|
Name |
Accession |
Description |
Interval |
E-value |
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
1-305 |
7.64e-179 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 495.77 E-value: 7.64e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 1 MIEFSHVSKLF-GAQKAVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEIRSLPVLELRRRMGY 79
Cdd:COG1125 1 MIEFENVTKRYpDGTVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRDLDPVELRRRIGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 80 AIQSIGLFPHWSVAQNIATVPQLQKWSRARIDDRIDELMALLGLE-SNLRERYPHQLSGGQQQRVGVARALAADPQVLLM 158
Cdd:COG1125 81 VIQQIGLFPHMTVAENIATVPRLLGWDKERIRARVDELLELVGLDpEEYRDRYPHELSGGQQQRVGVARALAADPPILLM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 159 DEPFGALDPVTRGALQQEMTRIHRLLGRTIVLVTHDIDEALRLAEHLVLMDHGEVVQQGNPLTMLTRPANDFVRQFFGRS 238
Cdd:COG1125 161 DEPFGALDPITREQLQDELLRLQRELGKTIVFVTHDIDEALKLGDRIAVMREGRIVQYDTPEEILANPANDFVADFVGAD 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446491464 239 ElGVRLLSLRSVADYVRREEraegEALAEEMTLRDALSLFVARGCEVLPVVNTQGQPSGTLHFQDLL 305
Cdd:COG1125 241 R-GLRRLSLLRVEDLMLPEP----PTVSPDASLREALSLMLERGVDWLLVVDEDGRPLGWLTLEDLL 302
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
2-241 |
1.49e-150 |
|
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: 421.71 E-value: 1.49e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 2 IEFSHVSKLFGA-QKAVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEIRSLPVLELRRRMGYA 80
Cdd:cd03295 1 IEFENVTKRYGGgKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 81 IQSIGLFPHWSVAQNIATVPQLQKWSRARIDDRIDELMALLGLES-NLRERYPHQLSGGQQQRVGVARALAADPQVLLMD 159
Cdd:cd03295 81 IQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLDPaEFADRYPHELSGGQQQRVGVARALAADPPLLLMD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 160 EPFGALDPVTRGALQQEMTRIHRLLGRTIVLVTHDIDEALRLAEHLVLMDHGEVVQQGNPLTMLTRPANDFVRQFFGRSE 239
Cdd:cd03295 161 EPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDFVAEFVGADR 240
|
..
gi 446491464 240 LG 241
Cdd:cd03295 241 LL 242
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-238 |
6.56e-96 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 286.99 E-value: 6.56e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 1 MIEFSHVSKLFGAQKAVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEIRSLPVlElRRRMGYA 80
Cdd:COG3842 5 ALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPP-E-KRNVGMV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 81 IQSIGLFPHWSVAQNIATVPQLQKWSRARIDDRIDELMALLGLEsNLRERYPHQLSGGQQQRVGVARALAADPQVLLMDE 160
Cdd:COG3842 83 FQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLE-GLADRYPHQLSGGQQQRVALARALAPEPRVLLLDE 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446491464 161 PFGALDPVTRGALQQEMTRIHRLLGRTIVLVTHDIDEALRLAEHLVLMDHGEVVQQGNPLTMLTRPANDFVRQFFGRS 238
Cdd:COG3842 162 PLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEIYERPATRFVADFIGEA 239
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
9-304 |
6.46e-93 |
|
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: 279.81 E-value: 6.46e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 9 KLFGAQKAVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEIRSLPVLEL----RRRMGYAIQSI 84
Cdd:TIGR01186 1 KKTGGKKGVNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEPTAGQIFIDGENIMKQSPVELrevrRKKIGMVFQQF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 85 GLFPHWSVAQNIATVPQLQKWSRARIDDRIDELMALLGLEsNLRERYPHQLSGGQQQRVGVARALAADPQVLLMDEPFGA 164
Cdd:TIGR01186 81 ALFPHMTILQNTSLGPELLGWPEQERKEKALELLKLVGLE-EYEHRYPDELSGGMQQRVGLARALAAEPDILLMDEAFSA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 165 LDPVTRGALQQEMTRIHRLLGRTIVLVTHDIDEALRLAEHLVLMDHGEVVQQGNPLTMLTRPANDFVRQFFGrselGVRL 244
Cdd:TIGR01186 160 LDPLIRDSMQDELKKLQATLQKTIVFITHDLDEAIRIGDRIVIMKAGEIVQVGTPDEILRNPANEYVEEFIG----KVDL 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 245 LSLRSVADYVRREERAEGEALAEEmTLRDALSLFVARGCEVLPVVNTQGQPSGTLHFQDL 304
Cdd:TIGR01186 236 SQVFDAERIAQRMNTGPITKTADK-GPRSALQLMRDERVDSLYVVDRQNKLVGVVDVESI 294
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
1-306 |
2.64e-87 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 266.20 E-value: 2.64e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 1 MIEFSHVSKLFGAQK------------------------AVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSG 56
Cdd:COG4175 3 KIEVRNLYKIFGKRPeralklldqgkskdeilektgqtvGVNDASFDVEEGEIFVIMGLSGSGKSTLVRCLNRLIEPTAG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 57 EIRFAGEEIRSLPVLEL----RRRMGYAIQSIGLFPHWSVAQNIATVPQLQKWSRARIDDRIDELMALLGLESNlRERYP 132
Cdd:COG4175 83 EVLIDGEDITKLSKKELrelrRKKMSMVFQHFALLPHRTVLENVAFGLEIQGVPKAERRERAREALELVGLAGW-EDSYP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 133 HQLSGGQQQRVGVARALAADPQVLLMDEPFGALDPVTRGALQQEMTRIHRLLGRTIVLVTHDIDEALRLAEHLVLMDHGE 212
Cdd:COG4175 162 DELSGGMQQRVGLARALATDPDILLMDEAFSALDPLIRREMQDELLELQAKLKKTIVFITHDLDEALRLGDRIAIMKDGR 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 213 VVQQGNPLTMLTRPANDFVRQFFG---RSelgvRLLSLRSVAdyvrreeRAEGEALAEEMTLRDALSLFVARGCEVLPVV 289
Cdd:COG4175 242 IVQIGTPEEILTNPANDYVADFVEdvdRS----KVLTAGSVM-------RPPEAVVSEKDGPRVALRRMREEGISSLYVV 310
|
330
....*....|....*..
gi 446491464 290 NTQGQPSGTLHFQDLLE 306
Cdd:COG4175 311 DRDRRLLGVVTADDALE 327
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
2-261 |
3.52e-86 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 262.00 E-value: 3.52e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 2 IEFSHVSKLFGAQKAVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEIRS-LPVLElrRRMGYA 80
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFTnLPPRE--RRVGFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 81 IQSIGLFPHWSVAQNIATVPQLQKWSRARIDDRIDELMALLGLEsNLRERYPHQLSGGQQQRVGVARALAADPQVLLMDE 160
Cdd:COG1118 81 FQHYALFPHMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLE-GLADRYPSQLSGGQRQRVALARALAVEPEVLLLDE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 161 PFGALDPVTRGALQQEMTRIHRLLGRTIVLVTHDIDEALRLAEHLVLMDHGEVVQQGNPLTMLTRPANDFVRQFFGRS-E 239
Cdd:COG1118 160 PFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDRPATPFVARFLGCVnV 239
|
250 260
....*....|....*....|..
gi 446491464 240 LGVRLLSLRSVADYVRREERAE 261
Cdd:COG1118 240 LRGRVIGGQLEADGLTLPVAEP 261
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-236 |
3.62e-85 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 259.62 E-value: 3.62e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 1 MIEFSHVSKLFGAQKAVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEIRSLPVLElrRRMGYA 80
Cdd:COG3839 3 SLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKD--RNIAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 81 IQSIGLFPHWSVAQNIATVPQLQKWSRARIDDRIDELMALLGLEsNLRERYPHQLSGGQQQRVGVARALAADPQVLLMDE 160
Cdd:COG3839 81 FQSYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLE-DLLDRKPKQLSGGQRQRVALGRALVREPKVFLLDE 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446491464 161 PFGALDPVTRGALQQEMTRIHRLLGRTIVLVTHDIDEALRLAEHLVLMDHGEVVQQGNPLTMLTRPANDFVRQFFG 236
Cdd:COG3839 160 PLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGTPEELYDRPANLFVAGFIG 235
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
2-217 |
1.58e-83 |
|
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: 250.51 E-value: 1.58e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 2 IEFSHVSKLFGAQKAVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEIRSLPVLelRRRMGYAI 81
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE--RRNIGMVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 82 QSIGLFPHWSVAQNIATVPQLQKWSRARIDDRIDELMALLGLEsNLRERYPHQLSGGQQQRVGVARALAADPQVLLMDEP 161
Cdd:cd03259 79 QDYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLE-GLLNRYPHELSGGQQQRVALARALAREPSLLLLDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446491464 162 FGALDPVTRGALQQEMTRIHRLLGRTIVLVTHDIDEALRLAEHLVLMDHGEVVQQG 217
Cdd:cd03259 158 LSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
7-235 |
1.27e-81 |
|
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: 247.94 E-value: 1.27e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 7 VSKLFGAQKAVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEIRSLP---VLELRR-RMGYAIQ 82
Cdd:cd03294 30 ILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSrkeLRELRRkKISMVFQ 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 83 SIGLFPHWSVAQNIATVPQLQKWSRARIDDRIDELMALLGLEsNLRERYPHQLSGGQQQRVGVARALAADPQVLLMDEPF 162
Cdd:cd03294 110 SFALLPHRTVLENVAFGLEVQGVPRAEREERAAEALELVGLE-GWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAF 188
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446491464 163 GALDPVTRGALQQEMTRIHRLLGRTIVLVTHDIDEALRLAEHLVLMDHGEVVQQGNPLTMLTRPANDFVRQFF 235
Cdd:cd03294 189 SALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDYVREFF 261
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-211 |
3.27e-81 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 246.54 E-value: 3.27e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 1 MIEFSHVSKLF----GAQKAVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEeirslPVLELRRR 76
Cdd:COG1116 7 ALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGK-----PVTGPGPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 77 MGYAIQSIGLFPHWSVAQNIATVPQLQKWSRARIDDRIDELMALLGLeSNLRERYPHQLSGGQQQRVGVARALAADPQVL 156
Cdd:COG1116 82 RGVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGL-AGFEDAYPHQLSGGMRQRVAIARALANDPEVL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446491464 157 LMDEPFGALDPVTRGALQQEMTRIHRLLGRTIVLVTHDIDEALRLAEHLVLMDHG 211
Cdd:COG1116 161 LMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFLADRVVVLSAR 215
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
2-236 |
1.09e-78 |
|
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: 239.06 E-value: 1.09e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 2 IEFSHVSKLFGAQKAVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEIRSLPVLelRRRMGYAI 81
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPH--KRPVNTVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 82 QSIGLFPHWSVAQNIATVPQLQKWSRARIDDRIDELMALLGLEsNLRERYPHQLSGGQQQRVGVARALAADPQVLLMDEP 161
Cdd:cd03300 79 QNYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLE-GYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEP 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446491464 162 FGALDPVTRGALQQEMTRIHRLLGRTIVLVTHDIDEALRLAEHLVLMDHGEVVQQGNPLTMLTRPANDFVRQFFG 236
Cdd:cd03300 158 LGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPANRFVADFIG 232
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
2-208 |
9.32e-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: 236.21 E-value: 9.32e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 2 IEFSHVSKLFG----AQKAVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEeirslPVLELRRRM 77
Cdd:cd03293 1 LEVRNVSKTYGggggAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGE-----PVTGPGPDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 78 GYAIQSIGLFPHWSVAQNIATVPQLQKWSRARIDDRIDELMALLGLEsNLRERYPHQLSGGQQQRVGVARALAADPQVLL 157
Cdd:cd03293 76 GYVFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLS-GFENAYPHQLSGGMRQRVALARALAVDPDVLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446491464 158 MDEPFGALDPVTRGALQQEMTRIHRLLGRTIVLVTHDIDEALRLAEHLVLM 208
Cdd:cd03293 155 LDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVL 205
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-235 |
5.43e-74 |
|
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: 227.17 E-value: 5.43e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 1 MIEFSHVSKLFGAQKAVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEIRSLPV---LELRRRM 77
Cdd:COG1127 5 MIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEkelYELRRRI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 78 GYAIQSIGLFPHWSVAQNIAtVP--QLQKWSRARIDDRIDELMALLGLEsNLRERYPHQLSGGQQQRVGVARALAADPQV 155
Cdd:COG1127 85 GMLFQGGALFDSLTVFENVA-FPlrEHTDLSEAEIRELVLEKLELVGLP-GAADKMPSELSGGMRKRVALARALALDPEI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 156 LLMDEPFGALDPVTRGALQQEMTRIHRLLGRTIVLVTHDIDEALRLAEHLVLMDHGEVVQQGNPLTMLTRPaNDFVRQFF 235
Cdd:COG1127 163 LLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLASD-DPWVRQFL 241
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
1-237 |
7.38e-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: 226.80 E-value: 7.38e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 1 MIEFSHVSKLFGAQKAVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEI--RSLPVLELRRRMG 78
Cdd:COG1126 1 MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLtdSKKDINKLRRKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 79 YAIQSIGLFPHWSVAQNIATVP-QLQKWSRARIDDRIDELMALLGLeSNLRERYPHQLSGGQQQRVGVARALAADPQVLL 157
Cdd:COG1126 81 MVFQQFNLFPHLTVLENVTLAPiKVKKMSKAEAEERAMELLERVGL-ADKADAYPAQLSGGQQQRVAIARALAMEPKVML 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 158 MDEPFGALDPvtrgalqqEMTR-----IHRL--LGRTIVLVTHDIDEALRLAEHLVLMDHGEVVQQGNPLTMLTRPANDF 230
Cdd:COG1126 160 FDEPTSALDP--------ELVGevldvMRDLakEGMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFENPQHER 231
|
....*..
gi 446491464 231 VRQFFGR 237
Cdd:COG1126 232 TRAFLSK 238
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
2-236 |
2.90e-71 |
|
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: 220.29 E-value: 2.90e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 2 IEFSHVSKLFGAQKAVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEIRSLPVLElrRRMGYAI 81
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQE--RNVGFVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 82 QSIGLFPHWSVAQNIA----TVPQLQKWSRARIDDRIDELMALLGLEsNLRERYPHQLSGGQQQRVGVARALAADPQVLL 157
Cdd:cd03296 81 QHYALFRHMTVFDNVAfglrVKPRSERPPEAEIRAKVHELLKLVQLD-WLADRYPAQLSGGQRQRVALARALAVEPKVLL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446491464 158 MDEPFGALDPVTRGALQQEMTRIHRLLGRTIVLVTHDIDEALRLAEHLVLMDHGEVVQQGNPLTMLTRPANDFVRQFFG 236
Cdd:cd03296 160 LDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPASPFVYSFLG 238
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
2-236 |
1.40e-68 |
|
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 213.51 E-value: 1.40e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 2 IEFSHVSKLFGAQKAVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEIRSLPVLelRRRMGYAI 81
Cdd:TIGR00968 1 IEIANISKRFGSFQALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGLEQPDSGRIRLNGQDATRVHAR--DRKIGFVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 82 QSIGLFPHWSVAQNIATVPQLQKWSRARIDDRIDELMALLGLEsNLRERYPHQLSGGQQQRVGVARALAADPQVLLMDEP 161
Cdd:TIGR00968 79 QHYALFKHLTVRDNIAFGLEIRKHPKAKIKARVEELLELVQLE-GLGDRYPNQLSGGQRQRVALARALAVEPQVLLLDEP 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446491464 162 FGALDPVTRGALQQEMTRIHRLLGRTIVLVTHDIDEALRLAEHLVLMDHGEVVQQGNPLTMLTRPANDFVRQFFG 236
Cdd:TIGR00968 158 FGALDAKVRKELRSWLRKLHDEVHVTTVFVTHDQEEAMEVADRIVVMSNGKIEQIGSPDEVYDHPANPFVMSFLG 232
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1-236 |
1.86e-68 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 216.48 E-value: 1.86e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 1 MIEFSHVSKLF----GAQKAVNDLNLNFQEGS-FSVlIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEIRSLPVLEL-- 73
Cdd:COG1135 1 MIELENLSKTFptkgGPVTALDDVSLTIEKGEiFGI-IGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELra 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 74 -RRRMGYAIQSIGLFPHWSVAQNIATVPQLQKWSRARIDDRIDELMALLGLeSNLRERYPHQLSGGQQQRVGVARALAAD 152
Cdd:COG1135 80 aRRKIGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGL-SDKADAYPSQLSGGQKQRVGIARALANN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 153 PQVLLMDEPFGALDPVTRGALQQEMTRIHRLLGRTIVLVTHDIDEALRLAEHLVLMDHGEVVQQGNPLTMLTRPANDFVR 232
Cdd:COG1135 159 PKVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVLDVFANPQSELTR 238
|
....
gi 446491464 233 QFFG 236
Cdd:COG1135 239 RFLP 242
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
2-239 |
2.34e-68 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 212.62 E-value: 2.34e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 2 IEFSHVSKLFGAQKAVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEIRSLPVlELRRRMGYAI 81
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPA-EVRRRIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 82 QSIGLFPHWSVAQNIATVPQLQKWSRARIDDRIDELMALLGLESnLRERYPHQLSGGQQQRVGVARALAADPQVLLMDEP 161
Cdd:COG1131 80 QEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTD-AADRKVGTLSGGMKQRLGLALALLHDPELLILDEP 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446491464 162 FGALDPVTRGALQQEMTRIHRlLGRTIVLVTHDIDEALRLAEHLVLMDHGEVVQQGNPLTMLTRPANDFVRQFFGRSE 239
Cdd:COG1131 159 TSGLDPEARRELWELLRELAA-EGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKARLLEDVFLELTGEEA 235
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
6-237 |
1.48e-67 |
|
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: 214.52 E-value: 1.48e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 6 HVSKLFGAQKAVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEIRSLPVLelRRRMGYAIQSIG 85
Cdd:TIGR03265 9 NIRKRFGAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRLPPQ--KRDYGIVFQSYA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 86 LFPHWSVAQNIATVPQLQKWSRARIDDRIDELMALLGLeSNLRERYPHQLSGGQQQRVGVARALAADPQVLLMDEPFGAL 165
Cdd:TIGR03265 87 LFPNLTVADNIAYGLKNRGMGRAEVAERVAELLDLVGL-PGSERKYPGQLSGGQQQRVALARALATSPGLLLLDEPLSAL 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446491464 166 DPVTRGALQQEMTRIHRLLGRTIVLVTHDIDEALRLAEHLVLMDHGEVVQQGNPLTMLTRPANDFVRQFFGR 237
Cdd:TIGR03265 166 DARVREHLRTEIRQLQRRLGVTTIMVTHDQEEALSMADRIVVMNHGVIEQVGTPQEIYRHPATPFVADFVGE 237
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
2-212 |
3.54e-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: 207.81 E-value: 3.54e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 2 IEFSHVSKLFGAQKAVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEIRSL--PVLELRRRMGY 79
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLedELPPLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 80 AIQSIGLFPHWSVAQNIAtvpqlqkwsrariddridelmallglesnlrerypHQLSGGQQQRVGVARALAADPQVLLMD 159
Cdd:cd03229 81 VFQDFALFPHLTVLENIA-----------------------------------LGLSGGQQQRVALARALAMDPDVLLLD 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446491464 160 EPFGALDPVTRGALQQEMTRIHRLLGRTIVLVTHDIDEALRLAEHLVLMDHGE 212
Cdd:cd03229 126 EPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
2-217 |
5.11e-67 |
|
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: 208.65 E-value: 5.11e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 2 IEFSHVSKLFGAQKAVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEIRSLPVLElrRRMGYAI 81
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKD--RDIAMVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 82 QSIGLFPHWSVAQNIATVPQLQKWSRARIDDRIDELMALLGLEsNLRERYPHQLSGGQQQRVGVARALAADPQVLLMDEP 161
Cdd:cd03301 79 QNYALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIE-HLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446491464 162 FGALDPVTRGALQQEMTRIHRLLGRTIVLVTHDIDEALRLAEHLVLMDHGEVVQQG 217
Cdd:cd03301 158 LSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| tungstate_WtpC |
NF040840 |
tungstate ABC transporter ATP-binding protein WtpC; |
1-236 |
6.27e-67 |
|
tungstate ABC transporter ATP-binding protein WtpC;
Pssm-ID: 468779 [Multi-domain] Cd Length: 347 Bit Score: 213.01 E-value: 6.27e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 1 MIEFSHVSKLFGAQKaVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEIRSLPvLElRRRMGYA 80
Cdd:NF040840 1 MIRIENLSKDWKEFK-LRDISLEVKEGEYFIILGPSGAGKTVLLELIAGIWPPDSGKIYLDGKDITNLP-PE-KRGIAYV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 81 IQSIGLFPHWSVAQNIATVPQLQKWSRARIDDRIDELMALLGLeSNLRERYPHQLSGGQQQRVGVARALAADPQVLLMDE 160
Cdd:NF040840 78 YQNYMLFPHKTVFENIAFGLKLRKVPKEEIERKVKEIMELLGI-SHLLHRKPRTLSGGEQQRVALARALIIEPKLLLLDE 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446491464 161 PFGALDPVTRGALQQEMTRIHRLLGRTIVLVTHDIDEALRLAEHLVLMDHGEVVQQGNPLTMLTRPANDFVRQFFG 236
Cdd:NF040840 157 PLSALDVQTRDELIREMKRWHREFGFTAIHVTHNFEEALSLADRVGIMLNGRLSQVGDVREVFRRPKNEFVARFVG 232
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-233 |
3.19e-66 |
|
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: 215.54 E-value: 3.19e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 1 MIEFSHVSKLF-----GAQKAVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEIRSLP---VLE 72
Cdd:COG1123 260 LLEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSrrsLRE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 73 LRRRMGYAIQ----SigLFPHWSVAQNIATVPQLQKW-SRARIDDRIDELMALLGLESNLRERYPHQLSGGQQQRVGVAR 147
Cdd:COG1123 340 LRRRVQMVFQdpysS--LNPRMTVGDIIAEPLRLHGLlSRAERRERVAELLERVGLPPDLADRYPHELSGGQRQRVAIAR 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 148 ALAADPQVLLMDEPFGALDPVTRGALQQEMTRIHRLLGRTIVLVTHDIDEALRLAEHLVLMDHGEVVQQGNPLTMLTRPA 227
Cdd:COG1123 418 ALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVFANPQ 497
|
....*.
gi 446491464 228 NDFVRQ 233
Cdd:COG1123 498 HPYTRA 503
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
2-226 |
1.33e-65 |
|
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: 205.64 E-value: 1.33e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 2 IEFSHVS-KLFGAQKAVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEIRSLPVLELRRRMGYA 80
Cdd:COG1122 1 IELENLSfSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 81 IQS--IGLF-PhwSVAQNIATVPQLQKWSRARIDDRIDELMALLGLEsNLRERYPHQLSGGQQQRVGVARALAADPQVLL 157
Cdd:COG1122 81 FQNpdDQLFaP--TVEEDVAFGPENLGLPREEIRERVEEALELVGLE-HLADRPPHELSGGQKQRVAIAGVLAMEPEVLV 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446491464 158 MDEPFGALDPVTRGALQQEMTRIHRlLGRTIVLVTHDIDEALRLAEHLVLMDHGEVVQQGNPLTMLTRP 226
Cdd:COG1122 158 LDEPTAGLDPRGRRELLELLKRLNK-EGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDY 225
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1-226 |
1.58e-65 |
|
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: 205.51 E-value: 1.58e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 1 MIEFSHVSKLFGAQ----KAVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEIRSLPVLEL--- 73
Cdd:cd03258 1 MIELKNVSKVFGDTggkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELrka 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 74 RRRMGYAIQSIGLFPHWSVAQNIATVPQLQKWSRARIDDRIDELMALLGLEsNLRERYPHQLSGGQQQRVGVARALAADP 153
Cdd:cd03258 81 RRRIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLE-DKADAYPAQLSGGQKQRVGIARALANNP 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446491464 154 QVLLMDEPFGALDPVTRGALQQEMTRIHRLLGRTIVLVTHDIDEALRLAEHLVLMDHGEVVQQGNPLTMLTRP 226
Cdd:cd03258 160 KVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFANP 232
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-216 |
2.11e-64 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 202.20 E-value: 2.11e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 1 MIEFSHVSKLFG----AQKAVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEIRSLPVLEL--- 73
Cdd:COG1136 4 LLELRNLTKSYGtgegEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELarl 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 74 -RRRMGYAIQSIGLFPHWSVAQNIATVPQLQKWSRARIDDRIDELMALLGLEsNLRERYPHQLSGGQQQRVGVARALAAD 152
Cdd:COG1136 84 rRRHIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLG-DRLDHRPSQLSGGQQQRVAIARALVNR 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446491464 153 PQVLLMDEPFGALDPVTRGALQQEMTRIHRLLGRTIVLVTHDiDEALRLAEHLVLMDHGEVVQQ 216
Cdd:COG1136 163 PKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHD-PELAARADRVIRLRDGRIVSD 225
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
2-234 |
2.17e-64 |
|
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: 202.73 E-value: 2.17e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 2 IEFSHVSKLFGAQKAVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEIRSLPVLEL---RRRMG 78
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELyrlRRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 79 YAIQSIGLFPHWSVAQNIAtVPQLQ--KWSRARIDDRIDELMALLGLEsNLRERYPHQLSGGQQQRVGVARALAADPQVL 156
Cdd:cd03261 81 MLFQSGALFDSLTVFENVA-FPLREhtRLSEEEIREIVLEKLEAVGLR-GAEDLYPAELSGGMKKRVALARALALDPELL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446491464 157 LMDEPFGALDPVTRGALQQEMTRIHRLLGRTIVLVTHDIDEALRLAEHLVLMDHGEVVQQGnPLTMLTRPANDFVRQF 234
Cdd:cd03261 159 LYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEG-TPEELRASDDPLVRQF 235
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
19-236 |
2.42e-64 |
|
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: 202.57 E-value: 2.42e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 19 DLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEIRSLPvlELRRRMGYAIQSIGLFPHWSVAQNIAT 98
Cdd:cd03299 17 NVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLP--PEKRDISYVPQNYALFPHMTVYKNIAY 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 99 VPQLQKWSRARIDDRIDELMALLGLeSNLRERYPHQLSGGQQQRVGVARALAADPQVLLMDEPFGALDPVTRGALQQEMT 178
Cdd:cd03299 95 GLKKRKVDKKEIERKVLEIAEMLGI-DHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLREELK 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446491464 179 RIHRLLGRTIVLVTHDIDEALRLAEHLVLMDHGEVVQQGNPLTMLTRPANDFVRQFFG 236
Cdd:cd03299 174 KIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPKNEFVAEFLG 231
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
2-236 |
4.44e-63 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 203.64 E-value: 4.44e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 2 IEFSHVSKLFGAQKAVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEIRSLPVLelRRRMGYAI 81
Cdd:PRK09452 15 VELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAE--NRHVNTVF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 82 QSIGLFPHWSVAQNIATVPQLQKWSRARIDDRIDELMALLGLEsNLRERYPHQLSGGQQQRVGVARALAADPQVLLMDEP 161
Cdd:PRK09452 93 QSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLE-EFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDES 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446491464 162 FGALDPVTRGALQQEMTRIHRLLGRTIVLVTHDIDEALRLAEHLVLMDHGEVVQQGNPLTMLTRPANDFVRQFFG 236
Cdd:PRK09452 172 LSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNLFVARFIG 246
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1-214 |
5.26e-63 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 198.74 E-value: 5.26e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 1 MIEFSHVSKLF-GAQKAVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEIRSLP---VLELRRR 76
Cdd:COG2884 1 MIRFENVSKRYpGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKrreIPYLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 77 MGYAIQSIGLFPHWSVAQNIATVPQLQKWSRARIDDRIDELMALLGLeSNLRERYPHQLSGGQQQRVGVARALAADPQVL 156
Cdd:COG2884 81 IGVVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGL-SDKAKALPHELSGGEQQRVAIARALVNRPELL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446491464 157 LMDEPFGALDPVTRGALQQEMTRIHRlLGRTIVLVTHDIDEALRLAEHLVLMDHGEVV 214
Cdd:COG2884 160 LADEPTGNLDPETSWEIMELLEEINR-RGTTVLIATHDLELVDRMPKRVLELEDGRLV 216
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
2-236 |
6.41e-63 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 202.62 E-value: 6.41e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 2 IEFSHVSKLFGAQKAVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEIRSLPVLElrRRMGYAI 81
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARD--RKVGFVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 82 QSIGLFPHWSVAQNIA---TV-PQLQKWSRARIDDRIDELMALLGLeSNLRERYPHQLSGGQQQRVGVARALAADPQVLL 157
Cdd:PRK10851 81 QHYALFRHMTVFDNIAfglTVlPRRERPNAAAIKAKVTQLLEMVQL-AHLADRYPAQLSGGQKQRVALARALAVEPQILL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446491464 158 MDEPFGALDPVTRGALQQEMTRIHRLLGRTIVLVTHDIDEALRLAEHLVLMDHGEVVQQGNPLTMLTRPANDFVRQFFG 236
Cdd:PRK10851 160 LDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREPATRFVLEFMG 238
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
2-213 |
2.19e-61 |
|
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: 194.29 E-value: 2.19e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 2 IEFSHVSKLFGAQKAVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEI--RSLPVLELRRRMGY 79
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLtdDKKNINELRQKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 80 AIQSIGLFPHWSVAQNIATVP-QLQKWSRARIDDRIDELMALLGLESNlRERYPHQLSGGQQQRVGVARALAADPQVLLM 158
Cdd:cd03262 81 VFQQFNLFPHLTVLENITLAPiKVKGMSKAEAEERALELLEKVGLADK-ADAYPAQLSGGQQQRVAIARALAMNPKVMLF 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446491464 159 DEPFGALDPVTRGALQQEMTRIHRlLGRTIVLVTHDIDEALRLAEHLVLMDHGEV 213
Cdd:cd03262 160 DEPTSALDPELVGEVLDVMKDLAE-EGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1-234 |
3.97e-61 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 194.54 E-value: 3.97e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 1 MIEFSHVSKLFGAQKAVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEIR--SLPVLELRRRMG 78
Cdd:PRK09493 1 MIEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNdpKVDERLIRQEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 79 YAIQSIGLFPHWSVAQNIATVP-QLQKWSRARIDDRIDELMALLGLESNLrERYPHQLSGGQQQRVGVARALAADPQVLL 157
Cdd:PRK09493 81 MVFQQFYLFPHLTALENVMFGPlRVRGASKEEAEKQARELLAKVGLAERA-HHYPSELSGGQQQRVAIARALAVKPKLML 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 158 MDEPFGALDPvtrgALQQEMTRIHRLL---GRTIVLVTHDIDEALRLAEHLVLMDHGEVVQQGNPLTMLTRPANDFVRQF 234
Cdd:PRK09493 160 FDEPTSALDP----ELRHEVLKVMQDLaeeGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPPSQRLQEF 235
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1-234 |
4.76e-61 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 197.33 E-value: 4.76e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 1 MIEFSHVSKLFGAQK----AVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEIRSLPVLELRRr 76
Cdd:PRK11153 1 MIELKNISKVFPQGGrtihALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRK- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 77 mgyAIQSIGL-FPHW------SVAQNIATVPQLQKWSRARIDDRIDELMALLGLeSNLRERYPHQLSGGQQQRVGVARAL 149
Cdd:PRK11153 80 ---ARRQIGMiFQHFnllssrTVFDNVALPLELAGTPKAEIKARVTELLELVGL-SDKADRYPAQLSGGQKQRVAIARAL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 150 AADPQVLLMDEPFGALDPVTRGALQQEMTRIHRLLGRTIVLVTHDIDEALRLAEHLVLMDHGEVVQQGNPLTMLTRPAND 229
Cdd:PRK11153 156 ASNPKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHPKHP 235
|
....*
gi 446491464 230 FVRQF 234
Cdd:PRK11153 236 LTREF 240
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1-236 |
4.94e-61 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 194.49 E-value: 4.94e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 1 MIEFSHVSKLFGAQKAVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEIRSLPVLELRRRMGYA 80
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 81 IQSIGLFPHWSVAQNIAT--VPQLQKWSRARIDDR--IDELMALLGLEsNLRERYPHQLSGGQQQRVGVARALAADPQVL 156
Cdd:COG1120 81 PQEPPAPFGLTVRELVALgrYPHLGLFGRPSAEDReaVEEALERTGLE-HLADRPVDELSGGERQRVLIARALAQEPPLL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 157 LMDEPFGALDPVTRGALQQEMTRIHRLLGRTIVLVTHDIDEALRLAEHLVLMDHGEVVQQGNPLTMLTrPANdfVRQFFG 236
Cdd:COG1120 160 LLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEVLT-PEL--LEEVYG 236
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
2-213 |
8.85e-61 |
|
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: 192.70 E-value: 8.85e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 2 IEFSHVSKLFGAQK----AVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEIRSLPVLEL---- 73
Cdd:cd03255 1 IELKNLSKTYGGGGekvqALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 74 RRRMGYAIQSIGLFPHWSVAQNIATVPQLQKWSRARIDDRIDELMALLGLEsNLRERYPHQLSGGQQQRVGVARALAADP 153
Cdd:cd03255 81 RRHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLG-DRLNHYPSELSGGQQQRVAIARALANDP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 154 QVLLMDEPFGALDPVTRGALQQEMTRIHRLLGRTIVLVTHDIDEAlRLAEHLVLMDHGEV 213
Cdd:cd03255 160 KIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELA-EYADRIIELRDGKI 218
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-239 |
2.94e-60 |
|
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: 192.33 E-value: 2.94e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 1 MIEFSHVSKLFGA----QKAVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEIRSLPVLELRRR 76
Cdd:COG1124 1 MLEVRNLSVSYGQggrrVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 77 MGYAIQSIG--LFPHWSVAQNIATVPQLQKwsRARIDDRIDELMALLGLESNLRERYPHQLSGGQQQRVGVARALAADPQ 154
Cdd:COG1124 81 VQMVFQDPYasLHPRHTVDRILAEPLRIHG--LPDREERIAELLEQVGLPPSFLDRYPHQLSGGQRQRVAIARALILEPE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 155 VLLMDEPFGALDPVTRGALQQEMTRIHRLLGRTIVLVTHDIDEALRLAEHLVLMDHGEVVQQGNPLTMLTRPANDFVRQF 234
Cdd:COG1124 159 LLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAGPKHPYTREL 238
|
....*
gi 446491464 235 FGRSE 239
Cdd:COG1124 239 LAASL 243
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1-219 |
1.45e-59 |
|
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: 190.45 E-value: 1.45e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 1 MIEFSHVSKLFGAQKAVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEIRSLPvLELRRRMGYA 80
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEP-REARRQIGVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 81 IQSIGLFPHWSVAQNIATVPQLQKWSRARIDDRIDELMALLGLESNLRERYpHQLSGGQQQRVGVARALAADPQVLLMDE 160
Cdd:COG4555 80 PDERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRV-GELSTGMKKKVALARALVHDPKVLLLDE 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446491464 161 PFGALDPVTRGALQQEMTRiHRLLGRTIVLVTHDIDEALRLAEHLVLMDHGEVVQQGNP 219
Cdd:COG4555 159 PTNGLDVMARRLLREILRA-LKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSL 216
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1-217 |
6.74e-59 |
|
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: 188.10 E-value: 6.74e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 1 MIEFSHVSKLF----GAQKAVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEIRSLPvLELRRR 76
Cdd:cd03257 1 LLEVKNLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLS-RRLRKI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 77 MGYAIQSIG------LFPHWSVAQNIATVPQLQK--WSRARIDDRIDELMALLGLESNLRERYPHQLSGGQQQRVGVARA 148
Cdd:cd03257 80 RRKEIQMVFqdpmssLNPRMTIGEQIAEPLRIHGklSKKEARKEAVLLLLVGVGLPEEVLNRYPHELSGGQRQRVAIARA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446491464 149 LAADPQVLLMDEPFGALDPVTRGALQQEMTRIHRLLGRTIVLVTHDIDEALRLAEHLVLMDHGEVVQQG 217
Cdd:cd03257 160 LALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
32-238 |
6.38e-58 |
|
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: 188.86 E-value: 6.38e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 32 LIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEIRSLPvlELRRRMGYAIQSIGLFPHWSVAQNIATVPQLQKWSRARID 111
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVP--PHLRHINMVFQSYALFPHMTVEENVAFGLKMRKVPRAEIK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 112 DRIDELMALLGLEsNLRERYPHQLSGGQQQRVGVARALAADPQVLLMDEPFGALDPVTRGALQQEMTRIHRLLGRTIVLV 191
Cdd:TIGR01187 79 PRVLEALRLVQLE-EFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITFVFV 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 446491464 192 THDIDEALRLAEHLVLMDHGEVVQQGNPLTMLTRPANDFVRQFFGRS 238
Cdd:TIGR01187 158 THDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFVARFIGEI 204
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
19-244 |
1.91e-57 |
|
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: 188.77 E-value: 1.91e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 19 DLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGE------EIRSLPVLelRRRMGYAIQSIGLFPHWSV 92
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEvlqdsaRGIFLPPH--RRRIGYVFQEARLFPHLSV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 93 AQNIatvpqLQKWSRARIDDR---IDELMALLGLESnLRERYPHQLSGGQQQRVGVARALAADPQVLLMDEPFGALDPVT 169
Cdd:COG4148 95 RGNL-----LYGRKRAPRAERrisFDEVVELLGIGH-LLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLAR 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446491464 170 RGALQQEMTRIHRLLGRTIVLVTHDIDEALRLAEHLVLMDHGEVVQQGNPLTMLTRPAndfVRQFFGRSELGVRL 244
Cdd:COG4148 169 KAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRPD---LLPLAGGEEAGSVL 240
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
2-219 |
2.76e-57 |
|
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: 183.92 E-value: 2.76e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 2 IEFSHVSKLFGAQKAVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEH-----DSGEIRFAGEEIRSL--PVLELR 74
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLipgapDEGEVLLDGKDIYDLdvDVLELR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 75 RRMGYAIQSIGLFPHwSVAQNIATVPQLQ-KWSRARIDDRIDELMALLGLESNLRER-YPHQLSGGQQQRVGVARALAAD 152
Cdd:cd03260 81 RRVGMVFQKPNPFPG-SIYDNVAYGLRLHgIKLKEELDERVEEALRKAALWDEVKDRlHALGLSGGQQQRLCLARALANE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446491464 153 PQVLLMDEPFGALDPVTRGALQQEMTRIHRllGRTIVLVTHDIDEALRLAEHLVLMDHGEVVQQGNP 219
Cdd:cd03260 160 PEVLLLDEPTSALDPISTAKIEELIAELKK--EYTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPT 224
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
3-212 |
9.33e-57 |
|
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: 182.28 E-value: 9.33e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 3 EFSHVSKLF--GAQKAVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEIRSLPVLELRRRMGYA 80
Cdd:cd03225 1 ELKNLSFSYpdGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 81 IQsiglFPHW-----SVAQNIATVPQLQKWSRARIDDRIDELMALLGLEsNLRERYPHQLSGGQQQRVGVARALAADPQV 155
Cdd:cd03225 81 FQ----NPDDqffgpTVEEEVAFGLENLGLPEEEIEERVEEALELVGLE-GLRDRSPFTLSGGQKQRVAIAGVLAMDPDI 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446491464 156 LLMDEPFGALDPVTRGALQQEMTRIHRlLGRTIVLVTHDIDEALRLAEHLVLMDHGE 212
Cdd:cd03225 156 LLLDEPTAGLDPAGRRELLELLKKLKA-EGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-227 |
1.50e-56 |
|
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: 190.50 E-value: 1.50e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 1 MIEFSHVSKLF--GAQKAVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHD---SGEIRFAGEEIRSLPVLELRR 75
Cdd:COG1123 4 LLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRGR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 76 RMGYAIQSIG--LFPhWSVAQNIATVPQLQKWSRARIDDRIDELMALLGLESnLRERYPHQLSGGQQQRVGVARALAADP 153
Cdd:COG1123 84 RIGMVFQDPMtqLNP-VTVGDQIAEALENLGLSRAEARARVLELLEAVGLER-RLDRYPHQLSGGQRQRVAIAMALALDP 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446491464 154 QVLLMDEPFGALDPVTRGALQQEMTRIHRLLGRTIVLVTHDIDEALRLAEHLVLMDHGEVVQQGNPLTMLTRPA 227
Cdd:COG1123 162 DLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAPQ 235
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
2-219 |
2.73e-56 |
|
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: 183.04 E-value: 2.73e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 2 IEFSHVSKLFGA-----QKAVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEIRS---LPVLEL 73
Cdd:TIGR04521 1 IKLKNVSYIYQPgtpfeKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAkkkKKLKDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 74 RRRMGYAIQsiglFPHW-----SVAQNIATVPQLQKWSRARIDDRIDELMALLGLESNLRERYPHQLSGGQQQRVGVARA 148
Cdd:TIGR04521 81 RKKVGLVFQ----FPEHqlfeeTVYKDIAFGPKNLGLSEEEAEERVKEALELVGLDEEYLERSPFELSGGQMRRVAIAGV 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446491464 149 LAADPQVLLMDEPFGALDPVTRGALQQEMTRIHRLLGRTIVLVTHDIDEALRLAEHLVLMDHGEVVQQGNP 219
Cdd:TIGR04521 157 LAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTP 227
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
7-236 |
4.03e-56 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 185.62 E-value: 4.03e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 7 VSKLFGAQKAVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEIRSLPVLElrRRMGYAIQSIGL 86
Cdd:PRK11000 9 VTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAE--RGVGMVFQSYAL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 87 FPHWSVAQNIATVPQLQKWSRARIDDRIDELMALLGLeSNLRERYPHQLSGGQQQRVGVARALAADPQVLLMDEPFGALD 166
Cdd:PRK11000 87 YPHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQL-AHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLD 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 167 PVTRGALQQEMTRIHRLLGRTIVLVTHDIDEALRLAEHLVLMDHGEVVQQGNPLTMLTRPANDFVRQFFG 236
Cdd:PRK11000 166 AALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPANRFVAGFIG 235
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-234 |
8.40e-55 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 178.90 E-value: 8.40e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 1 MIEFSHVSKLFG----AQKAVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEIRSlPVLElrrr 76
Cdd:COG4525 3 MLTVRHVSVRYPgggqPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTG-PGAD---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 77 MGYAIQSIGLFPHWSVAQNIATVPQLQKWSRARIDDRIDELMALLGLEsNLRERYPHQLSGGQQQRVGVARALAADPQVL 156
Cdd:COG4525 78 RGVVFQKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLA-DFARRRIWQLSGGMRQRVGIARALAADPRFL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446491464 157 LMDEPFGALDPVTRGALQQEMTRIHRLLGRTIVLVTHDIDEALRLAEHLVLMDhgevvqqGNPLTMLTRPANDFVRQF 234
Cdd:COG4525 157 LMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHSVEEALFLATRLVVMS-------PGPGRIVERLELDFSRRF 227
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
19-217 |
2.65e-54 |
|
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: 175.95 E-value: 2.65e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 19 DLNLNFQ-EGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAG------EEIRSLPVLelRRRMGYAIQSIGLFPHWS 91
Cdd:cd03297 14 TLKIDFDlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGtvlfdsRKKINLPPQ--QRKIGLVFQQYALFPHLN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 92 VAQNIATVpqLQKWSRARIDDRIDELMALLGLESnLRERYPHQLSGGQQQRVGVARALAADPQVLLMDEPFGALDPVTRG 171
Cdd:cd03297 92 VRENLAFG--LKRKRNREDRISVDELLDLLGLDH-LLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRL 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 446491464 172 ALQQEMTRIHRLLGRTIVLVTHDIDEALRLAEHLVLMDHGEVVQQG 217
Cdd:cd03297 169 QLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
2-213 |
4.19e-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: 4.19e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 2 IEFSHVSKLFGAQKAVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEIRSLPVlELRRRMGYAI 81
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPE-EVKRRIGYLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 82 QSIGLFPHWSVAQNIatvpqlqkwsrariddridelmallglesnlreryphQLSGGQQQRVGVARALAADPQVLLMDEP 161
Cdd:cd03230 80 EEPSLYENLTVRENL-------------------------------------KLSGGMKQRLALAQALLHDPELLILDEP 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446491464 162 FGALDPVTRGALQQEMTRIHRlLGRTIVLVTHDIDEALRLAEHLVLMDHGEV 213
Cdd:cd03230 123 TSGLDPESRREFWELLRELKK-EGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
1-239 |
5.41e-54 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 176.40 E-value: 5.41e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 1 MIEFSHVSKLF-GAQKAVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEIRSLP---VLELRRR 76
Cdd:COG3638 2 MLELRNLSKRYpGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRgraLRRLRRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 77 MGYAIQSIGLFPHWSVAQNI-----ATVPQLQKWSRARIDDRIDELMALL---GLESNLRERyPHQLSGGQQQRVGVARA 148
Cdd:COG3638 82 IGMIFQQFNLVPRLSVLTNVlagrlGRTSTWRSLLGLFPPEDRERALEALervGLADKAYQR-ADQLSGGQQQRVAIARA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 149 LAADPQVLLMDEPFGALDPVTRGALQQEMTRIHRLLGRTIVLVTHDIDEALRLAEHLVLMDHGEVVQQGNPlTMLTRpan 228
Cdd:COG3638 161 LVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRVVFDGPP-AELTD--- 236
|
250
....*....|.
gi 446491464 229 DFVRQFFGRSE 239
Cdd:COG3638 237 AVLREIYGGEA 247
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1-236 |
5.59e-54 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 180.42 E-value: 5.59e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 1 MIEFSHVSKLFGAQKAVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEIRSLPvlELRRRMGYA 80
Cdd:PRK11607 19 LLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVP--PYQRPINMM 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 81 IQSIGLFPHWSVAQNIATVPQLQKWSRARIDDRIDELMALLGLEsNLRERYPHQLSGGQQQRVGVARALAADPQVLLMDE 160
Cdd:PRK11607 97 FQSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQ-EFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDE 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446491464 161 PFGALDPVTRGALQQEMTRIHRLLGRTIVLVTHDIDEALRLAEHLVLMDHGEVVQQGNPLTMLTRPANDFVRQFFG 236
Cdd:PRK11607 176 PMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAEFIG 251
|
|
| PhnT |
TIGR03258 |
2-aminoethylphosphonate ABC transport system, ATP-binding component PhnT; This ATP-binding ... |
2-240 |
3.21e-53 |
|
2-aminoethylphosphonate ABC transport system, ATP-binding component PhnT; This ATP-binding component of an ABC transport system is found in Salmonella and Burkholderia lineages in the vicinity of enzymes for the breakdown of 2-aminoethylphosphonate.
Pssm-ID: 132302 [Multi-domain] Cd Length: 362 Bit Score: 177.88 E-value: 3.21e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 2 IEFSHVSKLFGAQKAVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHD--SGEIRFAGEEIRSLPvlELRRRMGY 79
Cdd:TIGR03258 6 IRIDHLRVAYGANTVLDDLSLEIEAGELLALIGKSGCGKTTLLRAIAGFVKAAglTGRIAIADRDLTHAP--PHKRGLAL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 80 AIQSIGLFPHWSVAQNIATVPQLQKWSRARIDDRIDELMALLGLeSNLRERYPHQLSGGQQQRVGVARALAADPQVLLMD 159
Cdd:TIGR03258 84 LFQNYALFPHLKVEDNVAFGLRAQKMPKADIAERVADALKLVGL-GDAAAHLPAQLSGGMQQRIAIARAIAIEPDVLLLD 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 160 EPFGALDPVTRGALQQEMTRIHRLLGR-TIVLVTHDIDEALRLAEHLVLMDHGEVVQQGNPLTMLTRPANDFVRQFFGRS 238
Cdd:TIGR03258 163 EPLSALDANIRANMREEIAALHEELPElTILCVTHDQDDALTLADKAGIMKDGRLAAHGEPQALYDAPADGFAAEFLGAA 242
|
..
gi 446491464 239 EL 240
Cdd:TIGR03258 243 NI 244
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
2-213 |
3.47e-52 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 170.38 E-value: 3.47e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 2 IEFSHVSKLFGAQKAVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEIRSLPVLELRRRMGYAI 81
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 82 QSIGLFPHwSVAQNIATVPQLQKwsRARIDDRIDELMALLGLESNLRERYPHQLSGGQQQRVGVARALAADPQVLLMDEP 161
Cdd:COG4619 81 QEPALWGG-TVRDNLPFPFQLRE--RKFDRERALELLERLGLPPDILDKPVERLSGGERQRLALIRALLLQPDVLLLDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446491464 162 FGALDPVTRGALQQEMTRIHRLLGRTIVLVTHDIDEALRLAEHLVLMDHGEV 213
Cdd:COG4619 158 TSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| 3a0107s01c2 |
TIGR00972 |
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein ... |
2-228 |
6.60e-52 |
|
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: 170.94 E-value: 6.60e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 2 IEFSHVSKLFGAQKAVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVE-----HDSGEIRFAGEEIRS--LPVLELR 74
Cdd:TIGR00972 2 IEIENLNLFYGEKEALKNINLDIPKNQVTALIGPSGCGKSTLLRSLNRMNDlvpgvRIEGKVLFDGQDIYDkkIDVVELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 75 RRMGYAIQSIGLFPHwSVAQNIATVPQLQKW-SRARIDDRIDELMALLGLESNLRER---YPHQLSGGQQQRVGVARALA 150
Cdd:TIGR00972 82 RRVGMVFQKPNPFPM-SIYDNIAYGPRLHGIkDKKELDEIVEESLKKAALWDEVKDRlhdSALGLSGGQQQRLCIARALA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446491464 151 ADPQVLLMDEPFGALDPVTRGALQQEMTRIHRLLgrTIVLVTHDIDEALRLAEHLVLMDHGEVVQQGNPLTMLTRPAN 228
Cdd:TIGR00972 161 VEPEVLLLDEPTSALDPIATGKIEELIQELKKKY--TIVIVTHNMQQAARISDRTAFFYDGELVEYGPTEQIFTNPKE 236
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
2-219 |
6.96e-52 |
|
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: 170.83 E-value: 6.96e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 2 IEFSHVSKLFGAQK-AVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEIRSLPVLEL---RRRM 77
Cdd:cd03256 1 IEVENLSKTYPNGKkALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALrqlRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 78 GYAIQSIGLFPHWSVAQNI-----ATVPQLqkWSRARIDDRIDELMAL-----LGLESNLRERyPHQLSGGQQQRVGVAR 147
Cdd:cd03256 81 GMIFQQFNLIERLSVLENVlsgrlGRRSTW--RSLFGLFPKEEKQRALaalerVGLLDKAYQR-ADQLSGGQQQRVAIAR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446491464 148 ALAADPQVLLMDEPFGALDPVTRGALQQEMTRIHRLLGRTIVLVTHDIDEALRLAEHLVLMDHGEVVQQGNP 219
Cdd:cd03256 158 ALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPP 229
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-219 |
7.38e-52 |
|
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: 170.99 E-value: 7.38e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 1 MIEFSHVSKLFGAQKAVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEIRSLPVLELRRR-MGY 79
Cdd:COG0411 4 LLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIARLgIAR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 80 AIQSIGLFPHWSVAQNIATVPQLQ---------------KWSRARIDDRIDELMALLGLESnLRERYPHQLSGGQQQRVG 144
Cdd:COG0411 84 TFQNPRLFPELTVLENVLVAAHARlgrgllaallrlpraRREEREARERAEELLERVGLAD-RADEPAGNLSYGQQRRLE 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446491464 145 VARALAADPQVLLMDEPFGALDPVTRGALQQEMTRIHRLLGRTIVLVTHDIDEALRLAEHLVLMDHGEVVQQGNP 219
Cdd:COG0411 163 IARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGTP 237
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
2-218 |
8.00e-52 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 170.58 E-value: 8.00e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 2 IEFSHVSKLFGAQKAVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEE------IRSLPVLELRR 75
Cdd:COG4161 3 IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQfdfsqkPSEKAIRLLRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 76 RMGYAIQSIGLFPHWSVAQNIATVP-QLQKWSRARIDDRIDELMALLGLeSNLRERYPHQLSGGQQQRVGVARALAADPQ 154
Cdd:COG4161 83 KVGMVFQQYNLWPHLTVMENLIEAPcKVLGLSKEQAREKAMKLLARLRL-TDKADRFPLHLSGGQQQRVAIARALMMEPQ 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446491464 155 VLLMDEPFGALDPvtrgALQQEMTRIHRLL---GRTIVLVTHDIDEALRLAEHLVLMDHGEVVQQGN 218
Cdd:COG4161 162 VLLFDEPTAALDP----EITAQVVEIIRELsqtGITQVIVTHEVEFARKVASQVVYMEKGRIIEQGD 224
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
12-256 |
2.29e-51 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 174.07 E-value: 2.29e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 12 GAQKAVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEIRSLPVLELR----RRMGYAIQSIGLF 87
Cdd:PRK10070 39 GLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELRevrrKKIAMVFQSFALM 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 88 PHWSVAQNIATVPQLQKWSRARIDDRIDELMALLGLEsNLRERYPHQLSGGQQQRVGVARALAADPQVLLMDEPFGALDP 167
Cdd:PRK10070 119 PHMTVLDNTAFGMELAGINAEERREKALDALRQVGLE-NYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDP 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 168 VTRGALQQEMTRIHRLLGRTIVLVTHDIDEALRLAEHLVLMDHGEVVQQGNPLTMLTRPANDFVRQFFgrseLGVRLLSL 247
Cdd:PRK10070 198 LIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFF----RGVDISQV 273
|
....*....
gi 446491464 248 RSVADYVRR 256
Cdd:PRK10070 274 FSAKDIARR 282
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-227 |
6.04e-51 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 168.34 E-value: 6.04e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 1 MIEFSHVSKLFGAQKAVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEIRslpvlELRRRMGYA 80
Cdd:COG1121 6 AIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPR-----RARRRIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 81 IQSIGL---FPhwsvaqniATV---------PQLQKWSRARIDDR--IDELMALLGLESnLRERYPHQLSGGQQQRVGVA 146
Cdd:COG1121 81 PQRAEVdwdFP--------ITVrdvvlmgryGRRGLFRRPSRADReaVDEALERVGLED-LADRPIGELSGGQQQRVLLA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 147 RALAADPQVLLMDEPFGALDPVTRGALQQEMTRIHRlLGRTIVLVTHDIDEALRLAEHLVLMDHGeVVQQGNPLTMLTRP 226
Cdd:COG1121 152 RALAQDPDLLLLDEPFAGVDAATEEALYELLRELRR-EGKTILVVTHDLGAVREYFDRVLLLNRG-LVAHGPPEEVLTPE 229
|
.
gi 446491464 227 A 227
Cdd:COG1121 230 N 230
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
3-217 |
8.87e-51 |
|
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: 165.69 E-value: 8.87e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 3 EFSHVSKLFGAQKAVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEIRSLPVLELRRRMGYaiq 82
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAY--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 83 siglfphwsvaqniatVPQlqkwsrariddrideLMALLGLEsNLRERYPHQLSGGQQQRVGVARALAADPQVLLMDEPF 162
Cdd:cd03214 78 ----------------VPQ---------------ALELLGLA-HLADRPFNELSGGERQRVLLARALAQEPPILLLDEPT 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446491464 163 GALDPVTRGALQQEMTRIHRLLGRTIVLVTHDIDEALRLAEHLVLMDHGEVVQQG 217
Cdd:cd03214 126 SHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
9-234 |
2.55e-50 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 167.28 E-value: 2.55e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 9 KLFGAQKAVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEIRSLP-------------VLELRR 75
Cdd:COG4598 16 KSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIRLKPdrdgelvpadrrqLQRIRT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 76 RMGYAIQSIGLFPHWSVAQNIATVP-QLQKWSRARIDDRIDELMALLGLeSNLRERYPHQLSGGQQQRVGVARALAADPQ 154
Cdd:COG4598 96 RLGMVFQSFNLWSHMTVLENVIEAPvHVLGRPKAEAIERAEALLAKVGL-ADKRDAYPAHLSGGQQQRAAIARALAMEPE 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 155 VLLMDEPFGALDPvtrgALQQEMTRIHRLL---GRTIVLVTHDIDEALRLAEHLVLMDHGEVVQQGNPLTMLTRPANDFV 231
Cdd:COG4598 175 VMLFDEPTSALDP----ELVGEVLKVMRDLaeeGRTMLVVTHEMGFARDVSSHVVFLHQGRIEEQGPPAEVFGNPKSERL 250
|
...
gi 446491464 232 RQF 234
Cdd:COG4598 251 RQF 253
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1-237 |
5.16e-50 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 165.70 E-value: 5.16e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 1 MIEFSHVSKLFGAQKAvnDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEIRSLPVLElrRRMGYA 80
Cdd:COG3840 1 MLRLDDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAE--RPVSML 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 81 IQSIGLFPHWSVAQNIA---------TVPQLQkwsrariddRIDELMALLGLEsNLRERYPHQLSGGQQQRVGVARALAA 151
Cdd:COG3840 77 FQENNLFPHLTVAQNIGlglrpglklTAEQRA---------QVEQALERVGLA-GLLDRLPGQLSGGQRQRVALARCLVR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 152 DPQVLLMDEPFGALDPvtrgALQQEM----TRIHRLLGRTIVLVTHDIDEALRLAEHLVLMDHGEVVQQGNPLTMLTRPA 227
Cdd:COG3840 147 KRPILLLDEPFSALDP----ALRQEMldlvDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEP 222
|
250
....*....|
gi 446491464 228 NDFVRQFFGR 237
Cdd:COG3840 223 PPALAAYLGI 232
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
2-219 |
6.17e-50 |
|
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: 165.30 E-value: 6.17e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 2 IEFSHVSKLFGAQKAVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEIRSLPVLELRRR-MGYA 80
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARLgIGRT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 81 IQSIGLFPHWSVAQNIATVPQLQK----------WSRARIDDRIDELMALLGLeSNLRERYPHQLSGGQQQRVGVARALA 150
Cdd:cd03219 81 FQIPRLFPELTVLENVMVAAQARTgsglllararREEREARERAEELLERVGL-ADLADRPAGELSYGQQRRLEIARALA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446491464 151 ADPQVLLMDEPFGALDPVTRGALQQEMTRIHRlLGRTIVLVTHDIDEALRLAEHLVLMDHGEVVQQGNP 219
Cdd:cd03219 160 TDPKLLLLDEPAAGLNPEETEELAELIRELRE-RGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTP 227
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2-236 |
3.04e-49 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 164.44 E-value: 3.04e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 2 IEFSHVSKLFGAQKAVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLveHD-------SGEIRFAGEEI--RSLPVLE 72
Cdd:COG1117 12 IEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRM--NDlipgarvEGEILLDGEDIydPDVDVVE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 73 LRRRMGYAIQSIGLFPHwSVAQNIATVPQLQKW-SRARIDDRIdelmallglESNLR------------ERYPHQLSGGQ 139
Cdd:COG1117 90 LRRRVGMVFQKPNPFPK-SIYDNVAYGLRLHGIkSKSELDEIV---------EESLRkaalwdevkdrlKKSALGLSGGQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 140 QQRVGVARALAADPQVLLMDEPFGALDPVTRGALqqEMTrIHRLLGR-TIVLVTHDIDEALRLAEHLVLMDHGEVVQQGN 218
Cdd:COG1117 160 QQRLCIARALAVEPEVLLMDEPTSALDPISTAKI--EEL-ILELKKDyTIVIVTHNMQQAARVSDYTAFFYLGELVEFGP 236
|
250 260
....*....|....*....|..
gi 446491464 219 PLTMLTRPAN----DFVRQFFG 236
Cdd:COG1117 237 TEQIFTNPKDkrteDYITGRFG 258
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-282 |
5.92e-49 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 164.90 E-value: 5.92e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 1 MIEFSHVSKLFGAQKAVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEIRSlpvlELRRRMGYA 80
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDP----EDRRRIGYL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 81 IQSIGLFPHWSVAQNIATVPQLQKWSRARIDDRIDELMALLGLESNLRERYpHQLSGGQQQRVGVARALAADPQVLLMDE 160
Cdd:COG4152 77 PEERGLYPKMKVGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDRANKKV-EELSKGNQQKVQLIAALLHDPELLILDE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 161 PFGALDPVTRGALQQEMTRiHRLLGRTIVLVTHDIDEALRLAEHLVLMDHGEVVQQGNPltmltrpanDFVRQFFGRSEL 240
Cdd:COG4152 156 PFSGLDPVNVELLKDVIRE-LAAKGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSV---------DEIRRQFGRNTL 225
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 446491464 241 GVRLLS----LRSVADyVRREERAEGEA---LAEEMTLRDALSLFVARG 282
Cdd:COG4152 226 RLEADGdagwLRALPG-VTVVEEDGDGAelkLEDGADAQELLRALLARG 273
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-237 |
1.74e-48 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 162.23 E-value: 1.74e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 1 MIEFSHVSKLFGAQKAVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEI---RSLP-----VLE 72
Cdd:PRK11264 3 AIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIdtaRSLSqqkglIRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 73 LRRRMGYAIQSIGLFPHWSVAQNIATVP-QLQKWSRARIDDRIDELMALLGLeSNLRERYPHQLSGGQQQRVGVARALAA 151
Cdd:PRK11264 83 LRQHVGFVFQNFNLFPHRTVLENIIEGPvIVKGEPKEEATARARELLAKVGL-AGKETSYPRRLSGGQQQRVAIARALAM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 152 DPQVLLMDEPFGALDPVTRGALqqeMTRIHRLL--GRTIVLVTHDIDEALRLAEHLVLMDHGEVVQQGNPLTMLTRPAND 229
Cdd:PRK11264 162 RPEVILFDEPTSALDPELVGEV---LNTIRQLAqeKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADPQQP 238
|
....*...
gi 446491464 230 FVRQFFGR 237
Cdd:PRK11264 239 RTRQFLEK 246
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
2-240 |
3.08e-48 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 164.51 E-value: 3.08e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 2 IEFSHVSKLFGAQKAVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEI--RSLPvlelRRRMGY 79
Cdd:PRK11432 7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVthRSIQ----QRDICM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 80 AIQSIGLFPHWSVAQNIATVPQLQKWSRARIDDRIDELMALLGLESnLRERYPHQLSGGQQQRVGVARALAADPQVLLMD 159
Cdd:PRK11432 83 VFQSYALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAG-FEDRYVDQISGGQQQRVALARALILKPKVLLFD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 160 EPFGALDPVTRGALQQEMTRIHRLLGRTIVLVTHDIDEALRLAEHLVLMDHGEVVQQGNPLTMLTRPANDFVRQFFGRSE 239
Cdd:PRK11432 162 EPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPASRFMASFMGDAN 241
|
.
gi 446491464 240 L 240
Cdd:PRK11432 242 I 242
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1-234 |
6.97e-48 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 161.02 E-value: 6.97e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 1 MIEFSHVSKLFGAQKAVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGeeirsLPVLELRRRMGYA 80
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDG-----KPVEGPGAERGVV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 81 IQSIGLFPHWSVAQNIATVPQLQKWSRARIDDRIDELMALLGLESnLRERYPHQLSGGQQQRVGVARALAADPQVLLMDE 160
Cdd:PRK11248 76 FQNEGLLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEG-AEKRYIWQLSGGQRQRVGIARALAANPQLLLLDE 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446491464 161 PFGALDPVTRGALQQEMTRIHRLLGRTIVLVTHDIDEALRLAEHLVLMDHGevvqqgnPLTMLTRPANDFVRQF 234
Cdd:PRK11248 155 PFGALDAFTREQMQTLLLKLWQETGKQVLLITHDIEEAVFMATELVLLSPG-------PGRVVERLPLNFARRF 221
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
2-217 |
7.39e-48 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 160.18 E-value: 7.39e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 2 IEFSHVSKLFGAQKAVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAG------EEIRSLPVLELRR 75
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGnhfdfsKTPSDKAIRELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 76 RMGYAIQSIGLFPHWSVAQNIATVP-QLQKWSRARIDDRIDELMALLGLEsNLRERYPHQLSGGQQQRVGVARALAADPQ 154
Cdd:PRK11124 83 NVGMVFQQYNLWPHLTVQQNLIEAPcRVLGLSKDQALARAEKLLERLRLK-PYADRFPLHLSGGQQQRVAIARALMMEPQ 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446491464 155 VLLMDEPFGALDP-VTrgalQQEMTRIHRL--LGRTIVLVTHDIDEALRLAEHLVLMDHGEVVQQG 217
Cdd:PRK11124 162 VLLFDEPTAALDPeIT----AQIVSIIRELaeTGITQVIVTHEVEVARKTASRVVYMENGHIVEQG 223
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1-226 |
1.81e-47 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 159.48 E-value: 1.81e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 1 MIEFSHVSKLFGAQKAVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEIRSLPVLELRRRMgyA 80
Cdd:COG4604 1 MIEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRL--A 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 81 I--QSI--------------GLFPHwsvaqniatvpqlqkwSRARI--DDR--IDELMALLGLESnLRERYPHQLSGGQQ 140
Cdd:COG4604 79 IlrQENhinsrltvrelvafGRFPY----------------SKGRLtaEDReiIDEAIAYLDLED-LADRYLDELSGGQR 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 141 QRVGVARALAADPQVLLMDEPFGALDPvtRGALQQeMTRIHRL---LGRTIVLVTHDIDEALRLAEHLVLMDHGEVVQQG 217
Cdd:COG4604 142 QRAFIAMVLAQDTDYVLLDEPLNNLDM--KHSVQM-MKLLRRLadeLGKTVVIVLHDINFASCYADHIVAMKDGRVVAQG 218
|
....*....
gi 446491464 218 NPLTMLTRP 226
Cdd:COG4604 219 TPEEIITPE 227
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
1-219 |
4.21e-47 |
|
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: 158.62 E-value: 4.21e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 1 MIEFSHVSKLFGAQK-AVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEIRSL---PVLELRRR 76
Cdd:TIGR02315 1 MLEVENLSKVYPNGKqALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLrgkKLRKLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 77 MGYAIQSIGLFPHWSVAQNI-----ATVPQLQKWSR--ARIDDRID-ELMALLGLESNLRERyPHQLSGGQQQRVGVARA 148
Cdd:TIGR02315 81 IGMIFQHYNLIERLTVLENVlhgrlGYKPTWRSLLGrfSEEDKERAlSALERVGLADKAYQR-ADQLSGGQQQRVAIARA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446491464 149 LAADPQVLLMDEPFGALDPVTRGALQQEMTRIHRLLGRTIVLVTHDIDEALRLAEHLVLMDHGEVVQQGNP 219
Cdd:TIGR02315 160 LAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAP 230
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
17-226 |
5.14e-47 |
|
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: 158.01 E-value: 5.14e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 17 VNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEIRSlPVLElrrRMgYAIQSIGLFPHWSVAQNI 96
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITE-PGPD---RM-VVFQNYSLLPWLTVRENI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 97 A-----TVPQLQKWSRARIddrIDELMALLGLeSNLRERYPHQLSGGQQQRVGVARALAADPQVLLMDEPFGALDPVTRG 171
Cdd:TIGR01184 76 AlavdrVLPDLSKSERRAI---VEEHIALVGL-TEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRG 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446491464 172 ALQQEMTRIHRLLGRTIVLVTHDIDEALRLAEHLVLMDHGEVVQQGNPLTM-LTRP 226
Cdd:TIGR01184 152 NLQEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAANIGQILEVpFPRP 207
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
2-225 |
1.56e-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: 166.55 E-value: 1.56e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 2 IEFSHVSklFG----AQKAVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEIRSLPVLELRRRM 77
Cdd:COG2274 474 IELENVS--FRypgdSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQI 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 78 GYAIQSIGLFpHWSVAQNI------ATVPQLQKWSR-ARIDDRIDELMalLGLESNLRERYpHQLSGGQQQRVGVARALA 150
Cdd:COG2274 552 GVVLQDVFLF-SGTIRENItlgdpdATDEEIIEAARlAGLHDFIEALP--MGYDTVVGEGG-SNLSGGQRQRLAIARALL 627
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446491464 151 ADPQVLLMDEPFGALDPVTRGALQQEMTRIHRllGRTIVLVTHDiDEALRLAEHLVLMDHGEVVQQGNPLTMLTR 225
Cdd:COG2274 628 RNPRILILDEATSALDAETEAIILENLRRLLK--GRTVIIIAHR-LSTIRLADRIIVLDKGRIVEDGTHEELLAR 699
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-227 |
2.36e-46 |
|
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: 158.68 E-value: 2.36e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 1 MIEFSHVSKLF----GAQKAVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVE---HDSGEIRFAGEEIRSLPVLEL 73
Cdd:COG0444 1 LLEVRNLKVYFptrrGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPppgITSGEILFDGEDLLKLSEKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 74 RRRMGYAIQSIglF--------PHWSVAQNIATVPQL-QKWSRARIDDRIDELMALLGLESNLR--ERYPHQLSGGQQQR 142
Cdd:COG0444 81 RKIRGREIQMI--FqdpmtslnPVMTVGDQIAEPLRIhGGLSKAEARERAIELLERVGLPDPERrlDRYPHELSGGMRQR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 143 VGVARALAADPQVLLMDEPFGALDPVTRGALQQEMTRIHRLLGRTIVLVTHDIDEALRLAEHLVLMDHGEVVQQGNPLTM 222
Cdd:COG0444 159 VMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGPVEEL 238
|
....*
gi 446491464 223 LTRPA 227
Cdd:COG0444 239 FENPR 243
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
2-220 |
3.97e-46 |
|
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: 154.97 E-value: 3.97e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 2 IEFSHVSKLFG--AQKAVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEIRSLPVlELRRRMGY 79
Cdd:cd03263 1 LQIRNLTKTYKkgTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRK-AARQSLGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 80 AIQSIGLFPHWSVAQNIATVPQLQKWSRARIDDRIDELMALLGLESnLRERYPHQLSGGQQQRVGVARALAADPQVLLMD 159
Cdd:cd03263 80 CPQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTD-KANKRARTLSGGMKRKLSLAIALIGGPSVLLLD 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446491464 160 EPFGALDPVTRgalqqemTRIHRLL-----GRTIVLVTHDIDEALRLAEHLVLMDHGEVVQQGNPL 220
Cdd:cd03263 159 EPTSGLDPASR-------RAIWDLIlevrkGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQ 217
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
2-240 |
4.02e-46 |
|
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: 156.44 E-value: 4.02e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 2 IEFSHVSKLF--GAQKAVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEIRSlP--VLELRRRM 77
Cdd:TIGR04520 1 IEVENVSFSYpeSEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLD-EenLWEIRKKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 78 GYAIQS-----IGLfphwSVAQNIATVPQLQKWSRARIDDRIDELMALLGLESnLRERYPHQLSGGQQQRVGVARALAAD 152
Cdd:TIGR04520 80 GMVFQNpdnqfVGA----TVEDDVAFGLENLGVPREEMRKRVDEALKLVGMED-FRDREPHLLSGGQKQRVAIAGVLAMR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 153 PQVLLMDEPFGALDPVTRGALQQEMTRIHRLLGRTIVLVTHDIDEALrLAEHLVLMDHGEVVQQGNPltmltrpandfvR 232
Cdd:TIGR04520 155 PDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEAV-LADRVIVMNKGKIVAEGTP------------R 221
|
....*...
gi 446491464 233 QFFGRSEL 240
Cdd:TIGR04520 222 EIFSQVEL 229
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
1-212 |
6.67e-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: 154.33 E-value: 6.67e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 1 MIEFSHVSKLF-GAQKAVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEIRSLP---VLELRRR 76
Cdd:TIGR02673 1 MIEFHNVSKAYpGGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLRgrqLPLLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 77 MGYAIQSIGLFPHWSVAQNIATVPQLQKWSRARIDDRIDELMALLGLESNLRErYPHQLSGGQQQRVGVARALAADPQVL 156
Cdd:TIGR02673 81 IGVVFQDFRLLPDRTVYENVALPLEVRGKKEREIQRRVGAALRQVGLEHKADA-FPEQLSGGEQQRVAIARAIVNSPPLL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446491464 157 LMDEPFGALDPVTRGALQQEMTRIHRlLGRTIVLVTHDIDEALRLAEHLVLMDHGE 212
Cdd:TIGR02673 160 LADEPTGNLDPDLSERILDLLKRLNK-RGTTVIVATHDLSLVDRVAHRVIILDDGR 214
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
2-212 |
6.96e-46 |
|
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: 152.92 E-value: 6.96e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 2 IEFSHVSklF----GAQKAVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEIRSLPVLELRRRM 77
Cdd:cd03228 1 IEFKNVS--FsypgRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 78 GYAIQSIGLFpHWSVAQNIatvpqlqkwsrariddridelmallglesnlreryphqLSGGQQQRVGVARALAADPQVLL 157
Cdd:cd03228 79 AYVPQDPFLF-SGTIRENI--------------------------------------LSGGQRQRIAIARALLRDPPILI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446491464 158 MDEPFGALDPVTRGALQQEMTRIHRllGRTIVLVTHDIdEALRLAEHLVLMDHGE 212
Cdd:cd03228 120 LDEATSALDPETEALILEALRALAK--GKTVIVIAHRL-STIRDADRIIVLDDGR 171
|
|
| ABC_ATP_SaoA |
NF040729 |
ABC transporter ATP-binding protein SaoA; SaoA is the ATP-binding subunit of an ABC ... |
2-215 |
7.61e-46 |
|
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: 155.28 E-value: 7.61e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 2 IEFSHVSKLFGAQKAVN----DLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEIrSLPVLElrrrM 77
Cdd:NF040729 2 LKIQNISKTFINNKKENevlkDISFDVEEGEFVSLLGPSGCGKTTLLTIIAGFQNATSGEILVNGNEV-TKPGPD----R 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 78 GYAIQSIGLFPHWSVAQNIATVPQLQKWSRARIDDRIDELMALLGLESNlRERYPHQLSGGQQQRVGVARALAADPQVLL 157
Cdd:NF040729 77 GFVFQNYALFPWMTVKENIEYPMKQQKMPKQEREKRLNELLEMAQLTGK-ENLYPHQISGGMKQRTAVIRALACKPEVLL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 158 MDEPFGALDPVTRGALQQEMTRIHRLLGRTIVLVTHDIDEALRLAEHLVLM--DHGEVVQ 215
Cdd:NF040729 156 MDEPLGAVDFQMRQILQEELESIWLKDKTTVLMVTHDVDEAVYLSDRVIVMsrDKGKILE 215
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-236 |
1.41e-45 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 157.70 E-value: 1.41e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 1 MIEFSHVSKLF-GAQKAVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEIRSLpvlELRRRmGY 79
Cdd:PRK11650 3 GLKLQAVRKSYdGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNEL---EPADR-DI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 80 AI--QSIGLFPHWSVAQNIATVPQLQKWSRARIDDRIDELMALLGLESNLrERYPHQLSGGQQQRVGVARALAADPQVLL 157
Cdd:PRK11650 79 AMvfQNYALYPHMSVRENMAYGLKIRGMPKAEIEERVAEAARILELEPLL-DRKPRELSGGQRQRVAMGRAIVREPAVFL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446491464 158 MDEPFGALDPVTRGALQQEMTRIHRLLGRTIVLVTHDIDEALRLAEHLVLMDHGEVVQQGNPLTMLTRPANDFVRQFFG 236
Cdd:PRK11650 158 FDEPLSNLDAKLRVQMRLEIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGGVAEQIGTPVEVYEKPASTFVASFIG 236
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-219 |
3.82e-45 |
|
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: 160.69 E-value: 3.82e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 2 IEFSHVSKLF-GAQKAVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEIRSLPVLELRRRMGYA 80
Cdd:COG4988 337 IELEDVSFSYpGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWV 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 81 IQSIGLFpHWSVAQNI------ATVPQLQKWSR-ARIDDRIDELMAllGLESNLRERyPHQLSGGQQQRVGVARALAADP 153
Cdd:COG4988 417 PQNPYLF-AGTIRENLrlgrpdASDEELEAALEaAGLDEFVAALPD--GLDTPLGEG-GRGLSGGQAQRLALARALLRDA 492
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446491464 154 QVLLMDEPFGALDPVTRGALQQEMTRIHRllGRTIVLVTHDIdEALRLAEHLVLMDHGEVVQQGNP 219
Cdd:COG4988 493 PLLLLDEPTAHLDAETEAEILQALRRLAK--GRTVILITHRL-ALLAQADRILVLDDGRIVEQGTH 555
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
3-212 |
8.12e-45 |
|
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: 149.70 E-value: 8.12e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 3 EFSHVSKLFGAQKAVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEIRSLPVLELRRRMGYAiq 82
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYV-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 83 siglfphwsvaqniatvpqlqkwsrariddridelmallglesnlrerypHQLSGGQQQRVGVARALAADPQVLLMDEPF 162
Cdd:cd00267 79 --------------------------------------------------PQLSGGQRQRVALARALLLNPDLLLLDEPT 108
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446491464 163 GALDPVTRGALQQEMTRIHRlLGRTIVLVTHDIDEALRLAEHLVLMDHGE 212
Cdd:cd00267 109 SGLDPASRERLLELLRELAE-EGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
2-217 |
1.44e-44 |
|
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: 150.81 E-value: 1.44e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 2 IEFSHVSKLFGAQKAVNDLNLNFQEGsFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEIRSLPVlELRRRMGYAI 81
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQ-KLRRRIGYLP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 82 QSIGLFPHWSVAQNIATVPQLQKWSRARIDDRIDELMALLGLEsNLRERYPHQLSGGQQQRVGVARALAADPQVLLMDEP 161
Cdd:cd03264 79 QEFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLG-DRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEP 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446491464 162 FGALDPVTRgalqqemTRIHRLLG-----RTIVLVTHDIDEALRLAEHLVLMDHGEVVQQG 217
Cdd:cd03264 158 TAGLDPEER-------IRFRNLLSelgedRIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
2-227 |
2.55e-44 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 152.48 E-value: 2.55e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 2 IEFSHVSKLFG-----AQKAVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEI----RSLPVLE 72
Cdd:PRK13634 3 ITFQKVEHRYQyktpfERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVItagkKNKKLKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 73 LRRRMGYAIQsiglFPHW-----SVAQNIATVPQLQKWSRARIDDRIDELMALLGLESNLRERYPHQLSGGQQQRVGVAR 147
Cdd:PRK13634 83 LRKKVGIVFQ----FPEHqlfeeTVEKDICFGPMNFGVSEEDAKQKAREMIELVGLPEELLARSPFELSGGQMRRVAIAG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 148 ALAADPQVLLMDEPFGALDPVTRGALQQEMTRIHRLLGRTIVLVTHDIDEALRLAEHLVLMDHGEVVQQGNPLTMLTRPA 227
Cdd:PRK13634 159 VLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADPD 238
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
2-233 |
8.64e-44 |
|
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: 149.62 E-value: 8.64e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 2 IEFSHVSKLFGAQKAVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEIRSLPVLELRRR-MGYA 80
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRARLgIGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 81 IQSIGLFPHWSVAQNIATVPQLQKWSRARIDDRIDELMALLGLESnLRERYPHQLSGGQQQRVGVARALAADPQVLLMDE 160
Cdd:cd03218 81 PQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITH-LRKSKASSLSGGERRRVEIARALATNPKFLLLDE 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446491464 161 PFGALDPVTRGALQQemtRIHRLLGRTI-VLVT-HDIDEALRLAEHLVLMDHGEVVQQGNPLTMLtrpANDFVRQ 233
Cdd:cd03218 160 PFAGVDPIAVQDIQK---IIKILKDRGIgVLITdHNVRETLSITDRAYIIYEGKVLAEGTPEEIA---ANELVRK 228
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
2-219 |
8.90e-44 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 157.25 E-value: 8.90e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 2 IEFSHVSklF---GAQKAVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEIRSLPVLELRRRMG 78
Cdd:COG1132 340 IEFENVS--FsypGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESLRRQIG 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 79 YAIQSIGLFpHWSVAQNI------ATVPQLQKWSR-ARIDDRIDELMAllGLESNLRERyPHQLSGGQQQRVGVARALAA 151
Cdd:COG1132 418 VVPQDTFLF-SGTIRENIrygrpdATDEEVEEAAKaAQAHEFIEALPD--GYDTVVGER-GVNLSGGQRQRIAIARALLK 493
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446491464 152 DPQVLLMDEPFGALDPVTRGALQQEMTRIHRllGRTIVLVTHDIdEALRLAEHLVLMDHGEVVQQGNP 219
Cdd:COG1132 494 DPPILILDEATSALDTETEALIQEALERLMK--GRTTIVIAHRL-STIRNADRILVLDDGRIVEQGTH 558
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-235 |
1.23e-43 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 149.41 E-value: 1.23e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 1 MIEFSHVSKLFGAQKAVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEIRSLPVLElRRRMG-- 78
Cdd:COG1137 3 TLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMHK-RARLGig 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 79 YAIQSIGLFPHWSVAQNIATVPQLQKWSRARIDDRIDELMALLGLEsNLRERYPHQLSGGQQQRVGVARALAADPQVLLM 158
Cdd:COG1137 82 YLPQEASIFRKLTVEDNILAVLELRKLSKKEREERLEELLEEFGIT-HLRKSKAYSLSGGERRRVEIARALATNPKFILL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446491464 159 DEPFGALDPVTRGALQQEmtrIHRLLGRTI-VLVT-HDIDEALRLAEHLVLMDHGEVVQQGNPLTMLtrpANDFVRQFF 235
Cdd:COG1137 161 DEPFAGVDPIAVADIQKI---IRHLKERGIgVLITdHNVRETLGICDRAYIISEGKVLAEGTPEEIL---NNPLVRKVY 233
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
6-194 |
2.27e-43 |
|
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly wide distribution consists of a polypeptide related to the lactococcin 972 (see TIGR01653) and multiple-membrane-spanning putative immunity protein (see TIGR01654). This model represents a small clade within the ABC transporters that regularly are found adjacent to these bacteriocin system gene pairs and are likely serve as export proteins. [Cellular processes, Toxin production and resistance, Transport and binding proteins, Unknown substrate]
Pssm-ID: 188353 [Multi-domain] Cd Length: 206 Bit Score: 147.76 E-value: 2.27e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 6 HVSKLFGAQKAVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEE---IRSLPVLELRR-RMGYAI 81
Cdd:TIGR03608 3 NISKKFGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQEtppLNSKKASKFRReKLGYLF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 82 QSIGLFPHWSVAQNIATVPQLQKWSRARIDDRIDELMALLGLESNLrERYPHQLSGGQQQRVGVARALAADPQVLLMDEP 161
Cdd:TIGR03608 83 QNFALIENETVEENLDLGLKYKKLSKKEKREKKKEALEKVGLNLKL-KQKIYELSGGEQQRVALARAILKPPPLILADEP 161
|
170 180 190
....*....|....*....|....*....|....*.
gi 446491464 162 FGALDPVTRgalqQEMTRIHRLL---GRTIVLVTHD 194
Cdd:TIGR03608 162 TGSLDPKNR----DEVLDLLLELndeGKTIIIVTHD 193
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
2-217 |
2.51e-43 |
|
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: 147.43 E-value: 2.51e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 2 IEFSHVSKLFGAQKAVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEIRSLPvlelRRRMGYAI 81
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAA----RNRIGYLP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 82 QSIGLFPHWSVAQNIATVPQLQKWSRARIDDRIDELMALLGLeSNLRERYPHQLSGGQQQRVGVARALAADPQVLLMDEP 161
Cdd:cd03269 77 EERGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLEL-SEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEP 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446491464 162 FGALDPVTRGALQQEMTRIHRlLGRTIVLVTHDIDEALRLAEHLVLMDHGEVVQQG 217
Cdd:cd03269 156 FSGLDPVNVELLKDVIRELAR-AGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| ABC_ATP_DarD |
NF038007 |
darobactin export ABC transporter ATP-binding protein; |
1-211 |
2.83e-43 |
|
darobactin export ABC transporter ATP-binding protein;
Pssm-ID: 411600 [Multi-domain] Cd Length: 218 Bit Score: 147.94 E-value: 2.83e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 1 MIEFSHVSKLFGAQ----KAVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEIRSLPVLE---L 73
Cdd:NF038007 1 MLNMQNAEKCYITKtiktKVLNHLNFSVEKGDFVSIMGPSGSGKSTLLNIIGMFDSLDSGSLTLAGKEVTNLSYSQkiiL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 74 RRRM-GYAIQSIGLFPHWSVAQNIATVPQLQKWSRARIDDRIDELMALLGLEsNLRERYPHQLSGGQQQRVGVARALAAD 152
Cdd:NF038007 81 RRELiGYIFQSFNLIPHLSIFDNVALPLKYRGVAKKERIERVNQVLNLFGID-NRRNHKPMQLSGGQQQRVAIARAMVSN 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446491464 153 PQVLLMDEPFGALDPVTRGALQQEMTRIHRlLGRTIVLVTHDiDEALRLAEHLVLMDHG 211
Cdd:NF038007 160 PALLLADEPTGNLDSKNARAVLQQLKYINQ-KGTTIIMVTHS-DEASTYGNRIINMKDG 216
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
2-219 |
3.28e-43 |
|
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: 147.52 E-value: 3.28e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 2 IEFSHVSKLFGAQKAVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEIRSLPVlELRRRMGYAI 81
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPR-EVRRRIGIVF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 82 QSIGLFPHWSVAQNIATVPQLQKWSRARIDDRIDELMALLGLeSNLRERYPHQLSGGQQQRVGVARALAADPQVLLMDEP 161
Cdd:cd03265 80 QDLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGL-LEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEP 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446491464 162 FGALDPVTRGALQQEMTRIHRLLGRTIVLVTHDIDEALRLAEHLVLMDHGEVVQQGNP 219
Cdd:cd03265 159 TIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTP 216
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
2-213 |
9.23e-43 |
|
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: 146.40 E-value: 9.23e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 2 IEFSHVSKLFGAQ-KAVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEIRSLP---VLELRRRM 77
Cdd:cd03292 1 IEFINVTKTYPNGtAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRgraIPYLRRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 78 GYAIQSIGLFPHWSVAQNIATVPQLQKWSRARIDDRIDELMALLGLESNLRErYPHQLSGGQQQRVGVARALAADPQVLL 157
Cdd:cd03292 81 GVVFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRA-LPAELSGGEQQRVAIARAIVNSPTILI 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446491464 158 MDEPFGALDPVTRGALQQEMTRIHrLLGRTIVLVTHDIDEALRLAEHLVLMDHGEV 213
Cdd:cd03292 160 ADEPTGNLDPDTTWEIMNLLKKIN-KAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
3-217 |
1.78e-42 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 145.37 E-value: 1.78e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 3 EFSHVSKLFGAQKAVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEeirslPVLELRRRMGYAIQ 82
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGK-----PLEKERKRIGYVPQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 83 ----------------SIGLFPHWSvaqniatvpqLQKWSRARIDDRIDELMALLGLeSNLRERYPHQLSGGQQQRVGVA 146
Cdd:cd03235 76 rrsidrdfpisvrdvvLMGLYGHKG----------LFRRLSKADKAKVDEALERVGL-SELADRQIGELSGGQQQRVLLA 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446491464 147 RALAADPQVLLMDEPFGALDPVTRGALQQEMTRIHRlLGRTIVLVTHDIDEALRLAEHLVLMDHgEVVQQG 217
Cdd:cd03235 145 RALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRR-EGMTILVVTHDLGLVLEYFDRVLLLNR-TVVASG 213
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-210 |
2.24e-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: 144.93 E-value: 2.24e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 1 MIEFSHVSKLFGAQKAVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEIRSLPVlELRRRMGYA 80
Cdd:COG4133 2 MLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDARE-DYRRRLAYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 81 IQSIGLFPHWSVAQNIATVPQLQKWSRARidDRIDELMALLGLESnLRERYPHQLSGGQQQRVGVARALAADPQVLLMDE 160
Cdd:COG4133 81 GHADGLKPELTVRENLRFWAALYGLRADR--EAIDEALEAVGLAG-LADLPVRQLSAGQKRRVALARLLLSPAPLWLLDE 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446491464 161 PFGALDPVTRGALQQEMTRiHRLLGRTIVLVTHDiDEALRLAEHLVLMDH 210
Cdd:COG4133 158 PFTALDAAGVALLAELIAA-HLARGGAVLLTTHQ-PLELAAARVLDLGDF 205
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1-224 |
6.06e-42 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 145.90 E-value: 6.06e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 1 MIEFSHVSKLFGAQK--AVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEIRSLPVLELRRRMG 78
Cdd:PRK13632 7 MIKVENVSFSYPNSEnnALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 79 YAIQS-----IGLfphwSVAQNIATVPQLQKWSRARIDDRIDELMALLGLESNLrERYPHQLSGGQQQRVGVARALAADP 153
Cdd:PRK13632 87 IIFQNpdnqfIGA----TVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYL-DKEPQNLSGGQKQRVAIASVLALNP 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446491464 154 QVLLMDEPFGALDPVTRGALQQEMTRIHRLLGRTIVLVTHDIDEALrLAEHLVLMDHGEVVQQGNPLTMLT 224
Cdd:PRK13632 162 EIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAI-LADKVIVFSEGKLIAQGKPKEILN 231
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
19-227 |
6.12e-42 |
|
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: 148.34 E-value: 6.12e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 19 DLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEIRS------LPVLelRRRMGYAIQSIGLFPHWSV 92
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDsrkgifLPPE--KRRIGYVFQEARLFPHLSV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 93 AQNIatvpqLQKWSRARIDDRI---DELMALLGLEsNLRERYPHQLSGGQQQRVGVARALAADPQVLLMDEPFGALDPVT 169
Cdd:TIGR02142 93 RGNL-----RYGMKRARPSERRisfERVIELLGIG-HLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPR 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446491464 170 RGALQQEMTRIHRLLGRTIVLVTHDIDEALRLAEHLVLMDHGEVVQQGNPLTMLTRPA 227
Cdd:TIGR02142 167 KYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPD 224
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
17-162 |
1.02e-41 |
|
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: 141.63 E-value: 1.02e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 17 VNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEIRSLPVLELRRRMGYAIQSIGLFPHWSVAQNI 96
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446491464 97 ATVPQLQKWSRARIDDRIDELMALLGLESNLRER---YPHQLSGGQQQRVGVARALAADPQVLLMDEPF 162
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEALEKLGLGDLADRPvgeRPGTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
13-219 |
1.94e-41 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 145.19 E-value: 1.94e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 13 AQKAVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEI--RSLPVLELRRRMGYAIQsiglFPHW 90
Cdd:PRK13637 19 EKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDItdKKVKLSDIRKKVGLVFQ----YPEY 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 91 -----SVAQNIATVPQLQKWSRARIDDRIDELMALLGLE-SNLRERYPHQLSGGQQQRVGVARALAADPQVLLMDEPFGA 164
Cdd:PRK13637 95 qlfeeTIEKDIAFGPINLGLSEEEIENRVKRAMNIVGLDyEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAG 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446491464 165 LDPVTRGALQQEMTRIHRLLGRTIVLVTHDIDEALRLAEHLVLMDHGEVVQQGNP 219
Cdd:PRK13637 175 LDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTP 229
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
9-296 |
3.49e-41 |
|
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: 144.84 E-value: 3.49e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 9 KLFGAQKAVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEIRSLPVlELRRRMGYAIQSIGLFP 88
Cdd:TIGR01188 1 KVYGDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVVREPR-KVRRSIGIVPQYASVDE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 89 HWSVAQNIATVPQLQKWSRARIDDRIDELMALLGLeSNLRERYPHQLSGGQQQRVGVARALAADPQVLLMDEPFGALDPV 168
Cdd:TIGR01188 80 DLTGRENLEMMGRLYGLPKDEAEERAEELLELFEL-GEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 169 TRGALQQEMTRIHRlLGRTIVLVTHDIDEALRLAEHLVLMDHGEVVQQGNPLTMLTRPANDFVRQFFG--------RSEL 240
Cdd:TIGR01188 159 TRRAIWDYIRALKE-EGVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPEELKRRLGKDTLESRPRdiqslkveVSML 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 446491464 241 GVRLL-SLRSVADYVRREERAEGEALAEEMTLRDALSLFVARGCEVLPVvnTQGQPS 296
Cdd:TIGR01188 238 IAELGeTGLGLLAVTVDSDRIKILVPDGDETVPEIVEAAIRNGIRIRSI--STERPS 292
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
11-234 |
6.00e-41 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 142.74 E-value: 6.00e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 11 FGAQKAVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVE-----HDSGEIRFAGEEIRSLPVLELRRRMGYAIQSIG 85
Cdd:PRK14247 13 FGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElypeaRVSGEVYLDGQDIFKMDVIELRRRVQMVFQIPN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 86 LFPHWSVAQNIATVPQLQKW--SRARIDDRIDELMALLGLESNLRERY---PHQLSGGQQQRVGVARALAADPQVLLMDE 160
Cdd:PRK14247 93 PIPNLSIFENVALGLKLNRLvkSKKELQERVRWALEKAQLWDEVKDRLdapAGKLSGGQQQRLCIARALAFQPEVLLADE 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446491464 161 PFGALDPVTRGALQQEMTRIHRLLgrTIVLVTHDIDEALRLAEHLVLMDHGEVVQQGNPLTMLTRPANDFVRQF 234
Cdd:PRK14247 173 PTANLDPENTAKIESLFLELKKDM--TIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTNPRHELTEKY 244
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-224 |
6.81e-41 |
|
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: 142.53 E-value: 6.81e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 1 MIEFSHVSKLFGAQKAVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRlvEH---DSGEIRFAGEEIRSLPVLELRRRM 77
Cdd:COG1119 3 LLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITG--DLpptYGNDVRLFGERRGGEDVWELRKRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 78 GY---AIQ-------------------SIGLFPHWSVAQniatvpqlqkwsrariDDRIDELMALLGLESnLRERYPHQL 135
Cdd:COG1119 81 GLvspALQlrfprdetvldvvlsgffdSIGLYREPTDEQ----------------RERARELLELLGLAH-LADRPFGTL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 136 SGGQQQRVGVARALAADPQVLLMDEPFGALDPVTRGALQQEMTRIHRLLGRTIVLVTHDIDEALRLAEHLVLMDHGEVVQ 215
Cdd:COG1119 144 SQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRVVA 223
|
....*....
gi 446491464 216 QGNPLTMLT 224
Cdd:COG1119 224 AGPKEEVLT 232
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-242 |
1.22e-40 |
|
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: 141.27 E-value: 1.22e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 1 MIEFSHVSKLFGAQKAVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEIRSLPVLELRRR-MGY 79
Cdd:COG0410 3 MLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIARLgIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 80 AIQSIGLFPHWSVAQNIATVPQLQKwSRARIDDRIDELMALLgleSNLRERYpHQ----LSGGQQQRVGVARALAADPQV 155
Cdd:COG0410 83 VPEGRRIFPSLTVEENLLLGAYARR-DRAEVRADLERVYELF---PRLKERR-RQragtLSGGEQQMLAIGRALMSRPKL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 156 LLMDEPFGALDPVtrgaLQQEMTR-IHRL--LGRTIVLVTHDIDEALRLAEHLVLMDHGEVVQQGNPLTMLTRPAndfVR 232
Cdd:COG0410 158 LLLDEPSLGLAPL----IVEEIFEiIRRLnrEGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLADPE---VR 230
|
250
....*....|
gi 446491464 233 QFFgrseLGV 242
Cdd:COG0410 231 EAY----LGV 236
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-227 |
2.83e-40 |
|
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: 147.61 E-value: 2.83e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 2 IEFSHVSklFG----AQKAVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEIRSLPVLELRRRM 77
Cdd:COG4987 334 LELEDVS--FRypgaGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRRI 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 78 GYAIQSIGLFpHWSVAQNI------ATVPQLqkWS---RARIDDRIDELMAllGLESNLRERyPHQLSGGQQQRVGVARA 148
Cdd:COG4987 412 AVVPQRPHLF-DTTLRENLrlarpdATDEEL--WAaleRVGLGDWLAALPD--GLDTWLGEG-GRRLSGGERRRLALARA 485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 149 LAADPQVLLMDEPFGALDPVTRGALqqeMTRIHRLL-GRTIVLVTHDIdEALRLAEHLVLMDHGEVVQQGNPLTMLTRPA 227
Cdd:COG4987 486 LLRDAPILLLDEPTEGLDAATEQAL---LADLLEALaGRTVLLITHRL-AGLERMDRILVLEDGRIVEQGTHEELLAQNG 561
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
2-219 |
3.10e-40 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 139.88 E-value: 3.10e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 2 IEFSHVSKLFGAQKAVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEIRSLPVLELRRR-MGYA 80
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARAgIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 81 IQSIGLFPHWSVAQNIATVPQLQKwsRARIDDRIDELMALLgleSNLRERYPH---QLSGGQQQRVGVARALAADPQVLL 157
Cdd:cd03224 81 PEGRRIFPELTVEENLLLGAYARR--RAKRKARLERVYELF---PRLKERRKQlagTLSGGEQQMLAIARALMSRPKLLL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446491464 158 MDEPFGALDPVTRGALQQEMTRIHRlLGRTIVLVTHDIDEALRLAEHLVLMDHGEVVQQGNP 219
Cdd:cd03224 156 LDEPSEGLAPKIVEEIFEAIRELRD-EGVTILLVEQNARFALEIADRAYVLERGRVVLEGTA 216
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
15-194 |
5.38e-39 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 139.87 E-value: 5.38e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 15 KAVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEIRSLP---VLELRRRMGYAIQ----SigLF 87
Cdd:COG4608 32 KAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSgreLRPLRRRMQMVFQdpyaS--LN 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 88 PHWSVAQNIATVPQLQK-WSRARIDDRIDELMALLGLESNLRERYPHQLSGGQQQRVGVARALAADPQVLLMDEPFGALD 166
Cdd:COG4608 110 PRMTVGDIIAEPLRIHGlASKAERRERVAELLELVGLRPEHADRYPHEFSGGQRQRIGIARALALNPKLIVCDEPVSALD 189
|
170 180 190
....*....|....*....|....*....|....*.
gi 446491464 167 pVTRGA--------LQQEmtrihrlLGRTIVLVTHD 194
Cdd:COG4608 190 -VSIQAqvlnlledLQDE-------LGLTYLFISHD 217
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
9-235 |
1.01e-38 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 137.02 E-value: 1.01e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 9 KLFGAQKAVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEIR-------SLPVLE------LRR 75
Cdd:PRK10619 13 KRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgQLKVADknqlrlLRT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 76 RMGYAIQSIGLFPHWSVAQNIATVP-QLQKWSRARIDDRIDELMALLGLESNLRERYPHQLSGGQQQRVGVARALAADPQ 154
Cdd:PRK10619 93 RLTMVFQHFNLWSHMTVLENVMEAPiQVLGLSKQEARERAVKYLAKVGIDERAQGKYPVHLSGGQQQRVSIARALAMEPE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 155 VLLMDEPFGALDPVTRGalqqEMTRIHRLL---GRTIVLVTHDIDEALRLAEHLVLMDHGEVVQQGNPLTMLTRPANDFV 231
Cdd:PRK10619 173 VLLFDEPTSALDPELVG----EVLRIMQQLaeeGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGNPQSPRL 248
|
....
gi 446491464 232 RQFF 235
Cdd:PRK10619 249 QQFL 252
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
2-217 |
5.31e-38 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 133.77 E-value: 5.31e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 2 IEFSHVSKLFGAQKAvnDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEIRSLPVLElrRRMGYAI 81
Cdd:cd03298 1 VRLDKIRFSYGEQPM--HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPAD--RPVSMLF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 82 QSIGLFPHWSVAQNI--ATVPQLQkwSRARIDDRIDELMALLGLeSNLRERYPHQLSGGQQQRVGVARALAADPQVLLMD 159
Cdd:cd03298 77 QENNLFAHLTVEQNVglGLSPGLK--LTAEDRQAIEVALARVGL-AGLEKRLPGELSGGERQRVALARVLVRDKPVLLLD 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446491464 160 EPFGALDPVTRGALQQEMTRIHRLLGRTIVLVTHDIDEALRLAEHLVLMDHGEVVQQG 217
Cdd:cd03298 154 EPFAALDPALRAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
1-207 |
1.33e-37 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 132.61 E-value: 1.33e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 1 MIEFSHVSKLFGAQKAVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHD---SGEIRFAGEEIRSLPVLelRRRM 77
Cdd:COG4136 1 MLSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRLTALPAE--QRRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 78 GYAIQSIGLFPHWSVAQNIA-TVPQlqKWSRARIDDRIDELMALLGLeSNLRERYPHQLSGGQQQRVGVARALAADPQVL 156
Cdd:COG4136 79 GILFQDDLLFPHLSVGENLAfALPP--TIGRAQRRARVEQALEEAGL-AGFADRDPATLSGGQRARVALLRALLAEPRAL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446491464 157 LMDEPFGALDPVTRGA-LQQEMTRIHRlLGRTIVLVTHDIDEALRLAEHLVL 207
Cdd:COG4136 156 LLDEPFSKLDAALRAQfREFVFEQIRQ-RGIPALLVTHDEEDAPAAGRVLDL 206
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
2-217 |
2.31e-37 |
|
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: 133.05 E-value: 2.31e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 2 IEFSHVSklFG-----AQKAVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEIRSLPVLELRRR 76
Cdd:cd03249 1 IEFKNVS--FRypsrpDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 77 MGYAIQSIGLFPHwSVAQNI------ATVPQLQKWSR-ARIDDRIDELMAllGLESNLRERYPhQLSGGQQQRVGVARAL 149
Cdd:cd03249 79 IGLVSQEPVLFDG-TIAENIrygkpdATDEEVEEAAKkANIHDFIMSLPD--GYDTLVGERGS-QLSGGQKQRIAIARAL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446491464 150 AADPQVLLMDEPFGALDPVTRGALQQEMTRIHRllGRTIVLVTHDIdEALRLAEHLVLMDHGEVVQQG 217
Cdd:cd03249 155 LRNPKILLLDEATSALDAESEKLVQEALDRAMK--GRTTIVIAHRL-STIRNADLIAVLQNGQVVEQG 219
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-226 |
2.65e-37 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 133.32 E-value: 2.65e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 1 MIEFSHVSKLFGAQKAVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEIRSLPVLELRRRMGYA 80
Cdd:COG4559 1 MLEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRRAVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 81 IQSIGL-FPhWSVAQNIA--TVPQLQkwSRARIDDRIDELMALLGLESnLRERYPHQLSGGQQQRVGVARALA------- 150
Cdd:COG4559 81 PQHSSLaFP-FTVEEVVAlgRAPHGS--SAAQDRQIVREALALVGLAH-LAGRSYQTLSGGEQQRVQLARVLAqlwepvd 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446491464 151 ADPQVLLMDEPFGALDPvtrgALQQEMTRIHRLL---GRTIVLVTHDIDEALRLAEHLVLMDHGEVVQQGNPLTMLTRP 226
Cdd:COG4559 157 GGPRWLFLDEPTSALDL----AHQHAVLRLARQLarrGGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPEEVLTDE 231
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1-217 |
4.37e-37 |
|
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: 131.72 E-value: 4.37e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 1 MIEFSHVSKLFGAQK----AVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEIRSLPvLELRRR 76
Cdd:cd03266 1 MITADALTKRFRDVKktvqAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEP-AEARRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 77 MGYAIQSIGLFPHWSVAQNIATVPQLQKWSRARIDDRIDELMALLGLESnLRERYPHQLSGGQQQRVGVARALAADPQVL 156
Cdd:cd03266 80 LGFVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEE-LLDRRVGGFSTGMRQKVAIARALVHDPPVL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446491464 157 LMDEPFGALDPVTRGALqQEMTRIHRLLGRTIVLVTHDIDEALRLAEHLVLMDHGEVVQQG 217
Cdd:cd03266 159 LLDEPTTGLDVMATRAL-REFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| heterocyst_DevA |
TIGR02982 |
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly ... |
2-214 |
9.48e-37 |
|
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: 130.91 E-value: 9.48e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 2 IEFSHVSKLFG---AQKAV-NDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEIRSLP---VLELR 74
Cdd:TIGR02982 2 ISIRNLNHYYGhgsLRKQVlFDINLEINPGEIVILTGPSGSGKTTLLTLIGGLRSVQEGSLKVLGQELHGASkkqLVQLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 75 RRMGYAIQSIGLFPHWSVAQNIATVPQLQ-KWSRARIDDRIDELMALLGLESNLrERYPHQLSGGQQQRVGVARALAADP 153
Cdd:TIGR02982 82 RRIGYIFQAHNLLGFLTARQNVQMALELQpNLSYQEARERARAMLEAVGLGDHL-NYYPHNLSGGQKQRVAIARALVHHP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446491464 154 QVLLMDEPFGALDPVTRGALQQEMTRIHRLLGRTIVLVTHDiDEALRLAEHLVLMDHGEVV 214
Cdd:TIGR02982 161 KLVLADEPTAALDSKSGRDVVELMQKLAKEQGCTILMVTHD-NRILDVADRILQMEDGKLL 220
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
10-234 |
2.29e-36 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 130.94 E-value: 2.29e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 10 LFGAQKAV-NDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVE-HDS-----GEIRFAGEEIRSLPVLELRRRMGYAIQ 82
Cdd:PRK14246 18 LYINDKAIlKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiYDSkikvdGKVLYFGKDIFQIDAIKLRKEVGMVFQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 83 SIGLFPHWSVAQNIATVPQLQKWSRAR-IDDRIDELMALLGLESNLRERY---PHQLSGGQQQRVGVARALAADPQVLLM 158
Cdd:PRK14246 98 QPNPFPHLSIYDNIAYPLKSHGIKEKReIKKIVEECLRKVGLWKEVYDRLnspASQLSGGQQQRLTIARALALKPKVLLM 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446491464 159 DEPFGALDPVTRGALQQEMTRIHRLLgrTIVLVTHDIDEALRLAEHLVLMDHGEVVQQGNPLTMLTRPANDFVRQF 234
Cdd:PRK14246 178 DEPTSMIDIVNSQAIEKLITELKNEI--AIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNELTEKY 251
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-234 |
2.44e-36 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 130.73 E-value: 2.44e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 2 IEFSHVSKLFGAQKAVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHD-----SGEIRFAGEEIRSLPV--LELR 74
Cdd:PRK14267 5 IETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNeearvEGEVRLFGRNIYSPDVdpIEVR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 75 RRMGYAIQSIGLFPHWSVAQNIATVPQLQKW--SRARIDDRIDELMALLGLESNLRER---YPHQLSGGQQQRVGVARAL 149
Cdd:PRK14267 85 REVGMVFQYPNPFPHLTIYDNVAIGVKLNGLvkSKKELDERVEWALKKAALWDEVKDRlndYPSNLSGGQRQRLVIARAL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 150 AADPQVLLMDEPFGALDPVTRGALQQEMTRIHRLLgrTIVLVTHDIDEALRLAEHLVLMDHGEVVQQGNPLTMLTRPAND 229
Cdd:PRK14267 165 AMKPKILLMDEPTANIDPVGTAKIEELLFELKKEY--TIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENPEHE 242
|
....*
gi 446491464 230 FVRQF 234
Cdd:PRK14267 243 LTEKY 247
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
15-233 |
2.82e-36 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 136.35 E-value: 2.82e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 15 KAVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHdSGEIRFAGEEIRSLP---VLELRRRMGYAIQ----SigLF 87
Cdd:COG4172 300 KAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIPS-EGEIRFDGQDLDGLSrraLRPLRRRMQVVFQdpfgS--LS 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 88 PHWSVAQNIA---TVPQLQkWSRARIDDRIDELMALLGLESNLRERYPHQLSGGQQQRVGVARALAADPQVLLMDEPFGA 164
Cdd:COG4172 377 PRMTVGQIIAeglRVHGPG-LSAAERRARVAEALEEVGLDPAARHRYPHEFSGGQRQRIAIARALILEPKLLVLDEPTSA 455
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446491464 165 LDpVTRGA--------LQQEmtriHRLlgrTIVLVTHDIDEALRLAEHLVLMDHGEVVQQGNPLTMLTRPANDFVRQ 233
Cdd:COG4172 456 LD-VSVQAqildllrdLQRE----HGL---AYLFISHDLAVVRALAHRVMVMKDGKVVEQGPTEQVFDAPQHPYTRA 524
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
2-219 |
2.86e-36 |
|
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: 130.04 E-value: 2.86e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 2 IEFSHVSKLFGAQK-AVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEIRSLPVLELRRRMGYA 80
Cdd:cd03254 3 IEFENVNFSYDEKKpVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMIGVV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 81 IQSIGLFPHwSVAQNI------ATVPQLQKWSR-ARIDDRIDELMAllGLESNLRERyPHQLSGGQQQRVGVARALAADP 153
Cdd:cd03254 83 LQDTFLFSG-TIMENIrlgrpnATDEEVIEAAKeAGAHDFIMKLPN--GYDTVLGEN-GGNLSQGERQLLAIARAMLRDP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446491464 154 QVLLMDEPFGALDPVTRGALQQEMTRIhrLLGRTIVLVTHDIDeALRLAEHLVLMDHGEVVQQGNP 219
Cdd:cd03254 159 KILILDEATSNIDTETEKLIQEALEKL--MKGRTSIIIAHRLS-TIKNADKILVLDDGKIIEEGTH 221
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
2-217 |
7.59e-36 |
|
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: 128.48 E-value: 7.59e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 2 IEFSHVSKLFGAQK--AVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEIRSLPVLELRRRMGY 79
Cdd:cd03245 3 IEFRNVSFSYPNQEipALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 80 AIQSIGLFpHWSVAQNIATvpqlqkwSRARIDDR----------IDELMALL--GLESNLRERyPHQLSGGQQQRVGVAR 147
Cdd:cd03245 83 VPQDVTLF-YGTLRDNITL-------GAPLADDErilraaelagVTDFVNKHpnGLDLQIGER-GRGLSGGQRQAVALAR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446491464 148 ALAADPQVLLMDEPFGALDpvtrgaLQQEMTRIHRL----LGRTIVLVTHDIdEALRLAEHLVLMDHGEVVQQG 217
Cdd:cd03245 154 ALLNDPPILLLDEPTSAMD------MNSEERLKERLrqllGDKTLIIITHRP-SLLDLVDRIIVMDSGRIVADG 220
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
34-218 |
1.17e-35 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 131.54 E-value: 1.17e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 34 GTSGSGKSTTLKMINRLVEHDSGEIRFAG------EEIRSLPVLelRRRMGYAIQSIGLFPHWSVAQNiatvpqLQKWSR 107
Cdd:PRK11144 31 GRSGAGKTSLINAISGLTRPQKGRIVLNGrvlfdaEKGICLPPE--KRRIGYVFQDARLFPHYKVRGN------LRYGMA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 108 ARIDDRIDELMALLGLESnLRERYPHQLSGGQQQRVGVARALAADPQVLLMDEPFGALD-PVTRgalqQEMTRIHRLLGR 186
Cdd:PRK11144 103 KSMVAQFDKIVALLGIEP-LLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDlPRKR----ELLPYLERLARE 177
|
170 180 190
....*....|....*....|....*....|....*
gi 446491464 187 T---IVLVTHDIDEALRLAEHLVLMDHGEVVQQGN 218
Cdd:PRK11144 178 InipILYVSHSLDEILRLADRVVVLEQGKVKAFGP 212
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-236 |
5.11e-35 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 127.20 E-value: 5.11e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 1 MIEFSHVSKLFGAQKAVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHD-----SGEIRFAGEEIRS--LPVLEL 73
Cdd:PRK14239 5 ILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLNpevtiTGSIVYNGHNIYSprTDTVDL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 74 RRRMGYAIQSIGLFPhWSVAQNIATVPQLQKW-SRARIDDRIDELMALLGLESNLRERYpHQ----LSGGQQQRVGVARA 148
Cdd:PRK14239 85 RKEIGMVFQQPNPFP-MSIYENVVYGLRLKGIkDKQVLDEAVEKSLKGASIWDEVKDRL-HDsalgLSGGQQQRVCIARV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 149 LAADPQVLLMDEPFGALDPVTRGALQQEMTRIHRllGRTIVLVTHDIDEALRLAEHLVLMDHGEVVQQGNPLTMLTRPAN 228
Cdd:PRK14239 163 LATSPKIILLDEPTSALDPISAGKIEETLLGLKD--DYTMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQMFMNPKH 240
|
250
....*....|..
gi 446491464 229 ----DFVRQFFG 236
Cdd:PRK14239 241 keteDYISGKFG 252
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-286 |
5.68e-35 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 132.06 E-value: 5.68e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 1 MIEFSHVSKLFGAQKAVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEIRSLPVLElRRRMGYA 80
Cdd:COG1129 4 LLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRD-AQAAGIA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 81 I--QSIGLFPHWSVAQNIATVPQLQKW---SRARIDDRIDELMALLGLESNLRERYpHQLSGGQQQRVGVARALAADPQV 155
Cdd:COG1129 83 IihQELNLVPNLSVAENIFLGREPRRGgliDWRAMRRRARELLARLGLDIDPDTPV-GDLSVAQQQLVEIARALSRDARV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 156 LLMDEPFGALDPVTRGALqqeMTRIHRL--LGRTIVLVTHDIDEALRLAEHL-VLMDhGEVVqqgnpltmLTRPANDFVR 232
Cdd:COG1129 162 LILDEPTASLTEREVERL---FRIIRRLkaQGVAIIYISHRLDEVFEIADRVtVLRD-GRLV--------GTGPVAELTE 229
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 446491464 233 QffgrsELgVRLLSLRSVADYVRREERAEGEAL--AEEMTLRDAL---SLFVARGcEVL 286
Cdd:COG1129 230 D-----EL-VRLMVGRELEDLFPKRAAAPGEVVleVEGLSVGGVVrdvSFSVRAG-EIL 281
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1-224 |
6.91e-35 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 127.05 E-value: 6.91e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 1 MIEFSHVSKLFGAQKAVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEIRSLPVLELRRRMGYA 80
Cdd:PRK11231 2 TLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 81 IQsIGLFPHW-SVAQNIA--TVPQLQKWSRARIDDR--IDELMALLGLESnLRERYPHQLSGGQQQRVGVARALAADPQV 155
Cdd:PRK11231 82 PQ-HHLTPEGiTVRELVAygRSPWLSLWGRLSAEDNarVNQAMEQTRINH-LADRRLTDLSGGQRQRAFLAMVLAQDTPV 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446491464 156 LLMDEPFGALDpVTRgalQQEMTRIHRLL---GRTIVLVTHDIDEALRLAEHLVLMDHGEVVQQGNPLTMLT 224
Cdd:PRK11231 160 VLLDEPTTYLD-INH---QVELMRLMRELntqGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVMT 227
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
2-217 |
7.52e-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: 133.45 E-value: 7.52e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 2 IEFSHVS-KLFGAQ-KAVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEIRSLPVLELRRRMGY 79
Cdd:TIGR03375 464 IEFRNVSfAYPGQEtPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQIDPADLRRNIGY 543
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 80 AIQSIGLFpHWSVAQNIATvpqlqkwSRARIDDR----------IDELMALL--GLESNLRERyPHQLSGGQQQRVGVAR 147
Cdd:TIGR03375 544 VPQDPRLF-YGTLRDNIAL-------GAPYADDEeilraaelagVTEFVRRHpdGLDMQIGER-GRSLSGGQRQAVALAR 614
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446491464 148 ALAADPQVLLMDEPFGALDpvtrgaLQQEMTRIHRL----LGRTIVLVTHDIdEALRLAEHLVLMDHGEVVQQG 217
Cdd:TIGR03375 615 ALLRDPPILLLDEPTSAMD------NRSEERFKDRLkrwlAGKTLVLVTHRT-SLLDLVDRIIVMDNGRIVADG 681
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
2-219 |
9.67e-35 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 127.17 E-value: 9.67e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 2 IEFSHVSKLFGA-----QKAVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEIRSLP----VLE 72
Cdd:PRK13649 3 INLQNVSYTYQAgtpfeGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSknkdIKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 73 LRRRMGYAIQsiglFPHW-----SVAQNIATVPQLQKWSRARIDDRIDELMALLGLESNLRERYPHQLSGGQQQRVGVAR 147
Cdd:PRK13649 83 IRKKVGLVFQ----FPESqlfeeTVLKDVAFGPQNFGVSQEEAEALAREKLALVGISESLFEKNPFELSGGQMRRVAIAG 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446491464 148 ALAADPQVLLMDEPFGALDPVTRGALQQEMTRIHRlLGRTIVLVTHDIDEALRLAEHLVLMDHGEVVQQGNP 219
Cdd:PRK13649 159 ILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQ-SGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKP 229
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
2-214 |
1.35e-34 |
|
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: 123.31 E-value: 1.35e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 2 IEFSHVSKLFGAQKAVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEIRSLPVLElRRRMGyai 81
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRD-ARRAG--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 82 qsiglfphwsvaqnIATVpqlqkwsrariddridelmallglesnlrerypHQLSGGQQQRVGVARALAADPQVLLMDEP 161
Cdd:cd03216 77 --------------IAMV---------------------------------YQLSVGERQMVEIARALARNARLLILDEP 109
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446491464 162 FGALDPVTRGALqqeMTRIHRL--LGRTIVLVTHDIDEALRLAEHLVLMDHGEVV 214
Cdd:cd03216 110 TAALTPAEVERL---FKVIRRLraQGVAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
15-227 |
1.62e-34 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 126.39 E-value: 1.62e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 15 KAVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEIRSLPVLELRRRMGYAIQSIG--LFPHwSV 92
Cdd:PRK13647 19 KALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGLVFQDPDdqVFSS-TV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 93 AQNIATVPQLQKWSRARIDDRIDELMALLGLEsNLRERYPHQLSGGQQQRVGVARALAADPQVLLMDEPFGALDPVTRGA 172
Cdd:PRK13647 98 WDDVAFGPVNMGLDKDEVERRVEEALKAVRMW-DFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQET 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446491464 173 LQQEMTRIHRlLGRTIVLVTHDIDEALRLAEHLVLMDHGEVVQQGNPlTMLTRPA 227
Cdd:PRK13647 177 LMEILDRLHN-QGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDK-SLLTDED 229
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-219 |
1.69e-34 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 127.23 E-value: 1.69e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 2 IEFSHVSKLFGAQKAVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEIRSlPVLELRRRMGYAI 81
Cdd:PRK13537 8 IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPS-RARHARQRVGVVP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 82 QSIGLFPHWSVAQNIATVPQLQKWSRARIDDRIDELMALLGLESNLRERYpHQLSGGQQQRVGVARALAADPQVLLMDEP 161
Cdd:PRK13537 87 QFDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKV-GELSGGMKRRLTLARALVNDPDVLVLDEP 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 162 FGALDPVTRGALQQemtRIHRLL--GRTIVLVTHDIDEALRLAEHLVLMDHGEVVQQGNP 219
Cdd:PRK13537 166 TTGLDPQARHLMWE---RLRSLLarGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAP 222
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
2-217 |
1.77e-34 |
|
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: 124.64 E-value: 1.77e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 2 IEFSHVSKLFGAQKAVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEIRSLPvlELRRRMGYAI 81
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNI--EALRRIGALI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 82 QSIGLFPHWSVAQNI---ATVPQLQKwsraridDRIDELMALLGLeSNLRERYPHQLSGGQQQRVGVARALAADPQVLLM 158
Cdd:cd03268 79 EAPGFYPNLTARENLrllARLLGIRK-------KRIDEVLDVVGL-KDSAKKKVKGFSLGMKQRLGIALALLGNPDLLIL 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 159 DEPFGALDPVtrGALQ-QEMTRIHRLLGRTIVLVTHDIDEALRLAEHLVLMDHGEVVQQG 217
Cdd:cd03268 151 DEPTNGLDPD--GIKElRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
15-224 |
2.24e-34 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 126.66 E-value: 2.24e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 15 KAVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEI-----RSLPVLELRRRMGYAIQsiglFPH 89
Cdd:PRK13645 25 KALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIpanlkKIKEVKRLRKEIGLVFQ----FPE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 90 W-----SVAQNIATVPQLQKWSRARIDDRIDELMALLGLESNLRERYPHQLSGGQQQRVGVARALAADPQVLLMDEPFGA 164
Cdd:PRK13645 101 YqlfqeTIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLPEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGG 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 165 LDPVTRGALQQEMTRIHRLLGRTIVLVTHDIDEALRLAEHLVLMDHGEVVQQGNPLTMLT 224
Cdd:PRK13645 181 LDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFS 240
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
12-226 |
3.77e-34 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 125.69 E-value: 3.77e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 12 GAQKAVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEIRSLPVLELRRRMGYAIQSIG--LFPH 89
Cdd:PRK13652 15 GSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLVFQNPDdqIFSP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 90 wSVAQNIATVPQLQKWSRARIDDRIDELMALLGLEsNLRERYPHQLSGGQQQRVGVARALAADPQVLLMDEPFGALDPVT 169
Cdd:PRK13652 95 -TVEQDIAFGPINLGLDEETVAHRVSSALHMLGLE-ELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQG 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446491464 170 RGALQQEMTRIHRLLGRTIVLVTHDIDEALRLAEHLVLMDHGEVVQQGNPLTMLTRP 226
Cdd:PRK13652 173 VKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1-224 |
5.39e-34 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 124.50 E-value: 5.39e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 1 MIEFSHVSKLFGAQKAVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEIRSLPVLELRRRMGYA 80
Cdd:PRK13548 2 MLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 81 IQSIGL-FPhWSVAQNIA--TVPqlqkWSRARIDDR--IDELMALLGLeSNLRERYPHQLSGGQQQRVGVARALA----- 150
Cdd:PRK13548 82 PQHSSLsFP-FTVEEVVAmgRAP----HGLSRAEDDalVAAALAQVDL-AHLAGRDYPQLSGGEQQRVQLARVLAqlwep 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446491464 151 -ADPQVLLMDEPFGALDPvtrgALQQEMTRIHRLL----GRTIVLVTHDIDEALRLAEHLVLMDHGEVVQQGNPLTMLT 224
Cdd:PRK13548 156 dGPPRWLLLDEPTSALDL----AHQHHVLRLARQLaherGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAEVLT 230
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
2-219 |
8.20e-34 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 124.89 E-value: 8.20e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 2 IEFSHVSKLFgaQK-------AVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEIRSLP----V 70
Cdd:PRK13646 3 IRFDNVSYTY--QKgtpyehqAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTkdkyI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 71 LELRRRMGYAIQsiglFPHW-----SVAQNIATVPQLQKWSRARIDDRIDELMALLGLESNLRERYPHQLSGGQQQRVGV 145
Cdd:PRK13646 81 RPVRKRIGMVFQ----FPESqlfedTVEREIIFGPKNFKMNLDEVKNYAHRLLMDLGFSRDVMSQSPFQMSGGQMRKIAI 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446491464 146 ARALAADPQVLLMDEPFGALDPVTRgalQQEMTRIHRLL---GRTIVLVTHDIDEALRLAEHLVLMDHGEVVQQGNP 219
Cdd:PRK13646 157 VSILAMNPDIIVLDEPTAGLDPQSK---RQVMRLLKSLQtdeNKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSP 230
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
1-219 |
9.48e-34 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 124.85 E-value: 9.48e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 1 MIEFSHVSKLFG-----AQKAVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEIRSLP----VL 71
Cdd:PRK13643 1 MIKFEKVNYTYQpnspfASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSkqkeIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 72 ELRRRMGYAIQsiglFPHW-----SVAQNIATVPQLQKWSRARIDDRIDELMALLGLESNLRERYPHQLSGGQQQRVGVA 146
Cdd:PRK13643 81 PVRKKVGVVFQ----FPESqlfeeTVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLADEFWEKSPFELSGGQMRRVAIA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446491464 147 RALAADPQVLLMDEPFGALDPVTRGALQQEMTRIHRlLGRTIVLVTHDIDEALRLAEHLVLMDHGEVVQQGNP 219
Cdd:PRK13643 157 GILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQ-SGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTP 228
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
13-219 |
1.29e-33 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 124.36 E-value: 1.29e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 13 AQKAVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEIRSLPVLELRRRMGYAIQSI-GLFPHWS 91
Cdd:PRK13635 19 ATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVGMVFQNPdNQFVGAT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 92 VAQNIATVPQLQKWSRARIDDRIDELMALLGLESNLrERYPHQLSGGQQQRVGVARALAADPQVLLMDEPFGALDPVTRg 171
Cdd:PRK13635 99 VQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFL-NREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGR- 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446491464 172 alQQEMTRIHRL---LGRTIVLVTHDIDEALRlAEHLVLMDHGEVVQQGNP 219
Cdd:PRK13635 177 --REVLETVRQLkeqKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTP 224
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
2-225 |
1.99e-33 |
|
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: 122.72 E-value: 1.99e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 2 IEFSHVSklFG---AQKAVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEIRSLPVLELRRRMG 78
Cdd:cd03253 1 IEFENVT--FAydpGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 79 YAIQSIGLFpHWSVAQNI------ATVPQLQKWSR-ARIDDRIDELMAllGLESNLRERyPHQLSGGQQQRVGVARALAA 151
Cdd:cd03253 79 VVPQDTVLF-NDTIGYNIrygrpdATDEEVIEAAKaAQIHDKIMRFPD--GYDTIVGER-GLKLSGGEKQRVAIARAILK 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446491464 152 DPQVLLMDEPFGALDPVTRGALQQEMTRIHRllGRTIVLVTHdidealRL-----AEHLVLMDHGEVVQQGNPLTMLTR 225
Cdd:cd03253 155 NPPILLLDEATSALDTHTEREIQAALRDVSK--GRTTIVIAH------RLstivnADKIIVLKDGRIVERGTHEELLAK 225
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
3-217 |
2.37e-33 |
|
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: 122.25 E-value: 2.37e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 3 EFSHVSKLFGAQKAVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEIRSLPVLELRRR-MGYAI 81
Cdd:TIGR03410 2 EVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERARAgIAYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 82 QSIGLFPHWSVAQNIATVPQLQKWSRARIDDRIDELMALLgleSNLRERYPHQLSGGQQQRVGVARALAADPQVLLMDEP 161
Cdd:TIGR03410 82 QGREIFPRLTVEENLLTGLAALPRRSRKIPDEIYELFPVL---KEMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDEP 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446491464 162 FGALDPVTRGALQQEMTRIHRLLGRTIVLVTHDIDEALRLAEHLVLMDHGEVVQQG 217
Cdd:TIGR03410 159 TEGIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRVVASG 214
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
12-233 |
2.56e-33 |
|
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: 127.88 E-value: 2.56e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 12 GAQKAVNDLNLNFQEGSFSVLIGTSGSGKSTT----LKMINRLVEHDSGEIRFAGEEIRSLPVLELRR----RMGYAIQ- 82
Cdd:COG4172 21 GTVEAVKGVSFDIAAGETLALVGESGSGKSVTalsiLRLLPDPAAHPSGSILFDGQDLLGLSERELRRirgnRIAMIFQe 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 83 -SIGLFPHWSVAQNIATVPQL-QKWSRARIDDRIDELMALLGL---ESNLReRYPHQLSGGQQQRVGVARALAADPQVLL 157
Cdd:COG4172 101 pMTSLNPLHTIGKQIAEVLRLhRGLSGAAARARALELLERVGIpdpERRLD-AYPHQLSGGQRQRVMIAMALANEPDLLI 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 158 MDEPFGALDpVTRGA--------LQQEMtrihrllGRTIVLVTHDIDEALRLAEHLVLMDHGEVVQQGNPLTMLTRPAND 229
Cdd:COG4172 180 ADEPTTALD-VTVQAqildllkdLQREL-------GMALLLITHDLGVVRRFADRVAVMRQGEIVEQGPTAELFAAPQHP 251
|
....
gi 446491464 230 FVRQ 233
Cdd:COG4172 252 YTRK 255
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
2-218 |
3.49e-33 |
|
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: 121.95 E-value: 3.49e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 2 IEFSHVSklFGAQK----AVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEIRSLPVLELRRRM 77
Cdd:cd03251 1 VEFKNVT--FRYPGdgppVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 78 GYAIQSIGLFpHWSVAQNI------ATVPQLQKWSR-ARIDDRIDELMalLGLESNLRERyPHQLSGGQQQRVGVARALA 150
Cdd:cd03251 79 GLVSQDVFLF-NDTVAENIaygrpgATREEVEEAARaANAHEFIMELP--EGYDTVIGER-GVKLSGGQRQRIAIARALL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446491464 151 ADPQVLLMDEPFGALDPVTRGALQQEMTRIHRllGRTIVLVTHDIdEALRLAEHLVLMDHGEVVQQGN 218
Cdd:cd03251 155 KDPPILILDEATSALDTESERLVQAALERLMK--NRTTFVIAHRL-STIENADRIVVLEDGKIVERGT 219
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
2-208 |
4.43e-33 |
|
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: 127.40 E-value: 4.43e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 2 IEFSHVSKLF-GAQKAVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEIRSLPVLELRRRMGYA 80
Cdd:TIGR02857 322 LEFSGVSVAYpGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWV 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 81 IQSIGLFPHwSVAQNI------ATVPQLQkwsRARIDDRIDELMALL--GLESNLRERyPHQLSGGQQQRVGVARALAAD 152
Cdd:TIGR02857 402 PQHPFLFAG-TIAENIrlarpdASDAEIR---EALERAGLDEFVAALpqGLDTPIGEG-GAGLSGGQAQRLALARAFLRD 476
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446491464 153 PQVLLMDEPFGALDPVTrgalQQEMTRIHRLL--GRTIVLVTHDiDEALRLAEHLVLM 208
Cdd:TIGR02857 477 APLLLLDEPTAHLDAET----EAEVLEALRALaqGRTVLLVTHR-LALAALADRIVVL 529
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1-234 |
4.99e-33 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 122.57 E-value: 4.99e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 1 MIEFSHVSKLFGAQKAVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEIRSLP---VLELRRRM 77
Cdd:PRK11831 7 LVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSrsrLYTVRKRM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 78 GYAIQSIGLFPHWSVAQNIAtvpqlqkW---SRARIDDRIDELMALLGLES-NLR---ERYPHQLSGGQQQRVGVARALA 150
Cdd:PRK11831 87 SMLFQSGALFTDMNVFDNVA-------YplrEHTQLPAPLLHSTVMMKLEAvGLRgaaKLMPSELSGGMARRAALARAIA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 151 ADPQVLLMDEPFGALDPVTRGALQQEMTRIHRLLGRTIVLVTHDIDEALRLAEHLVLMDHGEVVQQGNPLTMLTRPaNDF 230
Cdd:PRK11831 160 LEPDLIMFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQANP-DPR 238
|
....
gi 446491464 231 VRQF 234
Cdd:PRK11831 239 VRQF 242
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
2-219 |
2.48e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 121.09 E-value: 2.48e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 2 IEFSHVSKLFGA-----QKAVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEIR----SLPVLE 72
Cdd:PRK13641 3 IKFENVDYIYSPgtpmeKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpetgNKNLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 73 LRRRMGYAIQ--SIGLFPHwSVAQNIATVPQLQKWSRARIDDRIDELMALLGLESNLRERYPHQLSGGQQQRVGVARALA 150
Cdd:PRK13641 83 LRKKVSLVFQfpEAQLFEN-TVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLSEDLISKSPFELSGGQMRRVAIAGVMA 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446491464 151 ADPQVLLMDEPFGALDPVTRgalqQEMTRI---HRLLGRTIVLVTHDIDEALRLAEHLVLMDHGEVVQQGNP 219
Cdd:PRK13641 162 YEPEILCLDEPAAGLDPEGR----KEMMQLfkdYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASP 229
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-215 |
2.83e-32 |
|
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: 119.46 E-value: 2.83e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 1 MIEFSHVSK-LFGAQKAVN---DLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEIRSL---PVLEL 73
Cdd:COG4181 8 IIELRGLTKtVGTGAGELTilkGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALdedARARL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 74 RRR-MGYAIQSIGLFPHWSVAQNIATVPQLQKWSRARidDRIDELMALLGLESNLRErYPHQLSGGQQQRVGVARALAAD 152
Cdd:COG4181 88 RARhVGFVFQSFQLLPTLTALENVMLPLELAGRRDAR--ARARALLERVGLGHRLDH-YPAQLSGGEQQRVALARAFATE 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446491464 153 PQVLLMDEPFGALDPVTRGALQQEMTRIHRLLGRTIVLVTHDIDEALRlAEHLVLMDHGEVVQ 215
Cdd:COG4181 165 PAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAAR-CDRVLRLRAGRLVE 226
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
21-224 |
3.30e-32 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 119.30 E-value: 3.30e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 21 NLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEIRSLPvlELRRRMGYAIQSIGLFPHWSVAQNIA--T 98
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTP--PSRRPVSMLFQENNLFSHLTVAQNIGlgL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 99 VPQL-----QKWSRARIDDRIdelmallGLEsNLRERYPHQLSGGQQQRVGVARALAADPQVLLMDEPFGALDPvtrgAL 173
Cdd:PRK10771 97 NPGLklnaaQREKLHAIARQM-------GIE-DLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDP----AL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446491464 174 QQEM----TRIHRLLGRTIVLVTHDIDEALRLAEHLVLMDHGEVVQQGNPLTMLT 224
Cdd:PRK10771 165 RQEMltlvSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELLS 219
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
2-225 |
4.57e-32 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 119.13 E-value: 4.57e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 2 IEFSHVSKLFGAQKAV--NDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEIRSLPVLELRRRMGY 79
Cdd:cd03252 1 ITFEHVRFRYKPDGPVilDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 80 AIQSIGLFPHwSVAQNIATVPQLQKWSR----ARIDDRIDELMAL-LGLESNLRERyPHQLSGGQQQRVGVARALAADPQ 154
Cdd:cd03252 81 VLQENVLFNR-SIRDNIALADPGMSMERvieaAKLAGAHDFISELpEGYDTIVGEQ-GAGLSGGQRQRIAIARALIHNPR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446491464 155 VLLMDEPFGALDPVTRGALQQEMTRIhrLLGRTIVLVTHDIdEALRLAEHLVLMDHGEVVQQGNPLTMLTR 225
Cdd:cd03252 159 ILIFDEATSALDYESEHAIMRNMHDI--CAGRTVIIIAHRL-STVKNADRIIVMEKGRIVEQGSHDELLAE 226
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
6-235 |
6.18e-32 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 118.84 E-value: 6.18e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 6 HVSKLFGAQKAVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEIRSLPVLELRRR-MGYAIQSI 84
Cdd:PRK10895 8 NLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRgIGYLPQEA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 85 GLFPHWSVAQNIATVPQLQK-WSRARIDDRIDELMALLGLeSNLRERYPHQLSGGQQQRVGVARALAADPQVLLMDEPFG 163
Cdd:PRK10895 88 SIFRRLSVYDNLMAVLQIRDdLSAEQREDRANELMEEFHI-EHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFA 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446491464 164 ALDPVTRGALQQEMTRIhRLLGRTIVLVTHDIDEALRLAEHLVLMDHGEVVQQGNPLTMLtrpANDFVRQFF 235
Cdd:PRK10895 167 GVDPISVIDIKRIIEHL-RDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEIL---QDEHVKRVY 234
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
2-217 |
6.72e-32 |
|
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: 118.27 E-value: 6.72e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 2 IEFSHVSKLFGAQKAVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEI--RSLpvlelrRRMGY 79
Cdd:TIGR03740 1 LETKNLSKRFGKQTAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGHPWtrKDL------HKIGS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 80 AIQSIGLFPHWSVAQNIATVPQLQKWSrariDDRIDELMALLGLEsNLRERYPHQLSGGQQQRVGVARALAADPQVLLMD 159
Cdd:TIGR03740 75 LIESPPLYENLTARENLKVHTTLLGLP----DSRIDEVLNIVDLT-NTGKKKAKQFSLGMKQRLGIAIALLNHPKLLILD 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446491464 160 EPFGALDPVTrgalQQEMTRIHRLL---GRTIVLVTHDIDEALRLAEHLVLMDHGEVVQQG 217
Cdd:TIGR03740 150 EPTNGLDPIG----IQELRELIRSFpeqGITVILSSHILSEVQQLADHIGIISEGVLGYQG 206
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
7-213 |
1.02e-31 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 118.63 E-value: 1.02e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 7 VSKLFGAQKAVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRfAGeeirSLPVLELRRRMGYAIQSIGL 86
Cdd:PRK11247 18 VSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELL-AG----TAPLAEAREDTRLMFQDARL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 87 FPHWSVAQNIATvpQLQ-KWSraridDRIDELMALLGLESNLRErYPHQLSGGQQQRVGVARALAADPQVLLMDEPFGAL 165
Cdd:PRK11247 93 LPWKKVIDNVGL--GLKgQWR-----DAALQALAAVGLADRANE-WPAALSGGQKQRVALARALIHRPGLLLLDEPLGAL 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446491464 166 DPVTRGALQQEMTRIHRLLGRTIVLVTHDIDEALRLAEHLVLMDHGEV 213
Cdd:PRK11247 165 DALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
16-223 |
1.10e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 119.18 E-value: 1.10e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 16 AVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEI--RSLPVLELRRRMGYAIQSIG--LFPHwS 91
Cdd:PRK13636 21 ALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIdySRKGLMKLRESVGMVFQDPDnqLFSA-S 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 92 VAQNIATVPQLQKWSRARIDDRIDELMALLGLEsNLRERYPHQLSGGQQQRVGVARALAADPQVLLMDEPFGALDPVTRG 171
Cdd:PRK13636 100 VYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIE-HLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVS 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446491464 172 ALQQEMTRIHRLLGRTIVLVTHDIDEALRLAEHLVLMDHGEVVQQGNPLTML 223
Cdd:PRK13636 179 EIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVF 230
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
15-198 |
1.29e-31 |
|
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: 116.37 E-value: 1.29e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 15 KAVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEI----RSLpvLELRRRMGYAIQSIG--LFP 88
Cdd:TIGR01166 6 EVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPLdysrKGL--LERRQRVGLVFQDPDdqLFA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 89 HwSVAQNIATVPQLQKWSRARIDDRIDELMALLGLeSNLRERYPHQLSGGQQQRVGVARALAADPQVLLMDEPFGALDPv 168
Cdd:TIGR01166 84 A-DVDQDVAFGPLNLGLSEAEVERRVREALTAVGA-SGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAGLDP- 160
|
170 180 190
....*....|....*....|....*....|..
gi 446491464 169 tRGAlQQEMTRIHRLL--GRTIVLVTHDIDEA 198
Cdd:TIGR01166 161 -AGR-EQMLAILRRLRaeGMTVVISTHDVDLA 190
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
16-219 |
7.53e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 117.11 E-value: 7.53e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 16 AVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEIRSLP-VLELRRRMGYAIQ--------SIgl 86
Cdd:PRK13633 25 ALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEEnLWDIRNKAGMVFQnpdnqivaTI-- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 87 fphwsVAQNIATVPQLQKWSRARIDDRIDELMALLGLeSNLRERYPHQLSGGQQQRVGVARALAADPQVLLMDEPFGALD 166
Cdd:PRK13633 103 -----VEEDVAFGPENLGIPPEEIRERVDESLKKVGM-YEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLD 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446491464 167 PVTRGALQQEMTRIHRLLGRTIVLVTHDIDEALRlAEHLVLMDHGEVVQQGNP 219
Cdd:PRK13633 177 PSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTP 228
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
11-208 |
9.32e-31 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 114.25 E-value: 9.32e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 11 FGAQKAVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAG-----------EEIRSLPvLELRRRMgy 79
Cdd:NF040873 2 YGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGgarvayvpqrsEVPDSLP-LTVRDLV-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 80 aiqSIGLFPHwsvaqniatvpqLQKWSRARIDDR--IDELMALLGLEsNLRERYPHQLSGGQQQRVGVARALAADPQVLL 157
Cdd:NF040873 79 ---AMGRWAR------------RGLWRRLTRDDRaaVDDALERVGLA-DLAGRQLGELSGGQRQRALLAQGLAQEADLLL 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446491464 158 MDEPFGALDPVTRGALQQEMTRIHRlLGRTIVLVTHDIDEAlRLAEHLVLM 208
Cdd:NF040873 143 LDEPTTGLDAESRERIIALLAEEHA-RGATVVVVTHDLELV-RRADPCVLL 191
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
4-233 |
1.17e-30 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 116.09 E-value: 1.17e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 4 FSHVSKLFGAQK--AVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEI-------RSLPVlelr 74
Cdd:COG4167 14 FKYRTGLFRRQQfeAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLeygdykyRCKHI---- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 75 rRMGYAIQSIGLFPHWSVAQnIATVPqLQ---KWSRARIDDRIDELMALLGLESNLRERYPHQLSGGQQQRVGVARALAA 151
Cdd:COG4167 90 -RMIFQDPNTSLNPRLNIGQ-ILEEP-LRlntDLTAEEREERIFATLRLVGLLPEHANFYPHMLSSGQKQRVALARALIL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 152 DPQVLLMDEPFGALDPVTRGALQQEMTRIHRLLGRTIVLVTHDIDEALRLAEHLVLMDHGEVVQQGNPLTMLTRPANDFV 231
Cdd:COG4167 167 QPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKHISDKVLVMHQGEVVEYGKTAEVFANPQHEVT 246
|
..
gi 446491464 232 RQ 233
Cdd:COG4167 247 KR 248
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
2-223 |
2.12e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 116.34 E-value: 2.12e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 2 IEFSHVSKLFGAQ-----KAVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRF---------AGEEIRS 67
Cdd:PRK13651 3 IKVKNIVKIFNKKlptelKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWifkdeknkkKTKEKEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 68 LP---------------VLELRRRMGYAIQ--SIGLFPHwSVAQNIATVPQLQKWSRARIDDRIDELMALLGLESNLRER 130
Cdd:PRK13651 83 VLeklviqktrfkkikkIKEIRRRVGVVFQfaEYQLFEQ-TIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLDESYLQR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 131 YPHQLSGGQQQRVGVARALAADPQVLLMDEPFGALDPVtrGAlqQEMTRIHRLL---GRTIVLVTHDIDEALRLAEHLVL 207
Cdd:PRK13651 162 SPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQ--GV--KEILEIFDNLnkqGKTIILVTHDLDNVLEWTKRTIF 237
|
250
....*....|....*.
gi 446491464 208 MDHGEVVQQGNPLTML 223
Cdd:PRK13651 238 FKDGKIIKDGDTYDIL 253
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
17-247 |
2.29e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 115.60 E-value: 2.29e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 17 VNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEIRSLPVLELRRRMGYAIQSI-GLFPHWSVAQN 95
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIGMVFQNPdNQFVGATVEDD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 96 IATVPQLQKWSRARIDDRIDELMALLGLeSNLRERYPHQLSGGQQQRVGVARALAADPQVLLMDEPFGALDPVTRGALQQ 175
Cdd:PRK13650 103 VAFGLENKGIPHEEMKERVNEALELVGM-QDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELIK 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446491464 176 EMTRIHRLLGRTIVLVTHDIDEaLRLAEHLVLMDHGEVVQQGNPltmltrpandfvRQFFGRSElgvRLLSL 247
Cdd:PRK13650 182 TIKGIRDDYQMTVISITHDLDE-VALSDRVLVMKNGQVESTSTP------------RELFSRGN---DLLQL 237
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
21-217 |
3.30e-30 |
|
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: 113.42 E-value: 3.30e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 21 NLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEIRSLPvlELRRRMGYAIQSIGLFPHWSVAQNIA--T 98
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLA--PYQRPVSMLFQENNLFAHLTVRQNIGlgL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 99 VPQLQKwsRARIDDRIDELMALLGLeSNLRERYPHQLSGGQQQRVGVARALAADPQVLLMDEPFGALDPvtrgALQQEMT 178
Cdd:TIGR01277 96 HPGLKL--NAEQQEKVVDAAQQVGI-ADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDP----LLREEML 168
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 446491464 179 RIHRLLG----RTIVLVTHDIDEALRLAEHLVLMDHGEVVQQG 217
Cdd:TIGR01277 169 ALVKQLCserqRTLLMVTHHLSDARAIASQIAVVSQGKIKVVS 211
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-211 |
5.18e-30 |
|
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: 113.30 E-value: 5.18e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 1 MIEFSHVSKLF------GAQ-KAVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRF--AGEEI---RSL 68
Cdd:COG4778 4 LLEVENLSKTFtlhlqgGKRlPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrhDGGWVdlaQAS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 69 P--VLELRRR-MGYAIQSIGLFPHWSvAQNIATVPQLQK-WSRARIDDRIDELMALLGLESNLRERYPHQLSGGQQQRVG 144
Cdd:COG4778 84 PreILALRRRtIGYVSQFLRVIPRVS-ALDVVAEPLLERgVDREEARARARELLARLNLPERLWDLPPATFSGGEQQRVN 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446491464 145 VARALAADPQVLLMDEPFGALDPVTRGALQQemtRIHRLL--GRTIVLVTHDIDEALRLAEHLVLMDHG 211
Cdd:COG4778 163 IARGFIADPPLLLLDEPTASLDAANRAVVVE---LIEEAKarGTAIIGIFHDEEVREAVADRVVDVTPF 228
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-234 |
5.23e-30 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 114.36 E-value: 5.23e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 2 IEFSHVSKLFGAQKAVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDS-----GEIRFAGEEI--RSLPVLELR 74
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNIyeRRVNLNRLR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 75 RRMGYAIQSIGLFPhWSVAQNIATVPQLQKW-SRARIDDRIDELMALLGLESNLRERYPH---QLSGGQQQRVGVARALA 150
Cdd:PRK14258 88 RQVSMVHPKPNLFP-MSVYDNVAYGVKIVGWrPKLEIDDIVESALKDADLWDEIKHKIHKsalDLSGGQQQRLCIARALA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 151 ADPQVLLMDEPFGALDPVTRGALQqemTRIHRLLGR---TIVLVTHDIDEALRLAEHLVLMDH-----GEVVQQGNPLTM 222
Cdd:PRK14258 167 VKPKVLLMDEPCFGLDPIASMKVE---SLIQSLRLRselTMVIVSHNLHQVSRLSDFTAFFKGnenriGQLVEFGLTKKI 243
|
250
....*....|..
gi 446491464 223 LTRPANDFVRQF 234
Cdd:PRK14258 244 FNSPHDSRTREY 255
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-286 |
5.77e-30 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 118.21 E-value: 5.77e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 1 MIEFSHVSKLFGAQKAVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEE--IRSlPVLELRRRMG 78
Cdd:COG3845 5 ALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPvrIRS-PRDAIALGIG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 79 YAIQSIGLFPHWSVAQNIA---TVPQLQKWSRARIDDRIDELMALLGLESNLrERYPHQLSGGQQQRVGVARALAADPQV 155
Cdd:COG3845 84 MVHQHFMLVPNLTVAENIVlglEPTKGGRLDRKAARARIRELSERYGLDVDP-DAKVEDLSVGEQQRVEILKALYRGARI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 156 LLMDEPFGALDPvtrgalqQE----MTRIHRL--LGRTIVLVTHDIDEALRLAEHLVLMDHGEVVQqgnplTMLTRPANd 229
Cdd:COG3845 163 LILDEPTAVLTP-------QEadelFEILRRLaaEGKSIIFITHKLREVMAIADRVTVLRRGKVVG-----TVDTAETS- 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446491464 230 fvrqffgRSELgVRLLSLRSVADYVRREERAEGEAL--AEEMTLRDA--------LSLFVARGcEVL 286
Cdd:COG3845 230 -------EEEL-AELMVGREVLLRVEKAPAEPGEVVleVENLSVRDDrgvpalkdVSLEVRAG-EIL 287
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1-219 |
5.79e-30 |
|
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: 118.75 E-value: 5.79e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 1 MIEFSHVSKLF-----GAQKAVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRF-AGEEIRSL--PVLE 72
Cdd:TIGR03269 279 IIKVRNVSKRYisvdrGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrVGDEWVDMtkPGPD 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 73 LRRR----MGYAIQSIGLFPHWSVAQNIATVPQLQkwsrarIDDRIDELMALLGLES---------NLRERYPHQLSGGQ 139
Cdd:TIGR03269 359 GRGRakryIGILHQEYDLYPHRTVLDNLTEAIGLE------LPDELARMKAVITLKMvgfdeekaeEILDKYPDELSEGE 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 140 QQRVGVARALAADPQVLLMDEPFGALDPVTRGALQQEMTRIHRLLGRTIVLVTHDIDEALRLAEHLVLMDHGEVVQQGNP 219
Cdd:TIGR03269 433 RHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDP 512
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-219 |
7.05e-30 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 115.70 E-value: 7.05e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 2 IEFSHVSKLFGAQKAVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEIRSLPVLElRRRMGYAI 81
Cdd:PRK13536 42 IDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLA-RARIGVVP 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 82 QSIGLFPHWSVAQNIATVPQLQKWSRARIDDRIDELMALLGLESNLRERYPhQLSGGQQQRVGVARALAADPQVLLMDEP 161
Cdd:PRK13536 121 QFDNLDLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVS-DLSGGMKRRLTLARALINDPQLLILDEP 199
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 162 FGALDPVTRGALQQemtRIHRLL--GRTIVLVTHDIDEALRLAEHLVLMDHGEVVQQGNP 219
Cdd:PRK13536 200 TTGLDPHARHLIWE---RLRSLLarGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRP 256
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-226 |
7.08e-30 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 116.86 E-value: 7.08e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 1 MIEFSHVSKLFGAQKAVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEIRSLPVLELRRRMGYA 80
Cdd:PRK09536 3 MIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 81 IQSIGLFPHWSVAQNI--ATVPQLQKWSRARIDDR--IDELMALLGLeSNLRERYPHQLSGGQQQRVGVARALAADPQVL 156
Cdd:PRK09536 83 PQDTSLSFEFDVRQVVemGRTPHRSRFDTWTETDRaaVERAMERTGV-AQFADRPVTSLSGGERQRVLLARALAQATPVL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446491464 157 LMDEPFGALDpVTRGALQQEMTRihRLL--GRTIVLVTHDIDEALRLAEHLVLMDHGEVVQQGNPLTMLTRP 226
Cdd:PRK09536 162 LLDEPTASLD-INHQVRTLELVR--RLVddGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVLTAD 230
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1-195 |
1.02e-29 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 112.66 E-value: 1.02e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 1 MIEFSHVSKLF-GAQKAVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEIRSLPVLE---LRRR 76
Cdd:PRK10908 1 MIRFEHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREvpfLRRQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 77 MGYAIQSIGLFPHWSVAQNIATVPQLQKWSRARIDDRIDELMALLGLESNLRErYPHQLSGGQQQRVGVARALAADPQVL 156
Cdd:PRK10908 81 IGMIFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKN-FPIQLSGGEQQRVGIARAVVNKPAVL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 446491464 157 LMDEPFGALDpvtrGALQQEMTRIHRLLGR---TIVLVTHDI 195
Cdd:PRK10908 160 LADEPTGNLD----DALSEGILRLFEEFNRvgvTVLMATHDI 197
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
15-227 |
1.07e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 114.95 E-value: 1.07e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 15 KAVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIR----FAGEEIRSLPVL------------ELRRRMG 78
Cdd:PRK13631 40 VALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQvgdiYIGDKKNNHELItnpyskkiknfkELRRRVS 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 79 YAIQsiglFPHW-----SVAQNIATVPQLQKWSRARIDDRIDELMALLGLESNLRERYPHQLSGGQQQRVGVARALAADP 153
Cdd:PRK13631 120 MVFQ----FPEYqlfkdTIEKDIMFGPVALGVKKSEAKKLAKFYLNKMGLDDSYLERSPFGLSGGQKRRVAIAGILAIQP 195
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446491464 154 QVLLMDEPFGALDPvtrgALQQEMTRI---HRLLGRTIVLVTHDIDEALRLAEHLVLMDHGEVVQQGNPLTMLTRPA 227
Cdd:PRK13631 196 EILIFDEPTAGLDP----KGEHEMMQLildAKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTGTPYEIFTDQH 268
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
15-217 |
1.12e-29 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 115.19 E-value: 1.12e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 15 KAVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEIRSLPVLELRRRMGyAIQSI------GLFP 88
Cdd:PRK15079 35 KAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRAVRS-DIQMIfqdplaSLNP 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 89 HWSVAQNIAT-----VPQLqkwSRARIDDRIDELMALLGLESNLRERYPHQLSGGQQQRVGVARALAADPQVLLMDEPFG 163
Cdd:PRK15079 114 RMTIGEIIAEplrtyHPKL---SRQEVKDRVKAMMLKVGLLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVS 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446491464 164 ALDpVTRGA--------LQQEMtrihrllGRTIVLVTHDIDEALRLAEHLVLMDHGEVVQQG 217
Cdd:PRK15079 191 ALD-VSIQAqvvnllqqLQREM-------GLSLIFIAHDLAVVKHISDRVLVMYLGHAVELG 244
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
18-209 |
1.35e-29 |
|
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: 112.06 E-value: 1.35e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 18 NDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEIRSLPVLE---LR-RRMGYAIQSIGLFPHWSVA 93
Cdd:TIGR02211 22 KGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSSNErakLRnKKLGFIYQFHHLLPDFTAL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 94 QNIATVPQLQKWSRARIDDRIDELMALLGLESNLrERYPHQLSGGQQQRVGVARALAADPQVLLMDEPFGALDPVTRGAL 173
Cdd:TIGR02211 102 ENVAMPLLIGKKSVKEAKERAYEMLEKVGLEHRI-NHRPSELSGGERQRVAIARALVNQPSLVLADEPTGNLDNNNAKII 180
|
170 180 190
....*....|....*....|....*....|....*.
gi 446491464 174 QQEMTRIHRLLGRTIVLVTHDIDEALRLAEHLVLMD 209
Cdd:TIGR02211 181 FDLMLELNRELNTSFLVVTHDLELAKKLDRVLEMKD 216
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
15-237 |
2.45e-29 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 117.52 E-value: 2.45e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 15 KAVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEIRSL---PVLELRRR-MGYAIQSIGLFPHW 90
Cdd:PRK10535 22 EVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLdadALAQLRREhFGFIFQRYHLLSHL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 91 SVAQNI------ATVPQLQKWSRARiddridELMALLGLESNLrERYPHQLSGGQQQRVGVARALAADPQVLLMDEPFGA 164
Cdd:PRK10535 102 TAAQNVevpavyAGLERKQRLLRAQ------ELLQRLGLEDRV-EYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 165 LDPVTRgalQQEMTRIHRLL--GRTIVLVTHDIDEALRlAEHLVLMDHGEVV--------QQGNPLTMLTRPANDFVRQF 234
Cdd:PRK10535 175 LDSHSG---EEVMAILHQLRdrGHTVIIVTHDPQVAAQ-AERVIEIRDGEIVrnppaqekVNVAGGTEPVVNTASGWRQF 250
|
...
gi 446491464 235 FGR 237
Cdd:PRK10535 251 VSG 253
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
16-237 |
2.69e-29 |
|
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: 111.69 E-value: 2.69e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 16 AVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRL----VEHDSGEIRFAGEEIRSLPVLElrRRMGYAIQS-IGLF-PH 89
Cdd:TIGR02770 1 LVQDLNLSLKRGEVLALVGESGSGKSLTCLAILGLlppgLTQTSGEILLDGRPLLPLSIRG--RHIATIMQNpRTAFnPL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 90 WSVA-QNIATVPQLQKWSR-ARidDRIDELMALLGLE--SNLRERYPHQLSGGQQQRVGVARALAADPQVLLMDEPFGAL 165
Cdd:TIGR02770 79 FTMGnHAIETLRSLGKLSKqAR--ALILEALEAVGLPdpEEVLKKYPFQLSGGMLQRVMIALALLLEPPFLIADEPTTDL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446491464 166 DPVTRGALQQEMTRIHRLLGRTIVLVTHDIDEALRLAEHLVLMDHGEVVQQGNPLTMLTRPANDFVRQFFGR 237
Cdd:TIGR02770 157 DVVNQARVLKLLRELRQLFGTGILLITHDLGVVARIADEVAVMDDGRIVERGTVKEIFYNPKHETTRKLLSA 228
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
2-226 |
3.37e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 112.59 E-value: 3.37e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 2 IEFSHVSKLFGAQK--AVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLV---EHDSGEIRFAGEEIRSLPVLELRRR 76
Cdd:PRK13640 6 VEFKHVSFTYPDSKkpALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLlpdDNPNSKITVDGITLTAKTVWDIREK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 77 MGYAIQSI-GLFPHWSVAQNIATVPQLQKWSRARIDDRIDELMALLGLeSNLRERYPHQLSGGQQQRVGVARALAADPQV 155
Cdd:PRK13640 86 VGIVFQNPdNQFVGATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGM-LDYIDSEPANLSGGQKQRVAIAGILAVEPKI 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446491464 156 LLMDEPFGALDPVTRGALQQEMTRIHRLLGRTIVLVTHDIDEAlRLAEHLVLMDHGEVVQQGNPLTMLTRP 226
Cdd:PRK13640 165 IILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEA-NMADQVLVLDDGKLLAQGSPVEIFSKV 234
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
16-219 |
4.11e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 112.09 E-value: 4.11e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 16 AVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEI----RSLpvLELRRRMGYAIQSIG--LF-P 88
Cdd:PRK13639 17 ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIkydkKSL--LEVRKTVGIVFQNPDdqLFaP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 89 hwSVAQNIATVPQLQKWSRARIDDRIDELMALLGLEsNLRERYPHQLSGGQQQRVGVARALAADPQVLLMDEPFGALDPv 168
Cdd:PRK13639 95 --TVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGME-GFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDP- 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446491464 169 tRGALQqemtrIHRLL------GRTIVLVTHDIDEALRLAEHLVLMDHGEVVQQGNP 219
Cdd:PRK13639 171 -MGASQ-----IMKLLydlnkeGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTP 221
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
11-236 |
4.95e-29 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 112.00 E-value: 4.95e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 11 FGAQKAVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEIRSLPVLELRRRMGYAIQSI------ 84
Cdd:PRK10253 17 YGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNAttpgdi 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 85 --------GLFPHWsvaqniatvPQLQKWsRARIDDRIDELMALLGLeSNLRERYPHQLSGGQQQRVGVARALAADPQVL 156
Cdd:PRK10253 97 tvqelvarGRYPHQ---------PLFTRW-RKEDEEAVTKAMQATGI-THLADQSVDTLSGGQRQRAWIAMVLAQETAIM 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 157 LMDEPFGALDPVTRGALQQEMTRIHRLLGRTIVLVTHDIDEALRLAEHLVLMDHGEVVQQGNPLTMLTRpanDFVRQFFG 236
Cdd:PRK10253 166 LLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVTA---ELIERIYG 242
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1-218 |
1.16e-28 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 109.80 E-value: 1.16e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 1 MIEFSHVSKLFGAQKAVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEIRSLPVLELRRRMGYA 80
Cdd:PRK10247 7 LLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYC 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 81 IQSIGLFPHwSVAQNIATVPQLQKwsRARIDDRIDELMALLGLESNLRERYPHQLSGGQQQRVGVARALAADPQVLLMDE 160
Cdd:PRK10247 87 AQTPTLFGD-TVYDNLIFPWQIRN--QQPDPAIFLDDLERFALPDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDE 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446491464 161 PFGALDPVTRGALQQEMTRIHRLLGRTIVLVTHDIDEALRLAEHLVLMDHGEVVQQGN 218
Cdd:PRK10247 164 ITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDEINHADKVITLQPHAGEMQEAR 221
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1-269 |
3.12e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 110.08 E-value: 3.12e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 1 MIEFSHVSKLF-GAQKAVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEIRSLPVL-ELRRRMG 78
Cdd:PRK13644 1 MIRLENVSYSYpDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKLqGIRKLVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 79 YAIQSIGL-FPHWSVAQNIATVPQLQKWSRARIDDRIDELMALLGLEsNLRERYPHQLSGGQQQRVGVARALAADPQVLL 157
Cdd:PRK13644 81 IVFQNPETqFVGRTVEEDLAFGPENLCLPPIEIRKRVDRALAEIGLE-KYRHRSPKTLSGGQGQCVALAGILTMEPECLI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 158 MDEPFGALDPVTRGALQQEMTRIHRlLGRTIVLVTHDIDEaLRLAEHLVLMDHGEVVQQGNPLTMLTRPAndfvrqffgR 237
Cdd:PRK13644 160 FDEVTSMLDPDSGIAVLERIKKLHE-KGKTIVYITHNLEE-LHDADRIIVMDRGKIVLEGEPENVLSDVS---------L 228
|
250 260 270
....*....|....*....|....*....|....*....
gi 446491464 238 SELGVRLLSLRSVADYVRR-------EERAEGEALAEEM 269
Cdd:PRK13644 229 QTLGLTPPSLIELAENLKMhgvvipwENTSSPSSFAEEI 267
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-214 |
4.42e-28 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 109.02 E-value: 4.42e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 1 MIEFSHVSKLFGA-----QKAVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEIRSLPVLELRR 75
Cdd:COG1101 1 MLELKNLSKTFNPgtvneKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 76 RMGYAIQ--SIGLFPHWSVAQNIAtvpqL-----QKW------SRARIDDRIDELMAL-LGLESNLRERYPHqLSGGQQQ 141
Cdd:COG1101 81 YIGRVFQdpMMGTAPSMTIEENLA----LayrrgKRRglrrglTKKRRELFRELLATLgLGLENRLDTKVGL-LSGGQRQ 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446491464 142 RVGVARALAADPQVLLMDEPFGALDPVTRG---ALQQEMTRIHRLlgrTIVLVTHDIDEALRLAEHLVLMDHGEVV 214
Cdd:COG1101 156 ALSLLMATLTKPKLLLLDEHTAALDPKTAAlvlELTEKIVEENNL---TTLMVTHNMEQALDYGNRLIMMHEGRII 228
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
16-233 |
4.55e-28 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 113.26 E-value: 4.55e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 16 AVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEhDSGEIRFAGEEIRSL---PVLELRRRMGYAIQ--SIGLFPHW 90
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLIN-SQGEIWFDGQPLHNLnrrQLLPVRHRIQVVFQdpNSSLNPRL 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 91 SVAQNIAT-----VPQLqkwSRARIDDRIDELMALLGLESNLRERYPHQLSGGQQQRVGVARALAADPQVLLMDEPFGAL 165
Cdd:PRK15134 380 NVLQIIEEglrvhQPTL---SAAQREQQVIAVMEEVGLDPETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSL 456
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446491464 166 DPVTRG---ALQQEMTRIHRLlgrTIVLVTHDIDEALRLAEHLVLMDHGEVVQQGNPLTMLTRPANDFVRQ 233
Cdd:PRK15134 457 DKTVQAqilALLKSLQQKHQL---AYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERVFAAPQQEYTRQ 524
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
11-226 |
5.73e-28 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 109.42 E-value: 5.73e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 11 FGAQKAVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGeIRFAGEEI---RSL----PVLELRRRMGYAIQS 83
Cdd:PRK14271 31 FAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSG-YRYSGDVLlggRSIfnyrDVLEFRRRVGMLFQR 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 84 IGLFPHWSVAQNIATVPQLQKWSRARIDDRIDELMALLGLESNLRERY---PHQLSGGQQQRVGVARALAADPQVLLMDE 160
Cdd:PRK14271 110 PNPFPMSIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLWDAVKDRLsdsPFRLSGGQQQLLCLARTLAVNPEVLLLDE 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446491464 161 PFGALDPVTRGALQQEMTRIHRLLgrTIVLVTHDIDEALRLAEHLVLMDHGEVVQQGNPLTMLTRP 226
Cdd:PRK14271 190 PTSALDPTTTEKIEEFIRSLADRL--TVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSP 253
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
19-209 |
1.26e-27 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 107.21 E-value: 1.26e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 19 DLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEIRSLPV---LELR-RRMGYAIQSIGLFPHWSVAQ 94
Cdd:PRK11629 27 NVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSaakAELRnQKLGFIYQFHHLLPDFTALE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 95 NIATVPQLQKWSRARIDDRIDELMALLGLESNLRERyPHQLSGGQQQRVGVARALAADPQVLLMDEPFGALDPVTRGALQ 174
Cdd:PRK11629 107 NVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHR-PSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADSIF 185
|
170 180 190
....*....|....*....|....*....|....*
gi 446491464 175 QEMTRIHRLLGRTIVLVTHDIDEALRLAEHLVLMD 209
Cdd:PRK11629 186 QLLGELNRLQGTAFLVVTHDLQLAKRMSRQLEMRD 220
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
2-203 |
2.03e-27 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 107.56 E-value: 2.03e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 2 IEFSHVSKLFGAQKAVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRL--------VEhdsGEIRFAGEEIRSLPV--L 71
Cdd:PRK14243 11 LRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLndlipgfrVE---GKVTFHGKNLYAPDVdpV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 72 ELRRRMGYAIQSIGLFPHwSVAQNIATVPQLQKWsRARIDDRIDELMALLGLESNLRERYPHQ---LSGGQQQRVGVARA 148
Cdd:PRK14243 88 EVRRRIGMVFQKPNPFPK-SIYDNIAYGARINGY-KGDMDELVERSLRQAALWDEVKDKLKQSglsLSGGQQQRLCIARA 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446491464 149 LAADPQVLLMDEPFGALDPVTRGALQQEMtriHRLLGR-TIVLVTHDIDEALRLAE 203
Cdd:PRK14243 166 IAVQPEVILMDEPCSALDPISTLRIEELM---HELKEQyTIIIVTHNMQQAARVSD 218
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
17-219 |
2.94e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 107.49 E-value: 2.94e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 17 VNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEIRSLPVLELRRRMGYAIQSI-GLFPHWSVAQN 95
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIGMVFQNPdNQFVGATVEDD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 96 IATVPQLQKWSRARIDDRIDElmALLGLES-NLRERYPHQLSGGQQQRVGVARALAADPQVLLMDEPFGALDPVTRGALQ 174
Cdd:PRK13642 103 VAFGMENQGIPREEMIKRVDE--ALLAVNMlDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIM 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 446491464 175 QEMTRIHRLLGRTIVLVTHDIDEALRlAEHLVLMDHGEVVQQGNP 219
Cdd:PRK13642 181 RVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAP 224
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1-222 |
4.79e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 106.76 E-value: 4.79e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 1 MIEFSHVSKLFGAQKA--VNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEIRSLPVLELRRRMG 78
Cdd:PRK13648 7 IIVFKNVSFQYQSDASftLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 79 YAIQS-----IGLFPHWSVA---QNIAtVPQlqkwsrARIDDRIDELMALLGLeSNLRERYPHQLSGGQQQRVGVARALA 150
Cdd:PRK13648 87 IVFQNpdnqfVGSIVKYDVAfglENHA-VPY------DEMHRRVSEALKQVDM-LERADYEPNALSGGQKQRVAIAGVLA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446491464 151 ADPQVLLMDEPFGALDPVTRGALQQEMTRIHRLLGRTIVLVTHDIDEALRlAEHLVLMDHGEVVQQGNPLTM 222
Cdd:PRK13648 159 LNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEI 229
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
17-217 |
5.13e-27 |
|
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: 110.80 E-value: 5.13e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 17 VNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEIRSLPVLELRRRMGYAIQSIGLFpHWSVAQNI 96
Cdd:TIGR03796 495 IENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIPREEIPREVLANSVAMVDQDIFLF-EGTVRDNL 573
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 97 A----TVPQlQKWSRARIDDRI-DELMALLG-LESNLRERyPHQLSGGQQQRVGVARALAADPQVLLMDEPFGALDPVTR 170
Cdd:TIGR03796 574 TlwdpTIPD-ADLVRACKDAAIhDVITSRPGgYDAELAEG-GANLSGGQRQRLEIARALVRNPSILILDEATSALDPETE 651
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 446491464 171 GALQQEMTRihRllGRTIVLVTHDIdEALRLAEHLVLMDHGEVVQQG 217
Cdd:TIGR03796 652 KIIDDNLRR--R--GCTCIIVAHRL-STIRDCDEIIVLERGKVVQRG 693
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
12-222 |
5.16e-27 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 106.31 E-value: 5.16e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 12 GAQKAVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEeirslPVLELRRRMGYAIQ--------- 82
Cdd:PRK10419 23 QHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGE-----PLAKLNRAQRKAFRrdiqmvfqd 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 83 SIGLF-PHWSVAQNIAT-VPQLQKWSRARIDDRIDELMALLGLESNLRERYPHQLSGGQQQRVGVARALAADPQVLLMDE 160
Cdd:PRK10419 98 SISAVnPRKTVREIIREpLRHLLSLDKAERLARASEMLRAVDLDDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDE 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446491464 161 PFGALDPVTRGALQQEMTRIHRLLGRTIVLVTHDIDEALRLAEHLVLMDHGEVVQQ---GNPLTM 222
Cdd:PRK10419 178 AVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVETqpvGDKLTF 242
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
17-213 |
6.23e-27 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 103.84 E-value: 6.23e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 17 VNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEIRSLPVLELRRRMGYAIQSIGLFPHwSVAQNI 96
Cdd:cd03246 18 LRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGYLPQDDELFSG-SIAENI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 97 atvpqlqkwsrariddridelmallglesnlreryphqLSGGQQQRVGVARALAADPQVLLMDEPFGALDPVTRGALQQE 176
Cdd:cd03246 97 --------------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQA 138
|
170 180 190
....*....|....*....|....*....|....*..
gi 446491464 177 MTRIhRLLGRTIVLVTHDIdEALRLAEHLVLMDHGEV 213
Cdd:cd03246 139 IAAL-KAAGATRIVIAHRP-ETLASADRILVLEDGRV 173
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
12-214 |
8.33e-27 |
|
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: 104.26 E-value: 8.33e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 12 GAQKAVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGeeiRSLPVLELRRRMGYAIQSIG--LFPH 89
Cdd:cd03226 11 KGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNG---KPIKAKERRKSIGYVMQDVDyqLFTD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 90 wSVAQNIA-TVPQLqkwsrARIDDRIDELMALLGLeSNLRERYPHQLSGGQQQRVGVARALAADPQVLLMDEPFGALDPv 168
Cdd:cd03226 88 -SVREELLlGLKEL-----DAGNEQAETVLKDLDL-YALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDY- 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446491464 169 trgalqQEMTRIHRLL------GRTIVLVTHDIDEALRLAEHLVLMDHGEVV 214
Cdd:cd03226 160 ------KNMERVGELIrelaaqGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-219 |
1.25e-26 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 104.78 E-value: 1.25e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 1 MIEFSHVSK---------------LFGAQK-------AVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEI 58
Cdd:COG1134 4 MIEVENVSKsyrlyhepsrslkelLLRRRRtrreefwALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 59 RFAGeEIRSLpvLELrrrmgyaiqSIGLFPHWSVAQNIATVPQLQKWSRARIDDRIDELMALLGLESNLRE---RYphql 135
Cdd:COG1134 84 EVNG-RVSAL--LEL---------GAGFHPELTGRENIYLNGRLLGLSRKEIDEKFDEIVEFAELGDFIDQpvkTY---- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 136 SGGQQQRVGVARALAADPQVLLMDEPFGALDPvtrgALQQE-MTRIHRLL--GRTIVLVTHDIDEALRLAEHLVLMDHGE 212
Cdd:COG1134 148 SSGMRARLAFAVATAVDPDILLVDEVLAVGDA----AFQKKcLARIRELResGRTVIFVSHSMGAVRRLCDRAIWLEKGR 223
|
....*..
gi 446491464 213 VVQQGNP 219
Cdd:COG1134 224 LVMDGDP 230
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
16-236 |
3.86e-26 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 108.56 E-value: 3.86e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 16 AVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEIRSlPVLELRRRMGYAIQSIGLFPHWSVAQN 95
Cdd:TIGR01257 945 AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIET-NLDAVRQSLGMCPQHNILFHHLTVAEH 1023
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 96 IATVPQLQ--KWSRARIDdrIDELMALLGLESNlRERYPHQLSGGQQQRVGVARALAADPQVLLMDEPFGALDPVTRGAL 173
Cdd:TIGR01257 1024 ILFYAQLKgrSWEEAQLE--MEAMLEDTGLHHK-RNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSI 1100
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446491464 174 QQEMTRIHRllGRTIVLVTHDIDEALRLAEHLVLMDHGEVVQQGNPLtmltrpandFVRQFFG 236
Cdd:TIGR01257 1101 WDLLLKYRS--GRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTPL---------FLKNCFG 1152
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
4-212 |
3.87e-26 |
|
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: 102.55 E-value: 3.87e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 4 FSHVSKLFGAQKAVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGeeirslpvlelrrRMGYAIQS 83
Cdd:cd03250 8 FTWDSGEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG-------------SIAYVSQE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 84 iglfPhW----SVAQNIAtvpqlqkWSRARIDDRIDELMALLGLESNLrERYPHQ-----------LSGGQQQRVGVARA 148
Cdd:cd03250 75 ----P-WiqngTIRENIL-------FGKPFDEERYEKVIKACALEPDL-EILPDGdlteigekginLSGGQKQRISLARA 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446491464 149 LAADPQVLLMDEPFGALDPVTRGALQQEMTRIHRLLGRTIVLVTHDIdEALRLAEHLVLMDHGE 212
Cdd:cd03250 142 VYSDADIYLLDDPLSAVDAHVGRHIFENCILGLLLNNKTRILVTHQL-QLLPHADQIVVLDNGR 204
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
2-218 |
4.41e-26 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 107.74 E-value: 4.41e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 2 IEFSHVSKLF-GAQKAVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEIRSLPVLELRRRMGYA 80
Cdd:PRK13657 335 VEFDDVSFSYdNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAVV 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 81 IQSIGLFPHwSVAQNI------ATVPQLQK-WSRARIDDRIDElmALLGLESNLRERyPHQLSGGQQQRVGVARALAADP 153
Cdd:PRK13657 415 FQDAGLFNR-SIEDNIrvgrpdATDEEMRAaAERAQAHDFIER--KPDGYDTVVGER-GRQLSGGERQRLAIARALLKDP 490
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446491464 154 QVLLMDEPFGALDPVTRGALQQEMTRIHRllGRTIVLVTHDIdEALRLAEHLVLMDHGEVVQQGN 218
Cdd:PRK13657 491 PILILDEATSALDVETEAKVKAALDELMK--GRTTFIIAHRL-STVRNADRILVFDNGRVVESGS 552
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
12-217 |
7.36e-26 |
|
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: 107.14 E-value: 7.36e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 12 GAQKAV-NDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEIRSLPVLELRRRMGYAIQSIGLFPHw 90
Cdd:COG4618 342 GSKRPIlRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRHIGYLPQDVELFDG- 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 91 SVAQNIATVPQL---------QkwsRARIDDRIDELMalLGLESNLRERyPHQLSGGQQQRVGVARALAADPQVLLMDEP 161
Cdd:COG4618 421 TIAENIARFGDAdpekvvaaaK---LAGVHEMILRLP--DGYDTRIGEG-GARLSGGQRQRIGLARALYGDPRLVVLDEP 494
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446491464 162 FGALDPVTRGALQQEMTRIhRLLGRTIVLVTHDIdEALRLAEHLVLMDHGEVVQQG 217
Cdd:COG4618 495 NSNLDDEGEAALAAAIRAL-KARGATVVVITHRP-SLLAAVDKLLVLRDGRVQAFG 548
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1-217 |
1.78e-25 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 102.40 E-value: 1.78e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 1 MIEFSHVSKLFGAQKAVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDS---GEIRFAGEEIR-----SLPVLE 72
Cdd:PRK09984 4 IIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKsagSHIELLGRTVQregrlARDIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 73 LRRRMGYAIQSIGLFPHWSVAQN--IATVPQLQKWSRA-RIDDRIDELMALLGLESNLRERYPHQ----LSGGQQQRVGV 145
Cdd:PRK09984 84 SRANTGYIFQQFNLVNRLSVLENvlIGALGSTPFWRTCfSWFTREQKQRALQALTRVGMVHFAHQrvstLSGGQQQRVAI 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446491464 146 ARALAADPQVLLMDEPFGALDPVTRGALQQEMTRIHRLLGRTIVLVTHDIDEALRLAEHLVLMDHGEVVQQG 217
Cdd:PRK09984 164 ARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDG 235
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
12-213 |
2.90e-25 |
|
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: 105.51 E-value: 2.90e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 12 GAQKAVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEIRSLPVLELRRRMGYAIQSIGLFPHwS 91
Cdd:TIGR01842 329 GKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGKHIGYLPQDVELFPG-T 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 92 VAQNIAtvpqlqkwsraRIDDRID--------------ELMALL--GLESNLRERyPHQLSGGQQQRVGVARALAADPQV 155
Cdd:TIGR01842 408 VAENIA-----------RFGENADpekiieaaklagvhELILRLpdGYDTVIGPG-GATLSGGQRQRIALARALYGDPKL 475
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446491464 156 LLMDEPFGALDPVTRGALQQEMTRIhRLLGRTIVLVTHDIdEALRLAEHLVLMDHGEV 213
Cdd:TIGR01842 476 VVLDEPNSNLDEEGEQALANAIKAL-KARGITVVVITHRP-SLLGCVDKILVLQDGRI 531
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
16-256 |
2.90e-25 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 105.71 E-value: 2.90e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 16 AVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEIRSLP---VLELRRRMGYAIQS--IGLFPHW 90
Cdd:PRK10261 339 AVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSpgkLQALRRDIQFIFQDpyASLDPRQ 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 91 SVAQNIAT---VPQLQKWSRARidDRIDELMALLGLESNLRERYPHQLSGGQQQRVGVARALAADPQVLLMDEPFGALDP 167
Cdd:PRK10261 419 TVGDSIMEplrVHGLLPGKAAA--ARVAWLLERVGLLPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDV 496
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 168 VTRGALQQEMTRIHRLLGRTIVLVTHDIDEALRLAEHLVLMDHGEVVQQGNPLTMLTRPANDFVRqffgrselgvRLLSL 247
Cdd:PRK10261 497 SIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENPQHPYTR----------KLMAA 566
|
....*....
gi 446491464 248 RSVADYVRR 256
Cdd:PRK10261 567 VPVADPSRQ 575
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
16-217 |
3.89e-25 |
|
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: 100.48 E-value: 3.89e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 16 AVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGE---EIRSlpvlELRRRMGYAI-QSIGLFPHWS 91
Cdd:cd03267 36 ALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLvpwKRRK----KFLRRIGVVFgQKTQLWWDLP 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 92 VAQNIATVPQLQKWSRARIDDRIDELMALLGLESNLRERYpHQLSGGQQQRVGVARALAADPQVLLMDEPFGALDPVTRG 171
Cdd:cd03267 112 VIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPV-RQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQE 190
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 446491464 172 ALQQEMTRIHRLLGRTIVLVTHDIDEALRLAEHLVLMDHGEVVQQG 217
Cdd:cd03267 191 NIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
20-223 |
6.19e-25 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 101.02 E-value: 6.19e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 20 LNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEIRSLPVLELRRRMGYAIQSI----GLFPHWSVAqn 95
Cdd:PRK10575 30 LSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLPQQLpaaeGMTVRELVA-- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 96 IATVPQLQKWSRARIDDR--IDELMALLGLESnLRERYPHQLSGGQQQRVGVARALAADPQVLLMDEPFGALD---PVTR 170
Cdd:PRK10575 108 IGRYPWHGALGRFGAADRekVEEAISLVGLKP-LAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDiahQVDV 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446491464 171 GALQQEMTRIHrllGRTIVLVTHDIDEALRLAEHLVLMDHGEVVQQGNPLTML 223
Cdd:PRK10575 187 LALVHRLSQER---GLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELM 236
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
32-209 |
6.64e-25 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 99.85 E-value: 6.64e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 32 LIGTSGSGKSTTLKMINRLVEHDSGEIRFAG-------EEIRSlpvlELR-RRMGYAIQSIGLFPHWSVAQNIATVPQLQ 103
Cdd:PRK10584 41 LIGESGSGKSTLLAILAGLDDGSSGEVSLVGqplhqmdEEARA----KLRaKHVGFVFQSFMLIPTLNALENVELPALLR 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 104 KWSRARIDDRIDELMALLGLESNLRErYPHQLSGGQQQRVGVARALAADPQVLLMDEPFGALDPVTRGALQQEMTRIHRL 183
Cdd:PRK10584 117 GESSRQSRNGAKALLEQLGLGKRLDH-LPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNRE 195
|
170 180
....*....|....*....|....*.
gi 446491464 184 LGRTIVLVTHDIDEALRLAEHLVLMD 209
Cdd:PRK10584 196 HGTTLILVTHDLQLAARCDRRLRLVN 221
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
1-217 |
1.05e-24 |
|
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: 99.90 E-value: 1.05e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 1 MIEFSHVSKLFGAQKAVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGE-----EIRSLPVLELRR 75
Cdd:TIGR02323 3 LLQVSGLSKSYGGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMRsgaelELYQLSEAERRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 76 RM----GYAIQSI--GLFPHWSVAQNIATVP-------------QLQKW-SRARID-DRIDELmallglesnlreryPHQ 134
Cdd:TIGR02323 83 LMrtewGFVHQNPrdGLRMRVSAGANIGERLmaigarhygniraTAQDWlEEVEIDpTRIDDL--------------PRA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 135 LSGGQQQRVGVARALAADPQVLLMDEPFGALDPVTRGALQQEMTRIHRLLGRTIVLVTHDIDEALRLAEHLVLMDHGEVV 214
Cdd:TIGR02323 149 FSGGMQQRLQIARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRVV 228
|
...
gi 446491464 215 QQG 217
Cdd:TIGR02323 229 ESG 231
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
15-217 |
3.55e-24 |
|
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: 97.73 E-value: 3.55e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 15 KAVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHD---SGEIRFAGEEIRSLpvlELRRRMGYAIQSIGLFPHWS 91
Cdd:cd03234 21 RILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGgttSGQILFNGQPRKPD---QFQKCVAYVRQDDILLPGLT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 92 VAQNIATVPQ--LQKWSRARIDDRIDELMAL--LGLESnLRERYPHQLSGGQQQRVGVARALAADPQVLLMDEPFGALDP 167
Cdd:cd03234 98 VRETLTYTAIlrLPRKSSDAIRKKRVEDVLLrdLALTR-IGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDS 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446491464 168 VTRGALQQEMTRIHRlLGRTIVLVTHDI-DEALRLAEHLVLMDHGEVVQQG 217
Cdd:cd03234 177 FTALNLVSTLSQLAR-RNRIVILTIHQPrSDLFRLFDRILLLSSGEIVYSG 226
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
14-233 |
4.44e-24 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 101.71 E-value: 4.44e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 14 QKAVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRL-----VEHDSGEIRFAGEEIRSLPVLELRRRMGYAIQSI---- 84
Cdd:PRK15134 22 RTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLlpsppVVYPSGDIRFHGESLLHASEQTLRGVRGNKIAMIfqep 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 85 --GLFPHWSVAQNIATVPQL-----QKWSRARIDDRIDELmALLGLESNLRErYPHQLSGGQQQRVGVARALAADPQVLL 157
Cdd:PRK15134 102 mvSLNPLHTLEKQLYEVLSLhrgmrREAARGEILNCLDRV-GIRQAAKRLTD-YPHQLSGGERQRVMIAMALLTRPELLI 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446491464 158 MDEPFGALDPVTRGALQQEMTRIHRLLGRTIVLVTHDIDEALRLAEHLVLMDHGEVVQQGNPLTMLTRPANDFVRQ 233
Cdd:PRK15134 180 ADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAATLFSAPTHPYTQK 255
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
2-225 |
4.86e-24 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 102.02 E-value: 4.86e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 2 IEFSHVSKLF-GAQK-AVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEIRSLPVLELRRRMGY 79
Cdd:PRK11176 342 IEFRNVTFTYpGKEVpALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVAL 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 80 AIQSIGLFPHwSVAQNIATVPQlQKWSRARIddridELMALLGLESNLRERYPH-----------QLSGGQQQRVGVARA 148
Cdd:PRK11176 422 VSQNVHLFND-TIANNIAYART-EQYSREQI-----EEAARMAYAMDFINKMDNgldtvigengvLLSGGQRQRIAIARA 494
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 149 LAADPQVLLMDEPFGALDPVTRGALQQEMTRIHRllGRTIVLVTHdidealRL-----AEHLVLMDHGEVVQQGNPLTML 223
Cdd:PRK11176 495 LLRDSPILILDEATSALDTESERAIQAALDELQK--NRTSLVIAH------RLstiekADEILVVEDGEIVERGTHAELL 566
|
..
gi 446491464 224 TR 225
Cdd:PRK11176 567 AQ 568
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
4-233 |
5.26e-24 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 98.32 E-value: 5.26e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 4 FSHVSKLFGAQ--KAVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEI-------RSLpvlelR 74
Cdd:PRK15112 14 FRYRTGWFRRQtvEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLhfgdysyRSQ-----R 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 75 RRMGYAIQSIGLFPHWSVAQnIATVP-----QLQKWSRARiddRIDELMALLGLESNLRERYPHQLSGGQQQRVGVARAL 149
Cdd:PRK15112 89 IRMIFQDPSTSLNPRQRISQ-ILDFPlrlntDLEPEQREK---QIIETLRQVGLLPDHASYYPHMLAPGQKQRLGLARAL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 150 AADPQVLLMDEPFGALDPVTRGALQQEMTRIHRLLGRTIVLVTHDIDEALRLAEHLVLMDHGEVVQQGNPLTMLTRPAND 229
Cdd:PRK15112 165 ILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVLASPLHE 244
|
....
gi 446491464 230 FVRQ 233
Cdd:PRK15112 245 LTKR 248
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
2-217 |
5.71e-24 |
|
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: 97.22 E-value: 5.71e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 2 IEFSHVSKLF----------------------GAQKAVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIR 59
Cdd:cd03220 1 IELENVSKSYptykggssslkklgilgrkgevGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 60 FAGeeiRSLPVLELrrrmgyaiqSIGLFPHWSVAQNIATVPQLQKWSRARIDDRIDELMALLGLESNLRERYPHqLSGGQ 139
Cdd:cd03220 81 VRG---RVSSLLGL---------GGGFNPELTGRENIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKT-YSSGM 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 140 QQRVGVARALAADPQVLLMDEPFGALDPvtrgALQQEMT-RIHRLL--GRTIVLVTHDIDEALRLAEHLVLMDHGEVVQQ 216
Cdd:cd03220 148 KARLAFAIATALEPDILLIDEVLAVGDA----AFQEKCQrRLRELLkqGKTVILVSHDPSSIKRLCDRALVLEKGKIRFD 223
|
.
gi 446491464 217 G 217
Cdd:cd03220 224 G 224
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
2-217 |
7.27e-24 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 96.08 E-value: 7.27e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 2 IEFSHVSKLFGAQKAV-NDLNLNFQEGSFSVLIGTSGSGKSTTLKMIN--RLVEHDSGEIRFAGeeiRSLPVLELRRRMG 78
Cdd:cd03213 9 LTVTVKSSPSKSGKQLlKNVSGKAKPGELTAIMGPSGAGKSTLLNALAgrRTGLGVSGEVLING---RPLDKRSFRKIIG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 79 YAIQSIGLFPHWSVAQNiatvpqlqkwsrariddridelmalLGLESNLReryphQLSGGQQQRVGVARALAADPQVLLM 158
Cdd:cd03213 86 YVPQDDILHPTLTVRET-------------------------LMFAAKLR-----GLSGGERKRVSIALELVSNPSLLFL 135
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446491464 159 DEPFGALDPVTrgALQ-QEMTRIHRLLGRTIVLVTHDI-DEALRLAEHLVLMDHGEVVQQG 217
Cdd:cd03213 136 DEPTSGLDSSS--ALQvMSLLRRLADTGRTIICSIHQPsSEIFELFDKLLLLSQGRVIYFG 194
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
7-226 |
8.09e-24 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 98.88 E-value: 8.09e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 7 VSK-LFGAQ---KAVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEIRSLP--VLELRRRmgyA 80
Cdd:PRK11308 17 VKRgLFKPErlvKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADpeAQKLLRQ---K 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 81 IQSI------GLFPHWSVAQnIATVPQL--QKWSRARIDDRIDELMALLGLESNLRERYPHQLSGGQQQRVGVARALAAD 152
Cdd:PRK11308 94 IQIVfqnpygSLNPRKKVGQ-ILEEPLLinTSLSAAERREKALAMMAKVGLRPEHYDRYPHMFSGGQRQRIAIARALMLD 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 153 PQVLLMDEPFGALDPVTRGA-------LQQEMtrihrllGRTIVLVTHDIDEALRLAEHLVLMDHGEVVQQGNPLTMLTR 225
Cdd:PRK11308 173 PDVVVADEPVSALDVSVQAQvlnlmmdLQQEL-------GLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFNN 245
|
.
gi 446491464 226 P 226
Cdd:PRK11308 246 P 246
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
2-226 |
8.29e-24 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 101.34 E-value: 8.29e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 2 IEFSHVSKLFGAQKAV---NDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEIRSLPVLELRRRMG 78
Cdd:TIGR00958 479 IEFQDVSFSYPNRPDVpvlKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVA 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 79 YAIQSIGLFPHwSVAQNIA------TVPQLQKWSR-ARIDDRIDELMAllGLESNLRERyPHQLSGGQQQRVGVARALAA 151
Cdd:TIGR00958 559 LVGQEPVLFSG-SVRENIAygltdtPDEEIMAAAKaANAHDFIMEFPN--GYDTEVGEK-GSQLSGGQKQRIAIARALVR 634
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446491464 152 DPQVLLMDEPFGALDPVTRGALQQEMTRihrlLGRTIVLVTHDIDEALRlAEHLVLMDHGEVVQQGNPLTMLTRP 226
Cdd:TIGR00958 635 KPRVLILDEATSALDAECEQLLQESRSR----ASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQLMEDQ 704
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-225 |
1.47e-23 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 100.67 E-value: 1.47e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 2 IEFSHVSklFG----AQKAVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEIRSLPVLELRRRM 77
Cdd:PRK11160 339 LTLNNVS--FTypdqPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQAI 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 78 GYAIQSIGLFPHwSVAQNiatvpqLQKWSRARIDDRIDELMALLGLESNLRERYP---------HQLSGGQQQRVGVARA 148
Cdd:PRK11160 417 SVVSQRVHLFSA-TLRDN------LLLAAPNASDEALIEVLQQVGLEKLLEDDKGlnawlgeggRQLSGGEQRRLGIARA 489
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446491464 149 LAADPQVLLMDEPFGALDPVTRgalQQEMTRIHRLL-GRTIVLVTHDIdEALRLAEHLVLMDHGEVVQQGNPLTMLTR 225
Cdd:PRK11160 490 LLHDAPLLLLDEPTEGLDAETE---RQILELLAEHAqNKTVLMITHRL-TGLEQFDRICVMDNGQIIEQGTHQELLAQ 563
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
2-218 |
2.55e-23 |
|
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: 99.89 E-value: 2.55e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 2 IEFSHVSklFG---AQKAVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEIRSLPVLELRRRMG 78
Cdd:COG5265 358 VRFENVS--FGydpERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIG 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 79 YAIQSIGLFPHwSVAQNI------ATVPQLQKWSR-ARIDDRIDELMAllGLESNLRERyPHQLSGGQQQRVGVARALAA 151
Cdd:COG5265 436 IVPQDTVLFND-TIAYNIaygrpdASEEEVEAAARaAQIHDFIESLPD--GYDTRVGER-GLKLSGGEKQRVAIARTLLK 511
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446491464 152 DPQVLLMDEPFGALDPVTRGALQQEMTRIHRllGRTIVLVTHdidealRL-----AEHLVLMDHGEVVQQGN 218
Cdd:COG5265 512 NPPILIFDEATSALDSRTERAIQAALREVAR--GRTTLVIAH------RLstivdADEILVLEAGRIVERGT 575
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
12-227 |
3.78e-23 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 97.10 E-value: 3.78e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 12 GAQKAVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHD---SGEIRFAGEEIRSLPVLELRRRMGYAIQSI---- 84
Cdd:PRK09473 27 GDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANgriGGSATFNGREILNLPEKELNKLRAEQISMIfqdp 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 85 --GLFPHWSVAQNIATVPQLQK-WSRAR-IDDRIDELMALLGLESNLRER-YPHQLSGGQQQRVGVARALAADPQVLLMD 159
Cdd:PRK09473 107 mtSLNPYMRVGEQLMEVLMLHKgMSKAEaFEESVRMLDAVKMPEARKRMKmYPHEFSGGMRQRVMIAMALLCRPKLLIAD 186
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446491464 160 EPFGALDpVTRGAlqQEMTRIHRL---LGRTIVLVTHDIDEALRLAEHLVLMDHGEVVQQGNPLTMLTRPA 227
Cdd:PRK09473 187 EPTTALD-VTVQA--QIMTLLNELkreFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARDVFYQPS 254
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-281 |
3.95e-23 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 97.08 E-value: 3.95e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 1 MIEFSHVSK----------LFGAQK-----------AVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIR 59
Cdd:COG4586 1 IIEVENLSKtyrvyekepgLKGALKglfrreyreveAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 60 FAGEEirslPVlelRRRMGYAiQSIG--------LFPHWSVAQNIATVPQLQKWSRARIDDRIDELMALLGLESNLRE-- 129
Cdd:COG4586 81 VLGYV----PF---KRRKEFA-RRIGvvfgqrsqLWWDLPAIDSFRLLKAIYRIPDAEYKKRLDELVELLDLGELLDTpv 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 130 RyphQLSGGQQQRVGVARALAADPQVLLMDEPFGALDPVTRGALQQEMTRIHRLLGRTIVLVTHDIDEALRLAEHLVLMD 209
Cdd:COG4586 153 R---QLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEALCDRVIVID 229
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446491464 210 HGEVVQQGnpltmltrPANDFVRQFFGRSELGVRL---LSLRSVADYVRREERAEGEA---LAEEMTLRDALSLFVAR 281
Cdd:COG4586 230 HGRIIYDG--------SLEELKERFGPYKTIVLELaepVPPLELPRGGEVIEREGNRVrleVDPRESLAEVLARLLAR 299
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
15-213 |
5.39e-23 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 93.27 E-value: 5.39e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 15 KAVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEIRSLPVLELRRR-MGYAI---QSIGLFPHW 90
Cdd:cd03215 14 GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAgIAYVPedrKREGLVLDL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 91 SVAQNIATvpqlqkwsrariddridelmallglesnlreryPHQLSGGQQQRVGVARALAADPQVLLMDEPfgaldpvTR 170
Cdd:cd03215 94 SVAENIAL---------------------------------SSLLSGGNQQKVVLARWLARDPRVLILDEP-------TR 133
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446491464 171 G---ALQQEmtrIHRLL------GRTIVLVTHDIDEALRLAEHLVLMDHGEV 213
Cdd:cd03215 134 GvdvGAKAE---IYRLIreladaGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
32-224 |
5.41e-23 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 95.29 E-value: 5.41e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 32 LIGTSGSGKSTTLKMINRLVEHdSGEIRFAGEEIRSLPVLELRRRMGYaiqsiglfphwsVAQNIATVPQLQKW------ 105
Cdd:COG4138 27 LIGPNGAGKSTLLARMAGLLPG-QGEILLNGRPLSDWSAAELARHRAY------------LSQQQSPPFAMPVFqylalh 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 106 -----SRARIDDRIDELMALLGLESNLrERYPHQLSGGQQQRVGVARAL-----AADP--QVLLMDEPFGALDPVTRGAL 173
Cdd:COG4138 94 qpagaSSEAVEQLLAQLAEALGLEDKL-SRPLTQLSGGEWQRVRLAAVLlqvwpTINPegQLLLLDEPMNSLDVAQQAAL 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446491464 174 QQEMTRIHRlLGRTIVLVTHDIDEALRLAEHLVLMDHGEVVQQGNPLTMLT 224
Cdd:COG4138 173 DRLLRELCQ-QGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEVMT 222
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
7-217 |
1.26e-22 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 94.22 E-value: 1.26e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 7 VSKLFGAQKAVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEIRSLPVLEL---RRRM------ 77
Cdd:PRK11701 12 LTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYALseaERRRllrtew 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 78 GYAIQSI--GLFPHWSVAQNIATVPQLQKW--------------SRARID-DRIDELmallglesnlreryPHQLSGGQQ 140
Cdd:PRK11701 92 GFVHQHPrdGLRMQVSAGGNIGERLMAVGArhygdiratagdwlERVEIDaARIDDL--------------PTTFSGGMQ 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446491464 141 QRVGVARALAADPQVLLMDEPFGALDPVTRGALQQEMTRIHRLLGRTIVLVTHDIDEALRLAEHLVLMDHGEVVQQG 217
Cdd:PRK11701 158 QRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVVESG 234
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
12-194 |
2.25e-22 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 97.05 E-value: 2.25e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 12 GAQKAVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEIRSLPVLELRRRMGYAIQSIGLFpHWS 91
Cdd:TIGR02868 346 GAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLF-DTT 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 92 VAQNIATvpqlqkwsrARIDDRIDELMALL---GLESNLRERyPH-----------QLSGGQQQRVGVARALAADPQVLL 157
Cdd:TIGR02868 425 VRENLRL---------ARPDATDEELWAALervGLADWLRAL-PDgldtvlgeggaRLSGGERQRLALARALLADAPILL 494
|
170 180 190
....*....|....*....|....*....|....*..
gi 446491464 158 MDEPFGALDPVTRGALQQEMTRIHRllGRTIVLVTHD 194
Cdd:TIGR02868 495 LDEPTEHLDAETADELLEDLLAALS--GRTVVLITHH 529
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
16-226 |
2.58e-22 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 96.71 E-value: 2.58e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 16 AVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEIRSLPVLELRRRMGYAIQSIGLFPHwSVAQN 95
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFLFSD-TVANN 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 96 IA----TVPQLQKWSRARIDDRIDELMAL-LGLESNLRERyPHQLSGGQQQRVGVARALAADPQVLLMDEPFGALDPVTR 170
Cdd:PRK10789 409 IAlgrpDATQQEIEHVARLASVHDDILRLpQGYDTEVGER-GVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTE 487
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446491464 171 GALQQEMTRIHRllGRTIVLVTHDIdEALRLAEHLVLMDHGEVVQQGNPLTMLTRP 226
Cdd:PRK10789 488 HQILHNLRQWGE--GRTVIISAHRL-SALTEASEILVMQHGHIAQRGNHDQLAQQS 540
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
17-214 |
3.04e-22 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 96.24 E-value: 3.04e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 17 VNDLNLN--FQEGSFSV-------LIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEE--IRSlPVLELRRRMGYAI---Q 82
Cdd:COG1129 259 VEGLSVGgvVRDVSFSVrageilgIAGLVGAGRTELARALFGADPADSGEIRLDGKPvrIRS-PRDAIRAGIAYVPedrK 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 83 SIGLFPHWSVAQNIaTVPQLQKWSR------ARIDDRIDELMALLGLESNLRERYPHQLSGGQQQRVGVARALAADPQVL 156
Cdd:COG1129 338 GEGLVLDLSIRENI-TLASLDRLSRgglldrRRERALAEEYIKRLRIKTPSPEQPVGNLSGGNQQKVVLAKWLATDPKVL 416
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446491464 157 LMDEPfgaldpvTRG----ALQQemtrIHRLL------GRTIVLVTHDIDEALRLAEHLVLMDHGEVV 214
Cdd:COG1129 417 ILDEP-------TRGidvgAKAE----IYRLIrelaaeGKAVIVISSELPELLGLSDRILVMREGRIV 473
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
12-226 |
3.48e-22 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 94.59 E-value: 3.48e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 12 GAQKAVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMI------NRLVEHDsgEIRFAGEEIRSLPVLELRRRMGYAIQSI- 84
Cdd:COG4170 18 GRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAIcgitkdNWHVTAD--RFRWNGIDLLKLSPRERRKIIGREIAMIf 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 85 -----GLFPHWSV-AQNIATVPQLQK----WSRARidDRIDELMALL---GLESN--LRERYPHQLSGGQQQRVGVARAL 149
Cdd:COG4170 96 qepssCLDPSAKIgDQLIEAIPSWTFkgkwWQRFK--WRKKRAIELLhrvGIKDHkdIMNSYPHELTEGECQKVMIAMAI 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 150 AADPQVLLMDEPFGALDPVTRgalqqemTRIHRLLGR-------TIVLVTHDIDEALRLAEHLVLMDHGEVVQQGNPLTM 222
Cdd:COG4170 174 ANQPRLLIADEPTNAMESTTQ-------AQIFRLLARlnqlqgtSILLISHDLESISQWADTITVLYCGQTVESGPTEQI 246
|
....
gi 446491464 223 LTRP 226
Cdd:COG4170 247 LKSP 250
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
2-217 |
5.99e-22 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 90.45 E-value: 5.99e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 2 IEFSHVSKLFG--AQKAVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEIRSLPVlELRRRMGY 79
Cdd:cd03247 1 LSINNVSFSYPeqEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEK-ALSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 80 AIQSIGLFphwsvaqniatvpqlqkwsrariddridelmallglESNLRERYPHQLSGGQQQRVGVARALAADPQVLLMD 159
Cdd:cd03247 80 LNQRPYLF------------------------------------DTTLRNNLGRRFSGGERQRLALARILLQDAPIVLLD 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446491464 160 EPFGALDPVTRGALQQEMTRIhrLLGRTIVLVTHDIdEALRLAEHLVLMDHGEVVQQG 217
Cdd:cd03247 124 EPTVGLDPITERQLLSLIFEV--LKDKTLIWITHHL-TGIEHMDKILFLENGKIIMQG 178
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-232 |
2.50e-21 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 90.32 E-value: 2.50e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 1 MIEFSHVSKLFGAQKAVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEIRSLPVLELRRRmGYA 80
Cdd:PRK11614 5 MLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMRE-AVA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 81 IQSIG--LFPHWSVAQNIATVPQLQkwSRARIDDRIDELMALLGLESNLRERYPHQLSGGQQQRVGVARALAADPQVLLM 158
Cdd:PRK11614 84 IVPEGrrVFSRMTVEENLAMGGFFA--ERDQFQERIKWVYELFPRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446491464 159 DEPFGALDPVTrgaLQQEMTRIHRLL--GRTIVLVTHDIDEALRLAEHLVLMDHGEVVQQGNPLTMLtrpANDFVR 232
Cdd:PRK11614 162 DEPSLGLAPII---IQQIFDTIEQLReqGMTIFLVEQNANQALKLADRGYVLENGHVVLEDTGDALL---ANEAVR 231
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
20-218 |
4.71e-21 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 93.37 E-value: 4.71e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 20 LNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHdSGEIRFAGEEIRSLPVLELRRRMGYAIQSIGLFpHWSVAQNI--- 96
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPY-QGSLKINGIELRELDPESWRKHLSWVGQNPQLP-HGTLRDNVllg 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 97 ---ATVPQLQK-WSRARIDDRIDELMalLGLESNLRERyPHQLSGGQQQRVGVARALAADPQVLLMDEPFGALDPVTRGA 172
Cdd:PRK11174 447 npdASDEQLQQaLENAWVSEFLPLLP--QGLDTPIGDQ-AAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQL 523
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 446491464 173 LQQEMTRIHRllGRTIVLVTHDIDEaLRLAEHLVLMDHGEVVQQGN 218
Cdd:PRK11174 524 VMQALNAASR--RQTTLMVTHQLED-LAQWDQIWVMQDGQIVQQGD 566
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-218 |
5.63e-21 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 92.82 E-value: 5.63e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 4 FSHVSKLFGAQKAVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEirslpvlelrrRMGYAIQS 83
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGL-----------RIGYLPQE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 84 IGLFPHWSVAQNIATV----------------------PQLQKWSR--ARIDD--------RIDELMALLGLESNLRERY 131
Cdd:COG0488 70 PPLDDDLTVLDTVLDGdaelraleaeleeleaklaepdEDLERLAElqEEFEAlggweaeaRAEEILSGLGFPEEDLDRP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 132 PHQLSGGQQQRVGVARALAADPQVLLMDEPFGALDPVTRGALQQEmtrihrLLGR--TIVLVTHD---IDealRLAEHLV 206
Cdd:COG0488 150 VSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEF------LKNYpgTVLVVSHDryfLD---RVATRIL 220
|
250
....*....|...
gi 446491464 207 LMDHGEVVQ-QGN 218
Cdd:COG0488 221 ELDRGKLTLyPGN 233
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
16-282 |
5.64e-21 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 93.00 E-value: 5.64e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 16 AVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEI--RSLPVLELRRRMGYAIQSI--------- 84
Cdd:PRK10261 31 AVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLrrRSRQVIELSEQSAAQMRHVrgadmamif 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 85 -----GLFPHWSVAQNIATVPQL-QKWSR-------ARIDD--RIDELMALLGlesnlreRYPHQLSGGQQQRVGVARAL 149
Cdd:PRK10261 111 qepmtSLNPVFTVGEQIAESIRLhQGASReeamveaKRMLDqvRIPEAQTILS-------RYPHQLSGGMRQRVMIAMAL 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 150 AADPQVLLMDEPFGALDPVTRGALQQEMTRIHRLLGRTIVLVTHDIDEALRLAEHLVLMDHGEVVQQGNPLTMLTRPAND 229
Cdd:PRK10261 184 SCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQIFHAPQHP 263
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446491464 230 FVRQFFGR-SELGV-------RLLSLRSVADYVRREERAEGEALAEE---MTLRDALSLFVARG 282
Cdd:PRK10261 264 YTRALLAAvPQLGAmkgldypRRFPLISLEHPAKQEPPIEQDTVVDGepiLQVRNLVTRFPLRS 327
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
15-217 |
1.19e-20 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 90.19 E-value: 1.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 15 KAVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHD----SGEIRFAGEEIRSLPVLELRRRMGYAIQSI------ 84
Cdd:PRK11022 21 RAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDYPgrvmAEKLEFNGQDLQRISEKERRNLVGAEVAMIfqdpmt 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 85 GLFPHWSVA-QNIATVPQLQKWSRARIDDRIDELMALLGL---ESNLrERYPHQLSGGQQQRVGVARALAADPQVLLMDE 160
Cdd:PRK11022 101 SLNPCYTVGfQIMEAIKVHQGGNKKTRRQRAIDLLNQVGIpdpASRL-DVYPHQLSGGMSQRVMIAMAIACRPKLLIADE 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446491464 161 PFGALDPVTRGALQQEMTRIHRLLGRTIVLVTHDIDEALRLAEHLVLMDHGEVVQQG 217
Cdd:PRK11022 180 PTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETG 236
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
32-226 |
1.34e-20 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 88.45 E-value: 1.34e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 32 LIGTSGSGKSTTLKMINRLVEHdSGEIRFAGEEIRSLPVLELRRRMGYAIQSIGLFPHWSVAQNIAtVPQLQKWSRARID 111
Cdd:PRK03695 27 LVGPNGAGKSTLLARMAGLLPG-SGSIQFAGQPLEAWSAAELARHRAYLSQQQTPPFAMPVFQYLT-LHQPDKTRTEAVA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 112 DRIDELMALLGLESNLrERYPHQLSGGQQQRVGVA-------RALAADPQVLLMDEPFGALDPVTRGALQQEMTRIHRlL 184
Cdd:PRK03695 105 SALNEVAEALGLDDKL-GRSVNQLSGGEWQRVRLAavvlqvwPDINPAGQLLLLDEPMNSLDVAQQAALDRLLSELCQ-Q 182
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 446491464 185 GRTIVLVTHDIDEALRLAEHLVLMDHGEVVQQGNPLTMLTRP 226
Cdd:PRK03695 183 GIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVLTPE 224
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
17-232 |
4.29e-20 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 87.45 E-value: 4.29e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 17 VNDLNLNFQEGSFSVLIGTSGSGKSTT----LKMINRLVEHDSGEIRFAGEEIRSLpvlELRRRMgyaIQSIGLFPH--W 90
Cdd:PRK10418 19 VHGVSLTLQRGRVLALVGGSGSGKSLTcaaaLGILPAGVRQTAGRVLLDGKPVAPC---ALRGRK---IATIMQNPRsaF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 91 SVAQNIAT--VPQLQKWSRARIDDRIDELMALLGLESNLR--ERYPHQLSGGQQQRVGVARALAADPQVLLMDEPFGALD 166
Cdd:PRK10418 93 NPLHTMHThaRETCLALGKPADDATLTAALEAVGLENAARvlKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTTDLD 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446491464 167 PVTRGALQQEMTRIHRLLGRTIVLVTHDIDEALRLAEHLVLMDHGEVVQQGNPLTMLTRPANDFVR 232
Cdd:PRK10418 173 VVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPKHAVTR 238
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
2-219 |
4.48e-20 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 90.57 E-value: 4.48e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 2 IEFSHVSKLFGAQKAVNDLNLNFQEGS-FSVLiGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEIRSLPvLELRRRMGYA 80
Cdd:NF033858 267 IEARGLTMRFGDFTAVDHVSFRIRRGEiFGFL-GSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDAGD-IATRRRVGYM 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 81 IQSIGLFPHWSVAQNIATVPQLQKWSRARIDDRIDELMALLGLESNLRERyPHQLSGGQQQRVGVARALAADPQVLLMDE 160
Cdd:NF033858 345 SQAFSLYGELTVRQNLELHARLFHLPAAEIAARVAEMLERFDLADVADAL-PDSLPLGIRQRLSLAVAVIHKPELLILDE 423
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446491464 161 PFGALDPVTRGALQQEMTRIHRLLGRTIVLVTHDIDEALRlAEHLVLMDHGEVVQQGNP 219
Cdd:NF033858 424 PTSGVDPVARDMFWRLLIELSREDGVTIFISTHFMNEAER-CDRISLMHAGRVLASDTP 481
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
2-219 |
1.10e-19 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 85.62 E-value: 1.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 2 IEFSHVSKLF--GAQKAVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEIRSLPVLELRRRMGY 79
Cdd:cd03244 3 IEFKNVSLRYrpNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRISI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 80 AIQSIGLFPHwSVAQNIAtvPqLQKWS---------RARIDDRIDELmaLLGLESNLRERyPHQLSGGQQQRVGVARALA 150
Cdd:cd03244 83 IPQDPVLFSG-TIRSNLD--P-FGEYSdeelwqaleRVGLKEFVESL--PGGLDTVVEEG-GENLSVGQRQLLCLARALL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446491464 151 ADPQVLLMDEPFGALDPVTRgALQQEMTRiHRLLGRTIVLVTHDIDEALRLAEHLVlMDHGEVVQQGNP 219
Cdd:cd03244 156 RKSKILVLDEATASVDPETD-ALIQKTIR-EAFKDCTVLTIAHRLDTIIDSDRILV-LDKGRVVEFDSP 221
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
2-299 |
1.19e-19 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 89.09 E-value: 1.19e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 2 IEFSHVSKLFGAQKAVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRL--VEHDSGEIRF------------------- 60
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIYhvalcekcgyverpskvge 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 61 ----AGEEIRSLPV----------LELRRRMGYAIQ-SIGLFPHWSVAQN-IATVPQLQkwsrARIDDRIDELMALLGlE 124
Cdd:TIGR03269 81 pcpvCGGTLEPEEVdfwnlsdklrRRIRKRIAIMLQrTFALYGDDTVLDNvLEALEEIG----YEGKEAVGRAVDLIE-M 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 125 SNLRERYPH---QLSGGQQQRVGVARALAADPQVLLMDEPFGALDPVTRGALQQEMTRIHRLLGRTIVLVTHDIDEALRL 201
Cdd:TIGR03269 156 VQLSHRITHiarDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 202 AEHLVLMDHGEVVQQGNPLTMLTRpandFVRQF-----FGRSELGVRLLSLRSVADYVRREERAEGEALaeemtlrDALS 276
Cdd:TIGR03269 236 SDKAIWLENGEIKEEGTPDEVVAV----FMEGVsevekECEVEVGEPIIKVRNVSKRYISVDRGVVKAV-------DNVS 304
|
330 340
....*....|....*....|...
gi 446491464 277 LFVARGcEVLPVVNTQGQPSGTL 299
Cdd:TIGR03269 305 LEVKEG-EIFGIVGTSGAGKTTL 326
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-237 |
1.23e-19 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 88.83 E-value: 1.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 1 MIEFSHVSKLFGAQKAVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDS--GEIRFAGEEIRSLPVLELRRRmG 78
Cdd:PRK13549 5 LLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGTyeGEIIFEGEELQASNIRDTERA-G 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 79 YAI--QSIGLFPHWSVAQNIAtvpqL-QKWSRA-RIDD-----RIDELMALLGLESNLRERYPHqLSGGQQQRVGVARAL 149
Cdd:PRK13549 84 IAIihQELALVKELSVLENIF----LgNEITPGgIMDYdamylRAQKLLAQLKLDINPATPVGN-LGLGQQQLVEIAKAL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 150 AADPQVLLMDEPFGALdpvTRGALQQEMTRIHRLLGRTI--VLVTHDIDEALRLAEHLVLMDHGEvvqqgnplTMLTRPA 227
Cdd:PRK13549 159 NKQARLLILDEPTASL---TESETAVLLDIIRDLKAHGIacIYISHKLNEVKAISDTICVIRDGR--------HIGTRPA 227
|
250
....*....|....*
gi 446491464 228 -----NDFVRQFFGR 237
Cdd:PRK13549 228 agmteDDIITMMVGR 242
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
15-215 |
2.94e-19 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 87.92 E-value: 2.94e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 15 KAVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEIR-SLPVLELRRRMGYAIQS---IGLFPHW 90
Cdd:PRK09700 277 KKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISpRSPLDAVKKGMAYITESrrdNGFFPNF 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 91 SVAQNIATVPQLQK------W------SRARIDDRIDELMAL--LGLESNLREryphqLSGGQQQRVGVARALAADPQVL 156
Cdd:PRK09700 357 SIAQNMAISRSLKDggykgaMglfhevDEQRTAENQRELLALkcHSVNQNITE-----LSGGNQQKVLISKWLCCCPEVI 431
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446491464 157 LMDEPfgaldpvTRG---ALQQEMTRIHRLL---GRTIVLVTHDIDEALRLAEHLVLMDHGEVVQ 215
Cdd:PRK09700 432 IFDEP-------TRGidvGAKAEIYKVMRQLaddGKVILMVSSELPEIITVCDRIAVFCEGRLTQ 489
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
20-219 |
3.25e-19 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 85.44 E-value: 3.25e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 20 LNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEI----RSLpvLELRRRMGYAIQSIG--LFpHWSVA 93
Cdd:PRK13638 20 LNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLdyskRGL--LALRQQVATVFQDPEqqIF-YTDID 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 94 QNIATVPQLQKWSRARIDDRIDELMALLGLEsNLRERYPHQLSGGQQQRVGVARALAADPQVLLMDEPFGALDPVTRGal 173
Cdd:PRK13638 97 SDIAFSLRNLGVPEAEITRRVDEALTLVDAQ-HFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRT-- 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446491464 174 qQEMTRIHRLL--GRTIVLVTHDIDEALRLAEHLVLMDHGEVVQQGNP 219
Cdd:PRK13638 174 -QMIAIIRRIVaqGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAP 220
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1-214 |
4.91e-19 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 87.04 E-value: 4.91e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 1 MIEFSHVSKLFGAQKAVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFaGEEIRslpvlelrrrMGY- 79
Cdd:COG0488 315 VLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETVK----------IGYf 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 80 AIQSIGLFPHWSVAQNIatvpqlqkwSRARIDDRIDELMALLG--LESNLR-ERYPHQLSGGQQQRVGVARALAADPQVL 156
Cdd:COG0488 384 DQHQEELDPDKTVLDEL---------RDGAPGGTEQEVRGYLGrfLFSGDDaFKPVGVLSGGEKARLALAKLLLSPPNVL 454
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446491464 157 LMDEPFGALDPVTRGALQQemtrihrLLGR---TIVLVTHD---IDealRLAEHLVLMDHGEVV 214
Cdd:COG0488 455 LLDEPTNHLDIETLEALEE-------ALDDfpgTVLLVSHDryfLD---RVATRILEFEDGGVR 508
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
21-193 |
9.75e-19 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 82.61 E-value: 9.75e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 21 NLNF--QEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEIRSLPVLElrrRMGYAIQSIGLFPHWSVAQNiat 98
Cdd:PRK13539 20 GLSFtlAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAE---ACHYLGHRNAMKPALTVAEN--- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 99 vpqLQKWS--RARIDDRIDELMALLGLE--SNLRERYphqLSGGQQQRVGVARALAADPQVLLMDEPFGALDPVTRgALQ 174
Cdd:PRK13539 94 ---LEFWAafLGGEELDIAAALEAVGLAplAHLPFGY---LSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAV-ALF 166
|
170
....*....|....*....
gi 446491464 175 QEMTRIHRLLGRTIVLVTH 193
Cdd:PRK13539 167 AELIRAHLAQGGIVIAATH 185
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
19-213 |
2.12e-18 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 82.13 E-value: 2.12e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 19 DLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEIRSLPVLELRRRMGYAIQSIGLFPHwSVAQNIA- 97
Cdd:cd03248 32 DVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSKVSLVGQEPVLFAR-SLQDNIAy 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 98 ---TVPQ---LQKWSRARIDDRIDELMalLGLESNLRERyPHQLSGGQQQRVGVARALAADPQVLLMDEPFGALDPVTRG 171
Cdd:cd03248 111 glqSCSFecvKEAAQKAHAHSFISELA--SGYDTEVGEK-GSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAESEQ 187
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 446491464 172 ALQQEMTRIHRllGRTIVLVTHDIDEALRlAEHLVLMDHGEV 213
Cdd:cd03248 188 QVQQALYDWPE--RRTVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1-237 |
2.96e-18 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 84.88 E-value: 2.96e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 1 MIEFSHVSKLFGAQKAVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDS--GEIRFAGEEIRSLPVLELRRRmG 78
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTwdGEIYWSGSPLKASNIRDTERA-G 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 79 YAI--QSIGLFPHWSVAQNIATVPQLQKwSRARIDD-----RIDELMALLGLESNLRERYPHQLSGGQQQRVGVARALAA 151
Cdd:TIGR02633 80 IVIihQELTLVPELSVAENIFLGNEITL-PGGRMAYnamylRAKNLLRELQLDADNVTRPVGDYGGGQQQLVEIAKALNK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 152 DPQVLLMDEPFGALdpvTRGALQQEMTRIHRLLGRTI--VLVTHDIDEALRLAEHLVLMDHGEVVQQGNPLTMLTrpaND 229
Cdd:TIGR02633 159 QARLLILDEPSSSL---TEKETEILLDIIRDLKAHGVacVYISHKLNEVKAVCDTICVIRDGQHVATKDMSTMSE---DD 232
|
....*...
gi 446491464 230 FVRQFFGR 237
Cdd:TIGR02633 233 IITMMVGR 240
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1-219 |
4.06e-18 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 81.96 E-value: 4.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 1 MIEFSHVSKLFGAQKAVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEIRSLPVLELRRrMGY- 79
Cdd:PRK11300 5 LLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIAR-MGVv 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 80 -AIQSIGLFPHWSVAQN--IATVPQLQK-----------WSRARID--DRIDELMALLGLESnLRERYPHQLSGGQQQRV 143
Cdd:PRK11300 84 rTFQHVRLFREMTVIENllVAQHQQLKTglfsgllktpaFRRAESEalDRAATWLERVGLLE-HANRQAGNLAYGQQRRL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446491464 144 GVARALAADPQVLLMDEPFGALDPVTRGALQQEMTRIHRLLGRTIVLVTHDIDEALRLAEHLVLMDHGEVVQQGNP 219
Cdd:PRK11300 163 EIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTP 238
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-257 |
5.34e-18 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 84.07 E-value: 5.34e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 1 MIEFSHVSKLFGAQKAVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEIRSL-PVLELRRRMGY 79
Cdd:PRK09700 5 YISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLdHKLAAQLGIGI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 80 AIQSIGLFPHWSVAQNIATVPQLQK---------WSRARIddRIDELMALLGLESNLRERYPhQLSGGQQQRVGVARALA 150
Cdd:PRK09700 85 IYQELSVIDELTVLENLYIGRHLTKkvcgvniidWREMRV--RAAMMLLRVGLKVDLDEKVA-NLSISHKQMLEIAKTLM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 151 ADPQVLLMDEPFGALdpvTRGALQQEMTRIHRLL--GRTIVLVTHDIDEALRLAEHLVLMDHGEVVQQGnpltMLTRPAN 228
Cdd:PRK09700 162 LDAKVIIMDEPTSSL---TNKEVDYLFLIMNQLRkeGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSG----MVSDVSN 234
|
250 260 270
....*....|....*....|....*....|
gi 446491464 229 -DFVRQFFGRsELGVRLLSLRSVADYVRRE 257
Cdd:PRK09700 235 dDIVRLMVGR-ELQNRFNAMKENVSNLAHE 263
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
12-238 |
1.48e-17 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 81.77 E-value: 1.48e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 12 GAQKAVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMI------NRLVEHDsgEIRFAGEEIRSLPVLELRRRMGYAIQSI- 84
Cdd:PRK15093 18 GWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAIcgvtkdNWRVTAD--RMRFDDIDLLRLSPRERRKLVGHNVSMIf 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 85 -----GLFPHWSVA-QNIATVP---------QLQKWsRARiddRIDELMALLGLES--NLRERYPHQLSGGQQQRVGVAR 147
Cdd:PRK15093 96 qepqsCLDPSERVGrQLMQNIPgwtykgrwwQRFGW-RKR---RAIELLHRVGIKDhkDAMRSFPYELTEGECQKVMIAI 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 148 ALAADPQVLLMDEPFGALDPVTRGALQQEMTRIHRLLGRTIVLVTHDIDEALRLAEHLVLMDHGEVVQQGNPLTMLTRPA 227
Cdd:PRK15093 172 ALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTVETAPSKELVTTPH 251
|
250
....*....|....*..
gi 446491464 228 NDFVRQF------FGRS 238
Cdd:PRK15093 252 HPYTQALiraipdFGSA 268
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-216 |
1.56e-17 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 80.16 E-value: 1.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 1 MIEFSHVSKLFGAQKAVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGeeirslpvlelRRRMGYA 80
Cdd:PRK09544 4 LVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNG-----------KLRIGYV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 81 IQSIGLFPhwsvaqniaTVP-QLQKWSRARIDDRIDELM-ALLGLESNLRERYPHQ-LSGGQQQRVGVARALAADPQVLL 157
Cdd:PRK09544 73 PQKLYLDT---------TLPlTVNRFLRLRPGTKKEDILpALKRVQAGHLIDAPMQkLSGGETQRVLLARALLNRPQLLV 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446491464 158 MDEPFGALDPVTRGALQQEMTRIHRLLGRTIVLVTHDI-------DEALRLAEHLVLMDHGEVVQQ 216
Cdd:PRK09544 144 LDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLhlvmaktDEVLCLNHHICCSGTPEVVSL 209
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
17-193 |
2.06e-17 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 82.55 E-value: 2.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 17 VNDLNLNFQEGSfSVLI-GTSGSGKSTTLKMINRLVEHDSGEIRF-AGEEI-----RS-LPVLELRRrmgyAIqsigLFP 88
Cdd:COG4178 379 LEDLSLSLKPGE-RLLItGPSGSGKSTLLRAIAGLWPYGSGRIARpAGARVlflpqRPyLPLGTLRE----AL----LYP 449
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 89 HwsvaqniatvpqlqkwSRARIDD-RIDELMALLGLEsNLRERY------PHQLSGGQQQRVGVARALAADPQVLLMDEP 161
Cdd:COG4178 450 A----------------TAEAFSDaELREALEAVGLG-HLAERLdeeadwDQVLSLGEQQRLAFARLLLHKPDWLFLDEA 512
|
170 180 190
....*....|....*....|....*....|..
gi 446491464 162 FGALDPVTRGALQQEMtrIHRLLGRTIVLVTH 193
Cdd:COG4178 513 TSALDEENEAALYQLL--REELPGTTVISVGH 542
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
12-193 |
2.15e-17 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 78.55 E-value: 2.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 12 GAQKAVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEIRSLPVlELRRRMGYAIQSIGLFPHWS 91
Cdd:TIGR01189 11 GERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRD-EPHENILYLGHLPGLKPELS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 92 VAQNiatvpqLQKWSR--ARIDDRIDELMALLGLeSNLRERYPHQLSGGQQQRVGVARALAADPQVLLMDEPFGALDPVT 169
Cdd:TIGR01189 90 ALEN------LHFWAAihGGAQRTIEDALAAVGL-TGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAG 162
|
170 180
....*....|....*....|....
gi 446491464 170 RGALQQEMtRIHRLLGRTIVLVTH 193
Cdd:TIGR01189 163 VALLAGLL-RAHLARGGIVLLTTH 185
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
34-214 |
4.71e-17 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 81.23 E-value: 4.71e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 34 GTSGSGKSTTLKMINRLVEHDSGEIRFAGEEIRSLPVLELRRR-MGYaI----QSIGLFPHWSVAQNIA----TVPQLQK 104
Cdd:COG3845 291 GVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLgVAY-IpedrLGRGLVPDMSVAENLIlgryRRPPFSR 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 105 W---SRARIDDRIDELMAllglESNLRERYPHQ----LSGGQQQRVGVARALAADPQVLLMDEPFGALDPvtrGALQQem 177
Cdd:COG3845 370 GgflDRKAIRAFAEELIE----EFDVRTPGPDTparsLSGGNQQKVILARELSRDPKLLIAAQPTRGLDV---GAIEF-- 440
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 446491464 178 trIHRLL------GRTIVLVTHDIDEALRLAEHLVLMDHGEVV 214
Cdd:COG3845 441 --IHQRLlelrdaGAAVLLISEDLDEILALSDRIAVMYEGRIV 481
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
2-212 |
5.41e-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: 76.33 E-value: 5.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 2 IEFSHVSKLFGAQKAVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIrfageeirslpvlelrrrmgyai 81
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIV----------------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 82 qsiglfpHWSVAQNIATVPQLqkwsrariddridelmallglesnlreryphqlSGGQQQRVGVARALAADPQVLLMDEP 161
Cdd:cd03221 58 -------TWGSTVKIGYFEQL---------------------------------SGGEKMRLALAKLLLENPNLLLLDEP 97
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446491464 162 FGALDPVTRGALQQEMTRIHrllgRTIVLVTHD---IDealRLAEHLVLMDHGE 212
Cdd:cd03221 98 TNHLDLESIEALEEALKEYP----GTVILVSHDryfLD---QVATKIIELEDGK 144
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
16-236 |
8.88e-17 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 78.39 E-value: 8.88e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 16 AVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEIRSlpvlELRRRM-GYAIQSIGLfpHWSVAQ 94
Cdd:PRK15056 22 ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQ----ALQKNLvAYVPQSEEV--DWSFPV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 95 NIATVPQLQKWS------RARIDDR--IDELMALLGLeSNLRERYPHQLSGGQQQRVGVARALAADPQVLLMDEPFGALD 166
Cdd:PRK15056 96 LVEDVVMMGRYGhmgwlrRAKKRDRqiVTAALARVDM-VEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVD 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 167 PVTRGALqQEMTRIHRLLGRTIVLVTHDIDEALRLAEHLVlMDHGEVVQQGNPLTMLTrpANDFVRQFFG 236
Cdd:PRK15056 175 VKTEARI-ISLLRELRDEGKTMLVSTHNLGSVTEFCDYTV-MVKGTVLASGPTETTFT--AENLELAFSG 240
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
7-215 |
9.50e-17 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 77.31 E-value: 9.50e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 7 VSKLFGA------QKAVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVE--HDSGEIRFAGEEI-RSLPVLElrrrm 77
Cdd:COG2401 30 VLEAFGVelrvveRYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKgtPVAGCVDVPDNQFgREASLID----- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 78 gyaiqsiGLFPHWSVAQNIatvpqlqkwsrariddridELMALLGLESN--LRERYPHqLSGGQQQRVGVARALAADPQV 155
Cdd:COG2401 105 -------AIGRKGDFKDAV-------------------ELLNAVGLSDAvlWLRRFKE-LSTGQKFRFRLALLLAERPKL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446491464 156 LLMDEPFGALDPVTRGALQQEMTRIHRLLGRTIVLVTH--DIDEALRlAEHLVLMDHGEVVQ 215
Cdd:COG2401 158 LVIDEFCSHLDRQTAKRVARNLQKLARRAGITLVVATHhyDVIDDLQ-PDLLIFVGYGGVPE 218
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1-217 |
2.03e-16 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 79.32 E-value: 2.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 1 MIEFSHVSKLFGAQKAVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEIRSL-PVLElrRRMG- 78
Cdd:PRK15439 11 LLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLtPAKA--HQLGi 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 79 YAI-QSIGLFPHWSVAQNIATvpQLQKwsRARIDDRIDELMALLGLESNLrERYPHQLSGGQQQRVGVARALAADPQVLL 157
Cdd:PRK15439 89 YLVpQEPLLFPNLSVKENILF--GLPK--RQASMQKMKQLLAALGCQLDL-DSSAGSLEVADRQIVEILRGLMRDSRILI 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446491464 158 MDEPFGALDPVTRGALqqeMTRIHRLL--GRTIVLVTHDIDEALRLAEHLVLMDHGEVVQQG 217
Cdd:PRK15439 164 LDEPTASLTPAETERL---FSRIRELLaqGVGIVFISHKLPEIRQLADRISVMRDGTIALSG 222
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
2-225 |
4.43e-16 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 78.63 E-value: 4.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 2 IEFSHVSKLFGAQKAVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMIN--RLVEhdSGEIRFAGEEIRSLpvlELRRRMGY 79
Cdd:NF033858 2 ARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAgaRKIQ--QGRVEVLGGDMADA---RHRRAVCP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 80 AI----QSIG--LFPHWSVAQNIATVPQLQKWSRARIDDRIDELMALLGLESnLRERYPHQLSGGQQQRVGVARALAADP 153
Cdd:NF033858 77 RIaympQGLGknLYPTLSVFENLDFFGRLFGQDAAERRRRIDELLRATGLAP-FADRPAGKLSGGMKQKLGLCCALIHDP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446491464 154 QVLLMDEPFGALDPVTRGALQQEMTRIHRLLGRTIVLV-THDIDEALRLaEHLVLMDHGEVVQQGNPLTMLTR 225
Cdd:NF033858 156 DLLILDEPTTGVDPLSRRQFWELIDRIRAERPGMSVLVaTAYMEEAERF-DWLVAMDAGRVLATGTPAELLAR 227
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
1-268 |
9.41e-16 |
|
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: 78.03 E-value: 9.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 1 MIEFSHVSKLF--GAQKAVNDLNLNFQEG--------SFSV-------LIGTSGSGKSTTLKMINRLVEHDsGEIRFAGE 63
Cdd:TIGR01271 1202 VIENPHAQKCWpsGGQMDVQGLTAKYTEAgravlqdlSFSVeggqrvgLLGRTGSGKSTLLSALLRLLSTE-GEIQIDGV 1280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 64 EIRSLPVLELRRRMGYAIQSIGLFPHwSVAQNIATVPQlqkWSrariDDRIDELMALLGLESNLrERYPHQL-------- 135
Cdd:TIGR01271 1281 SWNSVTLQTWRKAFGVIPQKVFIFSG-TFRKNLDPYEQ---WS----DEEIWKVAEEVGLKSVI-EQFPDKLdfvlvdgg 1351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 136 ---SGGQQQRVGVARALAADPQVLLMDEPFGALDPVTRGALQQemTRIHRLLGRTIVLVTHDIDEALRLAEHLVLmdHGE 212
Cdd:TIGR01271 1352 yvlSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRK--TLKQSFSNCTVILSEHRVEALLECQQFLVI--EGS 1427
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 446491464 213 VVQQGNPLTMLTRPANDFvRQFFGRSELgVRLLSLRSVaDYVRREERAEGEALAEE 268
Cdd:TIGR01271 1428 SVKQYDSIQKLLNETSLF-KQAMSAADR-LKLFPLHRR-NSSKRKPQPKITALREE 1480
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
28-219 |
1.21e-15 |
|
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: 73.99 E-value: 1.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 28 SFSV-------LIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEIRSLPVLELRRRMGYAIQSIGLFphwsvaqnIATVp 100
Cdd:cd03369 28 SFKVkagekigIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSSLTIIPQDPTLF--------SGTI- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 101 qlqkwsRARID--DRID--ELMALLGL-ESNLreryphQLSGGQQQRVGVARALAADPQVLLMDEPFGALDPVTRGALQQ 175
Cdd:cd03369 99 ------RSNLDpfDEYSdeEIYGALRVsEGGL------NLSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDALIQK 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 446491464 176 EmtrIHRLL-GRTIVLVTHDIDEALRLAEHLVlMDHGEVVQQGNP 219
Cdd:cd03369 167 T---IREEFtNSTILTIAHRLRTIIDYDKILV-MDAGEVKEYDHP 207
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
2-218 |
5.57e-15 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 75.14 E-value: 5.57e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 2 IEFSHVSKLFGAQKAV-NDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEIRSLPVLELRRRMGYA 80
Cdd:PRK10790 341 IDIDNVSFAYRDDNLVlQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMV 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 81 IQ-----------SIGLFPHWS---VAQNIATVpQLQKWSRARIDdridelmallGLESNLRERyPHQLSGGQQQRVGVA 146
Cdd:PRK10790 421 QQdpvvladtflaNVTLGRDISeeqVWQALETV-QLAELARSLPD----------GLYTPLGEQ-GNNLSVGQKQLLALA 488
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446491464 147 RALAADPQVLLMDEPFGALDPVTRGALQQEMTRIHRllGRTIVLVTHdidealRL-----AEHLVLMDHGEVVQQGN 218
Cdd:PRK10790 489 RVLVQTPQILILDEATANIDSGTEQAIQQALAAVRE--HTTLVVIAH------RLstiveADTILVLHRGQAVEQGT 557
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
1-224 |
1.78e-14 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 72.17 E-value: 1.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 1 MIEFSHVSKLFGAQKAVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMI-NRLVEHD-------SGEIRFAGEEIRSLPVLE 72
Cdd:PRK13547 1 MLTADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALaGDLTGGGaprgarvTGDVTLNGEPLAAIDAPR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 73 L-RRRMGYAIQSIGLFPhWSVAQ--NIATVPQLQKWSRARIDDR--IDELMALLGLESnLRERYPHQLSGGQQQRVGVAR 147
Cdd:PRK13547 81 LaRLRAVLPQAAQPAFA-FSAREivLLGRYPHARRAGALTHRDGeiAWQALALAGATA-LVGRDVTTLSGGELARVQFAR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 148 ALA---------ADPQVLLMDEPFGALDPVTRGALQQEMTRIHRLLGRTIVLVTHDIDEALRLAEHLVLMDHGEVVQQGN 218
Cdd:PRK13547 159 VLAqlwpphdaaQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGA 238
|
....*.
gi 446491464 219 PLTMLT 224
Cdd:PRK13547 239 PADVLT 244
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
19-217 |
2.02e-14 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 74.04 E-value: 2.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 19 DLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIrfageeirslpvlelrrrmgyaiqsiglfphWSvAQNIAT 98
Cdd:PTZ00243 678 DVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV-------------------------------WA-ERSIAY 725
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 99 VPQlQKW----------------SRARIDD--RIDELMALL-----GLESNLRERYPHqLSGGQQQRVGVARALAADPQV 155
Cdd:PTZ00243 726 VPQ-QAWimnatvrgnilffdeeDAARLADavRVSQLEADLaqlggGLETEIGEKGVN-LSGGQKARVSLARAVYANRDV 803
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446491464 156 LLMDEPFGALDPVTrGALQQEMTRIHRLLGRTIVLVTHDIdEALRLAEHLVLMDHGEVVQQG 217
Cdd:PTZ00243 804 YLLDDPLSALDAHV-GERVVEECFLGALAGKTRVLATHQV-HVVPRADYVVALGDGRVEFSG 863
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
20-193 |
2.95e-14 |
|
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: 70.21 E-value: 2.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 20 LNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEIRSLPVlELRRRMGYAIQSIGLFPHWSVAQNiatv 99
Cdd:cd03231 19 LSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRD-SIARGLLYLGHAPGIKTTLSVLEN---- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 100 pqLQKWSRARIDDRIDELMALLGLeSNLRERYPHQLSGGQQQRVGVARALAADPQVLLMDEPFGALDPVTRGALQQEMtR 179
Cdd:cd03231 94 --LRFWHADHSDEQVEEALARVGL-NGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEAM-A 169
|
170
....*....|....
gi 446491464 180 IHRLLGRTIVLVTH 193
Cdd:cd03231 170 GHCARGGMVVLTTH 183
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
3-238 |
3.56e-14 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 72.64 E-value: 3.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 3 EFSHVSKLFGAQKAVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEIR---SLPVLElrrrMGY 79
Cdd:PRK11288 6 SFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRfasTTAALA----AGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 80 AI--QSIGLFPHWSVAQNI--ATVP---------QLQKWSR---ARIDDRIDElmallglESNLREryphqLSGGQQQRV 143
Cdd:PRK11288 82 AIiyQELHLVPEMTVAENLylGQLPhkggivnrrLLNYEAReqlEHLGVDIDP-------DTPLKY-----LSIGQRQMV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 144 GVARALAADPQVLLMDEPFGALDpvtrgalQQEMTRIHRLL------GRTIVLVTHDIDEALRLAEHLVLMDHGEVVQQG 217
Cdd:PRK11288 150 EIAKALARNARVIAFDEPTSSLS-------AREIEQLFRVIrelraeGRVILYVSHRMEEIFALCDAITVFKDGRYVATF 222
|
250 260
....*....|....*....|.
gi 446491464 218 NPLTMLTRpaNDFVRQFFGRS 238
Cdd:PRK11288 223 DDMAQVDR--DQLVQAMVGRE 241
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1-197 |
3.87e-14 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 72.34 E-value: 3.87e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 1 MIEFSHVSKLFGAQKAVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEIR-SLPvlELRRRMGY 79
Cdd:PRK10762 4 LLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTfNGP--KSSQEAGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 80 AI--QSIGLFPHWSVAQNIATVPQL-QKWSR---ARIDDRIDELMALLGLESNLRERYpHQLSGGQQQRVGVARALAADP 153
Cdd:PRK10762 82 GIihQELNLIPQLTIAENIFLGREFvNRFGRidwKKMYAEADKLLARLNLRFSSDKLV-GELSIGEQQMVEIAKVLSFES 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 446491464 154 QVLLMDEPFGALDPVTRGALqqeMTRIHRLL--GRTIVLVTHDIDE 197
Cdd:PRK10762 161 KVIIMDEPTDALTDTETESL---FRVIRELKsqGRGIVYISHRLKE 203
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1-211 |
6.14e-14 |
|
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: 72.35 E-value: 6.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 1 MIEFSHVSKLFG--AQKAVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEIRSlPVLELRRRMG 78
Cdd:TIGR01257 1937 ILRLNELTKVYSgtSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT-NISDVHQNMG 2015
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 79 YAIQSIGLFPHWSVAQNIATVPQLQKWSRARIDDRIDELMALLGLeSNLRERYPHQLSGGQQQRVGVARALAADPQVLLM 158
Cdd:TIGR01257 2016 YCPQFDAIDDLLTGREHLYLYARLRGVPAEEIEKVANWSIQSLGL-SLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLL 2094
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446491464 159 DEPFGALDPVTRGALQQEMTRIHRlLGRTIVLVTHDIDEALRLAEHLVLMDHG 211
Cdd:TIGR01257 2095 DEPTTGMDPQARRMLWNTIVSIIR-EGRAVVLTSHSMEECEALCTRLAIMVKG 2146
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
14-268 |
8.54e-14 |
|
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: 70.27 E-value: 8.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 14 QKAVNDLNLNFQEG--------SFSV-------LIGTSGSGKSTTLKMINRLVEHDsGEIRFAGEEIRSLPVLELRRRMG 78
Cdd:cd03289 2 QMTVKDLTAKYTEGgnavleniSFSIspgqrvgLLGRTGSGKSTLLSAFLRLLNTE-GDIQIDGVSWNSVPLQKWRKAFG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 79 YAIQSIGLFPHwSVAQNIatvPQLQKWSrariDDRIDELMALLGLESNLrERYPHQL-----------SGGQQQRVGVAR 147
Cdd:cd03289 81 VIPQKVFIFSG-TFRKNL---DPYGKWS----DEEIWKVAEEVGLKSVI-EQFPGQLdfvlvdggcvlSHGHKQLMCLAR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 148 ALAADPQVLLMDEPFGALDPVTRGALQQemTRIHRLLGRTIVLVTHDIdEALRLAEHLVLMDHGEVVQQGNPLTMLTRPA 227
Cdd:cd03289 152 SVLSKAKILLLDEPSAHLDPITYQVIRK--TLKQAFADCTVILSEHRI-EAMLECQRFLVIEENKVRQYDSIQKLLNEKS 228
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 446491464 228 ndFVRQFFGRSElGVRLLSLRSvADYVRREERAEGEALAEE 268
Cdd:cd03289 229 --HFKQAISPSD-RLKLFPRRN-SSKSKRKPRPQIQALQEE 265
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
18-219 |
1.11e-13 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 69.33 E-value: 1.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 18 NDLNLNFQEGSFSVLIGTSGSGKSTTLKMI--NRLVEHDSGEIRFAGEEIRSLPVLElRRRMG--YAIQSIGLFPHWSVA 93
Cdd:COG0396 17 KGVNLTIKPGEVHAIMGPNGSGKSTLAKVLmgHPKYEVTSGSILLDGEDILELSPDE-RARAGifLAFQYPVEIPGVSVS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 94 ---QNIATVPQLQKWSRARIDDRIDELMALLGLESNLRERYPHQ-LSGGQQQRVGVARALAADPQVLLMDEP-FG----A 164
Cdd:COG0396 96 nflRTALNARRGEELSAREFLKLLKEKMKELGLDEDFLDRYVNEgFSGGEKKRNEILQMLLLEPKLAILDETdSGldidA 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446491464 165 LDPVTRG--ALQQEmtrihrllGRTIVLVTHdideALRLAEHL------VLMDhGEVVQQGNP 219
Cdd:COG0396 176 LRIVAEGvnKLRSP--------DRGILIITH----YQRILDYIkpdfvhVLVD-GRIVKSGGK 225
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
2-205 |
1.15e-13 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 71.12 E-value: 1.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 2 IEFSHVSKLFGAQKAVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFaGEEIrslpvlelrrRMGYAI 81
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETV----------KLAYVD 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 82 QS-IGLFPHWSVAQNIA------TVPQLQKWSRARIddridelmALLGLESNLRERYPHQLSGGQQQRVGVARALAADPQ 154
Cdd:TIGR03719 392 QSrDALDPNKTVWEEISggldiiKLGKREIPSRAYV--------GRFNFKGSDQQKKVGQLSGGERNRVHLAKTLKSGGN 463
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446491464 155 VLLMDEPFGALDPVTRGALQQEMTRihrlLGRTIVLVTHD---IDealRLAEHL 205
Cdd:TIGR03719 464 VLLLDEPTNDLDVETLRALEEALLN----FAGCAVVISHDrwfLD---RIATHI 510
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
2-217 |
1.17e-13 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 70.53 E-value: 1.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 2 IEFSHVSKLFGAQKAVNDLNLNFQEGSFSVLIGTSGSGKSTTlKMINRLVEHDSGE--IRFAG--EEIRSLpvlelRRRM 77
Cdd:NF000106 14 VEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RG-ALPAHV*GPDAGRrpWRF*TwcANRRAL-----RRTI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 78 G-YAIQSIGLFPHWSVAQNIATVPQLQKWSRARIDDRIDELMALLGLeSNLRERYPHQLSGGQQQRVGVARALAADPQVL 156
Cdd:NF000106 88 G*HRPVR*GRRESFSGRENLYMIGR*LDLSRKDARARADELLERFSL-TEAAGRAAAKYSGGMRRRLDLAASMIGRPAVL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446491464 157 LMDEPFGALDPVTRGALQQEMTRIHRlLGRTIVLVTHDIDEALRLAEHLVLMDHGEVVQQG 217
Cdd:NF000106 167 YLDEPTTGLDPRTRNEVWDEVRSMVR-DGATVLLTTQYMEEAEQLAHELTVIDRGRVIADG 226
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
15-230 |
3.07e-13 |
|
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: 68.20 E-value: 3.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 15 KAVNDLNLNFQEGSFS-----VLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEIrslpvlelrrrmGYAIQSIG---- 85
Cdd:cd03237 8 KTLGEFTLEVEGGSISeseviGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTV------------SYKPQYIKadye 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 86 ------LFphwSVAQNIATVPQLQKwsrariddridELMALLGLESnLRERYPHQLSGGQQQRVGVARALAADPQVLLMD 159
Cdd:cd03237 76 gtvrdlLS---SITKDFYTHPYFKT-----------EIAKPLQIEQ-ILDREVPELSGGELQRVAIAACLSKDADIYLLD 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446491464 160 EPFGALDPVTRGALQQEMTRIHRLLGRTIVLVTHDIDEALRLAEHLVLMDhGE--VVQQGNPLTMLTRPANDF 230
Cdd:cd03237 141 EPSAYLDVEQRLMASKVIRRFAENNEKTAFVVEHDIIMIDYLADRLIVFE-GEpsVNGVANPPQSLRSGMNRF 212
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
1-165 |
3.94e-13 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 69.43 E-value: 3.94e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 1 MIEFSHVSKLFGAQKAVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDS--GEIRFAGEE-----IRSlpvlel 73
Cdd:NF040905 1 ILEMRGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGSyeGEILFDGEVcrfkdIRD------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 74 RRRMGYAI--QSIGLFPHWSVAQNIATVPQLQK-----WSRARIddRIDELMALLGLESNlreryPHQLSG----GQQQR 142
Cdd:NF040905 75 SEALGIVIihQELALIPYLSIAENIFLGNERAKrgvidWNETNR--RARELLAKVGLDES-----PDTLVTdigvGKQQL 147
|
170 180
....*....|....*....|...
gi 446491464 143 VGVARALAADPQVLLMDEPFGAL 165
Cdd:NF040905 148 VEIAKALSKDVKLLILDEPTAAL 170
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
14-193 |
3.94e-13 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 66.90 E-value: 3.94e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 14 QKAVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEIRSlPVLELRRRMGYAIQSIGLFPHWSVA 93
Cdd:PRK13540 14 QPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKK-DLCTYQKQLCFVGHRSGINPYLTLR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 94 QNIatvpqLQKWSRARIDDRIDELMALLGLESNLreRYP-HQLSGGQQQRVGVARALAADPQVLLMDEPFGALDPVtrgA 172
Cdd:PRK13540 93 ENC-----LYDIHFSPGAVGITELCRLFSLEHLI--DYPcGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDEL---S 162
|
170 180
....*....|....*....|...
gi 446491464 173 LQQEMTRI--HRLLGRTIVLVTH 193
Cdd:PRK13540 163 LLTIITKIqeHRAKGGAVLLTSH 185
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
2-193 |
4.78e-13 |
|
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: 66.02 E-value: 4.78e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 2 IEFSHVSKLFGAQKA-VNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEirslpvlelrrrmgya 80
Cdd:cd03223 1 IELENLSLATPDGRVlLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEGE---------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 81 iqsiglfphwsvaqNIATVPQLQKWSRAriddridelmallglesNLRE--RYP--HQLSGGQQQRVGVARALAADPQVL 156
Cdd:cd03223 65 --------------DLLFLPQRPYLPLG-----------------TLREqlIYPwdDVLSGGEQQRLAFARLLLHKPKFV 113
|
170 180 190
....*....|....*....|....*....|....*..
gi 446491464 157 LMDEPFGALDPvtrgALQQEMTRIHRLLGRTIVLVTH 193
Cdd:cd03223 114 FLDEATSALDE----ESEDRLYQLLKELGITVISVGH 146
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
17-211 |
5.72e-13 |
|
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: 66.97 E-value: 5.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 17 VNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEIRSLPVLELRRR----MGYAIQSIGLFpHWSV 92
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRnrysVAYAAQKPWLL-NATV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 93 AQNIATVPQLQKWSRARIDDR------IDELMalLGLESNLRERYPHqLSGGQQQRVGVARALAADPQVLLMDEPFGALD 166
Cdd:cd03290 96 EENITFGSPFNKQRYKAVTDAcslqpdIDLLP--FGDQTEIGERGIN-LSGGQRQRICVARALYQNTNIVFLDDPFSALD 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 446491464 167 PVTRGALQQE-MTRIHRLLGRTIVLVTHDIdEALRLAEHLVLMDHG 211
Cdd:cd03290 173 IHLSDHLMQEgILKFLQDDKRTLVLVTHKL-QYLPHADWIIAMKDG 217
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
2-212 |
1.91e-12 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 67.30 E-value: 1.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 2 IEFSHVSKLFGAQK-AVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEIRSLPVLELRRRMGYA 80
Cdd:PRK10522 323 LELRNVTFAYQDNGfSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFSAV 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 81 IQSIGLFPHWSVAQNIATVPQL-QKWsrariddridelMALLGLESNLRERYPH----QLSGGQQQRVGVARALAADPQV 155
Cdd:PRK10522 403 FTDFHLFDQLLGPEGKPANPALvEKW------------LERLKMAHKLELEDGRisnlKLSKGQKKRLALLLALAEERDI 470
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446491464 156 LLMDEPFGALDPVTRGALQQEMTRIHRLLGRTIVLVTHDiDEALRLAEHLVLMDHGE 212
Cdd:PRK10522 471 LLLDEWAADQDPHFRREFYQVLLPLLQEMGKTIFAISHD-DHYFIHADRLLEMRNGQ 526
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
24-219 |
5.53e-12 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 66.22 E-value: 5.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 24 FQEGSFSVLIGTSGSGKSTTLKMINRLVEHD---SGEIRFAGEEIRSLpvlELRRRMGYAIQSIGLFPHWSVAQNI---- 96
Cdd:TIGR00955 48 AKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGMPIDAK---EMRAISAYVQQDDLFIPTLTVREHLmfqa 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 97 -----ATVPQLQKwsRARIDDRIDELmallGLES--NLRERYPHQ---LSGGQQQRVGVARALAADPQVLLMDEPFGALD 166
Cdd:TIGR00955 125 hlrmpRRVTKKEK--RERVDEVLQAL----GLRKcaNTRIGVPGRvkgLSGGERKRLAFASELLTDPPLLFCDEPTSGLD 198
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446491464 167 PVTRGALQQEMTRIhRLLGRTIVLVTHD-IDEALRLAEHLVLMDHGEVVQQGNP 219
Cdd:TIGR00955 199 SFMAYSVVQVLKGL-AQKGKTIICTIHQpSSELFELFDKIILMAEGRVAYLGSP 251
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
19-213 |
5.71e-12 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 65.84 E-value: 5.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 19 DLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEIRSLPVLE-LRRRMGYAI---QSIGLFPHWSVAQ 94
Cdd:PRK15439 281 NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQrLARGLVYLPedrQSSGLYLDAPLAW 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 95 NIA--TVPQLQKWSRARIDDRIDE-LMALLGLESNLRERYPHQLSGGQQQRVGVARALAADPQVLLMDEPfgaldpvTRG 171
Cdd:PRK15439 361 NVCalTHNRRGFWIKPARENAVLErYRRALNIKFNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEP-------TRG 433
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446491464 172 ALQQEMTRIHRLL------GRTIVLVTHDIDEALRLAEHLVLMDHGEV 213
Cdd:PRK15439 434 VDVSARNDIYQLIrsiaaqNVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
32-232 |
7.94e-12 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 66.15 E-value: 7.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 32 LIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEIRSLPVLELRRRMGYAIQSIGLFPHwSVAQNIATVPQLQK---WS-- 106
Cdd:PLN03232 1267 VVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSG-TVRFNIDPFSEHNDadlWEal 1345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 107 -RARIDDRIDElmALLGLESNLRERyPHQLSGGQQQRVGVARALAADPQVLLMDEPFGALDpVTRGALQQEMTRiHRLLG 185
Cdd:PLN03232 1346 eRAHIKDVIDR--NPFGLDAEVSEG-GENFSVGQRQLLSLARALLRRSKILVLDEATASVD-VRTDSLIQRTIR-EEFKS 1420
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 446491464 186 RTIVLVTHDIDEALRLAEHLVLmDHGEVVQQGNPLTMLTRPANDFVR 232
Cdd:PLN03232 1421 CTMLVIAHRLNTIIDCDKILVL-SSGQVLEYDSPQELLSRDTSAFFR 1466
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
5-222 |
1.25e-11 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 64.75 E-value: 1.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 5 SHVSKLFGAQKAVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEIR---SLPVLELRRRMGYai 81
Cdd:PRK10982 2 SNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfksSKEALENGISMVH-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 82 QSIGLFPHWSVAQNIatvpQLQKWSR-------ARIDDRIDELMALLGLESNLRERYPhQLSGGQQQRVGVARALAADPQ 154
Cdd:PRK10982 80 QELNLVLQRSVMDNM----WLGRYPTkgmfvdqDKMYRDTKAIFDELDIDIDPRAKVA-TLSVSQMQMIEIAKAFSYNAK 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446491464 155 VLLMDEPFGALdpvTRGALQQEMTRIHRLLGR--TIVLVTHDIDEALRLAEHLVLMDHGEVV--QQGNPLTM 222
Cdd:PRK10982 155 IVIMDEPTSSL---TEKEVNHLFTIIRKLKERgcGIVYISHKMEEIFQLCDEITILRDGQWIatQPLAGLTM 223
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
32-230 |
1.91e-11 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 64.80 E-value: 1.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 32 LIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEIRSLPVLELRRRMGYAIQSIGLFPHwSVAQNIAtvPQLQKWSrarid 111
Cdd:PTZ00243 1341 IVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFSMIPQDPVLFDG-TVRQNVD--PFLEASS----- 1412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 112 driDELMALLGLeSNLRERYPHQLSG--------------GQQQRVGVARA-LAADPQVLLMDEPFGALDPvtrgAL--Q 174
Cdd:PTZ00243 1413 ---AEVWAALEL-VGLRERVASESEGidsrvleggsnysvGQRQLMCMARAlLKKGSGFILMDEATANIDP----ALdrQ 1484
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446491464 175 QEMTRIHRLLGRTIVLVTHDIDEALRLaEHLVLMDHGEVVQQGNPLTMLTRPANDF 230
Cdd:PTZ00243 1485 IQATVMSAFSAYTVITIAHRLHTVAQY-DKIIVMDHGAVAEMGSPRELVMNRQSIF 1539
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
22-214 |
1.93e-11 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 64.59 E-value: 1.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 22 LNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEIRS-LPVLELRRRMG--YAIQSIGL---------FPH 89
Cdd:PRK11147 24 LHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLIVArLQQDPPRNVEGtvYDFVAEGIeeqaeylkrYHD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 90 WS--VAQ-----NIATVPQLQK-------WsraRIDDRIDELMALLGL--ESNLREryphqLSGGQQQRVGVARALAADP 153
Cdd:PRK11147 104 IShlVETdpsekNLNELAKLQEqldhhnlW---QLENRINEVLAQLGLdpDAALSS-----LSGGWLRKAALGRALVSNP 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446491464 154 QVLLMDEPFGALDPVTRGALQQEMtrihRLLGRTIVLVTHDIDEALRLAEHLVLMDHGEVV 214
Cdd:PRK11147 176 DVLLLDEPTNHLDIETIEWLEGFL----KTFQGSIIFISHDRSFIRNMATRIVDLDRGKLV 232
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
36-195 |
4.25e-11 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 63.89 E-value: 4.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 36 SGSGKSTTlkminrlVEHDSGEIRFAGEEIRSLPVLELRRRMGYAIQSIGLFpHWSVAQNI------ATVPQLQKWSR-A 108
Cdd:PTZ00265 1264 GGSGEDST-------VFKNSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLF-NMSIYENIkfgkedATREDVKRACKfA 1335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 109 RIDDRIDELMAllGLESNLRErYPHQLSGGQQQRVGVARALAADPQVLLMDEPFGALDPVTRGALQQEMTRIHRLLGRTI 188
Cdd:PTZ00265 1336 AIDEFIESLPN--KYDTNVGP-YGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTI 1412
|
....*..
gi 446491464 189 VLVTHDI 195
Cdd:PTZ00265 1413 ITIAHRI 1419
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
4-212 |
6.29e-11 |
|
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: 61.80 E-value: 6.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 4 FSHVSkLFGAqKAVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGeeirslpvlelrrRMGYAIQS 83
Cdd:cd03291 42 FSNLC-LVGA-PVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG-------------RISFSSQF 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 84 IGLFPHwSVAQNIATVPQLQKWsrariddRIDELMALLGLESNLrERYPHQ-----------LSGGQQQRVGVARALAAD 152
Cdd:cd03291 107 SWIMPG-TIKENIIFGVSYDEY-------RYKSVVKACQLEEDI-TKFPEKdntvlgeggitLSGGQRARISLARAVYKD 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446491464 153 PQVLLMDEPFGALDPVTRGALQQEMtrIHRLLG-RTIVLVTHDIdEALRLAEHLVLMDHGE 212
Cdd:cd03291 178 ADLYLLDSPFGYLDVFTEKEIFESC--VCKLMAnKTRILVTSKM-EHLKKADKILILHEGS 235
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
17-219 |
6.51e-11 |
|
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: 60.62 E-value: 6.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 17 VNDLNLNFQEGSFSVLIGTSGSGKSTTLKMI--NRLVEHDSGEIRFAGEEIRSLPVLElRRRMgyaiqsiGLFPHWsvaQ 94
Cdd:cd03217 16 LKGVNLTIKKGEVHALMGPNGSGKSTLAKTImgHPKYEVTEGEILFKGEDITDLPPEE-RARL-------GIFLAF---Q 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 95 NIATVPQLqkwsrariddRIDELMallglesnlreRYPHQ-LSGGQQQRVGVARALAADPQVLLMDEPFGALDPVtrgAL 173
Cdd:cd03217 85 YPPEIPGV----------KNADFL-----------RYVNEgFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDID---AL 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446491464 174 QQEMTRIHRLL--GRTIVLVTHdideALRLAEHLV-----LMDHGEVVQQGNP 219
Cdd:cd03217 141 RLVAEVINKLReeGKSVLIITH----YQRLLDYIKpdrvhVLYDGRIVKSGDK 189
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
19-193 |
1.13e-10 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 59.82 E-value: 1.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 19 DLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEIRSLPVlELRRRMGYAIQSIGLFPHWSVAQNIAT 98
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRD-EYHQDLLYLGHQPGIKTELTALENLRF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 99 vpqLQKWSRARIDDRIDELMALLGLESnlRERYP-HQLSGGQQQRVGVARALAADPQVLLMDEPFGALDpvtrgalQQEM 177
Cdd:PRK13538 98 ---YQRLHGPGDDEALWEALAQVGLAG--FEDVPvRQLSAGQQRRVALARLWLTRAPLWILDEPFTAID-------KQGV 165
|
170 180
....*....|....*....|..
gi 446491464 178 TRIHRLL------GRTIVLVTH 193
Cdd:PRK13538 166 ARLEALLaqhaeqGGMVILTTH 187
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
15-213 |
1.26e-10 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 61.76 E-value: 1.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 15 KAVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMI----------NRLVEHDSGEIRFAGEEIRSLPVL--ELRRRMGyaiq 82
Cdd:TIGR02633 274 KRVDDVSFSLRRGEILGVAGLVGAGRTELVQALfgaypgkfegNVFINGKPVDIRNPAQAIRAGIAMvpEDRKRHG---- 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 83 sigLFPHWSVAQNIaTVPQLQKWS-RARIDDRiDELMALLGLESNLRERYPH------QLSGGQQQRVGVARALAADPQV 155
Cdd:TIGR02633 350 ---IVPILGVGKNI-TLSVLKSFCfKMRIDAA-AELQIIGSAIQRLKVKTASpflpigRLSGGNQQKAVLAKMLLTNPRV 424
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446491464 156 LLMDEPfgaldpvTRGALQQEMTRIHRLL------GRTIVLVTHDIDEALRLAEHLVLMDHGEV 213
Cdd:TIGR02633 425 LILDEP-------TRGVDVGAKYEIYKLInqlaqeGVAIIVVSSELAEVLGLSDRVLVIGEGKL 481
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
2-229 |
1.40e-10 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 62.35 E-value: 1.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 2 IEFSHVSKLFGAQKAV---NDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFA-GEEIRSLPVLELRRRM 77
Cdd:PTZ00265 383 IQFKNVRFHYDTRKDVeiyKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINdSHNLKDINLKWWRSKI 462
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 78 GYAIQSIGLFPHwSVAQNIA----TVPQLQKWS--------------------RARIDDRIDELM------ALLGLESN- 126
Cdd:PTZ00265 463 GVVSQDPLLFSN-SIKNNIKyslySLKDLEALSnyynedgndsqenknkrnscRAKCAGDLNDMSnttdsnELIEMRKNy 541
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 127 -----------------------LRERY-------PHQLSGGQQQRVGVARALAADPQVLLMDEPFGALDPVTRGALQQE 176
Cdd:PTZ00265 542 qtikdsevvdvskkvlihdfvsaLPDKYetlvgsnASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKT 621
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 446491464 177 MTRIHRLLGRTIVLVTHDIdEALRLAEHLVLMDHGEVVQQGNPLTMLTRPAND 229
Cdd:PTZ00265 622 INNLKGNENRITIIIAHRL-STIRYANTIFVLSNRERGSTVDVDIIGEDPTKD 673
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
4-218 |
1.53e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 61.92 E-value: 1.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 4 FSHVSKLfgAQKAVNDLNLNFQEGSFSVLIGTSGSGKSTtlkminrLVEHDSGEIRFAgeEIRSLpvlELRRRMGYAIQS 83
Cdd:PLN03232 622 FSWDSKT--SKPTLSDINLEIPVGSLVAIVGGTGEGKTS-------LISAMLGELSHA--ETSSV---VIRGSVAYVPQV 687
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 84 IGLFpHWSVAQNI--ATVPQLQKWSRArIDdrIDELMALLGL-----ESNLRERYPHqLSGGQQQRVGVARALAADPQVL 156
Cdd:PLN03232 688 SWIF-NATVRENIlfGSDFESERYWRA-ID--VTALQHDLDLlpgrdLTEIGERGVN-ISGGQKQRVSMARAVYSNSDIY 762
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446491464 157 LMDEPFGALDP-VTRGALQQEMTriHRLLGRTIVLVTHDIdEALRLAEHLVLMDHGEVVQQGN 218
Cdd:PLN03232 763 IFDDPLSALDAhVAHQVFDSCMK--DELKGKTRVLVTNQL-HFLPLMDRIILVSEGMIKEEGT 822
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
5-193 |
2.52e-10 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 61.05 E-value: 2.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 5 SHVSKLFGAQKAVNDLNLNFQE-------------GSFSVLIGTSGSGKSTTLKMI-NRLVEHD-SGEIRFAGEEirslP 69
Cdd:PLN03211 59 SNIKRILGHKPKISDETRQIQErtilngvtgmaspGEILAVLGPSGSGKSTLLNALaGRIQGNNfTGTILANNRK----P 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 70 VLELRRRMGYAIQSIGLFPHWSVAQNIATVPQLQKWSRARIDDRI---DELMALLGL----ESNLRERYPHQLSGGQQQR 142
Cdd:PLN03211 135 TKQILKRTGFVTQDDILYPHLTVRETLVFCSLLRLPKSLTKQEKIlvaESVISELGLtkceNTIIGNSFIRGISGGERKR 214
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446491464 143 VGVARALAADPQVLLMDEPFGALDPVTRGALQQEMTRIHRlLGRTIVLVTH 193
Cdd:PLN03211 215 VSIAHEMLINPSLLILDEPTSGLDATAAYRLVLTLGSLAQ-KGKTIVTSMH 264
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
25-195 |
4.54e-10 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 58.92 E-value: 4.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 25 QEGSFSVLIGTSGSGKSTTLK-----MINRLVEHDS----GEI--RFAGEEIRSL--PVLELRRRMGYAIQSIGLFPhws 91
Cdd:cd03236 24 REGQVLGLVGPNGIGKSTALKilagkLKPNLGKFDDppdwDEIldEFRGSELQNYftKLLEGDVKVIVKPQYVDLIP--- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 92 vAQNIATVPQLQKwsraRIDDR--IDELMALLGLEsNLRERYPHQLSGGQQQRVGVARALAADPQVLLMDEPFGALDpvt 169
Cdd:cd03236 101 -KAVKGKVGELLK----KKDERgkLDELVDQLELR-HVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLD--- 171
|
170 180 190
....*....|....*....|....*....|.
gi 446491464 170 rgaLQQEMTR---IHRLL--GRTIVLVTHDI 195
Cdd:cd03236 172 ---IKQRLNAarlIRELAedDNYVLVVEHDL 199
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
28-214 |
6.60e-10 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 59.54 E-value: 6.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 28 SFSV-------LIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEIRSlpvlelrRRMGYAIQS-----------IGLFPH 89
Cdd:PRK11288 273 SFSVrageivgLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDI-------RSPRDAIRAgimlcpedrkaEGIIPV 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 90 WSVAQNIATVPQL----------QKWSRARIDDRIDELmallglesNLRERYPHQ----LSGGQQQRVGVARALAADPQV 155
Cdd:PRK11288 346 HSVADNINISARRhhlragclinNRWEAENADRFIRSL--------NIKTPSREQlimnLSGGNQQKAILGRWLSEDMKV 417
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446491464 156 LLMDEPfgaldpvTRGALQQEMTRIHRLL------GRTIVLVTHDIDEALRLAEHLVLMDHGEVV 214
Cdd:PRK11288 418 ILLDEP-------TRGIDVGAKHEIYNVIyelaaqGVAVLFVSSDLPEVLGVADRIVVMREGRIA 475
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
85-213 |
8.08e-10 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 59.56 E-value: 8.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 85 GLFPHWSVAQNIaTVPQLQKWSRARIDDRIDELMALLGLESNLRERYPH------QLSGGQQQRVGVARALAADPQVLLM 158
Cdd:PRK13549 351 GIVPVMGVGKNI-TLAALDRFTGGSRIDDAAELKTILESIQRLKVKTASpelaiaRLSGGNQQKAVLAKCLLLNPKILIL 429
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446491464 159 DEPfgaldpvTRGALQQEMTRIHRLL------GRTIVLVTHDIDEALRLAEHLVLMDHGEV 213
Cdd:PRK13549 430 DEP-------TRGIDVGAKYEIYKLInqlvqqGVAIIVISSELPEVLGLSDRVLVMHEGKL 483
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
6-194 |
1.43e-09 |
|
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: 58.79 E-value: 1.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 6 HVSKLFGAQKAV-NDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAgeeirslpvleLRRRMGYAIQSI 84
Cdd:TIGR03719 9 RVSKVVPPKKEIlKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQ-----------PGIKVGYLPQEP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 85 GLFPHWSVAQNI--ATVPQLQKWSR--------ARIDDRIDELMALLG-------------LESNLRE-----RYP---- 132
Cdd:TIGR03719 78 QLDPTKTVRENVeeGVAEIKDALDRfneisakyAEPDADFDKLAAEQAelqeiidaadawdLDSQLEIamdalRCPpwda 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446491464 133 --HQLSGGQQQRVGVARALAADPQVLLMDEPFGALDPVTRGALQQEMtriHRLLGrTIVLVTHD 194
Cdd:TIGR03719 158 dvTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHL---QEYPG-TVVAVTHD 217
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
19-211 |
1.49e-09 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 59.15 E-value: 1.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 19 DLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGeeirslpvlelrrRMGYAIQSIGLFPHwSVAQNIAT 98
Cdd:TIGR01271 444 NISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG-------------RISFSPQTSWIMPG-TIKDNIIF 509
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 99 VPQLQKWsrariddRIDELMALLGLESNLrERYPHQ-----------LSGGQQQRVGVARALAADPQVLLMDEPFGALDP 167
Cdd:TIGR01271 510 GLSYDEY-------RYTSVIKACQLEEDI-ALFPEKdktvlgeggitLSGGQRARISLARAVYKDADLYLLDSPFTHLDV 581
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 446491464 168 VTRGALqQEMTRIHRLLGRTIVLVTHDIdEALRLAEHLVLMDHG 211
Cdd:TIGR01271 582 VTEKEI-FESCLCKLMSNKTRILVTSKL-EHLKKADKILLLHEG 623
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
2-173 |
2.14e-09 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 58.21 E-value: 2.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 2 IEFSHVSKLFGAQKAVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFaGEEIrslpvlelrrRMGYAI 81
Cdd:PRK11819 325 IEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GETV----------KLAYVD 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 82 QS-IGLFPHWSVAQNIA------TVPQLQKWSRARIddridelmALLGLESNLRERYPHQLSGGQQQRVGVARALAADPQ 154
Cdd:PRK11819 394 QSrDALDPNKTVWEEISggldiiKVGNREIPSRAYV--------GRFNFKGGDQQKKVGVLSGGERNRLHLAKTLKQGGN 465
|
170
....*....|....*....
gi 446491464 155 VLLMDEPFGALDPVTRGAL 173
Cdd:PRK11819 466 VLLLDEPTNDLDVETLRAL 484
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
7-213 |
2.46e-09 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 58.09 E-value: 2.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 7 VSKLFGAqkAVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEI--RSlP----------VLELR 74
Cdd:PRK10762 260 VDNLSGP--GVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVvtRS-PqdglangivyISEDR 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 75 RRMGYAIqsiGLfphwSVAQNIaTVPQLQKWSRA--RIDDRiDELMA------LLGLESNLRERYPHQLSGGQQQRVGVA 146
Cdd:PRK10762 337 KRDGLVL---GM----SVKENM-SLTALRYFSRAggSLKHA-DEQQAvsdfirLFNIKTPSMEQAIGLLSGGNQQKVAIA 407
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446491464 147 RALAADPQVLLMDEPfgaldpvTRGALQQEMTRIHRLL------GRTIVLVTHDIDEALRLAEHLVLMDHGEV 213
Cdd:PRK10762 408 RGLMTRPKVLILDEP-------TRGVDVGAKKEIYQLInqfkaeGLSIILVSSEMPEVLGMSDRILVMHEGRI 473
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
19-223 |
2.54e-09 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 58.42 E-value: 2.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 19 DLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEIRSLPVLELRRRMGYAIQSIGLFPHwSVAQNIAT 98
Cdd:TIGR00957 1304 HINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSG-SLRMNLDP 1382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 99 VPQLQK---WSRAriddridELMALLGLESNLRERYPHQ-------LSGGQQQRVGVARALAADPQVLLMDEPFGALDPV 168
Cdd:TIGR00957 1383 FSQYSDeevWWAL-------ELAHLKTFVSALPDKLDHEcaeggenLSVGQRQLVCLARALLRKTKILVLDEATAAVDLE 1455
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446491464 169 TRGALQQEM-TRIHRLlgrTIVLVTHDIDEALRLAEHLVLmDHGEVVQQGNPLTML 223
Cdd:TIGR00957 1456 TDNLIQSTIrTQFEDC---TVLTIAHRLNTIMDYTRVIVL-DKGEVAEFGAPSNLL 1507
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
32-232 |
3.42e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 57.83 E-value: 3.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 32 LIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEIRSLPVLELRRRMGYAIQSIGLFPHwSVAQNIATVPQLQK---W--- 105
Cdd:PLN03130 1270 IVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSG-TVRFNLDPFNEHNDadlWesl 1348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 106 SRARIDDRIDElmALLGLESNLRERyPHQLSGGQQQRVGVARALAADPQVLLMDEPFGALDpVTRGALQQEMTR------ 179
Cdd:PLN03130 1349 ERAHLKDVIRR--NSLGLDAEVSEA-GENFSVGQRQLLSLARALLRRSKILVLDEATAAVD-VRTDALIQKTIReefksc 1424
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446491464 180 -----IHRLlgRTIVlvthDIDEALrlaehlvLMDHGEVVQQGNPLTMLTRPANDFVR 232
Cdd:PLN03130 1425 tmliiAHRL--NTII----DCDRIL-------VLDAGRVVEFDTPENLLSNEGSAFSK 1469
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
19-217 |
3.88e-09 |
|
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: 55.73 E-value: 3.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 19 DLNLNFQEGSFSVLIGTSGSGKST----TLkminrlveHDSGEIRFageeIRSLPVLeLRRRMGY----AIQSI-GLFPH 89
Cdd:cd03270 13 NVDVDIPRNKLVVITGVSGSGKSSlafdTI--------YAEGQRRY----VESLSAY-ARQFLGQmdkpDVDSIeGLSPA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 90 WSVAQN---------IATVPQLQK-----WSRARIDDRIDELMAlLGLESNLRERYPHQLSGGQQQRVGVARALAADPQV 155
Cdd:cd03270 80 IAIDQKttsrnprstVGTVTEIYDylrllFARVGIRERLGFLVD-VGLGYLTLSRSAPTLSGGEAQRIRLATQIGSGLTG 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 156 LL--MDEPFGALDPVTRGALQQEMTRIhRLLGRTIVLVTHDiDEALRLAEHLVLM-----DH-GEVVQQG 217
Cdd:cd03270 159 VLyvLDEPSIGLHPRDNDRLIETLKRL-RDLGNTVLVVEHD-EDTIRAADHVIDIgpgagVHgGEIVAQG 226
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
17-291 |
8.40e-09 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 56.88 E-value: 8.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 17 VNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGeeirslpvlelrrrmgyaiqSIGLFPH--W---- 90
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKG--------------------SVAYVPQqaWiqnd 713
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 91 SVAQNIATVPQLQ-KWSRARIddridELMALL--------GLESNLRERYPHqLSGGQQQRVGVARALAADPQVLLMDEP 161
Cdd:TIGR00957 714 SLRENILFGKALNeKYYQQVL-----EACALLpdleilpsGDRTEIGEKGVN-LSGGQKQRVSLARAVYSNADIYLFDDP 787
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 162 FGALDP-VTRGALQQEMTRIHRLLGRTIVLVTHDIdEALRLAEHLVLMDHGEVVQQGNPLTMLTRPAndfvrqffgrsel 240
Cdd:TIGR00957 788 LSAVDAhVGKHIFEHVIGPEGVLKNKTRILVTHGI-SYLPQVDVIIVMSGGKISEMGSYQELLQRDG------------- 853
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 446491464 241 gvrllslrSVADYVRREERAEGEALAEEmtlrDALSLFVARGCEVLPVVNT 291
Cdd:TIGR00957 854 --------AFAEFLRTYAPDEQQGHLED----SWTALVSGEGKEAKLIENG 892
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
2-170 |
9.86e-09 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 56.18 E-value: 9.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 2 IEFSHVSKLFGAQKAVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMI---------NRLVEHdsGEIRFAGEEIrslpvLE 72
Cdd:PRK10938 261 IVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLItgdhpqgysNDLTLF--GRRRGSGETI-----WD 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 73 LRRRMGYA----------------------IQSIGLFPHWSVAQNIATvpqlQKWsrariddridelMALLGLESNLRER 130
Cdd:PRK10938 334 IKKHIGYVssslhldyrvstsvrnvilsgfFDSIGIYQAVSDRQQKLA----QQW------------LDILGIDKRTADA 397
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 446491464 131 YPHQLSGGQQQRVGVARALAADPQVLLMDEPFGALDPVTR 170
Cdd:PRK10938 398 PFHSLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNR 437
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
25-195 |
1.01e-08 |
|
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: 55.95 E-value: 1.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 25 QEGSFSVLIGTSGSGKSTTLKMInrlvehdSGEI------------------RFAGEEIRSLpvleLRR------RMGYA 80
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKIL-------SGELkpnlgdydeepswdevlkRFRGTELQDY----FKKlangeiKVAHK 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 81 IQSIGLFPhwSVAQniATVPQLQKwsraRIDDR--IDELMALLGLEsNLRERYPHQLSGGQQQRVGVARALAADPQVLLM 158
Cdd:COG1245 166 PQYVDLIP--KVFK--GTVRELLE----KVDERgkLDELAEKLGLE-NILDRDISELSGGELQRVAIAAALLRDADFYFF 236
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 446491464 159 DEPFGALDPVTR---GALQQEMTRIhrllGRTIVLVTHDI 195
Cdd:COG1245 237 DEPSSYLDIYQRlnvARLIRELAEE----GKYVLVVEHDL 272
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
17-217 |
1.10e-08 |
|
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: 54.19 E-value: 1.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 17 VNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHD---SGEIRFAGEEIRSLPVlELRRRMGYAIQSIGLFPHWSVA 93
Cdd:cd03233 23 LKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKEFAE-KYPGEIIYVSEEDVHFPTLTVR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 94 QNIATVPQLQKwsrariddridelmallglesnlrERYPHQLSGGQQQRVGVARALAADPQVLLMDEPFGALDPVTrgAL 173
Cdd:cd03233 102 ETLDFALRCKG------------------------NEFVRGISGGERKRVSIAEALVSRASVLCWDNSTRGLDSST--AL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 446491464 174 Q-----QEMTRIHRLLgrTIVLVTHDIDEALRLAEHLVLMDHGEVVQQG 217
Cdd:cd03233 156 EilkciRTMADVLKTT--TFVSLYQASDEIYDLFDKVLVLYEGRQIYYG 202
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
25-195 |
1.19e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 55.97 E-value: 1.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 25 QEGSFSVLIGTSGSGKSTTLK-----MINRLVEHDSG----EI--RFAGEEI----RSLPVLELRrrMGYAIQSIGLFPh 89
Cdd:PRK13409 97 KEGKVTGILGPNGIGKTTAVKilsgeLIPNLGDYEEEpswdEVlkRFRGTELqnyfKKLYNGEIK--VVHKPQYVDLIP- 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 90 wSVAQniATVPQLQKwsraRIDDR--IDELMALLGLEsNLRERYPHQLSGGQQQRVGVARALAADPQVLLMDEPFGALDP 167
Cdd:PRK13409 174 -KVFK--GKVRELLK----KVDERgkLDEVVERLGLE-NILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDI 245
|
170 180 190
....*....|....*....|....*....|.
gi 446491464 168 VTR---GALQQEMTRihrllGRTIVLVTHDI 195
Cdd:PRK13409 246 RQRlnvARLIRELAE-----GKYVLVVEHDL 271
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
17-218 |
1.25e-08 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 54.65 E-value: 1.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 17 VNDLNLNFQEGSFSVLIGTSGSGKSTTLKMInrlVEHDS-----GEIRFAGEEIRSLPVlELRRRMG------YAIQSIG 85
Cdd:CHL00131 23 LKGLNLSINKGEIHAIMGPNGSGKSTLSKVI---AGHPAykileGDILFKGESILDLEP-EERAHLGiflafqYPIEIPG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 86 ------LFPHWSVAQNIATVPQLQKWSRARIddrIDELMALLGLESNLRERYPHQ-LSGGQQQRVGVARALAADPQVLLM 158
Cdd:CHL00131 99 vsnadfLRLAYNSKRKFQGLPELDPLEFLEI---INEKLKLVGMDPSFLSRNVNEgFSGGEKKRNEILQMALLDSELAIL 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446491464 159 DEPFGALDPvtrGALQQEMTRIHRLLGRT--IVLVTHdideALRLAEHLV-----LMDHGEVVQQGN 218
Cdd:CHL00131 176 DETDSGLDI---DALKIIAEGINKLMTSEnsIILITH----YQRLLDYIKpdyvhVMQNGKIIKTGD 235
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
34-225 |
1.52e-08 |
|
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: 54.53 E-value: 1.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 34 GTSGSGKSTTLKMINRLVEHDSGEIRFAGEEIRSLPVLELRRRMGYAIQSIGLFPHwSVAQNIAtvPQlqkwsRARIDDR 113
Cdd:cd03288 54 GRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPILFSG-SIRFNLD--PE-----CKCTDDR 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 114 IDELMALLGLEsNLRERYPHQL-----------SGGQQQRVGVARALAADPQVLLMDEPFGALDPVTRGALQQ-EMTrih 181
Cdd:cd03288 126 LWEALEIAQLK-NMVKSLPGGLdavvteggenfSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENILQKvVMT--- 201
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 446491464 182 RLLGRTIVLVTHDIDEALRlAEHLVLMDHGEVVQQGNPLTMLTR 225
Cdd:cd03288 202 AFADRTVVTIAHRVSTILD-ADLVLVLSRGILVECDTPENLLAQ 244
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
112-217 |
1.69e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 55.41 E-value: 1.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 112 DRIDELMALLGLESNLRERYPHqLSGGQQQRVGVARALAADPQVLLMDEPFGALDPVTRGALQQEMTRIHRlLGRTIVLV 191
Cdd:PRK10938 114 ARCEQLAQQFGITALLDRRFKY-LSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQ-SGITLVLV 191
|
90 100
....*....|....*....|....*.
gi 446491464 192 THDIDEALRLAEHLVLMDHGEVVQQG 217
Cdd:PRK10938 192 LNRFDEIPDFVQFAGVLADCTLAETG 217
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
27-202 |
5.66e-08 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 51.22 E-value: 5.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 27 GSFSVLIGTSGSGKSTTLKMI-NRLVEHDSGEIRFAGEEIRSLPVLELRRRMGYaiqsiglfphwsvaqniatvpqlqkw 105
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALaRELGPPGGGVIYIDGEDILEEVLDQLLLIIVG-------------------------- 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 106 srariddridelmallglesnlreRYPHQLSGGQQQRVGVARALAADPQVLLMDEPFGALDPVTRGALQQE-----MTRI 180
Cdd:smart00382 56 ------------------------GKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLeelrlLLLL 111
|
170 180
....*....|....*....|..
gi 446491464 181 HRLLGRTIVLVTHDIDEALRLA 202
Cdd:smart00382 112 KSEKNLTVILTTNDEKDLGPAL 133
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
6-193 |
8.41e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 51.41 E-value: 8.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 6 HVSKLFGAQKAVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEIRSLPvlelRRRMGYAIQSIG 85
Cdd:PRK13541 5 HQLQFNIEQKNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIA----KPYCTYIGHNLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 86 LFPHWSVAQNiatvpqLQKWSraRIDDRIDELMALL---GLESNLRERYpHQLSGGQQQRVGVARALAADPQVLLMDEPF 162
Cdd:PRK13541 81 LKLEMTVFEN------LKFWS--EIYNSAETLYAAIhyfKLHDLLDEKC-YSLSSGMQKIVAIARLIACQSDLWLLDEVE 151
|
170 180 190
....*....|....*....|....*....|.
gi 446491464 163 GALDPVTRgALQQEMTRIHRLLGRTIVLVTH 193
Cdd:PRK13541 152 TNLSKENR-DLLNNLIVMKANSGGIVLLSSH 181
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
20-167 |
1.24e-07 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 51.39 E-value: 1.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 20 LNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEIRSLpvlELRRRMGYAIQSIGLFPHWSVAQNIATV 99
Cdd:PRK13543 30 LDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRG---DRSRFMAYLGHLPGLKADLSTLENLHFL 106
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446491464 100 PQLQKWSRARIDDRIDELMALLGLESNLREryphQLSGGQQQRVGVARALAADPQVLLMDEPFGALDP 167
Cdd:PRK13543 107 CGLHGRRAKQMPGSALAIVGLAGYEDTLVR----QLSAGQKKRLALARLWLSPAPLWLLDEPYANLDL 170
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
14-217 |
1.43e-07 |
|
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: 50.40 E-value: 1.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 14 QKAVNDLNLNFQEGSFSVLIGTSGSGKSTTLKminrlvehdsgEIRFAGEEIRSLPVLELrrrmgyaiqsiglFPHwsva 93
Cdd:cd03238 8 VHNLQNLDVSIPLNVLVVVTGVSGSGKSTLVN-----------EGLYASGKARLISFLPK-------------FSR---- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 94 QNIATVPQLQkwsrariddrideLMALLGLESNLRERYPHQLSGGQQQRVGVARALAADPQ--VLLMDEPFGALDPVTrg 171
Cdd:cd03238 60 NKLIFIDQLQ-------------FLIDVGLGYLTLGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQD-- 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446491464 172 aLQQEMTRIHRL--LGRTIVLVTHDiDEALRLAEHLVLMDH------GEVVQQG 217
Cdd:cd03238 125 -INQLLEVIKGLidLGNTVILIEHN-LDVLSSADWIIDFGPgsgksgGKVVFSG 176
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
18-211 |
1.74e-07 |
|
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: 50.70 E-value: 1.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 18 NDLNLNFQEGSFSVLIGTSGSGKSTTLKMI--NRLVEHDSGEIRFAGEEIRSlpvlELRRRMGYAIQSIGLFPHWSVAQn 95
Cdd:cd03232 24 NNISGYVKPGTLTALMGESGAGKTTLLDVLagRKTAGVITGEILINGRPLDK----NFQRSTGYVEQQDVHSPNLTVRE- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 96 iatvpqlqkwsrariddridelmALLgLESNLREryphqLSGGQQQRVGVARALAADPQVLLMDEPFGALDpvTRGALQQ 175
Cdd:cd03232 99 -----------------------ALR-FSALLRG-----LSVEQRKRLTIGVELAAKPSILFLDEPTSGLD--SQAAYNI 147
|
170 180 190
....*....|....*....|....*....|....*....
gi 446491464 176 eMTRIHRLL--GRTIVLVTHDIDEAL-RLAEHLVLMDHG 211
Cdd:cd03232 148 -VRFLKKLAdsGQAILCTIHQPSASIfEKFDRLLLLKRG 185
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
2-195 |
1.90e-07 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 52.09 E-value: 1.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 2 IEFSHVSKLFGaqkavnDLNLNFQEGSFS---VL--IGTSGSGKSTTLKMINRLVEHDSGEIrfageeirslpvlELRRR 76
Cdd:COG1245 342 VEYPDLTKSYG------GFSLEVEGGEIRegeVLgiVGPNGIGKTTFAKILAGVLKPDEGEV-------------DEDLK 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 77 MGYAIQSIGLFPHWSVAQNIatvpqlqkwsRARIDDRID------ELMALLGLEsNLRERYPHQLSGGQQQRVGVARALA 150
Cdd:COG1245 403 ISYKPQYISPDYDGTVEEFL----------RSANTDDFGssyyktEIIKPLGLE-KLLDKNVKDLSGGELQRVAIAACLS 471
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 446491464 151 ADPQVLLMDEPFGALDPVTRGALQQEMTRIHRLLGRTIVLVTHDI 195
Cdd:COG1245 472 RDADLYLLDEPSAHLDVEQRLAVAKAIRRFAENRGKTAMVVDHDI 516
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
27-217 |
2.46e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 52.03 E-value: 2.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 27 GSFSVLIGTSGSGKSTTLKMINRLVEH----DSGEIRFAG---EEIRSlpvlELRRRMGYAIQSIGLFPHWSVAQNIATV 99
Cdd:TIGR00956 87 GELTVVLGRPGSGCSTLLKTIASNTDGfhigVEGVITYDGitpEEIKK----HYRGDVVYNAETDVHFPHLTVGETLDFA 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 100 PQLQK-------WSR-ARIDDRIDELMALLGL----ESNLRERYPHQLSGGQQQRVGVARALAADPQVLLMDEPFGALDP 167
Cdd:TIGR00956 163 ARCKTpqnrpdgVSReEYAKHIADVYMATYGLshtrNTKVGNDFVRGVSGGERKRVSIAEASLGGAKIQCWDNATRGLDS 242
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446491464 168 VTrgALQ-----QEMTRIhrllGRTIVLVT--HDIDEALRLAEHLVLMDHGEVVQQG 217
Cdd:TIGR00956 243 AT--ALEfiralKTSANI----LDTTPLVAiyQCSQDAYELFDKVIVLYEGYQIYFG 293
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
24-220 |
2.51e-07 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 52.16 E-value: 2.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 24 FQEGSFSVLIGTSGSGKSTTLKMI--NRLVEHDSGEIRFAGeeirsLPVLE--LRRRMGYAIQSIGLFPHWSVAQNIATV 99
Cdd:PLN03140 903 FRPGVLTALMGVSGAGKTTLMDVLagRKTGGYIEGDIRISG-----FPKKQetFARISGYCEQNDIHSPQVTVRESLIYS 977
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 100 PQLQKWSRARIDDR---IDELMALLGLEsNLRER---YP--HQLSGGQQQRVGVARALAADPQVLLMDEPFGALDpVTRG 171
Cdd:PLN03140 978 AFLRLPKEVSKEEKmmfVDEVMELVELD-NLKDAivgLPgvTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLD-ARAA 1055
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446491464 172 ALQQEMTRIHRLLGRTIVLVTH----DIDEALrlaEHLVLMDHGEVVQQGNPL 220
Cdd:PLN03140 1056 AIVMRTVRNTVDTGRTVVCTIHqpsiDIFEAF---DELLLMKRGGQVIYSGPL 1105
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
135-217 |
3.68e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 51.66 E-value: 3.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 135 LSGGQQQRVGVARALAADPQVLLMDEPFGALDP-VTRGALQQEMTRihRLLGRTIVLVTHDIdEALRLAEHLVLMDHGEV 213
Cdd:PLN03130 741 ISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAhVGRQVFDKCIKD--ELRGKTRVLVTNQL-HFLSQVDRIILVHEGMI 817
|
....
gi 446491464 214 VQQG 217
Cdd:PLN03130 818 KEEG 821
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
33-195 |
5.77e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 50.58 E-value: 5.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 33 IGTSGSGKSTTLKMINRLVEHDSGEIrfageeirslpvlELRRRMGYAIQSIGLFPHWSVAQNIATVPqlqkwsraridD 112
Cdd:PRK13409 371 VGPNGIGKTTFAKLLAGVLKPDEGEV-------------DPELKISYKPQYIKPDYDGTVEDLLRSIT-----------D 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 113 RID------ELMALLGLEsNLRERYPHQLSGGQQQRVGVARALAADPQVLLMDEPFGALDPVTRGALQQEMTRIHRLLGR 186
Cdd:PRK13409 427 DLGssyyksEIIKPLQLE-RLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAEEREA 505
|
....*....
gi 446491464 187 TIVLVTHDI 195
Cdd:PRK13409 506 TALVVDHDI 514
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
7-194 |
6.90e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 50.50 E-value: 6.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 7 VSKLFGAQKAV-NDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAgEEIRslpvlelrrrMGYAIQSIG 85
Cdd:PRK11819 12 VSKVVPPKKQIlKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPA-PGIK----------VGYLPQEPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 86 LFPHWSVAQNI--ATVPQLQKWSR--------ARIDDRIDELMALLG-------------LESNLRE-----RYPH---- 133
Cdd:PRK11819 81 LDPEKTVRENVeeGVAEVKAALDRfneiyaayAEPDADFDALAAEQGelqeiidaadawdLDSQLEIamdalRCPPwdak 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446491464 134 --QLSGGQQQRVGVARALAADPQVLLMDEPFGALDPVTRGALQQEMtriHRLLGrTIVLVTHD 194
Cdd:PRK11819 161 vtKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLEQFL---HDYPG-TVVAVTHD 219
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
20-214 |
7.17e-07 |
|
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: 50.18 E-value: 7.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 20 LNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEIRSLPVLELRrrmgyaiqsiglfphwsvaQNIATV 99
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAYR-------------------QLFSAV 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 100 -------PQLQKWSRARIDDRIDELMALLGLE----------SNLreryphQLSGGQQQRVGVARALAADPQVLLMDEpF 162
Cdd:COG4615 412 fsdfhlfDRLLGLDGEADPARARELLERLELDhkvsvedgrfSTT------DLSQGQRKRLALLVALLEDRPILVFDE-W 484
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446491464 163 GA-LDPVTRgalqqemtRI--HRLL------GRTIVLVTHDiDEALRLAEHLVLMDHGEVV 214
Cdd:COG4615 485 AAdQDPEFR--------RVfyTELLpelkarGKTVIAISHD-DRYFDLADRVLKMDYGKLV 536
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
1-213 |
7.42e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 50.11 E-value: 7.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 1 MIEFSHVSKLfgAQKAVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEIRSLPVLELRRRmGYA 80
Cdd:PRK10982 250 ILEVRNLTSL--RQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANEAINH-GFA 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 81 I-----QSIGLFPHWSVAQNiatvpqlqkwsraRIDDRIDELMALLGLESN-------------LRERYP-HQ-----LS 136
Cdd:PRK10982 327 LvteerRSTGIYAYLDIGFN-------------SLISNIRNYKNKVGLLDNsrmksdtqwvidsMRVKTPgHRtqigsLS 393
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446491464 137 GGQQQRVGVARALAADPQVLLMDEPFGALDPVTRGALQQEMTRIHRlLGRTIVLVTHDIDEALRLAEHLVLMDHGEV 213
Cdd:PRK10982 394 GGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAK-KDKGIIIISSEMPELLGITDRILVMSNGLV 469
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
21-217 |
2.66e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 48.70 E-value: 2.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 21 NLNF--QEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIrFAGEEIRsLPVLELRRRMGYAIQSIglfPHWSVAQNIAT 98
Cdd:PLN03073 527 NLNFgiDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTV-FRSAKVR-MAVFSQHHVDGLDLSSN---PLLYMMRCFPG 601
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 99 VPQlqkwsraridDRIDELMALLGLESNLRERYPHQLSGGQQQRVGVARALAADPQVLLMDEPFGALDPVTRGALQQEMT 178
Cdd:PLN03073 602 VPE----------QKLRAHLGSFGVTGNLALQPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEALIQGLV 671
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 446491464 179 rihrLLGRTIVLVTHDidealrlaEHLVL--MDHGEVVQQG 217
Cdd:PLN03073 672 ----LFQGGVLMVSHD--------EHLISgsVDELWVVSEG 700
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
24-193 |
2.72e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 48.95 E-value: 2.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 24 FQEGSFSVLIGTSGSGKSTTLkmiNRLVEHDSGEIRFAGEEIRSLPVLE--LRRRMGYAIQSIGLFPHWSVAQNI---AT 98
Cdd:TIGR00956 786 VKPGTLTALMGASGAGKTTLL---NVLAERVTTGVITGGDRLVNGRPLDssFQRSIGYVQQQDLHLPTSTVRESLrfsAY 862
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 99 VPQLQKWSRARIDDRIDELMALLGLESnlrerYPHQLSG--------GQQQRVGVARALAADPQVLL-MDEPFGALDPVT 169
Cdd:TIGR00956 863 LRQPKSVSKSEKMEYVEEVIKLLEMES-----YADAVVGvpgeglnvEQRKRLTIGVELVAKPKLLLfLDEPTSGLDSQT 937
|
170 180
....*....|....*....|....*.
gi 446491464 170 RGALQQEMTRI--HrllGRTIVLVTH 193
Cdd:TIGR00956 938 AWSICKLMRKLadH---GQAILCTIH 960
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
121-226 |
4.19e-06 |
|
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: 48.09 E-value: 4.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 121 LGLESNLRERYPHQLSGGQQQRVGVARALAAD-PQVL-LMDEPFGALDPVTRGALQQEMTRIhRLLGRTIVLVTHDiDEA 198
Cdd:TIGR00630 475 VGLDYLSLSRAAGTLSGGEAQRIRLATQIGSGlTGVLyVLDEPSIGLHQRDNRRLINTLKRL-RDLGNTLIVVEHD-EDT 552
|
90 100 110
....*....|....*....|....*....|....
gi 446491464 199 LRLAEHLVLM-----DH-GEVVQQGNPLTMLTRP 226
Cdd:TIGR00630 553 IRAADYVIDIgpgagEHgGEVVASGTPEEILANP 586
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
133-194 |
1.42e-05 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 44.66 E-value: 1.42e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446491464 133 HQLSGGQQQRVGVARALA----ADPQVLLMDEPFGALDPVTRGALqQEMTRIHRLLGRTIVLVTHD 194
Cdd:cd03227 76 LQLSGGEKELSALALILAlaslKPRPLYILDEIDRGLDPRDGQAL-AEAILEHLVKGAQVIVITHL 140
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
55-171 |
1.79e-05 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 45.94 E-value: 1.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 55 SGEIRFAGEEIRSLPVLE-LRRRMGYAIQ---SIGLFPHWSVAQNIaTVPQLQKWSRARIDDRIDELMALLGLESNLRER 130
Cdd:NF040905 316 SGTVFKDGKEVDVSTVSDaIDAGLAYVTEdrkGYGLNLIDDIKRNI-TLANLGKVSRRGVIDENEEIKVAEEYRKKMNIK 394
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 446491464 131 YPH------QLSGGQQQRVGVARALAADPQVLLMDEPfgaldpvTRG 171
Cdd:NF040905 395 TPSvfqkvgNLSGGNQQKVVLSKWLFTDPDVLILDEP-------TRG 434
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
16-239 |
3.71e-05 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 44.42 E-value: 3.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 16 AVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEeirsLPVLelrrrmgyAIQSiGLFPHWSVAQN 95
Cdd:PRK13546 39 ALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGE----VSVI--------AISA-GLSGQLTGIEN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 96 IATVPQLQKWSRARIDDRIDELMALlgleSNLRErYPHQ----LSGGQQQRVGVARALAADPQVLLMDEpfgALDPVTRG 171
Cdd:PRK13546 106 IEFKMLCMGFKRKEIKAMTPKIIEF----SELGE-FIYQpvkkYSSGMRAKLGFSINITVNPDILVIDE---ALSVGDQT 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 172 ALQQEMTRIHRL--LGRTIVLVTHDIDEALRLAEHLVLMDHGEVVQQGNPLTMLTRpANDFVRQFFGRSE 239
Cdd:PRK13546 178 FAQKCLDKIYEFkeQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDVLPK-YEAFLNDFKKKSK 246
|
|
| CBS |
COG0517 |
CBS domain [Signal transduction mechanisms]; |
179-306 |
4.28e-05 |
|
CBS domain [Signal transduction mechanisms];
Pssm-ID: 440283 [Multi-domain] Cd Length: 128 Bit Score: 42.55 E-value: 4.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 179 RIHRLLGRTIVLVTHD--IDEALRL-AEH-----LVLMDHGEVVqqGnpltMLTRpaNDFVRQFFGRselGVRLLSLRsV 250
Cdd:COG0517 2 KVKDIMTTDVVTVSPDatVREALELmSEKrigglPVVDEDGKLV--G----IVTD--RDLRRALAAE---GKDLLDTP-V 69
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 446491464 251 ADYVRREeraeGEALAEEMTLRDALSLFVARGCEVLPVVNTQGQPSGTLHFQDLLE 306
Cdd:COG0517 70 SEVMTRP----PVTVSPDTSLEEAAELMEEHKIRRLPVVDDDGRLVGIITIKDLLK 121
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
2-166 |
4.83e-05 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 44.50 E-value: 4.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 2 IEFSHVSKLFGAQKAVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAgEEIrslpvlelrrrmgyai 81
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWS-ENA---------------- 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 82 qSIGLFP--HWSVAQNIATVPQ-LQKWSRARIDDRIdeLMALLG--LESNLRERYPHQ-LSGGQQQRVGVARALAADPQV 155
Cdd:PRK15064 383 -NIGYYAqdHAYDFENDLTLFDwMSQWRQEGDDEQA--VRGTLGrlLFSQDDIKKSVKvLSGGEKGRMLFGKLMMQKPNV 459
|
170
....*....|.
gi 446491464 156 LLMDEPFGALD 166
Cdd:PRK15064 460 LVMDEPTNHMD 470
|
|
| CBS_pair_SF |
cd02205 |
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ... |
187-305 |
5.62e-05 |
|
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).
Pssm-ID: 341358 [Multi-domain] Cd Length: 113 Bit Score: 41.85 E-value: 5.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 187 TIVLVTHDIDEALRL-AEH-----LVLMDHGEVVqqGnpltMLTRpaNDFVRQFFGRselgvRLLSLRSVADYVRREera 260
Cdd:cd02205 5 VTVDPDTTVREALELmAENgigalPVVDDDGKLV--G----IVTE--RDILRALVEG-----GLALDTPVAEVMTPD--- 68
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 446491464 261 eGEALAEEMTLRDALSLFVARGCEVLPVVNTQGQPSGTLHFQDLL 305
Cdd:cd02205 69 -VITVSPDTDLEEALELMLEHGIRRLPVVDDDGKLVGIVTRRDIL 112
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
1-218 |
7.14e-05 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 44.11 E-value: 7.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 1 MIEFSHVSKLFGAQKAVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEI--------------RFAGEEIR 66
Cdd:PRK15064 1 MLSTANITMQFGAKPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVsldpnerlgklrqdQFAFEEFT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 67 SLPVLelrrRMGYAiqsiglfPHWSVAQniatvpqlqkwSRARI--------DD--RIDELMA----------------- 119
Cdd:PRK15064 81 VLDTV----IMGHT-------ELWEVKQ-----------ERDRIyalpemseEDgmKVADLEVkfaemdgytaearagel 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 120 LLGLESNLRERYP--HQLSGGQQQRVGVARALAADPQVLLMDEPFGALDPVTRGALQQEmtrihrLLGR--TIVLVTHDI 195
Cdd:PRK15064 139 LLGVGIPEEQHYGlmSEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDINTIRWLEDV------LNERnsTMIIISHDR 212
|
250 260
....*....|....*....|....
gi 446491464 196 DEALRLAEHLVLMDHGEV-VQQGN 218
Cdd:PRK15064 213 HFLNSVCTHMADLDYGELrVYPGN 236
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
24-204 |
8.10e-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: 42.98 E-value: 8.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 24 FQEGsFSVLIGTSGSGKSTTLKMI-----------NRLVEHDSGEIRfAGEEIRSLPvLELRRRMG---YAIQSIglfph 89
Cdd:cd03240 20 FFSP-LTLIVGQNGAGKTTIIEALkyaltgelppnSKGGAHDPKLIR-EGEVRAQVK-LAFENANGkkyTITRSL----- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 90 wSVAQNIATVPQlqkwsrariddriDELMALLglesnlrERYPHQLSGGQQQ------RVGVARALAADPQVLLMDEPFG 163
Cdd:cd03240 92 -AILENVIFCHQ-------------GESNWPL-------LDMRGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTT 150
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 446491464 164 ALDPVTR-GALQQEMTRIHRLLGRTIVLVTHDiDEALRLAEH 204
Cdd:cd03240 151 NLDEENIeESLAEIIEERKSQKNFQLIVITHD-EELVDAADH 191
|
|
| COG2524 |
COG2524 |
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription]; |
172-306 |
1.02e-04 |
|
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];
Pssm-ID: 442013 [Multi-domain] Cd Length: 206 Bit Score: 42.56 E-value: 1.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 172 ALQQEMTRIHRLLGRTIVLVTHD--IDEALRLaehlvLMDHGE----VVQQGNPLTMLTRpaNDFVRQFFGRSELGVRll 245
Cdd:COG2524 80 LGLVLKMKVKDIMTKDVITVSPDttLEEALEL-----MLEKGIsglpVVDDGKLVGIITE--RDLLKALAEGRDLLDA-- 150
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446491464 246 slrSVADYVRREEraegEALAEEMTLRDALSLFVARGCEVLPVVNTQGQPSGTLHFQDLLE 306
Cdd:COG2524 151 ---PVSDIMTRDV----VTVSEDDSLEEALRLMLEHGIGRLPVVDDDGKLVGIITRTDILR 204
|
|
| CBS |
pfam00571 |
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ... |
265-307 |
1.36e-04 |
|
CBS domain; CBS domains are small intracellular modules that pair together to form a stable globular domain. This family represents a single CBS domain. Pairs of these domains have been termed a Bateman domain. CBS domains have been shown to bind ligands with an adenosyl group such as AMP, ATP and S-AdoMet. CBS domains are found attached to a wide range of other protein domains suggesting that CBS domains may play a regulatory role making proteins sensitive to adenosyl carrying ligands. The region containing the CBS domains in Cystathionine-beta synthase is involved in regulation by S-AdoMet. CBS domain pairs from AMPK bind AMP or ATP. The CBS domains from IMPDH and the chloride channel CLC2 bind ATP.
Pssm-ID: 425756 [Multi-domain] Cd Length: 57 Bit Score: 39.12 E-value: 1.36e-04
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 446491464 265 LAEEMTLRDALSLFVARGCEVLPVVNTQGQPSGTLHFQDLLEE 307
Cdd:pfam00571 12 VSPDTTLEEALELMREHGISRLPVVDEDGKLVGIVTLKDLLRA 54
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
121-219 |
1.81e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 43.28 E-value: 1.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 121 LGLESNLRERYPHQLSGGQQQRVGVARALAADPQ--VLLMDEPFGALDPVTRGALQQEMTRIhRLLGRTIVLVTHDiDEA 198
Cdd:PRK00635 463 LGLPYLTPERALATLSGGEQERTALAKHLGAELIgiTYILDEPSIGLHPQDTHKLINVIKKL-RDQGNTVLLVEHD-EQM 540
|
90 100
....*....|....*....|....*..
gi 446491464 199 LRLAEHLVLMD------HGEVVQQGNP 219
Cdd:PRK00635 541 ISLADRIIDIGpgagifGGEVLFNGSP 567
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
113-166 |
2.93e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 42.54 E-value: 2.93e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 446491464 113 RIDELMALLGLESNLRERYPHQLSGGQQQRVGVARALAADPQVLLMDEPFGALD 166
Cdd:PLN03073 323 RAASILAGLSFTPEMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLD 376
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
135-207 |
3.34e-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: 40.63 E-value: 3.34e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446491464 135 LSGGQQQRVGVARALAADPQVLLMDEPFGALDPVTRGALQQEMTRIHRLLGRTIVLVTHDIDEALRLAEHLVL 207
Cdd:cd03222 72 LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTALVVEHDLAVLDYLSDRIHV 144
|
|
| PRK01862 |
PRK01862 |
voltage-gated chloride channel ClcB; |
243-308 |
4.56e-04 |
|
voltage-gated chloride channel ClcB;
Pssm-ID: 234987 [Multi-domain] Cd Length: 574 Bit Score: 41.65 E-value: 4.56e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446491464 243 RLLSLRSVADYVRREeraeGEALAEEMTLRDALSLFVARGCEVLPVVNTQGQPS--GTLHFQDLLEEA 308
Cdd:PRK01862 507 RDTTDKTAADYAHTP----FPLLTPDMPLGDALEHFMAFQGERLPVVESEASPTlaGVVYKTSLLDAY 570
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
22-195 |
1.28e-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: 1.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 22 LNFQEGSFsVLIGTSGSGKSTTL---------------KMINRLVEHDSG------EIRFAGEEIRslpvleLRRRMGYA 80
Cdd:COG0419 19 IDFDDGLN-LIVGPNGAGKSTILeairyalygkarsrsKLRSDLINVGSEeasvelEFEHGGKRYR------IERRQGEF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 81 IQSIGLFPHwSVAQNIATVPQLQKWSRAR---------IDDRIDELMALLGLESNLRERY-----PHQLSGGQQQRVGVA 146
Cdd:COG0419 92 AEFLEAKPS-ERKEALKRLLGLEIYEELKerlkeleeaLESALEELAELQKLKQEILAQLsgldpIETLSGGERLRLALA 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 446491464 147 RALAadpqvLLMDepFGALDPVTRGALQQEMtrihrllgRTIVLVTHDI 195
Cdd:COG0419 171 DLLS-----LILD--FGSLDEERLERLLDAL--------EELAIITHVI 204
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
20-166 |
1.36e-03 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 39.39 E-value: 1.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 20 LNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEH--DSGEIRFAGEEIRSlpvLELRRRMG--------YAIQSIGLFPH 89
Cdd:PRK09580 20 LNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDYevTGGTVEFKGKDLLE---LSPEDRAGegifmafqYPVEIPGVSNQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 90 WSVAQNIATV---PQLQKWSRARIDDRIDELMALLGLESNLRERYPHQ-LSGGQQQRVGVARALAADPQVLLMDEPFGAL 165
Cdd:PRK09580 97 FFLQTALNAVrsyRGQEPLDRFDFQDLMEEKIALLKMPEDLLTRSVNVgFSGGEKKRNDILQMAVLEPELCILDESDSGL 176
|
.
gi 446491464 166 D 166
Cdd:PRK09580 177 D 177
|
|
| COG2905 |
COG2905 |
Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains ... |
180-305 |
1.45e-03 |
|
Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains [Signal transduction mechanisms];
Pssm-ID: 442149 [Multi-domain] Cd Length: 124 Bit Score: 37.89 E-value: 1.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 180 IHRLLGRTIVLVTHD--IDEALRL-AEH----LVLMDHgevvqQGNPLTMLTRpaNDFVRQFFGRselGVRLLSLRsVAD 252
Cdd:COG2905 1 VKDIMSRDVVTVSPDatVREAARLmTEKgvgsLVVVDD-----DGRLVGIITD--RDLRRRVLAE---GLDPLDTP-VSE 69
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 446491464 253 YVRREERAegeaLAEEMTLRDALSLFVARGCEVLPVVNtQGQPSGTLHFQDLL 305
Cdd:COG2905 70 VMTRPPIT----VSPDDSLAEALELMEEHRIRHLPVVD-DGKLVGIVSITDLL 117
|
|
| COG3448 |
COG3448 |
CBS-domain-containing membrane protein [Signal transduction mechanisms]; |
177-305 |
1.55e-03 |
|
CBS-domain-containing membrane protein [Signal transduction mechanisms];
Pssm-ID: 442671 [Multi-domain] Cd Length: 136 Bit Score: 37.92 E-value: 1.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 177 MTRIHRLLGRTIVLVTHD--IDEALRL-AEH-----LVLMDHGEVVqqGnpltMLTRpaNDFVRQFFGRSELGV-RLLSL 247
Cdd:COG3448 1 AMTVRDIMTRDVVTVSPDttLREALELmREHgirglPVVDEDGRLV--G----IVTE--RDLLRALLPDRLDELeERLLD 72
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 446491464 248 RSVADYVRREERAegeaLAEEMTLRDALSLFVARGCEVLPVVNTQGQPSGTLHFQDLL 305
Cdd:COG3448 73 LPVEDVMTRPVVT----VTPDTPLEEAAELMLEHGIHRLPVVDDDGRLVGIVTRTDLL 126
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
135-219 |
3.82e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 38.84 E-value: 3.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446491464 135 LSGGQQQRVGVARAL---AADPQVLLMDEPFGAL--DPVtrgalQQEMTRIHRL--LGRTIVLVTHDIDeALRLAEHLVL 207
Cdd:TIGR00630 830 LSGGEAQRIKLAKELskrSTGRTLYILDEPTTGLhfDDI-----KKLLEVLQRLvdKGNTVVVIEHNLD-VIKTADYIID 903
|
90
....*....|....*...
gi 446491464 208 M-----DH-GEVVQQGNP 219
Cdd:TIGR00630 904 LgpeggDGgGTVVASGTP 921
|
|
| YtoI |
COG4109 |
Predicted transcriptional regulator containing CBS domains [Transcription]; |
250-306 |
4.71e-03 |
|
Predicted transcriptional regulator containing CBS domains [Transcription];
Pssm-ID: 443285 [Multi-domain] Cd Length: 135 Bit Score: 36.81 E-value: 4.71e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 446491464 250 VADYVRREERAegeALAEEMTLRDALSLFVARGCEVLPVVNTQGQPSGTLHFQDLLE 306
Cdd:COG4109 18 VEDIMTLEDVA---TLSEDDTVEDALELLEKTGHSRFPVVDENGRLVGIVTSKDILG 71
|
|
| COG3448 |
COG3448 |
CBS-domain-containing membrane protein [Signal transduction mechanisms]; |
265-308 |
5.48e-03 |
|
CBS-domain-containing membrane protein [Signal transduction mechanisms];
Pssm-ID: 442671 [Multi-domain] Cd Length: 136 Bit Score: 36.38 E-value: 5.48e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 446491464 265 LAEEMTLRDALSLFVARGCEVLPVVNTQGQPSGTLHFQDLLEEA 308
Cdd:COG3448 15 VSPDTTLREALELMREHGIRGLPVVDEDGRLVGIVTERDLLRAL 58
|
|
| CBS_pair_SF |
cd02205 |
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ... |
265-306 |
6.67e-03 |
|
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).
Pssm-ID: 341358 [Multi-domain] Cd Length: 113 Bit Score: 35.68 E-value: 6.67e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 446491464 265 LAEEMTLRDALSLFVARGCEVLPVVNTQGQPSGTLHFQDLLE 306
Cdd:cd02205 7 VDPDTTVREALELMAENGIGALPVVDDDGKLVGIVTERDILR 48
|
|
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