7.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 20 VSLTMQRGTITALVGASGSGKSTLLRMI--NRLIAPTSGTIRIDGVDTATVAPEQlRRGIG------YAIQGHGLFPHWS 91
Cdd:PRK09580 20 LNLEVRPGEVHAIMGPNGSGKSTLSATLagREDYEVTGGTVEFKGKDLLELSPED-RAGEGifmafqYPVEIPGVSNQFF 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1861108599 92 VARNIATVPRLLGW-PADRIDAR--VNELLDLFHLAPAEFADKLPHELSGGQQQRVGVARALAAEPAMLLMDEPFGALD 167
Cdd:PRK09580 99 LQTALNAVRSYRGQePLDRFDFQdlMEEKIALLKMPEDLLTRSVNVGFSGGEKKRNDILQMAVLEPELCILDESDSGLD 177
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
110-227 |
7.14e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 41.15 E-value: 7.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 110 IDARVNELLD--LFHLAPAEFADKLphelSGGQQQRVGVARALAAE--PAMLLMDEPFGALDPIIRNKAQDDLFALqRRL 185
Cdd:TIGR00630 465 IRERLGFLIDvgLDYLSLSRAAGTL----SGGEAQRIRLATQIGSGltGVLYVLDEPSIGLHQRDNRRLINTLKRL-RDL 539
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1861108599 186 GITVVIVTHDiEEALKLGDTI------AVMDAGRLLQVASPAEILGKP 227
Cdd:TIGR00630 540 GNTLIVVEHD-EDTIRAADYVidigpgAGEHGGEVVASGTPEEILANP 586
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
107-167 |
1.25e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 40.23 E-value: 1.25e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1861108599 107 ADRIDARVNELLDLFHLAPaEFADKLPHELSGGQQQRVGVARALAAEPAMLLMDEPFGALD 167
Cdd:PLN03073 317 AYTAEARAASILAGLSFTP-EMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLD 376
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
29-196 |
1.54e-03 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 39.22 E-value: 1.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 29 ITALVGASGSGKSTLLRMINRLIAPTSGTIRIDGVDTATVAPEQLRRGIGYAIQGHglfpHWSVARNIATVPRLLGW-PA 107
Cdd:COG0419 25 LNLIVGPNGAGKSTILEAIRYALYGKARSRSKLRSDLINVGSEEASVELEFEHGGK----RYRIERRQGEFAEFLEAkPS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 108 DRIDArVNELLDL------------------FHLAPAEFADKL-------------PHELSGGQQQRVGVARALAaepam 156
Cdd:COG0419 101 ERKEA-LKRLLGLeiyeelkerlkeleealeSALEELAELQKLkqeilaqlsgldpIETLSGGERLRLALADLLS----- 174
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1861108599 157 LLMDepFGALDPIIRNKAQDDLFALQrrlgitvvIVTHDI 196
Cdd:COG0419 175 LILD--FGSLDEERLERLLDALEELA--------IITHVI 204
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
26-51 |
6.79e-03 |
|
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; YjeQ (YloQ in Bacillus subtilis) is a ribosomal small subunit-dependent GTPase; hence also known as RsgA. YjeQ is a late-stage ribosomal biogenesis factor involved in the 30S subunit maturation, and it represents a protein family whose members are broadly conserved in bacteria and have been shown to be essential to the growth of E. coli and B. subtilis. Proteins of the YjeQ family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. All YjeQ family proteins display a unique domain architecture, which includes an N-terminal OB-fold RNA-binding domain, the central permuted GTPase domain, and a zinc knuckle-like C-terminal cysteine domain.
Pssm-ID: 206747 [Multi-domain] Cd Length: 211 Bit Score: 36.99 E-value: 6.79e-03
10 20
....*....|....*....|....*.
gi 1861108599 26 RGTITALVGASGSGKSTLlrmINRLI 51
Cdd:cd01854 84 KGKTSVLVGQSGVGKSTL---LNALL 106
|
|
| ABC_MutS-like |
cd03283 |
ATP-binding cassette domain of MutS-like homolog; The MutS protein initiates DNA mismatch ... |
21-79 |
7.80e-03 |
|
ATP-binding cassette domain of MutS-like homolog; The MutS protein initiates DNA mismatch repair by recognizing mispaired and unpaired bases embedded in duplex DNA and activating endo- and exonucleases to remove the mismatch. Members of the MutS family possess C-terminal domain with a conserved ATPase activity that belongs to the ATP binding cassette (ABC) superfamily. MutS homologs (MSH) have been identified in most prokaryotic and all eukaryotic organisms examined. Prokaryotes have two homologs (MutS1 and MutS2), whereas seven MSH proteins (MSH1 to MSH7) have been identified in eukaryotes. The homodimer MutS1 and heterodimers MSH2-MSH3 and MSH2-MSH6 are primarily involved in mitotic mismatch repair, whereas MSH4-MSH5 is involved in resolution of Holliday junctions during meiosis. All members of the MutS family contain the highly conserved Walker A/B ATPase domain, and many share a common mechanism of action. MutS1, MSH2-MSH3, MSH2-MSH6, and MSH4-MSH5 dimerize to form sliding clamps, and recognition of specific DNA structures or lesions results in ADP/ATP exchange.
Pssm-ID: 213250 [Multi-domain] Cd Length: 199 Bit Score: 36.89 E-value: 7.80e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1861108599 21 SLTMQRGTITALVGASGSGKSTLLRMI--NRLIAPTSGT-------IRIDGVDTATVAPEQLRRGIGY 79
Cdd:cd03283 19 DIDMEKKNGILITGSNMSGKSTFLRTIgvNVILAQAGAPvcassfeLPPVKIFTSIRVSDDLRDGISY 86
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
27-234 |
8.65e-03 |
|
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: 36.96 E-value: 8.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 27 GTITALVGASGSGKSTLLRMINRLIAPTSGT-------------------------IRIDGVDtATVAPEQLRRgIGYAI 81
Cdd:cd03236 26 GQVLGLVGPNGIGKSTALKILAGKLKPNLGKfddppdwdeildefrgselqnyftkLLEGDVK-VIVKPQYVDL-IPKAV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861108599 82 QGhglfphwsvarniaTVPRLLgwpaDRIDAR--VNELLDLFHLAPaeFADKLPHELSGGQQQRVGVARALAAEPAMLLM 159
Cdd:cd03236 104 KG--------------KVGELL----KKKDERgkLDELVDQLELRH--VLDRNIDQLSGGELQRVAIAAALARDADFYFF 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1861108599 160 DEPFGALDPIIRNKAQddlfALQRRL---GITVVIVTHDIEEALKLGDTIAVMdagrllqvaspaeiLGKPAA-GVVEQ 234
Cdd:cd03236 164 DEPSSYLDIKQRLNAA----RLIRELaedDNYVLVVEHDLAVLDYLSDYIHCL--------------YGEPGAyGVVTL 224
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
19-64 |
9.10e-03 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 37.29 E-value: 9.10e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1861108599 19 DVSLTMQRGtITALVGASGSGKSTLLRMINRLIAPTSgTIRIDGVD 64
Cdd:COG3593 16 DLSIELSDD-LTVLVGENNSGKSSILEALRLLLGPSS-SRKFDEED 59
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
9-59 |
9.31e-03 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 37.28 E-value: 9.31e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1861108599 9 KRFGDIvavdDVSLTMQRGtITALVGASGSGKSTLLRMINRLIAPTSGTIR 59
Cdd:COG3950 12 RGFEDL----EIDFDNPPR-LTVLVGENGSGKTTLLEAIALALSGLLSRLD 57
|
|
| |
