|
Name |
Accession |
Description |
Interval |
E-value |
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
1-308 |
2.18e-177 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 492.30 E-value: 2.18e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 1 MIEFLDVSKTFA-GRPAASHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEIRSLPVLELRRRMGY 79
Cdd:COG1125 1 MIEFENVTKRYPdGTVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRDLDPVELRRRIGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 80 AIQSIGLFPHWTVAQNIATVLQLEKWSRANIADRVDELMALLGLEPA-LRDRYPHQLSGGQQQRVGVARALAANPQVLLM 158
Cdd:COG1125 81 VIQQIGLFPHMTVAENIATVPRLLGWDKERIRARVDELLELVGLDPEeYRDRYPHELSGGQQQRVGVARALAADPPILLM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 159 DEPFGALDPVTRGALQAEMTRIHRILGRTIVLVTHDIDEALRLADHLVLMDHGEVVQQGSPLELLTWPKNDFVREFFGRS 238
Cdd:COG1125 161 DEPFGALDPITREQLQDELLRLQRELGKTIVFVTHDIDEALKLGDRIAVMREGRIVQYDTPEEILANPANDFVADFVGAD 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 239 ElGVRLLSLRTVSDYMRREEMPVSgeplqEQMSLRDALSAFVARQCEVLPVSDARGAPCGTLHFRDLLAG 308
Cdd:COG1125 241 R-GLRRLSLLRVEDLMLPEPPTVS-----PDASLREALSLMLERGVDWLLVVDEDGRPLGWLTLEDLLRA 304
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
2-241 |
5.65e-147 |
|
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: 412.85 E-value: 5.65e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 2 IEFLDVSKTFAG-RPAASHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEIRSLPVLELRRRMGYA 80
Cdd:cd03295 1 IEFENVTKRYGGgKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 81 IQSIGLFPHWTVAQNIATVLQLEKWSRANIADRVDELMALLGLEPA-LRDRYPHQLSGGQQQRVGVARALAANPQVLLMD 159
Cdd:cd03295 81 IQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLDPAeFADRYPHELSGGQQQRVGVARALAADPPLLLMD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 160 EPFGALDPVTRGALQAEMTRIHRILGRTIVLVTHDIDEALRLADHLVLMDHGEVVQQGSPLELLTWPKNDFVREFFGRSE 239
Cdd:cd03295 161 EPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDFVAEFVGADR 240
|
..
gi 772671321 240 LG 241
Cdd:cd03295 241 LL 242
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-238 |
4.18e-95 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 285.45 E-value: 4.18e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 1 MIEFLDVSKTFAGRPAASHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEIRSLPVlElRRRMGYA 80
Cdd:COG3842 5 ALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPP-E-KRNVGMV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 81 IQSIGLFPHWTVAQNIATVLQLEKWSRANIADRVDELMALLGLEpALRDRYPHQLSGGQQQRVGVARALAANPQVLLMDE 160
Cdd:COG3842 83 FQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLE-GLADRYPHQLSGGQQQRVALARALAPEPRVLLLDE 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 772671321 161 PFGALDPVTRGALQAEMTRIHRILGRTIVLVTHDIDEALRLADHLVLMDHGEVVQQGSPLELLTWPKNDFVREFFGRS 238
Cdd:COG3842 162 PLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEIYERPATRFVADFIGEA 239
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
9-258 |
2.37e-89 |
|
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: 271.34 E-value: 2.37e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 9 KTFAGRPAASHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEIRSLPVLEL----RRRMGYAIQSI 84
Cdd:TIGR01186 1 KKTGGKKGVNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEPTAGQIFIDGENIMKQSPVELrevrRKKIGMVFQQF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 85 GLFPHWTVAQNIATVLQLEKWSRANIADRVDELMALLGLePALRDRYPHQLSGGQQQRVGVARALAANPQVLLMDEPFGA 164
Cdd:TIGR01186 81 ALFPHMTILQNTSLGPELLGWPEQERKEKALELLKLVGL-EEYEHRYPDELSGGMQQRVGLARALAAEPDILLMDEAFSA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 165 LDPVTRGALQAEMTRIHRILGRTIVLVTHDIDEALRLADHLVLMDHGEVVQQGSPLELLTWPKNDFVREFFGrselGVRL 244
Cdd:TIGR01186 160 LDPLIRDSMQDELKKLQATLQKTIVFITHDLDEAIRIGDRIVIMKAGEIVQVGTPDEILRNPANEYVEEFIG----KVDL 235
|
250
....*....|....
gi 772671321 245 LSLRTVSDYMRREE 258
Cdd:TIGR01186 236 SQVFDAERIAQRMN 249
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
2-236 |
1.83e-87 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 265.86 E-value: 1.83e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 2 IEFLDVSKTFAGRPAASHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEIRS-LPVLElrRRMGYA 80
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFTnLPPRE--RRVGFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 81 IQSIGLFPHWTVAQNIATVLQLEKWSRANIADRVDELMALLGLEPaLRDRYPHQLSGGQQQRVGVARALAANPQVLLMDE 160
Cdd:COG1118 81 FQHYALFPHMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEG-LADRYPSQLSGGQRQRVALARALAVEPEVLLLDE 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 772671321 161 PFGALDPVTRGALQAEMTRIHRILGRTIVLVTHDIDEALRLADHLVLMDHGEVVQQGSPLELLTWPKNDFVREFFG 236
Cdd:COG1118 160 PFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDRPATPFVARFLG 235
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-236 |
2.52e-85 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 260.39 E-value: 2.52e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 1 MIEFLDVSKTFAGRPAASHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEIRSLPVLElrRRMGYA 80
Cdd:COG3839 3 SLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKD--RNIAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 81 IQSIGLFPHWTVAQNIATVLQLEKWSRANIADRVDELMALLGLEPALrDRYPHQLSGGQQQRVGVARALAANPQVLLMDE 160
Cdd:COG3839 81 FQSYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLL-DRKPKQLSGGQRQRVALGRALVREPKVFLLDE 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 772671321 161 PFGALDPVTRGALQAEMTRIHRILGRTIVLVTHDIDEALRLADHLVLMDHGEVVQQGSPLELLTWPKNDFVREFFG 236
Cdd:COG3839 160 PLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGTPEELYDRPANLFVAGFIG 235
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
21-307 |
6.26e-84 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 258.11 E-value: 6.26e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 21 NLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEIRSLPVLEL----RRRMGYAIQSIGLFPHWTVAQNI 96
Cdd:COG4175 47 SFDVEEGEIFVIMGLSGSGKSTLVRCLNRLIEPTAGEVLIDGEDITKLSKKELrelrRKKMSMVFQHFALLPHRTVLENV 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 97 ATVLQLEKWSRANIADRVDELMALLGLEpALRDRYPHQLSGGQQQRVGVARALAANPQVLLMDEPFGALDPVTRGALQAE 176
Cdd:COG4175 127 AFGLEIQGVPKAERRERAREALELVGLA-GWEDSYPDELSGGMQQRVGLARALATDPDILLMDEAFSALDPLIRREMQDE 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 177 MTRIHRILGRTIVLVTHDIDEALRLADHLVLMDHGEVVQQGSPLELLTWPKNDFVREFFGrselGVRLLSLRTVSDYMRR 256
Cdd:COG4175 206 LLELQAKLKKTIVFITHDLDEALRLGDRIAIMKDGRIVQIGTPEEILTNPANDYVADFVE----DVDRSKVLTAGSVMRP 281
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 772671321 257 EEmpvsgEPLQEQMSLRDALSAFVARQCEVLPVSDARGAPCGTLHFRDLLA 307
Cdd:COG4175 282 PE-----AVVSEKDGPRVALRRMREEGISSLYVVDRDRRLLGVVTADDALE 327
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
2-217 |
2.56e-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: 2.56e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 2 IEFLDVSKTFAGRPAASHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEIRSLPVLelRRRMGYAI 81
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE--RRNIGMVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 82 QSIGLFPHWTVAQNIATVLQLEKWSRANIADRVDELMALLGLEPaLRDRYPHQLSGGQQQRVGVARALAANPQVLLMDEP 161
Cdd:cd03259 79 QDYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEG-LLNRYPHELSGGQQQRVALARALAREPSLLLLDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 772671321 162 FGALDPVTRGALQAEMTRIHRILGRTIVLVTHDIDEALRLADHLVLMDHGEVVQQG 217
Cdd:cd03259 158 LSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
6-235 |
1.39e-80 |
|
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: 245.63 E-value: 1.39e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 6 DVSKTFAGRPAASHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEIRSLP---VLELRR-RMGYAI 81
Cdd:cd03294 29 EILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSrkeLRELRRkKISMVF 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 82 QSIGLFPHWTVAQNIATVLQLEKWSRANIADRVDELMALLGLEPALrDRYPHQLSGGQQQRVGVARALAANPQVLLMDEP 161
Cdd:cd03294 109 QSFALLPHRTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWE-HKYPDELSGGMQQRVGLARALAVDPDILLMDEA 187
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 772671321 162 FGALDPVTRGALQAEMTRIHRILGRTIVLVTHDIDEALRLADHLVLMDHGEVVQQGSPLELLTWPKNDFVREFF 235
Cdd:cd03294 188 FSALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDYVREFF 261
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-211 |
5.71e-80 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 243.46 E-value: 5.71e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 1 MIEFLDVSKTFA----GRPAASHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEeirslPVLELRRR 76
Cdd:COG1116 7 ALELRGVSKRFPtgggGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGK-----PVTGPGPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 77 MGYAIQSIGLFPHWTVAQNIATVLQLEKWSRANIADRVDELMALLGLEPAlRDRYPHQLSGGQQQRVGVARALAANPQVL 156
Cdd:COG1116 82 RGVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGF-EDAYPHQLSGGMRQRVAIARALANDPEVL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 772671321 157 LMDEPFGALDPVTRGALQAEMTRIHRILGRTIVLVTHDIDEALRLADHLVLMDHG 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 |
3.63e-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: 237.91 E-value: 3.63e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 2 IEFLDVSKTFAGRPAASHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEIRSLPVLelRRRMGYAI 81
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPH--KRPVNTVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 82 QSIGLFPHWTVAQNIATVLQLEKWSRANIADRVDELMALLGLEpALRDRYPHQLSGGQQQRVGVARALAANPQVLLMDEP 161
Cdd:cd03300 79 QNYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLE-GYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEP 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 772671321 162 FGALDPVTRGALQAEMTRIHRILGRTIVLVTHDIDEALRLADHLVLMDHGEVVQQGSPLELLTWPKNDFVREFFG 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 |
3.70e-77 |
|
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: 235.06 E-value: 3.70e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 2 IEFLDVSKTFAGRPAA----SHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEeirslPVLELRRRM 77
Cdd:cd03293 1 LEVRNVSKTYGGGGGAvtalEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGE-----PVTGPGPDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 78 GYAIQSIGLFPHWTVAQNIATVLQLEKWSRANIADRVDELMALLGLEpALRDRYPHQLSGGQQQRVGVARALAANPQVLL 157
Cdd:cd03293 76 GYVFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLS-GFENAYPHQLSGGMRQRVALARALAVDPDVLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 772671321 158 MDEPFGALDPVTRGALQAEMTRIHRILGRTIVLVTHDIDEALRLADHLVLM 208
Cdd:cd03293 155 LDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVL 205
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-235 |
7.57e-73 |
|
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: 224.47 E-value: 7.57e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 1 MIEFLDVSKTFAGRPAASHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEIRSLPV---LELRRRM 77
Cdd:COG1127 5 MIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEkelYELRRRI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 78 GYAIQSIGLFPHWTVAQNIATVL-QLEKWSRANIADRVDELMALLGLEPAlRDRYPHQLSGGQQQRVGVARALAANPQVL 156
Cdd:COG1127 85 GMLFQGGALFDSLTVFENVAFPLrEHTDLSEAEIRELVLEKLELVGLPGA-ADKMPSELSGGMRKRVALARALALDPEIL 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 772671321 157 LMDEPFGALDPVTRGALQAEMTRIHRILGRTIVLVTHDIDEALRLADHLVLMDHGEVVQQGSPLELLTwPKNDFVREFF 235
Cdd:COG1127 164 LYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLA-SDDPWVRQFL 241
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1-236 |
1.73e-72 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 227.27 E-value: 1.73e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 1 MIEFLDVSKTFAGRPAASH----LNLNFAEGA-FSVlIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEIRSLPVLEL-- 73
Cdd:COG1135 1 MIELENLSKTFPTKGGPVTalddVSLTIEKGEiFGI-IGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELra 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 74 -RRRMGYAIQSIGLFPHWTVAQNIATVLQLEKWSRANIADRVDELMALLGLEpALRDRYPHQLSGGQQQRVGVARALAAN 152
Cdd:COG1135 80 aRRKIGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLS-DKADAYPSQLSGGQKQRVGIARALANN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 153 PQVLLMDEPFGALDPVTRGALQAEMTRIHRILGRTIVLVTHDIDEALRLADHLVLMDHGEVVQQGSPLELLTWPKNDFVR 232
Cdd:COG1135 159 PKVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVLDVFANPQSELTR 238
|
....
gi 772671321 233 EFFG 236
Cdd:COG1135 239 RFLP 242
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
1-237 |
2.84e-71 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 220.64 E-value: 2.84e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 1 MIEFLDVSKTFAGRPAASHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEI--RSLPVLELRRRMG 78
Cdd:COG1126 1 MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLtdSKKDINKLRRKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 79 YAIQSIGLFPHWTVAQNIA----TVLqleKWSRANIADRVDELMALLGLEpALRDRYPHQLSGGQQQRVGVARALAANPQ 154
Cdd:COG1126 81 MVFQQFNLFPHLTVLENVTlapiKVK---KMSKAEAEERAMELLERVGLA-DKADAYPAQLSGGQQQRVAIARALAMEPK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 155 VLLMDEPFGALDPvtrgalqaEMTRIhrIL---------GRTIVLVTHDIDEALRLADHLVLMDHGEVVQQGSPLELLTW 225
Cdd:COG1126 157 VMLFDEPTSALDP--------ELVGE--VLdvmrdlakeGMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFEN 226
|
250
....*....|..
gi 772671321 226 PKNDFVREFFGR 237
Cdd:COG1126 227 PQHERTRAFLSK 238
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
2-236 |
9.48e-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: 219.13 E-value: 9.48e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 2 IEFLDVSKTFAGRPAASHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEIRSLPVLElrRRMGYAI 81
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQE--RNVGFVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 82 QSIGLFPHWTVAQNIATVLQL----EKWSRANIADRVDELMALLGLEpALRDRYPHQLSGGQQQRVGVARALAANPQVLL 157
Cdd:cd03296 81 QHYALFRHMTVFDNVAFGLRVkprsERPPEAEIRAKVHELLKLVQLD-WLADRYPAQLSGGQRQRVALARALAVEPKVLL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 772671321 158 MDEPFGALDPVTRGALQAEMTRIHRILGRTIVLVTHDIDEALRLADHLVLMDHGEVVQQGSPLELLTWPKNDFVREFFG 236
Cdd:cd03296 160 LDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPASPFVYSFLG 238
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
2-236 |
3.21e-70 |
|
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 217.75 E-value: 3.21e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 2 IEFLDVSKTFAGRPAASHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEIRSLPVLelRRRMGYAI 81
Cdd:TIGR00968 1 IEIANISKRFGSFQALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGLEQPDSGRIRLNGQDATRVHAR--DRKIGFVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 82 QSIGLFPHWTVAQNIATVLQLEKWSRANIADRVDELMALLGLEpALRDRYPHQLSGGQQQRVGVARALAANPQVLLMDEP 161
Cdd:TIGR00968 79 QHYALFKHLTVRDNIAFGLEIRKHPKAKIKARVEELLELVQLE-GLGDRYPNQLSGGQRQRVALARALAVEPQVLLLDEP 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 772671321 162 FGALDPVTRGALQAEMTRIHRILGRTIVLVTHDIDEALRLADHLVLMDHGEVVQQGSPLELLTWPKNDFVREFFG 236
Cdd:TIGR00968 158 FGALDAKVRKELRSWLRKLHDEVHVTTVFVTHDQEEAMEVADRIVVMSNGKIEQIGSPDEVYDHPANPFVMSFLG 232
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1-227 |
3.70e-70 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 217.45 E-value: 3.70e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 1 MIEFLDVSKTFAGR----PAASHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEIRSLPVLEL--- 73
Cdd:cd03258 1 MIELKNVSKVFGDTggkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELrka 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 74 RRRMGYAIQSIGLFPHWTVAQNIATVLQLEKWSRANIADRVDELMALLGLEpALRDRYPHQLSGGQQQRVGVARALAANP 153
Cdd:cd03258 81 RRRIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLE-DKADAYPAQLSGGQKQRVGIARALANNP 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 772671321 154 QVLLMDEPFGALDPVTRGALQAEMTRIHRILGRTIVLVTHDIDEALRLADHLVLMDHGEVVQQGSPLELLTWPK 227
Cdd:cd03258 160 KVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFANPQ 233
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
2-217 |
1.71e-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: 210.19 E-value: 1.71e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 2 IEFLDVSKTFAGRPAASHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEIRSLPVLElrRRMGYAI 81
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKD--RDIAMVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 82 QSIGLFPHWTVAQNIATVLQLEKWSRANIADRVDELMALLGLEpALRDRYPHQLSGGQQQRVGVARALAANPQVLLMDEP 161
Cdd:cd03301 79 QNYALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIE-HLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 772671321 162 FGALDPVTRGALQAEMTRIHRILGRTIVLVTHDIDEALRLADHLVLMDHGEVVQQG 217
Cdd:cd03301 158 LSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
2-223 |
3.29e-67 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 209.92 E-value: 3.29e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 2 IEFLDVSKTFAGRPAASHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEIRSLPVlELRRRMGYAI 81
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPA-EVRRRIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 82 QSIGLFPHWTVAQNIATVLQLEKWSRANIADRVDELMALLGLEPAlRDRYPHQLSGGQQQRVGVARALAANPQVLLMDEP 161
Cdd:COG1131 80 QEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDA-ADRKVGTLSGGMKQRLGLALALLHDPELLILDEP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 772671321 162 FGALDPVTRGALQAEMTRIHRiLGRTIVLVTHDIDEALRLADHLVLMDHGEVVQQGSPLELL 223
Cdd:COG1131 159 TSGLDPEARRELWELLRELAA-EGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELK 219
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
6-237 |
3.92e-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: 213.75 E-value: 3.92e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 6 DVSKTFAGRPAASHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEIRSLPVLelRRRMGYAIQSIG 85
Cdd:TIGR03265 9 NIRKRFGAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRLPPQ--KRDYGIVFQSYA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 86 LFPHWTVAQNIATVLQLEKWSRANIADRVDELMALLGLePALRDRYPHQLSGGQQQRVGVARALAANPQVLLMDEPFGAL 165
Cdd:TIGR03265 87 LFPNLTVADNIAYGLKNRGMGRAEVAERVAELLDLVGL-PGSERKYPGQLSGGQQQRVALARALATSPGLLLLDEPLSAL 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 772671321 166 DPVTRGALQAEMTRIHRILGRTIVLVTHDIDEALRLADHLVLMDHGEVVQQGSPLELLTWPKNDFVREFFGR 237
Cdd:TIGR03265 166 DARVREHLRTEIRQLQRRLGVTTIMVTHDQEEALSMADRIVVMNHGVIEQVGTPQEIYRHPATPFVADFVGE 237
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
20-236 |
9.49e-67 |
|
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: 209.11 E-value: 9.49e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 20 LNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEIRSLPvlELRRRMGYAIQSIGLFPHWTVAQNIATV 99
Cdd:cd03299 18 VSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLP--PEKRDISYVPQNYALFPHMTVYKNIAYG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 100 LQLEKWSRANIADRVDELMALLGLEPALrDRYPHQLSGGQQQRVGVARALAANPQVLLMDEPFGALDPVTRGALQAEMTR 179
Cdd:cd03299 96 LKKRKVDKKEIERKVLEIAEMLGIDHLL-NRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLREELKK 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 772671321 180 IHRILGRTIVLVTHDIDEALRLADHLVLMDHGEVVQQGSPLELLTWPKNDFVREFFG 236
Cdd:cd03299 175 IRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPKNEFVAEFLG 231
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-233 |
1.91e-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: 216.69 E-value: 1.91e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 1 MIEFLDVSKTFAGR-----PAASHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEIRSLP---VLE 72
Cdd:COG1123 260 LLEVRNLSKRYPVRgkggvRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSrrsLRE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 73 LRRRMGYAIQ----SigLFPHWTVAQNIATVLQL-EKWSRANIADRVDELMALLGLEPALRDRYPHQLSGGQQQRVGVAR 147
Cdd:COG1123 340 LRRRVQMVFQdpysS--LNPRMTVGDIIAEPLRLhGLLSRAERRERVAELLERVGLPPDLADRYPHELSGGQRQRVAIAR 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 148 ALAANPQVLLMDEPFGALDPVTRGALQAEMTRIHRILGRTIVLVTHDIDEALRLADHLVLMDHGEVVQQGSPLELLTWPK 227
Cdd:COG1123 418 ALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVFANPQ 497
|
....*.
gi 772671321 228 NDFVRE 233
Cdd:COG1123 498 HPYTRA 503
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
2-236 |
2.44e-66 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 212.50 E-value: 2.44e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 2 IEFLDVSKTFAGRPAASHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEIRSLPVLelRRRMGYAI 81
Cdd:PRK09452 15 VELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAE--NRHVNTVF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 82 QSIGLFPHWTVAQNIATVLQLEKWSRANIADRVDELMALLGLEpALRDRYPHQLSGGQQQRVGVARALAANPQVLLMDEP 161
Cdd:PRK09452 93 QSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLE-EFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDES 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 772671321 162 FGALDPVTRGALQAEMTRIHRILGRTIVLVTHDIDEALRLADHLVLMDHGEVVQQGSPLELLTWPKNDFVREFFG 236
Cdd:PRK09452 172 LSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNLFVARFIG 246
|
|
| tungstate_WtpC |
NF040840 |
tungstate ABC transporter ATP-binding protein WtpC; |
1-236 |
5.07e-66 |
|
tungstate ABC transporter ATP-binding protein WtpC;
Pssm-ID: 468779 [Multi-domain] Cd Length: 347 Bit Score: 210.70 E-value: 5.07e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 1 MIEFLDVSKTFAGRPAAShLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEIRSLPvLElRRRMGYA 80
Cdd:NF040840 1 MIRIENLSKDWKEFKLRD-ISLEVKEGEYFIILGPSGAGKTVLLELIAGIWPPDSGKIYLDGKDITNLP-PE-KRGIAYV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 81 IQSIGLFPHWTVAQNIATVLQLEKWSRANIADRVDELMALLGLEpALRDRYPHQLSGGQQQRVGVARALAANPQVLLMDE 160
Cdd:NF040840 78 YQNYMLFPHKTVFENIAFGLKLRKVPKEEIERKVKEIMELLGIS-HLLHRKPRTLSGGEQQRVALARALIIEPKLLLLDE 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 772671321 161 PFGALDPVTRGALQAEMTRIHRILGRTIVLVTHDIDEALRLADHLVLMDHGEVVQQGSPLELLTWPKNDFVREFFG 236
Cdd:NF040840 157 PLSALDVQTRDELIREMKRWHREFGFTAIHVTHNFEEALSLADRVGIMLNGRLSQVGDVREVFRRPKNEFVARFVG 232
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1-234 |
7.34e-66 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 210.04 E-value: 7.34e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 1 MIEFLDVSKTFAGR----PAASHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEIRSLPVLELRRr 76
Cdd:PRK11153 1 MIELKNISKVFPQGgrtiHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRK- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 77 mgyAIQSIGL-FPHW------TVAQNIATVLQLEKWSRANIADRVDELMALLGLEpALRDRYPHQLSGGQQQRVGVARAL 149
Cdd:PRK11153 80 ---ARRQIGMiFQHFnllssrTVFDNVALPLELAGTPKAEIKARVTELLELVGLS-DKADRYPAQLSGGQKQRVAIARAL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 150 AANPQVLLMDEPFGALDPVTRGALQAEMTRIHRILGRTIVLVTHDIDEALRLADHLVLMDHGEVVQQGSPLELLTWPKND 229
Cdd:PRK11153 156 ASNPKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHPKHP 235
|
....*
gi 772671321 230 FVREF 234
Cdd:PRK11153 236 LTREF 240
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
2-224 |
1.08e-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: 206.03 E-value: 1.08e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 2 IEFLDVSKTFA-GRPAASHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEIRSLPVLELRRRMGYA 80
Cdd:COG1122 1 IELENLSFSYPgGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 81 IQS--IGLF-PhwTVAQNIATVLQLEKWSRANIADRVDELMALLGLEpALRDRYPHQLSGGQQQRVGVARALAANPQVLL 157
Cdd:COG1122 81 FQNpdDQLFaP--TVEEDVAFGPENLGLPREEIRERVEEALELVGLE-HLADRPPHELSGGQKQRVAIAGVLAMEPEVLV 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 772671321 158 MDEPFGALDPVTRGALQAEMTRIHRiLGRTIVLVTHDIDEALRLADHLVLMDHGEVVQQGSPLELLT 224
Cdd:COG1122 158 LDEPTAGLDPRGRRELLELLKRLNK-EGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFS 223
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
2-234 |
1.49e-65 |
|
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: 205.81 E-value: 1.49e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 2 IEFLDVSKTFAGRPAASHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEIRSLPVLEL---RRRMG 78
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELyrlRRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 79 YAIQSIGLFPHWTVAQNIATVL-QLEKWSRANIADRVDELMALLGLEPAlRDRYPHQLSGGQQQRVGVARALAANPQVLL 157
Cdd:cd03261 81 MLFQSGALFDSLTVFENVAFPLrEHTRLSEEEIREIVLEKLEAVGLRGA-EDLYPAELSGGMKKRVALARALALDPELLL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 772671321 158 MDEPFGALDPVTRGALQAEMTRIHRILGRTIVLVTHDIDEALRLADHLVLMDHGEVVQQGSPLELLTWPkNDFVREF 234
Cdd:cd03261 160 YDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRASD-DPLVRQF 235
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1-214 |
7.86e-64 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 201.05 E-value: 7.86e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 1 MIEFLDVSKTFA-GRPAASHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEIRSLP---VLELRRR 76
Cdd:COG2884 1 MIRFENVSKRYPgGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKrreIPYLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 77 MGYAIQSIGLFPHWTVAQNIATVLQLEKWSRANIADRVDELMALLGLEpALRDRYPHQLSGGQQQRVGVARALAANPQVL 156
Cdd:COG2884 81 IGVVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLS-DKAKALPHELSGGEQQRVAIARALVNRPELL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 772671321 157 LMDEPFGALDPVTRGALQAEMTRIHRiLGRTIVLVTHDIDEALRLADHLVLMDHGEVV 214
Cdd:COG2884 160 LADEPTGNLDPETSWEIMELLEEINR-RGTTVLIATHDLELVDRMPKRVLELEDGRLV 216
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
2-212 |
1.54e-63 |
|
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: 198.57 E-value: 1.54e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 2 IEFLDVSKTFAGRPAASHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEIRSL--PVLELRRRMGY 79
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLedELPPLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 80 AIQSIGLFPHWTVAQNIAtvlqlekwsraniadrvdelmallglepalrdrYPhqLSGGQQQRVGVARALAANPQVLLMD 159
Cdd:cd03229 81 VFQDFALFPHLTVLENIA---------------------------------LG--LSGGQQQRVALARALAMDPDVLLLD 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 772671321 160 EPFGALDPVTRGALQAEMTRIHRILGRTIVLVTHDIDEALRLADHLVLMDHGE 212
Cdd:cd03229 126 EPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-216 |
3.59e-63 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 199.50 E-value: 3.59e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 1 MIEFLDVSKTF----AGRPAASHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEIRSLPVLEL--- 73
Cdd:COG1136 4 LLELRNLTKSYgtgeGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELarl 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 74 -RRRMGYAIQSIGLFPHWTVAQNIATVLQLEKWSRANIADRVDELMALLGLEpALRDRYPHQLSGGQQQRVGVARALAAN 152
Cdd:COG1136 84 rRRHIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLG-DRLDHRPSQLSGGQQQRVAIARALVNR 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 772671321 153 PQVLLMDEPFGALDPVTRGALQAEMTRIHRILGRTIVLVTHDiDEALRLADHLVLMDHGEVVQQ 216
Cdd:COG1136 163 PKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHD-PELAARADRVIRLRDGRIVSD 225
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-239 |
7.31e-63 |
|
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: 199.26 E-value: 7.31e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 1 MIEFLDVSKTF----AGRPAASHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEIRSLPVLELRRR 76
Cdd:COG1124 1 MLEVRNLSVSYgqggRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 77 MGYAIQSIG--LFPHWTVAQNIATVLQLEKwsRANIADRVDELMALLGLEPALRDRYPHQLSGGQQQRVGVARALAANPQ 154
Cdd:COG1124 81 VQMVFQDPYasLHPRHTVDRILAEPLRIHG--LPDREERIAELLEQVGLPPSFLDRYPHQLSGGQRQRVAIARALILEPE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 155 VLLMDEPFGALDPVTrgalQAEM----TRIHRILGRTIVLVTHDIDEALRLADHLVLMDHGEVVQQGSPLELLTWPKNDF 230
Cdd:COG1124 159 LLLLDEPTSALDVSV----QAEIlnllKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAGPKHPY 234
|
....*....
gi 772671321 231 VREFFGRSE 239
Cdd:COG1124 235 TRELLAASL 243
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1-236 |
2.62e-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: 195.65 E-value: 2.62e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 1 MIEFLDVSKTFAGRPAASHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEIRSLPVLELRRRMGYA 80
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 81 IQSIGLFPHWTVAQniaTVLQ-----LEKWSRANIADR--VDELMALLGLEpALRDRYPHQLSGGQQQRVGVARALAANP 153
Cdd:COG1120 81 PQEPPAPFGLTVRE---LVALgryphLGLFGRPSAEDReaVEEALERTGLE-HLADRPVDELSGGERQRVLIARALAQEP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 154 QVLLMDEPFGALDPVTRGALQAEMTRIHRILGRTIVLVTHDIDEALRLADHLVLMDHGEVVQQGSPLELLTwpkNDFVRE 233
Cdd:COG1120 157 PLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEVLT---PELLEE 233
|
...
gi 772671321 234 FFG 236
Cdd:COG1120 234 VYG 236
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
32-238 |
4.89e-61 |
|
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: 197.33 E-value: 4.89e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 32 LIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEIRSLPvlELRRRMGYAIQSIGLFPHWTVAQNIATVLQLEKWSRANIA 111
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVP--PHLRHINMVFQSYALFPHMTVEENVAFGLKMRKVPRAEIK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 112 DRVDELMALLGLEpALRDRYPHQLSGGQQQRVGVARALAANPQVLLMDEPFGALDPVTRGALQAEMTRIHRILGRTIVLV 191
Cdd:TIGR01187 79 PRVLEALRLVQLE-EFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITFVFV 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 772671321 192 THDIDEALRLADHLVLMDHGEVVQQGSPLELLTWPKNDFVREFFGRS 238
Cdd:TIGR01187 158 THDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFVARFIGEI 204
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
2-236 |
4.01e-60 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 195.69 E-value: 4.01e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 2 IEFLDVSKTFAGRPAASHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEIRSLPVLElrRRMGYAI 81
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARD--RKVGFVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 82 QSIGLFPHWTVAQNIA---TVL-QLEKWSRANIADRVDELMALLGLEpALRDRYPHQLSGGQQQRVGVARALAANPQVLL 157
Cdd:PRK10851 81 QHYALFRHMTVFDNIAfglTVLpRRERPNAAAIKAKVTQLLEMVQLA-HLADRYPAQLSGGQKQRVALARALAVEPQILL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 772671321 158 MDEPFGALDPVTRGALQAEMTRIHRILGRTIVLVTHDIDEALRLADHLVLMDHGEVVQQGSPLELLTWPKNDFVREFFG 236
Cdd:PRK10851 160 LDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREPATRFVLEFMG 238
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
6-236 |
2.37e-59 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 194.09 E-value: 2.37e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 6 DVSKTFAGRPAASHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEIRSLPVLElrRRMGYAIQSIG 85
Cdd:PRK11000 8 NVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAE--RGVGMVFQSYA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 86 LFPHWTVAQNIATVLQLEKWSRANIADRVDELMALLGLEpALRDRYPHQLSGGQQQRVGVARALAANPQVLLMDEPFGAL 165
Cdd:PRK11000 86 LYPHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLA-HLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNL 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 772671321 166 DPVTRGALQAEMTRIHRILGRTIVLVTHDIDEALRLADHLVLMDHGEVVQQGSPLELLTWPKNDFVREFFG 236
Cdd:PRK11000 165 DAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPANRFVAGFIG 235
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
2-213 |
1.16e-58 |
|
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: 187.70 E-value: 1.16e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 2 IEFLDVSKTFAG----RPAASHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEIRSLPVLEL---- 73
Cdd:cd03255 1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 74 RRRMGYAIQSIGLFPHWTVAQNIATVLQLEKWSRANIADRVDELMALLGLEpALRDRYPHQLSGGQQQRVGVARALAANP 153
Cdd:cd03255 81 RRHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLG-DRLNHYPSELSGGQQQRVAIARALANDP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 154 QVLLMDEPFGALDPVTRGALQAEMTRIHRILGRTIVLVTHDIDEAlRLADHLVLMDHGEV 213
Cdd:cd03255 160 KIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELA-EYADRIIELRDGKI 218
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
2-213 |
1.79e-58 |
|
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: 186.97 E-value: 1.79e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 2 IEFLDVSKTFAGRPAASHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEI--RSLPVLELRRRMGY 79
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLtdDKKNINELRQKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 80 AIQSIGLFPHWTVAQNIATVL-QLEKWSRANIADRVDELMALLGLEPAlRDRYPHQLSGGQQQRVGVARALAANPQVLLM 158
Cdd:cd03262 81 VFQQFNLFPHLTVLENITLAPiKVKGMSKAEAEERALELLEKVGLADK-ADAYPAQLSGGQQQRVAIARALAMNPKVMLF 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 772671321 159 DEPFGALDPVTRGALQAEMTRIHRiLGRTIVLVTHDIDEALRLADHLVLMDHGEV 213
Cdd:cd03262 160 DEPTSALDPELVGEVLDVMKDLAE-EGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-227 |
1.03e-57 |
|
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: 193.58 E-value: 1.03e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 1 MIEFLDVSKTFAG--RPAASHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHD---SGMIRFAGEEIRSLPVLELRR 75
Cdd:COG1123 4 LLEVRDLSVRYPGgdVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRGR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 76 RMGYAIQSIG--LFPhWTVAQNIATVLQLEKWSRANIADRVDELMALLGLEpALRDRYPHQLSGGQQQRVGVARALAANP 153
Cdd:COG1123 84 RIGMVFQDPMtqLNP-VTVGDQIAEALENLGLSRAEARARVLELLEAVGLE-RRLDRYPHQLSGGQRQRVAIAMALALDP 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 772671321 154 QVLLMDEPFGALDPVTRGALQAEMTRIHRILGRTIVLVTHDIDEALRLADHLVLMDHGEVVQQGSPLELLTWPK 227
Cdd:COG1123 162 DLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAPQ 235
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1-223 |
2.57e-57 |
|
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: 185.06 E-value: 2.57e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 1 MIEFLDVSKTFAGRPAASHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEIRSLPvLELRRRMGYA 80
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEP-REARRQIGVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 81 IQSIGLFPHWTVAQNIATVLQLEKWSRANIADRVDELMALLGLEPaLRDRYPHQLSGGQQQRVGVARALAANPQVLLMDE 160
Cdd:COG4555 80 PDERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEE-FLDRRVGELSTGMKKKVALARALVHDPKVLLLDE 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 772671321 161 PFGALDPVTRGALQAEMTRiHRILGRTIVLVTHDIDEALRLADHLVLMDHGEVVQQGSPLELL 223
Cdd:COG4555 159 PTNGLDVMARRLLREILRA-LKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELR 220
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1-217 |
2.80e-57 |
|
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: 184.25 E-value: 2.80e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 1 MIEFLDVSKTFAGR----PAASHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEIRSLPvLELRRR 76
Cdd:cd03257 1 LLEVKNLSVSFPTGggsvKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLS-RRLRKI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 77 MGYAIQSIG------LFPHWTVAQNIATVLQLEK--WSRANIADRVDELMALLGLEPALRDRYPHQLSGGQQQRVGVARA 148
Cdd:cd03257 80 RRKEIQMVFqdpmssLNPRMTIGEQIAEPLRIHGklSKKEARKEAVLLLLVGVGLPEEVLNRYPHELSGGQRQRVAIARA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 772671321 149 LAANPQVLLMDEPFGALDPVTRGALQAEMTRIHRILGRTIVLVTHDIDEALRLADHLVLMDHGEVVQQG 217
Cdd:cd03257 160 LALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1-234 |
6.47e-57 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 183.76 E-value: 6.47e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 1 MIEFLDVSKTFAGRPAASHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEIR--SLPVLELRRRMG 78
Cdd:PRK09493 1 MIEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNdpKVDERLIRQEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 79 YAIQSIGLFPHWTVAQNIA-TVLQLEKWSRANIADRVDELMALLGLEpALRDRYPHQLSGGQQQRVGVARALAANPQVLL 157
Cdd:PRK09493 81 MVFQQFYLFPHLTALENVMfGPLRVRGASKEEAEKQARELLAKVGLA-ERAHHYPSELSGGQQQRVAIARALAVKPKLML 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 158 MDEPFGALDPvtrgALQAEMTRIHRIL---GRTIVLVTHDIDEALRLADHLVLMDHGEVVQQGSPLELLTWPKNDFVREF 234
Cdd:PRK09493 160 FDEPTSALDP----ELRHEVLKVMQDLaeeGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPPSQRLQEF 235
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
1-244 |
1.81e-56 |
|
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: 186.46 E-value: 1.81e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 1 MIEfLDVSKTFAGrpaaSHLNLNFA--EGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGE------EIRSLPVLe 72
Cdd:COG4148 2 MLE-VDFRLRRGG----FTLDVDFTlpGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEvlqdsaRGIFLPPH- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 73 lRRRMGYAIQSIGLFPHWTVAQNIatvlqLEKWSRANIADR---VDELMALLGLEPaLRDRYPHQLSGGQQQRVGVARAL 149
Cdd:COG4148 76 -RRRIGYVFQEARLFPHLSVRGNL-----LYGRKRAPRAERrisFDEVVELLGIGH-LLDRRPATLSGGERQRVAIGRAL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 150 AANPQVLLMDEPFGALDPVTRGALQAEMTRIHRILGRTIVLVTHDIDEALRLADHLVLMDHGEVVQQGSPLELLTWPKnd 229
Cdd:COG4148 149 LSSPRLLLMDEPLAALDLARKAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRPD-- 226
|
250
....*....|....*
gi 772671321 230 fVREFFGRSELGVRL 244
Cdd:COG4148 227 -LLPLAGGEEAGSVL 240
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1-236 |
2.11e-56 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 186.96 E-value: 2.11e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 1 MIEFLDVSKTFAGRPAASHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEIRSLPvlELRRRMGYA 80
Cdd:PRK11607 19 LLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVP--PYQRPINMM 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 81 IQSIGLFPHWTVAQNIATVLQLEKWSRANIADRVDELMALLGLEpALRDRYPHQLSGGQQQRVGVARALAANPQVLLMDE 160
Cdd:PRK11607 97 FQSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQ-EFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDE 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 772671321 161 PFGALDPVTRGALQAEMTRIHRILGRTIVLVTHDIDEALRLADHLVLMDHGEVVQQGSPLELLTWPKNDFVREFFG 236
Cdd:PRK11607 176 PMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAEFIG 251
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
3-212 |
2.28e-56 |
|
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: 181.51 E-value: 2.28e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 3 EFLDVSKTFAG--RPAASHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEIRSLPVLELRRRMGYA 80
Cdd:cd03225 1 ELKNLSFSYPDgaRPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 81 IQsiglFPHW-----TVAQNIATVLQLEKWSRANIADRVDELMALLGLEpALRDRYPHQLSGGQQQRVGVARALAANPQV 155
Cdd:cd03225 81 FQ----NPDDqffgpTVEEEVAFGLENLGLPEEEIEERVEEALELVGLE-GLRDRSPFTLSGGQKQRVAIAGVLAMDPDI 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 772671321 156 LLMDEPFGALDPVTRGALQAEMTRIHRiLGRTIVLVTHDIDEALRLADHLVLMDHGE 212
Cdd:cd03225 156 LLLDEPTAGLDPAGRRELLELLKKLKA-EGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
11-217 |
3.39e-56 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 181.34 E-value: 3.39e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 11 FAGRPAASHLNLNF-AEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAG------EEIRSLPVLelRRRMGYAIQS 83
Cdd:cd03297 6 IEKRLPDFTLKIDFdLNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGtvlfdsRKKINLPPQ--QRKIGLVFQQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 84 IGLFPHWTVAQNIATVLQleKWSRANIADRVDELMALLGLEPaLRDRYPHQLSGGQQQRVGVARALAANPQVLLMDEPFG 163
Cdd:cd03297 84 YALFPHLNVRENLAFGLK--RKRNREDRISVDELLDLLGLDH-LLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFS 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 772671321 164 ALDPVTRGALQAEMTRIHRILGRTIVLVTHDIDEALRLADHLVLMDHGEVVQQG 217
Cdd:cd03297 161 ALDRALRLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
2-224 |
1.07e-53 |
|
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: 176.87 E-value: 1.07e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 2 IEFLDVSKTFAG-----RPAASHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEIRS---LPVLEL 73
Cdd:TIGR04521 1 IKLKNVSYIYQPgtpfeKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAkkkKKLKDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 74 RRRMGYAIQsiglFPHW-----TVAQNIATVLQLEKWSRANIADRVDELMALLGLEPALRDRYPHQLSGGQQQRVGVARA 148
Cdd:TIGR04521 81 RKKVGLVFQ----FPEHqlfeeTVYKDIAFGPKNLGLSEEEAEERVKEALELVGLDEEYLERSPFELSGGQMRRVAIAGV 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 772671321 149 LAANPQVLLMDEPFGALDPVTRGALQAEMTRIHRILGRTIVLVTHDIDEALRLADHLVLMDHGEVVQQGSPLELLT 224
Cdd:TIGR04521 157 LAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVFS 232
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
2-219 |
3.56e-53 |
|
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: 173.91 E-value: 3.56e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 2 IEFLDVSKTFAGRPAASHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEH-----DSGMIRFAGEEIRSL--PVLELR 74
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLipgapDEGEVLLDGKDIYDLdvDVLELR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 75 RRMGYAIQSIGLFPHwTVAQNIATVLQL-EKWSRANIADRVDELMALLGLEPALRDR-YPHQLSGGQQQRVGVARALAAN 152
Cdd:cd03260 81 RRVGMVFQKPNPFPG-SIYDNVAYGLRLhGIKLKEELDERVEEALRKAALWDEVKDRlHALGLSGGQQQRLCLARALANE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 772671321 153 PQVLLMDEPFGALDPVTRGALQAEMTRIHRILgrTIVLVTHDIDEALRLADHLVLMDHGEVVQQGSP 219
Cdd:cd03260 160 PEVLLLDEPTSALDPISTAKIEELIAELKKEY--TIVIVTHNMQQAARVADRTAFLLNGRLVEFGPT 224
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
2-213 |
4.62e-53 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 173.08 E-value: 4.62e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 2 IEFLDVSKTFAGRPAASHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEIRSLPVLELRRRMGYAI 81
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 82 QSIGLFPHwTVAQNIATVLQLEKwsRANIADRVDELMALLGLEPALRDRYPHQLSGGQQQRVGVARALAANPQVLLMDEP 161
Cdd:COG4619 81 QEPALWGG-TVRDNLPFPFQLRE--RKFDRERALELLERLGLPPDILDKPVERLSGGERQRLALIRALLLQPDVLLLDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 772671321 162 FGALDPVTRGALQAEMTRIHRILGRTIVLVTHDIDEALRLADHLVLMDHGEV 213
Cdd:COG4619 158 TSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
1-239 |
4.72e-53 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 174.09 E-value: 4.72e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 1 MIEFLDVSKTFA-GRPAASHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEIRSLP---VLELRRR 76
Cdd:COG3638 2 MLELRNLSKRYPgGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRgraLRRLRRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 77 MGYAIQSIGLFPHWTVAQNI-----------ATVLQLekWSRANIaDRVDELMALLGLEPALRDRyPHQLSGGQQQRVGV 145
Cdd:COG3638 82 IGMIFQQFNLVPRLSVLTNVlagrlgrtstwRSLLGL--FPPEDR-ERALEALERVGLADKAYQR-ADQLSGGQQQRVAI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 146 ARALAANPQVLLMDEPFGALDPVTRGALQAEMTRIHRILGRTIVLVTHDIDEALRLADHLVLMDHGEVVQQGSPLELltw 225
Cdd:COG3638 158 ARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRVVFDGPPAEL--- 234
|
250
....*....|....
gi 772671321 226 pKNDFVREFFGRSE 239
Cdd:COG3638 235 -TDAVLREIYGGEA 247
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-234 |
8.69e-53 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 173.89 E-value: 8.69e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 1 MIEFLDVSKTFAG----RPAASHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEIRSlPVLElrrr 76
Cdd:COG4525 3 MLTVRHVSVRYPGggqpQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTG-PGAD---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 77 MGYAIQSIGLFPHWTVAQNIATVLQLEKWSRANIADRVDELMALLGLEpALRDRYPHQLSGGQQQRVGVARALAANPQVL 156
Cdd:COG4525 78 RGVVFQKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLA-DFARRRIWQLSGGMRQRVGIARALAADPRFL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 157 LMDEPFGALDPVTRGALQAEMTRIHRILGRTIVLVTHDIDEALRLADHLVLMDH--GEVVQQgspLELltwpknDFVREF 234
Cdd:COG4525 157 LMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHSVEEALFLATRLVVMSPgpGRIVER---LEL------DFSRRF 227
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-224 |
1.54e-52 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 172.58 E-value: 1.54e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 1 MIEFLDVSKTFAGRPAASHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEIRslpvlELRRRMGYA 80
Cdd:COG1121 6 AIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPR-----RARRRIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 81 IQSIGL---FPhwtvaqniATVLQ-----------LEKWSRANIADRVDELMALLGLEpALRDRYPHQLSGGQQQRVGVA 146
Cdd:COG1121 81 PQRAEVdwdFP--------ITVRDvvlmgrygrrgLFRRPSRADREAVDEALERVGLE-DLADRPIGELSGGQQQRVLLA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 772671321 147 RALAANPQVLLMDEPFGALDPVTRGALQAEMTRIHRiLGRTIVLVTHDIDEALRLADHLVLMDHGeVVQQGSPLELLT 224
Cdd:COG1121 152 RALAQDPDLLLLDEPFAGVDAATEEALYELLRELRR-EGKTILVVTHDLGAVREYFDRVLLLNRG-LVAHGPPEEVLT 227
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1-237 |
5.16e-52 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 171.09 E-value: 5.16e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 1 MIEFLDVSKTFAGRPAasHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEIRSLPVLElrRRMGYA 80
Cdd:COG3840 1 MLRLDDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAE--RPVSML 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 81 IQSIGLFPHWTVAQNIAtvLQLEKWSRANIADR--VDELMALLGLEpALRDRYPHQLSGGQQQRVGVARALAANPQVLLM 158
Cdd:COG3840 77 FQENNLFPHLTVAQNIG--LGLRPGLKLTAEQRaqVEQALERVGLA-GLLDRLPGQLSGGQRQRVALARCLVRKRPILLL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 159 DEPFGALDPvtrgALQAEM----TRIHRILGRTIVLVTHDIDEALRLADHLVLMDHGEVVQQGSPLELLTWPKNDFVREF 234
Cdd:COG3840 154 DEPFSALDP----ALRQEMldlvDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPPALAAY 229
|
...
gi 772671321 235 FGR 237
Cdd:COG3840 230 LGI 232
|
|
| PhnT |
TIGR03258 |
2-aminoethylphosphonate ABC transport system, ATP-binding component PhnT; This ATP-binding ... |
2-240 |
5.26e-52 |
|
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: 175.18 E-value: 5.26e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 2 IEFLDVSktFAGRPAASHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHD--SGMIRFAGEEIRSLPvlELRRRMGY 79
Cdd:TIGR03258 8 IDHLRVA--YGANTVLDDLSLEIEAGELLALIGKSGCGKTTLLRAIAGFVKAAglTGRIAIADRDLTHAP--PHKRGLAL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 80 AIQSIGLFPHWTVAQNIATVLQLEKWSRANIADRVDELMALLGLEPALRdRYPHQLSGGQQQRVGVARALAANPQVLLMD 159
Cdd:TIGR03258 84 LFQNYALFPHLKVEDNVAFGLRAQKMPKADIAERVADALKLVGLGDAAA-HLPAQLSGGMQQRIAIARAIAIEPDVLLLD 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 160 EPFGALDPVTRGALQAEMTRIHRILGR-TIVLVTHDIDEALRLADHLVLMDHGEVVQQGSPLELLTWPKNDFVREFFGRS 238
Cdd:TIGR03258 163 EPLSALDANIRANMREEIAALHEELPElTILCVTHDQDDALTLADKAGIMKDGRLAAHGEPQALYDAPADGFAAEFLGAA 242
|
..
gi 772671321 239 EL 240
Cdd:TIGR03258 243 NI 244
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
2-213 |
2.52e-50 |
|
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: 164.49 E-value: 2.52e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 2 IEFLDVSKTFAGRPAASHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEIRSLPVlELRRRMGYAI 81
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPE-EVKRRIGYLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 82 QSIGLFPHWTVAQNIatvlqlekwsraniadrvdelmallglepalrdryphQLSGGQQQRVGVARALAANPQVLLMDEP 161
Cdd:cd03230 80 EEPSLYENLTVRENL-------------------------------------KLSGGMKQRLALAQALLHDPELLILDEP 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 772671321 162 FGALDPVTRgalqAEMTRIHRIL---GRTIVLVTHDIDEALRLADHLVLMDHGEV 213
Cdd:cd03230 123 TSGLDPESR----REFWELLRELkkeGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
21-256 |
2.89e-50 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 171.37 E-value: 2.89e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 21 NLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEIRSLPVLELR----RRMGYAIQSIGLFPHWTVAQNI 96
Cdd:PRK10070 48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELRevrrKKIAMVFQSFALMPHMTVLDNT 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 97 ATVLQLEKWSRANIADRVDELMALLGLEPALRDrYPHQLSGGQQQRVGVARALAANPQVLLMDEPFGALDPVTRGALQAE 176
Cdd:PRK10070 128 AFGMELAGINAEERREKALDALRQVGLENYAHS-YPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDE 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 177 MTRIHRILGRTIVLVTHDIDEALRLADHLVLMDHGEVVQQGSPLELLTWPKNDFVREFFgrseLGVRLLSLRTVSDYMRR 256
Cdd:PRK10070 207 LVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFF----RGVDISQVFSAKDIARR 282
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
2-222 |
9.24e-50 |
|
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: 165.43 E-value: 9.24e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 2 IEFLDVSKTFA-GRPAASHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEIRSLPVLEL---RRRM 77
Cdd:cd03256 1 IEVENLSKTYPnGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALrqlRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 78 GYAIQSIGLFPHWTVAQNI-----------ATVLQLekWSRANIAdRVDELMALLGLEPALRDRyPHQLSGGQQQRVGVA 146
Cdd:cd03256 81 GMIFQQFNLIERLSVLENVlsgrlgrrstwRSLFGL--FPKEEKQ-RALAALERVGLLDKAYQR-ADQLSGGQQQRVAIA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 772671321 147 RALAANPQVLLMDEPFGALDPVTRGALQAEMTRIHRILGRTIVLVTHDIDEALRLADHLVLMDHGEVVQQGSPLEL 222
Cdd:cd03256 157 RALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAEL 232
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
2-227 |
1.10e-49 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 165.19 E-value: 1.10e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 2 IEFLDVSKTFAGRPAASHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEE------IRSLPVLELRR 75
Cdd:COG4161 3 IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQfdfsqkPSEKAIRLLRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 76 RMGYAIQSIGLFPHWTVAQN-IATVLQLEKWSRANIADRVDELMALLGLEPaLRDRYPHQLSGGQQQRVGVARALAANPQ 154
Cdd:COG4161 83 KVGMVFQQYNLWPHLTVMENlIEAPCKVLGLSKEQAREKAMKLLARLRLTD-KADRFPLHLSGGQQQRVAIARALMMEPQ 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 772671321 155 VLLMDEPFGALDPvtrgALQAEMTRIHRIL---GRTIVLVTHDIDEALRLADHLVLMDHGEVVQQGSpLELLTWPK 227
Cdd:COG4161 162 VLLFDEPTAALDP----EITAQVVEIIRELsqtGITQVIVTHEVEFARKVASQVVYMEKGRIIEQGD-ASHFTQPQ 232
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-237 |
3.90e-49 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 164.15 E-value: 3.90e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 1 MIEFLDVSKTFAGRPAASHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEI---RSLP-----VLE 72
Cdd:PRK11264 3 AIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIdtaRSLSqqkglIRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 73 LRRRMGYAIQSIGLFPHWTVAQN-IATVLQLEKWSRANIADRVDELMALLGLEpALRDRYPHQLSGGQQQRVGVARALAA 151
Cdd:PRK11264 83 LRQHVGFVFQNFNLFPHRTVLENiIEGPVIVKGEPKEEATARARELLAKVGLA-GKETSYPRRLSGGQQQRVAIARALAM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 152 NPQVLLMDEPFGALDPvtrgALQAEMTRIHRILG---RTIVLVTHDIDEALRLADHLVLMDHGEVVQQGSPLELLTWPKN 228
Cdd:PRK11264 162 RPEVILFDEPTSALDP----ELVGEVLNTIRQLAqekRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADPQQ 237
|
....*....
gi 772671321 229 DFVREFFGR 237
Cdd:PRK11264 238 PRTRQFLEK 246
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-236 |
5.02e-49 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 166.94 E-value: 5.02e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 1 MIEFLDVSKTFAGR-PAASHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEIRSLpvlELRRRmGY 79
Cdd:PRK11650 3 GLKLQAVRKSYDGKtQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNEL---EPADR-DI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 80 AI--QSIGLFPHWTVAQNIATVLQLEKWSRANIADRVDELMALLGLEPALrDRYPHQLSGGQQQRVGVARALAANPQVLL 157
Cdd:PRK11650 79 AMvfQNYALYPHMSVRENMAYGLKIRGMPKAEIEERVAEAARILELEPLL-DRKPRELSGGQRQRVAMGRAIVREPAVFL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 772671321 158 MDEPFGALDPVTRGALQAEMTRIHRILGRTIVLVTHDIDEALRLADHLVLMDHGEVVQQGSPLELLTWPKNDFVREFFG 236
Cdd:PRK11650 158 FDEPLSNLDAKLRVQMRLEIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGGVAEQIGTPVEVYEKPASTFVASFIG 236
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
6-221 |
7.31e-49 |
|
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: 163.67 E-value: 7.31e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 6 DVSKTFAGRPAASHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEIRSLPVLELRRR-MGYAIQSI 84
Cdd:COG0411 9 GLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIARLgIARTFQNP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 85 GLFPHWTVAQNI-------------ATVLQLEKWSR--ANIADRVDELMALLGLEpALRDRYPHQLSGGQQQRVGVARAL 149
Cdd:COG0411 89 RLFPELTVLENVlvaaharlgrgllAALLRLPRARReeREARERAEELLERVGLA-DRADEPAGNLSYGQQRRLEIARAL 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 772671321 150 AANPQVLLMDEPFGALDPVTRGALQAEMTRIHRILGRTIVLVTHDIDEALRLADHLVLMDHGEVVQQGSPLE 221
Cdd:COG0411 168 ATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGTPAE 239
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-227 |
8.69e-49 |
|
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: 165.23 E-value: 8.69e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 1 MIEFLDVSKTFAGR----PAASHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVE---HDSGMIRFAGEEIRSLPVLEL 73
Cdd:COG0444 1 LLEVRNLKVYFPTRrgvvKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPppgITSGEILFDGEDLLKLSEKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 74 RRRMGYAIQSIglF--------PHWTVAQNIATVLQL-EKWSRANIADRVDELMALLGLEPALR--DRYPHQLSGGQQQR 142
Cdd:COG0444 81 RKIRGREIQMI--FqdpmtslnPVMTVGDQIAEPLRIhGGLSKAEARERAIELLERVGLPDPERrlDRYPHELSGGMRQR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 143 VGVARALAANPQVLLMDEPFGALDpVTrgaLQAE----MTRIHRILGRTIVLVTHDIDEALRLADHLVLMDHGEVVQQGS 218
Cdd:COG0444 159 VMIARALALEPKLLIADEPTTALD-VT---IQAQilnlLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGP 234
|
....*....
gi 772671321 219 PLELLTWPK 227
Cdd:COG0444 235 VEELFENPR 243
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
32-234 |
1.93e-48 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 162.66 E-value: 1.93e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 32 LIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEIRSLP-------------VLELRRRMGYAIQSIGLFPHWTVAQNIAT 98
Cdd:COG4598 39 IIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIRLKPdrdgelvpadrrqLQRIRTRLGMVFQSFNLWSHMTVLENVIE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 99 V-LQLEKWSRANIADRVDELMALLGLEPAlRDRYPHQLSGGQQQRVGVARALAANPQVLLMDEPFGALDPvtrgALQAEM 177
Cdd:COG4598 119 ApVHVLGRPKAEAIERAEALLAKVGLADK-RDAYPAHLSGGQQQRAAIARALAMEPEVMLFDEPTSALDP----ELVGEV 193
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 178 TRIHRIL---GRTIVLVTHDIDEALRLADHLVLMDHGEVVQQGSPLELLTWPKNDFVREF 234
Cdd:COG4598 194 LKVMRDLaeeGRTMLVVTHEMGFARDVSSHVVFLHQGRIEEQGPPAEVFGNPKSERLRQF 253
|
|
| 3a0107s01c2 |
TIGR00972 |
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein ... |
2-228 |
4.83e-48 |
|
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: 161.31 E-value: 4.83e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 2 IEFLDVSKTFAGRPAASHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVE-----HDSGMIRFAGEEIRS--LPVLELR 74
Cdd:TIGR00972 2 IEIENLNLFYGEKEALKNINLDIPKNQVTALIGPSGCGKSTLLRSLNRMNDlvpgvRIEGKVLFDGQDIYDkkIDVVELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 75 RRMGYAIQSIGLFPHwTVAQNIATVLQLEKW-SRANIADRVDELMALLGLEPALRDR---YPHQLSGGQQQRVGVARALA 150
Cdd:TIGR00972 82 RRVGMVFQKPNPFPM-SIYDNIAYGPRLHGIkDKKELDEIVEESLKKAALWDEVKDRlhdSALGLSGGQQQRLCIARALA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 772671321 151 ANPQVLLMDEPFGALDPVTRGALQAEMTRIHRILgrTIVLVTHDIDEALRLADHLVLMDHGEVVQQGSPLELLTWPKN 228
Cdd:TIGR00972 161 VEPEVLLLDEPTSALDPIATGKIEELIQELKKKY--TIVIVTHNMQQAARISDRTAFFYDGELVEYGPTEQIFTNPKE 236
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
2-269 |
1.18e-47 |
|
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: 160.67 E-value: 1.18e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 2 IEFLDVSKTFAG--RPAASHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEIRSlP--VLELRRRM 77
Cdd:TIGR04520 1 IEVENVSFSYPEseKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLD-EenLWEIRKKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 78 GYaiqsiglfphwtVAQN-----IATVLQ------LEKW--SRANIADRVDELMALLGLEpALRDRYPHQLSGGQQQRVG 144
Cdd:TIGR04520 80 GM------------VFQNpdnqfVGATVEddvafgLENLgvPREEMRKRVDEALKLVGME-DFRDREPHLLSGGQKQRVA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 145 VARALAANPQVLLMDEPFGALDPVTRGALQAEMTRIHRILGRTIVLVTHDIDEALrLADHLVLMDHGEVVQQGSPlellt 224
Cdd:TIGR04520 147 IAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEAV-LADRVIVMNKGKIVAEGTP----- 220
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 772671321 225 wpkndfvREFFGRSE----LGVRLLSLRTVSDYMRREEMPVSGEPLQEQ 269
Cdd:TIGR04520 221 -------REIFSQVEllkeIGLDVPFITELAKALKKRGIPLPPDILTEE 262
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
20-222 |
3.21e-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: 158.78 E-value: 3.21e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 20 LNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEIRSlPVLElrrRMgYAIQSIGLFPHWTVAQNIATV 99
Cdd:TIGR01184 4 VNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITE-PGPD---RM-VVFQNYSLLPWLTVRENIALA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 100 L-----QLEKWSRANIadrVDELMALLGLEPAlRDRYPHQLSGGQQQRVGVARALAANPQVLLMDEPFGALDPVTRGALQ 174
Cdd:TIGR01184 79 VdrvlpDLSKSERRAI---VEEHIALVGLTEA-ADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQ 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 772671321 175 AEMTRIHRILGRTIVLVTHDIDEALRLADHLVLMDHGEVVQQGSPLEL 222
Cdd:TIGR01184 155 EELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAANIGQILEV 202
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
6-217 |
3.38e-47 |
|
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: 156.83 E-value: 3.38e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 6 DVSKTFAGRPAASHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEIRSLPVLELRRRMGYaiqsig 85
Cdd:cd03214 4 NLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAY------ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 86 lfphwtvaqniatVLQLekwsraniadrvdelMALLGLEpALRDRYPHQLSGGQQQRVGVARALAANPQVLLMDEPFGAL 165
Cdd:cd03214 78 -------------VPQA---------------LELLGLA-HLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHL 128
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 772671321 166 DPVTRGALQAEMTRIHRILGRTIVLVTHDIDEALRLADHLVLMDHGEVVQQG 217
Cdd:cd03214 129 DIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1-215 |
3.97e-47 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 159.09 E-value: 3.97e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 1 MIEFLDVSKTFAGRPAASHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGeeirsLPVLELRRRMGYA 80
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDG-----KPVEGPGAERGVV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 81 IQSIGLFPHWTVAQNIATVLQLEKWSRANIADRVDELMALLGLEPAlRDRYPHQLSGGQQQRVGVARALAANPQVLLMDE 160
Cdd:PRK11248 76 FQNEGLLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGA-EKRYIWQLSGGQRQRVGIARALAANPQLLLLDE 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 772671321 161 PFGALDPVTRGALQAEMTRIHRILGRTIVLVTHDIDEALRLADHLVLM--DHGEVVQ 215
Cdd:PRK11248 155 PFGALDAFTREQMQTLLLKLWQETGKQVLLITHDIEEAVFMATELVLLspGPGRVVE 211
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
1-212 |
5.35e-47 |
|
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: 157.41 E-value: 5.35e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 1 MIEFLDVSKTFAGRPAASH-LNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEIRSLP---VLELRRR 76
Cdd:TIGR02673 1 MIEFHNVSKAYPGGVAALHdVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLRgrqLPLLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 77 MGYAIQSIGLFPHWTVAQNIATVLQLEKWSRANIADRVDELMALLGLEPALrDRYPHQLSGGQQQRVGVARALAANPQVL 156
Cdd:TIGR02673 81 IGVVFQDFRLLPDRTVYENVALPLEVRGKKEREIQRRVGAALRQVGLEHKA-DAFPEQLSGGEQQRVAIARAIVNSPPLL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 772671321 157 LMDEPFGALDPVTRGALQAEMTRIHRiLGRTIVLVTHDIDEALRLADHLVLMDHGE 212
Cdd:TIGR02673 160 LADEPTGNLDPDLSERILDLLKRLNK-RGTTVIVATHDLSLVDRVAHRVIILDDGR 214
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
1-222 |
5.81e-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: 158.23 E-value: 5.81e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 1 MIEFLDVSKTFAGRPAASH-LNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEIRSL---PVLELRRR 76
Cdd:TIGR02315 1 MLEVENLSKVYPNGKQALKnINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLrgkKLRKLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 77 MGYAIQSIGLFPHWTVAQN-----------IATVLQLekWSRANIAdRVDELMALLGLEpALRDRYPHQLSGGQQQRVGV 145
Cdd:TIGR02315 81 IGMIFQHYNLIERLTVLENvlhgrlgykptWRSLLGR--FSEEDKE-RALSALERVGLA-DKAYQRADQLSGGQQQRVAI 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 772671321 146 ARALAANPQVLLMDEPFGALDPVTRGALQAEMTRIHRILGRTIVLVTHDIDEALRLADHLVLMDHGEVVQQGSPLEL 222
Cdd:TIGR02315 157 ARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSEL 233
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
6-219 |
1.13e-46 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 157.21 E-value: 1.13e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 6 DVSKTFAGRPAASHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEIRSLPVLELRRR-MGYAIQSI 84
Cdd:cd03219 5 GLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARLgIGRTFQIP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 85 GLFPHWTVAQNIATVLQ--------LEKWSRAN--IADRVDELMALLGLEPaLRDRYPHQLSGGQQQRVGVARALAANPQ 154
Cdd:cd03219 85 RLFPELTVLENVMVAAQartgsgllLARARREEreARERAEELLERVGLAD-LADRPAGELSYGQQRRLEIARALATDPK 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 772671321 155 VLLMDEPFGALDPVTRGALQAEMTRIHRiLGRTIVLVTHDIDEALRLADHLVLMDHGEVVQQGSP 219
Cdd:cd03219 164 LLLLDEPAAGLNPEETEELAELIRELRE-RGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTP 227
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
6-222 |
1.42e-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: 156.51 E-value: 1.42e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 6 DVSKTFAG--RPAASHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEIRSLPVlELRRRMGYAIQS 83
Cdd:cd03263 5 NLTKTYKKgtKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRK-AARQSLGYCPQF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 84 IGLFPHWTVAQNIATVLQLEKWSRANIADRVDELMALLGLEPaLRDRYPHQLSGGQQQRVGVARALAANPQVLLMDEPFG 163
Cdd:cd03263 84 DALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTD-KANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTS 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 772671321 164 ALDPVTRgalqaemTRIHRIL-----GRTIVLVTHDIDEALRLADHLVLMDHGEVVQQGSPLEL 222
Cdd:cd03263 163 GLDPASR-------RAIWDLIlevrkGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQEL 219
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
2-240 |
2.02e-46 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 160.27 E-value: 2.02e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 2 IEFLDVSKTFAGRPAASHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEI--RSLPvlelRRRMGY 79
Cdd:PRK11432 7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVthRSIQ----QRDICM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 80 AIQSIGLFPHWTVAQNIATVLQLEKWSRANIADRVDELMALLGLEpALRDRYPHQLSGGQQQRVGVARALAANPQVLLMD 159
Cdd:PRK11432 83 VFQSYALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLA-GFEDRYVDQISGGQQQRVALARALILKPKVLLFD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 160 EPFGALDPVTRGALQAEMTRIHRILGRTIVLVTHDIDEALRLADHLVLMDHGEVVQQGSPLELLTWPKNDFVREFFGRSE 239
Cdd:PRK11432 162 EPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPASRFMASFMGDAN 241
|
.
gi 772671321 240 L 240
Cdd:PRK11432 242 I 242
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
2-212 |
4.90e-45 |
|
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: 151.00 E-value: 4.90e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 2 IEFLDVSKTFAGR--PAASHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEIRSLPVLELRRRMGY 79
Cdd:cd03228 1 IEFKNVSFSYPGRpkPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 80 AIQSIGLFpHWTVAQNIatvlqlekwsraniadrvdelmallglepalrdryphqLSGGQQQRVGVARALAANPQVLLMD 159
Cdd:cd03228 81 VPQDPFLF-SGTIRENI--------------------------------------LSGGQRQRIAIARALLRDPPILILD 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 772671321 160 EPFGALDPVTRGALQAEMTRIHRilGRTIVLVTHDIdEALRLADHLVLMDHGE 212
Cdd:cd03228 122 EATSALDPETEALILEALRALAK--GKTVIVIAHRL-STIRDADRIIVLDDGR 171
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1-224 |
9.29e-45 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 152.93 E-value: 9.29e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 1 MIEFLDVSKTFAGRPAASHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEIRSLPVLELRRRMgyA 80
Cdd:COG4604 1 MIEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRL--A 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 81 I--QSI--------------GLFPHwtvaqniatvlqlekwS--RANIADR--VDELMALLGLEPaLRDRYPHQLSGGQQ 140
Cdd:COG4604 79 IlrQENhinsrltvrelvafGRFPY----------------SkgRLTAEDReiIDEAIAYLDLED-LADRYLDELSGGQR 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 141 QRVGVARALAANPQVLLMDEPFGALDPvtRGALQAeMTRIHRI---LGRTIVLVTHDIDEALRLADHLVLMDHGEVVQQG 217
Cdd:COG4604 142 QRAFIAMVLAQDTDYVLLDEPLNNLDM--KHSVQM-MKLLRRLadeLGKTVVIVLHDINFASCYADHIVAMKDGRVVAQG 218
|
....*..
gi 772671321 218 SPLELLT 224
Cdd:COG4604 219 TPEEIIT 225
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
3-212 |
1.85e-44 |
|
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: 148.93 E-value: 1.85e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 3 EFLDVSKTFAGRPAASHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEIRSLPVLELRRRMGYAiq 82
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYV-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 83 siglfphwtvaqniatvlqlekwsraniadrvdelmallglepalrdrypHQLSGGQQQRVGVARALAANPQVLLMDEPF 162
Cdd:cd00267 79 --------------------------------------------------PQLSGGQRQRVALARALLLNPDLLLLDEPT 108
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 772671321 163 GALDPVTRGALQAEMTRIHRiLGRTIVLVTHDIDEALRLADHLVLMDHGE 212
Cdd:cd00267 109 SGLDPASRERLLELLRELAE-EGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_ATP_SaoA |
NF040729 |
ABC transporter ATP-binding protein SaoA; SaoA is the ATP-binding subunit of an ABC ... |
2-215 |
2.00e-44 |
|
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: 151.82 E-value: 2.00e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 2 IEFLDVSKTFAGRPAASH----LNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEIrSLPVLElrrrM 77
Cdd:NF040729 2 LKIQNISKTFINNKKENEvlkdISFDVEEGEFVSLLGPSGCGKTTLLTIIAGFQNATSGEILVNGNEV-TKPGPD----R 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 78 GYAIQSIGLFPHWTVAQNIATVLQLEKWSRANIADRVDELMALLGLEpALRDRYPHQLSGGQQQRVGVARALAANPQVLL 157
Cdd:NF040729 77 GFVFQNYALFPWMTVKENIEYPMKQQKMPKQEREKRLNELLEMAQLT-GKENLYPHQISGGMKQRTAVIRALACKPEVLL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 158 MDEPFGALDPVTRGALQAEMTRIHRILGRTIVLVTHDIDEALRLADHLVLM--DHGEVVQ 215
Cdd:NF040729 156 MDEPLGAVDFQMRQILQEELESIWLKDKTTVLMVTHDVDEAVYLSDRVIVMsrDKGKILE 215
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
2-223 |
2.73e-44 |
|
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: 160.38 E-value: 2.73e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 2 IEFLDVSKTFAGR--PAASHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEIRSLPVLELRRRMGY 79
Cdd:COG2274 474 IELENVSFRYPGDspPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGV 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 80 AIQSIGLFpHWTVAQNI------ATVLQLEKWSR-ANIADRVDELMalLGLEPALRDRYpHQLSGGQQQRVGVARALAAN 152
Cdd:COG2274 554 VLQDVFLF-SGTIRENItlgdpdATDEEIIEAARlAGLHDFIEALP--MGYDTVVGEGG-SNLSGGQRQRLAIARALLRN 629
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 772671321 153 PQVLLMDEPFGALDPVTRGALQAEMTRIHRilGRTIVLVTHDiDEALRLADHLVLMDHGEVVQQGSPLELL 223
Cdd:COG2274 630 PRILILDEATSALDAETEAIILENLRRLLK--GRTVIIIAHR-LSTIRLADRIIVLDKGRIVEDGTHEELL 697
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
2-213 |
3.25e-44 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 150.25 E-value: 3.25e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 2 IEFLDVSKTF-AGRPAASHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEIRSLP---VLELRRRM 77
Cdd:cd03292 1 IEFINVTKTYpNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRgraIPYLRRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 78 GYAIQSIGLFPHWTVAQNIATVLQLEKWSRANIADRVDELMALLGLEPALRDrYPHQLSGGQQQRVGVARALAANPQVLL 157
Cdd:cd03292 81 GVVFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRA-LPAELSGGEQQRVAIARAIVNSPTILI 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 772671321 158 MDEPFGALDPVTRGALQAEMTRIHRiLGRTIVLVTHDIDEALRLADHLVLMDHGEV 213
Cdd:cd03292 160 ADEPTGNLDPDTTWEIMNLLKKINK-AGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
2-222 |
6.78e-44 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 151.71 E-value: 6.78e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 2 IEFLDVSKT------FAGRpAASHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEI----RSLPVL 71
Cdd:PRK13634 3 ITFQKVEHRyqyktpFERR-ALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVItagkKNKKLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 72 ELRRRMGYAIQsiglFPHW-----TVAQNIATVLQLEKWSRANIADRVDELMALLGLEPALRDRYPHQLSGGQQQRVGVA 146
Cdd:PRK13634 82 PLRKKVGIVFQ----FPEHqlfeeTVEKDICFGPMNFGVSEEDAKQKAREMIELVGLPEELLARSPFELSGGQMRRVAIA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 772671321 147 RALAANPQVLLMDEPFGALDPVTRGALQAEMTRIHRILGRTIVLVTHDIDEALRLADHLVLMDHGEVVQQGSPLEL 222
Cdd:PRK13634 158 GVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREI 233
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
3-217 |
7.03e-44 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 149.22 E-value: 7.03e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 3 EFLDVSKTFAGRPAASHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEeirslPVLELRRRMGYAIQ 82
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGK-----PLEKERKRIGYVPQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 83 SIGL---FPhWTVAQNIATVLQLEKW--SRANIADR--VDELMALLGLEpALRDRYPHQLSGGQQQRVGVARALAANPQV 155
Cdd:cd03235 76 RRSIdrdFP-ISVRDVVLMGLYGHKGlfRRLSKADKakVDEALERVGLS-ELADRQIGELSGGQQQRVLLARALVQDPDL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 772671321 156 LLMDEPFGALDPVTRGALQAEMTRIHRiLGRTIVLVTHDIDEALRLADHLVLMDHgEVVQQG 217
Cdd:cd03235 154 LLLDEPFAGVDPKTQEDIYELLRELRR-EGMTILVVTHDLGLVLEYFDRVLLLNR-TVVASG 213
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
6-235 |
8.90e-44 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 149.79 E-value: 8.90e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 6 DVSKTFAGRPAASHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEIRSLPVLElRRRMG--YAIQ- 82
Cdd:COG1137 8 NLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMHK-RARLGigYLPQe 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 83 -SIglFPHWTVAQNIATVLQLEKWSRANIADRVDELMALLGLEPaLRDRYPHQLSGGQQQRVGVARALAANPQVLLMDEP 161
Cdd:COG1137 87 aSI--FRKLTVEDNILAVLELRKLSKKEREERLEELLEEFGITH-LRKSKAYSLSGGERRRVEIARALATNPKFILLDEP 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 772671321 162 FGALDPVTRGALQAEmtrIHRILGRTI-VLVT-HDIDEALRLADHLVLMDHGEVVQQGSPLELLtwpKNDFVREFF 235
Cdd:COG1137 164 FAGVDPIAVADIQKI---IRHLKERGIgVLITdHNVRETLGICDRAYIISEGKVLAEGTPEEIL---NNPLVRKVY 233
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
20-217 |
1.06e-43 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 149.78 E-value: 1.06e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 20 LNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAG------EEIRSLPVLELRRRMGYAIQSIGLFPHWTVA 93
Cdd:PRK11124 21 ITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGnhfdfsKTPSDKAIRELRRNVGMVFQQYNLWPHLTVQ 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 94 QNI----ATVLQLEKwSRANiaDRVDELMALLGLEPaLRDRYPHQLSGGQQQRVGVARALAANPQVLLMDEPFGALDPvt 169
Cdd:PRK11124 101 QNLieapCRVLGLSK-DQAL--ARAEKLLERLRLKP-YADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDP-- 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 772671321 170 rgALQAEMTRIHRIL---GRTIVLVTHDIDEALRLADHLVLMDHGEVVQQG 217
Cdd:PRK11124 175 --EITAQIVSIIRELaetGITQVIVTHEVEVARKTASRVVYMENGHIVEQG 223
|
|
| ABC_ATP_DarD |
NF038007 |
darobactin export ABC transporter ATP-binding protein; |
18-211 |
1.41e-43 |
|
darobactin export ABC transporter ATP-binding protein;
Pssm-ID: 411600 [Multi-domain] Cd Length: 218 Bit Score: 148.71 E-value: 1.41e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 18 SHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEIRSLPVLE---LRRRM-GYAIQSIGLFPHWTVA 93
Cdd:NF038007 22 NHLNFSVEKGDFVSIMGPSGSGKSTLLNIIGMFDSLDSGSLTLAGKEVTNLSYSQkiiLRRELiGYIFQSFNLIPHLSIF 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 94 QNIATVLQLEKWSRANIADRVDELMALLGLEPAlRDRYPHQLSGGQQQRVGVARALAANPQVLLMDEPFGALDPV-TRGA 172
Cdd:NF038007 102 DNVALPLKYRGVAKKERIERVNQVLNLFGIDNR-RNHKPMQLSGGQQQRVAIARAMVSNPALLLADEPTGNLDSKnARAV 180
|
170 180 190
....*....|....*....|....*....|....*....
gi 772671321 173 LQaEMTRIHRiLGRTIVLVTHDiDEALRLADHLVLMDHG 211
Cdd:NF038007 181 LQ-QLKYINQ-KGTTIIMVTHS-DEASTYGNRIINMKDG 216
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
6-233 |
1.50e-43 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 149.23 E-value: 1.50e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 6 DVSKTFAGRPAASHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEIRSLPVLELRRR-MGYAIQSI 84
Cdd:cd03218 5 NLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRARLgIGYLPQEA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 85 GLFPHWTVAQNIATVLQLEKWSRANIADRVDELMALLGLEPaLRDRYPHQLSGGQQQRVGVARALAANPQVLLMDEPFGA 164
Cdd:cd03218 85 SIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITH-LRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAG 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 772671321 165 LDPVTRGALQAemtRIHRILGRTI-VLVT-HDIDEALRLADHLVLMDHGEVVQQGSPLELLTwpkNDFVRE 233
Cdd:cd03218 164 VDPIAVQDIQK---IIKILKDRGIgVLITdHNVRETLSITDRAYIIYEGKVLAEGTPEEIAA---NELVRK 228
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-223 |
1.82e-43 |
|
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: 156.46 E-value: 1.82e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 2 IEFLDVSKTFA-GRPAASHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEIRSLPVLELRRRMGYA 80
Cdd:COG4988 337 IELEDVSFSYPgGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWV 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 81 IQSIGLFpHWTVAQNI------ATVLQLEKWSR-ANIADRVDELMAllGLEPALRDRyPHQLSGGQQQRVGVARALAANP 153
Cdd:COG4988 417 PQNPYLF-AGTIRENLrlgrpdASDEELEAALEaAGLDEFVAALPD--GLDTPLGEG-GRGLSGGQAQRLALARALLRDA 492
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 154 QVLLMDEPFGALDPVTRGALQAEMTRIHRilGRTIVLVTHDIdEALRLADHLVLMDHGEVVQQGSPLELL 223
Cdd:COG4988 493 PLLLLDEPTAHLDAETEAEILQALRRLAK--GRTVILITHRL-ALLAQADRILVLDDGRIVEQGTHEELL 559
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2-236 |
4.25e-43 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 148.65 E-value: 4.25e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 2 IEFLDVSKTFAGRPAASHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLveHD-------SGMIRFAGEEI--RSLPVLE 72
Cdd:COG1117 12 IEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRM--NDlipgarvEGEILLDGEDIydPDVDVVE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 73 LRRRMGYAIQSIGLFPHwTVAQNIATVLQLEKW-SRANIADRVdelmallglEPALR---------DR---YPHQLSGGQ 139
Cdd:COG1117 90 LRRRVGMVFQKPNPFPK-SIYDNVAYGLRLHGIkSKSELDEIV---------EESLRkaalwdevkDRlkkSALGLSGGQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 140 QQRVGVARALAANPQVLLMDEPFGALDPVTrgALQAEMTrIHRILGR-TIVLVTHDIDEALRLADHLVLMDHGEVVQQGS 218
Cdd:COG1117 160 QQRLCIARALAVEPEVLLMDEPTSALDPIS--TAKIEEL-ILELKKDyTIVIVTHNMQQAARVSDYTAFFYLGELVEFGP 236
|
250 260
....*....|....*....|..
gi 772671321 219 PLELLTWPKN----DFVREFFG 236
Cdd:COG1117 237 TEQIFTNPKDkrteDYITGRFG 258
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-222 |
8.08e-43 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 149.10 E-value: 8.08e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 1 MIEFLDVSKTFAGRPAASHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEIRSlpvlELRRRMGYA 80
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDP----EDRRRIGYL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 81 IQSIGLFPHWTVAQNIATVLQLEKWSRANIADRVDELMALLGLEPALRDRYpHQLSGGQQQRVGVARALAANPQVLLMDE 160
Cdd:COG4152 77 PEERGLYPKMKVGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDRANKKV-EELSKGNQQKVQLIAALLHDPELLILDE 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 772671321 161 PFGALDPVTRGALQAEMTRIHRiLGRTIVLVTHDIDEALRLADHLVLMDHGEVVQQGSPLEL 222
Cdd:COG4152 156 PFSGLDPVNVELLKDVIRELAA-KGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEI 216
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-210 |
1.85e-42 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 145.31 E-value: 1.85e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 1 MIEFLDVSKTFAGRPAASHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEIRSLPVlELRRRMGYA 80
Cdd:COG4133 2 MLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDARE-DYRRRLAYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 81 IQSIGLFPHWTVAQNIATVLQLekWSRANIADRVDELMALLGLEPaLRDRYPHQLSGGQQQRVGVARALAANPQVLLMDE 160
Cdd:COG4133 81 GHADGLKPELTVRENLRFWAAL--YGLRADREAIDEALEAVGLAG-LADLPVRQLSAGQKRRVALARLLLSPAPLWLLDE 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 772671321 161 PFGALDPVTRGALQAEMTRiHRILGRTIVLVTHDiDEALRLADHLVLMDH 210
Cdd:COG4133 158 PFTALDAAGVALLAELIAA-HLARGGAVLLTTHQ-PLELAAARVLDLGDF 205
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1-224 |
2.68e-42 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 147.06 E-value: 2.68e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 1 MIEFLDVSKTFAG--RPAASHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEIRSLPVLELRRRMG 78
Cdd:PRK13632 7 MIKVENVSFSYPNseNNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 79 YAIQS-----IGLfphwTVAQNIATVLQLEKWSRANIADRVDELMALLGLEPALrDRYPHQLSGGQQQRVGVARALAANP 153
Cdd:PRK13632 87 IIFQNpdnqfIGA----TVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYL-DKEPQNLSGGQKQRVAIASVLALNP 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 772671321 154 QVLLMDEPFGALDPVTRGALQAEMTRIHRILGRTIVLVTHDIDEALrLADHLVLMDHGEVVQQGSPLELLT 224
Cdd:PRK13632 162 EIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAI-LADKVIVFSEGKLIAQGKPKEILN 231
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
7-226 |
4.31e-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: 148.72 E-value: 4.31e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 7 VSKTFAGRPAASHLNLNFAEGAFSV--LIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEIRS------LPVLelRRRMG 78
Cdd:TIGR02142 1 LSARFSKRLGDFSLDADFTLPGQGVtaIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDsrkgifLPPE--KRRIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 79 YAIQSIGLFPHWTVAQNIatvlqLEKWSRANIADRV---DELMALLGLEPALRdRYPHQLSGGQQQRVGVARALAANPQV 155
Cdd:TIGR02142 79 YVFQEARLFPHLSVRGNL-----RYGMKRARPSERRisfERVIELLGIGHLLG-RLPGRLSGGEKQRVAIGRALLSSPRL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 772671321 156 LLMDEPFGALDPVTRGALQAEMTRIHRILGRTIVLVTHDIDEALRLADHLVLMDHGEVVQQGSPLELLTWP 226
Cdd:TIGR02142 153 LLMDEPLAALDDPRKYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASP 223
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
2-223 |
1.25e-41 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 151.86 E-value: 1.25e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 2 IEFLDVSktFA---GRPAASHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEIRSLPVLELRRRMG 78
Cdd:COG1132 340 IEFENVS--FSypgDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESLRRQIG 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 79 YAIQSIGLFpHWTVAQNI------ATVLQLEKWSR-ANIADRVDELMAllGLEPALRDRyPHQLSGGQQQRVGVARALAA 151
Cdd:COG1132 418 VVPQDTFLF-SGTIRENIrygrpdATDEEVEEAAKaAQAHEFIEALPD--GYDTVVGER-GVNLSGGQRQRIAIARALLK 493
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 772671321 152 NPQVLLMDEPFGALDPVTRGALQAEMTRIHRilGRTIVLVTHDIdEALRLADHLVLMDHGEVVQQGSPLELL 223
Cdd:COG1132 494 DPPILILDEATSALDTETEALIQEALERLMK--GRTTIVIAHRL-STIRNADRILVLDDGRIVEQGTHEELL 562
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
2-222 |
6.10e-41 |
|
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: 142.12 E-value: 6.10e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 2 IEFLDVSKTFAGRPAASHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEIRSLPVlELRRRMGYAI 81
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPR-EVRRRIGIVF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 82 QSIGLFPHWTVAQNIATVLQLEKWSRANIADRVDELMALLGLEPAlRDRYPHQLSGGQQQRVGVARALAANPQVLLMDEP 161
Cdd:cd03265 80 QDLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEA-ADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 772671321 162 FGALDPVTRGALQAEMTRIHRILGRTIVLVTHDIDEALRLADHLVLMDHGEVVQQGSPLEL 222
Cdd:cd03265 159 TIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
20-242 |
1.15e-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: 141.66 E-value: 1.15e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 20 LNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEIRSLPVLELRRR-MGYAIQSIGLFPHWTVAQNIAT 98
Cdd:COG0410 22 VSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIARLgIGYVPEGRRIFPSLTVEENLLL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 99 VLQLEKwSRANIADRVDELMALLglePALRDRYpHQ----LSGGQQQRVGVARALAANPQVLLMDEPFGALDPVtrgaLQ 174
Cdd:COG0410 102 GAYARR-DRAEVRADLERVYELF---PRLKERR-RQragtLSGGEQQMLAIGRALMSRPKLLLLDEPSLGLAPL----IV 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 772671321 175 AEMTR-IHRI--LGRTIVLVTHDIDEALRLADHLVLMDHGEVVQQGSPLELLTwpkNDFVREFFgrseLGV 242
Cdd:COG0410 173 EEIFEiIRRLnrEGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLA---DPEVREAY----LGV 236
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
20-223 |
1.27e-40 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 141.03 E-value: 1.27e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 20 LNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEIRSLPVLELRRR-MGYAIQSIGLFPHWTVAQNIAT 98
Cdd:cd03224 19 VSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARAgIGYVPEGRRIFPELTVEENLLL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 99 VLQLEKwsRANIADRVDELMALLglePALRDRYPH---QLSGGQQQRVGVARALAANPQVLLMDEPFGALDPVTRGALQA 175
Cdd:cd03224 99 GAYARR--RAKRKARLERVYELF---PRLKERRKQlagTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLAPKIVEEIFE 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 772671321 176 EMTRIHRiLGRTIVLVTHDIDEALRLADHLVLMDHGEVVQQGSPLELL 223
Cdd:cd03224 174 AIRELRD-EGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELL 220
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
20-162 |
1.98e-40 |
|
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: 138.55 E-value: 1.98e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 20 LNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEIRSLPVLELRRRMGYAIQSIGLFPHWTVAQNIATV 99
Cdd:pfam00005 4 VSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRLTVRENLRLG 83
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 772671321 100 LQLEKWSRANIADRVDELMALLGLEPALRDR---YPHQLSGGQQQRVGVARALAANPQVLLMDEPF 162
Cdd:pfam00005 84 LLLKGLSKREKDARAEEALEKLGLGDLADRPvgeRPGTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
2-223 |
3.33e-40 |
|
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: 140.75 E-value: 3.33e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 2 IEFLDVSKTFAGRPAAS---HLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEIRSLPVLELRRRMG 78
Cdd:cd03249 1 IEFKNVSFRYPSRPDVPilkGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 79 YAIQSIGLFPHwTVAQNI------ATVLQLEKWSR-ANIADRVDELMAllGLEPALRDRYPhQLSGGQQQRVGVARALAA 151
Cdd:cd03249 81 LVSQEPVLFDG-TIAENIrygkpdATDEEVEEAAKkANIHDFIMSLPD--GYDTLVGERGS-QLSGGQKQRIAIARALLR 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 772671321 152 NPQVLLMDEPFGALDPVTRGALQAEMTRIHRilGRTIVLVTHDIdEALRLADHLVLMDHGEVVQQGSPLELL 223
Cdd:cd03249 157 NPKILLLDEATSALDAESEKLVQEALDRAMK--GRTTIVIAHRL-STIRNADLIAVLQNGQVVEQGTHDELM 225
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-234 |
3.46e-40 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 141.20 E-value: 3.46e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 2 IEFLDVSKTFAGRPAASHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVE-----HDSGMIRFAGEEIRSLPVLELRRR 76
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElypeaRVSGEVYLDGQDIFKMDVIELRRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 77 MGYAIQSIGLFPHWTVAQNIATVLQLEKW--SRANIADRVDELMALLGLEPALRDRY---PHQLSGGQQQRVGVARALAA 151
Cdd:PRK14247 84 VQMVFQIPNPIPNLSIFENVALGLKLNRLvkSKKELQERVRWALEKAQLWDEVKDRLdapAGKLSGGQQQRLCIARALAF 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 152 NPQVLLMDEPFGALDPVTRGALQAEMTRIHRILgrTIVLVTHDIDEALRLADHLVLMDHGEVVQQGSPLELLTWPKNDFV 231
Cdd:PRK14247 164 QPEVLLADEPTANLDPENTAKIESLFLELKKDM--TIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTNPRHELT 241
|
...
gi 772671321 232 REF 234
Cdd:PRK14247 242 EKY 244
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
2-217 |
3.58e-40 |
|
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: 139.64 E-value: 3.58e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 2 IEFLDVSKTFAGRPAASHLNLNFAEGAFsVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEIRSLPVlELRRRMGYAI 81
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPGMY-GLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQ-KLRRRIGYLP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 82 QSIGLFPHWTVAQNIATVLQLEKWSRANIADRVDELMALLGLEPAlRDRYPHQLSGGQQQRVGVARALAANPQVLLMDEP 161
Cdd:cd03264 79 QEFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDR-AKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEP 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 772671321 162 FGALDPvtrgalqAEMTRIHRILG-----RTIVLVTHDIDEALRLADHLVLMDHGEVVQQG 217
Cdd:cd03264 158 TAGLDP-------EERIRFRNLLSelgedRIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-236 |
5.30e-40 |
|
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: 140.22 E-value: 5.30e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 1 MIEFLDVSKTFAGRPAASHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRlvEH---DSGMIRFAGEEIRSLPVLELRRRM 77
Cdd:COG1119 3 LLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITG--DLpptYGNDVRLFGERRGGEDVWELRKRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 78 GY---AIQ-------------------SIGLFPHWTVAQniatvlqlekwsraniADRVDELMALLGLEpALRDRYPHQL 135
Cdd:COG1119 81 GLvspALQlrfprdetvldvvlsgffdSIGLYREPTDEQ----------------RERARELLELLGLA-HLADRPFGTL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 136 SGGQQQRVGVARALAANPQVLLMDEPFGALDPVTRGALQAEMTRIHRILGRTIVLVTHDIDEALRLADHLVLMDHGEVVQ 215
Cdd:COG1119 144 SQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRVVA 223
|
250 260
....*....|....*....|.
gi 772671321 216 QGSPLELLTwpkNDFVREFFG 236
Cdd:COG1119 224 AGPKEEVLT---SENLSEAFG 241
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
6-194 |
5.63e-40 |
|
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: 138.90 E-value: 5.63e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 6 DVSKTFAGRPAASHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEE---IRSLPVLELRR-RMGYAI 81
Cdd:TIGR03608 3 NISKKFGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQEtppLNSKKASKFRReKLGYLF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 82 QSIGLFPHWTVAQNIATVLQLEKWSRANIADRVDELMALLGLEPALRdRYPHQLSGGQQQRVGVARALAANPQVLLMDEP 161
Cdd:TIGR03608 83 QNFALIENETVEENLDLGLKYKKLSKKEKREKKKEALEKVGLNLKLK-QKIYELSGGEQQRVALARAILKPPPLILADEP 161
|
170 180 190
....*....|....*....|....*....|....*....
gi 772671321 162 FGALDPVTRGAlqaemtrIHRIL------GRTIVLVTHD 194
Cdd:TIGR03608 162 TGSLDPKNRDE-------VLDLLlelndeGKTIIIVTHD 193
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-223 |
7.05e-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: 146.83 E-value: 7.05e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 2 IEFLDVSKTF--AGRPAASHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEIRSLPVLELRRRMGY 79
Cdd:COG4987 334 LELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRRIAV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 80 AIQSIGLFpHWTVAQNIATVlqlekwsRANIADrvDELMALL---GLEPALRDRyPH-----------QLSGGQQQRVGV 145
Cdd:COG4987 414 VPQRPHLF-DTTLRENLRLA-------RPDATD--EELWAALervGLGDWLAAL-PDgldtwlgeggrRLSGGERRRLAL 482
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 772671321 146 ARALAANPQVLLMDEPFGALDPVTRGALqaeMTRIHRIL-GRTIVLVTHDIdEALRLADHLVLMDHGEVVQQGSPLELL 223
Cdd:COG4987 483 ARALLRDAPILLLDEPTEGLDAATEQAL---LADLLEALaGRTVLLITHRL-AGLERMDRILVLEDGRIVEQGTHEELL 557
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
2-217 |
9.72e-40 |
|
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: 138.57 E-value: 9.72e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 2 IEFLDVSKTFAGRPAASHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEIRSLPvlelRRRMGYAI 81
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAA----RNRIGYLP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 82 QSIGLFPHWTVAQNIATVLQLEKWSRANIADRVDELMALLGLEPaLRDRYPHQLSGGQQQRVGVARALAANPQVLLMDEP 161
Cdd:cd03269 77 EERGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSE-YANKRVEELSKGNQQKVQFIAAVIHDPELLILDEP 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 772671321 162 FGALDPVTRGALQAEMTRIHRiLGRTIVLVTHDIDEALRLADHLVLMDHGEVVQQG 217
Cdd:cd03269 156 FSGLDPVNVELLKDVIRELAR-AGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
16-221 |
2.21e-39 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 139.80 E-value: 2.21e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 16 AASHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEI--RSLPVLELRRRMGYAIQsiglFPHW--- 90
Cdd:PRK13637 22 ALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDItdKKVKLSDIRKKVGLVFQ----YPEYqlf 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 91 --TVAQNIATVLQLEKWSRANIADRVDELMALLGLE-PALRDRYPHQLSGGQQQRVGVARALAANPQVLLMDEPFGALDP 167
Cdd:PRK13637 98 eeTIEKDIAFGPINLGLSEEEIENRVKRAMNIVGLDyEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDP 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 772671321 168 VTRGALQAEMTRIHRILGRTIVLVTHDIDEALRLADHLVLMDHGEVVQQGSPLE 221
Cdd:PRK13637 178 KGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPRE 231
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
32-218 |
3.24e-39 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 140.64 E-value: 3.24e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 32 LIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEIRSLP---VLELRRRMGYAIQ----SigLFPHWTVAQNIATVLQL-E 103
Cdd:COG4608 49 LVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSgreLRPLRRRMQMVFQdpyaS--LNPRMTVGDIIAEPLRIhG 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 104 KWSRANIADRVDELMALLGLEPALRDRYPHQLSGGQQQRVGVARALAANPQVLLMDEPFGALDpVTrgaLQAE----MTR 179
Cdd:COG4608 127 LASKAERRERVAELLELVGLRPEHADRYPHEFSGGQRQRIGIARALALNPKLIVCDEPVSALD-VS---IQAQvlnlLED 202
|
170 180 190
....*....|....*....|....*....|....*....
gi 772671321 180 IHRILGRTIVLVTHDIDEALRLADHLVLMDHGEVVQQGS 218
Cdd:COG4608 203 LQDELGLTYLFISHDLSVVRHISDRVAVMYLGKIVEIAP 241
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
32-234 |
4.17e-39 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 138.26 E-value: 4.17e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 32 LIGTSGSGKSTTLKMINRLVE-HDS-----GMIRFAGEEIRSLPVLELRRRMGYAIQSIGLFPHWTVAQNIATVLQLEKW 105
Cdd:PRK14246 41 IMGPSGSGKSTLLKVLNRLIEiYDSkikvdGKVLYFGKDIFQIDAIKLRKEVGMVFQQPNPFPHLSIYDNIAYPLKSHGI 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 106 S-RANIADRVDELMALLGLEPALRDRY---PHQLSGGQQQRVGVARALAANPQVLLMDEPFGALDPVTRGALQAEMTRIH 181
Cdd:PRK14246 121 KeKREIKKIVEECLRKVGLWKEVYDRLnspASQLSGGQQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELK 200
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 772671321 182 RILgrTIVLVTHDIDEALRLADHLVLMDHGEVVQQGSPLELLTWPKNDFVREF 234
Cdd:PRK14246 201 NEI--AIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNELTEKY 251
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
9-222 |
7.03e-39 |
|
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: 139.06 E-value: 7.03e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 9 KTFAGRPAASHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEIRSLPVlELRRRMGYAIQSIGLFP 88
Cdd:TIGR01188 1 KVYGDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVVREPR-KVRRSIGIVPQYASVDE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 89 HWTVAQNIATVLQLEKWSRANIADRVDELMALLGLEPAlRDRYPHQLSGGQQQRVGVARALAANPQVLLMDEPFGALDPV 168
Cdd:TIGR01188 80 DLTGRENLEMMGRLYGLPKDEAEERAEELLELFELGEA-ADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPR 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 772671321 169 TRGALQAEMTRIHRiLGRTIVLVTHDIDEALRLADHLVLMDHGEVVQQGSPLEL 222
Cdd:TIGR01188 159 TRRAIWDYIRALKE-EGVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPEEL 211
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
32-235 |
8.13e-39 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 137.79 E-value: 8.13e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 32 LIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEIR-------SLPVLE------LRRRMGYAIQSIGLFPHWTVAQNIAT 98
Cdd:PRK10619 36 IIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgQLKVADknqlrlLRTRLTMVFQHFNLWSHMTVLENVME 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 99 V-LQLEKWSRANIADRVDELMALLGLEPALRDRYPHQLSGGQQQRVGVARALAANPQVLLMDEPFGALDPvtrgALQAEM 177
Cdd:PRK10619 116 ApIQVLGLSKQEARERAVKYLAKVGIDERAQGKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDP----ELVGEV 191
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 772671321 178 TRIHRIL---GRTIVLVTHDIDEALRLADHLVLMDHGEVVQQGSPLELLTWPKNDFVREFF 235
Cdd:PRK10619 192 LRIMQQLaeeGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGNPQSPRLQQFL 252
|
|
| heterocyst_DevA |
TIGR02982 |
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly ... |
20-214 |
8.67e-38 |
|
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: 133.61 E-value: 8.67e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 20 LNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEIRSLP---VLELRRRMGYAIQSIGLFPHWTVAQNI 96
Cdd:TIGR02982 24 INLEINPGEIVILTGPSGSGKTTLLTLIGGLRSVQEGSLKVLGQELHGASkkqLVQLRRRIGYIFQAHNLLGFLTARQNV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 97 ATVLQL-EKWSRANIADRVDELMALLGLEPALrDRYPHQLSGGQQQRVGVARALAANPQVLLMDEPFGALDPVTRGALQA 175
Cdd:TIGR02982 104 QMALELqPNLSYQEARERARAMLEAVGLGDHL-NYYPHNLSGGQKQRVAIARALVHHPKLVLADEPTAALDSKSGRDVVE 182
|
170 180 190
....*....|....*....|....*....|....*....
gi 772671321 176 EMTRIHRILGRTIVLVTHDiDEALRLADHLVLMDHGEVV 214
Cdd:TIGR02982 183 LMQKLAKEQGCTILMVTHD-NRILDVADRILQMEDGKLL 220
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
19-217 |
8.95e-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: 133.39 E-value: 8.95e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 19 HLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEIRSLPVLElrRRMGYAIQSIGLFPHWTVAQNIAt 98
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPAD--RPVSMLFQENNLFAHLTVEQNVG- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 99 vLQLEKWSRANIADR--VDELMALLGLEpALRDRYPHQLSGGQQQRVGVARALAANPQVLLMDEPFGALDPVTRGALQAE 176
Cdd:cd03298 93 -LGLSPGLKLTAEDRqaIEVALARVGLA-GLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDL 170
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 772671321 177 MTRIHRILGRTIVLVTHDIDEALRLADHLVLMDHGEVVQQG 217
Cdd:cd03298 171 VLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
1-207 |
1.09e-37 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 133.38 E-value: 1.09e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 1 MIEFLDVSKTFAGRPAASHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHD---SGMIRFAGEEIRSLPVLelRRRM 77
Cdd:COG4136 1 MLSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRLTALPAE--QRRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 78 GYAIQSIGLFPHWTVAQNIATVLQlEKWSRANIADRVDELMALLGLePALRDRYPHQLSGGQQQRVGVARALAANPQVLL 157
Cdd:COG4136 79 GILFQDDLLFPHLSVGENLAFALP-PTIGRAQRRARVEQALEEAGL-AGFADRDPATLSGGQRARVALLRALLAEPRALL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 772671321 158 MDEPFGALDPVTRGALQA---EMTRIHRIlgrTIVLVTHDIDEALRLADHLVL 207
Cdd:COG4136 157 LDEPFSKLDAALRAQFREfvfEQIRQRGI---PALLVTHDEEDAPAAGRVLDL 206
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
12-222 |
3.15e-37 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 133.99 E-value: 3.15e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 12 AGRPAASHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEIRSLPVLELRRRMGYAIQSI-GLFPHW 90
Cdd:PRK13635 18 AATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVGMVFQNPdNQFVGA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 91 TVAQNIATVLQLEKWSRANIADRVDELMALLGLEPALrDRYPHQLSGGQQQRVGVARALAANPQVLLMDEPFGALDPVTR 170
Cdd:PRK13635 98 TVQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFL-NREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGR 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 772671321 171 GALQAEMTRIHRILGRTIVLVTHDIDEALRlADHLVLMDHGEVVQQGSPLEL 222
Cdd:PRK13635 177 REVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEI 227
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
2-223 |
4.61e-37 |
|
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: 131.96 E-value: 4.61e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 2 IEFLDVSKTFA-GRPAASHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEIRSLPVLELRRRMGYA 80
Cdd:cd03254 3 IEFENVNFSYDeKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMIGVV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 81 IQSIGLFPHwTVAQNI------ATVlqlEKWSRANIADRVDELMALL--GLEPALRDRyPHQLSGGQQQRVGVARALAAN 152
Cdd:cd03254 83 LQDTFLFSG-TIMENIrlgrpnATD---EEVIEAAKEAGAHDFIMKLpnGYDTVLGEN-GGNLSQGERQLLAIARAMLRD 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 772671321 153 PQVLLMDEPFGALDPVTRGALQAEMTRIHRilGRTIVLVTHdidealRL-----ADHLVLMDHGEVVQQGSPLELL 223
Cdd:cd03254 158 PKILILDEATSNIDTETEKLIQEALEKLMK--GRTSIIIAH------RLstiknADKILVLDDGKIIEEGTHDELL 225
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
34-221 |
5.06e-37 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 135.39 E-value: 5.06e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 34 GTSGSGKSTTLKMINRLVEHDSGMIRFAG------EEIRSLPVlElRRRMGYAIQSIGLFPHWTVAQNiatvlqLEKWSR 107
Cdd:PRK11144 31 GRSGAGKTSLINAISGLTRPQKGRIVLNGrvlfdaEKGICLPP-E-KRRIGYVFQDARLFPHYKVRGN------LRYGMA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 108 ANIADRVDELMALLGLEPALrDRYPHQLSGGQQQRVGVARALAANPQVLLMDEPFGALDPVTRGALQAEMTRIHRILGRT 187
Cdd:PRK11144 103 KSMVAQFDKIVALLGIEPLL-DRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLERLAREINIP 181
|
170 180 190
....*....|....*....|....*....|....
gi 772671321 188 IVLVTHDIDEALRLADHLVLMDHGEVVQQGsPLE 221
Cdd:PRK11144 182 ILYVSHSLDEILRLADRVVVLEQGKVKAFG-PLE 214
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
32-233 |
5.18e-37 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 138.66 E-value: 5.18e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 32 LIGTSGSGKSTTLKMINRLVEHdSGMIRFAGEEIRSLP---VLELRRRMGYAIQ----SigLFPHWTVAQNIA---TVLQ 101
Cdd:COG4172 317 LVGESGSGKSTLGLALLRLIPS-EGEIRFDGQDLDGLSrraLRPLRRRMQVVFQdpfgS--LSPRMTVGQIIAeglRVHG 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 102 LEkWSRANIADRVDELMALLGLEPALRDRYPHQLSGGQQQRVGVARALAANPQVLLMDEPFGALDpVTrgaLQAEMT--- 178
Cdd:COG4172 394 PG-LSAAERRARVAEALEEVGLDPAARHRYPHEFSGGQRQRIAIARALILEPKLLVLDEPTSALD-VS---VQAQILdll 468
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 772671321 179 -RIHRILGRTIVLVTHDIDEALRLADHLVLMDHGEVVQQGSPLELLTWPKNDFVRE 233
Cdd:COG4172 469 rDLQREHGLAYLFISHDLAVVRALAHRVMVMKDGKVVEQGPTEQVFDAPQHPYTRA 524
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-224 |
6.59e-37 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 132.55 E-value: 6.59e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 1 MIEFLDVSKTFAGRPAASHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEIRSLPVLELRRRMGYA 80
Cdd:COG4559 1 MLEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRRAVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 81 IQSIGL-FPhWTVAQNIAtvLQLEKWSRANIADR--VDELMALLGLEpALRDRYPHQLSGGQQQRVGVARALA------- 150
Cdd:COG4559 81 PQHSSLaFP-FTVEEVVA--LGRAPHGSSAAQDRqiVREALALVGLA-HLAGRSYQTLSGGEQQRVQLARVLAqlwepvd 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 772671321 151 ANPQVLLMDEPFGALDPvtrgALQAEMTRIHRIL---GRTIVLVTHDIDEALRLADHLVLMDHGEVVQQGSPLELLT 224
Cdd:COG4559 157 GGPRWLFLDEPTSALDL----AHQHAVLRLARQLarrGGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPEEVLT 229
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
14-233 |
1.55e-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: 137.12 E-value: 1.55e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 14 RPAASHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRL----VEHDSGMIRFAGEEIRSLPVLELRR----RMGYAIQ--S 83
Cdd:COG4172 23 VEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLlpdpAAHPSGSILFDGQDLLGLSERELRRirgnRIAMIFQepM 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 84 IGLFPHWTVAQNIATVLQL-EKWSRANIADRVDELMALLGL-EPALR-DRYPHQLSGGQQQRVGVARALAANPQVLLMDE 160
Cdd:COG4172 103 TSLNPLHTIGKQIAEVLRLhRGLSGAAARARALELLERVGIpDPERRlDAYPHQLSGGQRQRVMIAMALANEPDLLIADE 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 772671321 161 PFGALDpVTrgaLQAE----MTRIHRILGRTIVLVTHDIDEALRLADHLVLMDHGEVVQQGSPLELLTWPKNDFVRE 233
Cdd:COG4172 183 PTTALD-VT---VQAQildlLKDLQRELGMALLLITHDLGVVRRFADRVAVMRQGEIVEQGPTAELFAAPQHPYTRK 255
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
2-223 |
2.79e-36 |
|
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: 130.43 E-value: 2.79e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 2 IEFLDVSKTF--AGRPAASHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEIRSLPVLELRRRMGY 79
Cdd:cd03251 1 VEFKNVTFRYpgDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 80 AIQSIGLFpHWTVAQNI------ATVLQLEKWSR-ANIADRVDELMalLGLEPALRDRyPHQLSGGQQQRVGVARALAAN 152
Cdd:cd03251 81 VSQDVFLF-NDTVAENIaygrpgATREEVEEAARaANAHEFIMELP--EGYDTVIGER-GVKLSGGQRQRIAIARALLKD 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 772671321 153 PQVLLMDEPFGALDPVTRGALQAEMTRIHRilGRTIVLVTHDIdEALRLADHLVLMDHGEVVQQGSPLELL 223
Cdd:cd03251 157 PPILILDEATSALDTESERLVQAALERLMK--NRTTFVIAHRL-STIENADRIVVLEDGKIVERGTHEELL 224
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
2-217 |
6.37e-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: 128.86 E-value: 6.37e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 2 IEFLDVSKTFAG--RPAASHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEIRSLPVLELRRRMGY 79
Cdd:cd03245 3 IEFRNVSFSYPNqeIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 80 AIQSIGLFpHWTVAQNIATVLQLEKWSR----ANIADrVDELMALL--GLEPALRDRyPHQLSGGQQQRVGVARALAANP 153
Cdd:cd03245 83 VPQDVTLF-YGTLRDNITLGAPLADDERilraAELAG-VTDFVNKHpnGLDLQIGER-GRGLSGGQRQAVALARALLNDP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 772671321 154 QVLLMDEPFGALDpvtrgaLQAEMTRIHR----ILGRTIVLVTHDIdEALRLADHLVLMDHGEVVQQG 217
Cdd:cd03245 160 PILLLDEPTSAMD------MNSEERLKERlrqlLGDKTLIIITHRP-SLLDLVDRIIVMDSGRIVADG 220
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1-217 |
7.03e-36 |
|
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: 128.64 E-value: 7.03e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 1 MIEFLDVSKTF---AGRPAA-SHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEIRSLPvLELRRR 76
Cdd:cd03266 1 MITADALTKRFrdvKKTVQAvDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEP-AEARRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 77 MGYAIQSIGLFPHWTVAQNIATVLQLEKWSRANIADRVDELMALLGLEPaLRDRYPHQLSGGQQQRVGVARALAANPQVL 156
Cdd:cd03266 80 LGFVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEE-LLDRRVGGFSTGMRQKVAIARALVHDPPVL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 772671321 157 LMDEPFGALDPVTRGALQaEMTRIHRILGRTIVLVTHDIDEALRLADHLVLMDHGEVVQQG 217
Cdd:cd03266 159 LLDEPTTGLDVMATRALR-EFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1-224 |
8.43e-36 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 129.51 E-value: 8.43e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 1 MIEFLDVSKTFAGRPAASHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEIRSLPVLELRRRMGYA 80
Cdd:PRK13548 2 MLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 81 IQSIGL-FPhWTVAQNIAtvLQLEKWSRANIADR--VDELMALLGLEpALRDRYPHQLSGGQQQRVGVARALA------A 151
Cdd:PRK13548 82 PQHSSLsFP-FTVEEVVA--MGRAPHGLSRAEDDalVAAALAQVDLA-HLAGRDYPQLSGGEQQRVQLARVLAqlwepdG 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 772671321 152 NPQVLLMDEPFGALDPvtrgALQAEMTRIHRIL----GRTIVLVTHDIDEALRLADHLVLMDHGEVVQQGSPLELLT 224
Cdd:PRK13548 158 PPRWLLLDEPTSALDL----AHQHHVLRLARQLaherGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAEVLT 230
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
20-234 |
1.33e-35 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 129.19 E-value: 1.33e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 20 LNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHD-----SGMIRFAGEEIRSLPV--LELRRRMGYAIQSIGLFPHWTV 92
Cdd:PRK14267 23 VDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNeearvEGEVRLFGRNIYSPDVdpIEVRREVGMVFQYPNPFPHLTI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 93 AQNIATVLQLEKW--SRANIADRVDELMALLGLEPALRDR---YPHQLSGGQQQRVGVARALAANPQVLLMDEPFGALDP 167
Cdd:PRK14267 103 YDNVAIGVKLNGLvkSKKELDERVEWALKKAALWDEVKDRlndYPSNLSGGQRQRLVIARALAMKPKILLMDEPTANIDP 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 772671321 168 VTRGALQAEMTRIHRILgrTIVLVTHDIDEALRLADHLVLMDHGEVVQQGSPLELLTWPKNDFVREF 234
Cdd:PRK14267 183 VGTAKIEELLFELKKEY--TIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENPEHELTEKY 247
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-215 |
3.48e-35 |
|
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: 127.16 E-value: 3.48e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 1 MIEFLDVSKTFAGRPAASH----LNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEIRSL---PVLEL 73
Cdd:COG4181 8 IIELRGLTKTVGTGAGELTilkgISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALdedARARL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 74 RRR-MGYAIQSIGLFPHWTVAQNIATVLQLEkwSRANIADRVDELMALLGLEpALRDRYPHQLSGGQQQRVGVARALAAN 152
Cdd:COG4181 88 RARhVGFVFQSFQLLPTLTALENVMLPLELA--GRRDARARARALLERVGLG-HRLDHYPAQLSGGEQQRVALARAFATE 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 772671321 153 PQVLLMDEPFGALDPVTRGALQAEMTRIHRILGRTIVLVTHDIDEALRlADHLVLMDHGEVVQ 215
Cdd:COG4181 165 PAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAAR-CDRVLRLRAGRLVE 226
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
2-217 |
4.57e-35 |
|
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: 126.18 E-value: 4.57e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 2 IEFLDVSKTFAGRPAASHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEIRSLPvlELRRRMGYAI 81
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNI--EALRRIGALI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 82 QSIGLFPHWTVAQNI---ATVLQLEKwsraniaDRVDELMALLGLEpALRDRYPHQLSGGQQQRVGVARALAANPQVLLM 158
Cdd:cd03268 79 EAPGFYPNLTARENLrllARLLGIRK-------KRIDEVLDVVGLK-DSAKKKVKGFSLGMKQRLGIALALLGNPDLLIL 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 772671321 159 DEPFGALDPVTRGALQaEMTRIHRILGRTIVLVTHDIDEALRLADHLVLMDHGEVVQQG 217
Cdd:cd03268 151 DEPTNGLDPDGIKELR-ELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1-226 |
6.29e-35 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 128.00 E-value: 6.29e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 1 MIEFLDVSKTFAGRPAASHlNLNFAEGAFS--VLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEIRSLPVLELRRRMG 78
Cdd:PRK13652 3 LIETRDLCYSYSGSKEALN-NINFIAPRNSriAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 79 YAIQSIG--LFPHwTVAQNIA---TVLQLEKwsrANIADRVDELMALLGLEpALRDRYPHQLSGGQQQRVGVARALAANP 153
Cdd:PRK13652 82 LVFQNPDdqIFSP-TVEQDIAfgpINLGLDE---ETVAHRVSSALHMLGLE-ELRDRVPHHLSGGEKKRVAIAGVIAMEP 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 772671321 154 QVLLMDEPFGALDPVTRGALQAEMTRIHRILGRTIVLVTHDIDEALRLADHLVLMDHGEVVQQGSPLELLTWP 226
Cdd:PRK13652 157 QVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
2-223 |
6.31e-35 |
|
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: 126.58 E-value: 6.31e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 2 IEFLDVskTFA---GRPAASHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEIRSLPVLELRRRMG 78
Cdd:cd03253 1 IEFENV--TFAydpGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 79 YAIQSIGLFpHWTVAQNI------ATVLQLEKWSR-ANIADRVDEL----MALLGlEPALRdryphqLSGGQQQRVGVAR 147
Cdd:cd03253 79 VVPQDTVLF-NDTIGYNIrygrpdATDEEVIEAAKaAQIHDKIMRFpdgyDTIVG-ERGLK------LSGGEKQRVAIAR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 148 ALAANPQVLLMDEPFGALDPVTRGALQAEMTRIHRilGRTIVLVTHdidealRL-----ADHLVLMDHGEVVQQGSPLEL 222
Cdd:cd03253 151 AILKNPPILLLDEATSALDTHTEREIQAALRDVSK--GRTTIVIAH------RLstivnADKIIVLKDGRIVERGTHEEL 222
|
.
gi 772671321 223 L 223
Cdd:cd03253 223 L 223
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
2-224 |
1.68e-34 |
|
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: 132.68 E-value: 1.68e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 2 IEFLDVSKTF--AGRPAASHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEIRSLPVLELRRRMGY 79
Cdd:TIGR03375 464 IEFRNVSFAYpgQETPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQIDPADLRRNIGY 543
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 80 AIQSIGLFpHWTVAQNIAT-VLQLEKWSRANIADR--VDELMALL--GLEPALRDRyPHQLSGGQQQRVGVARALAANPQ 154
Cdd:TIGR03375 544 VPQDPRLF-YGTLRDNIALgAPYADDEEILRAAELagVTEFVRRHpdGLDMQIGER-GRSLSGGQRQAVALARALLRDPP 621
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 772671321 155 VLLMDEPFGALDpvtrgaLQAEMTRIHR----ILGRTIVLVTHDIdEALRLADHLVLMDHGEVVQQGSPLELLT 224
Cdd:TIGR03375 622 ILLLDEPTSAMD------NRSEERFKDRlkrwLAGKTLVLVTHRT-SLLDLVDRIIVMDNGRIVADGPKDQVLE 688
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
20-224 |
2.59e-34 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 125.90 E-value: 2.59e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 20 LNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEIRSLPVLELRRRmgyaiqsIGLFP-HWTVAQNIaT 98
Cdd:PRK11231 21 LSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARR-------LALLPqHHLTPEGI-T 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 99 VLQL---------EKWSRANIADR--VDELMALLGLEpALRDRYPHQLSGGQQQRVGVARALAANPQVLLMDEPFGALDp 167
Cdd:PRK11231 93 VRELvaygrspwlSLWGRLSAEDNarVNQAMEQTRIN-HLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLD- 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 168 VTRgalQAEMTRIHRIL---GRTIVLVTHDIDEALRLADHLVLMDHGEVVQQGSPLELLT 224
Cdd:PRK11231 171 INH---QVELMRLMRELntqGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVMT 227
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1-224 |
5.58e-34 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 124.31 E-value: 5.58e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 1 MIEFLDVSKTFAGRPAasHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEIRSLPvlELRRRMGYA 80
Cdd:PRK10771 1 MLKLTDITWLYHHLPM--RFDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTP--PSRRPVSML 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 81 IQSIGLFPHWTVAQNIAtvLQLEKWSRANIADR--VDELMALLGLEPALrDRYPHQLSGGQQQRVGVARALAANPQVLLM 158
Cdd:PRK10771 77 FQENNLFSHLTVAQNIG--LGLNPGLKLNAAQRekLHAIARQMGIEDLL-ARLPGQLSGGQRQRVALARCLVREQPILLL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 159 DEPFGALDPvtrgALQAEM----TRIHRILGRTIVLVTHDIDEALRLADHLVLMDHGEVVQQGSPLELLT 224
Cdd:PRK10771 154 DEPFSALDP----ALRQEMltlvSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELLS 219
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
2-219 |
5.61e-34 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 125.63 E-value: 5.61e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 2 IEFLDVSKTF-AGRP----AASHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEIRSLP----VLE 72
Cdd:PRK13649 3 INLQNVSYTYqAGTPfegrALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSknkdIKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 73 LRRRMGYAIQsiglFPHW-----TVAQNIATVLQLEKWSRANIADRVDELMALLGLEPALRDRYPHQLSGGQQQRVGVAR 147
Cdd:PRK13649 83 IRKKVGLVFQ----FPESqlfeeTVLKDVAFGPQNFGVSQEEAEALAREKLALVGISESLFEKNPFELSGGQMRRVAIAG 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 772671321 148 ALAANPQVLLMDEPFGALDPVTRGALQAEMTRIHRiLGRTIVLVTHDIDEALRLADHLVLMDHGEVVQQGSP 219
Cdd:PRK13649 159 ILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQ-SGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKP 229
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
6-232 |
9.49e-34 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 124.56 E-value: 9.49e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 6 DVSKTFAGRP---------AASHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEI-------RSLP 69
Cdd:COG4167 9 NLSKTFKYRTglfrrqqfeAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLeygdykyRCKH 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 70 VlelrrRMGYAIQSIGLFPHWTVAQNIATVLQLE-KWSRANIADRVDELMALLGLEPALRDRYPHQLSGGQQQRVGVARA 148
Cdd:COG4167 89 I-----RMIFQDPNTSLNPRLNIGQILEEPLRLNtDLTAEEREERIFATLRLVGLLPEHANFYPHMLSSGQKQRVALARA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 149 LAANPQVLLMDEPFGALDPVTRGALQAEMTRIHRILGRTIVLVTHDIDEALRLADHLVLMDHGEVVQQGSPLELLTWPKN 228
Cdd:COG4167 164 LILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKHISDKVLVMHQGEVVEYGKTAEVFANPQH 243
|
....
gi 772671321 229 DFVR 232
Cdd:COG4167 244 EVTK 247
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
5-228 |
2.36e-33 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 123.67 E-value: 2.36e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 5 LDVSKTFAGRPAASHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMiRFAGEEI---RSL----PVLELRRRM 77
Cdd:PRK14271 25 VNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGY-RYSGDVLlggRSIfnyrDVLEFRRRV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 78 GYAIQSIGLFPHWTVAQNIATVLQLEKWSRANIADRVDELMALLGLEPALRDRY---PHQLSGGQQQRVGVARALAANPQ 154
Cdd:PRK14271 104 GMLFQRPNPFPMSIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLWDAVKDRLsdsPFRLSGGQQQLLCLARTLAVNPE 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 772671321 155 VLLMDEPFGALDPVTRGALQAEMTRIHRILgrTIVLVTHDIDEALRLADHLVLMDHGEVVQQGSPLELLTWPKN 228
Cdd:PRK14271 184 VLLLDEPTSALDPTTTEKIEEFIRSLADRL--TVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKH 255
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
6-223 |
2.39e-33 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 122.69 E-value: 2.39e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 6 DVSKTFAGRPAASHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEIRSLPVLELRRR-MGYAIQSI 84
Cdd:PRK10895 8 NLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRgIGYLPQEA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 85 GLFPHWTVAQNIATVLQLEK-WSRANIADRVDELMALLGLEpALRDRYPHQLSGGQQQRVGVARALAANPQVLLMDEPFG 163
Cdd:PRK10895 88 SIFRRLSVYDNLMAVLQIRDdLSAEQREDRANELMEEFHIE-HLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 164 ALDPVTRGALQAEMTRIhRILGRTIVLVTHDIDEALRLADHLVLMDHGEVVQQGSPLELL 223
Cdd:PRK10895 167 GVDPISVIDIKRIIEHL-RDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEIL 225
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1-234 |
4.49e-33 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 122.95 E-value: 4.49e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 1 MIEFLDVSKTFAGRPAASHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEIRSLP---VLELRRRM 77
Cdd:PRK11831 7 LVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSrsrLYTVRKRM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 78 GYAIQSIGLFPHWTVAQNIATVLQlEKWSRANIADRVDELMAL--LGLEPAlRDRYPHQLSGGQQQRVGVARALAANPQV 155
Cdd:PRK11831 87 SMLFQSGALFTDMNVFDNVAYPLR-EHTQLPAPLLHSTVMMKLeaVGLRGA-AKLMPSELSGGMARRAALARAIALEPDL 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 772671321 156 LLMDEPFGALDPVTRGALQAEMTRIHRILGRTIVLVTHDIDEALRLADHLVLMDHGEVVQQGSPLELLTWPkNDFVREF 234
Cdd:PRK11831 165 IMFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQANP-DPRVRQF 242
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
2-233 |
9.29e-33 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 122.63 E-value: 9.29e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 2 IEFLDVSKTFA-GRP--AASHLNLNF--AEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEIR----SLPVLE 72
Cdd:PRK13641 3 IKFENVDYIYSpGTPmeKKGLDNISFelEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpetgNKNLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 73 LRRRMGYAIQsiglFPHWTVAQNiaTVLQLEKWSRANIADRVDEL-------MALLGLEPALRDRYPHQLSGGQQQRVGV 145
Cdd:PRK13641 83 LRKKVSLVFQ----FPEAQLFEN--TVLKDVEFGPKNFGFSEDEAkekalkwLKKVGLSEDLISKSPFELSGGQMRRVAI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 146 ARALAANPQVLLMDEPFGALDPVTRgalqAEMTRI---HRILGRTIVLVTHDIDEALRLADHLVLMDHGEVVQQGSPLEL 222
Cdd:PRK13641 157 AGVMAYEPEILCLDEPAAGLDPEGR----KEMMQLfkdYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEI 232
|
250
....*....|....
gi 772671321 223 LT---WPKNDFVRE 233
Cdd:PRK13641 233 FSdkeWLKKHYLDE 246
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
20-218 |
1.58e-32 |
|
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: 120.32 E-value: 1.58e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 20 LNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEIRSLPVLELRRR-MGYAIQSIGLFPHWTVAQNIAT 98
Cdd:TIGR03410 19 VSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERARAgIAYVPQGREIFPRLTVEENLLT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 99 VLQLEKWSRANIADRVDELMallglePALRD---RYPHQLSGGQQQRVGVARALAANPQVLLMDEPFGALDPVTRGALQA 175
Cdd:TIGR03410 99 GLAALPRRSRKIPDEIYELF------PVLKEmlgRRGGDLSGGQQQQLAIARALVTRPKLLLLDEPTEGIQPSIIKDIGR 172
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 772671321 176 EMTRIHRILGRTIVLVTHDIDEALRLADHLVLMDHGEVVQQGS 218
Cdd:TIGR03410 173 VIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRVVASGA 215
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
6-236 |
3.24e-32 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 120.27 E-value: 3.24e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 6 DVSKTFAGRPAASHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHD-----SGMIRFAGEEIRS--LPVLELRRRMG 78
Cdd:PRK14239 10 DLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLNpevtiTGSIVYNGHNIYSprTDTVDLRKEIG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 79 YAIQSIGLFPhWTVAQNIATVLQLEKWSRANIADRVDElMALLG--LEPALRDRYpHQ----LSGGQQQRVGVARALAAN 152
Cdd:PRK14239 90 MVFQQPNPFP-MSIYENVVYGLRLKGIKDKQVLDEAVE-KSLKGasIWDEVKDRL-HDsalgLSGGQQQRVCIARVLATS 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 153 PQVLLMDEPFGALDPVTRGALQAEMTRIHRilGRTIVLVTHDIDEALRLADHLVLMDHGEVVQQGSPLELLTWPKN---- 228
Cdd:PRK14239 167 PKIILLDEPTSALDPISAGKIEETLLGLKD--DYTMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQMFMNPKHkete 244
|
....*...
gi 772671321 229 DFVREFFG 236
Cdd:PRK14239 245 DYISGKFG 252
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
32-222 |
3.83e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 120.61 E-value: 3.83e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 32 LIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEIRSLPVLELRRRMGYAIQSI-GLFPHWTVAQNIATVLQLEKWSRANI 110
Cdd:PRK13650 38 IIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIGMVFQNPdNQFVGATVEDDVAFGLENKGIPHEEM 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 111 ADRVDELMALLGLEpALRDRYPHQLSGGQQQRVGVARALAANPQVLLMDEPFGALDPVTRGALQAEMTRIHRILGRTIVL 190
Cdd:PRK13650 118 KERVNEALELVGMQ-DFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVIS 196
|
170 180 190
....*....|....*....|....*....|..
gi 772671321 191 VTHDIDEaLRLADHLVLMDHGEVVQQGSPLEL 222
Cdd:PRK13650 197 ITHDLDE-VALSDRVLVMKNGQVESTSTPREL 227
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
11-208 |
3.84e-32 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 118.11 E-value: 3.84e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 11 FAGRPAASHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAG-----------EEIRSLPvLELRRRMgy 79
Cdd:NF040873 2 YGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGgarvayvpqrsEVPDSLP-LTVRDLV-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 80 aiqSIGLFPHwtvaqniatvlqLEKWSRANIADR--VDELMALLGLEpALRDRYPHQLSGGQQQRVGVARALAANPQVLL 157
Cdd:NF040873 79 ---AMGRWAR------------RGLWRRLTRDDRaaVDDALERVGLA-DLAGRQLGELSGGQRQRALLAQGLAQEADLLL 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 772671321 158 MDEPFGALDPVTRGALQAEMTRIHRiLGRTIVLVTHDIDEAlRLADHLVLM 208
Cdd:NF040873 143 LDEPTTGLDAESRERIIALLAEEHA-RGATVVVVTHDLELV-RRADPCVLL 191
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
2-222 |
4.50e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 120.65 E-value: 4.50e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 2 IEFLDVSKTF-AGRP----AASHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEIRSLP----VLE 72
Cdd:PRK13646 3 IRFDNVSYTYqKGTPyehqAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTkdkyIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 73 LRRRMGYAIQsiglFPHW-----TVAQNIATVLQLEKWSRANIADRVDELMALLGLEPALRDRYPHQLSGGQQQRVGVAR 147
Cdd:PRK13646 83 VRKRIGMVFQ----FPESqlfedTVEREIIFGPKNFKMNLDEVKNYAHRLLMDLGFSRDVMSQSPFQMSGGQMRKIAIVS 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 772671321 148 ALAANPQVLLMDEPFGALDPVTRGALQAEMTRIHRILGRTIVLVTHDIDEALRLADHLVLMDHGEVVQQGSPLEL 222
Cdd:PRK13646 159 ILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKEL 233
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
6-224 |
4.65e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 120.88 E-value: 4.65e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 6 DVSKTFAGRP-----AASHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEI-----RSLPVLELRR 75
Cdd:PRK13645 11 NVSYTYAKKTpfefkALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIpanlkKIKEVKRLRK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 76 RMGYAIQsiglFPHW-----TVAQNIATVLQLEKWSRANIADRVDELMALLGLEPALRDRYPHQLSGGQQQRVGVARALA 150
Cdd:PRK13645 91 EIGLVFQ----FPEYqlfqeTIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLPEDYVKRSPFELSGGQKRRVALAGIIA 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 772671321 151 ANPQVLLMDEPFGALDPVTRGALQAEMTRIHRILGRTIVLVTHDIDEALRLADHLVLMDHGEVVQQGSPLELLT 224
Cdd:PRK13645 167 MDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFS 240
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
2-227 |
1.00e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 119.46 E-value: 1.00e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 2 IEFLDVSKTFA-GRPAASHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEIRSLPVLELRRRMGYA 80
Cdd:PRK13647 5 IEVEDLHFRYKdGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGLV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 81 IQSIG--LFPHwTVAQNIATVLQLEKWSRANIADRVDELMALLGLEpALRDRYPHQLSGGQQQRVGVARALAANPQVLLM 158
Cdd:PRK13647 85 FQDPDdqVFSS-TVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMW-DFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 772671321 159 DEPFGALDPVTRGALQAEMTRIHRiLGRTIVLVTHDIDEALRLADHLVLMDHGEVVQQGSPlELLTWPK 227
Cdd:PRK13647 163 DEPMAYLDPRGQETLMEILDRLHN-QGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDK-SLLTDED 229
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
2-208 |
1.37e-31 |
|
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: 123.55 E-value: 1.37e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 2 IEFLDVSKTFAGR-PAASHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEIRSLPVLELRRRMGYA 80
Cdd:TIGR02857 322 LEFSGVSVAYPGRrPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWV 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 81 IQSIGLFPHwTVAQNIAtvLQLEKWSRANIAdRVDELMALLGLEPALRDRY-------PHQLSGGQQQRVGVARALAANP 153
Cdd:TIGR02857 402 PQHPFLFAG-TIAENIR--LARPDASDAEIR-EALERAGLDEFVAALPQGLdtpigegGAGLSGGQAQRLALARAFLRDA 477
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 772671321 154 QVLLMDEPFGALDPVTRGALQAEMTRIHRilGRTIVLVTHDiDEALRLADHLVLM 208
Cdd:TIGR02857 478 PLLLLDEPTAHLDAETEAEVLEALRALAQ--GRTVLLVTHR-LALAALADRIVVL 529
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
2-214 |
2.46e-31 |
|
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: 115.22 E-value: 2.46e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 2 IEFLDVSKTFAGRPAASHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEIRSLPVLElRRRMGyai 81
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRD-ARRAG--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 82 qsiglfphwtvaqnIATVlqlekwsraniadrvdelmallglepalrdrypHQLSGGQQQRVGVARALAANPQVLLMDEP 161
Cdd:cd03216 77 --------------IAMV---------------------------------YQLSVGERQMVEIARALARNARLLILDEP 109
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 772671321 162 FGALDPVTRGALQAEMTRIhRILGRTIVLVTHDIDEALRLADHLVLMDHGEVV 214
Cdd:cd03216 110 TAALTPAEVERLFKVIRRL-RAQGVAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-211 |
2.74e-31 |
|
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: 116.76 E-value: 2.74e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 1 MIEFLDVSKTF-------AGRPAASHLNLNFAEGAFSVLIGTSGSGKSTTLKMINR---------LVEHDSGMIRFAGEE 64
Cdd:COG4778 4 LLEVENLSKTFtlhlqggKRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGnylpdsgsiLVRHDGGWVDLAQAS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 65 IRSlpVLELRRR-MGYAIQSIGLFPHWTVAQNIATVLQLEKWSRANIADRVDELMALLGLEPALRDRYPHQLSGGQQQRV 143
Cdd:COG4778 84 PRE--ILALRRRtIGYVSQFLRVIPRVSALDVVAEPLLERGVDREEARARARELLARLNLPERLWDLPPATFSGGEQQRV 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 144 GVARALAANPQVLLMDEPFGALDPVTRgalQAEMTRIHRIL--GRTIVLVTHDIDEALRLADHLVLMDHG 211
Cdd:COG4778 162 NIARGFIADPPLLLLDEPTASLDAANR---AVVVELIEEAKarGTAIIGIFHDEEVREAVADRVVDVTPF 228
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
6-213 |
3.37e-31 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 117.47 E-value: 3.37e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 6 DVSKTFAGRPAASHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRfAGeeirSLPVLELRRRMGYAIQSIG 85
Cdd:PRK11247 17 AVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELL-AG----TAPLAEAREDTRLMFQDAR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 86 LFPHWTVAQNIATVLqlekwsRANIADRVDELMALLGLEPALRDrYPHQLSGGQQQRVGVARALAANPQVLLMDEPFGAL 165
Cdd:PRK11247 92 LLPWKKVIDNVGLGL------KGQWRDAALQALAAVGLADRANE-WPAALSGGQKQRVALARALIHRPGLLLLDEPLGAL 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 772671321 166 DPVTRGALQAEMTRIHRILGRTIVLVTHDIDEALRLADHLVLMDHGEV 213
Cdd:PRK11247 165 DALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
1-242 |
5.51e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 117.91 E-value: 5.51e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 1 MIEFLDVSKTFA-GRPAASH----LNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEIRSLP----VL 71
Cdd:PRK13643 1 MIKFEKVNYTYQpNSPFASRalfdIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSkqkeIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 72 ELRRRMGYAIQsiglFPHW-----TVAQNIATVLQLEKWSRANIADRVDELMALLGLEPALRDRYPHQLSGGQQQRVGVA 146
Cdd:PRK13643 81 PVRKKVGVVFQ----FPESqlfeeTVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLADEFWEKSPFELSGGQMRRVAIA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 147 RALAANPQVLLMDEPFGALDPVTRGALQAEMTRIHRIlGRTIVLVTHDIDEALRLADHLVLMDHGEVVQQGSPLELLTwp 226
Cdd:PRK13643 157 GILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQS-GQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQ-- 233
|
250
....*....|....*.
gi 772671321 227 KNDFVREffgrSELGV 242
Cdd:PRK13643 234 EVDFLKA----HELGV 245
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-266 |
5.54e-31 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 118.37 E-value: 5.54e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 2 IEFLDVSKTFAGRPAASHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEIRSlPVLELRRRMGYAI 81
Cdd:PRK13537 8 IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPS-RARHARQRVGVVP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 82 QSIGLFPHWTVAQNIATVLQLEKWSRANIADRVDELMALLGLEPAlRDRYPHQLSGGQQQRVGVARALAANPQVLLMDEP 161
Cdd:PRK13537 87 QFDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENK-ADAKVGELSGGMKRRLTLARALVNDPDVLVLDEP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 162 FGALDPVTRgALQAEMTRIHRILGRTIVLVTHDIDEALRLADHLVLMDHGEVVQQGSPLELLTWPKNDFVREFFGRSelg 241
Cdd:PRK13537 166 TTGLDPQAR-HLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIESEIGCDVIEIYGPD--- 241
|
250 260
....*....|....*....|....*.
gi 772671321 242 vrLLSLRT-VSDYMRREEMpvSGEPL 266
Cdd:PRK13537 242 --PVALRDeLAPLAERTEI--SGETL 263
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
16-232 |
5.68e-31 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 118.66 E-value: 5.68e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 16 AASHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEIRSLPVLELRRRMGyAIQSI------GLFPH 89
Cdd:PRK15079 36 AVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRAVRS-DIQMIfqdplaSLNPR 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 90 WTVAQNIATVLQL--EKWSRANIADRVDELMALLGLEPALRDRYPHQLSGGQQQRVGVARALAANPQVLLMDEPFGALDP 167
Cdd:PRK15079 115 MTIGEIIAEPLRTyhPKLSRQEVKDRVKAMMLKVGLLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDV 194
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 772671321 168 vtrgALQAE----MTRIHRILGRTIVLVTHDIDEALRLADHLVLMDHGEVVQQGSPLELLTWPKNDFVR 232
Cdd:PRK15079 195 ----SIQAQvvnlLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNPLHPYTK 259
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
21-217 |
6.87e-31 |
|
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: 115.73 E-value: 6.87e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 21 NLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEIRSLPvlELRRRMGYAIQSIGLFPHWTVAQNIATVL 100
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLA--PYQRPVSMLFQENNLFAHLTVRQNIGLGL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 101 QLEKWSRANIADRVDELMALLGLEPALrDRYPHQLSGGQQQRVGVARALAANPQVLLMDEPFGALDPVTRGALQAEMTRI 180
Cdd:TIGR01277 96 HPGLKLNAEQQEKVVDAAQQVGIADYL-DRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALVKQL 174
|
170 180 190
....*....|....*....|....*....|....*..
gi 772671321 181 HRILGRTIVLVTHDIDEALRLADHLVLMDHGEVVQQG 217
Cdd:TIGR01277 175 CSERQRTLLMVTHHLSDARAIASQIAVVSQGKIKVVS 211
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
2-222 |
7.45e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 117.21 E-value: 7.45e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 2 IEFLDVSKTF--AGRPAASHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLV---EHDSGMIRFAGEEIRSLPVLELRRR 76
Cdd:PRK13640 6 VEFKHVSFTYpdSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLlpdDNPNSKITVDGITLTAKTVWDIREK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 77 MGYAIQSI-GLFPHWTVAQNIATVLQLEKWSRANIADRVDELMALLGLEPaLRDRYPHQLSGGQQQRVGVARALAANPQV 155
Cdd:PRK13640 86 VGIVFQNPdNQFVGATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLD-YIDSEPANLSGGQKQRVAIAGILAVEPKI 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 772671321 156 LLMDEPFGALDPVTRGALQAEMTRIHRILGRTIVLVTHDIDEAlRLADHLVLMDHGEVVQQGSPLEL 222
Cdd:PRK13640 165 IILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEA-NMADQVLVLDDGKLLAQGSPVEI 230
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1-222 |
1.13e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 116.73 E-value: 1.13e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 1 MIEFLDVSKTFAG------RPAASHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEIRSLP-VLEL 73
Cdd:PRK13633 4 MIKCKNVSYKYESneesteKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEEnLWDI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 74 RRRMGYAIQSiglfPHwtvAQNIATVLQLE-KWSRAN-------IADRVDELMALLGLEpALRDRYPHQLSGGQQQRVGV 145
Cdd:PRK13633 84 RNKAGMVFQN----PD---NQIVATIVEEDvAFGPENlgippeeIRERVDESLKKVGMY-EYRRHAPHLLSGGQKQRVAI 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 772671321 146 ARALAANPQVLLMDEPFGALDPVTRGALQAEMTRIHRILGRTIVLVTHDIDEALRlADHLVLMDHGEVVQQGSPLEL 222
Cdd:PRK13633 156 AGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEI 231
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
20-223 |
2.55e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 115.96 E-value: 2.55e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 20 LNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEIRSLPVLELRRRMGYAIQSI-GLFPHWTVAQNIAT 98
Cdd:PRK13642 26 VSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIGMVFQNPdNQFVGATVEDDVAF 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 99 VLQLEKWSRANIADRVDE-LMALLGLEpaLRDRYPHQLSGGQQQRVGVARALAANPQVLLMDEPFGALDPVTRGALqaeM 177
Cdd:PRK13642 106 GMENQGIPREEMIKRVDEaLLAVNMLD--FKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEI---M 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 772671321 178 TRIHRILGR---TIVLVTHDIDEALRlADHLVLMDHGEVVQQGSPLELL 223
Cdd:PRK13642 181 RVIHEIKEKyqlTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELF 228
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
6-223 |
2.86e-30 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 115.27 E-value: 2.86e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 6 DVSKTFAGRPAASHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEIRSLPVLELRRRMGYAIQSIG 85
Cdd:PRK10575 16 NVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLPQQLP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 86 LFPHWTVAQNIAtvLQLEKW----SRANIADR--VDELMALLGLEPaLRDRYPHQLSGGQQQRVGVARALAANPQVLLMD 159
Cdd:PRK10575 96 AAEGMTVRELVA--IGRYPWhgalGRFGAADRekVEEAISLVGLKP-LAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLD 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 772671321 160 EPFGALDPVTRGALQAEMTRIHRILGRTIVLVTHDIDEALRLADHLVLMDHGEVVQQGSPLELL 223
Cdd:PRK10575 173 EPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELM 236
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-266 |
3.67e-30 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 116.85 E-value: 3.67e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 2 IEFLDVSKTFAGRPAASHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEIRSLPVLElRRRMGYAI 81
Cdd:PRK13536 42 IDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLA-RARIGVVP 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 82 QSIGLFPHWTVAQNIATVLQLEKWSRANIADRVDELMALLGLEPALRDRYPhQLSGGQQQRVGVARALAANPQVLLMDEP 161
Cdd:PRK13536 121 QFDNLDLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVS-DLSGGMKRRLTLARALINDPQLLILDEP 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 162 FGALDPVTRgALQAEMTRIHRILGRTIVLVTHDIDEALRLADHLVLMDHGEVVQQGSPLELLTWPKNDFVREFFGRSELG 241
Cdd:PRK13536 200 TTGLDPHAR-HLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHALIDEHIGCQVIEIYGGDPHE 278
|
250 260
....*....|....*....|....*
gi 772671321 242 VRLLslrtVSDYMRREEmpVSGEPL 266
Cdd:PRK13536 279 LSSL----VKPYARRIE--VSGETL 297
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
13-223 |
4.08e-30 |
|
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: 114.12 E-value: 4.08e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 13 GRPAASHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEIRSLPVLELRRRMGYAIQSIGLFPHwTV 92
Cdd:cd03252 14 GPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGVVLQENVLFNR-SI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 93 AQNIA---TVLQLEK-WSRANIADRVDELMAL-LGLEPALRDRyPHQLSGGQQQRVGVARALAANPQVLLMDEPFGALDP 167
Cdd:cd03252 93 RDNIAladPGMSMERvIEAAKLAGAHDFISELpEGYDTIVGEQ-GAGLSGGQRQRIAIARALIHNPRILIFDEATSALDY 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 772671321 168 VTRGALQAEMtriHRIL-GRTIVLVTHDIdEALRLADHLVLMDHGEVVQQGSPLELL 223
Cdd:cd03252 172 ESEHAIMRNM---HDICaGRTVIIIAHRL-STVKNADRIIVMEKGRIVEQGSHDELL 224
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
18-237 |
4.11e-30 |
|
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: 114.00 E-value: 4.11e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 18 SHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVehDSGMIRFAGE-EIRSLPVLELR---RRMGYAIQS-IGLF-PHWT 91
Cdd:TIGR02770 3 QDLNLSLKRGEVLALVGESGSGKSLTCLAILGLL--PPGLTQTSGEiLLDGRPLLPLSirgRHIATIMQNpRTAFnPLFT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 92 VA-QNIATVLQLEKWSrANIADRVDELMALLGLEPALR--DRYPHQLSGGQQQRVGVARALAANPQVLLMDEPFGALDPV 168
Cdd:TIGR02770 81 MGnHAIETLRSLGKLS-KQARALILEALEAVGLPDPEEvlKKYPFQLSGGMLQRVMIALALLLEPPFLIADEPTTDLDVV 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 772671321 169 TRGALQAEMTRIHRILGRTIVLVTHDIDEALRLADHLVLMDHGEVVQQGSPLELLTWPKNDFVREFFGR 237
Cdd:TIGR02770 160 NQARVLKLLRELRQLFGTGILLITHDLGVVARIADEVAVMDDGRIVERGTVKEIFYNPKHETTRKLLSA 228
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1-195 |
9.42e-30 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 112.66 E-value: 9.42e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 1 MIEFLDVSKTF-AGRPAASHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEIRSLPVLE---LRRR 76
Cdd:PRK10908 1 MIRFEHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREvpfLRRQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 77 MGYAIQSIGLFPHWTVAQNIATVLQLEKWSRANIADRVDELMALLGLEPALRDrYPHQLSGGQQQRVGVARALAANPQVL 156
Cdd:PRK10908 81 IGMIFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKN-FPIQLSGGEQQRVGIARAVVNKPAVL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 772671321 157 LMDEPFGALDpvtrGALQAEMTRIHRILGR---TIVLVTHDI 195
Cdd:PRK10908 160 LADEPTGNLD----DALSEGILRLFEEFNRvgvTVLMATHDI 197
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1-222 |
1.06e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 114.08 E-value: 1.06e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 1 MIEFLDVSKTFAGRPAAS--HLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEIRSLPVLELRRRMG 78
Cdd:PRK13648 7 IIVFKNVSFQYQSDASFTlkDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 79 YAIQSI-GLFPHWTVAQNIATVLQLEKWSRANIADRVDELMALLGLEpALRDRYPHQLSGGQQQRVGVARALAANPQVLL 157
Cdd:PRK13648 87 IVFQNPdNQFVGSIVKYDVAFGLENHAVPYDEMHRRVSEALKQVDML-ERADYEPNALSGGQKQRVAIAGVLALNPSVII 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 772671321 158 MDEPFGALDPVTRGALQAEMTRIHRILGRTIVLVTHDIDEALRlADHLVLMDHGEVVQQGSPLEL 222
Cdd:PRK13648 166 LDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEI 229
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-214 |
1.47e-29 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 117.43 E-value: 1.47e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 1 MIEFLDVSKTFAGRPAASHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEIRSLPVLElRRRMGYA 80
Cdd:COG1129 4 LLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRD-AQAAGIA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 81 I--QSIGLFPHWTVAQNIATVLQLEKW---SRANIADRVDELMALLGLE--PA--LRDryphqLSGGQQQRVGVARALAA 151
Cdd:COG1129 83 IihQELNLVPNLSVAENIFLGREPRRGgliDWRAMRRRARELLARLGLDidPDtpVGD-----LSVAQQQLVEIARALSR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 152 NPQVLLMDEPFGALDPvtrgalqAEMTRIHRIL------GRTIVLVTHDIDEALRLADHL-VLMDhGEVV 214
Cdd:COG1129 158 DARVLILDEPTASLTE-------REVERLFRIIrrlkaqGVAIIYISHRLDEVFEIADRVtVLRD-GRLV 219
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
13-223 |
2.59e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 113.40 E-value: 2.59e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 13 GRPAASHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEI--RSLPVLELRRRMGYAIQSIG--LFP 88
Cdd:PRK13636 18 GTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIdySRKGLMKLRESVGMVFQDPDnqLFS 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 89 HwTVAQNIATVLQLEKWSRANIADRVDELMALLGLEPaLRDRYPHQLSGGQQQRVGVARALAANPQVLLMDEPFGALDPV 168
Cdd:PRK13636 98 A-SVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEH-LKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPM 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 772671321 169 TRGALQAEMTRIHRILGRTIVLVTHDIDEALRLADHLVLMDHGEVVQQGSPLELL 223
Cdd:PRK13636 176 GVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVF 230
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-226 |
3.75e-29 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 115.32 E-value: 3.75e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 1 MIEFLDVSKTFAGRPAASHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEIRSLPVLELRRRMGYA 80
Cdd:PRK09536 3 MIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 81 IQSIGLFPHWTVAQNI--ATVLQLEKWSRANIADR--VDELMALLGLEpALRDRYPHQLSGGQQQRVGVARALAANPQVL 156
Cdd:PRK09536 83 PQDTSLSFEFDVRQVVemGRTPHRSRFDTWTETDRaaVERAMERTGVA-QFADRPVTSLSGGERQRVLLARALAQATPVL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 157 LMDEPFGALDpVTRGALQAEMTRIHRILGRTIVLVTHDIDEALRLADHLVLMDHGEVVQQGSPLELLTWP 226
Cdd:PRK09536 162 LLDEPTASLD-INHQVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVLTAD 230
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
11-198 |
1.29e-28 |
|
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: 108.66 E-value: 1.29e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 11 FAGRPAA-SHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEI----RSLpvLELRRRMGYAIQSIG 85
Cdd:TIGR01166 1 YPGGPEVlKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPLdysrKGL--LERRQRVGLVFQDPD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 86 --LFPHwTVAQNIATVLQLEKWSRANIADRVDELMALLGLEpALRDRYPHQLSGGQQQRVGVARALAANPQVLLMDEPFG 163
Cdd:TIGR01166 79 dqLFAA-DVDQDVAFGPLNLGLSEAEVERRVREALTAVGAS-GLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTA 156
|
170 180 190
....*....|....*....|....*....|....*
gi 772671321 164 ALDPVTRGALQAEMTRIhRILGRTIVLVTHDIDEA 198
Cdd:TIGR01166 157 GLDPAGREQMLAILRRL-RAEGMTVVISTHDVDLA 190
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
2-223 |
1.44e-28 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 115.12 E-value: 1.44e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 2 IEFLDVSKTFAGR--PAASHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEIRSLPVLELRRRMGY 79
Cdd:PRK11176 342 IEFRNVTFTYPGKevPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVAL 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 80 AIQSIGLFPHwTVAQNIATVLQlEKWSRANI--ADRVDELMALL-----GLEPALRDRyPHQLSGGQQQRVGVARALAAN 152
Cdd:PRK11176 422 VSQNVHLFND-TIANNIAYART-EQYSREQIeeAARMAYAMDFInkmdnGLDTVIGEN-GVLLSGGQRQRIAIARALLRD 498
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 772671321 153 PQVLLMDEPFGALDPVTRGALQAEMTRIHRilGRTIVLVTHdidealRL-----ADHLVLMDHGEVVQQGSPLELL 223
Cdd:PRK11176 499 SPILILDEATSALDTESERAIQAALDELQK--NRTSLVIAH------RLstiekADEILVVEDGEIVERGTHAELL 566
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
16-223 |
1.45e-28 |
|
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: 114.90 E-value: 1.45e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 16 AASHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRF-AGEEIRSL--PVLELRRR----MGYAIQSIGLFP 88
Cdd:TIGR03269 299 AVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrVGDEWVDMtkPGPDGRGRakryIGILHQEYDLYP 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 89 HWTVAQNIATVLQLEkwsranIADRVDELMALLGLEPA---------LRDRYPHQLSGGQQQRVGVARALAANPQVLLMD 159
Cdd:TIGR03269 379 HRTVLDNLTEAIGLE------LPDELARMKAVITLKMVgfdeekaeeILDKYPDELSEGERHRVALAQVLIKEPRIVILD 452
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 772671321 160 EPFGALDPVTRGALQAEMTRIHRILGRTIVLVTHDIDEALRLADHLVLMDHGEVVQQGSPLELL 223
Cdd:TIGR03269 453 EPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEEIV 516
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1-227 |
1.58e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 110.94 E-value: 1.58e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 1 MIEFLDVSKTFA-GRPAASHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEI----RSLpvLELRR 75
Cdd:PRK13639 1 ILETRDLKYSYPdGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIkydkKSL--LEVRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 76 RMGYAIQSIG--LF-PhwTVAQNIATVLQLEKWSRANIADRVDELMALLGLEpALRDRYPHQLSGGQQQRVGVARALAAN 152
Cdd:PRK13639 79 TVGIVFQNPDdqLFaP--TVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGME-GFENKPPHHLSGGQKKRVAIAGILAMK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 153 PQVLLMDEPFGALDPvtRGALQaemtrIHRIL------GRTIVLVTHDIDEALRLADHLVLMDHGEVVQQGSPLELLTWP 226
Cdd:PRK13639 156 PEIIVLDEPTSGLDP--MGASQ-----IMKLLydlnkeGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDI 228
|
.
gi 772671321 227 K 227
Cdd:PRK13639 229 E 229
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1-264 |
1.74e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 110.85 E-value: 1.74e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 1 MIEFLDVSKTFA-GRPAASHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEIRSLPVL-ELRRRMG 78
Cdd:PRK13644 1 MIRLENVSYSYPdGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKLqGIRKLVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 79 YAIQSIGL-FPHWTVAQNIATVLQLEKWSRANIADRVDELMALLGLEpALRDRYPHQLSGGQQQRVGVARALAANPQVLL 157
Cdd:PRK13644 81 IVFQNPETqFVGRTVEEDLAFGPENLCLPPIEIRKRVDRALAEIGLE-KYRHRSPKTLSGGQGQCVALAGILTMEPECLI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 158 MDEPFGALDPVTRGALQAEMTRIHRiLGRTIVLVTHDIDEaLRLADHLVLMDHGEVVQQGSPLELLTWPKndfvreffgR 237
Cdd:PRK13644 160 FDEVTSMLDPDSGIAVLERIKKLHE-KGKTIVYITHNLEE-LHDADRIIVMDRGKIVLEGEPENVLSDVS---------L 228
|
250 260
....*....|....*....|....*..
gi 772671321 238 SELGVRLLSLRTVSDYMRREEMPVSGE 264
Cdd:PRK13644 229 QTLGLTPPSLIELAENLKMHGVVIPWE 255
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
13-235 |
2.88e-28 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 115.11 E-value: 2.88e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 13 GRPAASHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEIRSlPVLELRRRMGYAIQSIGLFPHWTV 92
Cdd:TIGR01257 942 GRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIET-NLDAVRQSLGMCPQHNILFHHLTV 1020
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 93 AQNIATVLQLE--KWSRANIadrvdELMALL---GLEPAlRDRYPHQLSGGQQQRVGVARALAANPQVLLMDEPFGALDP 167
Cdd:TIGR01257 1021 AEHILFYAQLKgrSWEEAQL-----EMEAMLedtGLHHK-RNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDP 1094
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 772671321 168 VTRGALQAEMTRIHRilGRTIVLVTHDIDEALRLADHLVLMDHGEVVQQGSPLELltwpKNDFVREFF 235
Cdd:TIGR01257 1095 YSRRSIWDLLLKYRS--GRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTPLFL----KNCFGTGFY 1156
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
22-224 |
3.77e-28 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 109.78 E-value: 3.77e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 22 LNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEeirslPVLELRRRMGYAIQ---------SIGLF-PHWT 91
Cdd:PRK10419 33 LSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGE-----PLAKLNRAQRKAFRrdiqmvfqdSISAVnPRKT 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 92 VAQNIATVLQ-LEKWSRANIADRVDELMALLGLEPALRDRYPHQLSGGQQQRVGVARALAANPQVLLMDEPFGALDPVTR 170
Cdd:PRK10419 108 VREIIREPLRhLLSLDKAERLARASEMLRAVDLDDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQ 187
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 772671321 171 GALQAEMTRIHRILGRTIVLVTHDIDEALRLADHLVLMDHGEVVQQGSPLELLT 224
Cdd:PRK10419 188 AGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVETQPVGDKLT 241
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
6-218 |
7.46e-28 |
|
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: 107.87 E-value: 7.46e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 6 DVSKTFAGRPAASHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEI--RSLpvlelrRRMGYAIQS 83
Cdd:TIGR03740 5 NLSKRFGKQTAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGHPWtrKDL------HKIGSLIES 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 84 IGLFPHWTVAQNI---ATVLQLEKwsraniaDRVDELMALLGLEPALRDRyPHQLSGGQQQRVGVARALAANPQVLLMDE 160
Cdd:TIGR03740 79 PPLYENLTARENLkvhTTLLGLPD-------SRIDEVLNIVDLTNTGKKK-AKQFSLGMKQRLGIAIALLNHPKLLILDE 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 772671321 161 PFGALDPVTRGALQaEMTRIHRILGRTIVLVTHDIDEALRLADHLVLMDHGEVVQQGS 218
Cdd:TIGR03740 151 PTNGLDPIGIQELR-ELIRSFPEQGITVILSSHILSEVQQLADHIGIISEGVLGYQGK 207
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
17-266 |
1.05e-27 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 108.54 E-value: 1.05e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 17 ASHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEIRSLPVLELRRRMGYAIQSI------------ 84
Cdd:PRK10253 23 AENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNAttpgditvqelv 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 85 --GLFPHwtvaQNIATvlqleKWsRANIADRVDELMALLGLEpALRDRYPHQLSGGQQQRVGVARALAANPQVLLMDEPF 162
Cdd:PRK10253 103 arGRYPH----QPLFT-----RW-RKEDEEAVTKAMQATGIT-HLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPT 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 163 GALDPVTRGALQAEMTRIHRILGRTIVLVTHDIDEALRLADHLVLMDHGEVVQQGSPLELLTwpkndfvreffgrSELGV 242
Cdd:PRK10253 172 TWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVT-------------AELIE 238
|
250 260
....*....|....*....|....*.
gi 772671321 243 RLLSLR--TVSDymrreemPVSGEPL 266
Cdd:PRK10253 239 RIYGLRcmIIDD-------PVAGTPL 257
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
20-214 |
2.80e-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: 105.80 E-value: 2.80e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 20 LNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGeeiRSLPVLELRRRMGYAIQSIG--LFPHwTVAQNIA 97
Cdd:cd03226 19 LSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNG---KPIKAKERRKSIGYVMQDVDyqLFTD-SVREELL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 98 tvLQLEKWSRANiaDRVDELMALLGLEpALRDRYPHQLSGGQQQRVGVARALAANPQVLLMDEPFGALDPvtrgalqAEM 177
Cdd:cd03226 95 --LGLKELDAGN--EQAETVLKDLDLY-ALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDY-------KNM 162
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 772671321 178 TRIHRIL------GRTIVLVTHDIDEALRLADHLVLMDHGEVV 214
Cdd:cd03226 163 ERVGELIrelaaqGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
32-261 |
2.97e-27 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 111.87 E-value: 2.97e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 32 LIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEIRSLP---VLELRRRMGYAIQS--IGLFPHWTVAQNIATVLQLEKWS 106
Cdd:PRK10261 355 LVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSpgkLQALRRDIQFIFQDpyASLDPRQTVGDSIMEPLRVHGLL 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 107 RANIA-DRVDELMALLGLEPALRDRYPHQLSGGQQQRVGVARALAANPQVLLMDEPFGALDPVTRGALQAEMTRIHRILG 185
Cdd:PRK10261 435 PGKAAaARVAWLLERVGLLPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFG 514
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 772671321 186 RTIVLVTHDIDEALRLADHLVLMDHGEVVQQGSPLELLTWPKNDFVReffgrselgvRLLSLRTVSDYMRREEMPV 261
Cdd:PRK10261 515 IAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENPQHPYTR----------KLMAAVPVADPSRQRPQRV 580
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
32-233 |
4.07e-27 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 110.95 E-value: 4.07e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 32 LIGTSGSGKSTTLKMINRLVEhDSGMIRFAGEEIRSL---PVLELRRRMGYAIQ--SIGLFPHWTVAQNIATVLQLEK-- 104
Cdd:PRK15134 317 LVGESGSGKSTTGLALLRLIN-SQGEIWFDGQPLHNLnrrQLLPVRHRIQVVFQdpNSSLNPRLNVLQIIEEGLRVHQpt 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 105 WSRANIADRVDELMALLGLEPALRDRYPHQLSGGQQQRVGVARALAANPQVLLMDEPFGALDPVTRG---ALQAEMTRIH 181
Cdd:PRK15134 396 LSAAQREQQVIAVMEEVGLDPETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAqilALLKSLQQKH 475
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 772671321 182 RIlgrTIVLVTHDIDEALRLADHLVLMDHGEVVQQGSPLELLTWPKNDFVRE 233
Cdd:PRK15134 476 QL---AYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERVFAAPQQEYTRQ 524
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
20-234 |
5.75e-27 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 106.27 E-value: 5.75e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 20 LNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDS-----GMIRFAGEEI--RSLPVLELRRRMGYAIQSIGLFPhWTV 92
Cdd:PRK14258 26 VSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNIyeRRVNLNRLRRQVSMVHPKPNLFP-MSV 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 93 AQNIATVLQLEKW-SRANIADRVDELMALLGLEPALRDRYPH---QLSGGQQQRVGVARALAANPQVLLMDEPFGALDPV 168
Cdd:PRK14258 105 YDNVAYGVKIVGWrPKLEIDDIVESALKDADLWDEIKHKIHKsalDLSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPI 184
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 772671321 169 trGALQAEmTRIHRILGR---TIVLVTHDIDEALRLADHLVLMDH-----GEVVQQGSPLELLTWPKNDFVREF 234
Cdd:PRK14258 185 --ASMKVE-SLIQSLRLRselTMVIVSHNLHQVSRLSDFTAFFKGnenriGQLVEFGLTKKIFNSPHDSRTREY 255
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
21-209 |
7.21e-27 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 105.28 E-value: 7.21e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 21 NLNFA--EGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEIRSLPV---LELR-RRMGYAIQSIGLFPHWTVAQ 94
Cdd:PRK11629 27 NVSFSigEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSaakAELRnQKLGFIYQFHHLLPDFTALE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 95 NIATVLQLEKWSRANIADRVDELMALLGLEPALRDRyPHQLSGGQQQRVGVARALAANPQVLLMDEPFGALDPVTRGALQ 174
Cdd:PRK11629 107 NVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHR-PSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADSIF 185
|
170 180 190
....*....|....*....|....*....|....*
gi 772671321 175 AEMTRIHRILGRTIVLVTHDIDEALRLADHLVLMD 209
Cdd:PRK11629 186 QLLGELNRLQGTAFLVVTHDLQLAKRMSRQLEMRD 220
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-214 |
8.29e-27 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 105.94 E-value: 8.29e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 1 MIEFLDVSKTF-AG----RPAASHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEIRSLPVLELRR 75
Cdd:COG1101 1 MLELKNLSKTFnPGtvneKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 76 RMGYAIQ--SIGLFPHWTVAQNIATVL---QLEKWSRANIADRVDELMALL-----GLEPALRDRYPHqLSGGQQQRVGV 145
Cdd:COG1101 81 YIGRVFQdpMMGTAPSMTIEENLALAYrrgKRRGLRRGLTKKRRELFRELLatlglGLENRLDTKVGL-LSGGQRQALSL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 146 ARALAANPQVLLMDEPFGALDPVTrGALQAEMT-RIHRILGRTIVLVTHDIDEALRLADHLVLMDHGEVV 214
Cdd:COG1101 160 LMATLTKPKLLLLDEHTAALDPKT-AALVLELTeKIVEENNLTTLMVTHNMEQALDYGNRLIMMHEGRII 228
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-214 |
1.11e-26 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 109.35 E-value: 1.11e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 1 MIEFLDVSKTFAGRPAASHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEE--IRSlPVLELRRRMG 78
Cdd:COG3845 5 ALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPvrIRS-PRDAIALGIG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 79 YAIQSIGLFPHWTVAQNIatVLQLEKW-----SRANIADRVDELMALLGLE--PalrDRYPHQLSGGQQQRVGVARALAA 151
Cdd:COG3845 84 MVHQHFMLVPNLTVAENI--VLGLEPTkggrlDRKAARARIRELSERYGLDvdP---DAKVEDLSVGEQQRVEILKALYR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 772671321 152 NPQVLLMDEPFGALDPVTRGALQAEMTRIhRILGRTIVLVTHDIDEALRLADHLVLMDHGEVV 214
Cdd:COG3845 159 GARILILDEPTAVLTPQEADELFEILRRL-AAEGKSIIFITHKLREVMAIADRVTVLRRGKVV 220
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
24-224 |
1.49e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 106.47 E-value: 1.49e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 24 FAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIR----FAGEEIRSLPVL------------ELRRRMGYAIQsiglF 87
Cdd:PRK13631 49 FEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQvgdiYIGDKKNNHELItnpyskkiknfkELRRRVSMVFQ----F 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 88 PHW-----TVAQNIA---TVLQLEKWSRANIADRVDELMallGLEPALRDRYPHQLSGGQQQRVGVARALAANPQVLLMD 159
Cdd:PRK13631 125 PEYqlfkdTIEKDIMfgpVALGVKKSEAKKLAKFYLNKM---GLDDSYLERSPFGLSGGQKRRVAIAGILAIQPEILIFD 201
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 160 EPFGALDPvtrgALQAEMTRIhrIL-----GRTIVLVTHDIDEALRLADHLVLMDHGEVVQQGSPLELLT 224
Cdd:PRK13631 202 EPTAGLDP----KGEHEMMQL--ILdakanNKTVFVITHTMEHVLEVADEVIVMDKGKILKTGTPYEIFT 265
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
12-213 |
2.43e-26 |
|
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: 102.29 E-value: 2.43e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 12 AGRPAASHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEIRSLPVLELRRRMGYAIQSIGLFPHwT 91
Cdd:cd03246 13 AEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGYLPQDDELFSG-S 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 92 VAQNIatvlqlekwsraniadrvdelmallglepalrdryphqLSGGQQQRVGVARALAANPQVLLMDEPFGALDPVTRG 171
Cdd:cd03246 92 IAENI--------------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGER 133
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 772671321 172 ALQAEMTRIhRILGRTIVLVTHDIdEALRLADHLVLMDHGEV 213
Cdd:cd03246 134 ALNQAIAAL-KAAGATRIVIAHRP-ETLASADRILVLEDGRV 173
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
20-237 |
4.97e-26 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 108.27 E-value: 4.97e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 20 LNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEIRSL---PVLELRRR-MGYAIQSIGLFPHWTVAQN 95
Cdd:PRK10535 27 ISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLdadALAQLRREhFGFIFQRYHLLSHLTAAQN 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 96 I---ATVLQLEKWSRAniaDRVDELMALLGLEPALrDRYPHQLSGGQQQRVGVARALAANPQVLLMDEPFGALDPVTRGA 172
Cdd:PRK10535 107 VevpAVYAGLERKQRL---LRAQELLQRLGLEDRV-EYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDSHSGEE 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 772671321 173 LQAEMTRIhRILGRTIVLVTHDIDEALRlADHLVLMDHGEVV--------QQGSPLELLTWPKNDFVREFFGR 237
Cdd:PRK10535 183 VMAILHQL-RDRGHTVIIVTHDPQVAAQ-AERVIEIRDGEIVrnppaqekVNVAGGTEPVVNTASGWRQFVSG 253
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
32-224 |
1.66e-25 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 102.23 E-value: 1.66e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 32 LIGTSGSGKSTTLKMINRLVEHdSGMIRFAGEEIRSLPVLELRRRMGYAIQSIGLFPHWTVAQNIATVLQlEKWSRANIA 111
Cdd:COG4138 27 LIGPNGAGKSTLLARMAGLLPG-QGEILLNGRPLSDWSAAELARHRAYLSQQQSPPFAMPVFQYLALHQP-AGASSEAVE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 112 DRVDELMALLGLEPALrDRYPHQLSGGQQQRVGVARAL-----AANP--QVLLMDEPFGALDPVTRGALQ---AEMTRih 181
Cdd:COG4138 105 QLLAQLAEALGLEDKL-SRPLTQLSGGEWQRVRLAAVLlqvwpTINPegQLLLLDEPMNSLDVAQQAALDrllRELCQ-- 181
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 772671321 182 riLGRTIVLVTHDIDEALRLADHLVLMDHGEVVQQGSPLELLT 224
Cdd:COG4138 182 --QGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEVMT 222
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
2-223 |
1.76e-25 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 106.20 E-value: 1.76e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 2 IEFLDVSKTFAG-RPAASHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEIRSLPVLELRRRMGYA 80
Cdd:PRK13657 335 VEFDDVSFSYDNsRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAVV 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 81 IQSIGLFPHwTVAQNI------ATVLQL-EKWSRANIADRVDElmALLGLEPALRDRyPHQLSGGQQQRVGVARALAANP 153
Cdd:PRK13657 415 FQDAGLFNR-SIEDNIrvgrpdATDEEMrAAAERAQAHDFIER--KPDGYDTVVGER-GRQLSGGERQRLAIARALLKDP 490
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 154 QVLLMDEPFGALDPVTRGALQAEMTRIHRilGRTIVLVTHDIdEALRLADHLVLMDHGEVVQQGSPLELL 223
Cdd:PRK13657 491 PILILDEATSALDVETEAKVKAALDELMK--GRTTFIIAHRL-STVRNADRILVFDNGRVVESGSFDELV 557
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
2-233 |
1.95e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 103.24 E-value: 1.95e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 2 IEFLDVSKTF-AGRP----AASHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRF---------AGEEIRS 67
Cdd:PRK13651 3 IKVKNIVKIFnKKLPtelkALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWifkdeknkkKTKEKEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 68 LP---------------VLELRRRMGYAIQ--SIGLFPHwTVAQNIATVLQLEKWSRANIADRVDELMALLGLEPALRDR 130
Cdd:PRK13651 83 VLeklviqktrfkkikkIKEIRRRVGVVFQfaEYQLFEQ-TIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLDESYLQR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 131 YPHQLSGGQQQRVGVARALAANPQVLLMDEPFGALDPVtrGALqaEMTRIHRIL---GRTIVLVTHDIDEALRLADHLVL 207
Cdd:PRK13651 162 SPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQ--GVK--EILEIFDNLnkqGKTIILVTHDLDNVLEWTKRTIF 237
|
250 260
....*....|....*....|....*.
gi 772671321 208 MDHGEVVQQGSPLELLTwpKNDFVRE 233
Cdd:PRK13651 238 FKDGKIIKDGDTYDILS--DNKFLIE 261
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
5-224 |
3.33e-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: 3.33e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 5 LDVSKTFAGRPAASHL---NLNFA--EGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEIRSLPVLELRRRMGY 79
Cdd:TIGR01842 317 LSVENVTIVPPGGKKPtlrGISFSlqAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGKHIGY 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 80 AIQSIGLFPHwTVAQNIA---TVLQLEKWSRANIADRVDELMALL--GLEPALRDRyPHQLSGGQQQRVGVARALAANPQ 154
Cdd:TIGR01842 397 LPQDVELFPG-TVAENIArfgENADPEKIIEAAKLAGVHELILRLpdGYDTVIGPG-GATLSGGQRQRIALARALYGDPK 474
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 155 VLLMDEPFGALDPVTRGALQAEMTRIhRILGRTIVLVTHDIdEALRLADHLVLMDHGEVVQQGSPLELLT 224
Cdd:TIGR01842 475 LVVLDEPNSNLDEEGEQALANAIKAL-KARGITVVVITHRP-SLLGCVDKILVLQDGRIARFGERDEVLA 542
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
33-264 |
6.06e-25 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 102.35 E-value: 6.06e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 33 IGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEIRSLP--VLELRRRmgyAIQSI------GLFPHWTVAQNIATVLQLE- 103
Cdd:PRK11308 47 VGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADpeAQKLLRQ---KIQIVfqnpygSLNPRKKVGQILEEPLLINt 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 104 KWSRANIADRVDELMALLGLEPALRDRYPHQLSGGQQQRVGVARALAANPQVLLMDEPFGALDPVTRGALQAEMTRIHRI 183
Cdd:PRK11308 124 SLSAAERREKALAMMAKVGLRPEHYDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQE 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 184 LGRTIVLVTHDIDEALRLADHLVLMDHGEVVQQGSPLELLTWPKNDFVREffgrselgvrLLSLR-TVSDYMRREEMPVS 262
Cdd:PRK11308 204 LGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFNNPRHPYTQA----------LLSATpRLNPDDRRERIKLT 273
|
..
gi 772671321 263 GE 264
Cdd:PRK11308 274 GE 275
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
14-233 |
6.65e-25 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 104.40 E-value: 6.65e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 14 RPAASHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRL-----VEHDSGMIRFAGEEIRSLPVLELRRRMGYAIQSI---- 84
Cdd:PRK15134 22 RTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLlpsppVVYPSGDIRFHGESLLHASEQTLRGVRGNKIAMIfqep 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 85 --GLFPHWTVAQNIATVLQLEKWSRANIAdRVDELMAL--LGLEPA---LRDrYPHQLSGGQQQRVGVARALAANPQVLL 157
Cdd:PRK15134 102 mvSLNPLHTLEKQLYEVLSLHRGMRREAA-RGEILNCLdrVGIRQAakrLTD-YPHQLSGGERQRVMIAMALLTRPELLI 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 772671321 158 MDEPFGALDPVTRGALQAEMTRIHRILGRTIVLVTHDIDEALRLADHLVLMDHGEVVQQGSPLELLTWPKNDFVRE 233
Cdd:PRK15134 180 ADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAATLFSAPTHPYTQK 255
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
13-224 |
1.70e-24 |
|
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: 103.87 E-value: 1.70e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 13 GRPAASHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEIRSLPVLELRRRMGYAIQSIGLFpHWTV 92
Cdd:TIGR03796 491 EPPLIENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIPREEIPREVLANSVAMVDQDIFLF-EGTV 569
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 93 AQNIATvlqlekWSRA-NIADRVDEL--MALLGLEPALRDRYPHQL-------SGGQQQRVGVARALAANPQVLLMDEPF 162
Cdd:TIGR03796 570 RDNLTL------WDPTiPDADLVRACkdAAIHDVITSRPGGYDAELaegganlSGGQRQRLEIARALVRNPSILILDEAT 643
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 772671321 163 GALDPVTRGALQAEMTRihRilGRTIVLVTHDIdEALRLADHLVLMDHGEVVQQGSPLELLT 224
Cdd:TIGR03796 644 SALDPETEKIIDDNLRR--R--GCTCIIVAHRL-STIRDCDEIIVLERGKVVQRGTHEELWA 700
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
16-203 |
1.96e-24 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 99.47 E-value: 1.96e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 16 AASHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRL--------VEhdsGMIRFAGEEIRSLPV--LELRRRMGYAIQSIG 85
Cdd:PRK14243 25 AVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLndlipgfrVE---GKVTFHGKNLYAPDVdpVEVRRRIGMVFQKPN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 86 LFPHwTVAQNIATVLQLEKWsRANIADRVDELMALLGLEPALRDRYPHQ---LSGGQQQRVGVARALAANPQVLLMDEPF 162
Cdd:PRK14243 102 PFPK-SIYDNIAYGARINGY-KGDMDELVERSLRQAALWDEVKDKLKQSglsLSGGQQQRLCIARAIAVQPEVILMDEPC 179
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 772671321 163 GALDPVTRGALQaEMtrIHRILGR-TIVLVTHDIDEALRLAD 203
Cdd:PRK14243 180 SALDPISTLRIE-EL--MHELKEQyTIIIVTHNMQQAARVSD 218
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
2-212 |
2.34e-24 |
|
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: 97.93 E-value: 2.34e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 2 IEFLDVSKTFAGRPAASH-----LNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGeeirslpvlelrrR 76
Cdd:cd03250 1 ISVEDASFTWDSGEQETSftlkdINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG-------------S 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 77 MGYAIQSiglfPhWtvAQNiATVlqlekwsRANI-------ADRVDELMALLGLEPALrDRYPHQ-----------LSGG 138
Cdd:cd03250 68 IAYVSQE----P-W--IQN-GTI-------RENIlfgkpfdEERYEKVIKACALEPDL-EILPDGdlteigekginLSGG 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 139 QQQRVGVARALAANPQVLLMDEPFGALDPVT---------RGALQaemtrihriLGRTIVLVTHDIdEALRLADHLVLMD 209
Cdd:cd03250 132 QKQRISLARAVYSDADIYLLDDPLSAVDAHVgrhifenciLGLLL---------NNKTRILVTHQL-QLLPHADQIVVLD 201
|
...
gi 772671321 210 HGE 212
Cdd:cd03250 202 NGR 204
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
12-216 |
2.69e-24 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 98.25 E-value: 2.69e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 12 AGRPAASHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEIRSLPVLELRRRMGYAIQSIGLFPHwT 91
Cdd:PRK10247 18 GDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQTPTLFGD-T 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 92 VAQNIATVLQLEKwsRANIADRVDELMALLGLEPALRDRYPHQLSGGQQQRVGVARALAANPQVLLMDEPFGALDPVTRG 171
Cdd:PRK10247 97 VYDNLIFPWQIRN--QQPDPAIFLDDLERFALPDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDESNKH 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 772671321 172 ALQAEMTRIHRILGRTIVLVTHDIDEALRLADHLVLMDHGEVVQQ 216
Cdd:PRK10247 175 NVNEIIHRYVREQNIAVLWVTHDKDEINHADKVITLQPHAGEMQE 219
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-223 |
4.57e-24 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 98.93 E-value: 4.57e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 1 MIEFLDVSKTFAGRPAASHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEI----RSLpvLELRRR 76
Cdd:PRK13638 1 MLATSDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLdyskRGL--LALRQQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 77 MGYAIQSIGLFPHWT-VAQNIATVLQLEKWSRANIADRVDELMALLGLEpalrdRYPHQ----LSGGQQQRVGVARALAA 151
Cdd:PRK13638 79 VATVFQDPEQQIFYTdIDSDIAFSLRNLGVPEAEITRRVDEALTLVDAQ-----HFRHQpiqcLSHGQKKRVAIAGALVL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 772671321 152 NPQVLLMDEPFGALDPVTRGALQAEMTRIHRiLGRTIVLVTHDIDEALRLADHLVLMDHGEVVQQGSPLELL 223
Cdd:PRK13638 154 QARYLLLDEPTAGLDPAGRTQMIAIIRRIVA-QGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVF 224
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
32-209 |
5.10e-24 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 97.54 E-value: 5.10e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 32 LIGTSGSGKSTTLKMINRLVEHDSGMIRFAG-------EEIRSlpvlELR-RRMGYAIQSIGLFPHWTVAQNIATVLQLE 103
Cdd:PRK10584 41 LIGESGSGKSTLLAILAGLDDGSSGEVSLVGqplhqmdEEARA----KLRaKHVGFVFQSFMLIPTLNALENVELPALLR 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 104 KWSRANIADRVDELMALLGLEPALrDRYPHQLSGGQQQRVGVARALAANPQVLLMDEPFGALDPVTRGALQAEMTRIHRI 183
Cdd:PRK10584 117 GESSRQSRNGAKALLEQLGLGKRL-DHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNRE 195
|
170 180
....*....|....*....|....*.
gi 772671321 184 LGRTIVLVTHDIDEALRLADHLVLMD 209
Cdd:PRK10584 196 HGTTLILVTHDLQLAARCDRRLRLVN 221
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
12-217 |
7.31e-24 |
|
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: 101.75 E-value: 7.31e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 12 AGRPAASHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEIRSLPVLELRRRMGYAIQSIGLFPHwT 91
Cdd:COG4618 343 SKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRHIGYLPQDVELFDG-T 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 92 VAQNIATVLQL--EKWSRANIADRVDELMALL--GLEPALRDRyPHQLSGGQQQRVGVARALAANPQVLLMDEPFGALDP 167
Cdd:COG4618 422 IAENIARFGDAdpEKVVAAAKLAGVHEMILRLpdGYDTRIGEG-GARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDD 500
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 772671321 168 VTRGALQAEMTRIhRILGRTIVLVTHDIdEALRLADHLVLMDHGEVVQQG 217
Cdd:COG4618 501 EGEAALAAAIRAL-KARGATVVVITHRP-SLLAAVDKLLVLRDGRVQAFG 548
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1-218 |
8.09e-24 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 97.78 E-value: 8.09e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 1 MIEFLDVSKTFAGRPAASHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDS---GMIRFAGEEIR-----SLPVLE 72
Cdd:PRK09984 4 IIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKsagSHIELLGRTVQregrlARDIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 73 LRRRMGYAIQSIGLFPHWTVAQNIAT-VLQLEKWSRANIA--DRVDELMALLGLEPALRDRYPHQ----LSGGQQQRVGV 145
Cdd:PRK09984 84 SRANTGYIFQQFNLVNRLSVLENVLIgALGSTPFWRTCFSwfTREQKQRALQALTRVGMVHFAHQrvstLSGGQQQRVAI 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 772671321 146 ARALAANPQVLLMDEPFGALDPVTRGALQAEMTRIHRILGRTIVLVTHDIDEALRLADHLVLMDHGEVVQQGS 218
Cdd:PRK09984 164 ARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGS 236
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-221 |
8.65e-24 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 97.46 E-value: 8.65e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 1 MIEFLDVSKTF----------------AGRP------AASHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMI 58
Cdd:COG1134 4 MIEVENVSKSYrlyhepsrslkelllrRRRTrreefwALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 59 RFAGEeIRSLpvLELrrrmgyaiqSIGLFPHWTVAQNI---ATVLQLekwSRANIADRVDELMALLGLEPALrDRYPHQL 135
Cdd:COG1134 84 EVNGR-VSAL--LEL---------GAGFHPELTGRENIylnGRLLGL---SRKEIDEKFDEIVEFAELGDFI-DQPVKTY 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 136 SGGQQQRVGVARALAANPQVLLMDEPFGALDPvtrgALQAE-MTRIHRIL--GRTIVLVTHDIDEALRLADHLVLMDHGE 212
Cdd:COG1134 148 SSGMRARLAFAVATAVDPDILLVDEVLAVGDA----AFQKKcLARIRELResGRTVIFVSHSMGAVRRLCDRAIWLEKGR 223
|
....*....
gi 772671321 213 VVQQGSPLE 221
Cdd:COG1134 224 LVMDGDPEE 232
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1-232 |
1.63e-23 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 97.17 E-value: 1.63e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 1 MIEFLDVSKTFAGRP---------AASHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEI------ 65
Cdd:PRK15112 4 LLEVRNLSKTFRYRTgwfrrqtveAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLhfgdys 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 66 -RSLpvlelRRRMGYAIQSIGLFPHWTVAQNIATVLQLE-KWSRANIADRVDELMALLGLEPALRDRYPHQLSGGQQQRV 143
Cdd:PRK15112 84 yRSQ-----RIRMIFQDPSTSLNPRQRISQILDFPLRLNtDLEPEQREKQIIETLRQVGLLPDHASYYPHMLAPGQKQRL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 144 GVARALAANPQVLLMDEPFGALDPVTRGALQAEMTRIHRILGRTIVLVTHDIDEALRLADHLVLMDHGEVVQQGSPLELL 223
Cdd:PRK15112 159 GLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVL 238
|
....*....
gi 772671321 224 TWPKNDFVR 232
Cdd:PRK15112 239 ASPLHELTK 247
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
7-217 |
2.55e-23 |
|
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: 96.44 E-value: 2.55e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 7 VSKTFAGRPAASHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEIRSLPVLEL----RRRMgyaiq 82
Cdd:TIGR02323 9 LSKSYGGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMRSGAELELYQLseaeRRRL----- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 83 sigLFPHW-TVAQNIATVLQLEKWSRANIADRvdeLMAL------------------LGLEPALRDRYPHQLSGGQQQRV 143
Cdd:TIGR02323 84 ---MRTEWgFVHQNPRDGLRMRVSAGANIGER---LMAIgarhygnirataqdwleeVEIDPTRIDDLPRAFSGGMQQRL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 772671321 144 GVARALAANPQVLLMDEPFGALDPVTRGALQAEMTRIHRILGRTIVLVTHDIDEALRLADHLVLMDHGEVVQQG 217
Cdd:TIGR02323 158 QIARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRVVESG 231
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
2-223 |
3.69e-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: 99.51 E-value: 3.69e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 2 IEFLDVSktFA---GRPAASHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEIRSLPVLELRRRMG 78
Cdd:COG5265 358 VRFENVS--FGydpERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIG 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 79 YAIQSIGLFPHwTVAQNI------ATVLQLEKWSR-ANIADRVDEL----MALLGlEPALRdryphqLSGGQQQRVGVAR 147
Cdd:COG5265 436 IVPQDTVLFND-TIAYNIaygrpdASEEEVEAAARaAQIHDFIESLpdgyDTRVG-ERGLK------LSGGEKQRVAIAR 507
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 148 ALAANPQVLLMDEPFGALDPVTRGALQAEMTRIHRilGRTIVLVTHdidealRL-----ADHLVLMDHGEVVQQGSPLEL 222
Cdd:COG5265 508 TLLKNPPILIFDEATSALDSRTERAIQAALREVAR--GRTTLVIAH------RLstivdADEILVLEAGRIVERGTHAEL 579
|
.
gi 772671321 223 L 223
Cdd:COG5265 580 L 580
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
2-224 |
4.12e-23 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 99.80 E-value: 4.12e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 2 IEFLDVSKTFAGRPAASHL-NLNF--AEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEIRSLPVLELRRRMG 78
Cdd:TIGR00958 479 IEFQDVSFSYPNRPDVPVLkGLTFtlHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVA 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 79 YAIQSIGLFPHwTVAQNIATVLQL----EKWSRANIADRVDELMALLGLEPALRDRYPHQLSGGQQQRVGVARALAANPQ 154
Cdd:TIGR00958 559 LVGQEPVLFSG-SVRENIAYGLTDtpdeEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPR 637
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 155 VLLMDEPFGALDPVTRGALQAEMTRihriLGRTIVLVTHDIDEALRlADHLVLMDHGEVVQQGSPLELLT 224
Cdd:TIGR00958 638 VLILDEATSALDAECEQLLQESRSR----ASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQLME 702
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-224 |
4.44e-23 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 99.13 E-value: 4.44e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 2 IEFLDVSKTFAGR--PAASHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEIRSLPVLELRRRMGY 79
Cdd:PRK11160 339 LTLNNVSFTYPDQpqPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQAISV 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 80 AIQSIGLFPHwTVAQNiatvLQLEKwsrANIADrvDELMALL---GLEPALRDRYP---------HQLSGGQQQRVGVAR 147
Cdd:PRK11160 419 VSQRVHLFSA-TLRDN----LLLAA---PNASD--EALIEVLqqvGLEKLLEDDKGlnawlgeggRQLSGGEQRRLGIAR 488
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 148 ALAANPQVLLMDEPFGALDPVTRG---ALQAEMTRihrilGRTIVLVTHDIdEALRLADHLVLMDHGEVVQQGSPLELLT 224
Cdd:PRK11160 489 ALLHDAPLLLLDEPTEGLDAETERqilELLAEHAQ-----NKTVLMITHRL-TGLEQFDRICVMDNGQIIEQGTHQELLA 562
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
20-217 |
8.20e-23 |
|
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: 94.26 E-value: 8.20e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 20 LNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHD---SGMIRFAGEEIRSLpvlELRRRMGYAIQSIGLFPHWTVAQNI 96
Cdd:cd03234 26 VSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGgttSGQILFNGQPRKPD---QFQKCVAYVRQDDILLPGLTVRETL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 97 ATVLQL---EKWSRANIADRV-DELMALLGLEPaLRDRYPHQLSGGQQQRVGVARALAANPQVLLMDEPFGALDPVTrgA 172
Cdd:cd03234 103 TYTAILrlpRKSSDAIRKKRVeDVLLRDLALTR-IGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFT--A 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 772671321 173 LQaeMTRIHRILGRT--IVLVT-HDI-DEALRLADHLVLMDHGEVVQQG 217
Cdd:cd03234 180 LN--LVSTLSQLARRnrIVILTiHQPrSDLFRLFDRILLLSSGEIVYSG 226
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
14-226 |
9.63e-23 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 98.25 E-value: 9.63e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 14 RPAASHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEIRSLPVLELRRRMGYAIQSIGLFPHwTVA 93
Cdd:PRK10789 328 HPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFLFSD-TVA 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 94 QNI------ATVLQLEKWSR-ANIADrvDELMALLGLEPALRDRyPHQLSGGQQQRVGVARALAANPQVLLMDEPFGALD 166
Cdd:PRK10789 407 NNIalgrpdATQQEIEHVARlASVHD--DILRLPQGYDTEVGER-GVMLSGGQKQRISIARALLLNAEILILDDALSAVD 483
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 772671321 167 PVTRgalqaemtriHRIL--------GRTIVLVTHDIdEALRLADHLVLMDHGEVVQQGSPLELLTWP 226
Cdd:PRK10789 484 GRTE----------HQILhnlrqwgeGRTVIISAHRL-SALTEASEILVMQHGHIAQRGNHDQLAQQS 540
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
34-213 |
1.29e-22 |
|
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: 92.50 E-value: 1.29e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 34 GTSGSGKSTTLKMINRLVEHDSGMIRFAGEEIRSLPVLELRRR-MGYAI---QSIGLFPHWTVAQNIATvlqlekwsran 109
Cdd:cd03215 33 GLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAgIAYVPedrKREGLVLDLSVAENIAL----------- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 110 iadrvdelmallglepalrdryPHQLSGGQQQRVGVARALAANPQVLLMDEPfgaldpvTRG---ALQAEmtrIHRIL-- 184
Cdd:cd03215 102 ----------------------SSLLSGGNQQKVVLARWLARDPRVLILDEP-------TRGvdvGAKAE---IYRLIre 149
|
170 180 190
....*....|....*....|....*....|...
gi 772671321 185 ----GRTIVLVTHDIDEALRLADHLVLMDHGEV 213
Cdd:cd03215 150 ladaGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
26-227 |
1.31e-22 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 95.96 E-value: 1.31e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 26 EGAFSVLIGTSGSGKSTTLKMINRLVEHDSGM----IRFAGEEIRSLPVLELRRRMGYAIQSI------GLFPHWTVAQN 95
Cdd:PRK11022 32 QGEVVGIVGESGSGKSVSSLAIMGLIDYPGRVmaekLEFNGQDLQRISEKERRNLVGAEVAMIfqdpmtSLNPCYTVGFQ 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 96 IATVLQLEKW-SRANIADRVDELMALLGL-EPALR-DRYPHQLSGGQQQRVGVARALAANPQVLLMDEPFGALDpVTrga 172
Cdd:PRK11022 112 IMEAIKVHQGgNKKTRRQRAIDLLNQVGIpDPASRlDVYPHQLSGGMSQRVMIAMAIACRPKLLIADEPTTALD-VT--- 187
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 772671321 173 LQAEMTRIHRILGR----TIVLVTHDIDEALRLADHLVLMDHGEVVQQGSPLELLTWPK 227
Cdd:PRK11022 188 IQAQIIELLLELQQkenmALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDIFRAPR 246
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
15-217 |
2.48e-22 |
|
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: 93.17 E-value: 2.48e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 15 PAASHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGE---EIRSlpvlELRRRMGYAI-QSIGLFPHW 90
Cdd:cd03267 35 EALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLvpwKRRK----KFLRRIGVVFgQKTQLWWDL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 91 TVAQNIATVLQLEKWSRANIADRVDELMALLGLEPALrDRYPHQLSGGQQQRVGVARALAANPQVLLMDEPFGALDPVTR 170
Cdd:cd03267 111 PVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELL-DTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQ 189
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 772671321 171 GALQAEMTRIHRILGRTIVLVTHDIDEALRLADHLVLMDHGEVVQQG 217
Cdd:cd03267 190 ENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
4-217 |
4.42e-22 |
|
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: 91.46 E-value: 4.42e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 4 FLDVSKTFAGRPAASHLNLNFAEGAFSVLIGTSGSGKSTTLKMIN--RLVEHDSGMIRFAGeeiRSLPVLELRRRMGYAI 81
Cdd:cd03213 12 TVKSSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAgrRTGLGVSGEVLING---RPLDKRSFRKIIGYVP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 82 QSIGLFPHWTVAQNIATVLQLEkwsraniadrvdelmallglepalrdryphQLSGGQQQRVGVARALAANPQVLLMDEP 161
Cdd:cd03213 89 QDDILHPTLTVRETLMFAAKLR------------------------------GLSGGERKRVSIALELVSNPSLLFLDEP 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 772671321 162 FGALDPVTrgALQ-AEMTRIHRILGRTIVLVTHDI-DEALRLADHLVLMDHGEVVQQG 217
Cdd:cd03213 139 TSGLDSSS--ALQvMSLLRRLADTGRTIICSIHQPsSEIFELFDKLLLLSQGRVIYFG 194
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
13-222 |
6.80e-22 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 95.68 E-value: 6.80e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 13 GRPAASHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHdSGMIRFAGEEIRSLPVLELRRRMGYAIQSIGLFpHWTV 92
Cdd:PRK11174 362 GKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPY-QGSLKINGIELRELDPESWRKHLSWVGQNPQLP-HGTL 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 93 AQNIA------------TVLQlekwsRANIADRVDELMalLGLEPALRDRyPHQLSGGQQQRVGVARALAANPQVLLMDE 160
Cdd:PRK11174 440 RDNVLlgnpdasdeqlqQALE-----NAWVSEFLPLLP--QGLDTPIGDQ-AAGLSVGQAQRLALARALLQPCQLLLLDE 511
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 772671321 161 PFGALDPVTRGALQAEMTRIHRilGRTIVLVTHDIDEaLRLADHLVLMDHGEVVQQGSPLEL 222
Cdd:PRK11174 512 PTASLDAHSEQLVMQALNAASR--RQTTLMVTHQLED-LAQWDQIWVMQDGQIVQQGDYAEL 570
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
32-224 |
7.27e-22 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 92.30 E-value: 7.27e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 32 LIGTSGSGKSTTLKMINRLVEHdSGMIRFAGEEIRSLPVLELRRRMGYAIQSIGLFPHWTVAQniatVLQLEKWSRANIA 111
Cdd:PRK03695 27 LVGPNGAGKSTLLARMAGLLPG-SGSIQFAGQPLEAWSAAELARHRAYLSQQQTPPFAMPVFQ----YLTLHQPDKTRTE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 112 D---RVDELMALLGLEPALrDRYPHQLSGGQQQRVGVARAL-----AANP--QVLLMDEPFGALDPVTRGALQAEMTRIH 181
Cdd:PRK03695 102 AvasALNEVAEALGLDDKL-GRSVNQLSGGEWQRVRLAAVVlqvwpDINPagQLLLLDEPMNSLDVAQQAALDRLLSELC 180
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 772671321 182 RiLGRTIVLVTHDIDEALRLADHLVLMDHGEVVQQGSPLELLT 224
Cdd:PRK03695 181 Q-QGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVLT 222
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
37-214 |
9.90e-22 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 95.09 E-value: 9.90e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 37 GSGKSTTLKMINRLVEHDSGMIRFAGEE--IRSlPVLELRRRMGYAI---QSIGLFPHWTVAQNIaTVLQLEKWSRANIA 111
Cdd:COG1129 288 GAGRTELARALFGADPADSGEIRLDGKPvrIRS-PRDAIRAGIAYVPedrKGEGLVLDLSIRENI-TLASLDRLSRGGLL 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 112 DR------VDELMALLGLEPALRDRYPHQLSGGQQQRVGVARALAANPQVLLMDEPfgaldpvTRG----AlQAEmtrIH 181
Cdd:COG1129 366 DRrreralAEEYIKRLRIKTPSPEQPVGNLSGGNQQKVVLAKWLATDPKVLILDEP-------TRGidvgA-KAE---IY 434
|
170 180 190
....*....|....*....|....*....|....*....
gi 772671321 182 RIL------GRTIVLVTHDIDEALRLADHLVLMDHGEVV 214
Cdd:COG1129 435 RLIrelaaeGKAVIVISSELPELLGLSDRILVMREGRIV 473
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
6-217 |
2.63e-21 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 90.76 E-value: 2.63e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 6 DVSKTFAGRPAASHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEIRSLPVLEL---RRRM----- 77
Cdd:PRK11701 11 GLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYALseaERRRllrte 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 78 -GYaiqsiglfphwtVAQNIATVLQLEKWSRANIADRvdeLMAL------------------LGLEPALRDRYPHQLSGG 138
Cdd:PRK11701 91 wGF------------VHQHPRDGLRMQVSAGGNIGER---LMAVgarhygdiratagdwlerVEIDAARIDDLPTTFSGG 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 772671321 139 QQQRVGVARALAANPQVLLMDEPFGALDPVTRGALQAEMTRIHRILGRTIVLVTHDIDEALRLADHLVLMDHGEVVQQG 217
Cdd:PRK11701 156 MQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVVESG 234
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
16-218 |
3.36e-21 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 92.09 E-value: 3.36e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 16 AASHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHD---SGMIRFAGEEIRSLPVLELRRRMGYAIQSI------GL 86
Cdd:PRK09473 31 AVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANgriGGSATFNGREILNLPEKELNKLRAEQISMIfqdpmtSL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 87 FPHWTVAQNIATVLQLEKwsRANIADRVDELMALLGL--EPALRDR---YPHQLSGGQQQRVGVARALAANPQVLLMDEP 161
Cdd:PRK09473 111 NPYMRVGEQLMEVLMLHK--GMSKAEAFEESVRMLDAvkMPEARKRmkmYPHEFSGGMRQRVMIAMALLCRPKLLIADEP 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 772671321 162 FGALDpVTrgaLQAE-MT---RIHRILGRTIVLVTHDIDEALRLADHLVLMDHGEVVQQGS 218
Cdd:PRK09473 189 TTALD-VT---VQAQiMTllnELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGN 245
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
6-213 |
6.96e-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: 6.96e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 6 DVSKTFAGRPAASHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEirslpvlelrrRMGYAIQSIG 85
Cdd:COG0488 3 NLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGL-----------RIGYLPQEPP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 86 LFPHWTVAQNIATVLQ----------------------LEKWSRA----------NIADRVDELMALLGLEPALRDRYPH 133
Cdd:COG0488 72 LDDDLTVLDTVLDGDAelraleaeleeleaklaepdedLERLAELqeefealggwEAEARAEEILSGLGFPEEDLDRPVS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 134 QLSGGQQQRVGVARALAANPQVLLMDEPFGALDpvtrgalqAEMTR-IHRILGR---TIVLVTHD---IDealRLADHLV 206
Cdd:COG0488 152 ELSGGWRRRVALARALLSEPDLLLLDEPTNHLD--------LESIEwLEEFLKNypgTVLVVSHDryfLD---RVATRIL 220
|
....*..
gi 772671321 207 LMDHGEV 213
Cdd:COG0488 221 ELDRGKL 227
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
2-217 |
1.85e-20 |
|
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: 86.60 E-value: 1.85e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 2 IEFLDVSKTFAG--RPAASHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEIRSLPVlELRRRMGY 79
Cdd:cd03247 1 LSINNVSFSYPEqeQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEK-ALSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 80 AIQSIGLFPHwTVAQNIATvlqlekwsraniadrvdelmallglepalrdryphQLSGGQQQRVGVARALAANPQVLLMD 159
Cdd:cd03247 80 LNQRPYLFDT-TLRNNLGR-----------------------------------RFSGGERQRLALARILLQDAPIVLLD 123
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 772671321 160 EPFGALDPVTRGALQ---AEMTRihrilGRTIVLVTHDIdEALRLADHLVLMDHGEVVQQG 217
Cdd:cd03247 124 EPTVGLDPITERQLLsliFEVLK-----DKTLIWITHHL-TGIEHMDKILFLENGKIIMQG 178
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
15-265 |
1.89e-20 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 91.84 E-value: 1.89e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 15 PAASHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEI--RSLPVLELRRRMGYAIQSI-------- 84
Cdd:PRK10261 30 AAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLrrRSRQVIELSEQSAAQMRHVrgadmami 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 85 ------GLFPHWTVAQNIATVLQLEKWSRANIADRVDELMALLGLEP---ALRDRYPHQLSGGQQQRVGVARALAANPQV 155
Cdd:PRK10261 110 fqepmtSLNPVFTVGEQIAESIRLHQGASREEAMVEAKRMLDQVRIPeaqTILSRYPHQLSGGMRQRVMIAMALSCRPAV 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 156 LLMDEPFGALDpVTrgaLQAEMTRIHRILGRT----IVLVTHDIDEALRLADHLVLMDHGEVVQQGSPLELLTWPKNDFV 231
Cdd:PRK10261 190 LIADEPTTALD-VT---IQAQILQLIKVLQKEmsmgVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQIFHAPQHPYT 265
|
250 260 270
....*....|....*....|....*....|....
gi 772671321 232 REFFGrselGVRLLSLRTVSDYMRREEMPVSGEP 265
Cdd:PRK10261 266 RALLA----AVPQLGAMKGLDYPRRFPLISLEHP 295
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
20-217 |
3.03e-20 |
|
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: 87.20 E-value: 3.03e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 20 LNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGeeiRSLPVLELrrrmgyaiqSIGLFPHWTVAQNIATV 99
Cdd:cd03220 41 VSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG---RVSSLLGL---------GGGFNPELTGRENIYLN 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 100 LQLEKWSRANIADRVDELMALLGLEPALRDRYPHqLSGGQQQRVGVARALAANPQVLLMDEPFGALDPvtrgALQAEMT- 178
Cdd:cd03220 109 GRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKT-YSSGMKARLAFAIATALEPDILLIDEVLAVGDA----AFQEKCQr 183
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 772671321 179 RIHRIL--GRTIVLVTHDIDEALRLADHLVLMDHGEVVQQG 217
Cdd:cd03220 184 RLRELLkqGKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
2-219 |
3.15e-20 |
|
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: 87.16 E-value: 3.15e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 2 IEFLDVSKTFA--GRPAASHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEIRSLPVLELRRRMGY 79
Cdd:cd03244 3 IEFKNVSLRYRpnLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRISI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 80 AIQSIGLFPHwTVAQNIATVLQL---EKWS---RANIADRVDELMALLGLEPALRDRyphQLSGGQQQRVGVARALAANP 153
Cdd:cd03244 83 IPQDPVLFSG-TIRSNLDPFGEYsdeELWQaleRVGLKEFVESLPGGLDTVVEEGGE---NLSVGQRQLLCLARALLRKS 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 772671321 154 QVLLMDEPFGALDPVTRGALQaEMTRiHRILGRTIVLVTHDIDEALRlADHLVLMDHGEVVQQGSP 219
Cdd:cd03244 159 KILVLDEATASVDPETDALIQ-KTIR-EAFKDCTVLTIAHRLDTIID-SDRILVLDKGRVVEFDSP 221
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
21-226 |
3.67e-20 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 89.19 E-value: 3.67e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 21 NLNFAEGAFSVLIGTSGSGKSTTLKMI------NRLVEHDSgmIRFAGEEIRSLPVLELRRRMGYAIQSI------GLFP 88
Cdd:COG4170 27 SLTLNEGEIRGLVGESGSGKSLIAKAIcgitkdNWHVTADR--FRWNGIDLLKLSPRERRKIIGREIAMIfqepssCLDP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 89 HWTVAQNIATVL----------QLEKWSRAniadRVDELMALLGLE--PALRDRYPHQLSGGQQQRVGVARALAANPQVL 156
Cdd:COG4170 105 SAKIGDQLIEAIpswtfkgkwwQRFKWRKK----RAIELLHRVGIKdhKDIMNSYPHELTEGECQKVMIAMAIANQPRLL 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 772671321 157 LMDEPFGALDPVTRgalqaemTRIHRILGR-------TIVLVTHDIDEALRLADHLVLMDHGEVVQQGSPLELLTWP 226
Cdd:COG4170 181 IADEPTNAMESTTQ-------AQIFRLLARlnqlqgtSILLISHDLESISQWADTITVLYCGQTVESGPTEQILKSP 250
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
2-213 |
6.15e-20 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 86.37 E-value: 6.15e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 2 IEFLDVSKTFAGRPAASHL-NLNFA--EGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEIRSLPVLELRRRMG 78
Cdd:cd03248 12 VKFQNVTFAYPTRPDTLVLqDVSFTlhPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSKVS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 79 YAIQSIGLFPHwTVAQNIATVLQ---LEKWSRANIADRVDELMALLGLEPALR-DRYPHQLSGGQQQRVGVARALAANPQ 154
Cdd:cd03248 92 LVGQEPVLFAR-SLQDNIAYGLQscsFECVKEAAQKAHAHSFISELASGYDTEvGEKGSQLSGGQKQRVAIARALIRNPQ 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 772671321 155 VLLMDEPFGALDPVTRGALQAEMTRIHRilGRTIVLVTHDIDEALRlADHLVLMDHGEV 213
Cdd:cd03248 171 VLILDEATSALDAESEQQVQQALYDWPE--RRTVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
33-222 |
1.72e-19 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 89.03 E-value: 1.72e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 33 IGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEIRSLPvLELRRRMGYAIQSIGLFPHWTVAQNIATVLQLEKWSRANIAD 112
Cdd:NF033858 298 LGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDAGD-IATRRRVGYMSQAFSLYGELTVRQNLELHARLFHLPAAEIAA 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 113 RVDELMALLGLEPALrDRYPHQLSGGQQQRVGVARALAANPQVLLMDEPFGALDPVTRGALQAEMTRIHRILGRTIVLVT 192
Cdd:NF033858 377 RVAEMLERFDLADVA-DALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVARDMFWRLLIELSREDGVTIFIST 455
|
170 180 190
....*....|....*....|....*....|
gi 772671321 193 HDIDEALRlADHLVLMDHGEVVQQGSPLEL 222
Cdd:NF033858 456 HFMNEAER-CDRISLMHAGRVLASDTPAAL 484
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1-193 |
1.75e-19 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 84.93 E-value: 1.75e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 1 MIEFLDVSKTFAGRPAASHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEIRSLPVLElrrRMGYA 80
Cdd:PRK13539 2 MLEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAE---ACHYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 81 IQSIGLFPHWTVAQNiatvlqLEKWS--RANIADRVDELMALLGLEPALRDRYPHqLSGGQQQRVGVARALAANPQVLLM 158
Cdd:PRK13539 79 GHRNAMKPALTVAEN------LEFWAafLGGEELDIAAALEAVGLAPLAHLPFGY-LSAGQKRRVALARLLVSNRPIWIL 151
|
170 180 190
....*....|....*....|....*....|....*
gi 772671321 159 DEPFGALDPVTRgALQAEMTRIHRILGRTIVLVTH 193
Cdd:PRK13539 152 DEPTAALDAAAV-ALFAELIRAHLAQGGIVIAATH 185
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
2-194 |
1.82e-19 |
|
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: 88.57 E-value: 1.82e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 2 IEFLDVSKTFAGRPAA-SHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEIRSLPVLELRRRMGYA 80
Cdd:TIGR02868 335 LELRDLSAGYPGAPPVlDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVC 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 81 IQSIGLFpHWTVAQNIATvlqlekwSRANIADrvDELMALL---GLEPALRDRyPH-----------QLSGGQQQRVGVA 146
Cdd:TIGR02868 415 AQDAHLF-DTTVRENLRL-------ARPDATD--EELWAALervGLADWLRAL-PDgldtvlgeggaRLSGGERQRLALA 483
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 772671321 147 RALAANPQVLLMDEPFGALDPVTRGALQAEMTRIHRilGRTIVLVTHD 194
Cdd:TIGR02868 484 RALLADAPILLLDEPTEHLDAETADELLEDLLAALS--GRTVVLITHH 529
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
16-291 |
3.39e-19 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 86.29 E-value: 3.39e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 16 AASHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEirslPVlelRRRMGYAiqsiglfphwtvaQN 95
Cdd:COG4586 37 AVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYV----PF---KRRKEFA-------------RR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 96 IATVL----QLekW------------------SRANIADRVDELMALLGLEPALrDRYPHQLSGGQQQRVGVARALAANP 153
Cdd:COG4586 97 IGVVFgqrsQL--WwdlpaidsfrllkaiyriPDAEYKKRLDELVELLDLGELL-DTPVRQLSLGQRMRCELAAALLHRP 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 154 QVLLMDEPFGALDPVTRGALQAEMTRIHRILGRTIVLVTHDIDEALRLADHLVLMDHGEVVQQGSplelltwpKNDFVRE 233
Cdd:COG4586 174 KILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEALCDRVIVIDHGRIIYDGS--------LEELKER 245
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 772671321 234 FFGRSELGVRLlslrtvSDYMRREEMPVSGEPLQE-------QMSLRDALSAFVARQCEVLPVSD 291
Cdd:COG4586 246 FGPYKTIVLEL------AEPVPPLELPRGGEVIERegnrvrlEVDPRESLAEVLARLLARYPVRD 304
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
2-253 |
3.57e-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: 87.55 E-value: 3.57e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 2 IEFLDVSKTFAGRPAASHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRL--VEHDSGMIRF------------------- 60
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIYhvalcekcgyverpskvge 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 61 ----AGEEIRSLPV----------LELRRRMGYAIQ-SIGLFPHWTVAQNIATVLQLEKWSRANIADRVDELMALLGLEp 125
Cdd:TIGR03269 81 pcpvCGGTLEPEEVdfwnlsdklrRRIRKRIAIMLQrTFALYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEMVQLS- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 126 alrDRYPH---QLSGGQQQRVGVARALAANPQVLLMDEPFGALDPVTRGALQAEMTRIHRILGRTIVLVTHDIDEALRLA 202
Cdd:TIGR03269 160 ---HRITHiarDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDLS 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 772671321 203 DHLVLMDHGEVVQQGSPLELLtwpkNDFVREF-----FGRSELGVRLLSLRTVSDY 253
Cdd:TIGR03269 237 DKAIWLENGEIKEEGTPDEVV----AVFMEGVsevekECEVEVGEPIIKVRNVSKR 288
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
13-193 |
3.09e-18 |
|
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: 81.25 E-value: 3.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 13 GRPAASHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEIRSLPVlELRRRMGYAIQSIGLFPHWTV 92
Cdd:TIGR01189 12 ERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRD-EPHENILYLGHLPGLKPELSA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 93 AQNIATVLQLEKWSRANIADRVdELMALLGLEpalrDRYPHQLSGGQQQRVGVARALAANPQVLLMDEPFGALDPVTRgA 172
Cdd:TIGR01189 91 LENLHFWAAIHGGAQRTIEDAL-AAVGLTGFE----DLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGV-A 164
|
170 180
....*....|....*....|.
gi 772671321 173 LQAEMTRIHRILGRTIVLVTH 193
Cdd:TIGR01189 165 LLAGLLRAHLARGGIVLLTTH 185
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-232 |
3.17e-18 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 82.23 E-value: 3.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 1 MIEFLDVSKTFAGRPAASHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEIRSLPVLELRRRmGYA 80
Cdd:PRK11614 5 MLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMRE-AVA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 81 IQSIG--LFPHWTVAQNIATVLQLEkwSRANIADRVDELMALLglePALRDRYPHQ---LSGGQQQRVGVARALAANPQV 155
Cdd:PRK11614 84 IVPEGrrVFSRMTVEENLAMGGFFA--ERDQFQERIKWVYELF---PRLHERRIQRagtMSGGEQQMLAIGRALMSQPRL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 772671321 156 LLMDEPFGALDPVTRGALQAEMTRIhRILGRTIVLVTHDIDEALRLADHLVLMDHGEVVQQGSPLELLTwpkNDFVR 232
Cdd:PRK11614 159 LLLDEPSLGLAPIIIQQIFDTIEQL-REQGMTIFLVEQNANQALKLADRGYVLENGHVVLEDTGDALLA---NEAVR 231
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1-214 |
3.27e-18 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 84.73 E-value: 3.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 1 MIEFLDVSKTFAGRPAASHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFaGEEIRslpvlelrrrMGY- 79
Cdd:COG0488 315 VLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETVK----------IGYf 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 80 AIQSIGLFPHWTVAQNIatvlqlekwSRANIADRVDELMALLG---LEPALRDRYPHQLSGGQQQRVGVARALAANPQVL 156
Cdd:COG0488 384 DQHQEELDPDKTVLDEL---------RDGAPGGTEQEVRGYLGrflFSGDDAFKPVGVLSGGEKARLALAKLLLSPPNVL 454
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 772671321 157 LMDEPFGALDPVTRGAL-QAemtrihriLGR---TIVLVTHD---IDealRLADHLVLMDHGEVV 214
Cdd:COG0488 455 LLDEPTNHLDIETLEALeEA--------LDDfpgTVLLVSHDryfLD---RVATRILEFEDGGVR 508
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1-238 |
3.59e-18 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 82.35 E-value: 3.59e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 1 MIEFLDVSKTFAGRPAASHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEIRSLPVLELRRrMGY- 79
Cdd:PRK11300 5 LLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIAR-MGVv 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 80 -AIQSIGLFPHWTVAQN--IATVLQLE-------------KWSRANIADRVDELMALLGLEPaLRDRYPHQLSGGQQQRV 143
Cdd:PRK11300 84 rTFQHVRLFREMTVIENllVAQHQQLKtglfsgllktpafRRAESEALDRAATWLERVGLLE-HANRQAGNLAYGQQRRL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 144 GVARALAANPQVLLMDEPFGALDPVTRGALQAEMTRIHRILGRTIVLVTHDIDEALRLADHLVLMDHGEVVQQGSPLELL 223
Cdd:PRK11300 163 EIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEIR 242
|
250
....*....|....*
gi 772671321 224 TWPknDFVREFFGRS 238
Cdd:PRK11300 243 NNP--DVIKAYLGEA 255
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
12-232 |
4.55e-18 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 82.05 E-value: 4.55e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 12 AGRPAASHLNLNFAEGAFSVLIGTSGSGKSTT----LKMINRLVEHDSGMIRFAGEEIRSLpvlELRRRMgyaIQSIGLF 87
Cdd:PRK10418 14 AAQPLVHGVSLTLQRGRVLALVGGSGSGKSLTcaaaLGILPAGVRQTAGRVLLDGKPVAPC---ALRGRK---IATIMQN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 88 P-------HWTVAQNIATVLQLEKWSRAniaDRVDELMALLGLEPALR--DRYPHQLSGGQQQRVGVARALAANPQVLLM 158
Cdd:PRK10418 88 PrsafnplHTMHTHARETCLALGKPADD---ATLTAALEAVGLENAARvlKLYPFEMSGGMLQRMMIALALLCEAPFIIA 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 772671321 159 DEPFGALDPVTRGALQAEMTRIHRILGRTIVLVTHDIDEALRLADHLVLMDHGEVVQQGSPLELLTWPKNDFVR 232
Cdd:PRK10418 165 DEPTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPKHAVTR 238
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
13-193 |
1.65e-17 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 82.93 E-value: 1.65e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 13 GRPAASHLNLNFAEGAfSVLI-GTSGSGKSTTLKMINRLVEHDSGMIRF-AGEEI-----RS-LPVLELRRRMGYAiQSI 84
Cdd:COG4178 375 GRPLLEDLSLSLKPGE-RLLItGPSGSGKSTLLRAIAGLWPYGSGRIARpAGARVlflpqRPyLPLGTLREALLYP-ATA 452
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 85 GLFPHWTVAQniatVLQ---LEKWsraniADRVDElmallglepalRDRYPHQLSGGQQQRVGVARALAANPQVLLMDEP 161
Cdd:COG4178 453 EAFSDAELRE----ALEavgLGHL-----AERLDE-----------EADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEA 512
|
170 180 190
....*....|....*....|....*....|...
gi 772671321 162 FGALDPVTRGALqaeMTRIHRIL-GRTIVLVTH 193
Cdd:COG4178 513 TSALDEENEAAL---YQLLREELpGTTVISVGH 542
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
14-215 |
5.56e-17 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 78.08 E-value: 5.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 14 RPAASHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVE--HDSGMIRFAGEEI-RSLPVLElrrrmgyaiqsiglfphw 90
Cdd:COG2401 43 RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKgtPVAGCVDVPDNQFgREASLID------------------ 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 91 tvaqNIatvlqlekWSRANIADRVdELMALLGL-EPALRDRYPHQLSGGQQQRVGVARALAANPQVLLMDEPFGALDPVT 169
Cdd:COG2401 105 ----AI--------GRKGDFKDAV-ELLNAVGLsDAVLWLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQT 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 772671321 170 RGALQAEMTRIHRILGRTIVLVTH--DIDEALRlADHLVLMDHGEVVQ 215
Cdd:COG2401 172 AKRVARNLQKLARRAGITLVVATHhyDVIDDLQ-PDLLIFVGYGGVPE 218
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
16-238 |
8.68e-17 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 79.46 E-value: 8.68e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 16 AASHLNLNFAEGAFSVLIGTSGSGKSTTLKMI------------NRLVEHDSGMIRFAGEEIRSL-------------PV 70
Cdd:PRK15093 22 AVDRVSMTLTEGEIRGLVGESGSGKSLIAKAIcgvtkdnwrvtaDRMRFDDIDLLRLSPRERRKLvghnvsmifqepqSC 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 71 LELRRRMGYA-IQSIglfPHWTVAqniATVLQLEKWSRAniadRVDELMALLGLE--PALRDRYPHQLSGGQQQRVGVAR 147
Cdd:PRK15093 102 LDPSERVGRQlMQNI---PGWTYK---GRWWQRFGWRKR----RAIELLHRVGIKdhKDAMRSFPYELTEGECQKVMIAI 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 148 ALAANPQVLLMDEPFGALDPVTRGALQAEMTRIHRILGRTIVLVTHDIDEALRLADHLVLMDHGEVVQQGSPLELLTWPK 227
Cdd:PRK15093 172 ALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTVETAPSKELVTTPH 251
|
250
....*....|....*..
gi 772671321 228 NDFVREF------FGRS 238
Cdd:PRK15093 252 HPYTQALiraipdFGSA 268
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1-218 |
9.30e-17 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 80.48 E-value: 9.30e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 1 MIEFLDVSKTFAGRPAASHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEIRSL-PVLElrRRMG- 78
Cdd:PRK15439 11 LLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLtPAKA--HQLGi 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 79 YAI-QSIGLFPHWTVAQNIATVLQlekwSRANIADRVDELMALLGLEPALrDRYPHQLSGGQQQRVGVARALAANPQVLL 157
Cdd:PRK15439 89 YLVpQEPLLFPNLSVKENILFGLP----KRQASMQKMKQLLAALGCQLDL-DSSAGSLEVADRQIVEILRGLMRDSRILI 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 772671321 158 MDEPFGALDPVTRGALQAEMtRIHRILGRTIVLVTHDIDEALRLADHLVLMDHGEVVQQGS 218
Cdd:PRK15439 164 LDEPTASLTPAETERLFSRI-RELLAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGK 223
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
2-212 |
1.03e-16 |
|
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: 75.56 E-value: 1.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 2 IEFLDVSKTFAGRPAASHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGmirfageEIRSLPVLElrrrmgyai 81
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEG-------IVTWGSTVK--------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 82 qsIGLFPhwtvaqniatvlqlekwsraniadrvdelmallglepalrdryphQLSGGQQQRVGVARALAANPQVLLMDEP 161
Cdd:cd03221 65 --IGYFE---------------------------------------------QLSGGEKMRLALAKLLLENPNLLLLDEP 97
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 772671321 162 FGALDPVTRGALQAEMTRIHrilgRTIVLVTHD---IDealRLADHLVLMDHGE 212
Cdd:cd03221 98 TNHLDLESIEALEEALKEYP----GTVILVSHDryfLD---QVATKIIELEDGK 144
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
34-214 |
2.50e-16 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 79.30 E-value: 2.50e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 34 GTSGSGKSTTLKMINRLVEHDSGMIRFAGEEIRSLPVLELRRR-MGYaI----QSIGLFPHWTVAQNIA-TVLQLEKWSR 107
Cdd:COG3845 291 GVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLgVAY-IpedrLGRGLVPDMSVAENLIlGRYRRPPFSR 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 108 ------ANIADRVDELMALLGLEPALRDRYPHQLSGGQQQRVGVARALAANPQVLLMDEPFGALDPvtrGALQAemtrIH 181
Cdd:COG3845 370 ggfldrKAIRAFAEELIEEFDVRTPGPDTPARSLSGGNQQKVILARELSRDPKLLIAAQPTRGLDV---GAIEF----IH 442
|
170 180 190
....*....|....*....|....*....|....*....
gi 772671321 182 RIL------GRTIVLVTHDIDEALRLADHLVLMDHGEVV 214
Cdd:COG3845 443 QRLlelrdaGAAVLLISEDLDEILALSDRIAVMYEGRIV 481
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-209 |
3.97e-16 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 78.43 E-value: 3.97e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 1 MIEFLDVSKTFAGRPAASHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDS--GMIRFAGEEIRSLPVLELRRRmG 78
Cdd:PRK13549 5 LLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGTyeGEIIFEGEELQASNIRDTERA-G 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 79 YAI--QSIGLFPHWTVAQNIatVLQLEkWSRANIAD------RVDELMALLGLE--PALRDRyphQLSGGQQQRVGVARA 148
Cdd:PRK13549 84 IAIihQELALVKELSVLENI--FLGNE-ITPGGIMDydamylRAQKLLAQLKLDinPATPVG---NLGLGQQQLVEIAKA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 772671321 149 LAANPQVLLMDEPFGALdpvTRGALQAEMTRIH--RILGRTIVLVTHDIDEALRLADHL-VLMD 209
Cdd:PRK13549 158 LNKQARLLILDEPTASL---TESETAVLLDIIRdlKAHGIACIYISHKLNEVKAISDTIcVIRD 218
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-257 |
6.90e-16 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 77.90 E-value: 6.90e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 1 MIEFLDVSKTFAGRPAASHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEIRSL-PVLELRRRMGY 79
Cdd:PRK09700 5 YISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLdHKLAAQLGIGI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 80 AIQSIGLFPHWTVAQNI-ATVLQLEKWSRANIAD------RVDELMALLGLEPALrDRYPHQLSGGQQQRVGVARALAAN 152
Cdd:PRK09700 85 IYQELSVIDELTVLENLyIGRHLTKKVCGVNIIDwremrvRAAMMLLRVGLKVDL-DEKVANLSISHKQMLEIAKTLMLD 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 153 PQVLLMDEPFGALDPVTRGALQAEMTRIhRILGRTIVLVTHDIDEALRLADHLVLMDHGEVVQQGSPLELltwPKNDFVR 232
Cdd:PRK09700 164 AKVIIMDEPTSSLTNKEVDYLFLIMNQL-RKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDV---SNDDIVR 239
|
250 260
....*....|....*....|....*
gi 772671321 233 EFFGRsELGVRLLSLRTVSDYMRRE 257
Cdd:PRK09700 240 LMVGR-ELQNRFNAMKENVSNLAHE 263
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
34-215 |
8.30e-16 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 77.52 E-value: 8.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 34 GTSGSGKSTTLKMINRLVEHDSGMIRFAGEEIR-SLPVLELRRRMGYAIQS---IGLFPHWTVAQNIATV--LQLEKWSR 107
Cdd:PRK09700 296 GLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISpRSPLDAVKKGMAYITESrrdNGFFPNFSIAQNMAISrsLKDGGYKG 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 108 A-NIADRVDEL------MALLGLEPALRDRYPHQLSGGQQQRVGVARALAANPQVLLMDEPfgaldpvTRG---ALQAEM 177
Cdd:PRK09700 376 AmGLFHEVDEQrtaenqRELLALKCHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEP-------TRGidvGAKAEI 448
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 772671321 178 TRIHRIL---GRTIVLVTHDIDEALRLADHLVLMDHGEVVQ 215
Cdd:PRK09700 449 YKVMRQLaddGKVILMVSSELPEIITVCDRIAVFCEGRLTQ 489
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-216 |
8.81e-16 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 75.54 E-value: 8.81e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 1 MIEFLDVSKTFAGRPAASHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRfageeirslpvLELRRRMGYA 80
Cdd:PRK09544 4 LVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK-----------RNGKLRIGYV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 81 IQSIGLFPhwTVAQNIATVLQLEKWSRaniadRVDELMALLGLEPALRDRYPHQ-LSGGQQQRVGVARALAANPQVLLMD 159
Cdd:PRK09544 73 PQKLYLDT--TLPLTVNRFLRLRPGTK-----KEDILPALKRVQAGHLIDAPMQkLSGGETQRVLLARALLNRPQLLVLD 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 772671321 160 EPFGALDPVTRGALQAEMTRIHRILGRTIVLVTHDI-------DEALRLADHLVLMDHGEVVQQ 216
Cdd:PRK09544 146 EPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLhlvmaktDEVLCLNHHICCSGTPEVVSL 209
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
32-219 |
1.54e-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: 1.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 32 LIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEIRSLPVLELRRRMGYAIQSIGLFPHwTVAQNIatvlqlekwSRANIA 111
Cdd:cd03369 39 IVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSSLTIIPQDPTLFSG-TIRSNL---------DPFDEY 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 112 DRVDELMALLGLEPALrdryphQLSGGQQQRVGVARALAANPQVLLMDEPFGALDPVTRGALQ----AEMTrihrilGRT 187
Cdd:cd03369 109 SDEEIYGALRVSEGGL------NLSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDALIQktirEEFT------NST 176
|
170 180 190
....*....|....*....|....*....|....*..
gi 772671321 188 IVLVTHdidealRLA-----DHLVLMDHGEVVQQGSP 219
Cdd:cd03369 177 ILTIAH------RLRtiidyDKILVMDAGEVKEYDHP 207
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
12-211 |
4.37e-15 |
|
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: 73.13 E-value: 4.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 12 AGRPAASHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEIRSLPVLELRRR----MGYAIQSIGLF 87
Cdd:cd03290 12 SGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRnrysVAYAAQKPWLL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 88 pHWTVAQNIATVLQLEKwsraniaDRVDELMALLGLEPALrDRYPH-----------QLSGGQQQRVGVARALAANPQVL 156
Cdd:cd03290 92 -NATVEENITFGSPFNK-------QRYKAVTDACSLQPDI-DLLPFgdqteigergiNLSGGQRQRICVARALYQNTNIV 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 772671321 157 LMDEPFGALD-PVTRGALQAEMTRIHRILGRTIVLVTHDIdEALRLADHLVLMDHG 211
Cdd:cd03290 163 FLDDPFSALDiHLSDHLMQEGILKFLQDDKRTLVLVTHKL-QYLPHADWIIAMKDG 217
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
6-212 |
1.23e-14 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 74.27 E-value: 1.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 6 DVSKTFAGRPAASHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEIR-SLPvlELRRRMGYAI--Q 82
Cdd:PRK10762 9 GIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTfNGP--KSSQEAGIGIihQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 83 SIGLFPHWTVAQNI------ATVLQLEKWSRANiaDRVDELMALLGLepalrDRYPHQLSG----GQQQRVGVARALAAN 152
Cdd:PRK10762 87 ELNLIPQLTIAENIflgrefVNRFGRIDWKKMY--AEADKLLARLNL-----RFSSDKLVGelsiGEQQMVEIAKVLSFE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 772671321 153 PQVLLMDEPFGAL-DPVTR------GALQAEmtrihrilGRTIVLVTHDIDEALRLADHLVLMDHGE 212
Cdd:PRK10762 160 SKVIIMDEPTDALtDTETEslfrviRELKSQ--------GRGIVYISHRLKEIFEICDDVTVFRDGQ 218
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1-214 |
1.27e-14 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 74.09 E-value: 1.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 1 MIEFLDVSKTFAGRPAASHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDS--GMIRFAGEEIRSLPVLELRRRmG 78
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTwdGEIYWSGSPLKASNIRDTERA-G 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 79 YAI--QSIGLFPHWTVAQNI----ATVLQLEKWSRANIADRVDELMALLGLEPALRDRYPHQLSGGQQQRVGVARALAAN 152
Cdd:TIGR02633 80 IVIihQELTLVPELSVAENIflgnEITLPGGRMAYNAMYLRAKNLLRELQLDADNVTRPVGDYGGGQQQLVEIAKALNKQ 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 772671321 153 PQVLLMDEPFGALdpvTRGALQAEMTRIHRILGRTI--VLVTHDIDEALRLADHLVLMDHGEVV 214
Cdd:TIGR02633 160 ARLLILDEPSSSL---TEKETEILLDIIRDLKAHGVacVYISHKLNEVKAVCDTICVIRDGQHV 220
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
1-204 |
1.63e-14 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 71.13 E-value: 1.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 1 MIEFLDVSKTFAGRPAASHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEIRSlPVLELRRRMGYA 80
Cdd:PRK13540 1 MLDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKK-DLCTYQKQLCFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 81 IQSIGLFPHWTVAQNIATVLQlekWSRANIAdrVDELMALLGLEPALrdRYP-HQLSGGQQQRVGVARALAANPQVLLMD 159
Cdd:PRK13540 80 GHRSGINPYLTLRENCLYDIH---FSPGAVG--ITELCRLFSLEHLI--DYPcGLLSSGQKRQVALLRLWMSKAKLWLLD 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 772671321 160 EPFGALDPVtrgALQAEMTRI--HRILGRTIVLVTHDiDEALRLADH 204
Cdd:PRK13540 153 EPLVALDEL---SLLTIITKIqeHRAKGGAVLLTSHQ-DLPLNKADY 195
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
13-193 |
2.10e-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: 70.60 E-value: 2.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 13 GRPAASHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEIRSLPVlELRRRMGYAIQSIGLFPHWTV 92
Cdd:cd03231 12 GRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRD-SIARGLLYLGHAPGIKTTLSV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 93 AQNiatvlqLEKWSRANIADRVDELMALLGLEpALRDRYPHQLSGGQQQRVGVARALAANPQVLLMDEPFGALDpVTRGA 172
Cdd:cd03231 91 LEN------LRFWHADHSDEQVEEALARVGLN-GFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALD-KAGVA 162
|
170 180
....*....|....*....|.
gi 772671321 173 LQAEMTRIHRILGRTIVLVTH 193
Cdd:cd03231 163 RFAEAMAGHCARGGMVVLTTH 183
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
27-217 |
3.15e-14 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 71.45 E-value: 3.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 27 GAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEIRSlpvlELRRRM-GYAIQSIGLfpHWTVAQNIATVLQLEKW 105
Cdd:PRK15056 33 GSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQ----ALQKNLvAYVPQSEEV--DWSFPVLVEDVVMMGRY 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 106 S------RANIADR--VDELMALLGLEpALRDRYPHQLSGGQQQRVGVARALAANPQVLLMDEPFGALDPVTRGALQAeM 177
Cdd:PRK15056 107 GhmgwlrRAKKRDRqiVTAALARVDMV-EFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARIIS-L 184
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 772671321 178 TRIHRILGRTIVLVTHDIDEALRLADHLVlMDHGEVVQQG 217
Cdd:PRK15056 185 LRELRDEGKTMLVSTHNLGSVTEFCDYTV-MVKGTVLASG 223
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
20-218 |
3.35e-14 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 73.27 E-value: 3.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 20 LNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIrfageeirslpvlelrrrmgYAIQSIGLFPH--W----TVA 93
Cdd:PTZ00243 679 VSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV--------------------WAERSIAYVPQqaWimnaTVR 738
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 94 QNIatvLQLEKWSRANIAD--RVDELMALL-----GLEPALRDRYPHqLSGGQQQRVGVARALAANPQVLLMDEPFGALD 166
Cdd:PTZ00243 739 GNI---LFFDEEDAARLADavRVSQLEADLaqlggGLETEIGEKGVN-LSGGQKARVSLARAVYANRDVYLLDDPLSALD 814
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 772671321 167 PVTrGALQAEMTRIHRILGRTIVLVTHDIdEALRLADHLVLMDHGEVVQQGS 218
Cdd:PTZ00243 815 AHV-GERVVEECFLGALAGKTRVLATHQV-HVVPRADYVVALGDGRVEFSGS 864
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
6-211 |
4.72e-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: 73.12 E-value: 4.72e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 6 DVSKTFAG--RPAASHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEIRSlPVLELRRRMGYAIQS 83
Cdd:TIGR01257 1942 ELTKVYSGtsSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT-NISDVHQNMGYCPQF 2020
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 84 IGLFPHWTVAQNIATVLQLEKWSRANIADRVDELMALLGLEpALRDRYPHQLSGGQQQRVGVARALAANPQVLLMDEPFG 163
Cdd:TIGR01257 2021 DAIDDLLTGREHLYLYARLRGVPAEEIEKVANWSIQSLGLS-LYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTT 2099
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 772671321 164 ALDPVTRGALQAEMTRIHRiLGRTIVLVTHDIDEALRLADHLVLMDHG 211
Cdd:TIGR01257 2100 GMDPQARRMLWNTIVSIIR-EGRAVVLTSHSMEECEALCTRLAIMVKG 2146
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
3-238 |
4.76e-14 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 72.25 E-value: 4.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 3 EFLDVSKTFAGRPAASHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEIR---SLPVLElrrrMGY 79
Cdd:PRK11288 6 SFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRfasTTAALA----AGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 80 AI--QSIGLFPHWTVAQNIatVL-QLEkwSRANIADR------VDELMALLGLE--PALRDRYphqLSGGQQQRVGVARA 148
Cdd:PRK11288 82 AIiyQELHLVPEMTVAENL--YLgQLP--HKGGIVNRrllnyeAREQLEHLGVDidPDTPLKY---LSIGQRQMVEIAKA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 149 LAANPQVLLMDEPFGALDpvtrgalQAEMTRIHRIL------GRTIVLVTHDIDEALRLADHLVLMDHGEVVQQGSPLEL 222
Cdd:PRK11288 155 LARNARVIAFDEPTSSLS-------AREIEQLFRVIrelraeGRVILYVSHRMEEIFALCDAITVFKDGRYVATFDDMAQ 227
|
250
....*....|....*.
gi 772671321 223 LTwpKNDFVREFFGRS 238
Cdd:PRK11288 228 VD--RDQLVQAMVGRE 241
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
20-223 |
1.36e-13 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 68.94 E-value: 1.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 20 LNLNFAEGAFSVLIGTSGSGKSTTLKMI--NRLVEHDSGMIRFAGEEIRSLPVLElRRRMG--YAIQSIGLFPHWTVAQN 95
Cdd:COG0396 19 VNLTIKPGEVHAIMGPNGSGKSTLAKVLmgHPKYEVTSGSILLDGEDILELSPDE-RARAGifLAFQYPVEIPGVSVSNF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 96 IATVLQ---LEKWSRANIADRVDELMALLGLEPALRDRYPHQ-LSGGQQQRVGVARALAANPQVLLMDEP-FG----ALD 166
Cdd:COG0396 98 LRTALNarrGEELSAREFLKLLKEKMKELGLDEDFLDRYVNEgFSGGEKKRNEILQMLLLEPKLAILDETdSGldidALR 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 772671321 167 PVTRG--ALQAEmtrihrilGRTIVLVTHdideALRL-----ADHLVLMDHGEVVQQGSPlELL 223
Cdd:COG0396 178 IVAEGvnKLRSP--------DRGILIITH----YQRIldyikPDFVHVLVDGRIVKSGGK-ELA 228
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
6-224 |
1.41e-13 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 71.31 E-value: 1.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 6 DVSKTFAGRPAASHLNLNFAEGAFSVLIGTSGSGKSTTLKMIN--RLVEhdSGMIRFAGEEIRSLPVlelRRRMGYAI-- 81
Cdd:NF033858 6 GVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAgaRKIQ--QGRVEVLGGDMADARH---RRAVCPRIay 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 82 --QSIG--LFPHWTVAQNIATVLQLEKWSRANIADRVDELMALLGLEPaLRDRYPHQLSGGQQQRVGVARALAANPQVLL 157
Cdd:NF033858 81 mpQGLGknLYPTLSVFENLDFFGRLFGQDAAERRRRIDELLRATGLAP-FADRPAGKLSGGMKQKLGLCCALIHDPDLLI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 772671321 158 MDEPFGALDPVTR-------GALQAE---MTrihrilgrtiVLV-THDIDEALRLaDHLVLMDHGEVVQQGSPLELLT 224
Cdd:NF033858 160 LDEPTTGVDPLSRrqfweliDRIRAErpgMS----------VLVaTAYMEEAERF-DWLVAMDAGRVLATGTPAELLA 226
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
2-223 |
3.04e-13 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 70.13 E-value: 3.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 2 IEFLDVSktFA---GRPAASHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEIRSLPVLELRRRMG 78
Cdd:PRK10790 341 IDIDNVS--FAyrdDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVA 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 79 YAIQ-----SIGLFPHWTVAQNIA--------TVLQLEKWSRAniadRVDELMALLGLEPalrdrypHQLSGGQQQRVGV 145
Cdd:PRK10790 419 MVQQdpvvlADTFLANVTLGRDISeeqvwqalETVQLAELARS----LPDGLYTPLGEQG-------NNLSVGQKQLLAL 487
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 146 ARALAANPQVLLMDEPFGALDPVTRGALQAEMTRIHRilGRTIVLVTHdidealRL-----ADHLVLMDHGEVVQQGSPL 220
Cdd:PRK10790 488 ARVLVQTPQILILDEATANIDSGTEQAIQQALAAVRE--HTTLVVIAH------RLstiveADTILVLHRGQAVEQGTHQ 559
|
...
gi 772671321 221 ELL 223
Cdd:PRK10790 560 QLL 562
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
94-224 |
4.26e-13 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 68.99 E-value: 4.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 94 QNIATVLQLEKWSRANIADRVDELMALLGLEPAlRDRYPHQLSGGQQQRVGVARALAANPQVLLMDEPFGALDPVTRGAL 173
Cdd:NF000106 105 ENLYMIGR*LDLSRKDARARADELLERFSLTEA-AGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEV 183
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 772671321 174 QAEMTRIHRIlGRTIVLVTHDIDEALRLADHLVLMDHGEVVQQGSPLELLT 224
Cdd:NF000106 184 WDEVRSMVRD-GATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDELKT 233
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
32-239 |
9.56e-13 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 69.04 E-value: 9.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 32 LIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEIRSLPVLELRRRMGYAIQSIGLFPHwTVAQNIATVLQlekwsrANIA 111
Cdd:PTZ00243 1341 IVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFSMIPQDPVLFDG-TVRQNVDPFLE------ASSA 1413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 112 drvdELMALLGLePALRDRYPHQLSG--------------GQQQRVGVARA-LAANPQVLLMDEPFGALDPVTRGALQAe 176
Cdd:PTZ00243 1414 ----EVWAALEL-VGLRERVASESEGidsrvleggsnysvGQRQLMCMARAlLKKGSGFILMDEATANIDPALDRQIQA- 1487
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 772671321 177 mTRIHRILGRTIVLVTHDIDEALRLaDHLVLMDHGEVVQQGSPLELLTWPKNDF--VREFFGRSE 239
Cdd:PTZ00243 1488 -TVMSAFSAYTVITIAHRLHTVAQY-DKIIVMDHGAVAEMGSPRELVMNRQSIFhsMVEALGRSE 1550
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
32-241 |
1.24e-12 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 68.15 E-value: 1.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 32 LIGTSGSGKSTTLKMINRLVEHD---SGMIRFAGEEIRSLpvlELRRRMGYAIQSIGLFPHWTVAQNI---ATVLQLEKW 105
Cdd:TIGR00955 56 VMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGMPIDAK---EMRAISAYVQQDDLFIPTLTVREHLmfqAHLRMPRRV 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 106 SRANIADRVDELMALLGLEPALRDR--YPHQ---LSGGQQQRVGVARALAANPQVLLMDEPFGALDPVTRGALQAEMTRI 180
Cdd:TIGR00955 133 TKKEKRERVDEVLQALGLRKCANTRigVPGRvkgLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGL 212
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 772671321 181 HRiLGRTIVLVTHD-IDEALRLADHLVLMDHGEVVQQGSPLELLtwpkndfvrEFFgrSELG 241
Cdd:TIGR00955 213 AQ-KGKTIICTIHQpSSELFELFDKIILMAEGRVAYLGSPDQAV---------PFF--SDLG 262
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
14-222 |
1.63e-12 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 68.08 E-value: 1.63e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 14 RPAASHLNLNFAEGAFSVLIGTSGSGKSTTLkminrlvehdSGMIrfaGEeirsLPVLE-----LRRRMGYAIQSIGLFp 88
Cdd:PLN03232 630 KPTLSDINLEIPVGSLVAIVGGTGEGKTSLI----------SAML---GE----LSHAEtssvvIRGSVAYVPQVSWIF- 691
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 89 HWTVAQNIATVLQLEKwSRANIADRVDELMALLGLEPAlRDRYP-----HQLSGGQQQRVGVARALAANPQVLLMDEPFG 163
Cdd:PLN03232 692 NATVRENILFGSDFES-ERYWRAIDVTALQHDLDLLPG-RDLTEigergVNISGGQKQRVSMARAVYSNSDIYIFDDPLS 769
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 164 ALDP-VTRGALQAEMTriHRILGRTIVLVTHDIdEALRLADHLVLMDHGEVVQQGSPLEL 222
Cdd:PLN03232 770 ALDAhVAHQVFDSCMK--DELKGKTRVLVTNQL-HFLPLMDRIILVSEGMIKEEGTFAEL 826
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
20-224 |
1.84e-12 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 66.39 E-value: 1.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 20 LNLNFAEGAFSVLIGTSGSGKSTTLKMI-NRLVEHD-------SGMIRFAGEEIRSLPVLELRRRM---------GYA-- 80
Cdd:PRK13547 20 LSLRIEPGRVTALLGRNGAGKSTLLKALaGDLTGGGaprgarvTGDVTLNGEPLAAIDAPRLARLRavlpqaaqpAFAfs 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 81 ---IQSIGLFPHWTVAQNIAtvlqlekwsranIADR--VDELMALLGLEPALRdRYPHQLSGGQQQRVGVARALA----- 150
Cdd:PRK13547 100 areIVLLGRYPHARRAGALT------------HRDGeiAWQALALAGATALVG-RDVTTLSGGELARVQFARVLAqlwpp 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 772671321 151 ----ANPQVLLMDEPFGALDPVTRGALQAEMTRIHRILGRTIVLVTHDIDEALRLADHLVLMDHGEVVQQGSPLELLT 224
Cdd:PRK13547 167 hdaaQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPADVLT 244
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
13-236 |
2.54e-12 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 67.63 E-value: 2.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 13 GRPAASHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGeeirslpvlelrrRMGYAIQSIGLFPHwTV 92
Cdd:TIGR01271 438 VTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG-------------RISFSPQTSWIMPG-TI 503
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 93 AQNIATVLQLEKWSRANI--ADRVDELMALLglepALRDRYPH-----QLSGGQQQRVGVARALAANPQVLLMDEPFGAL 165
Cdd:TIGR01271 504 KDNIIFGLSYDEYRYTSVikACQLEEDIALF----PEKDKTVLgeggiTLSGGQRARISLARAVYKDADLYLLDSPFTHL 579
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 772671321 166 DPVTRGALqAEMTRIHRILGRTIVLVTHDIdEALRLADHLVLMDHGEVVQQGSPLELLTwPKNDFVREFFG 236
Cdd:TIGR01271 580 DVVTEKEI-FESCLCKLMSNKTRILVTSKL-EHLKKADKILLLHEGVCYFYGTFSELQA-KRPDFSSLLLG 647
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
2-174 |
2.94e-12 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 66.88 E-value: 2.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 2 IEFLDVSKTFAGRPAASHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFaGEEIrslpvlelrrRMGYAI 81
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETV----------KLAYVD 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 82 QS-IGLFPHWTVAQNIA---TVLQLEKW---SRANIadrvdelmALLGLEPALRDRYPHQLSGGQQQRVGVARALAANPQ 154
Cdd:TIGR03719 392 QSrDALDPNKTVWEEISgglDIIKLGKReipSRAYV--------GRFNFKGSDQQKKVGQLSGGERNRVHLAKTLKSGGN 463
|
170 180
....*....|....*....|
gi 772671321 155 VLLMDEPFGALDPVTRGALQ 174
Cdd:TIGR03719 464 VLLLDEPTNDLDVETLRALE 483
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
5-269 |
3.48e-12 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 65.65 E-value: 3.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 5 LDVSKTFAGRPAASHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDsGMIRFAGEEIRSLPVLELRRRMGYAIQSI 84
Cdd:cd03289 8 LTAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GDIQIDGVSWNSVPLQKWRKAFGVIPQKV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 85 GLFPHwTVAQNIATvlqLEKWSRANIADRVDELmallGLEPALrDRYPHQL-----------SGGQQQRVGVARALAANP 153
Cdd:cd03289 87 FIFSG-TFRKNLDP---YGKWSDEEIWKVAEEV----GLKSVI-EQFPGQLdfvlvdggcvlSHGHKQLMCLARSVLSKA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 154 QVLLMDEPFGALDPVTRGALQAemTRIHRILGRTIVLVTHDIdEALRLADHLVLMDHGEVVQQGSPLELLTwpKNDFVRE 233
Cdd:cd03289 158 KILLLDEPSAHLDPITYQVIRK--TLKQAFADCTVILSEHRI-EAMLECQRFLVIEENKVRQYDSIQKLLN--EKSHFKQ 232
|
250 260 270
....*....|....*....|....*....|....*.
gi 772671321 234 FFGRSElGVRLLSLRTVSDYMRREEMPVSGepLQEQ 269
Cdd:cd03289 233 AISPSD-RLKLFPRRNSSKSKRKPRPQIQA--LQEE 265
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
13-222 |
9.72e-12 |
|
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: 64.49 E-value: 9.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 13 GRPAASHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGeeirslpvlelrrRMGYAIQSIGLFPHwTV 92
Cdd:cd03291 49 GAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG-------------RISFSSQFSWIMPG-TI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 93 AQNIATVLQLEKWSRANI--ADRVDELMALLglepALRDRYPH-----QLSGGQQQRVGVARALAANPQVLLMDEPFGAL 165
Cdd:cd03291 115 KENIIFGVSYDEYRYKSVvkACQLEEDITKF----PEKDNTVLgeggiTLSGGQRARISLARAVYKDADLYLLDSPFGYL 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 772671321 166 DPVTRG--------ALQAEMTRIhrilgrtivLVTHDIdEALRLADHLVLMDHGEVVQQGSPLEL 222
Cdd:cd03291 191 DVFTEKeifescvcKLMANKTRI---------LVTSKM-EHLKKADKILILHEGSSYFYGTFSEL 245
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
1-232 |
1.48e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 65.38 E-value: 1.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 1 MIEFLDVSKTF-AGRPAASHlNLNFAEGAFSVL--IGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEIRSLPVLELRRRM 77
Cdd:PLN03232 1234 SIKFEDVHLRYrPGLPPVLH-GLSFFVSPSEKVgvVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVL 1312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 78 GYAIQSIGLFPHwTVAQNIATVLQ------LEKWSRANIADRVDElmALLGLEPALRDRyPHQLSGGQQQRVGVARALAA 151
Cdd:PLN03232 1313 SIIPQSPVLFSG-TVRFNIDPFSEhndadlWEALERAHIKDVIDR--NPFGLDAEVSEG-GENFSVGQRQLLSLARALLR 1388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 152 NPQVLLMDEPFGALDPVTRGALQAEMTRIHRILgrTIVLVTHDIDEALRlADHLVLMDHGEVVQQGSPLELLTWPKNDFV 231
Cdd:PLN03232 1389 RSKILVLDEATASVDVRTDSLIQRTIREEFKSC--TMLVIAHRLNTIID-CDKILVLSSGQVLEYDSPQELLSRDTSAFF 1465
|
.
gi 772671321 232 R 232
Cdd:PLN03232 1466 R 1466
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
12-222 |
1.52e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 65.14 E-value: 1.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 12 AGRPAASHLNLNFAEGAFSVLIGTSGSGKSTTLkminrlvehdSGMIrfaGEeirsLPVLE-----LRRRMGYAIQSIGL 86
Cdd:PLN03130 628 AERPTLSNINLDVPVGSLVAIVGSTGEGKTSLI----------SAML---GE----LPPRSdasvvIRGTVAYVPQVSWI 690
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 87 FpHWTVAQNIATVLQLEKwSRANIADRVDELMALLGLEPA-----LRDRYPHqLSGGQQQRVGVARALAANPQVLLMDEP 161
Cdd:PLN03130 691 F-NATVRDNILFGSPFDP-ERYERAIDVTALQHDLDLLPGgdlteIGERGVN-ISGGQKQRVSMARAVYSNSDVYIFDDP 767
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 772671321 162 FGALDP-VTRgalQAEMTRIHRIL-GRTIVLVTHDIdEALRLADHLVLMDHGEVVQQGSPLEL 222
Cdd:PLN03130 768 LSALDAhVGR---QVFDKCIKDELrGKTRVLVTNQL-HFLSQVDRIILVHEGMIKEEGTYEEL 826
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
23-209 |
2.01e-11 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 62.81 E-value: 2.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 23 NFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEIrslpvlelrrrmGYAIQSIGLFPHWTVAQNIATVLQl 102
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTV------------SYKPQYIKADYEGTVRDLLSSITK- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 103 ekwSRANIADRVDELMALLGLEPALrDRYPHQLSGGQQQRVGVARALAANPQVLLMDEPFGALDPVTRGALQAEMTRIHR 182
Cdd:cd03237 88 ---DFYTHPYFKTEIAKPLQIEQIL-DREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFAE 163
|
170 180
....*....|....*....|....*..
gi 772671321 183 ILGRTIVLVTHDIDEALRLADHLVLMD 209
Cdd:cd03237 164 NNEKTAFVVEHDIIMIDYLADRLIVFE 190
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
14-223 |
3.34e-11 |
|
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: 62.62 E-value: 3.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 14 RPAASHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEIRSLPVLELRRRMGYAIQSIGLFphwtvA 93
Cdd:cd03288 34 KPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPILF-----S 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 94 QNIATVLQLEK-------WSRANIADRVDELMALLGLEPALRDRYPHQLSGGQQQRVGVARALAANPQVLLMDEPFGALD 166
Cdd:cd03288 109 GSIRFNLDPECkctddrlWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASID 188
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 772671321 167 PVTRGALQ-AEMTrihRILGRTIVLVTHDIDEALRlADHLVLMDHGEVVQQGSPLELL 223
Cdd:cd03288 189 MATENILQkVVMT---AFADRTVVTIAHRVSTILD-ADLVLVLSRGILVECDTPENLL 242
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
2-193 |
3.53e-11 |
|
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: 60.63 E-value: 3.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 2 IEFLDVS-KTFAGRPAASHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRF-AGEEIRSLPvlelrrRMGY 79
Cdd:cd03223 1 IELENLSlATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMpEGEDLLFLP------QRPY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 80 aiqsiglFPHWTVAQNIAtvlqlekwsraniadrvdelmallglepalrdrYP--HQLSGGQQQRVGVARALAANPQVLL 157
Cdd:cd03223 75 -------LPLGTLREQLI---------------------------------YPwdDVLSGGEQQRLAFARLLLHKPKFVF 114
|
170 180 190
....*....|....*....|....*....|....*.
gi 772671321 158 MDEPFGALDPvtrgALQAEMTRIHRILGRTIVLVTH 193
Cdd:cd03223 115 LDEATSALDE----ESEDRLYQLLKELGITVISVGH 146
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
1-209 |
3.59e-11 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 63.66 E-value: 3.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 1 MIEFLDVSKTFAGRPAASHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDS--GMIRFAGEE-----IRSlpvlel 73
Cdd:NF040905 1 ILEMRGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGSyeGEILFDGEVcrfkdIRD------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 74 RRRMGYAI--QSIGLFPHWTVAQNIatVLQLEK-------WSRANIadRVDELMALLGLEPAlrdryPHQLSG----GQQ 140
Cdd:NF040905 75 SEALGIVIihQELALIPYLSIAENI--FLGNERakrgvidWNETNR--RARELLAKVGLDES-----PDTLVTdigvGKQ 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 141 QRVGVARALAANPQVLLMDEPFGALDPVTRGALqAEMTRIHRILGRTIVLVTHDIDEALRLADHL-VLMD 209
Cdd:NF040905 146 QLVEIAKALSKDVKLLILDEPTAALNEEDSAAL-LDLLLELKAQGITSIIISHKLNEIRRVADSItVLRD 214
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
1-239 |
4.14e-11 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 63.78 E-value: 4.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 1 MIEFLDVSKTFAGRPAASHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDsGMIRFAGEEIRSLPVLELRRRMGYA 80
Cdd:TIGR01271 1219 DVQGLTAKYTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTE-GEIQIDGVSWNSVTLQTWRKAFGVI 1297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 81 IQSIGLFPHwTVAQNIATvlqLEKWSRANIADRVDELmallGLEPALrDRYPHQL-----------SGGQQQRVGVARAL 149
Cdd:TIGR01271 1298 PQKVFIFSG-TFRKNLDP---YEQWSDEEIWKVAEEV----GLKSVI-EQFPDKLdfvlvdggyvlSNGHKQLMCLARSI 1368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 150 AANPQVLLMDEPFGALDPVTRGALQAemTRIHRILGRTIVLVTHDIdEALRLADHLVLMDHGEVVQQGSPLELLTwpKND 229
Cdd:TIGR01271 1369 LSKAKILLLDEPSAHLDPVTLQIIRK--TLKQSFSNCTVILSEHRV-EALLECQQFLVIEGSSVKQYDSIQKLLN--ETS 1443
|
250
....*....|
gi 772671321 230 FVREFFGRSE 239
Cdd:TIGR01271 1444 LFKQAMSAAD 1453
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
2-224 |
4.64e-11 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 63.89 E-value: 4.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 2 IEFLDVSKTFAGRPAAS-HLNLNFA--EGAFSVLIGTSGSGKSTTLKMINRL---------------------------- 50
Cdd:PTZ00265 1166 IEIMDVNFRYISRPNVPiYKDLTFScdSKKTTAIVGETGSGKSTVMSLLMRFydlkndhhivfknehtndmtneqdyqgd 1245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 51 --------------------------VEHDSGMIRFAGEEIRSLPVLELRRRMGYAIQSIGLFpHWTVAQNI------AT 98
Cdd:PTZ00265 1246 eeqnvgmknvnefsltkeggsgedstVFKNSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLF-NMSIYENIkfgkedAT 1324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 99 vlqLEKWSRANIADRVDELMALLglePALRDR----YPHQLSGGQQQRVGVARALAANPQVLLMDEPFGALDPVTRGALQ 174
Cdd:PTZ00265 1325 ---REDVKRACKFAAIDEFIESL---PNKYDTnvgpYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIE 1398
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 772671321 175 AEMTRIHRILGRTIVLVTHDIdEALRLADHLVLMDH----GEVVQ-QGSPLELLT 224
Cdd:PTZ00265 1399 KTIVDIKDKADKTIITIAHRI-ASIKRSDKIVVFNNpdrtGSFVQaHGTHEELLS 1452
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
18-213 |
4.73e-11 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 63.15 E-value: 4.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 18 SHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEIRSLPVLE-LRRRMGYAI---QSIGLFPHWTVA 93
Cdd:PRK15439 280 RNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQrLARGLVYLPedrQSSGLYLDAPLA 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 94 QNIATVLQLEK--WSR-ANIADRVDELMALLGLEPALRDRYPHQLSGGQQQRVGVARALAANPQVLLMDEPfgaldpvTR 170
Cdd:PRK15439 360 WNVCALTHNRRgfWIKpARENAVLERYRRALNIKFNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEP-------TR 432
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 772671321 171 GALQAEMTRIHRIL------GRTIVLVTHDIDEALRLADHLVLMDHGEV 213
Cdd:PRK15439 433 GVDVSARNDIYQLIrsiaaqNVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
2-170 |
7.25e-11 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 62.72 E-value: 7.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 2 IEFLDVSKTFAGRPAASHLNLNFAEGAFSVLIGTSGSGKSTTLKMI---------NRLVEHdsGMIRFAGEEIrslpvLE 72
Cdd:PRK10938 261 IVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLItgdhpqgysNDLTLF--GRRRGSGETI-----WD 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 73 LRRRMGYAIQSIGLfpHWTVAQNIATVL-----------QlekwsraNIADR----VDELMALLGLEPALRDRYPHQLSG 137
Cdd:PRK10938 334 IKKHIGYVSSSLHL--DYRVSTSVRNVIlsgffdsigiyQ-------AVSDRqqklAQQWLDILGIDKRTADAPFHSLSW 404
|
170 180 190
....*....|....*....|....*....|...
gi 772671321 138 GQQQRVGVARALAANPQVLLMDEPFGALDPVTR 170
Cdd:PRK10938 405 GQQRLALIVRALVKHPTLLILDEPLQGLDPLNR 437
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
6-224 |
1.45e-10 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 61.67 E-value: 1.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 6 DVSKTFAGRPAASHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEIR---SLPVLELRRRMGYaiQ 82
Cdd:PRK10982 3 NISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfksSKEALENGISMVH--Q 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 83 SIGLFPHWTVAQNI--------ATVLQLEKWSRANIAdrvdeLMALLGLEPALRDRYPhQLSGGQQQRVGVARALAANPQ 154
Cdd:PRK10982 81 ELNLVLQRSVMDNMwlgryptkGMFVDQDKMYRDTKA-----IFDELDIDIDPRAKVA-TLSVSQMQMIEIAKAFSYNAK 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 772671321 155 VLLMDEPFGALDpvtrgalQAEMTRIHRIL------GRTIVLVTHDIDEALRLADHLVLMDHGEVVQQgSPLELLT 224
Cdd:PRK10982 155 IVIMDEPTSSLT-------EKEVNHLFTIIrklkerGCGIVYISHKMEEIFQLCDEITILRDGQWIAT-QPLAGLT 222
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
19-223 |
1.69e-10 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 61.89 E-value: 1.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 19 HLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEIRSLPVLELRRRMGYAIQSIGLFPHwTVAQNIAT 98
Cdd:TIGR00957 1304 HINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSG-SLRMNLDP 1382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 99 VLQL---EKWSRAniadrvdELMALLGLEPALRDRYPHQ-------LSGGQQQRVGVARALAANPQVLLMDEPFGALDPV 168
Cdd:TIGR00957 1383 FSQYsdeEVWWAL-------ELAHLKTFVSALPDKLDHEcaeggenLSVGQRQLVCLARALLRKTKILVLDEATAAVDLE 1455
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 772671321 169 TRGALQAEM-TRIHRIlgrTIVLVTHDIDEALRLADHLVLmDHGEVVQQGSPLELL 223
Cdd:TIGR00957 1456 TDNLIQSTIrTQFEDC---TVLTIAHRLNTIMDYTRVIVL-DKGEVAEFGAPSNLL 1507
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
25-195 |
3.75e-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: 59.30 E-value: 3.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 25 AEGAFSVLIGTSGSGKSTTLK-----MINRLVEHDS-----GMIR-FAGEEIRSL--PVLELRRRMGYAIQSIGLFPhwt 91
Cdd:cd03236 24 REGQVLGLVGPNGIGKSTALKilagkLKPNLGKFDDppdwdEILDeFRGSELQNYftKLLEGDVKVIVKPQYVDLIP--- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 92 vAQNIATVLQLEKwsRANIADRVDELMALLGLEPaLRDRYPHQLSGGQQQRVGVARALAANPQVLLMDEPFGALDPVTRg 171
Cdd:cd03236 101 -KAVKGKVGELLK--KKDERGKLDELVDQLELRH-VLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQR- 175
|
170 180
....*....|....*....|....*.
gi 772671321 172 aLQAEMTrIHRIL--GRTIVLVTHDI 195
Cdd:cd03236 176 -LNAARL-IRELAedDNYVLVVEHDL 199
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
20-223 |
3.93e-10 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 58.31 E-value: 3.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 20 LNLNFAEGAFSVLIGTSGSGKSTTLKMI--NRLVEHDSGMIRFAGEEIRSLPVLElRRRMgyaiqsiGLFPHWtvaQNIA 97
Cdd:cd03217 19 VNLTIKKGEVHALMGPNGSGKSTLAKTImgHPKYEVTEGEILFKGEDITDLPPEE-RARL-------GIFLAF---QYPP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 98 TV--LQLEKWSRAniadrVDElmallglepalrdryphQLSGGQQQRVGVARALAANPQVLLMDEPFGALDpVTRGALQA 175
Cdd:cd03217 88 EIpgVKNADFLRY-----VNE-----------------GFSGGEKKRNEILQLLLLEPDLAILDEPDSGLD-IDALRLVA 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 772671321 176 EMTRIHRILGRTIVLVTHdideALRLADHLV-----LMDHGEVVQQGsPLELL 223
Cdd:cd03217 145 EVINKLREEGKSVLIITH----YQRLLDYIKpdrvhVLYDGRIVKSG-DKELA 192
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
20-217 |
5.00e-10 |
|
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: 58.42 E-value: 5.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 20 LNLNFAEGAFSVLIGTSGSGKST----TLkminrlveHDSGMIRFageeIRSLPVLeLRRRMGY----AIQSI-GLFPHW 90
Cdd:cd03270 14 VDVDIPRNKLVVITGVSGSGKSSlafdTI--------YAEGQRRY----VESLSAY-ARQFLGQmdkpDVDSIeGLSPAI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 91 TVAQN---------IATVLQLEK-----WSRANIADRVDELMALlGLEPALRDRYPHQLSGGQQQRVGVARALAANPQVL 156
Cdd:cd03270 81 AIDQKttsrnprstVGTVTEIYDylrllFARVGIRERLGFLVDV-GLGYLTLSRSAPTLSGGEAQRIRLATQIGSGLTGV 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 772671321 157 L--MDEPFGALDPVTRGALQAEMTRIhRILGRTIVLVTHDiDEALRLADHLVLM-----DH-GEVVQQG 217
Cdd:cd03270 160 LyvLDEPSIGLHPRDNDRLIETLKRL-RDLGNTVLVVEHD-EDTIRAADHVIDIgpgagVHgGEIVAQG 226
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
8-217 |
6.36e-10 |
|
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: 58.04 E-value: 6.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 8 SKTFAGRPAASHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHD---SGMIRFAGE---EIRSLPvlelRRRMGYAI 81
Cdd:cd03233 14 GKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIpykEFAEKY----PGEIIYVS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 82 QSIGLFPHWTVAQNIATVLQLekwsRANiadrvdelmallglepalrdRYPHQLSGGQQQRVGVARALAANPQVLLMDEP 161
Cdd:cd03233 90 EEDVHFPTLTVRETLDFALRC----KGN--------------------EFVRGISGGERKRVSIAEALVSRASVLCWDNS 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 772671321 162 FGALDPVTrgALQ-----AEMTRIHRilGRTIVLVTHDIDEALRLADHLVLMDHGEVVQQG 217
Cdd:cd03233 146 TRGLDSST--ALEilkciRTMADVLK--TTTFVSLYQASDEIYDLFDKVLVLYEGRQIYYG 202
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
18-193 |
7.40e-10 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 57.51 E-value: 7.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 18 SHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEIRSLPVlELRRRMGYAIQSIGLFPHWTVAQNIA 97
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRD-EYHQDLLYLGHQPGIKTELTALENLR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 98 TVLQLEKWSRANIADRVDELMALLGLE--PAlrdrypHQLSGGQQQRVGVARALAANPQVLLMDEPFGALDpvTRGAlqA 175
Cdd:PRK13538 97 FYQRLHGPGDDEALWEALAQVGLAGFEdvPV------RQLSAGQQRRVALARLWLTRAPLWILDEPFTAID--KQGV--A 166
|
170 180
....*....|....*....|.
gi 772671321 176 EMTRI---HRILGRTIVLVTH 193
Cdd:PRK13538 167 RLEALlaqHAEQGGMVILTTH 187
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
85-213 |
9.08e-10 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 59.17 E-value: 9.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 85 GLFPHWTVAQNIaTVLQLEKWSRANIADRVDELMALLGLEPALRDRYPH------QLSGGQQQRVGVARALAANPQVLLM 158
Cdd:PRK13549 351 GIVPVMGVGKNI-TLAALDRFTGGSRIDDAAELKTILESIQRLKVKTASpelaiaRLSGGNQQKAVLAKCLLLNPKILIL 429
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 772671321 159 DEPfgaldpvTRGALQAEMTRIHRIL------GRTIVLVTHDIDEALRLADHLVLMDHGEV 213
Cdd:PRK13549 430 DEP-------TRGIDVGAKYEIYKLInqlvqqGVAIIVISSELPEVLGLSDRVLVMHEGKL 483
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
24-220 |
1.16e-09 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 59.47 E-value: 1.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 24 FAEGAFSVLIGTSGSGKSTTLKMI--NRLVEHDSGMIRFAGeeirsLPVLE--LRRRMGYAIQSIGLFPHWTVAQNI--A 97
Cdd:PLN03140 903 FRPGVLTALMGVSGAGKTTLMDVLagRKTGGYIEGDIRISG-----FPKKQetFARISGYCEQNDIHSPQVTVRESLiyS 977
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 98 TVLQLEKW-SRANIADRVDELMALLGLEpALRDR---YP--HQLSGGQQQRVGVARALAANPQVLLMDEPFGALDpvTRG 171
Cdd:PLN03140 978 AFLRLPKEvSKEEKMMFVDEVMELVELD-NLKDAivgLPgvTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLD--ARA 1054
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 772671321 172 AlqAEMTRIHR---ILGRTIVLVTH----DIDEALrlaDHLVLMDHGEVVQQGSPL 220
Cdd:PLN03140 1055 A--AIVMRTVRntvDTGRTVVCTIHqpsiDIFEAF---DELLLMKRGGQVIYSGPL 1105
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
6-193 |
1.50e-09 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 58.74 E-value: 1.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 6 DVSKTFAGRPAASHLNLNFAEGAFSVLIGTSGSGKSTTLKMI-NRLVEHD-SGMIRFAGEEirslPVLELRRRMGYAIQS 83
Cdd:PLN03211 73 DETRQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALaGRIQGNNfTGTILANNRK----PTKQILKRTGFVTQD 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 84 IGLFPHWTVAQNI--ATVLQLEK-WSRANIADRVDELMALLGLEPA----LRDRYPHQLSGGQQQRVGVARALAANPQVL 156
Cdd:PLN03211 149 DILYPHLTVRETLvfCSLLRLPKsLTKQEKILVAESVISELGLTKCentiIGNSFIRGISGGERKRVSIAHEMLINPSLL 228
|
170 180 190
....*....|....*....|....*....|....*..
gi 772671321 157 LMDEPFGALDPVTRGALQAEMTRIHRiLGRTIVLVTH 193
Cdd:PLN03211 229 ILDEPTSGLDATAAYRLVLTLGSLAQ-KGKTIVTSMH 264
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
20-212 |
2.09e-09 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 58.89 E-value: 2.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 20 LNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSG-MIRFAGEEIRSLPVLELRRRMGYAIQSIGLFPHwTVAQNIAT 98
Cdd:PTZ00265 404 LNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGdIIINDSHNLKDINLKWWRSKIGVVSQDPLLFSN-SIKNNIKY 482
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 99 VL----QLEKWS--------------------RANIADRVDELM------ALLGLE------------------------ 124
Cdd:PTZ00265 483 SLyslkDLEALSnyynedgndsqenknkrnscRAKCAGDLNDMSnttdsnELIEMRknyqtikdsevvdvskkvlihdfv 562
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 125 PALRDRY-------PHQLSGGQQQRVGVARALAANPQVLLMDEPFGALDPVTRGALQAEMTRIHRILGRTIVLVTHDIdE 197
Cdd:PTZ00265 563 SALPDKYetlvgsnASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAHRL-S 641
|
250
....*....|....*
gi 772671321 198 ALRLADHLVLMDHGE 212
Cdd:PTZ00265 642 TIRYANTIFVLSNRE 656
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
111-223 |
2.27e-09 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 58.10 E-value: 2.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 111 ADRVDELMALLGLEPALRDRYPHqLSGGQQQRVGVARALAANPQVLLMDEPFGALDPVTRGALQAEMTRIHRiLGRTIVL 190
Cdd:PRK10938 113 PARCEQLAQQFGITALLDRRFKY-LSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQ-SGITLVL 190
|
90 100 110
....*....|....*....|....*....|...
gi 772671321 191 VTHDIDEALRLADHLVLMDHGEVVQQGSPLELL 223
Cdd:PRK10938 191 VLNRFDEIPDFVQFAGVLADCTLAETGEREEIL 223
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
32-224 |
2.67e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 58.21 E-value: 2.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 32 LIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEIRSLPVLELRRRMGYAIQSIGLFPHwTVAQNiatvlqLEKWSRANIA 111
Cdd:PLN03130 1270 IVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSG-TVRFN------LDPFNEHNDA 1342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 112 DRVDelmallGLEPA-LRD---RYPHQL-----------SGGQQQRVGVARALAANPQVLLMDEPFGALDPVTRGALQ-- 174
Cdd:PLN03130 1343 DLWE------SLERAhLKDvirRNSLGLdaevseagenfSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDALIQkt 1416
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 772671321 175 -------AEMTRI-HRIlgRTIvlvthdIDealrlADHLVLMDHGEVVQQGSPLELLT 224
Cdd:PLN03130 1417 ireefksCTMLIIaHRL--NTI------ID-----CDRILVLDAGRVVEFDTPENLLS 1461
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
2-212 |
3.03e-09 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 57.67 E-value: 3.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 2 IEFLDVS-----KTFAGRPaashLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEIRSLPVLELRRR 76
Cdd:PRK10522 323 LELRNVTfayqdNGFSVGP----INLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKL 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 77 MGYAIQSIGLFPHWTVAQNI-ATVLQLEKW-SRANIADRV---DELMALLglepalrdryphQLSGGQQQRVGVARALAA 151
Cdd:PRK10522 399 FSAVFTDFHLFDQLLGPEGKpANPALVEKWlERLKMAHKLeleDGRISNL------------KLSKGQKKRLALLLALAE 466
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 772671321 152 NPQVLLMDEPFGALDPVTRGALQAEMTRIHRILGRTIVLVTHDiDEALRLADHLVLMDHGE 212
Cdd:PRK10522 467 ERDILLLDEWAADQDPHFRREFYQVLLPLLQEMGKTIFAISHD-DHYFIHADRLLEMRNGQ 526
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
15-223 |
3.05e-09 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 58.03 E-value: 3.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 15 PAASHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGeeirslpvlelrrrmgyaiqSIGLFPH--W-- 90
Cdd:TIGR00957 652 PTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKG--------------------SVAYVPQqaWiq 711
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 91 --TVAQNIATVLQL-EKWSRANIadRVDELMALLGLEPAlRDRYP-----HQLSGGQQQRVGVARALAANPQVLLMDEPF 162
Cdd:TIGR00957 712 ndSLRENILFGKALnEKYYQQVL--EACALLPDLEILPS-GDRTEigekgVNLSGGQKQRVSLARAVYSNADIYLFDDPL 788
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 772671321 163 GALDP-VTRGALQAEMTRIHRILGRTIVLVTHDIdEALRLADHLVLMDHGEVVQQGSPLELL 223
Cdd:TIGR00957 789 SAVDAhVGKHIFEHVIGPEGVLKNKTRILVTHGI-SYLPQVDVIIVMSGGKISEMGSYQELL 849
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
32-228 |
4.16e-09 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 57.65 E-value: 4.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 32 LIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEeirsLPVLELRRRMGYAIQ-SIGLFphwtVAQNIATVLQLEK------ 104
Cdd:PRK11147 34 LVGRNGAGKSTLMKILNGEVLLDDGRIIYEQD----LIVARLQQDPPRNVEgTVYDF----VAEGIEEQAEYLKryhdis 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 105 ------WSRANIA------------------DRVDELMALLGLEPalrDRYPHQLSGGQQQRVGVARALAANPQVLLMDE 160
Cdd:PRK11147 106 hlvetdPSEKNLNelaklqeqldhhnlwqleNRINEVLAQLGLDP---DAALSSLSGGWLRKAALGRALVSNPDVLLLDE 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 772671321 161 PFGALDPVTRGALQAEMtrihRILGRTIVLVTHDIDEALRLADHLVLMDHGEVVqqgsplellTWPKN 228
Cdd:PRK11147 183 PTNHLDIETIEWLEGFL----KTFQGSIIFISHDRSFIRNMATRIVDLDRGKLV---------SYPGN 237
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
7-194 |
5.71e-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: 56.87 E-value: 5.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 7 VSKTF-AGRPAASHLNLNFAEGAFSVLIGTSGSGKSTTLKmINRLVEHDsgmirFAGEEIRSLPVlelrrRMGYAIQSIG 85
Cdd:TIGR03719 10 VSKVVpPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLR-IMAGVDKD-----FNGEARPQPGI-----KVGYLPQEPQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 86 LFPHWTVAQNIATVLQLEKwsraNIADRVDELMALLGLEPA-----------LRDRYPHQ-------------------- 134
Cdd:TIGR03719 79 LDPTKTVRENVEEGVAEIK----DALDRFNEISAKYAEPDAdfdklaaeqaeLQEIIDAAdawdldsqleiamdalrcpp 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 772671321 135 -------LSGGQQQRVGVARALAANPQVLLMDEPFGALDPVTRGALQAEMtriHRILGrTIVLVTHD 194
Cdd:TIGR03719 155 wdadvtkLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHL---QEYPG-TVVAVTHD 217
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
32-202 |
6.07e-09 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 53.92 E-value: 6.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 32 LIGTSGSGKSTTLKMI-NRLVEHDSGMIRFAGEEIRSlpvlelrrrmgyaiqsiglfphwtvaqniatvlqlekwsrani 110
Cdd:smart00382 7 IVGPPGSGKTTLARALaRELGPPGGGVIYIDGEDILE------------------------------------------- 43
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 111 adrvdelMALLGLEPALRDRYPHQLSGGQQQRVGVARALAANPQVLLMDEPFGALDPVTRGALQAE-----MTRIHRILG 185
Cdd:smart00382 44 -------EVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLeelrlLLLLKSEKN 116
|
170
....*....|....*..
gi 772671321 186 RTIVLVTHDIDEALRLA 202
Cdd:smart00382 117 LTVILTTNDEKDLGPAL 133
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
85-213 |
6.84e-09 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 56.76 E-value: 6.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 85 GLFPHWTVAQNIaTVLQLEKWSRANIADRVDELMALLGLEPALRDRYPH------QLSGGQQQRVGVARALAANPQVLLM 158
Cdd:TIGR02633 349 GIVPILGVGKNI-TLSVLKSFCFKMRIDAAAELQIIGSAIQRLKVKTASpflpigRLSGGNQQKAVLAKMLLTNPRVLIL 427
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 772671321 159 DEPfgaldpvTRGALQAEMTRIHRIL------GRTIVLVTHDIDEALRLADHLVLMDHGEV 213
Cdd:TIGR02633 428 DEP-------TRGVDVGAKYEIYKLInqlaqeGVAIIVVSSELAEVLGLSDRVLVIGEGKL 481
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
121-223 |
9.47e-09 |
|
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: 56.56 E-value: 9.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 121 LGLEPALRDRYPHQLSGGQQQRVGVARALAAN-PQVL-LMDEPFGALDPVTRGALQAEMTRIhRILGRTIVLVTHDiDEA 198
Cdd:TIGR00630 475 VGLDYLSLSRAAGTLSGGEAQRIRLATQIGSGlTGVLyVLDEPSIGLHQRDNRRLINTLKRL-RDLGNTLIVVEHD-EDT 552
|
90 100 110
....*....|....*....|....*....|.
gi 772671321 199 LRLADHLVLM-----DHG-EVVQQGSPLELL 223
Cdd:TIGR00630 553 IRAADYVIDIgpgagEHGgEVVASGTPEEIL 583
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
22-208 |
1.92e-08 |
|
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: 52.75 E-value: 1.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 22 LNFAEGAFSVLIGTSGSGKSTTLKMInrlvehdsgmirfageeirslpvlelrrrmGYAiqsiglfphwTVAQNIATVLQ 101
Cdd:cd03227 16 VTFGEGSLTIITGPNGSGKSTILDAI------------------------------GLA----------LGGAQSATRRR 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 102 LEKWSRANIADRVDELMALLglepalrdrypHQLSGGQQQRVGVARALA----ANPQVLLMDEPFGALDPVTRGALqAEM 177
Cdd:cd03227 56 SGVKAGCIVAAVSAELIFTR-----------LQLSGGEKELSALALILAlaslKPRPLYILDEIDRGLDPRDGQAL-AEA 123
|
170 180 190
....*....|....*....|....*....|.
gi 772671321 178 TRIHRILGRTIVLVTHDiDEALRLADHLVLM 208
Cdd:cd03227 124 ILEHLVKGAQVIVITHL-PELAELADKLIHI 153
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
32-214 |
1.95e-08 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 55.30 E-value: 1.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 32 LIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEIRSlpvlelrRRMGYAIQS-----------IGLFPHWTVAQNI---- 96
Cdd:PRK11288 284 LFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDI-------RSPRDAIRAgimlcpedrkaEGIIPVHSVADNInisa 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 97 ------ATVLQLEKWSRANIADRVDELmallglepALRDRYPHQ----LSGGQQQRVGVARALAANPQVLLMDEPfgald 166
Cdd:PRK11288 357 rrhhlrAGCLINNRWEAENADRFIRSL--------NIKTPSREQlimnLSGGNQQKAILGRWLSEDMKVILLDEP----- 423
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 772671321 167 pvTRGALQAEMTRIHRIL------GRTIVLVTHDIDEALRLADHLVLMDHGEVV 214
Cdd:PRK11288 424 --TRGIDVGAKHEIYNVIyelaaqGVAVLFVSSDLPEVLGVADRIVVMREGRIA 475
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
135-213 |
2.00e-08 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 55.39 E-value: 2.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 135 LSGGQQQRVGVARALAANPQVLLMDEPfgaldpvTRGALQAEMTRIHRIL------GRTIVLVTHDIDEALRLADHLVLM 208
Cdd:PRK10762 396 LSGGNQQKVAIARGLMTRPKVLILDEP-------TRGVDVGAKKEIYQLInqfkaeGLSIILVSSEMPEVLGMSDRILVM 468
|
....*
gi 772671321 209 DHGEV 213
Cdd:PRK10762 469 HEGRI 473
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
26-212 |
4.69e-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: 54.02 E-value: 4.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 26 EGAFSVLIGTSGSGKSTTLKM-----------INRLVEHDSGMIRFAGEEIRSLpvleLRR------RMGYAIQSIGLFP 88
Cdd:COG1245 98 KGKVTGILGPNGIGKSTALKIlsgelkpnlgdYDEEPSWDEVLKRFRGTELQDY----FKKlangeiKVAHKPQYVDLIP 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 89 hwtvAQNIATVLQLEKwsRANIADRVDELMALLGLEPALrDRYPHQLSGGQQQRVGVARALAANPQVLLMDEPFGALDPV 168
Cdd:COG1245 174 ----KVFKGTVRELLE--KVDERGKLDELAEKLGLENIL-DRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIY 246
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 772671321 169 TRgalqAEMTRIHRIL---GRTIVLVTHDIdeAL--RLADHLVLMdHGE 212
Cdd:COG1245 247 QR----LNVARLIRELaeeGKYVLVVEHDL--AIldYLADYVHIL-YGE 288
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
27-211 |
5.34e-08 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 52.25 E-value: 5.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 27 GAFSVLIGTSGSGKSTTLKMI--NRLVEHDSGMIRFAGEEIRSlpvlELRRRMGYAIQSIGLFPHWTVAQniatVLQLEK 104
Cdd:cd03232 33 GTLTALMGESGAGKTTLLDVLagRKTAGVITGEILINGRPLDK----NFQRSTGYVEQQDVHSPNLTVRE----ALRFSA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 105 WSRAniadrvdelmallglepalrdryphqLSGGQQQRVGVARALAANPQVLLMDEPFGALDpvTRGALqAEMTRIHRIL 184
Cdd:cd03232 105 LLRG--------------------------LSVEQRKRLTIGVELAAKPSILFLDEPTSGLD--SQAAY-NIVRFLKKLA 155
|
170 180 190
....*....|....*....|....*....|
gi 772671321 185 --GRTIVLVTHDIDEAL-RLADHLVLMDHG 211
Cdd:cd03232 156 dsGQAILCTIHQPSASIfEKFDRLLLLKRG 185
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
2-173 |
7.32e-08 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 53.58 E-value: 7.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 2 IEFLDVSKTFAGRPAASHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFaGEEIrslpvlelrrRMGYAI 81
Cdd:PRK11819 325 IEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GETV----------KLAYVD 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 82 QS-IGLFPHWTVAQNI---ATVLQLEKW---SRANIA-------D---RVDelmallglepalrdryphQLSGGQQQRVG 144
Cdd:PRK11819 394 QSrDALDPNKTVWEEIsggLDIIKVGNReipSRAYVGrfnfkggDqqkKVG------------------VLSGGERNRLH 455
|
170 180
....*....|....*....|....*....
gi 772671321 145 VARALAANPQVLLMDEPFGALDPVTRGAL 173
Cdd:PRK11819 456 LAKTLKQGGNVLLLDEPTNDLDVETLRAL 484
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
27-218 |
1.07e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 53.19 E-value: 1.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 27 GAFSVLIGTSGSGKSTTLKMINRLVEH----DSGMIRFAG---EEIRSlpvlELRRRMGYAIQSIGLFPHWTVAQNIATV 99
Cdd:TIGR00956 87 GELTVVLGRPGSGCSTLLKTIASNTDGfhigVEGVITYDGitpEEIKK----HYRGDVVYNAETDVHFPHLTVGETLDFA 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 100 LQL-------EKWSRANIADRVDEL-MALLGL----EPALRDRYPHQLSGGQQQRVGVARALAANPQVLLMDEPFGALDP 167
Cdd:TIGR00956 163 ARCktpqnrpDGVSREEYAKHIADVyMATYGLshtrNTKVGNDFVRGVSGGERKRVSIAEASLGGAKIQCWDNATRGLDS 242
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 168 VTrgALQaemtrIHRILgRTIVLVTHDI---------DEALRLADHLVLMDHGEVVQQGS 218
Cdd:TIGR00956 243 AT--ALE-----FIRAL-KTSANILDTTplvaiyqcsQDAYELFDKVIVLYEGYQIYFGP 294
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
20-217 |
1.19e-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: 50.78 E-value: 1.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 20 LNLNFAEGAFSVLIGTSGSGKSTTLKMInrLVEHDSGMIrfageeIRSLPVLelrrrmgyaiqsiglFPHWTVaqniatv 99
Cdd:cd03238 14 LDVSIPLNVLVVVTGVSGSGKSTLVNEG--LYASGKARL------ISFLPKF---------------SRNKLI------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 100 lqlekwsraniadRVDELMAL--LGLEPALRDRYPHQLSGGQQQRVGVARALAANPQ--VLLMDEPFGALDPVTRGALQA 175
Cdd:cd03238 64 -------------FIDQLQFLidVGLGYLTLGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLE 130
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 772671321 176 EMTRIhRILGRTIVLVTHDiDEALRLADHLVLMDH------GEVVQQG 217
Cdd:cd03238 131 VIKGL-IDLGNTVILIEHN-LDVLSSADWIIDFGPgsgksgGKVVFSG 176
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
20-193 |
2.45e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 50.26 E-value: 2.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 20 LNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEIRSLPvlelRRRMGYAIQSIGLFPHWTVAQNiatv 99
Cdd:PRK13541 19 LSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIA----KPYCTYIGHNLGLKLEMTVFEN---- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 100 lqLEKWSRA-NIADRVDELMALLGLEPALrDRYPHQLSGGQQQRVGVARALAANPQVLLMDEPFGALDPVTRgALQAEMT 178
Cdd:PRK13541 91 --LKFWSEIyNSAETLYAAIHYFKLHDLL-DEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENR-DLLNNLI 166
|
170
....*....|....*
gi 772671321 179 RIHRILGRTIVLVTH 193
Cdd:PRK13541 167 VMKANSGGIVLLSSH 181
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
32-195 |
3.70e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 51.35 E-value: 3.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 32 LIGTSGSGKSTTLK-----MINRLVEHDSG------MIRFAGEEI----RSLPVLELRrrMGYAIQSIGLFPhwtvAQNI 96
Cdd:PRK13409 104 ILGPNGIGKTTAVKilsgeLIPNLGDYEEEpswdevLKRFRGTELqnyfKKLYNGEIK--VVHKPQYVDLIP----KVFK 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 97 ATVLQLEKwsRANIADRVDELMALLGLEPALrDRYPHQLSGGQQQRVGVARALAANPQVLLMDEPFGALDPVTRgalqAE 176
Cdd:PRK13409 178 GKVRELLK--KVDERGKLDEVVERLGLENIL-DRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRQR----LN 250
|
170 180
....*....|....*....|.
gi 772671321 177 MTRIHRIL--GRTIVLVTHDI 195
Cdd:PRK13409 251 VARLIRELaeGKYVLVVEHDL 271
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
14-204 |
6.65e-07 |
|
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: 49.14 E-value: 6.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 14 RPAASHLNLNFAEGaFSVLIGTSGSGKSTTLKMI-----------NRLVEHDSGMIRfAGEEIRSLPvLELRRRMG---Y 79
Cdd:cd03240 10 RSFHERSEIEFFSP-LTLIVGQNGAGKTTIIEALkyaltgelppnSKGGAHDPKLIR-EGEVRAQVK-LAFENANGkkyT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 80 AIQSIGLFphwtvaQNIATVLQlekwsraniadrvDELMALLGLEpalRDRyphqLSGGQQQ------RVGVARALAANP 153
Cdd:cd03240 87 ITRSLAIL------ENVIFCHQ-------------GESNWPLLDM---RGR----CSGGEKVlasliiRLALAETFGSNC 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 772671321 154 QVLLMDEPFGALDPVTR-GALQAEMTRIHRILGRTIVLVTHDiDEALRLADH 204
Cdd:cd03240 141 GILALDEPTTNLDEENIeESLAEIIEERKSQKNFQLIVITHD-EELVDAADH 191
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
33-195 |
6.79e-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: 50.55 E-value: 6.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 33 IGTSGSGKSTTLKMINRLVEHDSGmirfageeirslpVLELRRRMGYAIQSIGLFPHWTVAQNIatvlqlekwsRANIAD 112
Cdd:COG1245 372 VGPNGIGKTTFAKILAGVLKPDEG-------------EVDEDLKISYKPQYISPDYDGTVEEFL----------RSANTD 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 113 RVD------ELMALLGLEPaLRDRYPHQLSGGQQQRVGVARALAANPQVLLMDEPFGALDPVTRGALQAEMTRIHRILGR 186
Cdd:COG1245 429 DFGssyyktEIIKPLGLEK-LLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAENRGK 507
|
....*....
gi 772671321 187 TIVLVTHDI 195
Cdd:COG1245 508 TAMVVDHDI 516
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
2-214 |
2.74e-06 |
|
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: 48.64 E-value: 2.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 2 IEFLDVSKTFAGRPAASH-----LNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAGEEIRSLPVLELRRR 76
Cdd:COG4615 328 LELRGVTYRYPGEDGDEGftlgpIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAYRQL 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 77 MGyAIQSIG-LFPHwtvaqniatVLQLEKwsrANIADRVDELMALLGLE--PALRDRY--PHQLSGGQQQRVGVARALAA 151
Cdd:COG4615 408 FS-AVFSDFhLFDR---------LLGLDG---EADPARARELLERLELDhkVSVEDGRfsTTDLSQGQRKRLALLVALLE 474
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 772671321 152 NPQVLLMDEpFGA-LDPVTRgalqaemtRI--HRIL------GRTIVLVTHDiDEALRLADHLVLMDHGEVV 214
Cdd:COG4615 475 DRPILVFDE-WAAdQDPEFR--------RVfyTELLpelkarGKTVIAISHD-DRYFDLADRVLKMDYGKLV 536
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
33-195 |
4.25e-06 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 48.27 E-value: 4.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 33 IGTSGSGKSTTLKMINRLVEHDSGMIrfageeirslpvlELRRRMGYAIQSIGLFPHWTVAQNIAtvlqlekwsraNIAD 112
Cdd:PRK13409 371 VGPNGIGKTTFAKLLAGVLKPDEGEV-------------DPELKISYKPQYIKPDYDGTVEDLLR-----------SITD 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 113 RVD------ELMALLGLEPaLRDRYPHQLSGGQQQRVGVARALAANPQVLLMDEPFGALDPVTRgaLQAemTR-IHRIL- 184
Cdd:PRK13409 427 DLGssyyksEIIKPLQLER-LLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQR--LAV--AKaIRRIAe 501
|
170
....*....|...
gi 772671321 185 --GRTIVLVTHDI 195
Cdd:PRK13409 502 erEATALVVDHDI 514
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
27-211 |
5.57e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 48.18 E-value: 5.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 27 GAFSVLIGTSGSGKSTTLkmiNRLVEHDSGMIRFAGEEIRSLPVLE--LRRRMGYAIQSIGLFPHWTVAQNI---ATVLQ 101
Cdd:TIGR00956 789 GTLTALMGASGAGKTTLL---NVLAERVTTGVITGGDRLVNGRPLDssFQRSIGYVQQQDLHLPTSTVRESLrfsAYLRQ 865
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 102 LEKWSRANIADRVDELMALLGLEP---ALRDRYPHQLSGGQQQRVGVARALAANPQVLL-MDEPFGALDPVTrgalQAEM 177
Cdd:TIGR00956 866 PKSVSKSEKMEYVEEVIKLLEMESyadAVVGVPGEGLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLDSQT----AWSI 941
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 772671321 178 TRIHRIL---GRTIVLVTH----DIDEALrlaDHLVLMDHG 211
Cdd:TIGR00956 942 CKLMRKLadhGQAILCTIHqpsaILFEEF---DRLLLLQKG 979
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
34-167 |
5.82e-06 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 46.38 E-value: 5.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 34 GTSGSGKSTTLKMINRLVEHDSGMIRFAGEEIRSLpvlELRRRMGYAIQSIGLFPHWTVAQNIATVLQLEKWSRANIADR 113
Cdd:PRK13543 44 GDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRG---DRSRFMAYLGHLPGLKADLSTLENLHFLCGLHGRRAKQMPGS 120
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 772671321 114 VDELMALLGLEPALrdryPHQLSGGQQQRVGVARALAANPQVLLMDEPFGALDP 167
Cdd:PRK13543 121 ALAIVGLAGYEDTL----VRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDL 170
|
|
| CBS |
COG0517 |
CBS domain [Signal transduction mechanisms]; |
179-306 |
1.51e-05 |
|
CBS domain [Signal transduction mechanisms];
Pssm-ID: 440283 [Multi-domain] Cd Length: 128 Bit Score: 43.70 E-value: 1.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 179 RIHRILGRTIVLVTHD--IDEALRL-ADH-----LVLMDHGEVVqqGspleLLTwpKNDFVREFFGRselGVRLLSlRTV 250
Cdd:COG0517 2 KVKDIMTTDVVTVSPDatVREALELmSEKrigglPVVDEDGKLV--G----IVT--DRDLRRALAAE---GKDLLD-TPV 69
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 772671321 251 SDYMRREemPVSGEPlqeQMSLRDALSAFVARQCEVLPVSDARGAPCGTLHFRDLL 306
Cdd:COG0517 70 SEVMTRP--PVTVSP---DTSLEEAAELMEEHKIRRLPVVDDDGRLVGIITIKDLL 120
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
121-223 |
1.90e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 46.36 E-value: 1.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 121 LGLEPALRDRYPHQLSGGQQQRVGVARALAANPQ--VLLMDEPFGALDPVTRGALQAEMTRIhRILGRTIVLVTHDiDEA 198
Cdd:PRK00635 463 LGLPYLTPERALATLSGGEQERTALAKHLGAELIgiTYILDEPSIGLHPQDTHKLINVIKKL-RDQGNTVLLVEHD-EQM 540
|
90 100 110
....*....|....*....|....*....|.
gi 772671321 199 LRLADHLVLMD------HGEVVQQGSPLELL 223
Cdd:PRK00635 541 ISLADRIIDIGpgagifGGEVLFNGSPREFL 571
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
7-194 |
3.75e-05 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 45.11 E-value: 3.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 7 VSKTF-AGRPAASHLNLNFAEGAFSVLIGTSGSGKSTTLKmINRLVEHDsgmirFAGEEIRSLPVlelrrRMGYAIQSIG 85
Cdd:PRK11819 12 VSKVVpPKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLR-IMAGVDKE-----FEGEARPAPGI-----KVGYLPQEPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 86 LFPHWTVAQNIATVLQlEKwsrANIADRVDELMALLGLEPALRD--------------------------------RYPH 133
Cdd:PRK11819 81 LDPEKTVRENVEEGVA-EV---KAALDRFNEIYAAYAEPDADFDalaaeqgelqeiidaadawdldsqleiamdalRCPP 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 772671321 134 ------QLSGGQQQRVGVARALAANPQVLLMDEPFGALDpvtrgalqAEMTR-----IHRILGrTIVLVTHD 194
Cdd:PRK11819 157 wdakvtKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLD--------AESVAwleqfLHDYPG-TVVAVTHD 219
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
135-213 |
5.62e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 44.34 E-value: 5.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 135 LSGGQQQRVGVARALAANPQVLLMDEPfgaldpvTRGALQAEMTRIHRIL------GRTIVLVTHDIDEALRLADHLVLM 208
Cdd:PRK10982 392 LSGGNQQKVIIGRWLLTQPEILMLDEP-------TRGIDVGAKFEIYQLIaelakkDKGIIIISSEMPELLGITDRILVM 464
|
....*
gi 772671321 209 DHGEV 213
Cdd:PRK10982 465 SNGLV 469
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
115-207 |
7.92e-05 |
|
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: 42.56 E-value: 7.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 115 DELMALLGLEPALRDRYPhQLSGGQQQRVGVARALAANPQVLLMDEPFGALDPVTRGALQAEMTRIHRILGRTIVLVTHD 194
Cdd:cd03222 53 GDNDEWDGITPVYKPQYI-DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTALVVEHD 131
|
90
....*....|...
gi 772671321 195 IDEALRLADHLVL 207
Cdd:cd03222 132 LAVLDYLSDRIHV 144
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
1-166 |
1.00e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 44.08 E-value: 1.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 1 MIEFLDVSKTFAGRPAASHlNLNFAEGAFS--VLIGTSGSGKSTTLKMINRLVEHDSGMI------RFA--------GEE 64
Cdd:PLN03073 508 IISFSDASFGYPGGPLLFK-NLNFGIDLDSriAMVGPNGIGKSTILKLISGELQPSSGTVfrsakvRMAvfsqhhvdGLD 586
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 65 IRSLPVLELRRrmgyaiqsigLFPHwtvaqniatvlQLEKWSRANIADrvdelmalLGLEPALRDRYPHQLSGGQQQRVG 144
Cdd:PLN03073 587 LSSNPLLYMMR----------CFPG-----------VPEQKLRAHLGS--------FGVTGNLALQPMYTLSGGQKSRVA 637
|
170 180
....*....|....*....|..
gi 772671321 145 VARALAANPQVLLMDEPFGALD 166
Cdd:PLN03073 638 FAKITFKKPHILLLDEPSNHLD 659
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
6-166 |
1.15e-04 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 43.73 E-value: 1.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 6 DVSKTFAGRPAASHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEHDSGMIRFAgEEIrslpvlelrrrmgyaiqSIG 85
Cdd:PRK15064 324 NLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWS-ENA-----------------NIG 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 86 LFPHwTVAQNIATVLQLEKWSRANIADRVDELM--ALLGlepalR--------DRYPHQLSGGQQQRVGVARALAANPQV 155
Cdd:PRK15064 386 YYAQ-DHAYDFENDLTLFDWMSQWRQEGDDEQAvrGTLG-----RllfsqddiKKSVKVLSGGEKGRMLFGKLMMQKPNV 459
|
170
....*....|.
gi 772671321 156 LLMDEPFGALD 166
Cdd:PRK15064 460 LVMDEPTNHMD 470
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
113-166 |
1.41e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 43.31 E-value: 1.41e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 772671321 113 RVDELMALLGLEPALRDRYPHQLSGGQQQRVGVARALAANPQVLLMDEPFGALD 166
Cdd:PLN03073 323 RAASILAGLSFTPEMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLD 376
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
135-222 |
1.59e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 43.46 E-value: 1.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 135 LSGGQQQRVGVARAL---AANPQVLLMDEPfgaldpvTRGaLQAE-----MTRIHRI--LGRTIVLVTHDIDeALRLADH 204
Cdd:TIGR00630 830 LSGGEAQRIKLAKELskrSTGRTLYILDEP-------TTG-LHFDdikklLEVLQRLvdKGNTVVVIEHNLD-VIKTADY 900
|
90 100
....*....|....*....|....
gi 772671321 205 LVLM-----DH-GEVVQQGSPLEL 222
Cdd:TIGR00630 901 IIDLgpeggDGgGTVVASGTPEEV 924
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
91-171 |
2.57e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 42.47 E-value: 2.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 91 TVAQNIaTVLQLEKWSRANIADRVDELMALLGLEPALRDRYPH------QLSGGQQQRVGVARALAANPQVLLMDEPfga 164
Cdd:NF040905 356 DIKRNI-TLANLGKVSRRGVIDENEEIKVAEEYRKKMNIKTPSvfqkvgNLSGGNQQKVVLSKWLFTDPDVLILDEP--- 431
|
....*..
gi 772671321 165 ldpvTRG 171
Cdd:NF040905 432 ----TRG 434
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
182-227 |
3.38e-04 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 42.37 E-value: 3.38e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 772671321 182 RILGRTIVLVTHDiDEALRLADHLVLM-----DHG-EVVQQGSPLELLTWPK 227
Cdd:PRK00349 538 RDLGNTLIVVEHD-EDTIRAADYIVDIgpgagVHGgEVVASGTPEEIMKNPN 588
|
|
| COG2524 |
COG2524 |
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription]; |
179-306 |
4.21e-04 |
|
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];
Pssm-ID: 442013 [Multi-domain] Cd Length: 206 Bit Score: 40.64 E-value: 4.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 179 RIHRILGRTIVLVTHD--IDEALRLadhlvLMDHGE----VVQQGSPLELLTwpKNDFVREFFGRSELGVRllslrTVSD 252
Cdd:COG2524 87 KVKDIMTKDVITVSPDttLEEALEL-----MLEKGIsglpVVDDGKLVGIIT--ERDLLKALAEGRDLLDA-----PVSD 154
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 772671321 253 YMRREemPVSgepLQEQMSLRDALSAFVARQCEVLPVSDARGAPCGTLHFRDLL 306
Cdd:COG2524 155 IMTRD--VVT---VSEDDSLEEALRLMLEHGIGRLPVVDDDGKLVGIITRTDIL 203
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
1-217 |
6.15e-04 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 40.54 E-value: 6.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 1 MIEFLDVSKTFAGRPAASHLNLNFAEGAFSVLIGTSGSGKSTTLKMINRLVEH--DSGMIRFAGEEIRSlpvLELRRRMG 78
Cdd:PRK09580 1 MLSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDYevTGGTVEFKGKDLLE---LSPEDRAG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 79 --------YAIQSIGLFPHW---TVAQNIATVLQLEKWSRANIADRVDELMALLGLEPALRDRYPHQ-LSGGQQQRVGVA 146
Cdd:PRK09580 78 egifmafqYPVEIPGVSNQFflqTALNAVRSYRGQEPLDRFDFQDLMEEKIALLKMPEDLLTRSVNVgFSGGEKKRNDIL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 772671321 147 RALAANPQVLLMDEPFGALDpVTRGALQAEMTRIHRILGRTIVLVTHdideALRLADHlVLMDHGEVVQQG 217
Cdd:PRK09580 158 QMAVLEPELCILDESDSGLD-IDALKIVADGVNSLRDGKRSFIIVTH----YQRILDY-IKPDYVHVLYQG 222
|
|
| COG2905 |
COG2905 |
Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains ... |
180-306 |
6.80e-04 |
|
Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains [Signal transduction mechanisms];
Pssm-ID: 442149 [Multi-domain] Cd Length: 124 Bit Score: 39.04 E-value: 6.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 180 IHRILGRTIVLVTHD--IDEALRL-----ADHLVLMDHgevvqQGSPLELLTwpKNDFVREFFGRselGVRLLSLrTVSD 252
Cdd:COG2905 1 VKDIMSRDVVTVSPDatVREAARLmtekgVGSLVVVDD-----DGRLVGIIT--DRDLRRRVLAE---GLDPLDT-PVSE 69
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 772671321 253 YMRREemPVSgepLQEQMSLRDALSAFVARQCEVLPVSDArGAPCGTLHFRDLL 306
Cdd:COG2905 70 VMTRP--PIT---VSPDDSLAEALELMEEHRIRHLPVVDD-GKLVGIVSITDLL 117
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
14-195 |
9.91e-04 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 39.61 E-value: 9.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 14 RPAASHLNLNFAEGAFsVLIGTSGSGKSTTL---------------KMINRLVEHDS--GMIRF----AGEEIRslpvle 72
Cdd:COG0419 11 RSYRDTETIDFDDGLN-LIVGPNGAGKSTILeairyalygkarsrsKLRSDLINVGSeeASVELefehGGKRYR------ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 73 LRRRMGYAIQSIGLFPHwTVAQNIATVLQLEKWSRA---------NIADRVDELMALLGLEPALRDRY-----PHQLSGG 138
Cdd:COG0419 84 IERRQGEFAEFLEAKPS-ERKEALKRLLGLEIYEELkerlkeleeALESALEELAELQKLKQEILAQLsgldpIETLSGG 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 772671321 139 QQQRVGVARALAanpqvLLMDepFGALDPVTRGALQAEMtrihrilgRTIVLVTHDI 195
Cdd:COG0419 163 ERLRLALADLLS-----LILD--FGSLDEERLERLLDAL--------EELAIITHVI 204
|
|
| CBS |
pfam00571 |
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ... |
250-306 |
9.93e-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: 36.81 E-value: 9.93e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 772671321 250 VSDYMRREEMPVSgeplqEQMSLRDALSAFVARQCEVLPVSDARGAPCGTLHFRDLL 306
Cdd:pfam00571 1 VKDIMTKDVVTVS-----PDTTLEEALELMREHGISRLPVVDEDGKLVGIVTLKDLL 52
|
|
| COG3448 |
COG3448 |
CBS-domain-containing membrane protein [Signal transduction mechanisms]; |
177-307 |
1.26e-03 |
|
CBS-domain-containing membrane protein [Signal transduction mechanisms];
Pssm-ID: 442671 [Multi-domain] Cd Length: 136 Bit Score: 38.31 E-value: 1.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 177 MTRIHRILGRTIVLVTHD--IDEALRL-ADH-----LVLMDHGEVVqqGspleLLTwpKNDFVREFFGRSELGV-RLLSL 247
Cdd:COG3448 1 AMTVRDIMTRDVVTVSPDttLREALELmREHgirglPVVDEDGRLV--G----IVT--ERDLLRALLPDRLDELeERLLD 72
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 248 RTVSDYMRREEMPVSgeplqEQMSLRDALSAFVARQCEVLPVSDARGAPCGTLHFRDLLA 307
Cdd:COG3448 73 LPVEDVMTRPVVTVT-----PDTPLEEAAELMLEHGIHRLPVVDDDGRLVGIVTRTDLLR 127
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
135-223 |
1.76e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 40.01 E-value: 1.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 135 LSGGQQQRVGVARALAANpqvlLM------DEPfgaldpvTRGALQAEMTRIHRIL------GRTIVLVTHDiDEALRLA 202
Cdd:COG0178 486 LSGGEAQRIRLATQIGSG----LVgvlyvlDEP-------SIGLHQRDNDRLIETLkrlrdlGNTVIVVEHD-EDTIRAA 553
|
90 100
....*....|....*....|....*..
gi 772671321 203 DHLVLM-----DH-GEVVQQGSPLELL 223
Cdd:COG0178 554 DYIIDIgpgagEHgGEVVAQGTPEEIL 580
|
|
| CBS_pair_SF |
cd02205 |
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ... |
187-307 |
3.30e-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: 36.84 E-value: 3.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 187 TIVLVTHDIDEALRL-ADH-----LVLMDHGEVVqqGspleLLTwpKNDFVREFFGRselgvRLLSLRTVSDYMRREemP 260
Cdd:cd02205 5 VTVDPDTTVREALELmAENgigalPVVDDDGKLV--G----IVT--ERDILRALVEG-----GLALDTPVAEVMTPD--V 69
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 772671321 261 VSgepLQEQMSLRDALSAFVARQCEVLPVSDARGAPCGTLHFRDLLA 307
Cdd:cd02205 70 IT---VSPDTDLEEALELMLEHGIRRLPVVDDDGKLVGIVTRRDILR 113
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
135-219 |
5.67e-03 |
|
ATP-binding cassette domain II 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: 213238 [Multi-domain] Cd Length: 261 Bit Score: 37.59 E-value: 5.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772671321 135 LSGGQQQRVGVARAL---AANPQVLLMDEPFGALDPvtrGALQAEMTRIHRI--LGRTIVLVTHDIDeALRLADHLVLM- 208
Cdd:cd03271 170 LSGGEAQRIKLAKELskrSTGKTLYILDEPTTGLHF---HDVKKLLEVLQRLvdKGNTVVVIEHNLD-VIKCADWIIDLg 245
|
90
....*....|....*.
gi 772671321 209 ----DH-GEVVQQGSP 219
Cdd:cd03271 246 peggDGgGQVVASGTP 261
|
|
| |
