|
Name |
Accession |
Description |
Interval |
E-value |
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
8-343 |
2.79e-174 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 486.14 E-value: 2.79e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 8 IEFKSVFKTYGDNTV-VDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGEDNTARPAHELRRSMGYV 86
Cdd:COG1125 2 IEFENVTKRYPDGTVaVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRDLDPVELRRRIGYV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 87 LQQAGLMPHRTIVDNISTVPRLNGVSARQAKSQALELLNTVGLD-ESFAKRYPSQLSGGQAQRVGVARALASESSILLMD 165
Cdd:COG1125 82 IQQIGLFPHMTVAENIATVPRLLGWDKERIRARVDELLELVGLDpEEYRDRYPHELSGGQQQRVGVARALAADPPILLMD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 166 EPFSAVDPVVRADLQKELLRLQSTLGRTIIFVTHDMDEAILLGDYVAVFaRGGRIAQFGTPEEILREPADDFVASFVGRD 245
Cdd:COG1125 162 EPFGALDPITREQLQDELLRLQRELGKTIVFVTHDIDEALKLGDRIAVM-REGRIVQYDTPEEILANPANDFVADFVGAD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 246 RGMRRLTFASGADVPIHPLDAqqtpwqqwqlnvedgrpagwriddrvipggslFVAGGTLRDALDSVLSSPSGWGVAVNE 325
Cdd:COG1125 241 RGLRRLSLLRVEDLMLPEPPT--------------------------------VSPDASLREALSLMLERGVDWLLVVDE 288
|
330
....*....|....*...
gi 2735597802 326 QGQVLGLLKSDDVLEATE 343
Cdd:COG1125 289 DGRPLGWLTLEDLLRALA 306
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
8-246 |
2.53e-130 |
|
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: 372.40 E-value: 2.53e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 8 IEFKSVFKTYGDNT-VVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGEDNTARPAHELRRSMGYV 86
Cdd:cd03295 1 IEFENVTKRYGGGKkAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 87 LQQAGLMPHRTIVDNISTVPRLNGVSARQAKSQALELLNTVGLDE-SFAKRYPSQLSGGQAQRVGVARALASESSILLMD 165
Cdd:cd03295 81 IQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLDPaEFADRYPHELSGGQQQRVGVARALAADPPLLLMD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 166 EPFSAVDPVVRADLQKELLRLQSTLGRTIIFVTHDMDEAILLGDYVAVFaRGGRIAQFGTPEEILREPADDFVASFVGRD 245
Cdd:cd03295 161 EPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIM-KNGEIVQVGTPDEILRSPANDFVAEFVGAD 239
|
.
gi 2735597802 246 R 246
Cdd:cd03295 240 R 240
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
7-341 |
2.05e-102 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 306.64 E-value: 2.05e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 7 AIEFKSVFKTYGDN-----------------------TV-VDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSG 62
Cdd:COG4175 3 KIEVRNLYKIFGKRperalklldqgkskdeilektgqTVgVNDASFDVEEGEIFVIMGLSGSGKSTLVRCLNRLIEPTAG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 63 TILVNGEDNTARPAHEL----RRSMGYVLQQAGLMPHRTIVDNISTVPRLNGVSARQAKSQALELLNTVGLDEsFAKRYP 138
Cdd:COG4175 83 EVLIDGEDITKLSKKELrelrRKKMSMVFQHFALLPHRTVLENVAFGLEIQGVPKAERRERAREALELVGLAG-WEDSYP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 139 SQLSGGQAQRVGVARALASESSILLMDEPFSAVDPVVRADLQKELLRLQSTLGRTIIFVTHDMDEAILLGDYVAVFaRGG 218
Cdd:COG4175 162 DELSGGMQQRVGLARALATDPDILLMDEAFSALDPLIRREMQDELLELQAKLKKTIVFITHDLDEALRLGDRIAIM-KDG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 219 RIAQFGTPEEILREPADDFVASFV-GRDRG--------MRRL-TFASGADVPIHPLDAQQTPWQQWQLNV-EDGRPAGWR 287
Cdd:COG4175 241 RIVQIGTPEEILTNPANDYVADFVeDVDRSkvltagsvMRPPeAVVSEKDGPRVALRRMREEGISSLYVVdRDRRLLGVV 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2735597802 288 IDDRV-------------IPGGSLFVAGGT-LRDALDSVLSSPsgWGVAV-NEQGQVLGLLKSDDVLEA 341
Cdd:COG4175 321 TADDAleavkgekdleeiLLTDVPTVSPDTpLRDLLPLVAESP--YPLAVvDEDGRLLGVISRGSLLAA 387
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
7-244 |
7.07e-101 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 301.63 E-value: 7.07e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 7 AIEFKSVFKTYGDNTVVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGEDNTARPAHelRRSMGYV 86
Cdd:COG3842 5 ALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPE--KRNVGMV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 87 LQQAGLMPHRTIVDNISTVPRLNGVSARQAKSQALELLNTVGLDEsFAKRYPSQLSGGQAQRVGVARALASESSILLMDE 166
Cdd:COG3842 83 FQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEG-LADRYPHQLSGGQQQRVALARALAPEPRVLLLDE 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2735597802 167 PFSAVDPVVRADLQKELLRLQSTLGRTIIFVTHDMDEAILLGDYVAVFaRGGRIAQFGTPEEILREPADDFVASFVGR 244
Cdd:COG3842 162 PLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVM-NDGRIEQVGTPEEIYERPATRFVADFIGE 238
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
15-325 |
1.16e-93 |
|
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Functionally, this transport system is involved in osmoregulation. Under conditions of stress, the organism recruits these transport system to accumulate glycine betaine and other solutes which offer osmo-protection. It has been demonstrated that glycine betaine uptake is accompanied by symport with sodium ions. The locus has been named variously as proU or opuA. A gene library from L.lactis functionally complements an E.coli proU mutant. The comlementing locus is similar to a opuA locus in B.sutlis. This clarifies the differences in nomenclature. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 130254 [Multi-domain] Cd Length: 363 Bit Score: 283.67 E-value: 1.16e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 15 KTYGDNTVVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGEDNTARPAHEL----RRSMGYVLQQA 90
Cdd:TIGR01186 1 KKTGGKKGVNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEPTAGQIFIDGENIMKQSPVELrevrRKKIGMVFQQF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 91 GLMPHRTIVDNISTVPRLNGVSARQAKSQALELLNTVGLdESFAKRYPSQLSGGQAQRVGVARALASESSILLMDEPFSA 170
Cdd:TIGR01186 81 ALFPHMTILQNTSLGPELLGWPEQERKEKALELLKLVGL-EEYEHRYPDELSGGMQQRVGLARALAAEPDILLMDEAFSA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 171 VDPVVRADLQKELLRLQSTLGRTIIFVTHDMDEAILLGDYVAVFaRGGRIAQFGTPEEILREPADDFVASFVGRDRGMRR 250
Cdd:TIGR01186 160 LDPLIRDSMQDELKKLQATLQKTIVFITHDLDEAIRIGDRIVIM-KAGEIVQVGTPDEILRNPANEYVEEFIGKVDLSQV 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2735597802 251 LTFASGA----DVPIhPLDAQQTPWQQWQLNVEDGRPAGWRIDDRVIPGGSLFVaggtlrDALDSVLSSPSGWGVAVNE 325
Cdd:TIGR01186 239 FDAERIAqrmnTGPI-TKTADKGPRSALQLMRDERVDSLYVVDRQNKLVGVVDV------ESIKQARKKAQGLQDVLID 310
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
13-242 |
4.13e-93 |
|
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: 278.76 E-value: 4.13e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 13 VFKTYGDNTVVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGEDNTARPAHEL----RRSMGYVLQ 88
Cdd:cd03294 30 ILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELrelrRKKISMVFQ 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 89 QAGLMPHRTIVDNISTVPRLNGVSARQAKSQALELLNTVGLdESFAKRYPSQLSGGQAQRVGVARALASESSILLMDEPF 168
Cdd:cd03294 110 SFALLPHRTVLENVAFGLEVQGVPRAEREERAAEALELVGL-EGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAF 188
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2735597802 169 SAVDPVVRADLQKELLRLQSTLGRTIIFVTHDMDEAILLGDYVAVFaRGGRIAQFGTPEEILREPADDFVASFV 242
Cdd:cd03294 189 SALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIM-KDGRLVQVGTPEEILTNPANDYVREFF 261
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-221 |
7.56e-92 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 275.04 E-value: 7.56e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 1 MSVLNNAIEFKSVFKTY----GDNTVVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGedntaRPA 76
Cdd:COG1116 1 MSAAAPALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDG-----KPV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 77 HELRRSMGYVLQQAGLMPHRTIVDNISTVPRLNGVSARQAKSQALELLNTVGLDEsFAKRYPSQLSGGQAQRVGVARALA 156
Cdd:COG1116 76 TGPGPDRGVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAG-FEDAYPHQLSGGMRQRVAIARALA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2735597802 157 SESSILLMDEPFSAVDPVVRADLQKELLRLQSTLGRTIIFVTHDMDEAILLGDYVAVF-ARGGRIA 221
Cdd:COG1116 155 NDPEVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFLADRVVVLsARPGRIV 220
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
8-222 |
1.43e-88 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 265.49 E-value: 1.43e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 8 IEFKSVFKTYGDN----TVVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGEdntarPAHELRRSM 83
Cdd:cd03293 1 LEVRNVSKTYGGGggavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGE-----PVTGPGPDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 84 GYVLQQAGLMPHRTIVDNISTVPRLNGVSARQAKSQALELLNTVGLDEsFAKRYPSQLSGGQAQRVGVARALASESSILL 163
Cdd:cd03293 76 GYVFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSG-FENAYPHQLSGGMRQRVALARALAVDPDVLL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 164 MDEPFSAVDPVVRADLQKELLRLQSTLGRTIIFVTHDMDEAILLGDYVAVF-ARGGRIAQ 222
Cdd:cd03293 155 LDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLsARPGRIVA 214
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1-243 |
1.10e-87 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 267.78 E-value: 1.10e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 1 MSvlnnaIEFKSVFKTYGDNTVVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGED-NTARPAHEl 79
Cdd:COG1118 1 MS-----IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDlFTNLPPRE- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 80 rRSMGYVLQQAGLMPHRTIVDNISTVPRLNGVSARQAKSQALELLNTVGLDEsFAKRYPSQLSGGQAQRVGVARALASES 159
Cdd:COG1118 75 -RRVGFVFQHYALFPHMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEG-LADRYPSQLSGGQRQRVALARALAVEP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 160 SILLMDEPFSAVDPVVRADLQKELLRLQSTLGRTIIFVTHDMDEAILLGDYVAVFaRGGRIAQFGTPEEILREPADDFVA 239
Cdd:COG1118 153 EVLLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVM-NQGRIEQVGTPDEVYDRPATPFVA 231
|
....
gi 2735597802 240 SFVG 243
Cdd:COG1118 232 RFLG 235
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
7-243 |
6.71e-85 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 260.78 E-value: 6.71e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 7 AIEFKSVFKTYGDNTVVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGEDNTARPAHElrRSMGYV 86
Cdd:COG3839 3 SLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKD--RNIAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 87 LQQAGLMPHRTIVDNISTVPRLNGVSARQAKSQALELLNTVGLDEsFAKRYPSQLSGGQAQRVGVARALASESSILLMDE 166
Cdd:COG3839 81 FQSYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLED-LLDRKPKQLSGGQRQRVALGRALVREPKVFLLDE 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2735597802 167 PFSAVDPVVRADLQKELLRLQSTLGRTIIFVTHDMDEAILLGDYVAVFaRGGRIAQFGTPEEILREPADDFVASFVG 243
Cdd:COG3839 160 PLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVM-NDGRIQQVGTPEELYDRPANLFVAGFIG 235
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
8-243 |
1.55e-84 |
|
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: 255.62 E-value: 1.55e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 8 IEFKSVFKTYGDNTVVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGEDNTARPAHelRRSMGYVL 87
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPH--KRPVNTVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 88 QQAGLMPHRTIVDNISTVPRLNGVSARQAKSQALELLNTVGLDEsFAKRYPSQLSGGQAQRVGVARALASESSILLMDEP 167
Cdd:cd03300 79 QNYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEG-YANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEP 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2735597802 168 FSAVDPVVRADLQKELLRLQSTLGRTIIFVTHDMDEAILLGDYVAVFaRGGRIAQFGTPEEILREPADDFVASFVG 243
Cdd:cd03300 158 LGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVM-NKGKIQQIGTPEEIYEEPANRFVADFIG 232
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
8-224 |
1.32e-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: 252.44 E-value: 1.32e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 8 IEFKSVFKTYGDNTVVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGEDNTARPAHelRRSMGYVL 87
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE--RRNIGMVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 88 QQAGLMPHRTIVDNISTVPRLNGVSARQAKSQALELLNTVGLDEsFAKRYPSQLSGGQAQRVGVARALASESSILLMDEP 167
Cdd:cd03259 79 QDYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEG-LLNRYPHELSGGQQQRVALARALAREPSLLLLDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2735597802 168 FSAVDPVVRADLQKELLRLQSTLGRTIIFVTHDMDEAILLGDYVAVFaRGGRIAQFG 224
Cdd:cd03259 158 LSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVM-NEGRIVQVG 213
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
8-244 |
7.46e-76 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 233.73 E-value: 7.46e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 8 IEFKSVFKTYGDNTVVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGEDNTARPAH--ELRRSMGY 85
Cdd:COG1126 2 IEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKKDinKLRRKVGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 86 VLQQAGLMPHRTIVDNISTVPR-LNGVSARQAKSQALELLNTVGLDEsFAKRYPSQLSGGQAQRVGVARALASESSILLM 164
Cdd:COG1126 82 VFQQFNLFPHLTVLENVTLAPIkVKKMSKAEAEERAMELLERVGLAD-KADAYPAQLSGGQQQRVAIARALAMEPKVMLF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 165 DEPFSAVDP--------VVRaDLQKEllrlqstlGRTIIFVTHDMDEAILLGDYVaVFARGGRIAQFGTPEEILREPADD 236
Cdd:COG1126 161 DEPTSALDPelvgevldVMR-DLAKE--------GMTMVVVTHEMGFAREVADRV-VFMDGGRIVEEGPPEEFFENPQHE 230
|
....*...
gi 2735597802 237 FVASFVGR 244
Cdd:COG1126 231 RTRAFLSK 238
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
8-246 |
8.71e-75 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 230.72 E-value: 8.71e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 8 IEFKSVFKTYGDNTVVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGEDNTARPAhELRRSMGYVL 87
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPA-EVRRRIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 88 QQAGLMPHRTIVDNISTVPRLNGVSARQAKSQALELLNTVGLDEsFAKRYPSQLSGGQAQRVGVARALASESSILLMDEP 167
Cdd:COG1131 80 QEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTD-AADRKVGTLSGGMKQRLGLALALLHDPELLILDEP 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2735597802 168 FSAVDPVVRADLqKELLRLQSTLGRTIIFVTHDMDEAILLGDYVAVFARgGRIAQFGTPEEILREPADDFVASFVGRDR 246
Cdd:COG1131 159 TSGLDPEARREL-WELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDK-GRIVADGTPDELKARLLEDVFLELTGEEA 235
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1-243 |
9.38e-75 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 235.61 E-value: 9.38e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 1 MSVLNNAIEFKSVFKTYGDNTVVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGEDNTARPAHelR 80
Cdd:PRK09452 8 PSSLSPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAE--N 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 81 RSMGYVLQQAGLMPHRTIVDNISTVPRLNGVSARQAKSQALELLNTVGLdESFAKRYPSQLSGGQAQRVGVARALASESS 160
Cdd:PRK09452 86 RHVNTVFQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQL-EEFAQRKPHQLSGGQQQRVAIARAVVNKPK 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 161 ILLMDEPFSAVDPVVRADLQKELLRLQSTLGRTIIFVTHDMDEAILLGDYVAVFaRGGRIAQFGTPEEILREPADDFVAS 240
Cdd:PRK09452 165 VLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVM-RDGRIEQDGTPREIYEEPKNLFVAR 243
|
...
gi 2735597802 241 FVG 243
Cdd:PRK09452 244 FIG 246
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
7-243 |
1.17e-73 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 227.99 E-value: 1.17e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 7 AIEFKSVFKTYGDNTVVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGEDNTARPAHElrRSMGYV 86
Cdd:cd03296 2 SIEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQE--RNVGFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 87 LQQAGLMPHRTIVDNIS----TVPRLNGVSARQAKSQALELLNTVGLDeSFAKRYPSQLSGGQAQRVGVARALASESSIL 162
Cdd:cd03296 80 FQHYALFRHMTVFDNVAfglrVKPRSERPPEAEIRAKVHELLKLVQLD-WLADRYPAQLSGGQRQRVALARALAVEPKVL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 163 LMDEPFSAVDPVVRADLQKELLRLQSTLGRTIIFVTHDMDEAILLGDYVAVFARgGRIAQFGTPEEILREPADDFVASFV 242
Cdd:cd03296 159 LLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNK-GRIEQVGTPDEVYDHPASPFVYSFL 237
|
.
gi 2735597802 243 G 243
Cdd:cd03296 238 G 238
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
5-242 |
3.29e-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: 226.78 E-value: 3.29e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 5 NNAIEFKSVFKTYGDNTVVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGEDNTARPAHEL---RR 81
Cdd:COG1127 3 EPMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELyelRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 82 SMGYVLQQAGL---MphrTIVDNIStVP--RLNGVSARQAKSQALELLNTVGLdESFAKRYPSQLSGGQAQRVGVARALA 156
Cdd:COG1127 83 RIGMLFQGGALfdsL---TVFENVA-FPlrEHTDLSEAEIRELVLEKLELVGL-PGAADKMPSELSGGMRKRVALARALA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 157 SESSILLMDEPFSAVDPVVRADLQKELLRLQSTLGRTIIFVTHDMDEAILLGDYVAVFARgGRIAQFGTPEEILREPaDD 236
Cdd:COG1127 158 LDPEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLAD-GKIIAEGTPEELLASD-DP 235
|
....*.
gi 2735597802 237 FVASFV 242
Cdd:COG1127 236 WVRQFL 241
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
15-244 |
4.56e-72 |
|
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: 228.00 E-value: 4.56e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 15 KTYGDNTVVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGEDNTARPAHelRRSMGYVLQQAGLMP 94
Cdd:TIGR03265 12 KRFGAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRLPPQ--KRDYGIVFQSYALFP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 95 HRTIVDNISTVPRLNGVSARQAKSQALELLNTVGLDESfAKRYPSQLSGGQAQRVGVARALASESSILLMDEPFSAVDPV 174
Cdd:TIGR03265 90 NLTVADNIAYGLKNRGMGRAEVAERVAELLDLVGLPGS-ERKYPGQLSGGQQQRVALARALATSPGLLLLDEPLSALDAR 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 175 VRADLQKELLRLQSTLGRTIIFVTHDMDEAILLGDYVAVFaRGGRIAQFGTPEEILREPADDFVASFVGR 244
Cdd:TIGR03265 169 VREHLRTEIRQLQRRLGVTTIMVTHDQEEALSMADRIVVM-NHGVIEQVGTPQEIYRHPATPFVADFVGE 237
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
8-236 |
4.81e-68 |
|
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: 222.09 E-value: 4.81e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 8 IEFKSVFKTY-----GDNTVVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGED---NTARPAHEL 79
Cdd:COG1123 261 LEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDltkLSRRSLREL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 80 RRSMGYVLQ--QAGLMPHRTIVDNISTVPRLNGV-SARQAKSQALELLNTVGLDESFAKRYPSQLSGGQAQRVGVARALA 156
Cdd:COG1123 341 RRRVQMVFQdpYSSLNPRMTVGDIIAEPLRLHGLlSRAERRERVAELLERVGLPPDLADRYPHELSGGQRQRVAIARALA 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 157 SESSILLMDEPFSAVDPVVRADLQKELLRLQSTLGRTIIFVTHDMDEAILLGDYVAVFaRGGRIAQFGTPEEILREPADD 236
Cdd:COG1123 421 LEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVM-YDGRIVEDGPTEEVFANPQHP 499
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
8-243 |
9.17e-67 |
|
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 210.43 E-value: 9.17e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 8 IEFKSVFKTYGDNTVVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGEDNTARPAHelRRSMGYVL 87
Cdd:TIGR00968 1 IEIANISKRFGSFQALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGLEQPDSGRIRLNGQDATRVHAR--DRKIGFVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 88 QQAGLMPHRTIVDNISTVPRLNGVSARQAKSQALELLNTVGLdESFAKRYPSQLSGGQAQRVGVARALASESSILLMDEP 167
Cdd:TIGR00968 79 QHYALFKHLTVRDNIAFGLEIRKHPKAKIKARVEELLELVQL-EGLGDRYPNQLSGGQRQRVALARALAVEPQVLLLDEP 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2735597802 168 FSAVDPVVRADLQKELLRLQSTLGRTIIFVTHDMDEAILLGDYVAVFARgGRIAQFGTPEEILREPADDFVASFVG 243
Cdd:TIGR00968 158 FGALDAKVRKELRSWLRKLHDEVHVTTVFVTHDQEEAMEVADRIVVMSN-GKIEQIGSPDEVYDHPANPFVMSFLG 232
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
8-224 |
1.32e-66 |
|
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: 209.03 E-value: 1.32e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 8 IEFKSVFKTYGDNTVVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGEDNTARPAHElrRSMGYVL 87
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKD--RDIAMVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 88 QQAGLMPHRTIVDNISTVPRLNGVSARQAKSQALELLNTVGLDEsFAKRYPSQLSGGQAQRVGVARALASESSILLMDEP 167
Cdd:cd03301 79 QNYALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEH-LLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2735597802 168 FSAVDPVVRADLQKELLRLQSTLGRTIIFVTHDMDEAILLGDYVAVFARgGRIAQFG 224
Cdd:cd03301 158 LSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMND-GQIQQIG 213
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
8-241 |
3.33e-66 |
|
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: 208.90 E-value: 3.33e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 8 IEFKSVFKTYGDNTVVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGEDNTARPAHEL---RRSMG 84
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELyrlRRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 85 YVLQQAGLMPHRTIVDNISTVPRLNGV-SARQAKSQALELLNTVGLdESFAKRYPSQLSGGQAQRVGVARALASESSILL 163
Cdd:cd03261 81 MLFQSGALFDSLTVFENVAFPLREHTRlSEEEIREIVLEKLEAVGL-RGAEDLYPAELSGGMKKRVALARALALDPELLL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2735597802 164 MDEPFSAVDPVVRADLQKELLRLQSTLGRTIIFVTHDMDEAILLGDYVAVFARGGRIAQfGTPEEILREPaDDFVASF 241
Cdd:cd03261 160 YDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAE-GTPEELRASD-DPLVRQF 235
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
8-217 |
3.25e-65 |
|
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: 204.34 E-value: 3.25e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 8 IEFKSVFKTYGDNTVVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGEDNTA--RPAHELRRSMGY 85
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDleDELPPLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 86 VLQQAGLMPHRTIVDNIstvprlngvsarqaksqalellntvgldesfakRYPsqLSGGQAQRVGVARALASESSILLMD 165
Cdd:cd03229 81 VFQDFALFPHLTVLENI---------------------------------ALG--LSGGQQQRVALARALAMDPDVLLLD 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2735597802 166 EPFSAVDPVVRADLQKELLRLQSTLGRTIIFVTHDMDEAILLGDYVAVFARG 217
Cdd:cd03229 126 EPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDG 177
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
8-233 |
3.59e-65 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 206.28 E-value: 3.59e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 8 IEFKSVFKTYGDN----TVVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGEDNTARPAHEL---R 80
Cdd:cd03258 2 IELKNVSKVFGDTggkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELrkaR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 81 RSMGYVLQQAGLMPHRTIVDNISTVPRLNGVSARQAKSQALELLNTVGLdESFAKRYPSQLSGGQAQRVGVARALASESS 160
Cdd:cd03258 82 RRIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGL-EDKADAYPAQLSGGQKQRVGIARALANNPK 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2735597802 161 ILLMDEPFSAVDPVVRADLQKELLRLQSTLGRTIIFVTHDMDEAILLGDYVAVFARgGRIAQFGTPEEILREP 233
Cdd:cd03258 161 VLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEK-GEVVEEGTVEEVFANP 232
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
8-220 |
5.52e-65 |
|
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: 205.07 E-value: 5.52e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 8 IEFKSVFKTYGDNTVVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGE--DNTARPAHELRRSMGY 85
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLklTDDKKNINELRQKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 86 VLQQAGLMPHRTIVDNISTVPR-LNGVSARQAKSQALELLNTVGLDEsFAKRYPSQLSGGQAQRVGVARALASESSILLM 164
Cdd:cd03262 81 VFQQFNLFPHLTVLENITLAPIkVKGMSKAEAEERALELLEKVGLAD-KADAYPAQLSGGQQQRVAIARALAMNPKVMLF 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2735597802 165 DEPFSAVDPVVRADLQKELLRLQSTlGRTIIFVTHDMDEAILLGDYVaVFARGGRI 220
Cdd:cd03262 160 DEPTSALDPELVGEVLDVMKDLAEE-GMTMVVVTHEMGFAREVADRV-IFMDDGRI 213
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
7-302 |
6.84e-65 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 209.55 E-value: 6.84e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 7 AIEFKSVFKTYGDNTVVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGEDNTARPAHElrRSMGYV 86
Cdd:PRK10851 2 SIEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARD--RKVGFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 87 LQQAGLMPHRTIVDNI----STVPRLNGVSARQAKSQALELLNTVGLDEsFAKRYPSQLSGGQAQRVGVARALASESSIL 162
Cdd:PRK10851 80 FQHYALFRHMTVFDNIafglTVLPRRERPNAAAIKAKVTQLLEMVQLAH-LADRYPAQLSGGQKQRVALARALAVEPQIL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 163 LMDEPFSAVDPVVRADLQKELLRLQSTLGRTIIFVTHDMDEAILLGDYVAVFARgGRIAQFGTPEEILREPADDFVASFV 242
Cdd:PRK10851 159 LLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQ-GNIEQAGTPDQVWREPATRFVLEFM 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 243 G---RDRGMRRLT-FASGAD------VPIH--PLDAQQTPWQQ-------------------------WQLNVEdgrPAG 285
Cdd:PRK10851 238 GevnRLQGTIRGGqFHVGAHrwplgyTPAYqgPVDLFLRPWEVdisrrtsldsplpvqvlevspkghyWQLVVQ---PLG 314
|
330 340
....*....|....*....|....*..
gi 2735597802 286 WR--------IDDRVIP--GGSLFVAG 302
Cdd:PRK10851 315 WYnepltvvmHGDIDAPqrGERLFVGL 341
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
8-243 |
1.65e-64 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 208.01 E-value: 1.65e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 8 IEFKSVFKTY----GDNTVVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGEDNTARPAHEL---R 80
Cdd:COG1135 2 IELENLSKTFptkgGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELraaR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 81 RSMGYVLQQAGLMPHRTIVDNISTVPRLNGVSARQAKSQALELLNTVGLDEsFAKRYPSQLSGGQAQRVGVARALASESS 160
Cdd:COG1135 82 RKIGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSD-KADAYPSQLSGGQKQRVGIARALANNPK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 161 ILLMDEPFSAVDP-----VVraDLqkeLLRLQSTLGRTIIFVTHDMD--EAILlgDYVAVFaRGGRIAQFGTPEEILREP 233
Cdd:COG1135 161 VLLCDEATSALDPettrsIL--DL---LKDINRELGLTIVLITHEMDvvRRIC--DRVAVL-ENGRIVEQGPVLDVFANP 232
|
250
....*....|
gi 2735597802 234 ADDFVASFVG 243
Cdd:COG1135 233 QSELTRRFLP 242
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
8-229 |
3.68e-64 |
|
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: 203.18 E-value: 3.68e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 8 IEFKSVFKTYGDNTVVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEH-----TSGTILVNGEDNTARPAH--ELR 80
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLipgapDEGEVLLDGKDIYDLDVDvlELR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 81 RSMGYVLQQAGLMPhRTIVDNISTVPRLNGV-SARQAKSQALELLNTVGLDESFAKR-YPSQLSGGQAQRVGVARALASE 158
Cdd:cd03260 81 RRVGMVFQKPNPFP-GSIYDNVAYGLRLHGIkLKEELDERVEEALRKAALWDEVKDRlHALGLSGGQQQRLCLARALANE 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2735597802 159 SSILLMDEPFSAVDPVVRADLQKELLRLQSTLgrTIIFVTHDMDEAILLGDYVAVFARgGRIAQFGTPEEI 229
Cdd:cd03260 160 PEVLLLDEPTSALDPISTAKIEELIAELKKEY--TIVIVTHNMQQAARVADRTAFLLN-GRLVEFGPTEQI 227
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
39-283 |
3.77e-64 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 206.58 E-value: 3.77e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 39 VGPSGCGKTTSLRMINRMVEHTSGTILVNGEDNTARPAHelRRSMGYVLQQAGLMPHRTIVDNISTVPRLNGVSARQAKS 118
Cdd:TIGR01187 2 LGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPH--LRHINMVFQSYALFPHMTVEENVAFGLKMRKVPRAEIKP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 119 QALELLNTVGLDEsFAKRYPSQLSGGQAQRVGVARALASESSILLMDEPFSAVDPVVRADLQKELLRLQSTLGRTIIFVT 198
Cdd:TIGR01187 80 RVLEALRLVQLEE-FADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITFVFVT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 199 HDMDEAILLGDYVAVFaRGGRIAQFGTPEEILREPADDFVASFVGR---------DRGMRRLTFASgadVPIHPLDAQQT 269
Cdd:TIGR01187 159 HDQEEAMTMSDRIAIM-RKGKIAQIGTPEEIYEEPANLFVARFIGEinvfeatviERKSEQVVLAG---VEGRRCDIYTD 234
|
250
....*....|....
gi 2735597802 270 pwqqwqLNVEDGRP 283
Cdd:TIGR01187 235 ------VPVEKDQP 242
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
8-241 |
4.90e-64 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 203.40 E-value: 4.90e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 8 IEFKSVFKTYGDNTVVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGED--NTARPAHELRRSMGY 85
Cdd:PRK09493 2 IEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKvnDPKVDERLIRQEAGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 86 VLQQAGLMPHRTIVDNISTVP-RLNGVSARQAKSQALELLNTVGLDESfAKRYPSQLSGGQAQRVGVARALASESSILLM 164
Cdd:PRK09493 82 VFQQFYLFPHLTALENVMFGPlRVRGASKEEAEKQARELLAKVGLAER-AHHYPSELSGGQQQRVAIARALAVKPKLMLF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 165 DEPFSAVDPvvraDLQKELLRLQSTL---GRTIIFVTHDMDEAILLGDYVaVFARGGRIAQFGTPEEILREPADDFVASF 241
Cdd:PRK09493 161 DEPTSALDP----ELRHEVLKVMQDLaeeGMTMVIVTHEIGFAEKVASRL-IFIDKGRIAEDGDPQVLIKNPPSQRLQEF 235
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
5-243 |
6.54e-64 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 206.88 E-value: 6.54e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 5 NNAIEFKSVFKTYGDNTVVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGEDNTARPAHElrRSMG 84
Cdd:PRK11432 4 KNFVVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQ--RDIC 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 85 YVLQQAGLMPHRTIVDNISTVPRLNGVSARQAKSQALELLNTVGLdESFAKRYPSQLSGGQAQRVGVARALASESSILLM 164
Cdd:PRK11432 82 MVFQSYALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDL-AGFEDRYVDQISGGQQQRVALARALILKPKVLLF 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2735597802 165 DEPFSAVDPVVRADLQKELLRLQSTLGRTIIFVTHDMDEAILLGDYVAVFARgGRIAQFGTPEEILREPADDFVASFVG 243
Cdd:PRK11432 161 DEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNK-GKIMQIGSPQELYRQPASRFMASFMG 238
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
8-220 |
2.18e-63 |
|
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: 201.18 E-value: 2.18e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 8 IEFKSVFKTYGDN----TVVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGED----NTARPAHEL 79
Cdd:cd03255 1 IELKNLSKTYGGGgekvQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDisklSEKELAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 80 RRSMGYVLQQAGLMPHRTIVDNISTVPRLNGVSARQAKSQALELLNTVGLDESfAKRYPSQLSGGQAQRVGVARALASES 159
Cdd:cd03255 81 RRHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDR-LNHYPSELSGGQQQRVAIARALANDP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2735597802 160 SILLMDEPFSAVDPVVRADLQKELLRLQSTLGRTIIFVTHDMDEAiLLGDYVaVFARGGRI 220
Cdd:cd03255 160 KIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELA-EYADRI-IELRDGKI 218
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
8-233 |
3.86e-63 |
|
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: 200.64 E-value: 3.86e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 8 IEFKSVFKTYGDNT-VVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGEDNTARPAHELRRSMGYV 86
Cdd:COG1122 1 IELENLSFSYPGGTpALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 87 LQQAG---LMPhrTIVDNISTVPRLNGVSARQAKSQALELLNTVGLDEsFAKRYPSQLSGGQAQRVGVARALASESSILL 163
Cdd:COG1122 81 FQNPDdqlFAP--TVEEDVAFGPENLGLPREEIRERVEEALELVGLEH-LADRPPHELSGGQKQRVAIAGVLAMEPEVLV 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 164 MDEPFSAVDPVVRADLQKELLRLQSTlGRTIIFVTHDMDEAILLGDYVAVFARgGRIAQFGTPEEILREP 233
Cdd:COG1122 158 LDEPTAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDD-GRIVADGTPREVFSDY 225
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
7-250 |
4.06e-62 |
|
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: 198.87 E-value: 4.06e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 7 AIEFKSVFKTYG----DNTVVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGEDNTARPAHELRRS 82
Cdd:COG1124 1 MLEVRNLSVSYGqggrRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 83 MGYVLQQ--AGLMPHRTIVDNISTVPRLNGVSARQAksQALELLNTVGLDESFAKRYPSQLSGGQAQRVGVARALASESS 160
Cdd:COG1124 81 VQMVFQDpyASLHPRHTVDRILAEPLRIHGLPDREE--RIAELLEQVGLPPSFLDRYPHQLSGGQRQRVAIARALILEPE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 161 ILLMDEPFSAVDPVVRADLQKELLRLQSTLGRTIIFVTHDMDEAILLGDYVAVFaRGGRIAQFGTPEEILREPADDFVAS 240
Cdd:COG1124 159 LLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVM-QNGRIVEELTVADLLAGPKHPYTRE 237
|
250
....*....|
gi 2735597802 241 FVGRDRGMRR 250
Cdd:COG1124 238 LLAASLAFER 247
|
|
| tungstate_WtpC |
NF040840 |
tungstate ABC transporter ATP-binding protein WtpC; |
8-243 |
2.24e-61 |
|
tungstate ABC transporter ATP-binding protein WtpC;
Pssm-ID: 468779 [Multi-domain] Cd Length: 347 Bit Score: 200.30 E-value: 2.24e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 8 IEFKSVFKTYGDNTVVDnLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGEDNTARPAHelRRSMGYVL 87
Cdd:NF040840 2 IRIENLSKDWKEFKLRD-ISLEVKEGEYFIILGPSGAGKTVLLELIAGIWPPDSGKIYLDGKDITNLPPE--KRGIAYVY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 88 QQAGLMPHRTIVDNISTVPRLNGVSARQAKSQALELLNTVGLdESFAKRYPSQLSGGQAQRVGVARALASESSILLMDEP 167
Cdd:NF040840 79 QNYMLFPHKTVFENIAFGLKLRKVPKEEIERKVKEIMELLGI-SHLLHRKPRTLSGGEQQRVALARALIIEPKLLLLDEP 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2735597802 168 FSAVDPVVRADLQKELLRLQSTLGRTIIFVTHDMDEAILLGDYVAVFARgGRIAQFGTPEEILREPADDFVASFVG 243
Cdd:NF040840 158 LSALDVQTRDELIREMKRWHREFGFTAIHVTHNFEEALSLADRVGIMLN-GRLSQVGDVREVFRRPKNEFVARFVG 232
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
5-202 |
4.53e-60 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 192.57 E-value: 4.53e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 5 NNAIEFKSVFKTYGDN----TVVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGEDNTARPAHEL- 79
Cdd:COG1136 2 SPLLELRNLTKSYGTGegevTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELa 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 80 ---RRSMGYVLQQAGLMPHRTIVDNISTVPRLNGVSARQAKSQALELLNTVGLDEsFAKRYPSQLSGGQAQRVGVARALA 156
Cdd:COG1136 82 rlrRRHIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGD-RLDHRPSQLSGGQQQRVAIARALV 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2735597802 157 SESSILLMDEPFSAVDPVVRADLQKELLRLQSTLGRTIIFVTHDMD 202
Cdd:COG1136 161 NRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPE 206
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
20-243 |
7.94e-60 |
|
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: 192.55 E-value: 7.94e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 20 NTVVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGEDNTARPAHelRRSMGYVLQQAGLMPHRTIV 99
Cdd:cd03299 12 EFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE--KRDISYVPQNYALFPHMTVY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 100 DNISTVPRLNGVSARQAKSQALELLNTVGLDEsFAKRYPSQLSGGQAQRVGVARALASESSILLMDEPFSAVDPVVRADL 179
Cdd:cd03299 90 KNIAYGLKKRKVDKKEIERKVLEIAEMLGIDH-LLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKL 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2735597802 180 QKELLRLQSTLGRTIIFVTHDMDEAILLGDYVAVFaRGGRIAQFGTPEEILREPADDFVASFVG 243
Cdd:cd03299 169 REELKKIRKEFGVTVLHVTHDFEEAWALADKVAIM-LNGKLIQVGKPEEVFKKPKNEFVAEFLG 231
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
10-243 |
9.34e-60 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 196.40 E-value: 9.34e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 10 FKSVFKTYGDNTVVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGED-NTARPAhelRRSMGYVLQ 88
Cdd:PRK11000 6 LRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRmNDVPPA---ERGVGMVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 89 QAGLMPHRTIVDNISTVPRLNGVSARQAKS---QALELLNTVGLDEsfakRYPSQLSGGQAQRVGVARALASESSILLMD 165
Cdd:PRK11000 83 SYALYPHLSVAENMSFGLKLAGAKKEEINQrvnQVAEVLQLAHLLD----RKPKALSGGQRQRVAIGRTLVAEPSVFLLD 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2735597802 166 EPFSAVDPVVRADLQKELLRLQSTLGRTIIFVTHDMDEAILLGDYVAVFaRGGRIAQFGTPEEILREPADDFVASFVG 243
Cdd:PRK11000 159 EPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVL-DAGRVAQVGKPLELYHYPANRFVAGFIG 235
|
|
| 3a0107s01c2 |
TIGR00972 |
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein ... |
7-244 |
2.48e-59 |
|
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: 191.74 E-value: 2.48e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 7 AIEFKSVFKTYGDNTVVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVE-----HTSGTILVNGED--NTARPAHEL 79
Cdd:TIGR00972 1 AIEIENLNLFYGEKEALKNINLDIPKNQVTALIGPSGCGKSTLLRSLNRMNDlvpgvRIEGKVLFDGQDiyDKKIDVVEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 80 RRSMGYVLQQAGLMPhRTIVDNISTVPRLNGV-SARQAKSQALELLNTVGL-DE--SFAKRYPSQLSGGQAQRVGVARAL 155
Cdd:TIGR00972 81 RRRVGMVFQKPNPFP-MSIYDNIAYGPRLHGIkDKKELDEIVEESLKKAALwDEvkDRLHDSALGLSGGQQQRLCIARAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 156 ASESSILLMDEPFSAVDPVVRADLQKELLRLQSTLgrTIIFVTHDMDEAILLGDYVAVFARgGRIAQFGTPEEILREPAD 235
Cdd:TIGR00972 160 AVEPEVLLLDEPTSALDPIATGKIEELIQELKKKY--TIVIVTHNMQQAARISDRTAFFYD-GELVEYGPTEQIFTNPKE 236
|
250
....*....|
gi 2735597802 236 DFVASFV-GR 244
Cdd:TIGR00972 237 KRTEDYIsGR 246
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
8-236 |
3.81e-59 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 190.84 E-value: 3.81e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 8 IEFKSVFKTYGDNTVVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGEDNTARPAhELRRSMGYVL 87
Cdd:COG4555 2 IEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPR-EARRQIGVLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 88 QQAGLMPHRTIVDNISTVPRLNGVSARQAKSQALELLNTVGLDEsFAKRYPSQLSGGQAQRVGVARALASESSILLMDEP 167
Cdd:COG4555 81 DERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEE-FLDRRVGELSTGMKKKVALARALVHDPKVLLLDEP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2735597802 168 FSAVDPVVRADLQKELLRLqSTLGRTIIFVTHDMDEAILLGDYVAVFARGGRIAQfGTPEEILREPADD 236
Cdd:COG4555 160 TNGLDVMARRLLREILRAL-KKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQ-GSLDELREEIGEE 226
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
23-241 |
1.05e-58 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 194.87 E-value: 1.05e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 23 VDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGEDNTARPAHELR----RSMGYVLQQAGLMPHRTI 98
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELRevrrKKIAMVFQSFALMPHMTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 99 VDNISTVPRLNGVSARQAKSQALELLNTVGLdESFAKRYPSQLSGGQAQRVGVARALASESSILLMDEPFSAVDPVVRAD 178
Cdd:PRK10070 124 LDNTAFGMELAGINAEERREKALDALRQVGL-ENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTE 202
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2735597802 179 LQKELLRLQSTLGRTIIFVTHDMDEAILLGDYVAVFaRGGRIAQFGTPEEILREPADDFVASF 241
Cdd:PRK10070 203 MQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIM-QNGEVVQVGTPDEILNNPANDYVRTF 264
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
8-224 |
5.23e-58 |
|
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: 187.33 E-value: 5.23e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 8 IEFKSVFKTY----GDNTVVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGEDNTARPAHEL---R 80
Cdd:cd03257 2 LEVKNLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRkirR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 81 RSMGYVLQQAG--LMPHRTIVDNISTVPRLNGVSARQA--KSQALELLNTVGLDESFAKRYPSQLSGGQAQRVGVARALA 156
Cdd:cd03257 82 KEIQMVFQDPMssLNPRMTIGEQIAEPLRIHGKLSKKEarKEAVLLLLVGVGLPEEVLNRYPHELSGGQRQRVAIARALA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2735597802 157 SESSILLMDEPFSAVDPVVRADLQKELLRLQSTLGRTIIFVTHDMDEAILLGDYVAVFaRGGRIAQFG 224
Cdd:cd03257 162 LNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVM-YAGKIVEEG 228
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
7-259 |
5.63e-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: 193.20 E-value: 5.63e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 7 AIEFKSVFKTY--GDNTVVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHT---SGTILVNGEDNTARPAHELRR 81
Cdd:COG1123 4 LLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRGR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 82 SMGYVLQQAG--LMPHrTIVDNISTVPRLNGVSARQAKSQALELLNTVGLdESFAKRYPSQLSGGQAQRVGVARALASES 159
Cdd:COG1123 84 RIGMVFQDPMtqLNPV-TVGDQIAEALENLGLSRAEARARVLELLEAVGL-ERRLDRYPHQLSGGQRQRVAIAMALALDP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 160 SILLMDEPFSAVDPVVRADLQKELLRLQSTLGRTIIFVTHDMDEAILLGDYVAVFaRGGRIAQFGTPEEILREPADDFVA 239
Cdd:COG1123 162 DLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVM-DDGRIVEDGPPEEILAAPQALAAV 240
|
250 260
....*....|....*....|
gi 2735597802 240 SFVGRDRGMRRLTFASGADV 259
Cdd:COG1123 241 PRLGAARGRAAPAAAAAEPL 260
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
8-229 |
8.43e-57 |
|
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: 184.25 E-value: 8.43e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 8 IEFKSVFKTYGD--NTVVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGEDnTARPAHELRRSMGY 85
Cdd:cd03263 1 LQIRNLTKTYKKgtKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYS-IRTDRKAARQSLGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 86 VLQQAGLMPHRTIVDNISTVPRLNGVSARQAKSQALELLNTVGLdESFAKRYPSQLSGGQAQRVGVARALASESSILLMD 165
Cdd:cd03263 80 CPQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGL-TDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLD 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2735597802 166 EPFSAVDPVVRADLQKELLRLQStlGRTIIFVTHDMDEAILLGDYVAVFARGGRIAqFGTPEEI 229
Cdd:cd03263 159 EPTSGLDPASRRAIWDLILEVRK--GRSIILTTHSMDEAEALCDRIAIMSDGKLRC-IGSPQEL 219
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
7-232 |
1.53e-56 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 184.48 E-value: 1.53e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 7 AIEFKSVFKTYGDNTVVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGEDNTARPAHELRRSMGYV 86
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 87 LQQA--------------GLMPHRtivdnistvPRLNGVSA--RQAKSQALELLNTvgldESFAKRYPSQLSGGQAQRVG 150
Cdd:COG1120 81 PQEPpapfgltvrelvalGRYPHL---------GLFGRPSAedREAVEEALERTGL----EHLADRPVDELSGGERQRVL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 151 VARALASESSILLMDEPFSAVDPVVRADLQKELLRLQSTLGRTIIFVTHDMDEAILLGDYVAVFaRGGRIAQFGTPEEIL 230
Cdd:COG1120 148 IARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLL-KDGRIVAQGPPEEVL 226
|
..
gi 2735597802 231 RE 232
Cdd:COG1120 227 TP 228
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
8-243 |
3.53e-56 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 186.55 E-value: 3.53e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 8 IEFKSVFKTY--GDNTV--VDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGEDNTARPAHEL---R 80
Cdd:PRK11153 2 IELKNISKVFpqGGRTIhaLNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELrkaR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 81 RSMGYVLQQAGLMPHRTIVDNISTVPRLNGVSARQAKSQALELLNTVGLDEsFAKRYPSQLSGGQAQRVGVARALASESS 160
Cdd:PRK11153 82 RQIGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSD-KADRYPAQLSGGQKQRVAIARALASNPK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 161 ILLMDEPFSAVDP-VVRADLqkELLR-LQSTLGRTIIFVTHDMDEAILLGDYVAVFArGGRIAQFGTPEEILREPADDFV 238
Cdd:PRK11153 161 VLLCDEATSALDPaTTRSIL--ELLKdINRELGLTIVLITHEMDVVKRICDRVAVID-AGRLVEQGTVSEVFSHPKHPLT 237
|
....*
gi 2735597802 239 ASFVG 243
Cdd:PRK11153 238 REFIQ 242
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
14-234 |
2.03e-55 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 183.72 E-value: 2.03e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 14 FKTY-GDNTVVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVE---HTSGTILVNGEDNTARPAHELR----RSMGY 85
Cdd:COG0444 11 FPTRrGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPppgITSGEILFDGEDLLKLSEKELRkirgREIQM 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 86 VLQ--QAGLMPHRTIVDNISTVPRL-NGVSARQAKSQALELLNTVGLD--ESFAKRYPSQLSGGQAQRVGVARALASESS 160
Cdd:COG0444 91 IFQdpMTSLNPVMTVGDQIAEPLRIhGGLSKAEARERAIELLERVGLPdpERRLDRYPHELSGGMRQRVMIARALALEPK 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2735597802 161 ILLMDEPFSAVDPVVRADLQKELLRLQSTLGRTIIFVTHDMDEAILLGDYVAVFaRGGRIAQFGTPEEILREPA 234
Cdd:COG0444 171 LLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVM-YAGRIVEEGPVEELFENPR 243
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
8-217 |
6.18e-55 |
|
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: 177.59 E-value: 6.18e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 8 IEFKSVFKTYGDNTVVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGEDNTARPaHELRRSMGYVL 87
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEP-EEVKRRIGYLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 88 QQAGLMPHRTIVDNIstvprlngvsarqaksqalellntvgldesfakrypsQLSGGQAQRVGVARALASESSILLMDEP 167
Cdd:cd03230 80 EEPSLYENLTVRENL-------------------------------------KLSGGMKQRLALAQALLHDPELLILDEP 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2735597802 168 FSAVDPVVRADLQKELLRLQSTlGRTIIFVTHDMDEAILLGDYVAVFARG 217
Cdd:cd03230 123 TSGLDPESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNG 171
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
9-217 |
1.31e-54 |
|
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: 178.04 E-value: 1.31e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 9 EFKSVFKTYGDNT--VVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGEDNTARPAHELRRSMGYV 86
Cdd:cd03225 1 ELKNLSFSYPDGArpALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 87 LQQAG---LMPhrTIVDNISTVPRLNGVSARQAKSQALELLNTVGLDEsFAKRYPSQLSGGQAQRVGVARALASESSILL 163
Cdd:cd03225 81 FQNPDdqfFGP--TVEEEVAFGLENLGLPEEEIEERVEEALELVGLEG-LRDRSPFTLSGGQKQRVAIAGVLAMDPDILL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2735597802 164 MDEPFSAVDPVVRADLQKELLRLQSTlGRTIIFVTHDMDEAILLGDYVAVFARG 217
Cdd:cd03225 158 LDEPTAGLDPAGRRELLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVLEDG 210
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
7-232 |
1.65e-54 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 180.69 E-value: 1.65e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 7 AIEFKSVFKTYGDNTVVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGEDNTARPahelRRSMGYV 86
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPED----RRRIGYL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 87 LQQAGLMPHRTIVDNISTVPRLNGVSARQAKSQALELLNTVGLDESFAKRYpSQLSGGQAQRVGVARALASESSILLMDE 166
Cdd:COG4152 77 PEERGLYPKMKVGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDRANKKV-EELSKGNQQKVQLIAALLHDPELLILDE 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2735597802 167 PFSAVDPVVRADLQKELLRLQSTlGRTIIFVTHDMDEAILLGDYVAVFARGGRIAQfGTPEEILRE 232
Cdd:COG4152 156 PFSGLDPVNVELLKDVIRELAAK-GTTVIFSSHQMELVEELCDRIVIINKGRKVLS-GSVDEIRRQ 219
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
8-202 |
6.69e-54 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 176.78 E-value: 6.69e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 8 IEFKSVFKTY-GDNTVVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGEDNTARPAHE---LRRSM 83
Cdd:COG2884 2 IRFENVSKRYpGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREipyLRRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 84 GYVLQQAGLMPHRTIVDNISTVPRLNGVSARQAKSQALELLNTVGLdESFAKRYPSQLSGGQAQRVGVARALASESSILL 163
Cdd:COG2884 82 GVVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGL-SDKAKALPHELSGGEQQRVAIARALVNRPELLL 160
|
170 180 190
....*....|....*....|....*....|....*....
gi 2735597802 164 MDEPFSAVDPVVRADLQKELLRLQStLGRTIIFVTHDMD 202
Cdd:COG2884 161 ADEPTGNLDPETSWEIMELLEEINR-RGTTVLIATHDLE 198
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
8-229 |
1.00e-53 |
|
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: 176.99 E-value: 1.00e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 8 IEFKSVFKTYGDNT-VVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGEDNTARPAHEL---RRSM 83
Cdd:cd03256 1 IEVENLSKTYPNGKkALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALrqlRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 84 GYVLQQAGLMPHRTIVDNI--------STVPRLNGVSARQAKSQALELLNTVGLDESFAKRyPSQLSGGQAQRVGVARAL 155
Cdd:cd03256 81 GMIFQQFNLIERLSVLENVlsgrlgrrSTWRSLFGLFPKEEKQRALAALERVGLLDKAYQR-ADQLSGGQQQRVAIARAL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2735597802 156 ASESSILLMDEPFSAVDPVVRADLQKELLRLQSTLGRTIIFVTHDMDEAILLGDYVaVFARGGRIAQFGTPEEI 229
Cdd:cd03256 160 MQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRI-VGLKDGRIVFDGPPAEL 232
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-235 |
1.71e-53 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 176.77 E-value: 1.71e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 1 MSVLNNAIEFK--SVFktYGDNTVVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVE-----HTSGTILVNGED--N 71
Cdd:COG1117 5 ASTLEPKIEVRnlNVY--YGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDlipgaRVEGEILLDGEDiyD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 72 TARPAHELRRSMGYVLQQAGLMPHrTIVDNISTVPRLNGVSARQAKSQALE-LLNTVGL-DEsfAK----RYPSQLSGGQ 145
Cdd:COG1117 83 PDVDVVELRRRVGMVFQKPNPFPK-SIYDNVAYGLRLHGIKSKSELDEIVEeSLRKAALwDE--VKdrlkKSALGLSGGQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 146 AQRVGVARALASESSILLMDEPFSAVDPVVRA---DLqkeLLRLQSTLgrTIIFVTHDMDEAILLGDYVAVFArGGRIAQ 222
Cdd:COG1117 160 QQRLCIARALAVEPEVLLMDEPTSALDPISTAkieEL---ILELKKDY--TIVIVTHNMQQAARVSDYTAFFY-LGELVE 233
|
250
....*....|...
gi 2735597802 223 FGTPEEILREPAD 235
Cdd:COG1117 234 FGPTEQIFTNPKD 246
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
22-222 |
2.44e-53 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 176.59 E-value: 2.44e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 22 VVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGEDNTArPAHElrRsmGYVLQQAGLMPHRTIVDN 101
Cdd:COG4525 22 ALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTG-PGAD--R--GVVFQKDALLPWLNVLDN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 102 ISTVPRLNGVSARQAKSQALELLNTVGLDEsFAKRYPSQLSGGQAQRVGVARALASESSILLMDEPFSAVDPVVRADLQK 181
Cdd:COG4525 97 VAFGLRLRGVPKAERRARAEELLALVGLAD-FARRRIWQLSGGMRQRVGIARALAADPRFLLMDEPFGALDALTREQMQE 175
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2735597802 182 ELLRLQSTLGRTIIFVTHDMDEAILLGDYVAVFA-RGGRIAQ 222
Cdd:COG4525 176 LLLDVWQRTGKGVFLITHSVEEALFLATRLVVMSpGPGRIVE 217
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
8-233 |
4.53e-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: 176.49 E-value: 4.53e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 8 IEFKSVFKTYGDNT-----VVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGEDNTARPA---HEL 79
Cdd:TIGR04521 1 IKLKNVSYIYQPGTpfekkALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKkklKDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 80 RRSMGYVLQqaglMPH-----RTIVDNISTVPRLNGVSARQAKSQALELLNTVGLDESFAKRYPSQLSGGQAQRVGVARA 154
Cdd:TIGR04521 81 RKKVGLVFQ----FPEhqlfeETVYKDIAFGPKNLGLSEEEAEERVKEALELVGLDEEYLERSPFELSGGQMRRVAIAGV 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2735597802 155 LASESSILLMDEPFSAVDPVVRADLQKELLRLQSTLGRTIIFVTHDMDEAILLGDYVAVFARgGRIAQFGTPEEILREP 233
Cdd:TIGR04521 157 LAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHK-GKIVLDGTPREVFSDV 234
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
5-234 |
6.92e-53 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 174.89 E-value: 6.92e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 5 NNAIEFKSVFKTYGDNTVVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGedntaRPAHELRRSMG 84
Cdd:COG1121 4 MPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFG-----KPPRRARRRIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 85 YVLQQA----------------GLMPHRtivdnistvpRLNGVSARQAKSQALELLNTVGLDEsFAKRYPSQLSGGQAQR 148
Cdd:COG1121 79 YVPQRAevdwdfpitvrdvvlmGRYGRR----------GLFRRPSRADREAVDEALERVGLED-LADRPIGELSGGQQQR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 149 VGVARALASESSILLMDEPFSAVDPVVRADLQKELLRLQSTlGRTIIFVTHDMDEAILLGDYVAVFARgGRIAqFGTPEE 228
Cdd:COG1121 148 VLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRRE-GKTILVVTHDLGAVREYFDRVLLLNR-GLVA-HGPPEE 224
|
....*.
gi 2735597802 229 ILREPA 234
Cdd:COG1121 225 VLTPEN 230
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
7-229 |
8.85e-53 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 174.86 E-value: 8.85e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 7 AIEFKSVFKTY-GDNTVVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGEDNTA---RPAHELRRS 82
Cdd:COG3638 2 MLELRNLSKRYpGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTAlrgRALRRLRRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 83 MGYVLQQAGLMPHRTIVDN--------ISTVPRLNGVSARQAKSQALELLNTVGLDEsFAKRYPSQLSGGQAQRVGVARA 154
Cdd:COG3638 82 IGMIFQQFNLVPRLSVLTNvlagrlgrTSTWRSLLGLFPPEDRERALEALERVGLAD-KAYQRADQLSGGQQQRVAIARA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2735597802 155 LASESSILLMDEPFSAVDPVVRADLQKELLRLQSTLGRTIIFVTHDMDEAILLGDYVAVFaRGGRIAQFGTPEEI 229
Cdd:COG3638 161 LVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGL-RDGRVVFDGPPAEL 234
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
7-285 |
6.29e-52 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 175.80 E-value: 6.29e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 7 AIEFKSVFKTY-GDNTVVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGED-NTARPAHelrRSMG 84
Cdd:PRK11650 3 GLKLQAVRKSYdGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVvNELEPAD---RDIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 85 YVLQQAGLMPHRTIVDNISTVPRLNGVS-----ARQAKS-QALELlntvgldESFAKRYPSQLSGGQAQRVGVARALASE 158
Cdd:PRK11650 80 MVFQNYALYPHMSVRENMAYGLKIRGMPkaeieERVAEAaRILEL-------EPLLDRKPRELSGGQRQRVAMGRAIVRE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 159 SSILLMDEPFSAVDPVVRADLQKELLRLQSTLGRTIIFVTHDMDEAILLGDYVAVFaRGGRIAQFGTPEEILREPADDFV 238
Cdd:PRK11650 153 PAVFLFDEPLSNLDAKLRVQMRLEIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVM-NGGVAEQIGTPVEVYEKPASTFV 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 2735597802 239 ASFVG----------RDRGMRRLTFASGADVPIhPLDAQQTPWQQWQLNV--EDGRPAG 285
Cdd:PRK11650 232 ASFIGspamnlldgrVSADGAAFELAGGIALPL-GGGYRQYAGRKLTLGIrpEHIALSS 289
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
8-229 |
5.71e-51 |
|
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: 169.09 E-value: 5.71e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 8 IEFKSVFKTYGDNTVVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGEDNTARPAhELRRSMGYVL 87
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPR-EVRRRIGIVF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 88 QQAGLMPHRTIVDNISTVPRLNGVSARQAKSQALELLNTVGLDEsFAKRYPSQLSGGQAQRVGVARALASESSILLMDEP 167
Cdd:cd03265 80 QDLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLE-AADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2735597802 168 FSAVDPVVRADLQKELLRLQSTLGRTIIFVTHDMDEAILLGDYVAVFARgGRIAQFGTPEEI 229
Cdd:cd03265 159 TIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDH-GRIIAEGTPEEL 219
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
7-225 |
2.06e-50 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 168.27 E-value: 2.06e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 7 AIEFKSVFKTYGDNTVVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGE--DNTARPAH----ELR 80
Cdd:COG4161 2 SIQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHqfDFSQKPSEkairLLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 81 RSMGYVLQQAGLMPHRTIVDNISTVP-RLNGVSARQAKSQALELLNTVGLDEsFAKRYPSQLSGGQAQRVGVARALASES 159
Cdd:COG4161 82 QKVGMVFQQYNLWPHLTVMENLIEAPcKVLGLSKEQAREKAMKLLARLRLTD-KADRFPLHLSGGQQQRVAIARALMMEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2735597802 160 SILLMDEPFSAVDPVVRADLQKELLRLQSTlGRTIIFVTHDMDEAILLGDYVaVFARGGRIAQFGT 225
Cdd:COG4161 161 QVLLFDEPTAALDPEITAQVVEIIRELSQT-GITQVIVTHEVEFARKVASQV-VYMEKGRIIEQGD 224
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
8-244 |
2.64e-50 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 167.62 E-value: 2.64e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 8 IEFKSVFKTYGDNTVvdNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGEDNTARPAHElrRSMGYVL 87
Cdd:COG3840 2 LRLDDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAE--RPVSMLF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 88 QQAGLMPHRTIVDNIS--TVPRLNgVSARQaKSQALELLNTVGLdESFAKRYPSQLSGGQAQRVGVARALASESSILLMD 165
Cdd:COG3840 78 QENNLFPHLTVAQNIGlgLRPGLK-LTAEQ-RAQVEQALERVGL-AGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLD 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2735597802 166 EPFSAVDPVVRADLQKELLRLQSTLGRTIIFVTHDMDEAILLGDYVAVFARgGRIAQFGTPEEILREPADDFVASFVGR 244
Cdd:COG3840 155 EPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVAD-GRIAADGPTAALLDGEPPPALAAYLGI 232
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
9-222 |
2.96e-50 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 165.69 E-value: 2.96e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 9 EFKSVFKTYGDNTVVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGEDNTARPAHELRRSMGYVlq 88
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYV-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 89 qaglmphrtivdnistvprlngvsarqakSQALELLNTvgldESFAKRYPSQLSGGQAQRVGVARALASESSILLMDEPF 168
Cdd:cd03214 79 -----------------------------PQALELLGL----AHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPT 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2735597802 169 SAVDPVVRADLQKELLRLQSTLGRTIIFVTHDMDEAILLGDYVAVFARGGRIAQ 222
Cdd:cd03214 126 SHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQ 179
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
27-247 |
3.21e-50 |
|
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: 171.44 E-value: 3.21e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 27 NLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGE---DNTAR---PAHelRRSMGYVLQQAGLMPHRTIVD 100
Cdd:COG4148 19 DFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEvlqDSARGiflPPH--RRRIGYVFQEARLFPHLSVRG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 101 NIS-TVPRLNGVSARQAKSQALELLntvGLdESFAKRYPSQLSGGQAQRVGVARALASESSILLMDEPFSAVDPVVRADL 179
Cdd:COG4148 97 NLLyGRKRAPRAERRISFDEVVELL---GI-GHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAEI 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2735597802 180 QKELLRLQSTLGRTIIFVTHDMDEAILLGDYVAVFaRGGRIAQFGTPEEILREPadDFVASFVGRDRG 247
Cdd:COG4148 173 LPYLERLRDELDIPILYVSHSLDEVARLADHVVLL-EQGRVVASGPLAEVLSRP--DLLPLAGGEEAG 237
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
7-225 |
3.40e-50 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 167.88 E-value: 3.40e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 7 AIEFKSVFKTYGDNTVVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGE--DNTARPA----HELR 80
Cdd:PRK11124 2 SIQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNhfDFSKTPSdkaiRELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 81 RSMGYVLQQAGLMPHRTIVDNISTVP-RLNGVSARQAKSQALELLNTVGLDEsFAKRYPSQLSGGQAQRVGVARALASES 159
Cdd:PRK11124 82 RNVGMVFQQYNLWPHLTVQQNLIEAPcRVLGLSKDQALARAEKLLERLRLKP-YADRFPLHLSGGQQQRVAIARALMMEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2735597802 160 SILLMDEPFSAVDPVVRADLQKELLRLQSTlGRTIIFVTHDMDEAILLGDYVaVFARGGRIAQFGT 225
Cdd:PRK11124 161 QVLLFDEPTAALDPEITAQIVSIIRELAET-GITQVIVTHEVEVARKTASRV-VYMENGHIVEQGD 224
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
8-243 |
5.39e-50 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 171.56 E-value: 5.39e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 8 IEFKSVFKTYGDNTVVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGEDNTARPAHelRRSMGYVL 87
Cdd:PRK11607 20 LEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPY--QRPINMMF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 88 QQAGLMPHRTIVDNISTVPRLNGVSARQAKSQALELLNTVGLDEsFAKRYPSQLSGGQAQRVGVARALASESSILLMDEP 167
Cdd:PRK11607 98 QSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQE-FAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEP 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2735597802 168 FSAVDPVVRADLQKELLRLQSTLGRTIIFVTHDMDEAILLGDYVAVFARgGRIAQFGTPEEILREPADDFVASFVG 243
Cdd:PRK11607 177 MGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNR-GKFVQIGEPEEIYEHPTTRYSAEFIG 251
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
8-217 |
9.59e-50 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 165.37 E-value: 9.59e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 8 IEFKSVFKTYGDNTVVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGEDNTARPAHELRRSMGYVL 87
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 88 QQAGLMPHrTIVDNISTVPRLNGVSARQAKsqALELLNTVGLDESFAKRYPSQLSGGQAQRVGVARALASESSILLMDEP 167
Cdd:COG4619 81 QEPALWGG-TVRDNLPFPFQLRERKFDRER--ALELLERLGLPPDILDKPVERLSGGERQRLALIRALLLQPDVLLLDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2735597802 168 FSAVDPVVRADLQKELLRLQSTLGRTIIFVTHDMDEAILLGDYVAVFARG 217
Cdd:COG4619 158 TSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAG 207
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
8-229 |
3.82e-49 |
|
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: 165.16 E-value: 3.82e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 8 IEFKSVFKTYGDNTVV-DNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGEDNTARPAHEL---RRSM 83
Cdd:TIGR02315 2 LEVENLSKVYPNGKQAlKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKLrklRRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 84 GYVLQQAGLMPHRTIVDNI--------STVPRLNGVSARQAKSQALELLNTVGLDESFAKRyPSQLSGGQAQRVGVARAL 155
Cdd:TIGR02315 82 GMIFQHYNLIERLTVLENVlhgrlgykPTWRSLLGRFSEEDKERALSALERVGLADKAYQR-ADQLSGGQQQRVAIARAL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2735597802 156 ASESSILLMDEPFSAVDPVVRADLQKELLRLQSTLGRTIIFVTHDMDEAILLGDYVaVFARGGRIAQFGTPEEI 229
Cdd:TIGR02315 161 AQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRI-VGLKAGEIVFDGAPSEL 233
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
8-217 |
9.51e-49 |
|
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: 161.78 E-value: 9.51e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 8 IEFKSVFKTYGDNT--VVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGEDNTARPAHELRRSMGY 85
Cdd:cd03228 1 IEFKNVSFSYPGRPkpVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 86 VLQQAGLMpHRTIVDNIstvprlngvsarqaksqalellntvgldesfakrypsqLSGGQAQRVGVARALASESSILLMD 165
Cdd:cd03228 81 VPQDPFLF-SGTIRENI--------------------------------------LSGGQRQRIAIARALLRDPPILILD 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2735597802 166 EPFSAVDPVVRADLQKELLRLqsTLGRTIIFVTHDMdEAILLGDYVAVFARG 217
Cdd:cd03228 122 EATSALDPETEALILEALRAL--AKGKTVIVIAHRL-STIRDADRIIVLDDG 170
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
7-241 |
1.32e-48 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 164.20 E-value: 1.32e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 7 AIEFKSVFKTYGDNTVVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGE--------DNTARPAHE 78
Cdd:COG4598 8 ALEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEeirlkpdrDGELVPADR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 79 -----LRRSMGYVLQQAGLMPHRTIVDNISTVP-RLNGVSARQAKSQALELLNTVGLDEsFAKRYPSQLSGGQAQRVGVA 152
Cdd:COG4598 88 rqlqrIRTRLGMVFQSFNLWSHMTVLENVIEAPvHVLGRPKAEAIERAEALLAKVGLAD-KRDAYPAHLSGGQQQRAAIA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 153 RALASESSILLMDEPFSAVDPvvraDLQKELLRLQSTL---GRTIIFVTHDMDEAILLGDYVaVFARGGRIAQFGTPEEI 229
Cdd:COG4598 167 RALAMEPEVMLFDEPTSALDP----ELVGEVLKVMRDLaeeGRTMLVVTHEMGFARDVSSHV-VFLHQGRIEEQGPPAEV 241
|
250
....*....|..
gi 2735597802 230 LREPADDFVASF 241
Cdd:COG4598 242 FGNPKSERLRQF 253
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
9-217 |
1.73e-48 |
|
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: 160.49 E-value: 1.73e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 9 EFKSVFKTYGDNTVVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGEDNTARPAHELRRSMGYVlq 88
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYV-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 89 qaglmphrtivdnistvprlngvsarqaksqalellntvgldesfakrypSQLSGGQAQRVGVARALASESSILLMDEPF 168
Cdd:cd00267 79 --------------------------------------------------PQLSGGQRQRVALARALLLNPDLLLLDEPT 108
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2735597802 169 SAVDPVVRADLQKELLRLQSTlGRTIIFVTHDMDEAILLGDYVAVFARG 217
Cdd:cd00267 109 SGLDPASRERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDG 156
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
25-224 |
2.40e-48 |
|
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: 162.08 E-value: 2.40e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 25 NLNLSIPEGkITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNG------EDNTARPAHelRRSMGYVLQQAGLMPHRTI 98
Cdd:cd03297 16 KIDFDLNEE-VTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGtvlfdsRKKINLPPQ--QRKIGLVFQQYALFPHLNV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 99 VDNISTVprLNGVSARQAKSQALELLNTVGLDEsFAKRYPSQLSGGQAQRVGVARALASESSILLMDEPFSAVDPVVRAD 178
Cdd:cd03297 93 RENLAFG--LKRKRNREDRISVDELLDLLGLDH-LLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQ 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2735597802 179 LQKELLRLQSTLGRTIIFVTHDMDEAILLGDYVAVFaRGGRIAQFG 224
Cdd:cd03297 170 LLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVM-EDGRLQYIG 214
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
8-222 |
1.23e-47 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 160.14 E-value: 1.23e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 8 IEFKSVFKTYGDNTVVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGEDNTArpahELRRSMGYVL 87
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDI----AARNRIGYLP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 88 QQAGLMPHRTIVDNISTVPRLNGVSARQAKSQALELLNTVGLDESFAKRYpSQLSGGQAQRVGVARALASESSILLMDEP 167
Cdd:cd03269 77 EERGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRV-EELSKGNQQKVQFIAAVIHDPELLILDEP 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2735597802 168 FSAVDPvVRADLQKELLRLQSTLGRTIIFVTHDMDEAILLGDYVAVFARGGRIAQ 222
Cdd:cd03269 156 FSGLDP-VNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLY 209
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
9-234 |
2.11e-47 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 160.97 E-value: 2.11e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 9 EFKSVFKTYGDNTVVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGEDNTARPAHEL-RRSMGYVL 87
Cdd:COG0411 6 EVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIaRLGIARTF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 88 QQAGLMPHRTIVDNI-------------STVPRLNGVSA--RQAKSQALELLNTVGLDEsFAKRYPSQLSGGQAQRVGVA 152
Cdd:COG0411 86 QNPRLFPELTVLENVlvaaharlgrgllAALLRLPRARReeREARERAEELLERVGLAD-RADEPAGNLSYGQQRRLEIA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 153 RALASESSILLMDEPFSAVDPVVRADLQKELLRLQSTLGRTIIFVTHDMDeAIL-LGDYVAVFARGGRIAQfGTPEEILR 231
Cdd:COG0411 165 RALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMD-LVMgLADRIVVLDFGRVIAE-GTPAEVRA 242
|
...
gi 2735597802 232 EPA 234
Cdd:COG0411 243 DPR 245
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
4-230 |
2.50e-47 |
|
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: 170.40 E-value: 2.50e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 4 LNNAIEFKSVFKTYGDNT--VVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGEDNTARPAHELRR 81
Cdd:COG2274 470 LKGDIELENVSFRYPGDSppVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRR 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 82 SMGYVLQQAGLMpHRTIVDNIstvpRLNGVSARQAksQALELLNTVGLDEsFAKRYP-----------SQLSGGQAQRVG 150
Cdd:COG2274 550 QIGVVLQDVFLF-SGTIRENI----TLGDPDATDE--EIIEAARLAGLHD-FIEALPmgydtvvgeggSNLSGGQRQRLA 621
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 151 VARALASESSILLMDEPFSAVDPVVRADLQKELLRLqsTLGRTIIFVTHDMdEAILLGDYVAVFARgGRIAQFGTPEEIL 230
Cdd:COG2274 622 IARALLRNPRILILDEATSALDAETEAIILENLRRL--LKGRTVIIIAHRL-STIRLADRIIVLDK-GRIVEDGTHEELL 697
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
23-234 |
3.09e-47 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 162.59 E-value: 3.09e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 23 VDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGEDNTARPAHEL---RRSMGYVLQ--QAGLMPHRT 97
Cdd:COG4608 34 VDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELrplRRRMQMVFQdpYASLNPRMT 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 98 IVDNISTVPRLNGV-SARQAKSQALELLNTVGLDESFAKRYPSQLSGGQAQRVGVARALASESSILLMDEPFSAVDPVVR 176
Cdd:COG4608 114 VGDIIAEPLRIHGLaSKAERRERVAELLELVGLRPEHADRYPHEFSGGQRQRIGIARALALNPKLIVCDEPVSALDVSIQ 193
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2735597802 177 A-------DLQKEllrlqstLGRTIIFVTHDmdeailLG------DYVAVFARgGRIAQFGTPEEILREPA 234
Cdd:COG4608 194 AqvlnlleDLQDE-------LGLTYLFISHD------LSvvrhisDRVAVMYL-GKIVEIAPRDELYARPL 250
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
23-169 |
7.26e-47 |
|
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: 156.27 E-value: 7.26e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 23 VDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGEDNTARPAHELRRSMGYVLQQAGLMPHRTIVDNI 102
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 103 STVPRLNGVSARQAKSQALELLNTVGLDE---SFAKRYPSQLSGGQAQRVGVARALASESSILLMDEPFS 169
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEALEKLGLGDladRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
17-222 |
2.57e-46 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 158.32 E-value: 2.57e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 17 YGDNTVVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGEdNTARPAHElrrsMGYVLQQAGLMPHR 96
Cdd:PRK11248 11 YGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGK-PVEGPGAE----RGVVFQNEGLLPWR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 97 TIVDNISTVPRLNGVSARQAKSQALELLNTVGLdESFAKRYPSQLSGGQAQRVGVARALASESSILLMDEPFSAVDPVVR 176
Cdd:PRK11248 86 NVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGL-EGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTR 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2735597802 177 ADLQKELLRLQSTLGRTIIFVTHDMDEAILLGDYVAVFARG-GRIAQ 222
Cdd:PRK11248 165 EQMQTLLLKLWQETGKQVLLITHDIEEAVFMATELVLLSPGpGRVVE 211
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
8-230 |
2.63e-46 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 158.36 E-value: 2.63e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 8 IEFKSVFKTYGDNT--VVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGEDnTARPAH--ELRRSM 83
Cdd:TIGR04520 1 IEVENVSFSYPESEkpALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLD-TLDEENlwEIRKKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 84 GYVLQQaglmPHRTIVDniSTV-------PRLNGVSARQAKSQALELLNTVGLdESFAKRYPSQLSGGQAQRVGVARALA 156
Cdd:TIGR04520 80 GMVFQN----PDNQFVG--ATVeddvafgLENLGVPREEMRKRVDEALKLVGM-EDFRDREPHLLSGGQKQRVAIAGVLA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2735597802 157 SESSILLMDEPFSAVDPVVRADLQKELLRLQSTLGRTIIFVTHDMDEAIlLGDYVAVFARGGRIAQfGTPEEIL 230
Cdd:TIGR04520 153 MRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEAV-LADRVIVMNKGKIVAE-GTPREIF 224
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
15-234 |
3.15e-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: 3.15e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 15 KTYGDNTVVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGEDNTARPAHEL-RRSMGYVLQQAGLM 93
Cdd:cd03219 8 KRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIaRLGIGRTFQIPRLF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 94 PHRTIVDNI----------STVPRLNGVSARQAKSQALELLNTVGLDEsFAKRYPSQLSGGQAQRVGVARALASESSILL 163
Cdd:cd03219 88 PELTVLENVmvaaqartgsGLLLARARREEREARERAEELLERVGLAD-LADRPAGELSYGQQRRLEIARALATDPKLLL 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2735597802 164 MDEPFSAVDPVVRADLqKELLRLQSTLGRTIIFVTHDMDEAILLGDYVAVFARGGRIAQfGTPEEILREPA 234
Cdd:cd03219 167 LDEPAAGLNPEETEEL-AELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAE-GTPDEVRNNPR 235
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
7-232 |
1.75e-45 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 163.39 E-value: 1.75e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 7 AIEFKSV-FKTYGDNTVVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGEDNTARPAHELRRSMGY 85
Cdd:COG4988 336 SIELEDVsFSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAW 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 86 VLQQAGLmPHRTIVDNIstvpRLngvSARQAKSQAL-ELLNTVGLDEsFAKRYP-----------SQLSGGQAQRVGVAR 153
Cdd:COG4988 416 VPQNPYL-FAGTIRENL----RL---GRPDASDEELeAALEAAGLDE-FVAALPdgldtplgeggRGLSGGQAQRLALAR 486
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2735597802 154 ALASESSILLMDEPFSAVDPVVRADLQKELLRLqsTLGRTIIFVTHDMdEAILLGDYVAVFaRGGRIAQFGTPEEILRE 232
Cdd:COG4988 487 ALLRDAPLLLLDEPTAHLDAETEAEILQALRRL--AKGRTVILITHRL-ALLAQADRILVL-DDGRIVEQGTHEELLAK 561
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
9-224 |
9.85e-45 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 152.69 E-value: 9.85e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 9 EFKSVFKTYGDNTVVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGedntaRPAHELRRSMGYVLQ 88
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFG-----KPLEKERKRIGYVPQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 89 QA----------------GLMPHRTIVDNIStvprlngvsaRQAKSQALELLNTVGLDEsFAKRYPSQLSGGQAQRVGVA 152
Cdd:cd03235 76 RRsidrdfpisvrdvvlmGLYGHKGLFRRLS----------KADKAKVDEALERVGLSE-LADRQIGELSGGQQQRVLLA 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2735597802 153 RALASESSILLMDEPFSAVDPVVRADLqKELLRLQSTLGRTIIFVTHDMDEAILLGDYVAVFARggRIAQFG 224
Cdd:cd03235 145 RALVQDPDLLLLDEPFAGVDPKTQEDI-YELLRELRREGMTILVVTHDLGLVLEYFDRVLLLNR--TVVASG 213
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
8-202 |
2.31e-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: 151.79 E-value: 2.31e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 8 IEFKSVFKTYGDNTV-VDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGEDNT---ARPAHELRRSM 83
Cdd:cd03292 1 IEFINVTKTYPNGTAaLDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSdlrGRAIPYLRRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 84 GYVLQQAGLMPHRTIVDNISTVPRLNGVSARQAKSQALELLNTVGLdESFAKRYPSQLSGGQAQRVGVARALASESSILL 163
Cdd:cd03292 81 GVVFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGL-SHKHRALPAELSGGEQQRVAIARAIVNSPTILI 159
|
170 180 190
....*....|....*....|....*....|....*....
gi 2735597802 164 MDEPFSAVDPVVRADLQkELLRLQSTLGRTIIFVTHDMD 202
Cdd:cd03292 160 ADEPTGNLDPDTTWEIM-NLLKKINKAGTTVVVATHAKE 197
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
11-201 |
7.35e-44 |
|
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: 150.07 E-value: 7.35e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 11 KSVFKTYGDNTVVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGEDN---TARPAHELRRS-MGYV 86
Cdd:TIGR03608 2 KNISKKFGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETpplNSKKASKFRREkLGYL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 87 LQQAGLMPHRTIVDNIStVP----RLNGVSARQAKSQALEllnTVGLDESFaKRYPSQLSGGQAQRVGVARALASESSIL 162
Cdd:TIGR03608 82 FQNFALIENETVEENLD-LGlkykKLSKKEKREKKKEALE---KVGLNLKL-KQKIYELSGGEQQRVALARAILKPPPLI 156
|
170 180 190
....*....|....*....|....*....|....*....
gi 2735597802 163 LMDEPFSAVDPVVRADLQKELLRLQSTlGRTIIFVTHDM 201
Cdd:TIGR03608 157 LADEPTGSLDPKNRDEVLDLLLELNDE-GKTIIIVTHDP 194
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
6-247 |
2.29e-43 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 150.29 E-value: 2.29e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 6 NAIEFKSVFKTYGDNTVVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILV-NGEDNTARP-------AH 77
Cdd:PRK11264 2 SAIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVgDITIDTARSlsqqkglIR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 78 ELRRSMGYVLQQAGLMPHRTIVDNISTVPRL-NGVSARQAKSQALELLNTVGLdESFAKRYPSQLSGGQAQRVGVARALA 156
Cdd:PRK11264 82 QLRQHVGFVFQNFNLFPHRTVLENIIEGPVIvKGEPKEEATARARELLAKVGL-AGKETSYPRRLSGGQQQRVAIARALA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 157 SESSILLMDEPFSAVDPvvraDLQKELLRLQSTLG---RTIIFVTHDMDEAILLGDYvAVFARGGRIAQFGTPEEILREP 233
Cdd:PRK11264 161 MRPEVILFDEPTSALDP----ELVGEVLNTIRQLAqekRTMVIVTHEMSFARDVADR-AIFMDQGRIVEQGPAKALFADP 235
|
250
....*....|....
gi 2735597802 234 ADDFVASFVGRDRG 247
Cdd:PRK11264 236 QQPRTRQFLEKFLL 249
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
8-224 |
2.64e-43 |
|
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: 148.88 E-value: 2.64e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 8 IEFKSVFKTYGDNTVVDNLNLSIPEGkITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGEDNTARPaHELRRSMGYVL 87
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQP-QKLRRRIGYLP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 88 QQAGLMPHRTIVDNISTVPRLNGVSARQAKSQALELLNTVGLDEsFAKRYPSQLSGGQAQRVGVARALASESSILLMDEP 167
Cdd:cd03264 79 QEFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGD-RAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2735597802 168 FSAVDPVVRADLqKELLRLQSTlGRTIIFVTHDMDEAILLGDYVAVFArGGRIAQFG 224
Cdd:cd03264 158 TAGLDPEERIRF-RNLLSELGE-DRIVILSTHIVEDVESLCNQVAVLN-KGKLVFEG 211
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
2-232 |
4.87e-43 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 156.86 E-value: 4.87e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 2 SVLNNAIEFKSVFKTYGDNT-VVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGEDNTARPAHELR 80
Cdd:COG1132 334 PPVRGEIEFENVSFSYPGDRpVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESLR 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 81 RSMGYVLQQAGLMpHRTIVDNIstvpRLNGVSARQAK-SQALELlntVGLDEsFAKRYP-----------SQLSGGQAQR 148
Cdd:COG1132 414 RQIGVVPQDTFLF-SGTIRENI----RYGRPDATDEEvEEAAKA---AQAHE-FIEALPdgydtvvgergVNLSGGQRQR 484
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 149 VGVARALASESSILLMDEPFSAVDPVVRADLQKELLRLqsTLGRTIIFVTH------DMDEAILLgdyvavfaRGGRIAQ 222
Cdd:COG1132 485 IAIARALLKDPPILILDEATSALDTETEALIQEALERL--MKGRTTIVIAHrlstirNADRILVL--------DDGRIVE 554
|
250
....*....|
gi 2735597802 223 FGTPEEILRE 232
Cdd:COG1132 555 QGTHEELLAR 564
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
5-233 |
1.62e-42 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 148.58 E-value: 1.62e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 5 NNAIEFKSVFKTYGDNTVVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGEDNT------------ 72
Cdd:PRK10619 3 ENKLNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgqlkva 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 73 -ARPAHELRRSMGYVLQQAGLMPHRTIVDNISTVP-RLNGVSARQAKSQALELLNTVGLDESFAKRYPSQLSGGQAQRVG 150
Cdd:PRK10619 83 dKNQLRLLRTRLTMVFQHFNLWSHMTVLENVMEAPiQVLGLSKQEARERAVKYLAKVGIDERAQGKYPVHLSGGQQQRVS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 151 VARALASESSILLMDEPFSAVDPvvraDLQKELLRLQSTL---GRTIIFVTHDMDEAILLGDYVaVFARGGRIAQFGTPE 227
Cdd:PRK10619 163 IARALAMEPEVLLFDEPTSALDP----ELVGEVLRIMQQLaeeGKTMVVVTHEMGFARHVSSHV-IFLHQGKIEEEGAPE 237
|
....*.
gi 2735597802 228 EILREP 233
Cdd:PRK10619 238 QLFGNP 243
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
6-242 |
1.64e-42 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 148.14 E-value: 1.64e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 6 NAIEFKSVFKTYGDNTVVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVE-----HTSGTILVNGEDNTARPAHELR 80
Cdd:PRK14247 2 NKIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElypeaRVSGEVYLDGQDIFKMDVIELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 81 RSMGYVLQQAGLMPHRTIVDNISTVPRLNGV--SARQAKSQALELLNTVGLDESFAKRY---PSQLSGGQAQRVGVARAL 155
Cdd:PRK14247 82 RRVQMVFQIPNPIPNLSIFENVALGLKLNRLvkSKKELQERVRWALEKAQLWDEVKDRLdapAGKLSGGQQQRLCIARAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 156 ASESSILLMDEPFSAVDPVVRADLQKELLRLQSTLgrTIIFVTHDMDEAILLGDYVAvFARGGRIAQFGTPEEILREPAD 235
Cdd:PRK14247 162 AFQPEVLLADEPTANLDPENTAKIESLFLELKKDM--TIVLVTHFPQQAARISDYVA-FLYKGQIVEWGPTREVFTNPRH 238
|
....*..
gi 2735597802 236 DFVASFV 242
Cdd:PRK14247 239 ELTEKYV 245
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-242 |
2.40e-42 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 147.68 E-value: 2.40e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 4 LNNAIEFKSVFKTYGDNTVVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVE-----HTSGTILVNGED--NTARPA 76
Cdd:PRK14267 1 MKFAIETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElneeaRVEGEVRLFGRNiySPDVDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 77 HELRRSMGYVLQQAGLMPHRTIVDNISTVPRLNG-VSARQAKSQALE-LLNTVGLDESFAKR---YPSQLSGGQAQRVGV 151
Cdd:PRK14267 81 IEVRREVGMVFQYPNPFPHLTIYDNVAIGVKLNGlVKSKKELDERVEwALKKAALWDEVKDRlndYPSNLSGGQRQRLVI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 152 ARALASESSILLMDEPFSAVDPVVRADLQKELLRLQSTLgrTIIFVTHDMDEAILLGDYVAvFARGGRIAQFGTPEEILR 231
Cdd:PRK14267 161 ARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEY--TIVLVTHSPAQAARVSDYVA-FLYLGKLIEVGPTRKVFE 237
|
250
....*....|.
gi 2735597802 232 EPADDFVASFV 242
Cdd:PRK14267 238 NPEHELTEKYV 248
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
8-233 |
9.54e-42 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 146.00 E-value: 9.54e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 8 IEFKSVFKTYGDNTVVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGEDNTARPAHELRRSMGyVL 87
Cdd:COG4604 2 IEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLA-IL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 88 QQAGLMPHRTivdnisTV---------P----RLNgVSARQAKSQALELLNtvgLdESFAKRYPSQLSGGQAQRVGVARA 154
Cdd:COG4604 81 RQENHINSRL------TVrelvafgrfPyskgRLT-AEDREIIDEAIAYLD---L-EDLADRYLDELSGGQRQRAFIAMV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 155 LASESSILLMDEPFSAVDPVVRADLQKELLRLQSTLGRTIIFVTHDMDEAILLGDY-VAVfaRGGRIAQFGTPEEILREP 233
Cdd:COG4604 150 LAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHiVAM--KDGRVVAQGTPEEIITPE 227
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
8-211 |
1.52e-40 |
|
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: 141.46 E-value: 1.52e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 8 IEFKSVFKTYGDNTVVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGEDNTARPAhELRRSMGYVL 87
Cdd:COG4133 3 LEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDARE-DYRRRLAYLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 88 QQAGLMPHRTIVDNISTVPRLNGVSARQAksQALELLNTVGLdESFAKRYPSQLSGGQAQRVGVARALASESSILLMDEP 167
Cdd:COG4133 82 HADGLKPELTVRENLRFWAALYGLRADRE--AIDEALEAVGL-AGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEP 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2735597802 168 FSAVDPVVRADLQkELLRLQSTLGRTIIFVTHD-----MDEAILLGDYV 211
Cdd:COG4133 159 FTALDAAGVALLA-ELIAAHLARGGAVLLTTHQplelaAARVLDLGDFK 206
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
8-230 |
3.38e-40 |
|
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: 141.21 E-value: 3.38e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 8 IEFKSVFKTY-GDNTVVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGEDNTARPAHELRRSMGYV 86
Cdd:cd03254 3 IEFENVNFSYdEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMIGVV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 87 LQQAGLMPhRTIVDNIstvpRLNGVSARQAKSQalELLNTVGLDEsFAKRYP-----------SQLSGGQAQRVGVARAL 155
Cdd:cd03254 83 LQDTFLFS-GTIMENI----RLGRPNATDEEVI--EAAKEAGAHD-FIMKLPngydtvlgengGNLSQGERQLLAIARAM 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 156 ASESSILLMDEPFSAVDPVVRADLQKELLRLQStlGRTIIFVTH------DMDEAILLgdyvavfaRGGRIAQFGTPEEI 229
Cdd:cd03254 155 LRDPKILILDEATSNIDTETEKLIQEALEKLMK--GRTSIIIAHrlstikNADKILVL--------DDGKIIEEGTHDEL 224
|
.
gi 2735597802 230 L 230
Cdd:cd03254 225 L 225
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
8-235 |
3.40e-40 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 143.24 E-value: 3.40e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 8 IEFKSVFKTYGDNT-----VVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTI------LVNGEDNTA-RP 75
Cdd:PRK13634 3 ITFQKVEHRYQYKTpferrALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVtigervITAGKKNKKlKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 76 aheLRRSMGYVLQ--QAGLMpHRTIVDNISTVPRLNGVSARQAKSQALELLNTVGLDESFAKRYPSQLSGGQAQRVGVAR 153
Cdd:PRK13634 83 ---LRKKVGIVFQfpEHQLF-EETVEKDICFGPMNFGVSEEDAKQKAREMIELVGLPEELLARSPFELSGGQMRRVAIAG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 154 ALASESSILLMDEPFSAVDPVVRADLQKELLRLQSTLGRTIIFVTHDMDEAILLGDYVAVFARGGrIAQFGTPEEILREP 233
Cdd:PRK13634 159 VLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGT-VFLQGTPREIFADP 237
|
..
gi 2735597802 234 AD 235
Cdd:PRK13634 238 DE 239
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
7-234 |
3.66e-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: 148.76 E-value: 3.66e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 7 AIEFKSVFKTY--GDNTVVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGEDNTARPAHELRRSMG 84
Cdd:COG4987 333 SLELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRRIA 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 85 YVLQQAGLMpHRTIVDNIstvpRLngvsARQAKS--QALELLNTVGLDEsFAKRYP-----------SQLSGGQAQRVGV 151
Cdd:COG4987 413 VVPQRPHLF-DTTLRENL----RL----ARPDATdeELWAALERVGLGD-WLAALPdgldtwlgeggRRLSGGERRRLAL 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 152 ARALASESSILLMDEPFSAVDPVVRADLQKELLRLqsTLGRTIIFVTHD------MDEAILLGDyvavfargGRIAQFGT 225
Cdd:COG4987 483 ARALLRDAPILLLDEPTEGLDAATEQALLADLLEA--LAGRTVLLITHRlaglerMDRILVLED--------GRIVEQGT 552
|
....*....
gi 2735597802 226 PEEILREPA 234
Cdd:COG4987 553 HEELLAQNG 561
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
17-232 |
4.87e-40 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 141.69 E-value: 4.87e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 17 YGDNTVVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGEDNTARPAHELRRSMGYVLQQAgLMPHR 96
Cdd:PRK11231 12 YGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQHH-LTPEG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 97 TIVDNISTV---PRLN-----GVSARQAKSQALELLNTvgldESFAKRYPSQLSGGQAQRVGVARALASESSILLMDEPF 168
Cdd:PRK11231 91 ITVRELVAYgrsPWLSlwgrlSAEDNARVNQAMEQTRI----NHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPT 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2735597802 169 SAVDPVVRADLQKeLLRLQSTLGRTIIFVTHDMDEAILLGDYVAVFARGGRIAQfGTPEEILRE 232
Cdd:PRK11231 167 TYLDINHQVELMR-LMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQ-GTPEEVMTP 228
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
23-232 |
5.82e-40 |
|
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: 147.64 E-value: 5.82e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 23 VDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVN-GED--NTARPAHELR----RSMGYVLQQAGLMPH 95
Cdd:TIGR03269 300 VDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRvGDEwvDMTKPGPDGRgrakRYIGILHQEYDLYPH 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 96 RTIVDNISTVPRLNgVSARQAKSQALELLNTVGLDESFAK----RYPSQLSGGQAQRVGVARALASESSILLMDEPFSAV 171
Cdd:TIGR03269 380 RTVLDNLTEAIGLE-LPDELARMKAVITLKMVGFDEEKAEeildKYPDELSEGERHRVALAQVLIKEPRIVILDEPTGTM 458
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2735597802 172 DPVVRADLQKELLRLQSTLGRTIIFVTHDMDEAILLGDYVAVFaRGGRIAQFGTPEEILRE 232
Cdd:TIGR03269 459 DPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALM-RDGKIVKIGDPEEIVEE 518
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
8-224 |
6.61e-40 |
|
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: 139.94 E-value: 6.61e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 8 IEFKSVFKTYGDNTVvdNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGEDNTARPAHELRRSMgyVL 87
Cdd:cd03298 1 VRLDKIRFSYGEQPM--HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRPVSM--LF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 88 QQAGLMPHRTIVDNI--STVPRLNgvsARQAKSQALE-LLNTVGLDEsFAKRYPSQLSGGQAQRVGVARALASESSILLM 164
Cdd:cd03298 77 QENNLFAHLTVEQNVglGLSPGLK---LTAEDRQAIEvALARVGLAG-LEKRLPGELSGGERQRVALARVLVRDKPVLLL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 165 DEPFSAVDPVVRADLQKELLRLQSTLGRTIIFVTHDMDEAILLGDYVaVFARGGRIAQFG 224
Cdd:cd03298 153 DEPFAALDPALRAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRV-VFLDNGRIAAQG 211
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
11-211 |
1.27e-39 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 140.58 E-value: 1.27e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 11 KSVFKTYGDNTVVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNgedntARPAHELRRSMGYVLQQA 90
Cdd:PRK11247 16 NAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAG-----TAPLAEAREDTRLMFQDA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 91 GLMPHRTIVDNISTvpRLNGvsarQAKSQALELLNTVGLdESFAKRYPSQLSGGQAQRVGVARALASESSILLMDEPFSA 170
Cdd:PRK11247 91 RLLPWKKVIDNVGL--GLKG----QWRDAALQALAAVGL-ADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGA 163
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2735597802 171 VDPVVRADLQKELLRLQSTLGRTIIFVTHDMDEAILLGDYV 211
Cdd:PRK11247 164 LDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRV 204
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
17-244 |
1.39e-39 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 141.07 E-value: 1.39e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 17 YGDNTVVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVE-----HTSGTILVNGEDNTAR---PAhELRRSMGYVLQ 88
Cdd:PRK14243 20 YGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDlipgfRVEGKVTFHGKNLYAPdvdPV-EVRRRIGMVFQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 89 QAGLMPhRTIVDNISTVPRLNGV----------SARQAK--SQALELLNTVGLdesfakrypsQLSGGQAQRVGVARALA 156
Cdd:PRK14243 99 KPNPFP-KSIYDNIAYGARINGYkgdmdelverSLRQAAlwDEVKDKLKQSGL----------SLSGGQQQRLCIARAIA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 157 SESSILLMDEPFSAVDPVVRADLQkELLRlqsTLGR--TIIFVTHDMDEAILLGDYVAVF--------ARGGRIAQFGTP 226
Cdd:PRK14243 168 VQPEVILMDEPCSALDPISTLRIE-ELMH---ELKEqyTIIIVTHNMQQAARVSDMTAFFnvelteggGRYGYLVEFDRT 243
|
250
....*....|....*....
gi 2735597802 227 EEILREPADDFVASFV-GR 244
Cdd:PRK14243 244 EKIFNSPQQQATRDYVsGR 262
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
15-234 |
2.16e-39 |
|
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: 142.94 E-value: 2.16e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 15 KTYGDNTVvdNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGE---DNTAR---PAHelRRSMGYVLQ 88
Cdd:TIGR02142 7 KRLGDFSL--DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRtlfDSRKGiflPPE--KRRIGYVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 89 QAGLMPHRTIVDNIS-TVPRLNGVSARQAKSQALELLNTvgldESFAKRYPSQLSGGQAQRVGVARALASESSILLMDEP 167
Cdd:TIGR02142 83 EARLFPHLSVRGNLRyGMKRARPSERRISFERVIELLGI----GHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2735597802 168 FSAVDPVVRADLQKELLRLQSTLGRTIIFVTHDMDEAILLGDYVAVFaRGGRIAQFGTPEEILREPA 234
Cdd:TIGR02142 159 LAALDDPRKYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVL-EDGRVAAAGPIAEVWASPD 224
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
8-217 |
3.18e-39 |
|
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: 138.12 E-value: 3.18e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 8 IEFKSVFKTYGDNTVVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGeDNTARPAHELRRsMGYVL 87
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDG-KSYQKNIEALRR-IGALI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 88 QQAGLMPHRTIVDNISTVPRLNGVSarqaKSQALELLNTVGLDESfAKRYPSQLSGGQAQRVGVARALASESSILLMDEP 167
Cdd:cd03268 79 EAPGFYPNLTARENLRLLARLLGIR----KKRIDEVLDVVGLKDS-AKKKVKGFSLGMKQRLGIALALLGNPDLLILDEP 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2735597802 168 FSAVDPVVRADLQKELLRLQSTlGRTIIFVTHDMDEAILLGDYVAVFARG 217
Cdd:cd03268 154 TNGLDPDGIKELRELILSLRDQ-GITVLISSHLLSEIQKVADRIGIINKG 202
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
8-202 |
4.00e-39 |
|
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: 138.15 E-value: 4.00e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 8 IEFKSVFKTYGDNT-VVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGEDNTARPAHE---LRRSM 83
Cdd:TIGR02673 2 IEFHNVSKAYPGGVaALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLRGRQlplLRRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 84 GYVLQQAGLMPHRTIVDNISTVPRLNGVSARQAKSQALELLNTVGLDESfAKRYPSQLSGGQAQRVGVARALASESSILL 163
Cdd:TIGR02673 82 GVVFQDFRLLPDRTVYENVALPLEVRGKKEREIQRRVGAALRQVGLEHK-ADAFPEQLSGGEQQRVAIARAIVNSPPLLL 160
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2735597802 164 MDEPFSAVDPvvraDLQKELLRLQSTL---GRTIIFVTHDMD 202
Cdd:TIGR02673 161 ADEPTGNLDP----DLSERILDLLKRLnkrGTTVIVATHDLS 198
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
11-233 |
1.84e-38 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 137.08 E-value: 1.84e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 11 KSVFKTYGDNTVVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGEDNTARPAHE-LRRSMGYVLQQ 89
Cdd:COG1137 7 ENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMHKrARLGIGYLPQE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 90 AGLMPHRTIVDNISTVPRLNGVSARQAKSQALELLNTVGLdESFAKRYPSQLSGGQAQRVGVARALASESSILLMDEPFS 169
Cdd:COG1137 87 ASIFRKLTVEDNILAVLELRKLSKKEREERLEELLEEFGI-THLRKSKAYSLSGGERRRVEIARALATNPKFILLDEPFA 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2735597802 170 AVDPVVRADLQKELLRLQStlgRTI-IFVT-HDMDEAILLGDYVAVFaRGGRIAQFGTPEEILREP 233
Cdd:COG1137 166 GVDPIAVADIQKIIRHLKE---RGIgVLITdHNVRETLGICDRAYII-SEGKVLAEGTPEEILNNP 227
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
23-217 |
1.88e-38 |
|
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: 136.83 E-value: 1.88e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 23 VDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGEDNTaRPAHElrRSMgyVLQQAGLMPHRTIVDNI 102
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQIT-EPGPD--RMV--VFQNYSLLPWLTVRENI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 103 -----STVPRLNGVSARQAKSQALELlntVGLDESfAKRYPSQLSGGQAQRVGVARALASESSILLMDEPFSAVDPVVRA 177
Cdd:TIGR01184 76 alavdRVLPDLSKSERRAIVEEHIAL---VGLTEA-ADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRG 151
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2735597802 178 DLQKELLRLQSTLGRTIIFVTHDMDEAILLGDYVAVFARG 217
Cdd:TIGR01184 152 NLQEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
5-242 |
2.46e-38 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 137.59 E-value: 2.46e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 5 NNAIEFKSVFKTYGDNTVVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGEDNTARPAHEL---RR 81
Cdd:PRK11831 5 ANLVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLytvRK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 82 SMGYVLQQAGLMPHRTIVDNISTVPRLNG-VSARQAKSQALELLNTVGLDESfAKRYPSQLSGGQAQRVGVARALASESS 160
Cdd:PRK11831 85 RMSMLFQSGALFTDMNVFDNVAYPLREHTqLPAPLLHSTVMMKLEAVGLRGA-AKLMPSELSGGMARRAALARAIALEPD 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 161 ILLMDEPFSAVDPVVRADLQKELLRLQSTLGRTIIFVTHDMDEAILLGDYVAVFARGGRIAQfGTPEEiLREPADDFVAS 240
Cdd:PRK11831 164 LIMFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAH-GSAQA-LQANPDPRVRQ 241
|
..
gi 2735597802 241 FV 242
Cdd:PRK11831 242 FL 243
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
12-234 |
2.57e-38 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 137.21 E-value: 2.57e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 12 SVFktYGDNTVVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVE-----HTSGTILVNGEDNTARPAH--ELRRSMG 84
Cdd:PRK14239 12 SVY--YNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDlnpevTITGSIVYNGHNIYSPRTDtvDLRKEIG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 85 YVLQQAGLMPHrTIVDNISTVPRLNGVSARQAKSQALE--LLNTVGLDESFAKRYPSQ--LSGGQAQRVGVARALASESS 160
Cdd:PRK14239 90 MVFQQPNPFPM-SIYENVVYGLRLKGIKDKQVLDEAVEksLKGASIWDEVKDRLHDSAlgLSGGQQQRVCIARVLATSPK 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2735597802 161 ILLMDEPFSAVDPVVRADLQKELLRLQSTLgrTIIFVTHDMDEAILLGDYVAVFArGGRIAQFGTPEEILREPA 234
Cdd:PRK14239 169 IILLDEPTSALDPISAGKIEETLLGLKDDY--TMLLVTRSMQQASRISDRTGFFL-DGDLIEYNDTKQMFMNPK 239
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
7-230 |
3.56e-38 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 138.40 E-value: 3.56e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 7 AIEFKSVFKTYGDNTVVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGEDNTARpAHELRRSMGYV 86
Cdd:PRK13537 7 PIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSR-ARHARQRVGVV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 87 LQQAGLMPHRTIVDNISTVPRLNGVSARQAKSQALELLNTVGLdESFAKRYPSQLSGGQAQRVGVARALASESSILLMDE 166
Cdd:PRK13537 86 PQFDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKL-ENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDE 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2735597802 167 PFSAVDPVVRaDLQKELLRLQSTLGRTIIFVTHDMDEAILLGDYVAVFARGGRIAQfGTPEEIL 230
Cdd:PRK13537 165 PTTGLDPQAR-HLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAE-GAPHALI 226
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
19-242 |
8.04e-38 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 135.95 E-value: 8.04e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 19 DNTVVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVE------HTSGTILVNGEDNTARPAHELRRSMGYVLQQAGL 92
Cdd:PRK14246 22 DKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiydskiKVDGKVLYFGKDIFQIDAIKLRKEVGMVFQQPNP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 93 MPHRTIVDNISTVPRLNGVS-ARQAKSQALELLNTVGLDESFAKRY---PSQLSGGQAQRVGVARALASESSILLMDEPF 168
Cdd:PRK14246 102 FPHLSIYDNIAYPLKSHGIKeKREIKKIVEECLRKVGLWKEVYDRLnspASQLSGGQQQRLTIARALALKPKVLLMDEPT 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2735597802 169 SAVDPVVRADLQKELLRLQSTLgrTIIFVTHDMDEAILLGDYVAvFARGGRIAQFGTPEEILREPADDFVASFV 242
Cdd:PRK14246 182 SMIDIVNSQAIEKLITELKNEI--AIVIVSHNPQQVARVADYVA-FLYNGELVEWGSSNEIFTSPKNELTEKYV 252
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
8-230 |
9.60e-38 |
|
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: 135.36 E-value: 9.60e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 8 IEFKSVFKTY---GDNTVVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGEDNTARPAHELRRSMG 84
Cdd:cd03249 1 IEFKNVSFRYpsrPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 85 YVLQQAGLMPhRTIVDNIS-TVPRLNGVSARQAKSQAlELLNTVgldESFAKRYP-------SQLSGGQAQRVGVARALA 156
Cdd:cd03249 81 LVSQEPVLFD-GTIAENIRyGKPDATDEEVEEAAKKA-NIHDFI---MSLPDGYDtlvgergSQLSGGQKQRIAIARALL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2735597802 157 SESSILLMDEPFSAVDPVVRADLQKELLRLqsTLGRTIIFVTHDMdEAILLGDYVAVFaRGGRIAQFGTPEEIL 230
Cdd:cd03249 156 RNPKILLLDEATSALDAESEKLVQEALDRA--MKGRTTIVIAHRL-STIRNADLIAVL-QNGQVVEQGTHDELM 225
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
17-232 |
2.19e-37 |
|
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: 133.71 E-value: 2.19e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 17 YGDNTVVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGEDNTARPAHE-LRRSMGYVLQQAGLMPH 95
Cdd:cd03224 10 YGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHErARAGIGYVPEGRRIFPE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 96 RTIVDNISTVPRLNGVSARQAK-SQALELLNTvgLDEsFAKRYPSQLSGGQAQRVGVARALASESSILLMDEPFSAVDPV 174
Cdd:cd03224 90 LTVEENLLLGAYARRRAKRKARlERVYELFPR--LKE-RRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLAPK 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2735597802 175 VRADLQKELLRLQSTlGRTIIFVTHDMDEAILLGDYVAVFARgGRIAQFGTPEEILRE 232
Cdd:cd03224 167 IVEEIFEAIRELRDE-GVTILLVEQNARFALEIADRAYVLER-GRVVLEGTAAELLAD 222
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
15-234 |
2.42e-37 |
|
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: 133.82 E-value: 2.42e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 15 KTYGDNTVVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGEDNTARPAHE-LRRSMGYVLQQAGLM 93
Cdd:cd03218 8 KRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKrARLGIGYLPQEASIF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 94 PHRTIVDNISTVPRLNGVSARQAKSQALELLNTVGLdESFAKRYPSQLSGGQAQRVGVARALASESSILLMDEPFSAVDP 173
Cdd:cd03218 88 RKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHI-THLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVDP 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2735597802 174 VVRADLQKELLRL-QSTLGrtiIFVT-HDMDEAILLGDYVAVFaRGGRIAQFGTPEEILREPA 234
Cdd:cd03218 167 IAVQDIQKIIKILkDRGIG---VLITdHNVRETLSITDRAYII-YEGKVLAEGTPEEIAANEL 225
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
14-236 |
3.29e-37 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 140.20 E-value: 3.29e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 14 FKTYGDNTVVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEhTSGTILVNGEDNTARPAHE---LRRSMGYVLQQ- 89
Cdd:COG4172 293 RRTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIP-SEGEIRFDGQDLDGLSRRAlrpLRRRMQVVFQDp 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 90 -AGLMPHRTIVDNIS---TVPRLnGVSARQAKSQALELLNTVGLDESFAKRYPSQLSGGQAQRVGVARALASESSILLMD 165
Cdd:COG4172 372 fGSLSPRMTVGQIIAeglRVHGP-GLSAAERRARVAEALEEVGLDPAARHRYPHEFSGGQRQRIAIARALILEPKLLVLD 450
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2735597802 166 EPFSAVDPVVRADLQKELLRLQSTLGRTIIFVTHDMDEAILLGDYVAVFaRGGRIAQFGTPEEILREPADD 236
Cdd:COG4172 451 EPTSALDVSVQAQILDLLRDLQREHGLAYLFISHDLAVVRALAHRVMVM-KDGKVVEQGPTEQVFDAPQHP 520
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
7-233 |
3.75e-37 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 134.96 E-value: 3.75e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 7 AIEFKSVFKTYGDNTV-----VDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGEDNTARPAH---- 77
Cdd:PRK13641 2 SIKFENVDYIYSPGTPmekkgLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNknlk 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 78 ELRRSMGYVLQ--QAGLMpHRTIVDNISTVPRLNGVSARQAKSQALELLNTVGLDESFAKRYPSQLSGGQAQRVGVARAL 155
Cdd:PRK13641 82 KLRKKVSLVFQfpEAQLF-ENTVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLSEDLISKSPFELSGGQMRRVAIAGVM 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2735597802 156 ASESSILLMDEPFSAVDPVVRADLQKELLRLQSTlGRTIIFVTHDMDEAILLGDYVAVFARgGRIAQFGTPEEILREP 233
Cdd:PRK13641 161 AYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKA-GHTVILVTHNMDDVAEYADDVLVLEH-GKLIKHASPKEIFSDK 236
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
16-204 |
7.05e-37 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 132.22 E-value: 7.05e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 16 TYGDNTVVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVE---HTSGTILVNGEDNTARPAHelRRSMGYVLQQAGL 92
Cdd:COG4136 10 TLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSpafSASGEVLLNGRRLTALPAE--QRRIGILFQDDLL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 93 MPHRTIVDNIS-TVPrlNGVSARQAKSQALELLNTVGLDeSFAKRYPSQLSGGQAQRVGVARALASESSILLMDEPFSAV 171
Cdd:COG4136 88 FPHLSVGENLAfALP--PTIGRAQRRARVEQALEEAGLA-GFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKL 164
|
170 180 190
....*....|....*....|....*....|....*.
gi 2735597802 172 DPVVRADLQK---ELLRlqsTLGRTIIFVTHDMDEA 204
Cdd:COG4136 165 DAALRAQFREfvfEQIR---QRGIPALLVTHDEEDA 197
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
18-236 |
7.05e-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: 139.43 E-value: 7.05e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 18 GDNTVVDNLNLSIPEGKITVFVGPSGCGKTTS----LRMINRMVEHTSGTILVNGEDNTARPAHELRR----SMGYVLQQ 89
Cdd:COG4172 21 GTVEAVKGVSFDIAAGETLALVGESGSGKSVTalsiLRLLPDPAAHPSGSILFDGQDLLGLSERELRRirgnRIAMIFQE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 90 --AGLMPHRTIVDNISTVPRL-NGVSARQAKSQALELLNTVGLD--ESFAKRYPSQLSGGQAQRVGVARALASESSILLM 164
Cdd:COG4172 101 pmTSLNPLHTIGKQIAEVLRLhRGLSGAAARARALELLERVGIPdpERRLDAYPHQLSGGQRQRVMIAMALANEPDLLIA 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2735597802 165 DEPFSAVDPVVRADLQKELLRLQSTLGRTIIFVTHDMdeAIL--LGDYVAVFaRGGRIAQFGTPEEILREPADD 236
Cdd:COG4172 181 DEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDL--GVVrrFADRVAVM-RQGEIVEQGPTAELFAAPQHP 251
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
7-232 |
2.87e-36 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 132.42 E-value: 2.87e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 7 AIEFKSVFKTYGD--NTVVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGEDNTARPAHELRRSMG 84
Cdd:PRK13632 7 MIKVENVSFSYPNseNNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 85 YVLQQA-----GLmphrTIVDNISTVPRLNGVSARQAKSQALELLNTVGLDEsFAKRYPSQLSGGQAQRVGVARALASES 159
Cdd:PRK13632 87 IIFQNPdnqfiGA----TVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMED-YLDKEPQNLSGGQKQRVAIASVLALNP 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2735597802 160 SILLMDEPFSAVDPVVRADLQKELLRLQSTLGRTIIFVTHDMDEAIlLGDYVAVFARGGRIAQfGTPEEILRE 232
Cdd:PRK13632 162 EIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAI-LADKVIVFSEGKLIAQ-GKPKEILNN 232
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
8-232 |
3.20e-36 |
|
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: 131.20 E-value: 3.20e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 8 IEFKSVFKTYGDN-TVVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGEDNTARPAHELRRSMGYV 86
Cdd:cd03253 1 IEFENVTFAYDPGrPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 87 LQQAGLMpHRTIVDNIstvpRLNGVSArqAKSQALELLNTVGLDE---SFAKRYPSQ-------LSGGQAQRVGVARALA 156
Cdd:cd03253 81 PQDTVLF-NDTIGYNI----RYGRPDA--TDEEVIEAAKAAQIHDkimRFPDGYDTIvgerglkLSGGEKQRVAIARAIL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 157 SESSILLMDEPFSAVDPVVRADLQKELLRLQStlGRTIIFVTH------DMDEAILLGDyvavfargGRIAQFGTPEEIL 230
Cdd:cd03253 154 KNPPILLLDEATSALDTHTEREIQAALRDVSK--GRTTIVIAHrlstivNADKIIVLKD--------GRIVERGTHEELL 223
|
..
gi 2735597802 231 RE 232
Cdd:cd03253 224 AK 225
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
23-244 |
4.43e-36 |
|
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: 130.57 E-value: 4.43e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 23 VDNLNLSIPEGKITVFVGPSGCGKTTS----LRMINRMVEHTSGTILVNGedntaRPAHELR---RSMGYVLQ--QAGLM 93
Cdd:TIGR02770 2 VQDLNLSLKRGEVLALVGESGSGKSLTclaiLGLLPPGLTQTSGEILLDG-----RPLLPLSirgRHIATIMQnpRTAFN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 94 PHRTIVDNISTVPRLNGVSARQAKSQALELLNTVGLD--ESFAKRYPSQLSGGQAQRVGVARALASESSILLMDEPFSAV 171
Cdd:TIGR02770 77 PLFTMGNHAIETLRSLGKLSKQARALILEALEAVGLPdpEEVLKKYPFQLSGGMLQRVMIALALLLEPPFLIADEPTTDL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2735597802 172 DPVVRADLQKELLRLQSTLGRTIIFVTHDMDEAILLGDYVAVFARgGRIAQFGTPEEILREPADDFVASFVGR 244
Cdd:TIGR02770 157 DVVNQARVLKLLRELRQLFGTGILLITHDLGVVARIADEVAVMDD-GRIVERGTVKEIFYNPKHETTRKLLSA 228
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
7-232 |
5.74e-36 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 131.79 E-value: 5.74e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 7 AIEFKSVFKTYGDNTVVD-----NLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGEDNTARPAHE--- 78
Cdd:PRK13649 2 GINLQNVSYTYQAGTPFEgralfDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNKdik 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 79 -LRRSMGYVLQQA-GLMPHRTIVDNISTVPRLNGVSARQAKSQALELLNTVGLDESFAKRYPSQLSGGQAQRVGVARALA 156
Cdd:PRK13649 82 qIRKKVGLVFQFPeSQLFEETVLKDVAFGPQNFGVSQEEAEALAREKLALVGISESLFEKNPFELSGGQMRRVAIAGILA 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2735597802 157 SESSILLMDEPFSAVDPVVRadlqKELLRLQSTL---GRTIIFVTHDMDEAILLGDYVAVFaRGGRIAQFGTPEEILRE 232
Cdd:PRK13649 162 MEPKILVLDEPTAGLDPKGR----KELMTLFKKLhqsGMTIVLVTHLMDDVANYADFVYVL-EKGKLVLSGKPKDIFQD 235
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-232 |
1.41e-35 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 132.26 E-value: 1.41e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 1 MSVLNNAIEFKSVFKTYGDNTVVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGEDNTARpAHELR 80
Cdd:PRK13536 35 GSMSTVAIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPAR-ARLAR 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 81 RSMGYVLQQAGLMPHRTIVDNISTVPRLNGVSARQAKSQALELLNTVGLdESFAKRYPSQLSGGQAQRVGVARALASESS 160
Cdd:PRK13536 114 ARIGVVPQFDNLDLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARL-ESKADARVSDLSGGMKRRLTLARALINDPQ 192
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2735597802 161 ILLMDEPFSAVDPVVRaDLQKELLRLQSTLGRTIIFVTHDMDEAILLGDYVAVFARGGRIAQfGTPEEILRE 232
Cdd:PRK13536 193 LLILDEPTTGLDPHAR-HLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAE-GRPHALIDE 262
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
23-232 |
2.12e-35 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 130.55 E-value: 2.12e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 23 VDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGEDNTARPAH--ELRRSMGYVLQqaglMPH----- 95
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKlsDIRKKVGLVFQ----YPEyqlfe 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 96 RTIVDNISTVPRLNGVSARQAKSQALELLNTVGLD-ESFAKRYPSQLSGGQAQRVGVARALASESSILLMDEPFSAVDPV 174
Cdd:PRK13637 99 ETIEKDIAFGPINLGLSEEEIENRVKRAMNIVGLDyEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPK 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2735597802 175 VRADLQKELLRLQSTLGRTIIFVTHDMDEAILLGDYVAVFARgGRIAQFGTPEEILRE 232
Cdd:PRK13637 179 GRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNK-GKCELQGTPREVFKE 235
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
13-226 |
1.98e-34 |
|
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: 134.37 E-value: 1.98e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 13 VFKTYGdNTVVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGED-NTARPAheLRRSMGYVLQQAG 91
Cdd:TIGR01257 937 IFEPSG-RPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDiETNLDA--VRQSLGMCPQHNI 1013
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 92 LMPHRTIVDNISTVPRLNGVSARQAKSQALELLNTVGLDESFAKRyPSQLSGGQAQRVGVARALASESSILLMDEPFSAV 171
Cdd:TIGR01257 1014 LFHHLTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEE-AQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGV 1092
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2735597802 172 DPVVRADLQKELLRLQStlGRTIIFVTHDMDEAILLGDYVAVFARgGRIAQFGTP 226
Cdd:TIGR01257 1093 DPYSRRSIWDLLLKYRS--GRTIIMSTHHMDEADLLGDRIAIISQ-GRLYCSGTP 1144
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
8-217 |
3.26e-34 |
|
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: 125.17 E-value: 3.26e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 8 IEFKSVFKTYGDNT----VVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGEDNTARPAhELRRSM 83
Cdd:cd03266 2 ITADALTKRFRDVKktvqAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPA-EARRRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 84 GYVLQQAGLMPHRTIVDNISTVPRLNGVSARQAKSQALELLNTVGLDEsFAKRYPSQLSGGQAQRVGVARALASESSILL 163
Cdd:cd03266 81 GFVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEE-LLDRRVGGFSTGMRQKVAIARALVHDPPVLL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2735597802 164 MDEPFSAVDPVVRADLqKELLRLQSTLGRTIIFVTHDMDEAILLGDYVAVFARG 217
Cdd:cd03266 160 LDEPTTGLDVMATRAL-REFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRG 212
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
15-233 |
3.85e-34 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 125.85 E-value: 3.85e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 15 KTYGDNTVVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGEDNTARPAHE-LRRSMGYVLQQAGLM 93
Cdd:TIGR04406 9 KSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHLPMHErARLGIGYLPQEASIF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 94 PHRTIVDNISTVPRLNGVSARQAKSQALE-LLNTVGLDESFAKRYPSqLSGGQAQRVGVARALASESSILLMDEPFSAVD 172
Cdd:TIGR04406 89 RKLTVEENIMAVLEIRKDLDRAEREERLEaLLEEFQISHLRDNKAMS-LSGGERRRVEIARALATNPKFILLDEPFAGVD 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2735597802 173 PVVRADLQKELLRLQStlgRTI-IFVT-HDMDEAILLGDYVAVFARGGRIAQfGTPEEILREP 233
Cdd:TIGR04406 168 PIAVGDIKKIIKHLKE---RGIgVLITdHNVRETLDICDRAYIISDGKVLAE-GTPAEIVANE 226
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
16-224 |
5.03e-34 |
|
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: 124.59 E-value: 5.03e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 16 TYGDNTVVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGEDNTARPAHELRRSMgyVLQQAGLMPH 95
Cdd:TIGR01277 7 RYEYEHLPMEFDLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPYQRPVSM--LFQENNLFAH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 96 RTIVDNIS--TVPRLNgVSARQaKSQALELLNTVGLDESFAkRYPSQLSGGQAQRVGVARALASESSILLMDEPFSAVDP 173
Cdd:TIGR01277 85 LTVRQNIGlgLHPGLK-LNAEQ-QEKVVDAAQQVGIADYLD-RLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDP 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2735597802 174 VVRADLQKELLRLQSTLGRTIIFVTHDMDEAILLGDYVAVFARgGRIAQFG 224
Cdd:TIGR01277 162 LLREEMLALVKQLCSERQRTLLMVTHHLSDARAIASQIAVVSQ-GKIKVVS 211
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
5-232 |
9.37e-34 |
|
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: 125.20 E-value: 9.37e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 5 NNAIEFKSVFKTYGDNTVVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSG-TILVNGEDNTARPAHELRRSM 83
Cdd:COG1119 1 DPLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRGGEDVWELRKRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 84 GYV---LQQAglMPHRTIVDNI------STVPRLNGVSARQaKSQALELLNTVGLDEsFAKRYPSQLSGGQAQRVGVARA 154
Cdd:COG1119 81 GLVspaLQLR--FPRDETVLDVvlsgffDSIGLYREPTDEQ-RERARELLELLGLAH-LADRPFGTLSQGEQRRVLIARA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 155 LASESSILLMDEPFSAVDPVVRADLQKELLRLQSTLGRTIIFVTHDMDE-------AILLgdyvavfaRGGRIAQFGTPE 227
Cdd:COG1119 157 LVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEippgithVLLL--------KDGRVVAAGPKE 228
|
....*
gi 2735597802 228 EILRE 232
Cdd:COG1119 229 EVLTS 233
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
8-232 |
1.02e-33 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 126.00 E-value: 1.02e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 8 IEFKSVFKTYGDNT-----VVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTI----LVNGEDNTARPAHE 78
Cdd:PRK13643 2 IKFEKVNYTYQPNSpfasrALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVtvgdIVVSSTSKQKEIKP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 79 LRRSMGYVLQ-QAGLMPHRTIVDNISTVPRLNGVSARQAKSQALELLNTVGLDESFAKRYPSQLSGGQAQRVGVARALAS 157
Cdd:PRK13643 82 VRKKVGVVFQfPESQLFEETVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLADEFWEKSPFELSGGQMRRVAIAGILAM 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2735597802 158 ESSILLMDEPFSAVDPVVRADLQKELLRLQSTlGRTIIFVTHDMDEAILLGDYVAVFARgGRIAQFGTPEEILRE 232
Cdd:PRK13643 162 EPEVLVLDEPTAGLDPKARIEMMQLFESIHQS-GQTVVLVTHLMDDVADYADYVYLLEK-GHIISCGTPSDVFQE 234
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
7-213 |
1.28e-33 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 130.10 E-value: 1.28e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 7 AIEFKSVFKTYGDNT-VVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGEDNTARPAHELRRSMGY 85
Cdd:TIGR02857 321 SLEFSGVSVAYPGRRpALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAW 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 86 VLQQAGLMPhRTIVDNIstvpRL--NGVSA---RQAKSQA--LELLNTV--GLDESFAKRyPSQLSGGQAQRVGVARALA 156
Cdd:TIGR02857 401 VPQHPFLFA-GTIAENI----RLarPDASDaeiREALERAglDEFVAALpqGLDTPIGEG-GAGLSGGQAQRLALARAFL 474
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2735597802 157 SESSILLMDEPFSAVDPVVRADLQKELLRLQStlGRTIIFVTHDmDEAILLGDYVAV 213
Cdd:TIGR02857 475 RDAPLLLLDEPTAHLDAETEAEVLEALRALAQ--GRTVLLVTHR-LALAALADRIVV 528
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
8-232 |
1.31e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 126.35 E-value: 1.31e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 8 IEFKSVFKTYGDNT-----VVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTI---LVNGEDNTA------ 73
Cdd:PRK13651 3 IKVKNIVKIFNKKLptelkALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewiFKDEKNKKKtkekek 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 74 ---------------RPAHELRRSMGYVLQQAGL-MPHRTIVDNISTVPRLNGVSARQAKSQALELLNTVGLDESFAKRY 137
Cdd:PRK13651 83 vleklviqktrfkkiKKIKEIRRRVGVVFQFAEYqLFEQTIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLDESYLQRS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 138 PSQLSGGQAQRVGVARALASESSILLMDEPFSAVDPVVradlQKELLRLQSTL---GRTIIFVTHDMDEAILLGDYVAVF 214
Cdd:PRK13651 163 PFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQG----VKEILEIFDNLnkqGKTIILVTHDLDNVLEWTKRTIFF 238
|
250
....*....|....*...
gi 2735597802 215 aRGGRIAQFGTPEEILRE 232
Cdd:PRK13651 239 -KDGKIIKDGDTYDILSD 255
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
8-230 |
3.29e-33 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 123.11 E-value: 3.29e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 8 IEFKSVFKTYGD--NTVVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGEDNTARPAHELRRSMGY 85
Cdd:cd03251 1 VEFKNVTFRYPGdgPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 86 VLQQAGLMpHRTIVDNI----STVPRLNGVSARQAkSQALELLNTV--GLDESFAKRyPSQLSGGQAQRVGVARALASES 159
Cdd:cd03251 81 VSQDVFLF-NDTVAENIaygrPGATREEVEEAARA-ANAHEFIMELpeGYDTVIGER-GVKLSGGQRQRIAIARALLKDP 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2735597802 160 SILLMDEPFSAVDPVVRADLQKELLRLQStlGRTIIFVTH------DMDEAILLGDyvavfargGRIAQFGTPEEIL 230
Cdd:cd03251 158 PILILDEATSALDTESERLVQAALERLMK--NRTTFVIAHrlstieNADRIVVLED--------GKIVERGTHEELL 224
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-243 |
6.03e-33 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 123.22 E-value: 6.03e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 1 MSVLNNAIEFKSVFKTYGDNTVVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVE-----HTSGTILVNGEDNTARP 75
Cdd:PRK14258 1 MSKLIPAIKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNElesevRVEGRVEFFNQNIYERR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 76 AH--ELRRSMGYVLQQAGLMPhRTIVDNISTVPRLNGVSARQAKSQALE-LLNTVGL-DESFAKRYPS--QLSGGQAQRV 149
Cdd:PRK14258 81 VNlnRLRRQVSMVHPKPNLFP-MSVYDNVAYGVKIVGWRPKLEIDDIVEsALKDADLwDEIKHKIHKSalDLSGGQQQRL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 150 GVARALASESSILLMDEPFSAVDPVVRADLQKEL--LRLQSTLgrTIIFVTHDMDEAILLGDYVAVF----ARGGRIAQF 223
Cdd:PRK14258 160 CIARALAVKPKVLLMDEPCFGLDPIASMKVESLIqsLRLRSEL--TMVIVSHNLHQVSRLSDFTAFFkgneNRIGQLVEF 237
|
250 260
....*....|....*....|....
gi 2735597802 224 GTPEEILREPAD----DFVASFVG 243
Cdd:PRK14258 238 GLTKKIFNSPHDsrtrEYVLSRLG 261
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
8-233 |
8.78e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 123.37 E-value: 8.78e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 8 IEFKSVFKTY-GDNTVVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGEDNTARPAHELRRSMGYV 86
Cdd:PRK13652 4 IETRDLCYSYsGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 87 LQQAGLMPHRTIVD-NISTVPRLNGVSARQAKSQALELLNTVGLDEsFAKRYPSQLSGGQAQRVGVARALASESSILLMD 165
Cdd:PRK13652 84 FQNPDDQIFSPTVEqDIAFGPINLGLDEETVAHRVSSALHMLGLEE-LRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLD 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2735597802 166 EPFSAVDPVVRADLQKELLRLQSTLGRTIIFVTHDMDEAILLGDYVAVFARgGRIAQFGTPEEILREP 233
Cdd:PRK13652 163 EPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDK-GRIVAYGTVEEIFLQP 229
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
8-316 |
1.95e-32 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 124.95 E-value: 1.95e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 8 IEFKSVFKTYGDNTVVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGEDNTARPAHELRRSMGYVL 87
Cdd:PRK09536 4 IDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 88 QQAGL---MPHRTIVDNISTVPRLNGVSARQAKSQALE-LLNTVGLDEsFAKRYPSQLSGGQAQRVGVARALASESSILL 163
Cdd:PRK09536 84 QDTSLsfeFDVRQVVEMGRTPHRSRFDTWTETDRAAVErAMERTGVAQ-FADRPVTSLSGGERQRVLLARALAQATPVLL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 164 MDEPFSAVDpVVRADLQKELLRLQSTLGRTIIFVTHDMDEAILLGDYVAVFArGGRIAQFGTPEEILREP--ADDFVA-S 240
Cdd:PRK09536 163 LDEPTASLD-INHQVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLA-DGRVRAAGPPADVLTADtlRAAFDArT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 241 FVGRDRGMrrltfASGADVPIHPLDAQQTPWQQWQLNVEDGRP----------AGWRIDDRVIPGGSlfVAGGTLRDALD 310
Cdd:PRK09536 241 AVGTDPAT-----GAPTVTPLPDPDRTEAAADTRVHVVGGGQPaaravsrlvaAGASVSVGPVPEGD--TAAETAARVGC 313
|
....*.
gi 2735597802 311 SVLSSP 316
Cdd:PRK09536 314 EAVTVP 319
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
17-229 |
2.17e-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: 120.71 E-value: 2.17e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 17 YGDNTVVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGEDNTARPAHEL-RRSMGYVLQQAGLMPH 95
Cdd:TIGR03410 10 YGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERaRAGIAYVPQGREIFPR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 96 RTIVDNISTvprlnGVSARQAKSQAL--ELLNTVGLDESFAKRYPSQLSGGQAQRVGVARALASESSILLMDEPFSAVDP 173
Cdd:TIGR03410 90 LTVEENLLT-----GLAALPRRSRKIpdEIYELFPVLKEMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDEPTEGIQP 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2735597802 174 VVRADLQKELLRLQSTLGRTIIFVTHDMDEAILLGDYVAVFARgGRIAQFGTPEEI 229
Cdd:TIGR03410 165 SIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMER-GRVVASGAGDEL 219
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
17-234 |
2.21e-32 |
|
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: 120.86 E-value: 2.21e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 17 YGDNTVVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGEDNTARPAHEL-RRSMGYVLQQAGLMPH 95
Cdd:COG0410 13 YGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIaRLGIGYVPEGRRIFPS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 96 RTIVDN--ISTVPRLNGVSARQAKSQALEL---LntvgldESFAKRYPSQLSGGQAQRVGVARALASESSILLMDEPFSA 170
Cdd:COG0410 93 LTVEENllLGAYARRDRAEVRADLERVYELfprL------KERRRQRAGTLSGGEQQMLAIGRALMSRPKLLLLDEPSLG 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2735597802 171 VDPVVRADLQKELLRLQSTlGRTIIFVTHDMDEAILLGDYVAVFARgGRIAQFGTPEEILREPA 234
Cdd:COG0410 167 LAPLIVEEIFEIIRRLNRE-GVTILLVEQNARFALEIADRAYVLER-GRIVLEGTAAELLADPE 228
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
13-209 |
3.35e-32 |
|
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: 119.67 E-value: 3.35e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 13 VFKTYGDNTVVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGEDntaRPAHELRRSMGYVLQQagl 92
Cdd:cd03226 6 SFSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKP---IKAKERRKSIGYVMQD--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 93 mphrtiVDNI---STVPRLNGVSARQA---KSQALELLNTVGLDEsFAKRYPSQLSGGQAQRVGVARALASESSILLMDE 166
Cdd:cd03226 80 ------VDYQlftDSVREELLLGLKELdagNEQAETVLKDLDLYA-LKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDE 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2735597802 167 PFSAVDPVVRADLQKELLRLQSTlGRTIIFVTHDM-------DEAILLGD 209
Cdd:cd03226 153 PTSGLDYKNMERVGELIRELAAQ-GKAVIVITHDYeflakvcDRVLLLAN 201
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
27-230 |
4.26e-32 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 120.07 E-value: 4.26e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 27 NLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGEDNTARPAHelRRSMGYVLQQAGLMPHRTIVDNIS--T 104
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPS--RRPVSMLFQENNLFSHLTVAQNIGlgL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 105 VP--RLNGvsarQAKSQALELLNTVGLdESFAKRYPSQLSGGQAQRVGVARALASESSILLMDEPFSAVDPVVRAdlqkE 182
Cdd:PRK10771 97 NPglKLNA----AQREKLHAIARQMGI-EDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQ----E 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2735597802 183 LLRLQSTLGR----TIIFVTHDMDEAILLGDYVAVFArGGRIAQFGTPEEIL 230
Cdd:PRK10771 168 MLTLVSQVCQerqlTLLMVSHSLEDAARIAPRSLVVA-DGRIAWDGPTDELL 218
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
15-230 |
5.18e-32 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 120.38 E-value: 5.18e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 15 KTYGDNTVVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGEDNTARPAHE-LRRSMGYVLQQAGLM 93
Cdd:PRK10895 11 KAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHArARRGIGYLPQEASIF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 94 PHRTIVDNISTVPRL-NGVSARQAKSQALELL---NTVGLDESFAKrypsQLSGGQAQRVGVARALASESSILLMDEPFS 169
Cdd:PRK10895 91 RRLSVYDNLMAVLQIrDDLSAEQREDRANELMeefHIEHLRDSMGQ----SLSGGERRRVEIARALAANPKFILLDEPFA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2735597802 170 AVDPVVRADLQKELLRLQSTlGRTIIFVTHDMDEAILLGDYVAVFARGGRIAQfGTPEEIL 230
Cdd:PRK10895 167 GVDPISVIDIKRIIEHLRDS-GLGVLITDHNVRETLAVCERAYIVSQGHLIAH-GTPTEIL 225
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
16-271 |
5.55e-32 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 120.61 E-value: 5.55e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 16 TYGDNTVVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGEDNTARPAHELRRSMGyVLQQA----- 90
Cdd:COG4559 10 RLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRRA-VLPQHsslaf 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 91 ----------GLMPHRTivdnistvprlngvSARQAKSQALELLNTVGLDEsFAKRYPSQLSGGQAQRVGVARALA---- 156
Cdd:COG4559 89 pftveevvalGRAPHGS--------------SAAQDRQIVREALALVGLAH-LAGRSYQTLSGGEQQRVQLARVLAqlwe 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 157 ---SESSILLMDEPFSAVDPVvradLQKELLRLQSTL---GRTIIFVTHDMDEAILLGDYVAVFARgGRIAQFGTPEEIL 230
Cdd:COG4559 154 pvdGGPRWLFLDEPTSALDLA----HQHAVLRLARQLarrGGGVVAVLHDLNLAAQYADRILLLHQ-GRLVAQGTPEEVL 228
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 2735597802 231 REPaddfvasfvgrdrgmrRLTFASGADVPIHPLDAQQTPW 271
Cdd:COG4559 229 TDE----------------LLERVYGADLRVLAHPEGGCPQ 253
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
6-229 |
6.18e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 120.99 E-value: 6.18e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 6 NAIEFKSVFKTYGDNT---VVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGEDNTARPAHELRRS 82
Cdd:PRK13650 3 NIIEVKNLTFKYKEDQekyTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 83 MGYVLQQaglmPHR-----TIVDNISTVPRLNGVSARQAKSQALELLNTVGLdESFAKRYPSQLSGGQAQRVGVARALAS 157
Cdd:PRK13650 83 IGMVFQN----PDNqfvgaTVEDDVAFGLENKGIPHEEMKERVNEALELVGM-QDFKEREPARLSGGQKQRVAIAGAVAM 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2735597802 158 ESSILLMDEPFSAVDPVVRADLQKELLRLQSTLGRTIIFVTHDMDEaILLGDYVAVFARgGRIAQFGTPEEI 229
Cdd:PRK13650 158 RPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDE-VALSDRVLVMKN-GQVESTSTPREL 227
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-204 |
7.44e-32 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 119.46 E-value: 7.44e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 1 MSVLNN-AIEFKSVFKTYGDN----TVVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGEDNT--- 72
Cdd:COG4181 1 MSSSSApIIELRGLTKTVGTGagelTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFald 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 73 --ARpAHELRRSMGYVLQQAGLMPHRTIVDNISTVPRLNGvsARQAKSQALELLNTVGLDESfAKRYPSQLSGGQAQRVG 150
Cdd:COG4181 81 edAR-ARLRARHVGFVFQSFQLLPTLTALENVMLPLELAG--RRDARARARALLERVGLGHR-LDHYPAQLSGGEQQRVA 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2735597802 151 VARALASESSILLMDEPFSAVDPVVRADLQKELLRLQSTLGRTIIFVTHDMDEA 204
Cdd:COG4181 157 LARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALA 210
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
5-233 |
1.20e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 120.29 E-value: 1.20e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 5 NNAIEFKSVFKTYGDN--TVVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMV---EHTSGTILVNGEDNTARPAHEL 79
Cdd:PRK13640 3 DNIVEFKHVSFTYPDSkkPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLlpdDNPNSKITVDGITLTAKTVWDI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 80 RRSMGYVLQQaglmPHR-----TIVDNISTVPRLNGVSARQAKSQALELLNTVGLDEsFAKRYPSQLSGGQAQRVGVARA 154
Cdd:PRK13640 83 REKVGIVFQN----PDNqfvgaTVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLD-YIDSEPANLSGGQKQRVAIAGI 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2735597802 155 LASESSILLMDEPFSAVDPVVRADLQKELLRLQSTLGRTIIFVTHDMDEAIlLGDYVAVFARGGRIAQfGTPEEILREP 233
Cdd:PRK13640 158 LAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEAN-MADQVLVLDDGKLLAQ-GSPVEIFSKV 234
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
8-230 |
3.39e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 119.34 E-value: 3.39e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 8 IEFKSVFKTYGDNT-----VVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNgedNTARPAH----- 77
Cdd:PRK13645 7 IILDNVSYTYAKKTpfefkALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVG---DYAIPANlkkik 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 78 ---ELRRSMGYVLQqaglMP-----HRTIVDNISTVPRLNGVSARQAKSQALELLNTVGLDESFAKRYPSQLSGGQAQRV 149
Cdd:PRK13645 84 evkRLRKEIGLVFQ----FPeyqlfQETIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLPEDYVKRSPFELSGGQKRRV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 150 GVARALASESSILLMDEPFSAVDPVVRADLQKELLRLQSTLGRTIIFVTHDMDEAILLGDYVAVFARgGRIAQFGTPEEI 229
Cdd:PRK13645 160 ALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHE-GKVISIGSPFEI 238
|
.
gi 2735597802 230 L 230
Cdd:PRK13645 239 F 239
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
4-232 |
3.60e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 118.68 E-value: 3.60e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 4 LNNAIEFKSVFKTYGDNT-VVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGEDNTARPAHELRRS 82
Cdd:PRK13647 1 MDNIIEVEDLHFRYKDGTkALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 83 MGYVLQ----QAGLMphrTIVDNISTVPRLNGVSARQAKSQALELLNTVGLdESFAKRYPSQLSGGQAQRVGVARALASE 158
Cdd:PRK13647 81 VGLVFQdpddQVFSS---TVWDDVAFGPVNMGLDKDEVERRVEEALKAVRM-WDFRDKPPYHLSYGQKKRVAIAGVLAMD 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2735597802 159 SSILLMDEPFSAVDPVVRADLQKELLRLQSTlGRTIIFVTHDMDEAILLGDYVAVFARGGRIAQfGTPEEILRE 232
Cdd:PRK13647 157 PDVIVLDEPMAYLDPRGQETLMEILDRLHNQ-GKTVIVATHDVDLAAEWADQVIVLKEGRVLAE-GDKSLLTDE 228
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1-229 |
4.04e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 118.70 E-value: 4.04e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 1 MSVLNNAIEFKSV-FKTYGDNT-VVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGEDNTARPAHE 78
Cdd:PRK13648 1 MEDKNSIIVFKNVsFQYQSDASfTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 79 LRRSMGYVLQQaglmPHRTIVDniSTVP-------RLNGVSARQAKSQALELLNTVGLDEsFAKRYPSQLSGGQAQRVGV 151
Cdd:PRK13648 81 LRKHIGIVFQN----PDNQFVG--SIVKydvafglENHAVPYDEMHRRVSEALKQVDMLE-RADYEPNALSGGQKQRVAI 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2735597802 152 ARALASESSILLMDEPFSAVDPVVRADLQKELLRLQSTLGRTIIFVTHDMDEAiLLGDYVAVFARgGRIAQFGTPEEI 229
Cdd:PRK13648 154 AGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEA-MEADHVIVMNK-GTVYKEGTPTEI 229
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
7-245 |
4.13e-31 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 122.82 E-value: 4.13e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 7 AIEFKSVFKTYGDNTVVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGED---NTARPAHELRRSM 83
Cdd:COG1129 4 LLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPvrfRSPRDAQAAGIAI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 84 gyVLQQAGLMPHRTIVDNI--STVPRLNG-VSARQAKSQALELLNTVGLDESFAKRYpSQLSGGQAQRVGVARALASESS 160
Cdd:COG1129 84 --IHQELNLVPNLSVAENIflGREPRRGGlIDWRAMRRRARELLARLGLDIDPDTPV-GDLSVAQQQLVEIARALSRDAR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 161 ILLMDEPFSAVDPVVRADLQKELLRLQSTlGRTIIFVTHDMDEAILLGDYVAVFaRGGRIAQFGTPEEIlrePADDFVAS 240
Cdd:COG1129 161 VLILDEPTASLTEREVERLFRIIRRLKAQ-GVAIIYISHRLDEVFEIADRVTVL-RDGRLVGTGPVAEL---TEDELVRL 235
|
....*
gi 2735597802 241 FVGRD 245
Cdd:COG1129 236 MVGRE 240
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
23-233 |
6.10e-31 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 119.43 E-value: 6.10e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 23 VDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGEDNT---ARPAHELRRSMGYVLQQ--AGLMPHRT 97
Cdd:PRK15079 37 VDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLgmkDDEWRAVRSDIQMIFQDplASLNPRMT 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 98 IVDNIST-----VPRLngvSARQAKSQALELLNTVGLDESFAKRYPSQLSGGQAQRVGVARALASESSILLMDEPFSAVD 172
Cdd:PRK15079 117 IGEIIAEplrtyHPKL---SRQEVKDRVKAMMLKVGLLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALD 193
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2735597802 173 PVVRADLQKELLRLQSTLGRTIIFVTHDMDEAILLGDYVAVFARGGRIaQFGTPEEILREP 233
Cdd:PRK15079 194 VSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAV-ELGTYDEVYHNP 253
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
8-221 |
1.91e-30 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 113.68 E-value: 1.91e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 8 IEFKSVFKTYGDNTVVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGED-NTARPAHELRrsmgyv 86
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEvSFASPRDARR------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 87 lqqAGlmphrtivdnISTVPrlngvsarqaksqalellntvgldesfakrypsQLSGGQAQRVGVARALASESSILLMDE 166
Cdd:cd03216 75 ---AG----------IAMVY---------------------------------QLSVGERQMVEIARALARNARLLILDE 108
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2735597802 167 PFSAVDPVVRADLQKELLRLQSTlGRTIIFVTHDMDEAILLGDYVAVFaRGGRIA 221
Cdd:cd03216 109 PTAALTPAEVERLFKVIRRLRAQ-GVAVIFISHRLDEVFEIADRVTVL-RDGRVV 161
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
12-201 |
2.18e-30 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 116.71 E-value: 2.18e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 12 SVFKTYGDNTVVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGEDNTA---RPAHELRRSMGYVLQ 88
Cdd:PRK10419 17 GLSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKlnrAQRKAFRRDIQMVFQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 89 QA--GLMPHRTIVDNISTVPR-LNGVSARQAKSQALELLNTVGLDESFAKRYPSQLSGGQAQRVGVARALASESSILLMD 165
Cdd:PRK10419 97 DSisAVNPRKTVREIIREPLRhLLSLDKAERLARASEMLRAVDLDDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILD 176
|
170 180 190
....*....|....*....|....*....|....*.
gi 2735597802 166 EPFSAVDPVVRADLQKELLRLQSTLGRTIIFVTHDM 201
Cdd:PRK10419 177 EAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDL 212
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
23-233 |
2.64e-30 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 117.76 E-value: 2.64e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 23 VDNLNLSIPEGKITVFVGPSGCGKTTSLRMINrMVEH-TSGTILVNGEDnTARPAHE----LRRSMGYVLQQ--AGLMPH 95
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTLARLLT-MIETpTGGELYYQGQD-LLKADPEaqklLRQKIQIVFQNpyGSLNPR 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 96 RTIVDNISTVPRLN-GVSARQAKSQALELLNTVGLDESFAKRYPSQLSGGQAQRVGVARALASESSILLMDEPFSAVDPV 174
Cdd:PRK11308 109 KKVGQILEEPLLINtSLSAAERREKALAMMAKVGLRPEHYDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALDVS 188
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2735597802 175 VRADLQKELLRLQSTLGRTIIFVTHDMDEAILLGDYVAVFARgGRIAQFGTPEEILREP 233
Cdd:PRK11308 189 VQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYL-GRCVEKGTKEQIFNNP 246
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
15-234 |
3.59e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 117.26 E-value: 3.59e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 15 KTYGDNTVVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTI----LVNGEDNTARP------------AHE 78
Cdd:PRK13631 34 KQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIqvgdIYIGDKKNNHElitnpyskkiknFKE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 79 LRRSMGYVLQqaglMPH-----RTIVDNISTVPRLNGVSARQAKSQALELLNTVGLDESFAKRYPSQLSGGQAQRVGVAR 153
Cdd:PRK13631 114 LRRRVSMVFQ----FPEyqlfkDTIEKDIMFGPVALGVKKSEAKKLAKFYLNKMGLDDSYLERSPFGLSGGQKRRVAIAG 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 154 ALASESSILLMDEPFSAVDPVVRADLQkELLRLQSTLGRTIIFVTHDMDEAILLGDYVAVFARgGRIAQFGTPEEILREP 233
Cdd:PRK13631 190 ILAIQPEILIFDEPTAGLDPKGEHEMM-QLILDAKANNKTVFVITHTMEHVLEVADEVIVMDK-GKILKTGTPYEIFTDQ 267
|
.
gi 2735597802 234 A 234
Cdd:PRK13631 268 H 268
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
2-232 |
8.55e-30 |
|
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: 120.36 E-value: 8.55e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 2 SVLNNAIEFKSV-FKTYGDNT-VVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGEDNTARPAHEL 79
Cdd:TIGR03375 458 PRLQGEIEFRNVsFAYPGQETpALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQIDPADL 537
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 80 RRSMGYVLQQAGLMpHRTIVDNIStvprlngVSARQAKSQA-LELLNTVGLDEsFAKRYPS-----------QLSGGQAQ 147
Cdd:TIGR03375 538 RRNIGYVPQDPRLF-YGTLRDNIA-------LGAPYADDEEiLRAAELAGVTE-FVRRHPDgldmqigergrSLSGGQRQ 608
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 148 RVGVARALASESSILLMDEPFSAVDPVVRADLQKellRLQSTL-GRTIIFVTHDMdeAIL-LGDYVAVFaRGGRIAQFGT 225
Cdd:TIGR03375 609 AVALARALLRDPPILLLDEPTSAMDNRSEERFKD---RLKRWLaGKTLVLVTHRT--SLLdLVDRIIVM-DNGRIVADGP 682
|
....*..
gi 2735597802 226 PEEILRE 232
Cdd:TIGR03375 683 KDQVLEA 689
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
7-222 |
9.69e-30 |
|
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: 113.45 E-value: 9.69e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 7 AIEFKSVFKTYGD--NTVVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGEDNTARPAHELRRSMG 84
Cdd:cd03245 2 RIEFRNVSFSYPNqeIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 85 YVLQQAGLMpHRTIVDNIStvprlngVSARQAKSQA-LELLNTVGLDEsFAKRYP-----------SQLSGGQAQRVGVA 152
Cdd:cd03245 82 YVPQDVTLF-YGTLRDNIT-------LGAPLADDERiLRAAELAGVTD-FVNKHPngldlqigergRGLSGGQRQAVALA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2735597802 153 RALASESSILLMDEPFSAVDPVVRADLqKELLRlQSTLGRTIIFVTHDMdeAIL-LGDYVAVFARGGRIAQ 222
Cdd:cd03245 153 RALLNDPPILLLDEPTSAMDMNSEERL-KERLR-QLLGDKTLIIITHRP--SLLdLVDRIIVMDSGRIVAD 219
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
1-236 |
1.42e-29 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 114.16 E-value: 1.42e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 1 MSVLnnaIEFKSVFKTYGDNT---------VVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGED- 70
Cdd:COG4167 1 MSAL---LEVRNLSKTFKYRTglfrrqqfeAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKl 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 71 ---NTARPAHELRrsMgyVLQQAG--LMPHRTIVDNISTVPRLN-GVSARQAKSQALELLNTVGLDESFAKRYPSQLSGG 144
Cdd:COG4167 78 eygDYKYRCKHIR--M--IFQDPNtsLNPRLNIGQILEEPLRLNtDLTAEEREERIFATLRLVGLLPEHANFYPHMLSSG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 145 QAQRVGVARALASESSILLMDEPFSAVDPVVRADLQKELLRLQSTLGRTIIFVTHDMDEAILLGDYVAVFARgGRIAQFG 224
Cdd:COG4167 154 QKQRVALARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKHISDKVLVMHQ-GEVVEYG 232
|
250
....*....|..
gi 2735597802 225 TPEEILREPADD 236
Cdd:COG4167 233 KTAEVFANPQHE 244
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
23-233 |
2.23e-29 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 118.80 E-value: 2.23e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 23 VDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGE--DN-TARPAHELRRSMGYVLQQ--AGLMPHRT 97
Cdd:PRK10261 340 VEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQriDTlSPGKLQALRRDIQFIFQDpyASLDPRQT 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 98 IVDNISTVPRLNGV-SARQAKSQALELLNTVGLDESFAKRYPSQLSGGQAQRVGVARALASESSILLMDEPFSAVDPVVR 176
Cdd:PRK10261 420 VGDSIMEPLRVHGLlPGKAAAARVAWLLERVGLLPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIR 499
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2735597802 177 ADLQKELLRLQSTLGRTIIFVTHDMDEAILLGDYVAVFARgGRIAQFGTPEEILREP 233
Cdd:PRK10261 500 GQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYL-GQIVEIGPRRAVFENP 555
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
17-249 |
2.67e-29 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 113.54 E-value: 2.67e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 17 YGDNTVVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGEDNTARPAHELRRSMGYVLQQA------ 90
Cdd:PRK10253 17 YGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNAttpgdi 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 91 --------GLMPHRTIV--------DNISTVPRLNGVSarqaksqalellntvgldeSFAKRYPSQLSGGQAQRVGVARA 154
Cdd:PRK10253 97 tvqelvarGRYPHQPLFtrwrkedeEAVTKAMQATGIT-------------------HLADQSVDTLSGGQRQRAWIAMV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 155 LASESSILLMDEPFSAVDPVVRADLQKELLRLQSTLGRTIIFVTHDMDEAILLGDYVAVFaRGGRIAQFGTPEEILrepa 234
Cdd:PRK10253 158 LAQETAIMLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIAL-REGKIVAQGAPKEIV---- 232
|
250
....*....|....*
gi 2735597802 235 ddfVASFVGRDRGMR 249
Cdd:PRK10253 233 ---TAELIERIYGLR 244
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
8-229 |
3.50e-29 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 115.36 E-value: 3.50e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 8 IEFKsvfKTYGDNTVvdNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNG------EDNTARPAHelRR 81
Cdd:PRK11144 4 LNFK---QQLGDLCL--TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGrvlfdaEKGICLPPE--KR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 82 SMGYVLQQAGLMPHRTIVDNIstvprLNGVsARQAKSQALELLNTVGLdESFAKRYPSQLSGGQAQRVGVARALASESSI 161
Cdd:PRK11144 77 RIGYVFQDARLFPHYKVRGNL-----RYGM-AKSMVAQFDKIVALLGI-EPLLDRYPGSLSGGEKQRVAIGRALLTAPEL 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2735597802 162 LLMDEPFSAVDpVVRadlQKELLRLQSTLGRT----IIFVTHDMDEAILLGDYVAVFARgGRIAQFGTPEEI 229
Cdd:PRK11144 150 LLMDEPLASLD-LPR---KRELLPYLERLAREinipILYVSHSLDEILRLADRVVVLEQ-GKVKAFGPLEEV 216
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
21-199 |
4.66e-29 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 111.10 E-value: 4.66e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 21 TVVDNLNLSIPEGKITVFVGPSGCGKTTSLRMIN--RMVEHTSGTILVNGEDntaRPAHELRRSMGYVLQQAGLMPHRTI 98
Cdd:cd03213 23 QLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAgrRTGLGVSGEVLINGRP---LDKRSFRKIIGYVPQDDILHPTLTV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 99 vdnistvprlngvsaRQAKSQALELlntvgldesfakrypSQLSGGQAQRVGVARALASESSILLMDEPFSAVDPVVRAD 178
Cdd:cd03213 100 ---------------RETLMFAAKL---------------RGLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQ 149
|
170 180
....*....|....*....|.
gi 2735597802 179 LQKELLRLQSTlGRTIIFVTH 199
Cdd:cd03213 150 VMSLLRRLADT-GRTIICSIH 169
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
17-243 |
7.06e-29 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 112.88 E-value: 7.06e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 17 YGDNTVVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSG-----TILVNGED-NTARPAHELRRSMGYVLQQA 90
Cdd:PRK14271 31 FAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSiFNYRDVLEFRRRVGMLFQRP 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 91 GLMPhRTIVDNISTVPRLNGVSARQA-KSQALELLNTVGLDESFAKRY---PSQLSGGQAQRVGVARALASESSILLMDE 166
Cdd:PRK14271 111 NPFP-MSIMDNVLAGVRAHKLVPRKEfRGVAQARLTEVGLWDAVKDRLsdsPFRLSGGQQQLLCLARTLAVNPEVLLLDE 189
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2735597802 167 PFSAVDPVVRADLQKELLRLQSTLgrTIIFVTHDMDEAILLGDYVAVFArGGRIAQFGTPEEILREPADDFVASFVG 243
Cdd:PRK14271 190 PTSALDPTTTEKIEEFIRSLADRL--TVIIVTHNLAQAARISDRAALFF-DGRLVEEGPTEQLFSSPKHAETARYVA 263
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
5-231 |
1.09e-28 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 112.42 E-value: 1.09e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 5 NNAIEFKSVFKTYGDNT--VVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGEDNTARPAHELRRS 82
Cdd:PRK13635 3 EEIIRVEHISFRYPDAAtyALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 83 MGYVLQQaglmPHR-----TIVDNISTVPRLNGVSARQAKSQALELLNTVGLdESFAKRYPSQLSGGQAQRVGVARALAS 157
Cdd:PRK13635 83 VGMVFQN----PDNqfvgaTVQDDVAFGLENIGVPREEMVERVDQALRQVGM-EDFLNREPHRLSGGQKQRVAIAGVLAL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2735597802 158 ESSILLMDEPFSAVDPVVRADLQKELLRLQSTLGRTIIFVTHDMDEAiLLGDYVAVFaRGGRIAQFGTPEEILR 231
Cdd:PRK13635 158 QPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEA-AQADRVIVM-NKGEILEEGTPEEIFK 229
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
17-232 |
1.24e-28 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 111.40 E-value: 1.24e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 17 YGDNTVVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGEDNTARPAHELRRSMGyVLQQA------ 90
Cdd:PRK13548 12 LGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRA-VLPQHsslsfp 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 91 ---------GLMPHRTivdnistvprlngvSARQAKSQALELLNTVGLDEsFAKRYPSQLSGGQAQRVGVARALA----- 156
Cdd:PRK13548 91 ftveevvamGRAPHGL--------------SRAEDDALVAAALAQVDLAH-LAGRDYPQLSGGEQQRVQLARVLAqlwep 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 157 -SESSILLMDEPFSAVDPVvradLQKELLRLQSTL----GRTIIFVTHDMDEAILLGDYVAVFArGGRIAQFGTPEEILR 231
Cdd:PRK13548 156 dGPPRWLLLDEPTSALDLA----HQHHVLRLARQLaherGLAVIVVLHDLNLAARYADRIVLLH-QGRLVADGTPAEVLT 230
|
.
gi 2735597802 232 E 232
Cdd:PRK13548 231 P 231
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
8-232 |
2.14e-28 |
|
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: 110.27 E-value: 2.14e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 8 IEFKSVFKTYGDNT--VVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGED-NTARPAHeLRRSMG 84
Cdd:cd03252 1 ITFEHVRFRYKPDGpvILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDlALADPAW-LRRQVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 85 YVLQQAGLMpHRTIVDNIS---TVPRLNGV--SARQAKSQALELLNTVGLDESFAKRyPSQLSGGQAQRVGVARALASES 159
Cdd:cd03252 80 VVLQENVLF-NRSIRDNIAladPGMSMERVieAAKLAGAHDFISELPEGYDTIVGEQ-GAGLSGGQRQRIAIARALIHNP 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2735597802 160 SILLMDEPFSAVDPVVRADLQKELLRLQStlGRTIIFVTHDMdEAILLGDYVAVFaRGGRIAQFGTPEEILRE 232
Cdd:cd03252 158 RILIFDEATSALDYESEHAIMRNMHDICA--GRTVIIIAHRL-STVKNADRIIVM-EKGRIVEQGSHDELLAE 226
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
8-233 |
4.73e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 110.55 E-value: 4.73e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 8 IEFKSVFKTYGDNTVV-DNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGE--DNTARPAHELRRSMG 84
Cdd:PRK13639 2 LETRDLKYSYPDGTEAlKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEpiKYDKKSLLEVRKTVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 85 YVLQQAG---LMPhrTIVDNISTVPRLNGVSARQAKSQALELLNTVGLdESFAKRYPSQLSGGQAQRVGVARALASESSI 161
Cdd:PRK13639 82 IVFQNPDdqlFAP--TVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGM-EGFENKPPHHLSGGQKKRVAIAGILAMKPEI 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2735597802 162 LLMDEPFSAVDPVVRADLQKELLRLQSTlGRTIIFVTHDMDEAILLGDYVAVFArGGRIAQFGTPEEILREP 233
Cdd:PRK13639 159 IVLDEPTSGLDPMGASQIMKLLYDLNKE-GITIIISTHDVDLVPVYADKVYVMS-DGKIIKEGTPKEVFSDI 228
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
5-232 |
6.52e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 110.18 E-value: 6.52e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 5 NNAIEFKSVFKTYGDN------TVVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGEDnTARPAH- 77
Cdd:PRK13633 2 NEMIKCKNVSYKYESNeestekLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLD-TSDEENl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 78 -ELRRSMGYVLQQAGLMPHRTIVD-NISTVPRLNGVSARQAKSQALELLNTVGLDEsFAKRYPSQLSGGQAQRVGVARAL 155
Cdd:PRK13633 81 wDIRNKAGMVFQNPDNQIVATIVEeDVAFGPENLGIPPEEIRERVDESLKKVGMYE-YRRHAPHLLSGGQKQRVAIAGIL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2735597802 156 ASESSILLMDEPFSAVDPVVRADLQKELLRLQSTLGRTIIFVTHDMDEAIlLGDYVAVFaRGGRIAQFGTPEEILRE 232
Cdd:PRK13633 160 AMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAV-EADRIIVM-DSGKVVMEGTPKEIFKE 234
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
20-217 |
2.56e-27 |
|
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: 106.40 E-value: 2.56e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 20 NTVVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGedntarpahelrrSMGYVLQQAGLMPhRTIV 99
Cdd:cd03250 18 SFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG-------------SIAYVSQEPWIQN-GTIR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 100 DNI---STV--PRLNGVSARQAKSQALELL----NTV----GLDesfakrypsqLSGGQAQRVGVARALASESSILLMDE 166
Cdd:cd03250 84 ENIlfgKPFdeERYEKVIKACALEPDLEILpdgdLTEigekGIN----------LSGGQKQRISLARAVYSDADIYLLDD 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2735597802 167 PFSAVDPVVRADLQKELLRLQSTLGRTIIFVTHDMdEAILLGDYVAVFARG 217
Cdd:cd03250 154 PLSAVDAHVGRHIFENCILGLLLNNKTRILVTHQL-QLLPHADQIVVLDNG 203
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
17-204 |
4.35e-27 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 105.78 E-value: 4.35e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 17 YGDNTVVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGednTARPAH-----ELRRSMGYVLQQA- 90
Cdd:NF040873 2 YGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG---GARVAYvpqrsEVPDSLPLTVRDLv 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 91 --GLMPHRTIVdnistvpRLNGVSARQAKSQALEllnTVGLDEsFAKRYPSQLSGGQAQRVGVARALASESSILLMDEPF 168
Cdd:NF040873 79 amGRWARRGLW-------RRLTRDDRAAVDDALE---RVGLAD-LAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPT 147
|
170 180 190
....*....|....*....|....*....|....*.
gi 2735597802 169 SAVDPVVRADLqKELLRLQSTLGRTIIFVTHDMDEA 204
Cdd:NF040873 148 TGLDAESRERI-IALLAEEHARGATVVVVTHDLELV 182
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
8-217 |
1.06e-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: 103.84 E-value: 1.06e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 8 IEFKSVFKTYGDNT--VVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGED-NTARPAhELRRSMG 84
Cdd:cd03246 1 LEVENVSFRYPGAEppVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADiSQWDPN-ELGDHVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 85 YVLQQAGLMPHrTIVDNIstvprlngvsarqaksqalellntvgldesfakrypsqLSGGQAQRVGVARALASESSILLM 164
Cdd:cd03246 80 YLPQDDELFSG-SIAENI--------------------------------------LSGGQRQRLGLARALYGNPRILVL 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2735597802 165 DEPFSAVDPVVRADLQKELLRLQSTlGRTIIFVTHDMdEAILLGDYVAVFARG 217
Cdd:cd03246 121 DEPNSHLDVEGERALNQAIAALKAA-GATRIVIAHRP-ETLASADRILVLEDG 171
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
8-232 |
1.61e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 106.79 E-value: 1.61e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 8 IEFKSVFKTYGDNT-----VVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNG-------EDNTARP 75
Cdd:PRK13646 3 IRFDNVSYTYQKGTpyehqAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDitithktKDKYIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 76 aheLRRSMGYVLQ--QAGLMpHRTIVDNISTVPRLNGVSARQAKSQALELLNTVGLDESFAKRYPSQLSGGQAQRVGVAR 153
Cdd:PRK13646 83 ---VRKRIGMVFQfpESQLF-EDTVEREIIFGPKNFKMNLDEVKNYAHRLLMDLGFSRDVMSQSPFQMSGGQMRKIAIVS 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2735597802 154 ALASESSILLMDEPFSAVDPVVRADLQKELLRLQSTLGRTIIFVTHDMDEAILLGDYVAVFARGGRIAQfGTPEEILRE 232
Cdd:PRK13646 159 ILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQ-TSPKELFKD 236
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
22-202 |
3.24e-26 |
|
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: 104.44 E-value: 3.24e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 22 VVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGEDN-------TARPAHELRRS-MGYVLQQAGLM 93
Cdd:COG4778 26 VLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDGGwvdlaqaSPREILALRRRtIGYVSQFLRVI 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 94 PHRTIVDNISTVPRLNGVSARQAKSQALELLNTVGLDESFAKRYPSQLSGGQAQRVGVARALASESSILLMDEPFSAVDP 173
Cdd:COG4778 106 PRVSALDVVAEPLLERGVDREEARARARELLARLNLPERLWDLPPATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDA 185
|
170 180
....*....|....*....|....*....
gi 2735597802 174 VVRADLqKELLRLQSTLGRTIIFVTHDMD 202
Cdd:COG4778 186 ANRAVV-VELIEEAKARGTAIIGIFHDEE 213
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
5-232 |
5.97e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 104.93 E-value: 5.97e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 5 NNAIEFKSVFKTYGDNT-VVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGE--DNTARPAHELRR 81
Cdd:PRK13636 3 DYILKVEELNYNYSDGThALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKpiDYSRKGLMKLRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 82 SMGYVLQQA-GLMPHRTIVDNISTVPRLNGVSARQAKSQALELLNTVGLdeSFAKRYPSQ-LSGGQAQRVGVARALASES 159
Cdd:PRK13636 83 SVGMVFQDPdNQLFSASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGI--EHLKDKPTHcLSFGQKKRVAIAGVLVMEP 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2735597802 160 SILLMDEPFSAVDPVVRADLQKELLRLQSTLGRTIIFVTHDMDEAILLGDYVAVFARGGRIAQfGTPEEILRE 232
Cdd:PRK13636 161 KVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQ-GNPKEVFAE 232
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
19-233 |
7.04e-26 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 104.48 E-value: 7.04e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 19 DNTVVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGEDNTARPAHELRRSMGYVLQQ---AGLMPH 95
Cdd:PRK10575 23 GRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLPQQlpaAEGMTV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 96 RTIVdNISTVP------RLnGVSARQAKSQALELlntVGLdESFAKRYPSQLSGGQAQRVGVARALASESSILLMDEPFS 169
Cdd:PRK10575 103 RELV-AIGRYPwhgalgRF-GAADREKVEEAISL---VGL-KPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTS 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2735597802 170 AVDPVVRADLQKELLRLQSTLGRTIIFVTHDMDEAILLGDYVaVFARGGRIAQFGTPEEILREP 233
Cdd:PRK10575 177 ALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYL-VALRGGEMIAQGTPAELMRGE 239
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
18-232 |
8.28e-26 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 108.30 E-value: 8.28e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 18 GDNTVVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGEDNTARPAHELRRSMGYVLQQAGLMPHrT 97
Cdd:COG4618 343 SKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRHIGYLPQDVELFDG-T 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 98 IVDNIStvpRLNGVSARQAKsQALELlntVGLDE---SFAKRY-------PSQLSGGQAQRVGVARALASESSILLMDEP 167
Cdd:COG4618 422 IAENIA---RFGDADPEKVV-AAAKL---AGVHEmilRLPDGYdtrigegGARLSGGQRQRIGLARALYGDPRLVVLDEP 494
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2735597802 168 FSAVDPVVRADLQKELLRLQSTlGRTIIFVTHDMdeAIL-LGDYVAVFaRGGRIAQFGTPEEILRE 232
Cdd:COG4618 495 NSNLDDEGEAALAAAIRALKAR-GATVVVITHRP--SLLaAVDKLLVL-RDGRVQAFGPRDEVLAR 556
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
22-204 |
1.23e-25 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 102.97 E-value: 1.23e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 22 VVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGE-----DNTARPahELR-RSMGYVLQQAGLMPH 95
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQpmsklSSAAKA--ELRnQKLGFIYQFHHLLPD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 96 RTIVDNISTVPRLNGVSARQAKSQALELLNTVGLDESfAKRYPSQLSGGQAQRVGVARALASESSILLMDEPFSAVDpVV 175
Cdd:PRK11629 102 FTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHR-ANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLD-AR 179
|
170 180 190
....*....|....*....|....*....|
gi 2735597802 176 RADLQKELL-RLQSTLGRTIIFVTHDMDEA 204
Cdd:PRK11629 180 NADSIFQLLgELNRLQGTAFLVVTHDLQLA 209
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
4-235 |
2.42e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 103.25 E-value: 2.42e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 4 LNNAIEFKSVFKTYGDNTVVDNLN---LSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGEDNTARPAHELR 80
Cdd:PRK13642 1 MNKILEVENLVFKYEKESDVNQLNgvsFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 81 RSMGYVLQQA-GLMPHRTIVDNISTVPRLNGVSARQAKSQALELLNTVGLDEsFAKRYPSQLSGGQAQRVGVARALASES 159
Cdd:PRK13642 81 RKIGMVFQNPdNQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLD-FKTREPARLSGGQKQRVAVAGIIALRP 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2735597802 160 SILLMDEPFSAVDPVVRADLQKELLRLQSTLGRTIIFVTHDMDEAIlLGDYVAVFaRGGRIAQFGTPEEILREPAD 235
Cdd:PRK13642 160 EIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAA-SSDRILVM-KAGEIIKEAAPSELFATSED 233
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
8-226 |
2.55e-25 |
|
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: 101.80 E-value: 2.55e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 8 IEFKSVFKTYGDN--TVVDNLNLSIPEG-KITVfVGPSGCGKTTSLRMINRMVEHTSGTILVNGEDNTARPAHELRRSMG 84
Cdd:cd03244 3 IEFKNVSLRYRPNlpPVLKNISFSIKPGeKVGI-VGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRIS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 85 YVLQQAGLMPHrTIVDNIStvPrlNGVSARQAKSQALEllnTVGLDESFAKRYP----------SQLSGGQAQRVGVARA 154
Cdd:cd03244 82 IIPQDPVLFSG-TIRSNLD--P--FGEYSDEELWQALE---RVGLKEFVESLPGgldtvveeggENLSVGQRQLLCLARA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2735597802 155 LASESSILLMDEPFSAVDPvvradlQKELLrLQSTL-----GRTIIFVTHDMDeAILLGDYVAVFARgGRIAQFGTP 226
Cdd:cd03244 154 LLRKSKILVLDEATASVDP------ETDAL-IQKTIreafkDCTVLTIAHRLD-TIIDSDRILVLDK-GRVVEFDSP 221
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
8-201 |
2.78e-25 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 101.49 E-value: 2.78e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 8 IEFKSVFKTY-GDNTVVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGEDNTARPAHE---LRRSM 83
Cdd:PRK10908 2 IRFEHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREvpfLRRQI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 84 GYVLQQAGLMPHRTIVDNISTVPRLNGVSARQAKSQALELLNTVGLDESfAKRYPSQLSGGQAQRVGVARALASESSILL 163
Cdd:PRK10908 82 GMIFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDK-AKNFPIQLSGGEQQRVGIARAVVNKPAVLL 160
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2735597802 164 MDEPFSAVDpvvrADLQKELLRLQSTLGR---TIIFVTHDM 201
Cdd:PRK10908 161 ADEPTGNLD----DALSEGILRLFEEFNRvgvTVLMATHDI 197
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
22-220 |
1.06e-24 |
|
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: 99.04 E-value: 1.06e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 22 VVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGEDNTARPAHELRRS-MGYVL---QQAGLMPHRT 97
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAgIAYVPedrKREGLVLDLS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 98 IVDNISTvprlngvsarqaksqalellntvgldesfakryPSQLSGGQAQRVGVARALASESSILLMDEPFSAVDPVVRA 177
Cdd:cd03215 95 VAENIAL---------------------------------SSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKA 141
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2735597802 178 DLQKELLRLQSTlGRTIIFVTHDMDEAILLGDYVAVFARgGRI 220
Cdd:cd03215 142 EIYRLIRELADA-GKAVLLISSELDELLGLCDRILVMYE-GRI 182
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
8-200 |
1.28e-24 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 104.81 E-value: 1.28e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 8 IEFKSVFKTY--GDNT--VVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGEDNTARPAHEL---- 79
Cdd:PRK10535 5 LELKDIRRSYpsGEEQveVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALaqlr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 80 RRSMGYVLQQAGLMPHRTIVDNISTVPRLNGVSARQAKSQALELLNTVGLDESFAKRyPSQLSGGQAQRVGVARALASES 159
Cdd:PRK10535 85 REHFGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQ-PSQLSGGQQQRVSIARALMNGG 163
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2735597802 160 SILLMDEPFSAVDPVVRADLQKELLRLQSTlGRTIIFVTHD 200
Cdd:PRK10535 164 QVILADEPTGALDSHSGEEVMAILHQLRDR-GHTVIIVTHD 203
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
4-205 |
2.56e-24 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 100.09 E-value: 2.56e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 4 LNNAIEFKSVFKTYGDNTVVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMV--EHTSGT---ILVNGEDNTARPAHE 78
Cdd:PRK09984 1 MQTIIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgDKSAGShieLLGRTVQREGRLARD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 79 LRRS---MGYVLQQAGLMPHRTIVDNI------STVPRLNGVS--ARQAKSQALELLNTVGLdESFAKRYPSQLSGGQAQ 147
Cdd:PRK09984 81 IRKSranTGYIFQQFNLVNRLSVLENVligalgSTPFWRTCFSwfTREQKQRALQALTRVGM-VHFAHQRVSTLSGGQQQ 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2735597802 148 RVGVARALASESSILLMDEPFSAVDPVVRADLQKELLRLQSTLGRTIIFVTHDMDEAI 205
Cdd:PRK09984 160 RVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYAL 217
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-232 |
5.49e-24 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 98.62 E-value: 5.49e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 1 MSvlnNAIEFKSVFKTY----------------------GDNTVVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVE 58
Cdd:COG1134 1 MS---SMIEVENVSKSYrlyhepsrslkelllrrrrtrrEEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 59 HTSGTILVNGedntarpahelrrSMGYVLQ-QAGLMPHRTIVDNISTVPRLNGVSARQAKSQalellntvgLDE--SFA- 134
Cdd:COG1134 78 PTSGRVEVNG-------------RVSALLElGAGFHPELTGRENIYLNGRLLGLSRKEIDEK---------FDEivEFAe 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 135 ---------KRYPSqlsgGQAQRVGVARALASESSILLMDEPFSAVDPVVRADLQKELLRLQSTlGRTIIFVTHDM---- 201
Cdd:COG1134 136 lgdfidqpvKTYSS----GMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRES-GRTVIFVSHSMgavr 210
|
250 260 270
....*....|....*....|....*....|....
gi 2735597802 202 ---DEAILLgdyvavfaRGGRIAQFGTPEEILRE 232
Cdd:COG1134 211 rlcDRAIWL--------EKGRLVMDGDPEEVIAA 236
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
23-233 |
7.30e-24 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 98.52 E-value: 7.30e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 23 VDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGEDNTARPAHELRRsMGYV--LQQAGLMPHRTIVD 100
Cdd:PRK11300 21 VNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIAR-MGVVrtFQHVRLFREMTVIE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 101 NI-------STVPRLNGV----SARQAKSQALEL----LNTVGLDEsFAKRYPSQLSGGQAQRVGVARALASESSILLMD 165
Cdd:PRK11300 100 NLlvaqhqqLKTGLFSGLlktpAFRRAESEALDRaatwLERVGLLE-HANRQAGNLAYGQQRRLEIARCMVTQPEILMLD 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2735597802 166 EPFSAVDPVVRADLQKELLRLQSTLGRTIIFVTHDMDEAILLGDYVAVFARGGRIAQfGTPEEILREP 233
Cdd:PRK11300 179 EPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLAN-GTPEEIRNNP 245
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
23-255 |
9.85e-24 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 98.23 E-value: 9.85e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 23 VDNLNLSIPEGKITVFVGPSGCGKTTS----LRMINRMVEHTSGTILVNGEdntARPAHELR-RSMGYVLQ--QAGLMPH 95
Cdd:PRK10418 19 VHGVSLTLQRGRVLALVGGSGSGKSLTcaaaLGILPAGVRQTAGRVLLDGK---PVAPCALRgRKIATIMQnpRSAFNPL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 96 RTIVDNISTVPRLNGVSARQAksQALELLNTVGLDES--FAKRYPSQLSGGQAQRVGVARALASESSILLMDEPFSAVDP 173
Cdd:PRK10418 96 HTMHTHARETCLALGKPADDA--TLTAALEAVGLENAarVLKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTTDLDV 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 174 VVRADLQKELLRLQSTLGRTIIFVTHDMDEAILLGDYVAVFARgGRIAQFGTPEEILREPADDFVASFVGRDRGMRRLTF 253
Cdd:PRK10418 174 VAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSH-GRIVEQGDVETLFNAPKHAVTRSLVSAHLALYGMEL 252
|
..
gi 2735597802 254 AS 255
Cdd:PRK10418 253 AS 254
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
19-270 |
1.10e-23 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 101.71 E-value: 1.10e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 19 DNTVVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRM-----VEHTSGTILVNGEDNTARPAHELRR----SMGYVLQQ 89
Cdd:PRK15134 21 VRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLlpsppVVYPSGDIRFHGESLLHASEQTLRGvrgnKIAMIFQE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 90 --AGLMPHRTIVDNISTVPRLN-GVSARQAKSQALELLNTVGLDESfAKR---YPSQLSGGQAQRVGVARALASESSILL 163
Cdd:PRK15134 101 pmVSLNPLHTLEKQLYEVLSLHrGMRREAARGEILNCLDRVGIRQA-AKRltdYPHQLSGGERQRVMIAMALLTRPELLI 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 164 MDEPFSAVDPVVRADLQKELLRLQSTLGRTIIFVTHDMDEAILLGDYVAVFaRGGRIAQFGTPEEILREPADDFVasfvg 243
Cdd:PRK15134 180 ADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVM-QNGRCVEQNRAATLFSAPTHPYT----- 253
|
250 260
....*....|....*....|....*..
gi 2735597802 244 rdrgmRRLTFASGADVPIhPLDAQQTP 270
Cdd:PRK15134 254 -----QKLLNSEPSGDPV-PLPEPASP 274
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
15-237 |
1.11e-23 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 101.71 E-value: 1.11e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 15 KTYGDNTVVDNLNLSIPEGKITVFVGPSGCGKTTS----LRMINrmvehTSGTILVNGedntaRPAHELRRSMgyvlqqa 90
Cdd:PRK15134 294 RTVDHNVVVKNISFTLRPGETLGLVGESGSGKSTTglalLRLIN-----SQGEIWFDG-----QPLHNLNRRQ------- 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 91 gLMPHRTIVD------NISTVPRLN--------------GVSARQAKSQALELLNTVGLDESFAKRYPSQLSGGQAQRVG 150
Cdd:PRK15134 357 -LLPVRHRIQvvfqdpNSSLNPRLNvlqiieeglrvhqpTLSAAQREQQVIAVMEEVGLDPETRHRYPAEFSGGQRQRIA 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 151 VARALASESSILLMDEPFSAVDPVVRADLQKELLRLQSTLGRTIIFVTHDMDEAILLGDYVAVFaRGGRIAQFGTPEEIL 230
Cdd:PRK15134 436 IARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVL-RQGEVVEQGDCERVF 514
|
....*..
gi 2735597802 231 REPADDF 237
Cdd:PRK15134 515 AAPQQEY 521
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1-219 |
1.11e-23 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 97.48 E-value: 1.11e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 1 MSVLNNAIEFKSVFKTYGDNTVVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGEDNTARPAHELR 80
Cdd:PRK10247 1 MQENSPLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 81 RSMGYVLQQAGLMPHrTIVDNISTVPRLNGVSARQAKSQAleLLNTVGLDESFAKRYPSQLSGGQAQRVGVARALASESS 160
Cdd:PRK10247 81 QQVSYCAQTPTLFGD-TVYDNLIFPWQIRNQQPDPAIFLD--DLERFALPDTILTKNIAELSGGEKQRISLIRNLQFMPK 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2735597802 161 ILLMDEPFSAVDPVVRADLQKELLRLQSTLGRTIIFVTHDMDEAILLGDYVAVFARGGR 219
Cdd:PRK10247 158 VLLLDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDEINHADKVITLQPHAGE 216
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
8-207 |
1.25e-23 |
|
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: 95.84 E-value: 1.25e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 8 IEFKSVFKTYGDN--TVVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGEdNTARPAHELRRSMGy 85
Cdd:cd03247 1 LSINNVSFSYPEQeqQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGV-PVSDLEKALSSLIS- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 86 VLQQAGLMPHRTIVDNISTvprlngvsarqaksqalellntvgldesfakrypsQLSGGQAQRVGVARALASESSILLMD 165
Cdd:cd03247 79 VLNQRPYLFDTTLRNNLGR-----------------------------------RFSGGERQRLALARILLQDAPIVLLD 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2735597802 166 EPFSAVDPVVradlQKELLRL--QSTLGRTIIFVTH------DMDEAILL 207
Cdd:cd03247 124 EPTVGLDPIT----ERQLLSLifEVLKDKTLIWITHhltgieHMDKILFL 169
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
18-200 |
2.18e-23 |
|
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: 100.90 E-value: 2.18e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 18 GDNTVVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGEDNTARPAHELRRSMGYVLQQAGLMpHRT 97
Cdd:TIGR02868 346 GAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLF-DTT 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 98 IVDNIstvpRLNGVSARQAksQALELLNTVGLdESFAKRYP-----------SQLSGGQAQRVGVARALASESSILLMDE 166
Cdd:TIGR02868 425 VRENL----RLARPDATDE--ELWAALERVGL-ADWLRALPdgldtvlgeggARLSGGERQRLALARALLADAPILLLDE 497
|
170 180 190
....*....|....*....|....*....|....
gi 2735597802 167 PFSAVDPVVRADLQKELlrLQSTLGRTIIFVTHD 200
Cdd:TIGR02868 498 PTEHLDAETADELLEDL--LAALSGRTVVLITHH 529
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
7-235 |
2.23e-23 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 101.19 E-value: 2.23e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 7 AIEFKSV-FKTYGDNTVVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGEDNTARPAHELRRSMGY 85
Cdd:PRK13657 334 AVEFDDVsFSYDNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 86 VLQQAGLMpHRTIVDNIStVPRLNGVSA--RQA--KSQALELL--NTVGLDESFAKRyPSQLSGGQAQRVGVARALASES 159
Cdd:PRK13657 414 VFQDAGLF-NRSIEDNIR-VGRPDATDEemRAAaeRAQAHDFIerKPDGYDTVVGER-GRQLSGGERQRLAIARALLKDP 490
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 160 SILLMDEPFSAVDPVVRADLQKELLRLQStlGRTIIFVTH------DMDEAILL--------GDYVAVFARGGRI----- 220
Cdd:PRK13657 491 PILILDEATSALDVETEAKVKAALDELMK--GRTTFIIAHrlstvrNADRILVFdngrvvesGSFDELVARGGRFaallr 568
|
250
....*....|....*
gi 2735597802 221 AQFGTPEEILREPAD 235
Cdd:PRK13657 569 AQGMLQEDERRKQPA 583
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
7-223 |
2.27e-23 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 101.05 E-value: 2.27e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 7 AIEFKSVFKTYGDNT--VVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGEDNTARPAHELRRSMG 84
Cdd:PRK11160 338 SLTLNNVSFTYPDQPqpVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQAIS 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 85 YVLQQAGLMPHrTIVDNIstvprlngvsaRQAKSQA-----LELLNTVGLDESFAKRYP---------SQLSGGQAQRVG 150
Cdd:PRK11160 418 VVSQRVHLFSA-TLRDNL-----------LLAAPNAsdealIEVLQQVGLEKLLEDDKGlnawlgeggRQLSGGEQRRLG 485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 151 VARALASESSILLMDEPFSAVDpvvrADLQKELLRL--QSTLGRTIIFVTH------DMDEAILL--------GDYVAVF 214
Cdd:PRK11160 486 IARALLHDAPLLLLDEPTEGLD----AETERQILELlaEHAQNKTVLMITHrltgleQFDRICVMdngqiieqGTHQELL 561
|
....*....
gi 2735597802 215 ARGGRIAQF 223
Cdd:PRK11160 562 AQQGRYYQL 570
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
23-283 |
8.91e-23 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 99.54 E-value: 8.91e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 23 VDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVN--------------GEDNTARPAHELRRSMGYVLQ 88
Cdd:PRK10261 32 VRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDkmllrrrsrqvielSEQSAAQMRHVRGADMAMIFQ 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 89 Q--AGLMPHRTIVDNISTVPRLN-GVSARQAKSQALELLNTVGLDESFA--KRYPSQLSGGQAQRVGVARALASESSILL 163
Cdd:PRK10261 112 EpmTSLNPVFTVGEQIAESIRLHqGASREEAMVEAKRMLDQVRIPEAQTilSRYPHQLSGGMRQRVMIAMALSCRPAVLI 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 164 MDEPFSAVDPVVRADLQKELLRLQSTLGRTIIFVTHDMDEAILLGDYVAVFARgGRIAQFGTPEEILREPADDFVASFVG 243
Cdd:PRK10261 192 ADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQ-GEAVETGSVEQIFHAPQHPYTRALLA 270
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 2735597802 244 rdrGMRRLTFASGADVP-----IHPLDAQQTPWQQWQLNVEDGRP 283
Cdd:PRK10261 271 ---AVPQLGAMKGLDYPrrfplISLEHPAKQEPPIEQDTVVDGEP 312
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
22-233 |
1.25e-22 |
|
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: 99.25 E-value: 1.25e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 22 VVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGEDNTARPAHELRRSMGYVlQQAGLMPHRTIVDN 101
Cdd:TIGR03796 494 LIENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIPREEIPREVLANSVAMV-DQDIFLFEGTVRDN 572
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 102 IS----TVPRLNGVSArqAKSQAL--ELLNTVGLDESFAKRYPSQLSGGQAQRVGVARALASESSILLMDEPFSAVDPVV 175
Cdd:TIGR03796 573 LTlwdpTIPDADLVRA--CKDAAIhdVITSRPGGYDAELAEGGANLSGGQRQRLEIARALVRNPSILILDEATSALDPET 650
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2735597802 176 RADLQKELLRlqstLGRTIIFVTH------DMDEAILLgDYvavfargGRIAQFGTPEEILREP 233
Cdd:TIGR03796 651 EKIIDDNLRR----RGCTCIIVAHrlstirDCDEIIVL-ER-------GKVVQRGTHEELWAVG 702
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
21-202 |
1.62e-22 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 94.25 E-value: 1.62e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 21 TVVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGEDNTarpahelrrsmgyvlqqagLMPHRTIVD 100
Cdd:COG2401 44 YVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVDVPDNQ-------------------FGREASLID 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 101 NIstvprlngvSARQAKSQALELLNTVGLDESFA-KRYPSQLSGGQAQRVGVARALASESSILLMDEPFSAVDPVVRADL 179
Cdd:COG2401 105 AI---------GRKGDFKDAVELLNAVGLSDAVLwLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRV 175
|
170 180
....*....|....*....|...
gi 2735597802 180 QKELLRLQSTLGRTIIFVTHDMD 202
Cdd:COG2401 176 ARNLQKLARRAGITLVVATHHYD 198
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
4-233 |
2.01e-22 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 98.64 E-value: 2.01e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 4 LNNAIEFKSVFKTY---GDNTVVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGEDNTARPAHELR 80
Cdd:TIGR00958 475 LEGLIEFQDVSFSYpnrPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLH 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 81 RSMGYVLQQAGLMpHRTIVDNISTVPRLNGVSARQAKSQALELLNTVGldeSFAKRYP-------SQLSGGQAQRVGVAR 153
Cdd:TIGR00958 555 RQVALVGQEPVLF-SGSVRENIAYGLTDTPDEEIMAAAKAANAHDFIM---EFPNGYDtevgekgSQLSGGQKQRIAIAR 630
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 154 ALASESSILLMDEPFSAVDPVVRADLQKellrLQSTLGRTIIFVTHDMdEAILLGDYVAVFaRGGRIAQFGTPEEILREP 233
Cdd:TIGR00958 631 ALVRKPRVLILDEATSALDAECEQLLQE----SRSRASRTVLLIAHRL-STVERADQILVL-KKGSVVEMGTHKQLMEDQ 704
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
15-224 |
2.31e-22 |
|
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: 93.75 E-value: 2.31e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 15 KTYGDNTVVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGEDntaRPAHELrrsmgyvlqQAGLMP 94
Cdd:cd03220 30 GEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRV---SSLLGL---------GGGFNP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 95 HRTIVDNISTVPRLNGVSARQAKSQALELLNTVGLDESFAKRYpSQLSGGQAQRVGVARALASESSILLMDEPFSAVDPV 174
Cdd:cd03220 98 ELTGRENIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPV-KTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAA 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2735597802 175 VRADLQKELLRLQSTlGRTIIFVTHDMDEAILLGDYVAVFARgGRIAQFG 224
Cdd:cd03220 177 FQEKCQRRLRELLKQ-GKTVILVSHDPSSIKRLCDRALVLEK-GKIRFDG 224
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
22-199 |
6.68e-22 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 92.33 E-value: 6.68e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 22 VVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEH---TSGTILVNGEdntARPAHELRRSMGYVLQQAGLMPHRTI 98
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGggtTSGQILFNGQ---PRKPDQFQKCVAYVRQDDILLPGLTV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 99 VD-----NISTVPRLNGVSARQaKSQALELLNTVGlDESFAKRYPSQLSGGQAQRVGVARALASESSILLMDEPFSAVDP 173
Cdd:cd03234 99 REtltytAILRLPRKSSDAIRK-KRVEDVLLRDLA-LTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDS 176
|
170 180
....*....|....*....|....*.
gi 2735597802 174 VVRADLQKELLRLqSTLGRTIIFVTH 199
Cdd:cd03234 177 FTALNLVSTLSQL-ARRNRIVILTIH 201
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
18-232 |
1.01e-21 |
|
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: 96.26 E-value: 1.01e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 18 GDNTVVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGEDNTARPAHELRRSMGYVLQQAGLMPHrT 97
Cdd:TIGR01842 329 GKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGKHIGYLPQDVELFPG-T 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 98 IVDNISTVPRlnGVSARQ----AK-SQALELLNTV--GLDESFAKRyPSQLSGGQAQRVGVARALASESSILLMDEPFSA 170
Cdd:TIGR01842 408 VAENIARFGE--NADPEKiieaAKlAGVHELILRLpdGYDTVIGPG-GATLSGGQRQRIALARALYGDPKLVVLDEPNSN 484
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2735597802 171 VDPVVRADLQKELLRLQSTlGRTIIFVTHDMdEAILLGDYVAVFaRGGRIAQFGTPEEILRE 232
Cdd:TIGR01842 485 LDEEGEQALANAIKALKAR-GITVVVITHRP-SLLGCVDKILVL-QDGRIARFGERDEVLAK 543
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
11-217 |
1.26e-21 |
|
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: 92.01 E-value: 1.26e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 11 KSVFK-TYGDNTVVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGEDNTARpAHELRRSMGYVL-Q 88
Cdd:cd03267 24 KSLFKrKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKR-RKKFLRRIGVVFgQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 89 QAGLMPHRTIVDNISTVPRLNGVSARQAKSQALELLNTVGLdESFAKRYPSQLSGGQAQRVGVARALASESSILLMDEPF 168
Cdd:cd03267 103 KTQLWWDLPVIDSFYLLAAIYDLPPARFKKRLDELSELLDL-EELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPT 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2735597802 169 SAVDPVVRADLQKELLRLQSTLGRTIIFVTHDMDEAILLGDYVAVFARG 217
Cdd:cd03267 182 IGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKG 230
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
8-234 |
2.05e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 92.36 E-value: 2.05e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 8 IEFKSVFKTYGDNT-VVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGEDnTARPA--HELRRSMG 84
Cdd:PRK13644 2 IRLENVSYSYPDGTpALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGID-TGDFSklQGIRKLVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 85 YVLQQaglmPH-----RTIVDNISTVPR---LNGVSARQAKSQALEllnTVGLdESFAKRYPSQLSGGQAQRVGVARALA 156
Cdd:PRK13644 81 IVFQN----PEtqfvgRTVEEDLAFGPEnlcLPPIEIRKRVDRALA---EIGL-EKYRHRSPKTLSGGQGQCVALAGILT 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2735597802 157 SESSILLMDEPFSAVDPVVRADLQKELLRLQSTlGRTIIFVTHDMDEaILLGDYVAVFARgGRIAQFGTPEEILREPA 234
Cdd:PRK13644 153 MEPECLIFDEVTSMLDPDSGIAVLERIKKLHEK-GKTIVYITHNLEE-LHDADRIIVMDR-GKIVLEGEPENVLSDVS 227
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
15-233 |
2.19e-21 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 91.91 E-value: 2.19e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 15 KTYGDNTVVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGEDNT-----ARPAHELRRSM----GY 85
Cdd:PRK11701 14 KLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQlrdlyALSEAERRRLLrtewGF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 86 VLQQA--GLMPHRTIVDNISTvpRLNGVSAR---QAKSQALELLNTVGLDESFAKRYPSQLSGGQAQRVGVARALASESS 160
Cdd:PRK11701 94 VHQHPrdGLRMQVSAGGNIGE--RLMAVGARhygDIRATAGDWLERVEIDAARIDDLPTTFSGGMQQRLQIARNLVTHPR 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2735597802 161 ILLMDEPFSAVDPVVRADLQKELLRLQSTLGRTIIFVTHDMDEAILLGDYVAVFaRGGRIAQFGTPEEILREP 233
Cdd:PRK11701 172 LVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVM-KQGRVVESGLTDQVLDDP 243
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
14-234 |
2.19e-21 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 93.25 E-value: 2.19e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 14 FKTY-GDNTVVDNLNLSIPEGKITVFVGPSGCGKT-TSLRMINRMVE--HTSGTILVNGEDNTARPAHELRR------SM 83
Cdd:PRK09473 22 FSTPdGDVTAVNDLNFSLRAGETLGIVGESGSGKSqTAFALMGLLAAngRIGGSATFNGREILNLPEKELNKlraeqiSM 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 84 GYVLQQAGLMPHRTIVDNISTVPRLN-GVSARQAKSQALELLNTVGLDESfAKR---YPSQLSGGQAQRVGVARALASES 159
Cdd:PRK09473 102 IFQDPMTSLNPYMRVGEQLMEVLMLHkGMSKAEAFEESVRMLDAVKMPEA-RKRmkmYPHEFSGGMRQRVMIAMALLCRP 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2735597802 160 SILLMDEPFSAVDPVVRADLQKELLRLQSTLGRTIIFVTHDMDEAILLGDYVAVFaRGGRIAQFGTPEEILREPA 234
Cdd:PRK09473 181 KLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVM-YAGRTMEYGNARDVFYQPS 254
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
8-232 |
4.34e-21 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 94.32 E-value: 4.34e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 8 IEFKSVFKTY--GDNTVVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGEDNTARPAHELRRSMGY 85
Cdd:PRK11176 342 IEFRNVTFTYpgKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVAL 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 86 VLQQAGLMpHRTIVDNIStVPRLNGVS-------ARQAksQALELLNTV--GLDESFAKRYPSqLSGGQAQRVGVARALA 156
Cdd:PRK11176 422 VSQNVHLF-NDTIANNIA-YARTEQYSreqieeaARMA--YAMDFINKMdnGLDTVIGENGVL-LSGGQRQRIAIARALL 496
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 157 SESSILLMDEPFSAVDPVVRADLQKELLRLQSTlgRTIIFVTHDM------DEAILLGDyvavfargGRIAQFGTPEEIL 230
Cdd:PRK11176 497 RDSPILILDEATSALDTESERAIQAALDELQKN--RTSLVIAHRLstiekaDEILVVED--------GEIVERGTHAELL 566
|
..
gi 2735597802 231 RE 232
Cdd:PRK11176 567 AQ 568
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
21-200 |
7.01e-21 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 89.84 E-value: 7.01e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 21 TVVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGE-----DNTARPAheLR-RSMGYVLQQAGLMP 94
Cdd:PRK10584 24 SILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQplhqmDEEARAK--LRaKHVGFVFQSFMLIP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 95 HRTIVDNISTVPRLNGVSARQAKSQALELLNTVGLDESFaKRYPSQLSGGQAQRVGVARALASESSILLMDEPFSAVDPV 174
Cdd:PRK10584 102 TLNALENVELPALLRGESSRQSRNGAKALLEQLGLGKRL-DHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQ 180
|
170 180
....*....|....*....|....*.
gi 2735597802 175 VRADLQKELLRLQSTLGRTIIFVTHD 200
Cdd:PRK10584 181 TGDKIADLLFSLNREHGTTLILVTHD 206
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
10-200 |
7.50e-21 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 93.59 E-value: 7.50e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 10 FKSVFKTYGDNTVVDNLNLSIPEG-KITVfVGPSGCGKTTSLRMINRMVEHTSGTILVNGEdntarpaheLRrsMGYVLQ 88
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGdRIGL-VGRNGAGKSTLLKILAGELEPDSGEVSIPKG---------LR--IGYLPQ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 89 QAGLMPHRTIVDNI--------STVPRLNGVSAR------------------------QAKSQALELLNTVGLDESFAKR 136
Cdd:COG0488 69 EPPLDDDLTVLDTVldgdaelrALEAELEELEAKlaepdedlerlaelqeefealggwEAEARAEEILSGLGFPEEDLDR 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2735597802 137 YPSQLSGGQAQRVGVARALASESSILLMDEP-----FSAVdpvvrADLQKELLRLQSTLgrtiIFVTHD 200
Cdd:COG0488 149 PVSELSGGWRRRVALARALLSEPDLLLLDEPtnhldLESI-----EWLEEFLKNYPGTV----LVVSHD 208
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
4-199 |
2.56e-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: 88.30 E-value: 2.56e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 4 LNNAIEFKSV---FKTYGDNTVVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGEDNTARPAHELR 80
Cdd:cd03248 8 LKGIVKFQNVtfaYPTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLH 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 81 RSMGYVLQQAGLMPhRTIVDNIS----TVPrLNGVSARQAKSQALELLNTV--GLDESFAKRyPSQLSGGQAQRVGVARA 154
Cdd:cd03248 88 SKVSLVGQEPVLFA-RSLQDNIAyglqSCS-FECVKEAAQKAHAHSFISELasGYDTEVGEK-GSQLSGGQKQRVAIARA 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2735597802 155 LASESSILLMDEPFSAVDpvVRADLQKELLRLQSTLGRTIIFVTH 199
Cdd:cd03248 165 LIRNPQVLILDEATSALD--AESEQQVQQALYDWPERRTVLVIAH 207
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
17-230 |
7.02e-20 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 88.14 E-value: 7.02e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 17 YGDNTVVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGE--DNTARPAHELRRSMGYVLQQAGLMP 94
Cdd:PRK13638 11 YQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKplDYSKRGLLALRQQVATVFQDPEQQI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 95 HRTIVD-NISTVPRLNGVSARQAKSQALELLNTVglDESFAKRYPSQ-LSGGQAQRVGVARALASESSILLMDEPFSAVD 172
Cdd:PRK13638 91 FYTDIDsDIAFSLRNLGVPEAEITRRVDEALTLV--DAQHFRHQPIQcLSHGQKKRVAIAGALVLQARYLLLDEPTAGLD 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2735597802 173 PVVRADLQKELLRLQSTlGRTIIFVTHDMDEAILLGDYVAVFARGGRIAQfGTPEEIL 230
Cdd:PRK13638 169 PAGRTQMIAIIRRIVAQ-GNHVIISSHDIDLIYEISDAVYVLRQGQILTH-GAPGEVF 224
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
22-231 |
1.22e-19 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 89.69 E-value: 1.22e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 22 VVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGED-NTARPAHELRRSMGYV---LQQAGLMPHRT 97
Cdd:COG1129 267 VVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPvRIRSPRDAIRAGIAYVpedRKGEGLVLDLS 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 98 IVDNIsTVPRLNG------VSARQAKSQALELLNTVGLdesfakRYPS------QLSGGQAQRVGVARALASESSILLMD 165
Cdd:COG1129 347 IRENI-TLASLDRlsrgglLDRRRERALAEEYIKRLRI------KTPSpeqpvgNLSGGNQQKVVLAKWLATDPKVLILD 419
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2735597802 166 EPFSAVDpvVRAdlQKELLRLQSTL---GRTIIFVTHDMDEAILLGDYVAVFaRGGRI-AQFG----TPEEILR 231
Cdd:COG1129 420 EPTRGID--VGA--KAEIYRLIRELaaeGKAVIVISSELPELLGLSDRILVM-REGRIvGELDreeaTEEAIMA 488
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
23-233 |
1.39e-19 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 89.90 E-value: 1.39e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 23 VDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTsGTILVNG-EDNTARPAHeLRRSMGYVLQQAGLmPHRTIVDN 101
Cdd:PRK11174 366 AGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPYQ-GSLKINGiELRELDPES-WRKHLSWVGQNPQL-PHGTLRDN 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 102 IS-TVPRLNGVSARQA--KSQALELLN--TVGLDesfakrYP-----SQLSGGQAQRVGVARALASESSILLMDEPFSAV 171
Cdd:PRK11174 443 VLlGNPDASDEQLQQAleNAWVSEFLPllPQGLD------TPigdqaAGLSVGQAQRLALARALLQPCQLLLLDEPTASL 516
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2735597802 172 dpvvraDLQKELLRLQS----TLGRTIIFVTH------DMDEAILLgdyvavfaRGGRIAQFGTPEEILREP 233
Cdd:PRK11174 517 ------DAHSEQLVMQAlnaaSRRQTTLMVTHqledlaQWDQIWVM--------QDGQIVQQGDYAELSQAG 574
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1-233 |
1.66e-19 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 87.87 E-value: 1.66e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 1 MSVLNnaIEFKSVfkTYGDNTV----VDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEH----TSGTILVNGEDNT 72
Cdd:PRK11022 1 MALLN--VDKLSV--HFGDESApfraVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDYpgrvMAEKLEFNGQDLQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 73 ARPAHELRRSMG----YVLQQA--GLMPHRTIVDNISTVPRLN-GVSARQAKSQALELLNTVGLD--ESFAKRYPSQLSG 143
Cdd:PRK11022 77 RISEKERRNLVGaevaMIFQDPmtSLNPCYTVGFQIMEAIKVHqGGNKKTRRQRAIDLLNQVGIPdpASRLDVYPHQLSG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 144 GQAQRVGVARALASESSILLMDEPFSAVDPVVRADLQKELLRLQSTLGRTIIFVTHDMDEAILLGDYVAVFaRGGRIAQF 223
Cdd:PRK11022 157 GMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVM-YAGQVVET 235
|
250
....*....|
gi 2735597802 224 GTPEEILREP 233
Cdd:PRK11022 236 GKAHDIFRAP 245
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
5-200 |
1.98e-19 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 89.35 E-value: 1.98e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 5 NNAIEFKSVFKTYGDNTVVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTIlvngedntaRPAHELRrsMG 84
Cdd:COG0488 313 KKVLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTV---------KLGETVK--IG 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 85 YVLQ-QAGLMPHRTIVDNISTV-PRLNGVSARQaksqaleLLNTVGLDESFAKRYPSQLSGGQAQRVGVARALASESSIL 162
Cdd:COG0488 382 YFDQhQEELDPDKTVLDELRDGaPGGTEQEVRG-------YLGRFLFSGDDAFKPVGVLSGGEKARLALAKLLLSPPNVL 454
|
170 180 190
....*....|....*....|....*....|....*...
gi 2735597802 163 LMDEPFSAVDPVVRADLQKELLRLQstlGrTIIFVTHD 200
Cdd:COG0488 455 LLDEPTNHLDIETLEALEEALDDFP---G-TVLLVSHD 488
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
8-200 |
2.19e-19 |
|
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: 83.27 E-value: 2.19e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 8 IEFKSVFKTYGDNTVVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGedntarpahelRRSMGYVl 87
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGS-----------TVKIGYF- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 88 qqaglmphrtivdnistvprlngvsarqaksqalellntvgldesfakrypSQLSGGQAQRVGVARALASESSILLMDEP 167
Cdd:cd03221 69 ---------------------------------------------------EQLSGGEKMRLALAKLLLENPNLLLLDEP 97
|
170 180 190
....*....|....*....|....*....|...
gi 2735597802 168 FSAVDPVVRADLQKELLRLQstlgRTIIFVTHD 200
Cdd:cd03221 98 TNHLDLESIEALEEALKEYP----GTVILVSHD 126
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
22-233 |
2.34e-19 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 87.65 E-value: 2.34e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 22 VVDNLNLSIPEGKITVFVGPSGCGKTTSLRMI------------NRMVehtsgtilVNGEDNTARPAHELRRSMG----Y 85
Cdd:COG4170 22 AVDRVSLTLNEGEIRGLVGESGSGKSLIAKAIcgitkdnwhvtaDRFR--------WNGIDLLKLSPRERRKIIGreiaM 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 86 VLQ--QAGLMPHRTIVDNISTV---PRLNGV---SARQAKSQALELLNTVGL--DESFAKRYPSQLSGGQAQRVGVARAL 155
Cdd:COG4170 94 IFQepSSCLDPSAKIGDQLIEAipsWTFKGKwwqRFKWRKKRAIELLHRVGIkdHKDIMNSYPHELTEGECQKVMIAMAI 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2735597802 156 ASESSILLMDEPFSAVDPVVRADLQKELLRLQSTLGRTIIFVTHDMDEAILLGDYVAVFaRGGRIAQFGTPEEILREP 233
Cdd:COG4170 174 ANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVL-YCGQTVESGPTEQILKSP 250
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
7-245 |
3.95e-19 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 88.16 E-value: 3.95e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 7 AIEFKSVFKTYGDNTVVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGEDNTAR-PAHELRRSMGY 85
Cdd:COG3845 5 ALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRsPRDAIALGIGM 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 86 VLQQAGLMPHRTIVDNI--STVPRLNGV-SARQAKSQALELLNTVGLDESfAKRYPSQLSGGQAQRVGVARALASESSIL 162
Cdd:COG3845 85 VHQHFMLVPNLTVAENIvlGLEPTKGGRlDRKAARARIRELSERYGLDVD-PDAKVEDLSVGEQQRVEILKALYRGARIL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 163 LMDEPFSAVDPVVRADLQKELLRLQSTlGRTIIFVTHDMDEAILLGDYVAVFaRGGRIAQFGTPEEilrEPADDFVASFV 242
Cdd:COG3845 164 ILDEPTAVLTPQEADELFEILRRLAAE-GKSIIFITHKLREVMAIADRVTVL-RRGKVVGTVDTAE---TSEEELAELMV 238
|
...
gi 2735597802 243 GRD 245
Cdd:COG3845 239 GRE 241
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
18-173 |
5.50e-19 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 83.95 E-value: 5.50e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 18 GDNTVVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGEDnTARPAHELRRSMGYVLQQAGLMPHRT 97
Cdd:TIGR01189 11 GERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTP-LAEQRDEPHENILYLGHLPGLKPELS 89
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2735597802 98 IVDNISTVPRLNGvSARQAKSQALEllnTVGLDeSFAKRYPSQLSGGQAQRVGVARALASESSILLMDEPFSAVDP 173
Cdd:TIGR01189 90 ALENLHFWAAIHG-GAQRTIEDALA---AVGLT-GFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDK 160
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
7-243 |
1.33e-18 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 87.10 E-value: 1.33e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 7 AIEFKSVFKTYGDNTVVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGEDNTARPaHELRRSMGYV 86
Cdd:NF033858 266 AIEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDAGD-IATRRRVGYM 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 87 LQQAGLMPHRTIVDNISTVPRLNGVSARQAKSQALELLNTVGLDEsFAKRYPSQLSGGQAQRVGVARALASESSILLMDE 166
Cdd:NF033858 345 SQAFSLYGELTVRQNLELHARLFHLPAAEIAARVAEMLERFDLAD-VADALPDSLPLGIRQRLSLAVAVIHKPELLILDE 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 167 PFSAVDPVVRADLQKELLRLQSTLGRTiIFV-THDMDEAillgdyvavfARGGRIAQF--------GTPEEILRE-PADD 236
Cdd:NF033858 424 PTSGVDPVARDMFWRLLIELSREDGVT-IFIsTHFMNEA----------ERCDRISLMhagrvlasDTPAALVAArGAAT 492
|
....*..
gi 2735597802 237 FVASFVG 243
Cdd:NF033858 493 LEEAFIA 499
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
6-246 |
1.37e-18 |
|
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: 87.31 E-value: 1.37e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 6 NAIEFKSVFKTY--GDNTVVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGedntarpahelrrSM 83
Cdd:TIGR00957 635 NSITVHNATFTWarDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKG-------------SV 701
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 84 GYVLQQAGLMpHRTIVDNISTVPRLNGVSARQAkSQALELLNTV----GLDESFAKRYPSQLSGGQAQRVGVARALASES 159
Cdd:TIGR00957 702 AYVPQQAWIQ-NDSLRENILFGKALNEKYYQQV-LEACALLPDLeilpSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNA 779
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 160 SILLMDEPFSAVDPVVRADLQKELLRLQSTL-GRTIIFVTHDM------DEAILL--------GDYVAVFARGGRIAQF- 223
Cdd:TIGR00957 780 DIYLFDDPLSAVDAHVGKHIFEHVIGPEGVLkNKTRILVTHGIsylpqvDVIIVMsggkisemGSYQELLQRDGAFAEFl 859
|
250 260
....*....|....*....|....*
gi 2735597802 224 --GTPEEILREPADDFVASFVGRDR 246
Cdd:TIGR00957 860 rtYAPDEQQGHLEDSWTALVSGEGK 884
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
23-236 |
2.46e-18 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 83.69 E-value: 2.46e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 23 VDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGEDNTARPAHELRRSMGYVLQQA--GLMPhRTIVD 100
Cdd:PRK15112 29 VKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSQRIRMIFQDPstSLNP-RQRIS 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 101 NISTVP-RLN-GVSARQAKSQALELLNTVGLDESFAKRYPSQLSGGQAQRVGVARALASESSILLMDEPFSAVDPVVRAD 178
Cdd:PRK15112 108 QILDFPlRLNtDLEPEQREKQIIETLRQVGLLPDHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQ 187
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2735597802 179 LQKELLRLQSTLGRTIIFVTHDMDEAILLGDYVAVFaRGGRIAQFGTPEEILREPADD 236
Cdd:PRK15112 188 LINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVM-HQGEVVERGSTADVLASPLHE 244
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
7-231 |
2.48e-18 |
|
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: 86.03 E-value: 2.48e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 7 AIEFKSVFKTY-GDNTVVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGEDNTARPAHELRRSMGY 85
Cdd:COG5265 357 EVRFENVSFGYdPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGI 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 86 VLQQAGLMpHRTIVDNIstvpRLNGVSARQAK-SQALELLNTVGLDESFAKRYPSQ-------LSGGQAQRVGVARALAS 157
Cdd:COG5265 437 VPQDTVLF-NDTIAYNI----AYGRPDASEEEvEAAARAAQIHDFIESLPDGYDTRvgerglkLSGGEKQRVAIARTLLK 511
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 158 ESSILLMDEPFSAVDPVVRADLQKELLRLqsTLGRTIIFVTH------DMDEAILLGDyvavfargGRIAQFGTPEEILR 231
Cdd:COG5265 512 NPPILIFDEATSALDSRTERAIQAALREV--ARGRTTLVIAHrlstivDADEILVLEA--------GRIVERGTHAELLA 581
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
5-200 |
3.30e-18 |
|
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: 85.76 E-value: 3.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 5 NNAIEFKSVFKTYGDNTVVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVnGEdnTARpahelrrsMG 84
Cdd:TIGR03719 320 DKVIEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GE--TVK--------LA 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 85 YVLQQ-AGLMPHRTIVDNISTVPRLNGVSARQAKSQA-LELLNTVGLDEsfaKRYPSQLSGGQAQRVGVARALASESSIL 162
Cdd:TIGR03719 389 YVDQSrDALDPNKTVWEEISGGLDIIKLGKREIPSRAyVGRFNFKGSDQ---QKKVGQLSGGERNRVHLAKTLKSGGNVL 465
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2735597802 163 LMDEPFSavdpvvraDLQKELLR-LQSTL----GRTIIfVTHD 200
Cdd:TIGR03719 466 LLDEPTN--------DLDVETLRaLEEALlnfaGCAVV-ISHD 499
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
18-232 |
4.67e-18 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 82.42 E-value: 4.67e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 18 GDNTVVDNLNLSIPEGKITVFVGPSGCGKTTSLRMI--NRMVEHTSGTILVNGEDNTARPAHE-LRRSMGYVLQQ----- 89
Cdd:COG0396 11 EGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLmgHPKYEVTSGSILLDGEDILELSPDErARAGIFLAFQYpveip 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 90 ----AGLMphRTIVDNIstvpRLNGVSARQAKSQALELLNTVGLDESFAKRYPSQ-LSGGQAQRVGVARALASESSILLM 164
Cdd:COG0396 91 gvsvSNFL--RTALNAR----RGEELSAREFLKLLKEKMKELGLDEDFLDRYVNEgFSGGEKKRNEILQMLLLEPKLAIL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 165 DEPFSAVD-----PVVRA--DLQKEllrlqstlGRTIIFVTH-----DMDEAillgDYVAVFArGGRIAQFGTPE---EI 229
Cdd:COG0396 165 DETDSGLDidalrIVAEGvnKLRSP--------DRGILIITHyqrilDYIKP----DFVHVLV-DGRIVKSGGKElalEL 231
|
...
gi 2735597802 230 LRE 232
Cdd:COG0396 232 EEE 234
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
4-241 |
6.33e-18 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 82.08 E-value: 6.33e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 4 LNNAIEFKSVFKTYGDNTVVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTIlvngedntaRPAHELRrsM 83
Cdd:PRK09544 1 MTSLVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI---------KRNGKLR--I 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 84 GYVLQQAGLMPhrTIVDNISTVPRLNGVSARQAKSQALELLNTVGLDEsfakrYPSQ-LSGGQAQRVGVARALASESSIL 162
Cdd:PRK09544 70 GYVPQKLYLDT--TLPLTVNRFLRLRPGTKKEDILPALKRVQAGHLID-----APMQkLSGGETQRVLLARALLNRPQLL 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2735597802 163 LMDEPFSAVDPVVRADLQKELLRLQSTLGRTIIFVTHDMDEAILLGDyvAVFARGGRIAQFGTPEEILREPadDFVASF 241
Cdd:PRK09544 143 VLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTD--EVLCLNHHICCSGTPEVVSLHP--EFISMF 217
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
14-201 |
6.84e-18 |
|
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: 81.22 E-value: 6.84e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 14 FKTYGDN-TVVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGEDNTARPAHEL----RRSMGYVLQ 88
Cdd:cd03290 7 YFSWGSGlATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATrsrnRYSVAYAAQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 89 QAGLMpHRTIVDNISTVPRLNGvSARQAKSQALELLNTVGL----DESFAKRYPSQLSGGQAQRVGVARALASESSILLM 164
Cdd:cd03290 87 KPWLL-NATVEENITFGSPFNK-QRYKAVTDACSLQPDIDLlpfgDQTEIGERGINLSGGQRQRICVARALYQNTNIVFL 164
|
170 180 190
....*....|....*....|....*....|....*...
gi 2735597802 165 DEPFSAVDPVVRADLQKE-LLRLQSTLGRTIIFVTHDM 201
Cdd:cd03290 165 DDPFSALDIHLSDHLMQEgILKFLQDDKRTLVLVTHKL 202
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
15-233 |
1.01e-17 |
|
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: 81.42 E-value: 1.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 15 KTYGDNTVVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTIlvnGEDNTARPAHEL--------RRSM--- 83
Cdd:TIGR02323 11 KSYGGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTA---TYIMRSGAELELyqlseaerRRLMrte 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 84 -GYVLQQA--GLMPHRTIVDNISTvpRLNGVSAR---QAKSQALELLNTVGLDESFAKRYPSQLSGGQAQRVGVARALAS 157
Cdd:TIGR02323 88 wGFVHQNPrdGLRMRVSAGANIGE--RLMAIGARhygNIRATAQDWLEEVEIDPTRIDDLPRAFSGGMQQRLQIARNLVT 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2735597802 158 ESSILLMDEPFSAVDPVVRADLQKELLRLQSTLGRTIIFVTHDMDEAILLGDYVAVFARgGRIAQFGTPEEILREP 233
Cdd:TIGR02323 166 RPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQ-GRVVESGLTDQVLDDP 240
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
8-245 |
1.19e-17 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 83.68 E-value: 1.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 8 IEFKSVFKTYGDNTVVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGED-NTARPAHELRRSMGYV 86
Cdd:PRK09700 6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINyNKLDHKLAAQLGIGII 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 87 LQQAGLMPHRTIVDNI-------STVPRLNGVSARQAKSQALELLNTVGLDESFAKRYpSQLSGGQAQRVGVARALASES 159
Cdd:PRK09700 86 YQELSVIDELTVLENLyigrhltKKVCGVNIIDWREMRVRAAMMLLRVGLKVDLDEKV-ANLSISHKQMLEIAKTLMLDA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 160 SILLMDEPFSA-----VDPV--VRADLQKEllrlqstlGRTIIFVTHDMDEAILLGDYVAVFARGGRIAQfgtpEEILRE 232
Cdd:PRK09700 165 KVIIMDEPTSSltnkeVDYLflIMNQLRKE--------GTAIVYISHKLAEIRRICDRYTVMKDGSSVCS----GMVSDV 232
|
250
....*....|...
gi 2735597802 233 PADDFVASFVGRD 245
Cdd:PRK09700 233 SNDDIVRLMVGRE 245
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
9-245 |
1.28e-17 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 83.81 E-value: 1.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 9 EFKSVFKTYGDNTVVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGED---NTARPAheLRRSMGY 85
Cdd:PRK11288 6 SFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEmrfASTTAA--LAAGVAI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 86 VLQQAGLMPHRTIVDNI--STVP-RLNGVSARQAKSQALELLNTVGLDESfakryPSQ----LSGGQAQRVGVARALASE 158
Cdd:PRK11288 84 IYQELHLVPEMTVAENLylGQLPhKGGIVNRRLLNYEAREQLEHLGVDID-----PDTplkyLSIGQRQMVEIAKALARN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 159 SSILLMDEPFSAVDP--------VVRAdlqkelLRLQstlGRTIIFVTHDMDEAILLGDYVAVFARGGRIAQFGTPEEIL 230
Cdd:PRK11288 159 ARVIAFDEPTSSLSAreieqlfrVIRE------LRAE---GRVILYVSHRMEEIFALCDAITVFKDGRYVATFDDMAQVD 229
|
250
....*....|....*
gi 2735597802 231 RepaDDFVASFVGRD 245
Cdd:PRK11288 230 R---DQLVQAMVGRE 241
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
8-229 |
1.65e-17 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 83.31 E-value: 1.65e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 8 IEFKSVFKTYGDNTVVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRM--VEHTSGTILVN----------------GE 69
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIYHvalcekcgyverpskvGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 70 D----------------NTARPA-HELRRSMGYVLQQA-GLMPHRTIVDNISTVPRLNGVSARQAKSQALELLNTVGLDE 131
Cdd:TIGR03269 81 PcpvcggtlepeevdfwNLSDKLrRRIRKRIAIMLQRTfALYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEMVQLSH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 132 SFAkRYPSQLSGGQAQRVGVARALASESSILLMDEPFSAVDPVVRADLQKELLRLQSTLGRTIIFVTH------DM-DEA 204
Cdd:TIGR03269 161 RIT-HIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHwpevieDLsDKA 239
|
250 260
....*....|....*....|....*
gi 2735597802 205 ILLGDyvavfargGRIAQFGTPEEI 229
Cdd:TIGR03269 240 IWLEN--------GEIKEEGTPDEV 256
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
18-199 |
1.84e-17 |
|
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: 79.84 E-value: 1.84e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 18 GDNTVVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGEdNTARPAHELRRSMGYVLQQAGLMPHRT 97
Cdd:cd03231 11 DGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGG-PLDFQRDSIARGLLYLGHAPGIKTTLS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 98 IVDNISTVPRLNGvsarqaKSQALELLNTVGLDeSFAKRYPSQLSGGQAQRVGVARALASESSILLMDEPFSAVDpVVRA 177
Cdd:cd03231 90 VLENLRFWHADHS------DEQVEEALARVGLN-GFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALD-KAGV 161
|
170 180
....*....|....*....|..
gi 2735597802 178 DLQKELLRLQSTLGRTIIFVTH 199
Cdd:cd03231 162 ARFAEAMAGHCARGGMVVLTTH 183
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
8-201 |
2.14e-17 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 83.93 E-value: 2.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 8 IEFKSV---FKTYGDNTVVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGEDNTARPAHELRRSMG 84
Cdd:PTZ00265 383 IQFKNVrfhYDTRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDSHNLKDINLKWWRSKI 462
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 85 YVLQQAGLMPHRTIVDNI----------------------STVPRLNGVSARQAKSQAL--ELLNTVGLDE--------- 131
Cdd:PTZ00265 463 GVVSQDPLLFSNSIKNNIkyslyslkdlealsnyynedgnDSQENKNKRNSCRAKCAGDlnDMSNTTDSNEliemrknyq 542
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 132 -----------------SFAKRYP-----------SQLSGGQAQRVGVARALASESSILLMDEPFSAVDPVVRADLQKEL 183
Cdd:PTZ00265 543 tikdsevvdvskkvlihDFVSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTI 622
|
250
....*....|....*...
gi 2735597802 184 LRLQSTLGRTIIFVTHDM 201
Cdd:PTZ00265 623 NNLKGNENRITIIIAHRL 640
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
18-199 |
2.36e-17 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 79.46 E-value: 2.36e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 18 GDNTVVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGED-NTARPahELRRSMGYVLQQAGLMPHR 96
Cdd:PRK13538 12 DERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPiRRQRD--EYHQDLLYLGHQPGIKTEL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 97 TIVDNISTVPRLNGVSARQAKSQALELLNTVGLDESFAKrypsQLSGGQAQRVGVARALASESSILLMDEPFSAVDPVVR 176
Cdd:PRK13538 90 TALENLRFYQRLHGPGDDEALWEALAQVGLAGFEDVPVR----QLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGV 165
|
170 180
....*....|....*....|...
gi 2735597802 177 ADLQkELLRLQSTLGRTIIFVTH 199
Cdd:PRK13538 166 ARLE-ALLAQHAEQGGMVILTTH 187
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
18-199 |
2.99e-17 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 79.15 E-value: 2.99e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 18 GDNTVVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGEDNTARpahELRRSMGYVLQQAGLMPHRT 97
Cdd:PRK13539 13 GGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDP---DVAEACHYLGHRNAMKPALT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 98 IVDNISTVPRLNGvsarQAKSQALELLNTVGLDESFAKRYpSQLSGGQAQRVGVARALASESSILLMDEPFSAVDpvVRA 177
Cdd:PRK13539 90 VAENLEFWAAFLG----GEELDIAAALEAVGLAPLAHLPF-GYLSAGQKRRVALARLLVSNRPIWILDEPTAALD--AAA 162
|
170 180
....*....|....*....|...
gi 2735597802 178 D-LQKELLRLQSTLGRTIIFVTH 199
Cdd:PRK13539 163 VaLFAELIRAHLAQGGIVIAATH 185
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
26-233 |
7.21e-17 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 78.82 E-value: 7.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 26 LNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHtSGTILVNGEDNTARPAHELRRSMGYVLQQ---AGLMPhrtiVDNI 102
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPG-SGSIQFAGQPLEAWSAAELARHRAYLSQQqtpPFAMP----VFQY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 103 STVPRLNGVSARQAKSQALELLNTVGLDESFAkRYPSQLSGGQAQRVGVA-------RALASESSILLMDEPFSAVDpVV 175
Cdd:PRK03695 90 LTLHQPDKTRTEAVASALNEVAEALGLDDKLG-RSVNQLSGGEWQRVRLAavvlqvwPDINPAGQLLLLDEPMNSLD-VA 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2735597802 176 RADLQKELLRLQSTLGRTIIFVTHDMDEAILLGDYVAVFARGGRIAQfGTPEEILREP 233
Cdd:PRK03695 168 QQAALDRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLAS-GRRDEVLTPE 224
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
11-231 |
9.57e-17 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 80.98 E-value: 9.57e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 11 KSVFK----TYGDNTVVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGEDNTAR-PAHELRRSMGY 85
Cdd:PRK09700 263 ETVFEvrnvTSRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRsPLDAVKKGMAY 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 86 VLQ---QAGLMPHRTIVDNISTVPRL------------NGVSARQAKSQALELLNtvgLDESFAKRYPSQLSGGQAQRVG 150
Cdd:PRK09700 343 ITEsrrDNGFFPNFSIAQNMAISRSLkdggykgamglfHEVDEQRTAENQRELLA---LKCHSVNQNITELSGGNQQKVL 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 151 VARALASESSILLMDEPFSAVDPVVRADLQKeLLRLQSTLGRTIIFVTHDMDEAILLGDYVAVFaRGGRIAQF------G 224
Cdd:PRK09700 420 ISKWLCCCPEVIIFDEPTRGIDVGAKAEIYK-VMRQLADDGKVILMVSSELPEIITVCDRIAVF-CEGRLTQIltnrddM 497
|
....*..
gi 2735597802 225 TPEEILR 231
Cdd:PRK09700 498 SEEEIMA 504
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
8-245 |
2.01e-16 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 80.25 E-value: 2.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 8 IEFKSVFKTYGDNTVVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTS--GTILVNGEDNTARPAHELRRSmGY 85
Cdd:TIGR02633 2 LEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTwdGEIYWSGSPLKASNIRDTERA-GI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 86 VL--QQAGLMPHRTIVDNISTVPRLNGVSARQAKS----QALELLNTVGLDESFAKRYPSQLSGGQAQRVGVARALASES 159
Cdd:TIGR02633 81 VIihQELTLVPELSVAENIFLGNEITLPGGRMAYNamylRAKNLLRELQLDADNVTRPVGDYGGGQQQLVEIAKALNKQA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 160 SILLMDEPFSAvdpVVRADLQK--ELLRLQSTLGRTIIFVTHDMDEAILLGDYVAVFARGGRIAQfgTPEEILREpaDDF 237
Cdd:TIGR02633 161 RLLILDEPSSS---LTEKETEIllDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQHVAT--KDMSTMSE--DDI 233
|
....*...
gi 2735597802 238 VASFVGRD 245
Cdd:TIGR02633 234 ITMMVGRE 241
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
5-199 |
2.73e-16 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 79.85 E-value: 2.73e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 5 NNAIEFKSV-FKTYGDNTVVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTIlvngedntARPAHElrRSM 83
Cdd:COG4178 360 DGALALEDLtLRTPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRI--------ARPAGA--RVL 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 84 gyvlqqagLMPHRtivdnistvPRLNGVSARQA-----------KSQALELLNTVGLDEsFAKRY------PSQLSGGQA 146
Cdd:COG4178 430 --------FLPQR---------PYLPLGTLREAllypataeafsDAELREALEAVGLGH-LAERLdeeadwDQVLSLGEQ 491
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2735597802 147 QRVGVARALASESSILLMDEPFSAVDPvvraDLQKELLR-LQSTL-GRTIIFVTH 199
Cdd:COG4178 492 QRLAFARLLLHKPDWLFLDEATSALDE----ENEAALYQlLREELpGTTVISVGH 542
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
7-252 |
3.47e-16 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 79.78 E-value: 3.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 7 AIEFKSVFKTYGDNTVVDNLNLSIPEGKITVFVGPSGCGKTTSLRMIN--RMVEhtSGTILVNGEDnTARPAHelRRSMG 84
Cdd:NF033858 1 VARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAgaRKIQ--QGRVEVLGGD-MADARH--RRAVC 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 85 ----YVLQQAG--LMPHRTIVDNISTVPRLNGVSARQAKSQALELLNTVGLDeSFAKRYPSQLSGGQAQRVGVARALASE 158
Cdd:NF033858 76 priaYMPQGLGknLYPTLSVFENLDFFGRLFGQDAAERRRRIDELLRATGLA-PFADRPAGKLSGGMKQKLGLCCALIHD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 159 SSILLMDEPFSAVDPVVRA---DLQKElLRLQSTlGRTIIFVTHDMDEAillgdyvavfAR--------GGRIAQFGTPE 227
Cdd:NF033858 155 PDLLILDEPTTGVDPLSRRqfwELIDR-IRAERP-GMSVLVATAYMEEA----------ERfdwlvamdAGRVLATGTPA 222
|
250 260 270
....*....|....*....|....*....|.
gi 2735597802 228 EIL-REPADDFVASFV-----GRDRGMRRLT 252
Cdd:NF033858 223 ELLaRTGADTLEAAFIallpeEKRRGHQPVV 253
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
8-199 |
3.48e-16 |
|
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: 75.27 E-value: 3.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 8 IEFKSV-FKTYGDNTVVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTIlvngedntARPAHElrRSMgyv 86
Cdd:cd03223 1 IELENLsLATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI--------GMPEGE--DLL--- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 87 lqqagLMPHRtivdnistvPRLNGVSARQAksqaleLLntvgldesfakrYPSQ--LSGGQAQRVGVARALASESSILLM 164
Cdd:cd03223 68 -----FLPQR---------PYLPLGTLREQ------LI------------YPWDdvLSGGEQQRLAFARLLLHKPKFVFL 115
|
170 180 190
....*....|....*....|....*....|....*
gi 2735597802 165 DEPFSAVDPvvraDLQKELLRLQSTLGRTIIFVTH 199
Cdd:cd03223 116 DEATSALDE----ESEDRLYQLLKELGITVISVGH 146
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
5-167 |
3.67e-16 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 79.39 E-value: 3.67e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 5 NNAIEFKSVFKTYGDNTVVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVnGEdnTARpahelrrsMG 84
Cdd:PRK11819 322 DKVIEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GE--TVK--------LA 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 85 YVLQQ-AGLMPHRTIVDNIStvprlNG-----VSARQAKSQA-LELLNTVGLDESfaKRYpSQLSGGQAQRVGVARALAS 157
Cdd:PRK11819 391 YVDQSrDALDPNKTVWEEIS-----GGldiikVGNREIPSRAyVGRFNFKGGDQQ--KKV-GVLSGGERNRLHLAKTLKQ 462
|
170
....*....|
gi 2735597802 158 ESSILLMDEP 167
Cdd:PRK11819 463 GGNVLLLDEP 472
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
8-226 |
7.68e-16 |
|
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: 75.14 E-value: 7.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 8 IEFKSVFKTYGDN--TVVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGEDNTARPAHELRRSMGY 85
Cdd:cd03369 7 IEVENLSVRYAPDlpPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSSLTI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 86 VLQQAGLMPHrTIVDNISTVPRLNGVSARQAKSQALELLNtvgldesfakrypsqLSGGQAQRVGVARALASESSILLMD 165
Cdd:cd03369 87 IPQDPTLFSG-TIRSNLDPFDEYSDEEIYGALRVSEGGLN---------------LSQGQRQLLCLARALLKRPRVLVLD 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2735597802 166 EPFSAVDPVVRADLQKeLLRlQSTLGRTIIFVTHDMdEAILLGDYVAVFARgGRIAQFGTP 226
Cdd:cd03369 151 EATASIDYATDALIQK-TIR-EEFTNSTILTIAHRL-RTIIDYDKILVMDA-GEVKEYDHP 207
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
6-221 |
2.22e-15 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 76.31 E-value: 2.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 6 NAIEFKSVFKTYGDNTVVDNLNLSIPEGKITVFVGPSGCGKTTSlrminRMVEHtsgtilVNGEDNTARP---------A 76
Cdd:NF000106 12 NAVEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RG-----ALPAH------V*GPDAGRRPwrf*twcanR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 77 HELRRSMG-YVLQQAGLMPHRTIVDNISTVPRLNGVSARQAKSQALELLNTVGLDESfAKRYPSQLSGGQAQRVGVARAL 155
Cdd:NF000106 81 RALRRTIG*HRPVR*GRRESFSGRENLYMIGR*LDLSRKDARARADELLERFSLTEA-AGRAAAKYSGGMRRRLDLAASM 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2735597802 156 ASESSILLMDEPFSAVDPVVRADLQKElLRLQSTLGRTIIFVTHDMDEAILLGDYVAVFARGGRIA 221
Cdd:NF000106 160 IGRPAVLYLDEPTTGLDPRTRNEVWDE-VRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIA 224
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
23-232 |
2.82e-15 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 74.49 E-value: 2.82e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 23 VDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHtSGTILVNGEDNTARPAHELRRSMGYVLQQ---AGLMP----- 94
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLLPG-QGEILLNGRPLSDWSAAELARHRAYLSQQqspPFAMPvfqyl 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 95 --HrtivdnistvprLNGVSARQAKSQAL-ELLNTVGLDESFAkRYPSQLSGGQAQRVGVARALA-------SESSILLM 164
Cdd:COG4138 91 alH------------QPAGASSEAVEQLLaQLAEALGLEDKLS-RPLTQLSGGEWQRVRLAAVLLqvwptinPEGQLLLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2735597802 165 DEPFSAVDPVVRADLQKeLLRLQSTLGRTIIFVTHDMDEAILLGDYVAVFARGGRIAQfGTPEEILRE 232
Cdd:COG4138 158 DEPMNSLDVAQQAALDR-LLRELCQQGITVVMSSHDLNHTLRHADRVWLLKQGKLVAS-GETAEVMTP 223
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
5-233 |
4.36e-15 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 75.22 E-value: 4.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 5 NNAIEFKSvfkTYGDNTVVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEH----TSGTILVNGEDNTARPAHELR 80
Cdd:PRK15093 8 NLTIEFKT---SDGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDnwrvTADRMRFDDIDLLRLSPRERR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 81 RSMGY----VLQ--QAGLMPHRTIVDN-ISTVP----------RLNgvsarQAKSQALELLNTVGLDE--SFAKRYPSQL 141
Cdd:PRK15093 85 KLVGHnvsmIFQepQSCLDPSERVGRQlMQNIPgwtykgrwwqRFG-----WRKRRAIELLHRVGIKDhkDAMRSFPYEL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 142 SGGQAQRVGVARALASESSILLMDEPFSAVDPVVRADLQKELLRLQSTLGRTIIFVTHDMDEAILLGDYVAVFaRGGRIA 221
Cdd:PRK15093 160 TEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVL-YCGQTV 238
|
250
....*....|..
gi 2735597802 222 QFGTPEEILREP 233
Cdd:PRK15093 239 ETAPSKELVTTP 250
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
19-173 |
8.35e-15 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 72.57 E-value: 8.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 19 DNTVVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGEDNTARpahELRRSMGYVLQQAGLMPHRTI 98
Cdd:PRK13543 23 EEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRG---DRSRFMAYLGHLPGLKADLST 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2735597802 99 VDNISTVPRLNGVSARQAKSQALELLNTVGLDESFAKrypsQLSGGQAQRVGVARALASESSILLMDEPFSAVDP 173
Cdd:PRK13543 100 LENLHFLCGLHGRRAKQMPGSALAIVGLAGYEDTLVR----QLSAGQKKRLALARLWLSPAPLWLLDEPYANLDL 170
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
15-240 |
8.45e-15 |
|
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: 73.21 E-value: 8.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 15 KTYGDNTvvdnLNL---SIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGEDNTARPAHELRRSMGYVlqQAG 91
Cdd:cd03237 8 KTLGEFT----LEVeggSISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSYKPQYIKADYEGTV--RDL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 92 LMphrTIVDNISTVPRLNGvsarqaksqalELLNTVGLDESFAKRYPsQLSGGQAQRVGVARALASESSILLMDEPFSAV 171
Cdd:cd03237 82 LS---SITKDFYTHPYFKT-----------EIAKPLQIEQILDREVP-ELSGGELQRVAIAACLSKDADIYLLDEPSAYL 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2735597802 172 DPVVRADLQKELLRLQSTLGRTIIFVTHDMDEAILLGDYVAVFArgGRIAQFGT--PEEILREPADDFVAS 240
Cdd:cd03237 147 DVEQRLMASKVIRRFAENNEKTAFVVEHDIIMIDYLADRLIVFE--GEPSVNGVanPPQSLRSGMNRFLKN 215
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
10-202 |
1.02e-14 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 73.97 E-value: 1.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 10 FKSVFK-TYGDNTVVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGEDNTARpAHELRRSMGYVL- 87
Cdd:COG4586 24 LKGLFRrEYREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPFKR-RKEFARRIGVVFg 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 88 --QQagLMPHRTIVDNIstvpRLN----GVSARQAKsQALELLNTVgLD-ESFAKRYPSQLSGGQAQRVGVARALASESS 160
Cdd:COG4586 103 qrSQ--LWWDLPAIDSF----RLLkaiyRIPDAEYK-KRLDELVEL-LDlGELLDTPVRQLSLGQRMRCELAAALLHRPK 174
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2735597802 161 ILLMDEPFSAVDPVVRADLQKELLRLQSTLGRTIIFVTHDMD 202
Cdd:COG4586 175 ILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMD 216
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
25-233 |
1.33e-14 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 75.20 E-value: 1.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 25 NLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVngedntarpahelRRSMGYVLQQAGLMpHRTIVDNI-- 102
Cdd:PTZ00243 678 DVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWA-------------ERSIAYVPQQAWIM-NATVRGNIlf 743
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 103 ---STVPRLNG---VSARQAKSQALellnTVGLDESFAKRyPSQLSGGQAQRVGVARALASESSILLMDEPFSAVDPVVR 176
Cdd:PTZ00243 744 fdeEDAARLADavrVSQLEADLAQL----GGGLETEIGEK-GVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVG 818
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2735597802 177 ADLQKELLrLQSTLGRTIIFVTHDMdEAILLGDYVAVFARgGRIAQFGTPEEILREP 233
Cdd:PTZ00243 819 ERVVEECF-LGALAGKTRVLATHQV-HVVPRADYVVALGD-GRVEFSGSSADFMRTS 872
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
24-222 |
1.99e-14 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 74.27 E-value: 1.99e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 24 DNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGEDNT-ARPAHELRRSMGYVLQQAGLMPHRTIVDNI 102
Cdd:PRK10762 21 SGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTfNGPKSSQEAGIGIIHQELNLIPQLTIAENI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 103 ----STVPRLNGVSARQAKSQALELLNTVGLDESfAKRYPSQLSGGQAQRVGVARALASESSILLMDEPFSAVDPVVRAD 178
Cdd:PRK10762 101 flgrEFVNRFGRIDWKKMYAEADKLLARLNLRFS-SDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDALTDTETES 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2735597802 179 LQKELLRLQSTlGRTIIFVTHDMDEAILLGDYVAVFARGGRIAQ 222
Cdd:PRK10762 180 LFRVIRELKSQ-GRGIVYISHRLKEIFEICDDVTVFRDGQFIAE 222
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
21-232 |
3.15e-14 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 73.52 E-value: 3.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 21 TVVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGEDNTARPAHELRRS-MGYVL---QQAGLMPHR 96
Cdd:COG3845 272 PALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLgVAYIPedrLGRGLVPDM 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 97 TIVDNI-----STVPRLNG--VSARQAKSQALELLntvgldESFAKRYPS------QLSGGQAQRVGVARALASESSILL 163
Cdd:COG3845 352 SVAENLilgryRRPPFSRGgfLDRKAIRAFAEELI------EEFDVRTPGpdtparSLSGGNQQKVILARELSRDPKLLI 425
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2735597802 164 MDEPFSAVDPVVRADLQKELLRLQSTlGRTIIFVTHDMDEAILLGDYVAVFARgGRIAQFGTPEEILRE 232
Cdd:COG3845 426 AAQPTRGLDVGAIEFIHQRLLELRDA-GAAVLLISEDLDEILALSDRIAVMYE-GRIVGEVPAAEATRE 492
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
8-245 |
4.43e-14 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 73.04 E-value: 4.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 8 IEFKSVFKTYGDNTVVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTS--GTILVNGEDNTARPAHELRRSmGY 85
Cdd:PRK13549 6 LEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGTyeGEIIFEGEELQASNIRDTERA-GI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 86 VL--QQAGLMPHRTIVDNI--STVPRLNGVSARQAK-SQALELLNTVGLDESFAKRYpSQLSGGQAQRVGVARALASESS 160
Cdd:PRK13549 85 AIihQELALVKELSVLENIflGNEITPGGIMDYDAMyLRAQKLLAQLKLDINPATPV-GNLGLGQQQLVEIAKALNKQAR 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 161 ILLMDEPFSAVDpvvradlQKE---LLRLQSTL---GRTIIFVTHDMDEAILLGDYVAVFARGGRIAQfgTPEEILREpa 234
Cdd:PRK13549 164 LLILDEPTASLT-------ESEtavLLDIIRDLkahGIACIYISHKLNEVKAISDTICVIRDGRHIGT--RPAAGMTE-- 232
|
250
....*....|.
gi 2735597802 235 DDFVASFVGRD 245
Cdd:PRK13549 233 DDIITMMVGRE 243
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
23-217 |
4.50e-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: 73.89 E-value: 4.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 23 VDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGEdNTARPAHELRRSMGYVLQQAGLMPHRTIVDNI 102
Cdd:TIGR01257 1955 VDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGK-SILTNISDVHQNMGYCPQFDAIDDLLTGREHL 2033
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 103 STVPRLNGVSARQAKSQALELLNTVGLdESFAKRYPSQLSGGQAQRVGVARALASESSILLMDEPFSAVDPVVRADLQKE 182
Cdd:TIGR01257 2034 YLYARLRGVPAEEIEKVANWSIQSLGL-SLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNT 2112
|
170 180 190
....*....|....*....|....*....|....*
gi 2735597802 183 LLRLQSTlGRTIIFVTHDMDEAILLGDYVAVFARG 217
Cdd:TIGR01257 2113 IVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKG 2146
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
3-217 |
7.51e-14 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 70.29 E-value: 7.51e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 3 VLNNAIEFKSVFKTYGDNTVVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGEDNTARP-AHELRR 81
Cdd:PRK11614 1 MEKVMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQtAKIMRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 82 SMGYVLQQAGLMPHRTIVDNIStvprLNGVSA-RQAKSQALELLNTV--GLDESFAKRyPSQLSGGQAQRVGVARALASE 158
Cdd:PRK11614 81 AVAIVPEGRRVFSRMTVEENLA----MGGFFAeRDQFQERIKWVYELfpRLHERRIQR-AGTMSGGEQQMLAIGRALMSQ 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2735597802 159 SSILLMDEPFSAVDPVVRADLQKELLRLQSTlGRTIIFVTHDMDEAILLGDYVAVFARG 217
Cdd:PRK11614 156 PRLLLLDEPSLGLAPIIIQQIFDTIEQLREQ-GMTIFLVEQNANQALKLADRGYVLENG 213
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
19-233 |
2.17e-13 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 70.90 E-value: 2.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 19 DNTVVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGedntaRPAHELR----RSMGYVLQQAGLMP 94
Cdd:PRK10789 327 DHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHD-----IPLTKLQldswRSRLAVVSQTPFLF 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 95 HRTIVDNIStvprLNGVSARQAKSQALELLNTV---------GLDESFAKRyPSQLSGGQAQRVGVARALASESSILLMD 165
Cdd:PRK10789 402 SDTVANNIA----LGRPDATQQEIEHVARLASVhddilrlpqGYDTEVGER-GVMLSGGQKQRISIARALLLNAEILILD 476
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2735597802 166 EPFSAVDPVVRADLQKELLRLQStlGRTIIFVTH------DMDEAILLgdyvavfaRGGRIAQFGTPEEILREP 233
Cdd:PRK10789 477 DALSAVDGRTEHQILHNLRQWGE--GRTVIISAHrlsaltEASEILVM--------QHGHIAQRGNHDQLAQQS 540
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
8-229 |
5.39e-13 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 69.69 E-value: 5.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 8 IEFKSVFKTYGDNTVVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGEDNT-ARPAHELRRSMGYV 86
Cdd:PRK15439 12 LCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCArLTPAKAHQLGIYLV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 87 LQQAGLMPHRTIVDNIstvprLNGVSARQAKSQALE-LLNTVG----LDESfakryPSQLSGGQAQRVGVARALASESSI 161
Cdd:PRK15439 92 PQEPLLFPNLSVKENI-----LFGLPKRQASMQKMKqLLAALGcqldLDSS-----AGSLEVADRQIVEILRGLMRDSRI 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2735597802 162 LLMDEPFSAVDPVVRADLQKELLRLQStLGRTIIFVTHDMDEAILLGDYVAVFaRGGRIAQFGTPEEI 229
Cdd:PRK15439 162 LILDEPTASLTPAETERLFSRIRELLA-QGVGIVFISHKLPEIRQLADRISVM-RDGTIALSGKTADL 227
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
18-231 |
9.42e-13 |
|
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: 66.40 E-value: 9.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 18 GDNTVVDNLNLSIPEGKITVFVGPSGCGKTTSLRMI--NRMVEHTSGTILVNGEDNTARPAHElRRSMG-YVLQQaglMP 94
Cdd:cd03217 11 GGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTImgHPKYEVTEGEILFKGEDITDLPPEE-RARLGiFLAFQ---YP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 95 hrtivdnistvPRLNGVSarqaksqALELLNTVglDESFakrypsqlSGGQAQRVGVARALASESSILLMDEPFSAVDpV 174
Cdd:cd03217 87 -----------PEIPGVK-------NADFLRYV--NEGF--------SGGEKKRNEILQLLLLEPDLAILDEPDSGLD-I 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 175 VRADLQKELLRLQSTLGRTIIFVTHdmDEAILL---GDYVAVFARgGRIAQFGTPEEILR 231
Cdd:cd03217 138 DALRLVAEVINKLREEGKSVLIITH--YQRLLDyikPDRVHVLYD-GRIVKSGDKELALE 194
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
20-210 |
1.35e-12 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 67.22 E-value: 1.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 20 NTVVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGEdntarPAHE-LRRSM-GYVLQQAGL-MPHR 96
Cdd:PRK15056 20 HTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQ-----PTRQaLQKNLvAYVPQSEEVdWSFP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 97 TIVDNISTVPRLNGVS-ARQAKSQALEL----LNTVGLDEsFAKRYPSQLSGGQAQRVGVARALASESSILLMDEPFSAV 171
Cdd:PRK15056 95 VLVEDVVMMGRYGHMGwLRRAKKRDRQIvtaaLARVDMVE-FRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGV 173
|
170 180 190
....*....|....*....|....*....|....*....
gi 2735597802 172 DPVVRADLqKELLRLQSTLGRTIIFVTHDMDEAILLGDY 210
Cdd:PRK15056 174 DVKTEARI-ISLLRELRDEGKTMLVSTHNLGSVTEFCDY 211
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
22-246 |
1.63e-12 |
|
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: 66.86 E-value: 1.63e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 22 VVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGEDNTARPAHELRRSMGYVLQQAGLMphrtivdn 101
Cdd:cd03288 36 VLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPILF-------- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 102 iSTVPRLNGVSARQAKS----QALE---LLNTV-----GLDeSFAKRYPSQLSGGQAQRVGVARALASESSILLMDEPFS 169
Cdd:cd03288 108 -SGSIRFNLDPECKCTDdrlwEALEiaqLKNMVkslpgGLD-AVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATA 185
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2735597802 170 AVDPVVRADLQKELlrLQSTLGRTIIFVTHDMdEAILLGDYVAVFARGGrIAQFGTPEEILREpADDFVASFVGRDR 246
Cdd:cd03288 186 SIDMATENILQKVV--MTAFADRTVVTIAHRV-STILDADLVLVLSRGI-LVECDTPENLLAQ-EDGVFASLVRTDK 257
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
25-211 |
1.98e-12 |
|
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: 65.74 E-value: 1.98e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 25 NLNLSIPEGKITVFVGPSGCGKTtSLRMinrmvehtsGTILVNGEdntarpahelRRSM----GYVLQQAGLMPhRTIVD 100
Cdd:cd03270 13 NVDVDIPRNKLVVITGVSGSGKS-SLAF---------DTIYAEGQ----------RRYVeslsAYARQFLGQMD-KPDVD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 101 NI-------------------STVPRLNGVS-------ARQAKSQALELLNTVGLDESFAKRYPSQLSGGQAQRVGVARA 154
Cdd:cd03270 72 SIeglspaiaidqkttsrnprSTVGTVTEIYdylrllfARVGIRERLGFLVDVGLGYLTLSRSAPTLSGGEAQRIRLATQ 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2735597802 155 LASESS--ILLMDEPFSAVDPvvrADLQK--ELLRLQSTLGRTIIFVTHDmDEAILLGDYV 211
Cdd:cd03270 152 IGSGLTgvLYVLDEPSIGLHP---RDNDRliETLKRLRDLGNTVLVVEHD-EDTIRAADHV 208
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
27-235 |
3.24e-12 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 67.24 E-value: 3.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 27 NLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGEDNTAR-PAHELRRsmGYVL-----QQAGLMPHRTIVD 100
Cdd:PRK11288 273 SFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRsPRDAIRA--GIMLcpedrKAEGIIPVHSVAD 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 101 NIStvprlngVSARQAKSQALELLNTvGLDESFAKRY--------PS------QLSGGQAQRVGVARALASESSILLMDE 166
Cdd:PRK11288 351 NIN-------ISARRHHLRAGCLINN-RWEAENADRFirslniktPSreqlimNLSGGNQQKAILGRWLSEDMKVILLDE 422
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2735597802 167 PFSAVDPVVRADLQKELLRLQSTlGRTIIFVTHDMDEAILLGDYVAVFaRGGRIAQfgtpeEILREPAD 235
Cdd:PRK11288 423 PTRGIDVGAKHEIYNVIYELAAQ-GVAVLFVSSDLPEVLGVADRIVVM-REGRIAG-----ELAREQAT 484
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
20-231 |
6.02e-12 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 65.23 E-value: 6.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 20 NTVVDNLNLSIPEGKITVFVGPSGCGKTTSLRMI---------NRMVEHTsGTILVNGEDNTARPAHELRRsMGYVLQQA 90
Cdd:PRK13547 14 RAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALagdltgggaPRGARVT-GDVTLNGEPLAAIDAPRLAR-LRAVLPQA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 91 GLMPHRTIVDNISTVPRLNGVSA--------RQAKSQALELLNTVGLDesfaKRYPSQLSGGQAQRVGVARALA------ 156
Cdd:PRK13547 92 AQPAFAFSAREIVLLGRYPHARRagalthrdGEIAWQALALAGATALV----GRDVTTLSGGELARVQFARVLAqlwpph 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2735597802 157 ---SESSILLMDEPFSAVDPVVRADLQKELLRLQSTLGRTIIFVTHDMDEAILLGDYVAVFARGGRIAQfGTPEEILR 231
Cdd:PRK13547 168 daaQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAH-GAPADVLT 244
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
32-228 |
8.94e-12 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 66.22 E-value: 8.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 32 EGKITVFVGPSGCGKTTSLRMI-NRMVEHT--SGTILVNGEdntARPAHELRRSMGYVLQQAGLMPHRTIVD--NISTVP 106
Cdd:TIGR00955 50 PGELLAVMGSSGAGKTTLMNALaFRSPKGVkgSGSVLLNGM---PIDAKEMRAISAYVQQDDLFIPTLTVREhlMFQAHL 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 107 RL-NGVSARQAKSQALELLNTVGL---------DESFAKrypsQLSGGQAQRVGVARALASESSILLMDEPFSAVDPVVR 176
Cdd:TIGR00955 127 RMpRRVTKKEKRERVDEVLQALGLrkcantrigVPGRVK----GLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMA 202
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2735597802 177 ADLQKELLRLqSTLGRTIIFVTHDMDEAIL-LGDYVAVFArGGRIAQFGTPEE 228
Cdd:TIGR00955 203 YSVVQVLKGL-AQKGKTIICTIHQPSSELFeLFDKIILMA-EGRVAYLGSPDQ 253
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
15-199 |
1.39e-11 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 65.67 E-value: 1.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 15 KTYGDNTVVDNLNLSIPEGKITVFVGPSGCGKTTSLRMI-NRMVEHT-SGTILVNGEdntaRPAHELRRSMGYVLQQAGL 92
Cdd:PLN03211 76 RQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALaGRIQGNNfTGTILANNR----KPTKQILKRTGFVTQDDIL 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 93 MPHRTIVDNI--STVPRLNGVSARQAKSQALE-LLNTVGLDES----FAKRYPSQLSGGQAQRVGVARALASESSILLMD 165
Cdd:PLN03211 152 YPHLTVRETLvfCSLLRLPKSLTKQEKILVAEsVISELGLTKCentiIGNSFIRGISGGERKRVSIAHEMLINPSLLILD 231
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2735597802 166 EPFSAVDPVVRadlqkelLRLQSTL------GRTIIFVTH 199
Cdd:PLN03211 232 EPTSGLDATAA-------YRLVLTLgslaqkGKTIVTSMH 264
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
10-245 |
1.82e-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: 65.70 E-value: 1.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 10 FKSVFKTYGdNTVVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTIlvngedntarpAHELRRSmgYVLQQ 89
Cdd:TIGR01271 430 FFSNFSLYV-TPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKI-----------KHSGRIS--FSPQT 495
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 90 AGLMPHrTIVDNIstvprLNGVSARQAKSQALelLNTVGLDESFAKrYPSQ-----------LSGGQAQRVGVARALASE 158
Cdd:TIGR01271 496 SWIMPG-TIKDNI-----IFGLSYDEYRYTSV--IKACQLEEDIAL-FPEKdktvlgeggitLSGGQRARISLARAVYKD 566
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 159 SSILLMDEPFSAVDPVVRADL-QKELLRLQSTlgRTIIFVTHDM------DEAILLGDYVAVFarggriaqFGTPEEiLR 231
Cdd:TIGR01271 567 ADLYLLDSPFTHLDVVTEKEIfESCLCKLMSN--KTRILVTSKLehlkkaDKILLLHEGVCYF--------YGTFSE-LQ 635
|
250
....*....|....
gi 2735597802 232 EPADDFVASFVGRD 245
Cdd:TIGR01271 636 AKRPDFSSLLLGLE 649
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
4-237 |
2.30e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 65.38 E-value: 2.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 4 LNNAIEFKSVFKTY--GDNTVVDNLNLSI-PEGKITVfVGPSGCGKTTSLRMINRMVEHTSGTILVNGEDNTARPAHELR 80
Cdd:PLN03232 1231 SRGSIKFEDVHLRYrpGLPPVLHGLSFFVsPSEKVGV-VGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLR 1309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 81 RSMGyVLQQAGLMPHRTIVDNISTVPRLNGVSARQAKSQA----LELLNTVGLDESFAKRYPSqLSGGQAQRVGVARALA 156
Cdd:PLN03232 1310 RVLS-IIPQSPVLFSGTVRFNIDPFSEHNDADLWEALERAhikdVIDRNPFGLDAEVSEGGEN-FSVGQRQLLSLARALL 1387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 157 SESSILLMDEPFSAVDpvVRAD-LQKELLRlQSTLGRTIIFVTHDMDeAILLGDYVAVFArGGRIAQFGTPEEILREPAD 235
Cdd:PLN03232 1388 RRSKILVLDEATASVD--VRTDsLIQRTIR-EEFKSCTMLVIAHRLN-TIIDCDKILVLS-SGQVLEYDSPQELLSRDTS 1462
|
..
gi 2735597802 236 DF 237
Cdd:PLN03232 1463 AF 1464
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
8-200 |
3.14e-11 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 64.22 E-value: 3.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 8 IEFKSVFKTYGDNTV-VDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGEDNTARPAHELRRSM--- 83
Cdd:PRK10522 323 LELRNVTFAYQDNGFsVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFsav 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 84 -------GYVLQQAGLMPHRTIVDniSTVPRLNgvSARQAKSQALELLNTvgldesfakrypsQLSGGQAQRVGVARALA 156
Cdd:PRK10522 403 ftdfhlfDQLLGPEGKPANPALVE--KWLERLK--MAHKLELEDGRISNL-------------KLSKGQKKRLALLLALA 465
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2735597802 157 SESSILLMDEPFSAVDPVVRADLQKELLRLQSTLGRTIIFVTHD 200
Cdd:PRK10522 466 EERDILLLDEWAADQDPHFRREFYQVLLPLLQEMGKTIFAISHD 509
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
54-230 |
3.33e-11 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 64.67 E-value: 3.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 54 NRMVEHTSGTILVNGEDNTARPAHELRRSMGYVLQQAGLMpHRTIVDNI------STVPRLNGVSARQAKSQALELL--- 124
Cdd:PTZ00265 1269 DSTVFKNSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLF-NMSIYENIkfgkedATREDVKRACKFAAIDEFIESLpnk 1347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 125 --NTVGldesfakRYPSQLSGGQAQRVGVARALASESSILLMDEPFSAVDPVVRADLQKELLRLQSTLGRTIIFVTHDMd 202
Cdd:PTZ00265 1348 ydTNVG-------PYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRI- 1419
|
170 180 190
....*....|....*....|....*....|..
gi 2735597802 203 EAILLGDYVAVFARGGRIAQF----GTPEEIL 230
Cdd:PTZ00265 1420 ASIKRSDKIVVFNNPDRTGSFvqahGTHEELL 1451
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
18-224 |
3.70e-11 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 61.49 E-value: 3.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 18 GDNTVVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVE--HTSGTILVNGEDNTArpahELRRSMGYVLQQAGLMPH 95
Cdd:cd03232 18 GKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTagVITGEILINGRPLDK----NFQRSTGYVEQQDVHSPN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 96 RTIVDNISTVPRLNGVSARQAKsqalellntvgldesfakrypsqlsggqaqRVGVARALASESSILLMDEPFSAVDPVV 175
Cdd:cd03232 94 LTVREALRFSALLRGLSVEQRK------------------------------RLTIGVELAAKPSILFLDEPTSGLDSQA 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2735597802 176 RADLQKELLRLQSTlGRTIIFVTHDMDEAIL-LGDYVAVFARGGRIAQFG 224
Cdd:cd03232 144 AYNIVRFLKKLADS-GQAILCTIHQPSASIFeKFDRLLLLKRGGKTVYFG 192
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
8-227 |
4.10e-11 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 62.35 E-value: 4.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 8 IEFKSVFKTYGDNTVVDNLNLSIPEGKITVFVGPSGCGKTTSLRMInrmVEH-----TSGTILVNGEDNTARPAhELRRS 82
Cdd:CHL00131 8 LEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVI---AGHpaykiLEGDILFKGESILDLEP-EERAH 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 83 MG------YVLQQAGlmphrtiVDNISTVpRLnGVSARQAKSQALEL------------LNTVGLDESFAKRYPSQ-LSG 143
Cdd:CHL00131 84 LGiflafqYPIEIPG-------VSNADFL-RL-AYNSKRKFQGLPELdplefleiinekLKLVGMDPSFLSRNVNEgFSG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 144 GQAQRVGVARALASESSILLMDEPFSAVDPVVRADLQKELLRLqSTLGRTIIFVTHDMDeaiLLG----DYVAVFaRGGR 219
Cdd:CHL00131 155 GEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKL-MTSENSIILITHYQR---LLDyikpDYVHVM-QNGK 229
|
....*...
gi 2735597802 220 IAQFGTPE 227
Cdd:CHL00131 230 IIKTGDAE 237
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
14-214 |
4.37e-11 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 64.04 E-value: 4.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 14 FKTYGdntvvdnlnLSIP-EGKITVFVGPSGCGKTTSLRM-----------------INRMVEHTSGTIL-------VNG 68
Cdd:COG1245 88 FRLYG---------LPVPkKGKVTGILGPNGIGKSTALKIlsgelkpnlgdydeepsWDEVLKRFRGTELqdyfkklANG 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 69 EdntARPAHELrrsmgyvlQQaglmphrtiVDNISTVPR------LNGVSARQAKSQALELLNtvgLDESFaKRYPSQLS 142
Cdd:COG1245 159 E---IKVAHKP--------QY---------VDLIPKVFKgtvrelLEKVDERGKLDELAEKLG---LENIL-DRDISELS 214
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2735597802 143 GGQAQRVGVARALASESSILLMDEPFSAVDPVVR---ADLQKELLRlqstLGRTIIFVTHDMdeAIL--LGDYVAVF 214
Cdd:COG1245 215 GGELQRVAIAAALLRDADFYFFDEPSSYLDIYQRlnvARLIRELAE----EGKYVLVVEHDL--AILdyLADYVHIL 285
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
9-245 |
4.98e-11 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 63.66 E-value: 4.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 9 EFKSVFKTYGDNTVVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTS--GTILVNGEdntARPAHELRRS--MG 84
Cdd:NF040905 3 EMRGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGSyeGEILFDGE---VCRFKDIRDSeaLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 85 YVL--QQAGLMPHRTIVDNI--STVPRLNGV-SARQAKSQALELLNTVGLDESFAKRYpSQLSGGQAQRVGVARALASES 159
Cdd:NF040905 80 IVIihQELALIPYLSIAENIflGNERAKRGViDWNETNRRARELLAKVGLDESPDTLV-TDIGVGKQQLVEIAKALSKDV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 160 SILLMDEPFSAVDpvvRADLQKeLLRLQSTL---GRTIIFVTHDMDEAILLGDYVAVFARGGRIAQFGTPEEILREpaDD 236
Cdd:NF040905 159 KLLILDEPTAALN---EEDSAA-LLDLLLELkaqGITSIIISHKLNEIRRVADSITVLRDGRTIETLDCRADEVTE--DR 232
|
....*....
gi 2735597802 237 FVASFVGRD 245
Cdd:NF040905 233 IIRGMVGRD 241
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
33-205 |
5.57e-11 |
|
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: 60.08 E-value: 5.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 33 GKITVFVGPSGCGKTTSLRMI-NRMVEHTSGTILVNGEDNTARPAHELRRSMGYvlqqaglmphrtivdnistvprlngv 111
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALaRELGPPGGGVIYIDGEDILEEVLDQLLLIIVG-------------------------- 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 112 sarqaksqalellntvgldesfakRYPSQLSGGQAQRVGVARALASESSILLMDEPFSAVDPVVRADLQKE-----LLRL 186
Cdd:smart00382 56 ------------------------GKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLeelrlLLLL 111
|
170
....*....|....*....
gi 2735597802 187 QSTLGRTIIFVTHDMDEAI 205
Cdd:smart00382 112 KSEKNLTVILTTNDEKDLG 130
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
10-245 |
7.13e-11 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 62.18 E-value: 7.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 10 FKSVFKTYGdNTVVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTIlvngedntarpAHELRRSmgYVLQQ 89
Cdd:cd03291 41 FFSNLCLVG-APVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKI-----------KHSGRIS--FSSQF 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 90 AGLMPHrTIVDNIstvprLNGVSARQAKSQALelLNTVGLDESFAKrYPSQ-----------LSGGQAQRVGVARALASE 158
Cdd:cd03291 107 SWIMPG-TIKENI-----IFGVSYDEYRYKSV--VKACQLEEDITK-FPEKdntvlgeggitLSGGQRARISLARAVYKD 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 159 SSILLMDEPFSAVDPVVRADL-QKELLRLQSTlgRTIIFVTHDMdEAILLGDYVAVFARGGRIAqFGTPEEiLREPADDF 237
Cdd:cd03291 178 ADLYLLDSPFGYLDVFTEKEIfESCVCKLMAN--KTRILVTSKM-EHLKKADKILILHEGSSYF-YGTFSE-LQSLRPDF 252
|
....*...
gi 2735597802 238 VASFVGRD 245
Cdd:cd03291 253 SSKLMGYD 260
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
16-206 |
8.41e-11 |
|
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: 61.79 E-value: 8.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 16 TYGDNTVVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVeHTSGTILVNGEDNTARPAHELRRSMGYVLQQaglmph 95
Cdd:cd03289 13 TEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLL-NTEGDIQIDGVSWNSVPLQKWRKAFGVIPQK------ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 96 rtiVDNISTVPRLNGVSARQAKSQAL-ELLNTVGLdESFAKRYPSQL-----------SGGQAQRVGVARALASESSILL 163
Cdd:cd03289 86 ---VFIFSGTFRKNLDPYGKWSDEEIwKVAEEVGL-KSVIEQFPGQLdfvlvdggcvlSHGHKQLMCLARSVLSKAKILL 161
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2735597802 164 MDEPFSAVDPVVRADLQKELlrLQSTLGRTIIFVTHDMdEAIL 206
Cdd:cd03289 162 LDEPSAHLDPITYQVIRKTL--KQAFADCTVILSEHRI-EAML 201
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
19-231 |
9.59e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 63.46 E-value: 9.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 19 DNTVVDNLNLSIPEGKITVFVGPSGCGKTTslrMINRMVEHtsgtiLVNGEDNTArpahELRRSMGYVLQQAGLMpHRTI 98
Cdd:PLN03232 629 SKPTLSDINLEIPVGSLVAIVGGTGEGKTS---LISAMLGE-----LSHAETSSV----VIRGSVAYVPQVSWIF-NATV 695
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 99 VDNI--------STVPRLNGVSARQaksQALELLntVGLDESFAKRYPSQLSGGQAQRVGVARALASESSILLMDEPFSA 170
Cdd:PLN03232 696 RENIlfgsdfesERYWRAIDVTALQ---HDLDLL--PGRDLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSA 770
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2735597802 171 VDPVVRADL----QKELLRlqstlGRTIIFVTHD------MDEAILLGDyvavfargGRIAQFGTPEEILR 231
Cdd:PLN03232 771 LDAHVAHQVfdscMKDELK-----GKTRVLVTNQlhflplMDRIILVSE--------GMIKEEGTFAELSK 828
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
13-200 |
1.35e-10 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 62.26 E-value: 1.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 13 VFKTYGDN-TVVDNLNLS-IPEGKITVfVGPSGCGKTTSLRmINRMVEHTSgtilvNGEdntARPAHELRrsMGYVLQQA 90
Cdd:TIGR03719 10 VSKVVPPKkEILKDISLSfFPGAKIGV-LGLNGAGKSTLLR-IMAGVDKDF-----NGE---ARPQPGIK--VGYLPQEP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 91 GLMPHRTIVDNI--------STVPRLNGVSA--------------RQAKSQalELLNTVG---LDESF-----AKRYP-- 138
Cdd:TIGR03719 78 QLDPTKTVRENVeegvaeikDALDRFNEISAkyaepdadfdklaaEQAELQ--EIIDAADawdLDSQLeiamdALRCPpw 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2735597802 139 ----SQLSGGQAQRVGVARALASESSILLMDEPFSAVDPVVRADLQKELLRLQStlgrTIIFVTHD 200
Cdd:TIGR03719 156 dadvTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPG----TVVAVTHD 217
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
7-230 |
2.92e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 61.68 E-value: 2.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 7 AIEFKSVFKTYGDN--TVVDNLNLSI-PEGKITVfVGPSGCGKTTSLRMINRMVEHTSGTILVNGEDNTARPAHELRRSM 83
Cdd:PLN03130 1237 SIKFEDVVLRYRPElpPVLHGLSFEIsPSEKVGI-VGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVL 1315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 84 GyVLQQAGLMPHRTIVDNISTVPRLNGV----SARQAKSQALELLNTVGLDESFAKRyPSQLSGGQAQRVGVARALASES 159
Cdd:PLN03130 1316 G-IIPQAPVLFSGTVRFNLDPFNEHNDAdlweSLERAHLKDVIRRNSLGLDAEVSEA-GENFSVGQRQLLSLARALLRRS 1393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 160 SILLMDEPFSAVDpvVRAD--LQK---------ELLRLQSTLgRTIIfvthDMDEAILLGdyvavfarGGRIAQFGTPEE 228
Cdd:PLN03130 1394 KILVLDEATAAVD--VRTDalIQKtireefkscTMLIIAHRL-NTII----DCDRILVLD--------AGRVVEFDTPEN 1458
|
..
gi 2735597802 229 IL 230
Cdd:PLN03130 1459 LL 1460
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
23-220 |
3.98e-10 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 60.79 E-value: 3.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 23 VDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGEDNTAR-PAHELRRSMGYVLQQA---GLMPHRTI 98
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRsPQDGLANGIVYISEDRkrdGLVLGMSV 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 99 VDNIS---------TVPRLNGVSARQAKSQALELLN--TVGLDESFAKrypsqLSGGQAQRVGVARALASESSILLMDEP 167
Cdd:PRK10762 348 KENMSltalryfsrAGGSLKHADEQQAVSDFIRLFNikTPSMEQAIGL-----LSGGNQQKVAIARGLMTRPKVLILDEP 422
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2735597802 168 FSAVDpvVRAdlQKELLRLQSTL---GRTIIFVTHDMDEAILLGDYVAVFaRGGRI 220
Cdd:PRK10762 423 TRGVD--VGA--KKEIYQLINQFkaeGLSIILVSSEMPEVLGMSDRILVM-HEGRI 473
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
14-212 |
5.87e-10 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 60.59 E-value: 5.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 14 FKTYGdntvvdnlnLSIP-EGKITVFVGPSGCGKTTSLRMInrmvehtSGTILVNGEDNTARPAHE--LRRSMGYVLQ-- 88
Cdd:PRK13409 88 FKLYG---------LPIPkEGKVTGILGPNGIGKTTAVKIL-------SGELIPNLGDYEEEPSWDevLKRFRGTELQny 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 89 -----QAGLMPHRTI--VDNISTVPR------LNGVSARQAKSQALELLNtvgLDESFAKRYpSQLSGGQAQRVGVARAL 155
Cdd:PRK13409 152 fkklyNGEIKVVHKPqyVDLIPKVFKgkvrelLKKVDERGKLDEVVERLG---LENILDRDI-SELSGGELQRVAIAAAL 227
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 156 ASESSILLMDEPFSAVDPVVR---ADLQKELLRlqstlGRTIIFVTHDMdeAILlgDYVA 212
Cdd:PRK13409 228 LRDADFYFFDEPTSYLDIRQRlnvARLIRELAE-----GKYVLVVEHDL--AVL--DYLA 278
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
23-249 |
7.12e-10 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 60.13 E-value: 7.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 23 VDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGED---NTARPAHELRRSMgyVLQQAGLMPHRTIV 99
Cdd:PRK10982 14 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEidfKSSKEALENGISM--VHQELNLVLQRSVM 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 100 DNI--STVPrLNGVSARQAK--SQALELLNTVGLDESfAKRYPSQLSGGQAQRVGVARALASESSILLMDEPFSAVDPVV 175
Cdd:PRK10982 92 DNMwlGRYP-TKGMFVDQDKmyRDTKAIFDELDIDID-PRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLTEKE 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2735597802 176 RADLQKELLRLQSTlGRTIIFVTHDMDEAILLGDYVAVFARGGRIAQfgtpEEILREPADDFVASFVGRDRGMR 249
Cdd:PRK10982 170 VNHLFTIIRKLKER-GCGIVYISHKMEEIFQLCDEITILRDGQWIAT----QPLAGLTMDKIIAMMVGRSLTQR 238
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
121-233 |
7.45e-10 |
|
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: 60.41 E-value: 7.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 121 LELLNTVGLDESFAKRYPSQLSGGQAQRVGVARALASESS--ILLMDEPFSAVDPVVRADLQKELLRLQStLGRTIIFVT 198
Cdd:TIGR00630 469 LGFLIDVGLDYLSLSRAAGTLSGGEAQRIRLATQIGSGLTgvLYVLDEPSIGLHQRDNRRLINTLKRLRD-LGNTLIVVE 547
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 2735597802 199 HDmDEAILLGDYV-------AVFarGGRIAQFGTPEEILREP 233
Cdd:TIGR00630 548 HD-EDTIRAADYVidigpgaGEH--GGEVVASGTPEEILANP 586
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
6-204 |
7.69e-10 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 60.03 E-value: 7.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 6 NAIEFKSVFKTYGDNTVVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRmvEHTSG----TILVNGEDNTARPAHELRR 81
Cdd:PRK10938 259 PRIVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITG--DHPQGysndLTLFGRRRGSGETIWDIKK 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 82 SMGYVLQQAGlMPHRtivdnISTVPR---LNG----------VSARQAKsQALELLNTVGLDESFAKRYPSQLSGGQAQR 148
Cdd:PRK10938 337 HIGYVSSSLH-LDYR-----VSTSVRnviLSGffdsigiyqaVSDRQQK-LAQQWLDILGIDKRTADAPFHSLSWGQQRL 409
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2735597802 149 VGVARALASESSILLMDEPFSAVDPVVRaDLQKELLRLQSTLGRT-IIFVTHDMDEA 204
Cdd:PRK10938 410 ALIVRALVKHPTLLILDEPLQGLDPLNR-QLVRRFVDVLISEGETqLLFVSHHAEDA 465
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
21-167 |
1.43e-09 |
|
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: 57.27 E-value: 1.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 21 TVVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHT---SGTILVNGEDNtARPAHELRRSMGYVLQQAGLMPHRT 97
Cdd:cd03233 21 PILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPY-KEFAEKYPGEIIYVSEEDVHFPTLT 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 98 IVDNISTVPRLNGvsarqaksqalellntvgldesfaKRYPSQLSGGQAQRVGVARALASESSILLMDEP 167
Cdd:cd03233 100 VRETLDFALRCKG------------------------NEFVRGISGGERKRVSIAEALVSRASVLCWDNS 145
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
25-217 |
3.19e-09 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 58.14 E-value: 3.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 25 NLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGEDNTAR-PAHELRRSMGYV---LQQAGLMPHRTIVD 100
Cdd:PRK15439 281 NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALsTAQRLARGLVYLpedRQSSGLYLDAPLAW 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 101 NISTVPR-LNGVSARQAKSQA-LELLN-TVGLDESFAKRYPSQLSGGQAQRVGVARALASESSILLMDEPFSAVDPVVRA 177
Cdd:PRK15439 361 NVCALTHnRRGFWIKPARENAvLERYRrALNIKFNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARN 440
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2735597802 178 DLQkELLRLQSTLGRTIIFVTHDMDEAILLGDYVAVFARG 217
Cdd:PRK15439 441 DIY-QLIRSIAAQNVAVLFISSDLEEIEQMADRVLVMHQG 479
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
19-199 |
3.71e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 55.65 E-value: 3.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 19 DNTVVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILV--NGEDNTARPahelrrSMGYVLQQAGLMPHR 96
Cdd:PRK13541 12 EQKNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYknCNINNIAKP------YCTYIGHNLGLKLEM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 97 TIVDNISTVPRL-NGVSARQAKSQALELLNTvgLDESFAKrypsqLSGGQAQRVGVARALASESSILLMDEPFSAVDPVV 175
Cdd:PRK13541 86 TVFENLKFWSEIyNSAETLYAAIHYFKLHDL--LDEKCYS-----LSSGMQKIVAIARLIACQSDLWLLDEVETNLSKEN 158
|
170 180
....*....|....*....|....
gi 2735597802 176 RaDLQKELLRLQSTLGRTIIFVTH 199
Cdd:PRK13541 159 R-DLLNNLIVMKANSGGIVLLSSH 181
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
23-247 |
3.77e-09 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 56.75 E-value: 3.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 23 VDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGEDNTarpahelrrsmgyVLQQAGLMPHRTIVDNI 102
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEVSV-------------IAISAGLSGQLTGIENI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 103 STVPRLNGVSARQAKSQALELLNTVGLDEsFAKRYPSQLSGGQAQRVGVARALASESSILLMDEPFSAVDPVVRadlQKE 182
Cdd:PRK13546 107 EFKMLCMGFKRKEIKAMTPKIIEFSELGE-FIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFA---QKC 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2735597802 183 LLRLQS--TLGRTIIFVTHDMDEAILLGDYVAvFARGGRIAQFGTPEEILREpADDFVASFVGRDRG 247
Cdd:PRK13546 183 LDKIYEfkEQNKTIFFVSHNLGQVRQFCTKIA-WIEGGKLKDYGELDDVLPK-YEAFLNDFKKKSKA 247
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
17-200 |
3.99e-09 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 58.04 E-value: 3.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 17 YGDNTVVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGEDNTAR-----PAHELRRSMGYV---LQ 88
Cdd:PRK11147 13 FSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLIVARlqqdpPRNVEGTVYDFVaegIE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 89 QAG--LMPHRTIVDNISTVPR---LNGVSARQAK-------------SQALELLntvGLDesfAKRYPSQLSGGQAQRVG 150
Cdd:PRK11147 93 EQAeyLKRYHDISHLVETDPSeknLNELAKLQEQldhhnlwqlenriNEVLAQL---GLD---PDAALSSLSGGWLRKAA 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2735597802 151 VARALASESSILLMDEPFSAVDPVVRADLQKELLRLQStlgrTIIFVTHD 200
Cdd:PRK11147 167 LGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQG----SIIFISHD 212
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
18-229 |
4.60e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 58.21 E-value: 4.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 18 GDNTVVDNLNLSIPEGKITVFVGPSGCGKTTSLR-MINRMVEHTSGTILVNGedntarpahelrrSMGYVLQQAGLMpHR 96
Cdd:PLN03130 628 AERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISaMLGELPPRSDASVVIRG-------------TVAYVPQVSWIF-NA 693
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 97 TIVDNI-----STVPRLNGVSARQAKSQALELLNtvGLDESFAKRYPSQLSGGQAQRVGVARALASESSILLMDEPFSAV 171
Cdd:PLN03130 694 TVRDNIlfgspFDPERYERAIDVTALQHDLDLLP--GGDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSAL 771
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2735597802 172 DPVVRADLQKELLR--LQstlGRTIIFVTHDM------DEAILLGDyvavfargGRIAQFGTPEEI 229
Cdd:PLN03130 772 DAHVGRQVFDKCIKdeLR---GKTRVLVTNQLhflsqvDRIILVHE--------GMIKEEGTYEEL 826
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
31-237 |
5.17e-09 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 57.87 E-value: 5.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 31 PEGKITVfVGPSGCGKTTSLRMINRMVEHTSGTILVNGEDNTARPAHELRRSMGYVLQQAGLMpHRTIVDNIStvPRLNG 110
Cdd:PTZ00243 1335 PREKVGI-VGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFSMIPQDPVLF-DGTVRQNVD--PFLEA 1410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 111 VSARQAKsqALELlntVGLDESFAKRYP----------SQLSGGQAQRVGVARALASE-SSILLMDEPFSAVDPVVRADL 179
Cdd:PTZ00243 1411 SSAEVWA--ALEL---VGLRERVASESEgidsrvleggSNYSVGQRQLMCMARALLKKgSGFILMDEATANIDPALDRQI 1485
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2735597802 180 QKELLRLQStlGRTIIFVTHDMD-----EAILLGDYvavfargGRIAQFGTPEEILREPADDF 237
Cdd:PTZ00243 1486 QATVMSAFS--AYTVITIAHRLHtvaqyDKIIVMDH-------GAVAEMGSPRELVMNRQSIF 1539
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
16-232 |
6.11e-09 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 57.61 E-value: 6.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 16 TYGDNTVVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEhTSGTILVNGEDNTARPAHELRRSMGYVlqqaglmPH 95
Cdd:TIGR01271 1228 TEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVSWNSVTLQTWRKAFGVI-------PQ 1299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 96 RTIVdnISTVPRLNGVSARQAKSQAL-ELLNTVGLdESFAKRYPSQL-----------SGGQAQRVGVARALASESSILL 163
Cdd:TIGR01271 1300 KVFI--FSGTFRKNLDPYEQWSDEEIwKVAEEVGL-KSVIEQFPDKLdfvlvdggyvlSNGHKQLMCLARSILSKAKILL 1376
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2735597802 164 MDEPFSAVDPVVRADLQKELlrLQSTLGRTIIFVTHDMdEAILLGDYVAVFaRGGRIAQFGTPEEILRE 232
Cdd:TIGR01271 1377 LDEPSAHLDPVTLQIIRKTL--KQSFSNCTVILSEHRV-EALLECQQFLVI-EGSSVKQYDSIQKLLNE 1441
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
17-172 |
6.54e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 55.34 E-value: 6.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 17 YGDNTVVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGEdNTARPAHELRRSMGYVLQQAGLMPHR 96
Cdd:PRK13540 11 YHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQ-SIKKDLCTYQKQLCFVGHRSGINPYL 89
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2735597802 97 TIVDNIstvprLNGVSARQAKSQALELLNTVGLDESFakRYP-SQLSGGQAQRVGVARALASESSILLMDEPFSAVD 172
Cdd:PRK13540 90 TLRENC-----LYDIHFSPGAVGITELCRLFSLEHLI--DYPcGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALD 159
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
8-232 |
7.07e-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: 57.65 E-value: 7.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 8 IEFKSVFKTY--GDNTVVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGEDNTARPAHELRRSMGY 85
Cdd:TIGR00957 1285 VEFRNYCLRYreDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITI 1364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 86 VLQQAGLMphrtivdniSTVPRLN----GVSARQAKSQALELLNTVGLDESFAKRYPSQ-------LSGGQAQRVGVARA 154
Cdd:TIGR00957 1365 IPQDPVLF---------SGSLRMNldpfSQYSDEEVWWALELAHLKTFVSALPDKLDHEcaeggenLSVGQRQLVCLARA 1435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 155 LASESSILLMDEPFSAVdpvvraDLQKELLrLQSTLGR-----TIIFVTHDMDEAIllgDYVAVFA-RGGRIAQFGTPEE 228
Cdd:TIGR00957 1436 LLRKTKILVLDEATAAV------DLETDNL-IQSTIRTqfedcTVLTIAHRLNTIM---DYTRVIVlDKGEVAEFGAPSN 1505
|
....
gi 2735597802 229 ILRE 232
Cdd:TIGR00957 1506 LLQQ 1509
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
13-200 |
7.82e-09 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 57.05 E-value: 7.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 13 VFKTYGDNTVV-DNLNLS-IPEGKITVfVGPSGCGKTTSLRMinrM--VEHTSgtilvNGEdntARPAHELRrsMGYVLQ 88
Cdd:PRK11819 12 VSKVVPPKKQIlKDISLSfFPGAKIGV-LGLNGAGKSTLLRI---MagVDKEF-----EGE---ARPAPGIK--VGYLPQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 89 QAGLMPHRTIVDNI--------STVPRLNGVSA--------------RQAKSQA-LELLNTVGLDESF-----AKRYP-- 138
Cdd:PRK11819 78 EPQLDPEKTVRENVeegvaevkAALDRFNEIYAayaepdadfdalaaEQGELQEiIDAADAWDLDSQLeiamdALRCPpw 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2735597802 139 ----SQLSGGQAQRVGVARALASESSILLMDEPFSAVDPVVRADLQKELLRLQStlgrTIIFVTHD 200
Cdd:PRK11819 158 dakvTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLEQFLHDYPG----TVVAVTHD 219
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
17-249 |
8.08e-09 |
|
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: 55.84 E-value: 8.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 17 YGDNTVVDNlNLSIP-EGKITVFVGPSGCGKTTSLRMInrmvehtSGTILVNGEDNTARPAHE--LRRSMGYVLQQaglM 93
Cdd:cd03236 10 YGPNSFKLH-RLPVPrEGQVLGLVGPNGIGKSTALKIL-------AGKLKPNLGKFDDPPDWDeiLDEFRGSELQN---Y 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 94 PHRTIVDNISTV--PRLNGVSARQAKSQALELLNTVglDESFAK--------------RYPSQLSGGQAQRVGVARALAS 157
Cdd:cd03236 79 FTKLLEGDVKVIvkPQYVDLIPKAVKGKVGELLKKK--DERGKLdelvdqlelrhvldRNIDQLSGGELQRVAIAAALAR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 158 ESSILLMDEPFSAVDPVVRADLQKeLLRLQSTLGRTIIFVTHDMdeAIL--LGDYVAVFArgGRIAQFG--TPEEILREP 233
Cdd:cd03236 157 DADFYFFDEPSSYLDIKQRLNAAR-LIRELAEDDNYVLVVEHDL--AVLdyLSDYIHCLY--GEPGAYGvvTLPKSVREG 231
|
250
....*....|....*.
gi 2735597802 234 ADDFVASFVgRDRGMR 249
Cdd:cd03236 232 INEFLDGYL-PTENMR 246
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
7-230 |
9.92e-09 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 56.65 E-value: 9.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 7 AIEFKSV-FKTYGDNTVVDNLNLSIPEGKITVFVGPSGCGKTT--SLRMINRMVehTSGTILVNGedntaRP----AHE- 78
Cdd:PRK10790 340 RIDIDNVsFAYRDDNLVLQNINLSVPSRGFVALVGHTGSGKSTlaSLLMGYYPL--TEGEIRLDG-----RPlsslSHSv 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 79 LRRSMGYVlQQAGLMPHRTIVDNIsTVPRlnGVSARQAkSQALEllnTVGLDEsFAKRYP-----------SQLSGGQAQ 147
Cdd:PRK10790 413 LRQGVAMV-QQDPVVLADTFLANV-TLGR--DISEEQV-WQALE---TVQLAE-LARSLPdglytplgeqgNNLSVGQKQ 483
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 148 RVGVARALASESSILLMDEPFSAVDPVVRADLQKEL--LRLQSTLgrtiIFVTHDMdEAILLGDYVAVFARGGRIAQfGT 225
Cdd:PRK10790 484 LLALARVLVQTPQILILDEATANIDSGTEQAIQQALaaVREHTTL----VVIAHRL-STIVEADTILVLHRGQAVEQ-GT 557
|
....*
gi 2735597802 226 PEEIL 230
Cdd:PRK10790 558 HQQLL 562
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
8-214 |
1.73e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 55.97 E-value: 1.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 8 IEFKSVFKTYGDNTvvdnLNLS---IPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVngedntarpahELRRSmg 84
Cdd:PRK13409 341 VEYPDLTKKLGDFS----LEVEggeIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDP-----------ELKIS-- 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 85 YVLQQAGLMPHRTIVDNISTVPRLNGVSARQAksqalELLNTVGLDESFaKRYPSQLSGGQAQRVGVARALASESSILLM 164
Cdd:PRK13409 404 YKPQYIKPDYDGTVEDLLRSITDDLGSSYYKS-----EIIKPLQLERLL-DKNVKDLSGGELQRVAIAACLSRDADLYLL 477
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2735597802 165 DEPFSAVDPVVRADLQKELLRLQSTLGRTIIFVTHDmdeaILLGDYVA----VF 214
Cdd:PRK13409 478 DEPSAHLDVEQRLAVAKAIRRIAEEREATALVVDHD----IYMIDYISdrlmVF 527
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
14-200 |
1.90e-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: 53.13 E-value: 1.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 14 FKTYGDNTVVdnlnlSIPEGKITVFVGPSGCGKTTSLRminrmvehtsgtilvngedntarpahelrrSMGYVLQQAGLM 93
Cdd:cd03227 7 FPSYFVPNDV-----TFGEGSLTIITGPNGSGKSTILD------------------------------AIGLALGGAQSA 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 94 PHRTIVDNI-STVPRlngvsarqaksQALELLNTVgldesfakrypSQLSGGQAQRVGVARALAS----ESSILLMDEPF 168
Cdd:cd03227 52 TRRRSGVKAgCIVAA-----------VSAELIFTR-----------LQLSGGEKELSALALILALaslkPRPLYILDEID 109
|
170 180 190
....*....|....*....|....*....|..
gi 2735597802 169 SAVDPVVRADLqKELLRLQSTLGRTIIFVTHD 200
Cdd:cd03227 110 RGLDPRDGQAL-AEAILEHLVKGAQVIVITHL 140
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
8-202 |
2.01e-08 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 55.95 E-value: 2.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 8 IEFKSVFKTYGDNTVVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTIL---------VNGEDNT-ARPAH 77
Cdd:PRK10636 2 IVFSSLQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTfpgnwqlawVNQETPAlPQPAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 78 EL-------RRSMGYVLQQAGlmpHRTIVDNISTV-PRLNGVSARQAKSQALELLNTVGLDESFAKRYPSQLSGGQAQRV 149
Cdd:PRK10636 82 EYvidgdreYRQLEAQLHDAN---ERNDGHAIATIhGKLDAIDAWTIRSRAASLLHGLGFSNEQLERPVSDFSGGWRMRL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2735597802 150 GVARALASESSILLMDEPFSAVDPVVRADLQKELLRLQSTLgrtiIFVTHDMD 202
Cdd:PRK10636 159 NLAQALICRSDLLLLDEPTNHLDLDAVIWLEKWLKSYQGTL----ILISHDRD 207
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
26-200 |
2.76e-08 |
|
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: 55.19 E-value: 2.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 26 LNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGE--DNTARPAHelrRSMgyvlqqaglmphrtivdnIS 103
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQpvTADNREAY---RQL------------------FS 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 104 TV-------PRLNGVSARQAKSQALELLNTVGLDE--SFAKRYPS--QLSGGQAQRVGVARALASESSILLMDEPFSAVD 172
Cdd:COG4615 410 AVfsdfhlfDRLLGLDGEADPARARELLERLELDHkvSVEDGRFSttDLSQGQRKRLALLVALLEDRPILVFDEWAADQD 489
|
170 180
....*....|....*....|....*....
gi 2735597802 173 PVVRADLQKELL-RLQStLGRTIIFVTHD 200
Cdd:COG4615 490 PEFRRVFYTELLpELKA-RGKTVIAISHD 517
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
8-241 |
3.61e-08 |
|
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: 52.57 E-value: 3.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 8 IEFKSVFKTYGDNTVVDNLNlSIPEGKITVFVGPSGCGKTTSLRMInrmvehtSGTILVNGEDNTarpahelrrsmgyvl 87
Cdd:cd03222 1 QLYPDCVKRYGVFFLLVELG-VVKEGEVIGIVGPNGTGKTTAVKIL-------AGQLIPNGDNDE--------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 88 qqaglMPHRTIVdnistvprlngvsarqAKSQALELlntvgldesfakrypsqlSGGQAQRVGVARALASESSILLMDEP 167
Cdd:cd03222 58 -----WDGITPV----------------YKPQYIDL------------------SGGELQRVAIAAALLRNATFYLFDEP 98
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2735597802 168 FSAVDPVVRADLQKELLRLQSTLGRTIIFVTHDMDEAILLGDYVAVFArgGRIAQFGT--PEEILREPADDFVASF 241
Cdd:cd03222 99 SAYLDIEQRLNAARAIRRLSEEGKKTALVVEHDLAVLDYLSDRIHVFE--GEPGVYGIasQPKGTREGINRFLRGY 172
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
8-214 |
5.26e-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: 54.41 E-value: 5.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 8 IEFKSVFKTYGDntvvdnLNLSIPEGKITV-----FVGPSGCGKTTSLRMINRMVEHTSGTIlvngeDNTARPAHELRrs 82
Cdd:COG1245 342 VEYPDLTKSYGG------FSLEVEGGEIREgevlgIVGPNGIGKTTFAKILAGVLKPDEGEV-----DEDLKISYKPQ-- 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 83 mgYVLQQAglmpHRTIVDNISTV--PRLNGVSARQaksqalELLNTVGLDESFaKRYPSQLSGGQAQRVGVARALASESS 160
Cdd:COG1245 409 --YISPDY----DGTVEEFLRSAntDDFGSSYYKT------EIIKPLGLEKLL-DKNVKDLSGGELQRVAIAACLSRDAD 475
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2735597802 161 ILLMDEPFSAVDPVVRADLQKELLRLQSTLGRTIIFVTHDmdeaILLGDYVA----VF 214
Cdd:COG1245 476 LYLLDEPSAHLDVEQRLAVAKAIRRFAENRGKTAMVVDHD----IYLIDYISdrlmVF 529
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
25-218 |
1.50e-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: 1.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 25 NLNLSIPEGKITVFVGPSGCGKTTslrminrmvehtsgtiLVNGedntarpahelrrsmgyVLQQAGlmpHRTIVDNIST 104
Cdd:cd03238 13 NLDVSIPLNVLVVVTGVSGSGKST----------------LVNE-----------------GLYASG---KARLISFLPK 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 105 VPRLNGVSARQaksqaLELLNTVGLDESFAKRYPSQLSGGQAQRVGVARALASES--SILLMDEPFSAVDPVVRADLQKE 182
Cdd:cd03238 57 FSRNKLIFIDQ-----LQFLIDVGLGYLTLGQKLSTLSGGELQRVKLASELFSEPpgTLFILDEPSTGLHQQDINQLLEV 131
|
170 180 190
....*....|....*....|....*....|....*.
gi 2735597802 183 LLRLQStLGRTIIFVTHDmDEAILLGDYVAVFARGG 218
Cdd:cd03238 132 IKGLID-LGNTVILIEHN-LDVLSSADWIIDFGPGS 165
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
118-229 |
3.43e-07 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 51.94 E-value: 3.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 118 SQALELLNTVGLDESFAKRYPSQLSGGQAQRVGVARALASES---SILLMDEPFSAVDpvvRADLQKELLRLQS--TLGR 192
Cdd:TIGR00630 807 SRKLQTLCDVGLGYIRLGQPATTLSGGEAQRIKLAKELSKRStgrTLYILDEPTTGLH---FDDIKKLLEVLQRlvDKGN 883
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 2735597802 193 TIIFVTHDMDeAILLGDYVAVF-----ARGGRIAQFGTPEEI 229
Cdd:TIGR00630 884 TVVVIEHNLD-VIKTADYIIDLgpeggDGGGTVVASGTPEEV 924
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
33-224 |
3.47e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 52.03 E-value: 3.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 33 GKITVFVGPSGCGKTTSLRMINRMVEH---TSGTILVNGedntaRPAHE-LRRSMGYVLQQAGLMPHRTIVDNISTVPRL 108
Cdd:TIGR00956 789 GTLTALMGASGAGKTTLLNVLAERVTTgviTGGDRLVNG-----RPLDSsFQRSIGYVQQQDLHLPTSTVRESLRFSAYL 863
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 109 ngvsaRQAKS-----------QALELLNTVGLDESFAKRYPSQLSGGQAQRVGVARAL-ASESSILLMDEPFSAVDPVVR 176
Cdd:TIGR00956 864 -----RQPKSvsksekmeyveEVIKLLEMESYADAVVGVPGEGLNVEQRKRLTIGVELvAKPKLLLFLDEPTSGLDSQTA 938
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2735597802 177 ADLQKeLLRLQSTLGRTIIFVTHDmDEAILLG--DYVAVFARGGRIAQFG 224
Cdd:TIGR00956 939 WSICK-LMRKLADHGQAILCTIHQ-PSAILFEefDRLLLLQKGGQTVYFG 986
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
23-217 |
5.72e-07 |
|
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: 50.98 E-value: 5.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 23 VDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVE-HTSGTILVNGED-NTARPAHELRRSMGYV---LQQAGLMPHRT 97
Cdd:TIGR02633 276 VDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPgKFEGNVFINGKPvDIRNPAQAIRAGIAMVpedRKRHGIVPILG 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 98 IVDNI--------STVPRLNGVSARQAKSQALELLNTvgldESFAKRYP-SQLSGGQAQRVGVARALASESSILLMDEPF 168
Cdd:TIGR02633 356 VGKNItlsvlksfCFKMRIDAAAELQIIGSAIQRLKV----KTASPFLPiGRLSGGNQQKAVLAKMLLTNPRVLILDEPT 431
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2735597802 169 SAVDPVVRADLQKeLLRLQSTLGRTIIFVTHDMDEAILLGDYVAVFARG 217
Cdd:TIGR02633 432 RGVDVGAKYEIYK-LINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEG 479
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
9-200 |
6.87e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 51.10 E-value: 6.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 9 EFKSVFKTYGDNTVVDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGEDNTArpahelrrsmgYVLQ 88
Cdd:PRK11147 321 EMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTKLEVA-----------YFDQ 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 89 -QAGLMPHRTIVDNI----STVpRLNGVsarqaKSQALELLNtvglDESFA-KR--YPSQ-LSGGQAQRVGVARALASES 159
Cdd:PRK11147 390 hRAELDPEKTVMDNLaegkQEV-MVNGR-----PRHVLGYLQ----DFLFHpKRamTPVKaLSGGERNRLLLARLFLKPS 459
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2735597802 160 SILLMDEPFSAVDpVVRADLQKELL-RLQSTLgrtiIFVTHD 200
Cdd:PRK11147 460 NLLILDEPTNDLD-VETLELLEELLdSYQGTV----LLVSHD 496
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
121-234 |
9.17e-07 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 50.80 E-value: 9.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 121 LELLNTVGLDesfakrY-----PS-QLSGGQAQRVGVARALASESS---ILLMDEP-----FsavdpvvrADLQKeLLR- 185
Cdd:COG0178 807 LQTLQDVGLG------YiklgqPAtTLSGGEAQRVKLASELSKRSTgktLYILDEPttglhF--------HDIRK-LLEv 871
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 2735597802 186 LQS--TLGRTIIFVTHDMDeAILLGDYVAVF-----ARGGRIAQFGTPEEILREPA 234
Cdd:COG0178 872 LHRlvDKGNTVVVIEHNLD-VIKTADWIIDLgpeggDGGGEIVAEGTPEEVAKVKA 926
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
5-200 |
4.30e-06 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 48.35 E-value: 4.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 5 NNAIEFKSVFKTYGDNTVVDNLNLSIPEG-KITVfVGPSGCGKTTSLRMINRMVEHTSGTilVNGEDNTarpahelrrSM 83
Cdd:PRK15064 317 RNALEVENLTKGFDNGPLFKNLNLLLEAGeRLAI-IGENGVGKTTLLRTLVGELEPDSGT--VKWSENA---------NI 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 84 GYVLQQaglmpHRTIVDNISTVprLNGVSA-RQAKSQALELLNTVGL-----DEsfAKRYPSQLSGGQAQRVGVARALAS 157
Cdd:PRK15064 385 GYYAQD-----HAYDFENDLTL--FDWMSQwRQEGDDEQAVRGTLGRllfsqDD--IKKSVKVLSGGEKGRMLFGKLMMQ 455
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2735597802 158 ESSILLMDEPFSAVDPVVRADLQKELLRLQSTLgrtiIFVTHD 200
Cdd:PRK15064 456 KPNVLVMDEPTNHMDMESIESLNMALEKYEGTL----IFVSHD 494
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
121-234 |
7.47e-06 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 47.71 E-value: 7.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 121 LELLNTVGLDesfakrY-----PSQ-LSGGQAQRVGVARALASEssilLM------DEPfSA------VDPVVRAdlqke 182
Cdd:COG0178 466 LGFLVDVGLD------YltldrSAGtLSGGEAQRIRLATQIGSG----LVgvlyvlDEP-SIglhqrdNDRLIET----- 529
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 2735597802 183 LLRLQStLGRTIIFVTHDmDEAILLGDYVAVF-----ARGGRI-AQfGTPEEILREPA 234
Cdd:COG0178 530 LKRLRD-LGNTVIVVEHD-EDTIRAADYIIDIgpgagEHGGEVvAQ-GTPEEILKNPD 584
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
121-226 |
7.54e-06 |
|
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: 46.84 E-value: 7.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 121 LELLNTVGLDESFAKRYPSQLSGGQAQRVGVARALASESS---ILLMDEPFSAVDPvvrADLQKELLRLQS--TLGRTII 195
Cdd:cd03271 150 LQTLCDVGLGYIKLGQPATTLSGGEAQRIKLAKELSKRSTgktLYILDEPTTGLHF---HDVKKLLEVLQRlvDKGNTVV 226
|
90 100 110
....*....|....*....|....*....|....*.
gi 2735597802 196 FVTHDMDeAILLGDYVAVF-----ARGGRIAQFGTP 226
Cdd:cd03271 227 VIEHNLD-VIKCADWIIDLgpeggDGGGQVVASGTP 261
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
22-217 |
8.69e-06 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 47.23 E-value: 8.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 22 VVDNLNLSIPEGKITVFVGPSGCGKTtslrminRMVE--------HTSGTILVNGEDNTAR-PAHELRRSMGYVLQ---Q 89
Cdd:PRK13549 277 RVDDVSFSLRRGEILGIAGLVGAGRT-------ELVQclfgaypgRWEGEIFIDGKPVKIRnPQQAIAQGIAMVPEdrkR 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 90 AGLMPHRTIVDNIsTVPRLNGVSARQAKSQALELlntVGLDESFAK---RYPS------QLSGGQAQRVGVARALASESS 160
Cdd:PRK13549 350 DGIVPVMGVGKNI-TLAALDRFTGGSRIDDAAEL---KTILESIQRlkvKTASpelaiaRLSGGNQQKAVLAKCLLLNPK 425
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2735597802 161 ILLMDEPFSAVDPVVRADLQKELLRLQSTlGRTIIFVTHDMDEAILLGDYVAVFARG 217
Cdd:PRK13549 426 ILILDEPTRGIDVGAKYEIYKLINQLVQQ-GVAIIVISSELPEVLGLSDRVLVMHEG 481
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
121-233 |
1.40e-05 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 46.99 E-value: 1.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 121 LELLNTVGLDesfakrYPS------QLSGGQAQRVgvaRaLAS--------------ESSILLMdepfsavdpvvradlQ 180
Cdd:PRK00349 470 LKFLVDVGLD------YLTlsrsagTLSGGEAQRI---R-LATqigsgltgvlyvldEPSIGLH---------------Q 524
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2735597802 181 KELLRLQSTL------GRTIIFVTHDmDEAILLGDYV-------AVFarGGRIAQFGTPEEILREP 233
Cdd:PRK00349 525 RDNDRLIETLkhlrdlGNTLIVVEHD-EDTIRAADYIvdigpgaGVH--GGEVVASGTPEEIMKNP 587
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
140-232 |
1.62e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 46.55 E-value: 1.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 140 QLSGGQAQRVGVARALASESSILLMDEPFSAVDPVVRADLQKELLRLQSTlGRTIIFVTHDMDEAILLGDYVAVFARGGR 219
Cdd:PRK10938 135 YLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQS-GITLVLVLNRFDEIPDFVQFAGVLADCTL 213
|
90
....*....|...
gi 2735597802 220 IAQfGTPEEILRE 232
Cdd:PRK10938 214 AET-GEREEILQQ 225
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
23-231 |
5.48e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 44.72 E-value: 5.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 23 VDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGEDNTARPAHEL-----------RRSMG-YVLQQA 90
Cdd:PRK10982 264 IRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANEAinhgfalvteeRRSTGiYAYLDI 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 91 GLmphRTIVDNI-STVPRLNGVSARQAKSQALELLNTVGLDESFAKRYPSQLSGGQAQRVGVARALASESSILLMDEPFS 169
Cdd:PRK10982 344 GF---NSLISNIrNYKNKVGLLDNSRMKSDTQWVIDSMRVKTPGHRTQIGSLSGGNQQKVIIGRWLLTQPEILMLDEPTR 420
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2735597802 170 AVDPVVRADLQKELLRLQSTlGRTIIFVTHDMDEAILLGDYVAVFArGGRIAQF-----GTPEEILR 231
Cdd:PRK10982 421 GIDVGAKFEIYQLIAELAKK-DKGIIIISSEMPELLGITDRILVMS-NGLVAGIvdtktTTQNEILR 485
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
121-244 |
5.86e-05 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 45.06 E-value: 5.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 121 LELLNTVGLDesfakrY-----PS-QLSGGQAQRVGVARALASES---SILLMDEP-----FsavdpvvrADLQKELLRL 186
Cdd:PRK00349 811 LQTLVDVGLG------YiklgqPAtTLSGGEAQRVKLAKELSKRStgkTLYILDEPttglhF--------EDIRKLLEVL 876
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2735597802 187 QS--TLGRTIIFVTHDMDeAILLGDYVAVF-----ARGGRIAQFGTPEEILREPaddfvASFVGR 244
Cdd:PRK00349 877 HRlvDKGNTVVVIEHNLD-VIKTADWIIDLgpeggDGGGEIVATGTPEEVAKVE-----ASYTGR 935
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
33-166 |
9.11e-05 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 44.33 E-value: 9.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 33 GKITVFVGPSGCGKTTSLRMINRMVEH----TSGTILVNGedntaRPAHELRRSM-GYVLQQAGL---MPHRTIVDNIST 104
Cdd:TIGR00956 87 GELTVVLGRPGSGCSTLLKTIASNTDGfhigVEGVITYDG-----ITPEEIKKHYrGDVVYNAETdvhFPHLTVGETLDF 161
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2735597802 105 VPRLNGVSAR--------QAKSQALELLNTVGLDESFAKRYPSQL----SGGQAQRVGVARALASESSILLMDE 166
Cdd:TIGR00956 162 AARCKTPQNRpdgvsreeYAKHIADVYMATYGLSHTRNTKVGNDFvrgvSGGERKRVSIAEASLGGAKIQCWDN 235
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
107-199 |
2.38e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 42.92 E-value: 2.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 107 RLNGVSARQAKSQALELLNTVGLDESFAKRYPSQLSGGQAQRVGVARALASESSILLMDEPFSAVDPVVRADLQKELLRL 186
Cdd:PLN03073 311 RLELIDAYTAEARAASILAGLSFTPEMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKW 390
|
90
....*....|...
gi 2735597802 187 QstlgRTIIFVTH 199
Cdd:PLN03073 391 P----KTFIVVSH 399
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
115-230 |
2.47e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 43.28 E-value: 2.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 115 QAKSQALELLNTVGLDESFAKRYPSQLSGGQAQRVGVARALASESS--ILLMDEPFSAVDPVVRADLQKELLRLQSTlGR 192
Cdd:PRK00635 451 QGLKSRLSILIDLGLPYLTPERALATLSGGEQERTALAKHLGAELIgiTYILDEPSIGLHPQDTHKLINVIKKLRDQ-GN 529
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 2735597802 193 TIIFVTHD------MDEAILLGDYVAVFarGGRIAQFGTPEEIL 230
Cdd:PRK00635 530 TVLLVEHDeqmislADRIIDIGPGAGIF--GGEVLFNGSPREFL 571
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
23-203 |
5.69e-04 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 41.80 E-value: 5.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 23 VDNLNLSIPEGKITVFVGPSGCGKTTSLRMINRMVEHTSGTILVNGedntarpahelrrSMGYVLQQAGLMPHRTIVDNI 102
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKG-------------SAALIAISSGLNGQLTGIENI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 103 STVPRLNGVSARQAKSQALELLNTVGLDEsFAKRYPSQLSGGQAQRVGVARALASESSILLMDEPFSAVDPVVRADLQKE 182
Cdd:PRK13545 107 ELKGLMMGLTKEKIKEIIPEIIEFADIGK-FIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKCLDK 185
|
170 180
....*....|....*....|.
gi 2735597802 183 LLRLQSTlGRTIIFVTHDMDE 203
Cdd:PRK13545 186 MNEFKEQ-GKTIFFISHSLSQ 205
|
|
| PRK06647 |
PRK06647 |
DNA polymerase III subunits gamma and tau; Validated |
18-55 |
1.55e-03 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 235845 [Multi-domain] Cd Length: 563 Bit Score: 40.52 E-value: 1.55e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 2735597802 18 GDNTVVDNLNLSIPEGKIT---VFVGPSGCGKTTSLRMINR 55
Cdd:PRK06647 20 GQDFVVETLKHSIESNKIAnayIFSGPRGVGKTSSARAFAR 60
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
22-167 |
1.92e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 40.16 E-value: 1.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 22 VVDNLNLSIPEGKITVFVGPSGCGKT---TSL--RMINRmveHTSGTILVNGED---NTARPAheLRRSMGYVLQ---QA 90
Cdd:NF040905 275 VVDDVSLNVRRGEIVGIAGLMGAGRTelaMSVfgRSYGR---NISGTVFKDGKEvdvSTVSDA--IDAGLAYVTEdrkGY 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 91 GLMPHRTIVDNIsTVPRLNGVSARQAKSQALELLNTVGLDESFAKRYPS------QLSGGQAQRVGVARALASESSILLM 164
Cdd:NF040905 350 GLNLIDDIKRNI-TLANLGKVSRRGVIDENEEIKVAEEYRKKMNIKTPSvfqkvgNLSGGNQQKVVLSKWLFTDPDVLIL 428
|
...
gi 2735597802 165 DEP 167
Cdd:NF040905 429 DEP 431
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
119-230 |
2.85e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 39.81 E-value: 2.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 119 QALELLNTVGLDESFAKRYPSQLSGGQAQRVGVARALASES---SILLMDEPFSAVDPvvrADLQKELLRLQST--LGRT 193
Cdd:PRK00635 788 EKIHALCSLGLDYLPLGRPLSSLSGGEIQRLKLAYELLAPSkkpTLYVLDEPTTGLHT---HDIKALIYVLQSLthQGHT 864
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 2735597802 194 IIFVTHDMdEAILLGDYVAVFA-----RGGRIAQFGTPEEIL 230
Cdd:PRK00635 865 VVIIEHNM-HVVKVADYVLELGpeggnLGGYLLASCSPEELI 905
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
135-200 |
4.01e-03 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 38.52 E-value: 4.01e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 135 KRYPSQLSGGQaQR----VGVARALASESSILLMDEPFSAVDPVVRADLQkELLRLQSTLGRTIIFVTHD 200
Cdd:pfam13304 231 ELPAFELSDGT-KRllalLAALLSALPKGGLLLIDEPESGLHPKLLRRLL-ELLKELSRNGAQLILTTHS 298
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
116-200 |
4.15e-03 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 39.10 E-value: 4.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735597802 116 AKSQALELLNTVGLDESFAKRYPSQLSGGQAQRVGVARALASESSILLMDEPFSAVDPVVRADLQKELLRLQStlgrTII 195
Cdd:PRK15064 131 AEARAGELLLGVGIPEEQHYGLMSEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDINTIRWLEDVLNERNS----TMI 206
|
....*
gi 2735597802 196 FVTHD 200
Cdd:PRK15064 207 IISHD 211
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
14-46 |
4.89e-03 |
|
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a tight junction-associated protein expressed in rat epithelial cells which is thought to have an important regulatory role in tight junction barrier function. Barmotin belongs to the SMC protein family. SMC proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213245 [Multi-domain] Cd Length: 197 Bit Score: 37.83 E-value: 4.89e-03
10 20 30
....*....|....*....|....*....|...
gi 2735597802 14 FKTYGDNTVVDnlnlsIPEGkITVFVGPSGCGK 46
Cdd:cd03278 9 FKSFADKTTIP-----FPPG-LTAIVGPNGSGK 35
|
|
| PRK00098 |
PRK00098 |
GTPase RsgA; Reviewed |
32-57 |
8.63e-03 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234631 [Multi-domain] Cd Length: 298 Bit Score: 37.49 E-value: 8.63e-03
10 20
....*....|....*....|....*.
gi 2735597802 32 EGKITVFVGPSGCGKTTslrMINRMV 57
Cdd:PRK00098 163 AGKVTVLAGQSGVGKST---LLNALA 185
|
|
| |
