|
Name |
Accession |
Description |
Interval |
E-value |
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-330 |
1.12e-139 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 400.24 E-value: 1.12e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 1 MTAALHIGHLSKSFQNTPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIfsknTNLPVRER 80
Cdd:COG3842 2 AMPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDV----TGLPPEKR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 81 RLGYLVQEGVLFPHLTVYRNIAYGLGNGKGRTAQERQRIEAMLELTGISELAGRYPHELSGGQQQRVALARALAPDPELI 160
Cdd:COG3842 78 NVGMVFQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 161 LLDEPFSALDEQLRRQIREDMIAALRANGKSAVFVSHDREEALQYADRIAVMKQGRILQTASPHELYRQPADLDAALFIG 240
Cdd:COG3842 158 LLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEIYERPATRFVADFIG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 241 EGIVFPAALNADGTADCRLG----RLPVQSGAPAGTRGTLLIRPEQFSLHPhSAPAASIHAVVLKTTPKARHTEISLRAG 316
Cdd:COG3842 238 EANLLPGTVLGDEGGGVRTGgrtlEVPADAGLAAGGPVTVAIRPEDIRLSP-EGPENGLPGTVEDVVFLGSHVRYRVRLG 316
|
330
....*....|....*
gi 1067578656 317 Q-TVLTLNLPSAPTL 330
Cdd:COG3842 317 DgQELVVRVPNRAAL 331
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
5-318 |
4.97e-121 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 352.53 E-value: 4.97e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 5 LHIGHLSKSFQNTPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIFsknTNLPVRERRLGY 84
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLF---TNLPPRERRVGF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 85 LVQEGVLFPHLTVYRNIAYGLGNGKGRTAQERQRIEAMLELTGISELAGRYPHELSGGQQQRVALARALAPDPELILLDE 164
Cdd:COG1118 80 VFQHYALFPHMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLLLDE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 165 PFSALDEQLRRQIREDMIAALRANGKSAVFVSHDREEALQYADRIAVMKQGRILQTASPHELYRQPADLDAALFIGEGIV 244
Cdd:COG1118 160 PFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDRPATPFVARFLGCVNV 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1067578656 245 FPAALnADGTADCRLGRLPVQSGAPAGTrGTLLIRPEQFSLHPHSAPAASIHAVVLKTTPKARHTEISLRAGQT 318
Cdd:COG1118 240 LRGRV-IGGQLEADGLTLPVAEPLPDGP-AVAGVRPHDIEVSREPEGENTFPATVARVSELGPEVRVELKLEDG 311
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
3-347 |
9.64e-114 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 334.35 E-value: 9.64e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 3 AALHIGHLSKSFQNTPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIfsknTNLPVRERRL 82
Cdd:COG3839 2 ASLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDV----TDLPPKDRNI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 83 GYLVQEGVLFPHLTVYRNIAYGLGNgKGRTAQER-QRIEAMLELTGISELAGRYPHELSGGQQQRVALARALAPDPELIL 161
Cdd:COG3839 78 AMVFQSYALYPHMTVYENIAFPLKL-RKVPKAEIdRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 162 LDEPFSALDEQLRRQIREDMIAALRANGKSAVFVSHDREEALQYADRIAVMKQGRILQTASPHELYRQPADLDAALFIGE 241
Cdd:COG3839 157 LDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGTPEELYDRPANLFVAGFIGS 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 242 G--IVFPAALNADG--TADCRLgRLPVQSGAPAGTRGTLLIRPEQFSLHPhsAPAASIHAVVLKTTPKARHTEISLRAGQ 317
Cdd:COG3839 237 PpmNLLPGTVEGGGvrLGGVRL-PLPAALAAAAGGEVTLGIRPEHLRLAD--EGDGGLEATVEVVEPLGSETLVHVRLGG 313
|
330 340 350
....*....|....*....|....*....|
gi 1067578656 318 TVLTLNLPSAPTLSDGISAVLHLDGPALFF 347
Cdd:COG3839 314 QELVARVPGDTRLRPGDTVRLAFDPERLHL 343
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
5-221 |
1.26e-109 |
|
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: 318.69 E-value: 1.26e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 5 LHIGHLSKSFQNTPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIfsknTNLPVRERRLGY 84
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDV----TGVPPERRNIGM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 85 LVQEGVLFPHLTVYRNIAYGLGNGKGRTAQERQRIEAMLELTGISELAGRYPHELSGGQQQRVALARALAPDPELILLDE 164
Cdd:cd03259 77 VFQDYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1067578656 165 PFSALDEQLRRQIREDMIAALRANGKSAVFVSHDREEALQYADRIAVMKQGRILQTA 221
Cdd:cd03259 157 PLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
1-315 |
3.03e-100 |
|
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: 300.03 E-value: 3.03e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 1 MTAALHIGHLSKSFQNTPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIfsknTNLPVRER 80
Cdd:TIGR03265 1 SSPYLSIDNIRKRFGAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDI----TRLPPQKR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 81 RLGYLVQEGVLFPHLTVYRNIAYGLGNGKGRTAQERQRIEAMLELTGISELAGRYPHELSGGQQQRVALARALAPDPELI 160
Cdd:TIGR03265 77 DYGIVFQSYALFPNLTVADNIAYGLKNRGMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALATSPGLL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 161 LLDEPFSALDEQLRRQIREDMIAALRANGKSAVFVSHDREEALQYADRIAVMKQGRILQTASPHELYRQPADLDAALFIG 240
Cdd:TIGR03265 157 LLDEPLSALDARVREHLRTEIRQLQRRLGVTTIMVTHDQEEALSMADRIVVMNHGVIEQVGTPQEIYRHPATPFVADFVG 236
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1067578656 241 EGIVFPAALNADGTADCRLGRLPV-QSGAPAGTRGTLLIRPEQFSLHPHSAPAASIHAVVLKTTPKARHTEISLRA 315
Cdd:TIGR03265 237 EVNWLPGTRGGGSRARVGGLTLACaPGLAQPGASVRLAVRPEDIRVSPAGNAANLLLARVEDMEFLGAFYRLRLRL 312
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
9-240 |
4.99e-93 |
|
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: 277.20 E-value: 4.99e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 9 HLSKSFQNTPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIfsknTNLPVRERRLGYLVQE 88
Cdd:cd03300 5 NVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDI----TNLPPHKRPVNTVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 89 GVLFPHLTVYRNIAYGLGNGKGRTAQERQRIEAMLELTGISELAGRYPHELSGGQQQRVALARALAPDPELILLDEPFSA 168
Cdd:cd03300 81 YALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1067578656 169 LDEQLRRQIREDMIAALRANGKSAVFVSHDREEALQYADRIAVMKQGRILQTASPHELYRQPADLDAALFIG 240
Cdd:cd03300 161 LDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPANRFVADFIG 232
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-217 |
1.54e-89 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 269.27 E-value: 1.54e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 1 MTAALHIGHLSKSFQ----NTPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIFSKNtnlp 76
Cdd:COG1116 4 AAPALELRGVSKRFPtgggGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPG---- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 77 vreRRLGYLVQEGVLFPHLTVYRNIAYGLGNGKGRTAQERQRIEAMLELTGISELAGRYPHELSGGQQQRVALARALAPD 156
Cdd:COG1116 80 ---PDRGVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALAND 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1067578656 157 PELILLDEPFSALDEQLRRQIREDMIAALRANGKSAVFVSHDREEALQYADRIAVMKQ--GRI 217
Cdd:COG1116 157 PEVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFLADRVVVLSArpGRI 219
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
10-281 |
3.21e-88 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 269.89 E-value: 3.21e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 10 LSKSFQNTPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIfsknTNLPVRERRLGYLVQEG 89
Cdd:PRK09452 20 ISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDI----THVPAENRHVNTVFQSY 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 90 VLFPHLTVYRNIAYGLGNGKGRTAQERQRIEAMLELTGISELAGRYPHELSGGQQQRVALARALAPDPELILLDEPFSAL 169
Cdd:PRK09452 96 ALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSAL 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 170 DEQLRRQIREDMIAALRANGKSAVFVSHDREEALQYADRIAVMKQGRILQTASPHELYRQPADLDAALFIGEGIVFPAAL 249
Cdd:PRK09452 176 DYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNLFVARFIGEINIFDATV 255
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1067578656 250 -----------NADGTaDCRL-GRLPVQsgapAGTRGTLLIRPE 281
Cdd:PRK09452 256 ierldeqrvraNVEGR-ECNIyVNFAVE----PGQKLHVLLRPE 294
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
5-220 |
4.20e-87 |
|
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: 261.64 E-value: 4.20e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 5 LHIGHLSKSFQN----TPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKtifskntnlPVRE- 79
Cdd:cd03293 1 LEVRNVSKTYGGgggaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGE---------PVTGp 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 80 -RRLGYLVQEGVLFPHLTVYRNIAYGLGNGKGRTAQERQRIEAMLELTGISELAGRYPHELSGGQQQRVALARALAPDPE 158
Cdd:cd03293 72 gPDRGYVFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPD 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1067578656 159 LILLDEPFSALDEQLRRQIREDMIAALRANGKSAVFVSHDREEALQYADRIAVMKQ--GRILQT 220
Cdd:cd03293 152 VLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLSArpGRIVAE 215
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
9-242 |
5.56e-83 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 254.24 E-value: 5.56e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 9 HLSKSFQN-TPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIFSKNtnlPVRERR-LGYLV 86
Cdd:COG1125 6 NVTKRYPDgTVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRDLD---PVELRRrIGYVI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 87 QEGVLFPHLTVYRNIA---YGLGNGKGRTaqeRQRIEAMLELTGI--SELAGRYPHELSGGQQQRVALARALAPDPELIL 161
Cdd:COG1125 83 QQIGLFPHMTVAENIAtvpRLLGWDKERI---RARVDELLELVGLdpEEYRDRYPHELSGGQQQRVGVARALAADPPILL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 162 LDEPFSALDEQLRRQIREDMIAALRANGKSAVFVSHDREEALQYADRIAVMKQGRILQTASPHELYRQPADLDAALFIGE 241
Cdd:COG1125 160 MDEPFGALDPITREQLQDELLRLQRELGKTIVFVTHDIDEALKLGDRIAVMREGRIVQYDTPEEILANPANDFVADFVGA 239
|
.
gi 1067578656 242 G 242
Cdd:COG1125 240 D 240
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
7-241 |
1.13e-82 |
|
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: 251.10 E-value: 1.13e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 7 IGHLSKSFQNTPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIfsknTNLPVRERRLGYLV 86
Cdd:cd03296 5 VRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDA----TDVPVQERNVGFVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 87 QEGVLFPHLTVYRNIAYGLGNGKGRT----AQERQRIEAMLELTGISELAGRYPHELSGGQQQRVALARALAPDPELILL 162
Cdd:cd03296 81 QHYALFRHMTVFDNVAFGLRVKPRSErppeAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 163 DEPFSALDEQLRRQIRedmiAALR----ANGKSAVFVSHDREEALQYADRIAVMKQGRILQTASPHELYRQPADLDAALF 238
Cdd:cd03296 161 DEPFGALDAKVRKELR----RWLRrlhdELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPASPFVYSF 236
|
...
gi 1067578656 239 IGE 241
Cdd:cd03296 237 LGE 239
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
5-232 |
2.90e-79 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 242.21 E-value: 2.90e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 5 LHIGHLSKSFQNTPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIFSKNTNLPVRERRLGY 84
Cdd:COG1126 2 IEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKKDINKLRRKVGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 85 LVQEGVLFPHLTVYRNIAYGLGNGKGRTAQE-RQRIEAMLELTGISELAGRYPHELSGGQQQRVALARALAPDPELILLD 163
Cdd:COG1126 82 VFQQFNLFPHLTVLENVTLAPIKVKKMSKAEaEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKVMLFD 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1067578656 164 EPFSALDEQLrrqIRE--DMIAALRANGKSAVFVSHDREEALQYADRIAVMKQGRILQTASPHELYRQPAD 232
Cdd:COG1126 162 EPTSALDPEL---VGEvlDVMRDLAKEGMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFENPQH 229
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
7-241 |
1.38e-77 |
|
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 238.16 E-value: 1.38e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 7 IGHLSKSFQNTPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIfsknTNLPVRERRLGYLV 86
Cdd:TIGR00968 3 IANISKRFGSFQALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGLEQPDSGRIRLNGQDA----TRVHARDRKIGFVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 87 QEGVLFPHLTVYRNIAYGLGNGKGRTAQERQRIEAMLELTGISELAGRYPHELSGGQQQRVALARALAPDPELILLDEPF 166
Cdd:TIGR00968 79 QHYALFKHLTVRDNIAFGLEIRKHPKAKIKARVEELLELVQLEGLGDRYPNQLSGGQRQRVALARALAVEPQVLLLDEPF 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1067578656 167 SALDEQLRRQIRedmiAALRANGK----SAVFVSHDREEALQYADRIAVMKQGRILQTASPHELYRQPADLDAALFIGE 241
Cdd:TIGR00968 159 GALDAKVRKELR----SWLRKLHDevhvTTVFVTHDQEEAMEVADRIVVMSNGKIEQIGSPDEVYDHPANPFVMSFLGE 233
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
7-322 |
1.63e-77 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 241.91 E-value: 1.63e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 7 IGHLSKSFQNTPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIfsknTNLPVRERRLGYLV 86
Cdd:PRK10851 5 IANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDV----SRLHARDRKVGFVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 87 QEGVLFPHLTVYRNIAYGLGNGKGR----TAQERQRIEAMLELTGISELAGRYPHELSGGQQQRVALARALAPDPELILL 162
Cdd:PRK10851 81 QHYALFRHMTVFDNIAFGLTVLPRRerpnAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 163 DEPFSALDEQLRRQIREdMIAALRANGK-SAVFVSHDREEALQYADRIAVMKQGRILQTASPHELYRQPADLDAALFIGE 241
Cdd:PRK10851 161 DEPFGALDAQVRKELRR-WLRQLHEELKfTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREPATRFVLEFMGE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 242 -----GIVFPAALNAdGTADCRLGRLPVQSGapagtRGTLLIRPEQFSLHPHSAPAASIHAVVLKTTPKARHTEISLRA- 315
Cdd:PRK10851 240 vnrlqGTIRGGQFHV-GAHRWPLGYTPAYQG-----PVDLFLRPWEVDISRRTSLDSPLPVQVLEVSPKGHYWQLVVQPl 313
|
....*....
gi 1067578656 316 --GQTVLTL 322
Cdd:PRK10851 314 gwYNEPLTV 322
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
9-242 |
2.93e-77 |
|
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: 237.20 E-value: 2.93e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 9 HLSKSFQN-TPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIFSKNtnlPVRERR-LGYLV 86
Cdd:cd03295 5 NVTKRYGGgKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQD---PVELRRkIGYVI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 87 QEGVLFPHLTVYRNIAYGLGNGKGRTAQERQRIEAMLELTGI--SELAGRYPHELSGGQQQRVALARALAPDPELILLDE 164
Cdd:cd03295 82 QQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLdpAEFADRYPHELSGGQQQRVGVARALAADPPLLLMDE 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1067578656 165 PFSALDEQLRRQIREDMIAALRANGKSAVFVSHDREEALQYADRIAVMKQGRILQTASPHELYRQPADLDAALFIGEG 242
Cdd:cd03295 162 PFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDFVAEFVGAD 239
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1-253 |
1.30e-76 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 240.51 E-value: 1.30e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 1 MTAALHIGHLSKSFQNTPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIfsknTNLPVRER 80
Cdd:PRK11607 16 LTPLLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDL----SHVPPYQR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 81 RLGYLVQEGVLFPHLTVYRNIAYGLGNGKGRTAQERQRIEAMLELTGISELAGRYPHELSGGQQQRVALARALAPDPELI 160
Cdd:PRK11607 92 PINMMFQSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 161 LLDEPFSALDEQLRRQIREDMIAALRANGKSAVFVSHDREEALQYADRIAVMKQGRILQTASPHELYRQPADLDAALFIG 240
Cdd:PRK11607 172 LLDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAEFIG 251
|
250
....*....|...
gi 1067578656 241 EGIVFPAALNADG 253
Cdd:PRK11607 252 SVNVFEGVLKERQ 264
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
35-285 |
3.78e-76 |
|
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: 237.39 E-value: 3.78e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 35 IIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIfsknTNLPVRERRLGYLVQEGVLFPHLTVYRNIAYGLGNGKGRTAQ 114
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDV----TNVPPHLRHINMVFQSYALFPHMTVEENVAFGLKMRKVPRAE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 115 ERQRIEAMLELTGISELAGRYPHELSGGQQQRVALARALAPDPELILLDEPFSALDEQLRRQIREDMIAALRANGKSAVF 194
Cdd:TIGR01187 77 IKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITFVF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 195 VSHDREEALQYADRIAVMKQGRILQTASPHELYRQPADLDAALFIGEGIVFPAA-LNADGTADCRLGRLPVQSGA----- 268
Cdd:TIGR01187 157 VTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFVARFIGEINVFEATvIERKSEQVVLAGVEGRRCDIytdvp 236
|
250
....*....|....*...
gi 1067578656 269 -PAGTRGTLLIRPEQFSL 285
Cdd:TIGR01187 237 vEKDQPLHVVLRPEKIVI 254
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
5-244 |
7.15e-75 |
|
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: 231.07 E-value: 7.15e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 5 LHIGHLSKSFQNTpVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIfsknTNLPVRERRLGY 84
Cdd:cd03299 1 LKVENLSKDWKEF-KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDI----TNLPPEKRDISY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 85 LVQEGVLFPHLTVYRNIAYGLGNGKGRTAQERQRIEAMLELTGISELAGRYPHELSGGQQQRVALARALAPDPELILLDE 164
Cdd:cd03299 76 VPQNYALFPHMTVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 165 PFSALDEQLRRQIREDMIAALRANGKSAVFVSHDREEALQYADRIAVMKQGRILQTASPHELYRQPADLDAALFIGEGIV 244
Cdd:cd03299 156 PFSALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPKNEFVAEFLGFNNI 235
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
20-219 |
1.42e-74 |
|
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: 229.49 E-value: 1.42e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 20 LNDISLSLD---PGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIF--SKNTNLPVRERRLGYLVQEGVLFPH 94
Cdd:cd03297 10 LPDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFdsRKKINLPPQQRKIGLVFQQYALFPH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 95 LTVYRNIAYGLGngKGRTAQERQRIEAMLELTGISELAGRYPHELSGGQQQRVALARALAPDPELILLDEPFSALDEQLR 174
Cdd:cd03297 90 LNVRENLAFGLK--RKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALR 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1067578656 175 RQIREDMIAALRANGKSAVFVSHDREEALQYADRIAVMKQGRILQ 219
Cdd:cd03297 168 LQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQY 212
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
9-221 |
2.90e-74 |
|
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: 228.68 E-value: 2.90e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 9 HLSKSFQNTPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIfsknTNLPVRERRLGYLVQE 88
Cdd:cd03301 5 NVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDV----TDLPPKDRDIAMVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 89 GVLFPHLTVYRNIAYGLGNGKGRTAQERQRIEAMLELTGISELAGRYPHELSGGQQQRVALARALAPDPELILLDEPFSA 168
Cdd:cd03301 81 YALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSN 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1067578656 169 LDEQLRRQIREDMIAALRANGKSAVFVSHDREEALQYADRIAVMKQGRILQTA 221
Cdd:cd03301 161 LDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
2-233 |
4.50e-74 |
|
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: 237.88 E-value: 4.50e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 2 TAALHIGHLSKSF-----QNTPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIfsknTNLP 76
Cdd:COG1123 258 EPLLEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDL----TKLS 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 77 VRE-----RRLGYLVQ--EGVLFPHLTVYRNIAYGLGN-GKGRTAQERQRIEAMLELTGIS-ELAGRYPHELSGGQQQRV 147
Cdd:COG1123 334 RRSlrelrRRVQMVFQdpYSSLNPRMTVGDIIAEPLRLhGLLSRAERRERVAELLERVGLPpDLADRYPHELSGGQRQRV 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 148 ALARALAPDPELILLDEPFSALDEQLRRQIReDMIAALRAN-GKSAVFVSHDREEALQYADRIAVMKQGRILQTASPHEL 226
Cdd:COG1123 414 AIARALALEPKLLILDEPTSALDVSVQAQIL-NLLRDLQRElGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEV 492
|
....*..
gi 1067578656 227 YRQPADL 233
Cdd:COG1123 493 FANPQHP 499
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
5-229 |
1.41e-73 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 227.64 E-value: 1.41e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 5 LHIGHLSKSFQNTPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIFSKNTNlpVReRRLGY 84
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAE--VR-RRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 85 LVQEGVLFPHLTVYRNIAYgLGNGKGRTAQE-RQRIEAMLELTGISELAGRYPHELSGGQQQRVALARALAPDPELILLD 163
Cdd:COG1131 78 VPQEPALYPDLTVRENLRF-FARLYGLPRKEaRERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILD 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1067578656 164 EPFSALDEQLRRQIReDMIAALRANGKSAVFVSHDREEALQYADRIAVMKQGRILQTASPHELYRQ 229
Cdd:COG1131 157 EPTSGLDPEARRELW-ELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKAR 221
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
9-235 |
1.49e-73 |
|
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: 227.22 E-value: 1.49e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 9 HLSKSFQN-TPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIFSKNTNlPVReRRLGYLVQ 87
Cdd:COG1122 5 NLSFSYPGgTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLR-ELR-RKVGLVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 88 egvlFP-----HLTVYRNIAYGLGNgKGRTAQE-RQRIEAMLELTGISELAGRYPHELSGGQQQRVALARALAPDPELIL 161
Cdd:COG1122 83 ----NPddqlfAPTVEEDVAFGPEN-LGLPREEiRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLV 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1067578656 162 LDEPFSALDEQLRRQIREdMIAALRANGKSAVFVSHDREEALQYADRIAVMKQGRILQTASPHELYRQPADLDA 235
Cdd:COG1122 158 LDEPTAGLDPRGRRELLE-LLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDYELLEE 230
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-226 |
2.60e-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: 227.17 E-value: 2.60e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 1 MTAALHIGHLSKSFQNTPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIfsknTNLPVRE- 79
Cdd:COG1127 2 SEPMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDI----TGLSEKEl 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 80 ----RRLGYLVQEGVLFPHLTVYRNIAYGLGNGKGRTAQE-RQRIEAMLELTGISELAGRYPHELSGGQQQRVALARALA 154
Cdd:COG1127 78 yelrRRIGMLFQGGALFDSLTVFENVAFPLREHTDLSEAEiRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1067578656 155 PDPELILLDEPFSALDEQLRRQIrEDMIAALR-ANGKSAVFVSHDREEALQYADRIAVMKQGRILQTASPHEL 226
Cdd:COG1127 158 LDPEILLYDEPTAGLDPITSAVI-DELIRELRdELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEEL 229
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
9-342 |
2.25e-72 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 228.45 E-value: 2.25e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 9 HLSKSFQNTPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIfsknTNLPVRERRLGYLVQE 88
Cdd:PRK11432 11 NITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDV----THRSIQQRDICMVFQS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 89 GVLFPHLTVYRNIAYGLgNGKGRTAQER-QRIEAMLELTGISELAGRYPHELSGGQQQRVALARALAPDPELILLDEPFS 167
Cdd:PRK11432 87 YALFPHMSLGENVGYGL-KMLGVPKEERkQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLS 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 168 ALDEQLRRQIREDMIAALRANGKSAVFVSHDREEALQYADRIAVMKQGRILQTASPHELYRQPADLDAALFIGEGIVFPA 247
Cdd:PRK11432 166 NLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPASRFMASFMGDANIFPA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 248 ALNADgTADCRLGRLP----VQSGAPAGTrGTLLIRPEQFSLHPHSAPA--ASIHAVVLkttpKARHTEISLR-AGQTVL 320
Cdd:PRK11432 246 TLSGD-YVDIYGYRLPrpaaFAFNLPDGE-CTVGVRPEAITLSEQGEESqrCTIKHVAY----MGPQYEVTVDwHGQELL 319
|
330 340
....*....|....*....|....*
gi 1067578656 321 tLNLPSA---PTLSDGISAVLHLDG 342
Cdd:PRK11432 320 -LQVNATqlqPDLGEHYYLEIHPYG 343
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
10-232 |
4.39e-72 |
|
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: 225.22 E-value: 4.39e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 10 LSKSFQNTPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTI--FSKNTNLPVRERRLGYLVQ 87
Cdd:cd03294 30 ILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIaaMSRKELRELRRKKISMVFQ 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 88 EGVLFPHLTVYRNIAYGLgNGKGRTAQER-QRIEAMLELTGISELAGRYPHELSGGQQQRVALARALAPDPELILLDEPF 166
Cdd:cd03294 110 SFALLPHRTVLENVAFGL-EVQGVPRAEReERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAF 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1067578656 167 SALDEQLRRQIREDMIAALRANGKSAVFVSHDREEALQYADRIAVMKQGRILQTASPHELYRQPAD 232
Cdd:cd03294 189 SALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPAN 254
|
|
| PhnT |
TIGR03258 |
2-aminoethylphosphonate ABC transport system, ATP-binding component PhnT; This ATP-binding ... |
2-319 |
1.49e-71 |
|
2-aminoethylphosphonate ABC transport system, ATP-binding component PhnT; This ATP-binding component of an ABC transport system is found in Salmonella and Burkholderia lineages in the vicinity of enzymes for the breakdown of 2-aminoethylphosphonate.
Pssm-ID: 132302 [Multi-domain] Cd Length: 362 Bit Score: 226.80 E-value: 1.49e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 2 TAALHIGHLSKSFQNTPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPD--SGEISLSGKTIfsknTNLPVRE 79
Cdd:TIGR03258 3 CGGIRIDHLRVAYGANTVLDDLSLEIEAGELLALIGKSGCGKTTLLRAIAGFVKAAglTGRIAIADRDL----THAPPHK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 80 RRLGYLVQEGVLFPHLTVYRNIAYGLGNGKGRTAQERQRIEAMLELTGISELAGRYPHELSGGQQQRVALARALAPDPEL 159
Cdd:TIGR03258 79 RGLALLFQNYALFPHLKVEDNVAFGLRAQKMPKADIAERVADALKLVGLGDAAAHLPAQLSGGMQQRIAIARAIAIEPDV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 160 ILLDEPFSALDEQLRRQIREDmIAAL--RANGKSAVFVSHDREEALQYADRIAVMKQGRILQTASPHELYRQPADLDAAL 237
Cdd:TIGR03258 159 LLLDEPLSALDANIRANMREE-IAALheELPELTILCVTHDQDDALTLADKAGIMKDGRLAAHGEPQALYDAPADGFAAE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 238 FIGEGIVFPA----ALNADGTADCRLGRLPVQS---GAPAGTRGTLLIRPEQFSLHPHSAPAASIHAVV--LKTTPKARH 308
Cdd:TIGR03258 238 FLGAANILPAialgITEAPGLVDVSCGGAVIFAfgdGRHDGRDKLACIRPEHLALTPRPAGEGRFHATIasVEWHGAALH 317
|
330
....*....|.
gi 1067578656 309 TEISLRAGQTV 319
Cdd:TIGR03258 318 LLCDLDAACDE 328
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
5-217 |
2.13e-71 |
|
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: 221.59 E-value: 2.13e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 5 LHIGHLSKSFQN----TPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIFSKNTN--LPVR 78
Cdd:cd03255 1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKelAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 79 ERRLGYLVQEGVLFPHLTVYRNIAYGLGNGKGRTAQERQRIEAMLELTGISELAGRYPHELSGGQQQRVALARALAPDPE 158
Cdd:cd03255 81 RRHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1067578656 159 LILLDEPFSALDEQLRRQIREDMIAALRANGKSAVFVSHDREEAlQYADRIAVMKQGRI 217
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELA-EYADRIIELRDGKI 218
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-217 |
2.97e-71 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 221.46 E-value: 2.97e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 1 MTAALHIGHLSKSFQN----TPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIFSKN---- 72
Cdd:COG1136 1 MSPLLELRNLTKSYGTgegeVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSerel 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 73 TNLpvRERRLGYLVQEGVLFPHLTVYRNIAYGLGNGKGRTAQERQRIEAMLELTGISELAGRYPHELSGGQQQRVALARA 152
Cdd:COG1136 81 ARL--RRRHIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1067578656 153 LAPDPELILLDEPFSALDEQLRRQIREDMIAALRANGKSAVFVSHDrEEALQYADRIAVMKQGRI 217
Cdd:COG1136 159 LVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHD-PELAARADRVIRLRDGRI 222
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
22-320 |
5.32e-71 |
|
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: 225.36 E-value: 5.32e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 22 DISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIFS--KNTNLPVRERRLGYLVQEGVLFPHLTVYR 99
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLQDsaRGIFLPPHRRRIGYVFQEARLFPHLSVRG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 100 NIAYGLGNGkgRTAQERQRIEAMLELTGISELAGRYPHELSGGQQQRVALARALAPDPELILLDEPFSALDEQLRRQIRe 179
Cdd:COG4148 97 NLLYGRKRA--PRAERRISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAEIL- 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 180 DMIAALRANGK-SAVFVSHDREEALQYADRIAVMKQGRILQTASPHELYRQPADLDAALFIGEGIVFPAAL----NADGT 254
Cdd:COG4148 174 PYLERLRDELDiPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRPDLLPLAGGEEAGSVLEATVaahdPDYGL 253
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1067578656 255 ADCRLG----RLPvQSGAPAGTRGTLLIRPEQFSLHPHSAPAASI----HAVVLKTTPKAR-HTEISLRAGQTVL 320
Cdd:COG4148 254 TRLALGggrlWVP-RLDLPPGTRVRVRIRARDVSLALEPPEGSSIlnilPGRVVEIEPADGgQVLVRLDLGGQTL 327
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
4-246 |
8.53e-71 |
|
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: 221.07 E-value: 8.53e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 4 ALHIGHLSKSFQNTPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIfsknTNLPVRE--RR 81
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDL----ASLSRRElaRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 82 LGYLVQEGVLFPHLTVYRNIAYG----LGNGKGRTAQERQRIEAMLELTGISELAGRYPHELSGGQQQRVALARALAPDP 157
Cdd:COG1120 77 IAYVPQEPPAPFGLTVRELVALGryphLGLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 158 ELILLDEPFSALDeqLRRQIR-EDMIAAL-RANGKSAVFVSHDREEALQYADRIAVMKQGRILQTASPHE---------L 226
Cdd:COG1120 157 PLLLLDEPTSHLD--LAHQLEvLELLRRLaRERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEvltpelleeV 234
|
250 260
....*....|....*....|
gi 1067578656 227 YRQPADLDAALFIGEGIVFP 246
Cdd:COG1120 235 YGVEARVIEDPVTGRPLVLP 254
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
5-216 |
7.98e-70 |
|
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: 215.90 E-value: 7.98e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 5 LHIGHLSKSFQNTPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIFSKNTNLPVRERRLGY 84
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPPLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 85 LVQEGVLFPHLTVYRNIAYGlgngkgrtaqerqrieamleltgiselagrypheLSGGQQQRVALARALAPDPELILLDE 164
Cdd:cd03229 81 VFQDFALFPHLTVLENIALG----------------------------------LSGGQQQRVALARALAMDPDVLLLDE 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1067578656 165 PFSALDEQLRRQIReDMIAALRAN-GKSAVFVSHDREEALQYADRIAVMKQGR 216
Cdd:cd03229 127 PTSALDPITRREVR-ALLKSLQAQlGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
9-216 |
1.26e-68 |
|
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: 214.25 E-value: 1.26e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 9 HLSKSF--QNTPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIfsKNTNLPVRERRLGYLV 86
Cdd:cd03225 4 NLSFSYpdGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDL--TKLSLKELRRKVGLVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 87 Q--EGVLFpHLTVYRNIAYGLGNGKGRTAQERQRIEAMLELTGISELAGRYPHELSGGQQQRVALARALAPDPELILLDE 164
Cdd:cd03225 82 QnpDDQFF-GPTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDE 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1067578656 165 PFSALDEQLRRQIREdMIAALRANGKSAVFVSHDREEALQYADRIAVMKQGR 216
Cdd:cd03225 161 PTAGLDPAGRRELLE-LLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
20-232 |
1.00e-67 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 217.66 E-value: 1.00e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 20 LNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTI--FSKNTNLPVRERRLGYLVQEGVLFPHLTV 97
Cdd:COG4175 43 VNDASFDVEEGEIFVIMGLSGSGKSTLVRCLNRLIEPTAGEVLIDGEDItkLSKKELRELRRKKMSMVFQHFALLPHRTV 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 98 YRNIAYGL---GNGKgrtAQERQRIEAMLELTGISELAGRYPHELSGGQQQRVALARALAPDPELILLDEPFSALDEQLR 174
Cdd:COG4175 123 LENVAFGLeiqGVPK---AERRERAREALELVGLAGWEDSYPDELSGGMQQRVGLARALATDPDILLMDEAFSALDPLIR 199
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1067578656 175 RQIREDMIAALRANGKSAVFVSHDREEALQYADRIAVMKQGRILQTASPHELYRQPAD 232
Cdd:COG4175 200 REMQDELLELQAKLKKTIVFITHDLDEALRLGDRIAIMKDGRIVQIGTPEEILTNPAN 257
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
9-226 |
1.26e-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: 209.67 E-value: 1.26e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 9 HLSKSFQNTPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIF--SKNTNLPVReRRLGYLV 86
Cdd:cd03261 5 GLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISglSEAELYRLR-RRMGMLF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 87 QEGVLFPHLTVYRNIAYGL-GNGKGRTAQERQRIEAMLELTGISELAGRYPHELSGGQQQRVALARALAPDPELILLDEP 165
Cdd:cd03261 84 QSGALFDSLTVFENVAFPLrEHTRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLYDEP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1067578656 166 FSALDEQLRRQIrEDMIAAL-RANGKSAVFVSHDREEALQYADRIAVMKQGRILQTASPHEL 226
Cdd:cd03261 164 TAGLDPIASGVI-DDLIRSLkKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEEL 224
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
5-217 |
1.29e-66 |
|
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: 208.92 E-value: 1.29e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 5 LHIGHLSKSFQNTPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIFSKNTNLPVRERRLGY 84
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNINELRQKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 85 LVQEGVLFPHLTVYRNIAYGLGNGKGRTAQERQRI-EAMLELTGISELAGRYPHELSGGQQQRVALARALAPDPELILLD 163
Cdd:cd03262 81 VFQQFNLFPHLTVLENITLAPIKVKGMSKAEAEERaLELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1067578656 164 EPFSALDEQLRRQIrEDMIAALRANGKSAVFVSHDREEALQYADRIAVMKQGRI 217
Cdd:cd03262 161 EPTSALDPELVGEV-LDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-217 |
4.91e-65 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 206.09 E-value: 4.91e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 1 MTAALHIGHLSKSFQNTPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIFSKNtnlpvreR 80
Cdd:COG1121 3 MMPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRAR-------R 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 81 RLGYLVQEGVL---FPhLTVYRNIAYGL----GNGKGRTAQERQRIEAMLELTGISELAGRYPHELSGGQQQRVALARAL 153
Cdd:COG1121 76 RIGYVPQRAEVdwdFP-ITVRDVVLMGRygrrGLFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARAL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1067578656 154 APDPELILLDEPFSALDEQLRRQIrEDMIAALRANGKSAVFVSHDREEALQYADRIAVMKQGRI 217
Cdd:COG1121 155 AQDPDLLLLDEPFAGVDAATEEAL-YELLRELRREGKTILVVTHDLGAVREYFDRVLLLNRGLV 217
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
9-238 |
9.42e-65 |
|
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: 205.48 E-value: 9.42e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 9 HLSKSFQNTPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIFSKNtnlPVRERRLGYLVQE 88
Cdd:COG4555 6 NLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEP---REARRQIGVLPDE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 89 GVLFPHLTVYRNIAYgLGNGKGRTAQE-RQRIEAMLELTGISELAGRYPHELSGGQQQRVALARALAPDPELILLDEPFS 167
Cdd:COG4555 83 RGLYDRLTVRENIRY-FAELYGLFDEElKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTN 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1067578656 168 ALDEQLRRQIREDmIAALRANGKSAVFVSHDREEALQYADRIAVMKQGRILQTASPHELYRQ--PADLDAALF 238
Cdd:COG4555 162 GLDVMARRLLREI-LRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREEigEENLEDAFV 233
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
3-299 |
1.07e-64 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 208.93 E-value: 1.07e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 3 AALHIGHLSKSFQN-TPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIfsknTNLPVRERR 81
Cdd:PRK11650 2 AGLKLQAVRKSYDGkTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVV----NELEPADRD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 82 LGYLVQEGVLFPHLTVYRNIAYGLGNGKGRTAQERQRIEAMLELTGISELAGRYPHELSGGQQQRVALARALAPDPELIL 161
Cdd:PRK11650 78 IAMVFQNYALYPHMSVRENMAYGLKIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 162 LDEPFSALDEQLRRQIR-EdmIAAL-RANGKSAVFVSHDREEALQYADRIAVMKQGRILQTASPHELYRQPADLDAALFI 239
Cdd:PRK11650 158 FDEPLSNLDAKLRVQMRlE--IQRLhRRLKTTSLYVTHDQVEAMTLADRVVVMNGGVAEQIGTPVEVYEKPASTFVASFI 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1067578656 240 GEGIV--FPAALNADGTA---DCRL-GRLPVQSGAPAGTRGTLLIRPEQFSLHPHsapAASIHAVV 299
Cdd:PRK11650 236 GSPAMnlLDGRVSADGAAfelAGGIaLPLGGGYRQYAGRKLTLGIRPEHIALSSA---EGGVPLTV 298
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
4-230 |
1.26e-64 |
|
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: 205.04 E-value: 1.26e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 4 ALHIGHLSKSF----QNTPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIfsKNTNLPVRE 79
Cdd:COG1124 1 MLEVRNLSVSYgqggRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPV--TRRRRKAFR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 80 RRLGYLVQ--EGVLFPHLTVYRNIAYGLgNGKGRTAQERqRIEAMLELTGI-SELAGRYPHELSGGQQQRVALARALAPD 156
Cdd:COG1124 79 RRVQMVFQdpYASLHPRHTVDRILAEPL-RIHGLPDREE-RIAELLEQVGLpPSFLDRYPHQLSGGQRQRVAIARALILE 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1067578656 157 PELILLDEPFSALDEQLRRQIReDMIAALRA-NGKSAVFVSHDREEALQYADRIAVMKQGRILQTASPHELYRQP 230
Cdd:COG1124 157 PELLLLDEPTSALDVSVQAEIL-NLLKDLREeRGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAGP 230
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
20-240 |
1.96e-64 |
|
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: 208.55 E-value: 1.96e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 20 LNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIF--SKNTNLPVRERRLGYLVQEGVLFPHLTV 97
Cdd:TIGR01186 9 VNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEPTAGQIFIDGENIMkqSPVELREVRRKKIGMVFQQFALFPHMTI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 98 YRNIAYGLGNGKGRTAQERQRIEAMLELTGISELAGRYPHELSGGQQQRVALARALAPDPELILLDEPFSALDEQLRRQI 177
Cdd:TIGR01186 89 LQNTSLGPELLGWPEQERKEKALELLKLVGLEEYEHRYPDELSGGMQQRVGLARALAAEPDILLMDEAFSALDPLIRDSM 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1067578656 178 REDMIAALRANGKSAVFVSHDREEALQYADRIAVMKQGRILQTASPHELYRQPADLDAALFIG 240
Cdd:TIGR01186 169 QDELKKLQATLQKTIVFITHDLDEAIRIGDRIVIMKAGEIVQVGTPDEILRNPANEYVEEFIG 231
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
5-217 |
3.31e-64 |
|
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: 203.51 E-value: 3.31e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 5 LHIGHLSKSFQN----TPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIFSKNTN-LPVRE 79
Cdd:cd03257 2 LEVKNLSVSFPTgggsVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRlRKIRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 80 RRLGYLVQE--GVLFPHLTVYRNIAYGLGNGKGRTAQERQRIEAMLELTGI---SELAGRYPHELSGGQQQRVALARALA 154
Cdd:cd03257 82 KEIQMVFQDpmSSLNPRMTIGEQIAEPLRIHGKLSKKEARKEAVLLLLVGVglpEEVLNRYPHELSGGQRQRVAIARALA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1067578656 155 PDPELILLDEPFSALDEQLRRQIrEDMIAALRA-NGKSAVFVSHDREEALQYADRIAVMKQGRI 217
Cdd:cd03257 162 LNPKLLIADEPTSALDVSVQAQI-LDLLKKLQEeLGLTLLFITHDLGVVAKIADRVAVMYAGKI 224
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
5-217 |
1.09e-63 |
|
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: 199.93 E-value: 1.09e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 5 LHIGHLSKSFQNTPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIFSKNTNLPvreRRLGY 84
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVK---RRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 85 LVQEGVLFPHLTVYRNIayglgngkgrtaqerqrieamleltgiselagryphELSGGQQQRVALARALAPDPELILLDE 164
Cdd:cd03230 78 LPEEPSLYENLTVRENL------------------------------------KLSGGMKQRLALAQALLHDPELLILDE 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1067578656 165 PFSALDEQLRRQIREdMIAALRANGKSAVFVSHDREEALQYADRIAVMKQGRI 217
Cdd:cd03230 122 PTSGLDPESRREFWE-LLRELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
3-223 |
2.24e-63 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 202.40 E-value: 2.24e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 3 AALHIGHLSKSF----QNTPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIFSkntnlPVR 78
Cdd:COG4525 2 SMLTVRHVSVRYpgggQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTG-----PGA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 79 ERrlGYLVQEGVLFPHLTVYRNIAYGLG-NGKGRtAQERQRIEAMLELTGISELAGRYPHELSGGQQQRVALARALAPDP 157
Cdd:COG4525 77 DR--GVVFQKDALLPWLNVLDNVAFGLRlRGVPK-AERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADP 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1067578656 158 ELILLDEPFSALDEQLRRQIREDMIAALRANGKSAVFVSHDREEALQYADRIAVMK--QGRILQTASP 223
Cdd:COG4525 154 RFLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHSVEEALFLATRLVVMSpgPGRIVERLEL 221
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
5-241 |
3.21e-63 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 201.14 E-value: 3.21e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 5 LHIGHLSKSFQNTPVlnDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIfsknTNLPVRERRLGY 84
Cdd:COG3840 2 LRLDDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDL----TALPPAERPVSM 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 85 LVQEGVLFPHLTVYRNIAYGLGNGKGRTAQERQRIEAMLELTGISELAGRYPHELSGGQQQRVALARALAPDPELILLDE 164
Cdd:COG3840 76 LFQENNLFPHLTVAQNIGLGLRPGLKLTAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDE 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1067578656 165 PFSALDEQLRRQIReDMIAALRAN-GKSAVFVSHDREEALQYADRIAVMKQGRILQTASPHELYRQPADLDAALFIGE 241
Cdd:COG3840 156 PFSALDPALRQEML-DLVDELCRErGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPPALAAYLGI 232
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-254 |
2.32e-62 |
|
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: 207.06 E-value: 2.32e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 1 MTAALHIGHLSKSF--QNTPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPD---SGEISLSGKTIFSknTNL 75
Cdd:COG1123 1 MTPLLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLE--LSE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 76 PVRERRLGYLVQE--GVLFPhLTVYRNIAYGLGNGKGRTAQERQRIEAMLELTGISELAGRYPHELSGGQQQRVALARAL 153
Cdd:COG1123 79 ALRGRRIGMVFQDpmTQLNP-VTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMAL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 154 APDPELILLDEPFSALDEQLRRQIREDMIAALRANGKSAVFVSHDREEALQYADRIAVMKQGRILQTASPHELYRQPADL 233
Cdd:COG1123 158 ALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAPQAL 237
|
250 260
....*....|....*....|.
gi 1067578656 234 DAALFIGEGIVFPAALNADGT 254
Cdd:COG1123 238 AAVPRLGAARGRAAPAAAAAE 258
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
5-230 |
1.17e-61 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 197.03 E-value: 1.17e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 5 LHIGHLSKSFQNT----PVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIFS-KNTNLPVRE 79
Cdd:cd03258 2 IELKNVSKVFGDTggkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLlSGKELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 80 RRLGYLVQEGVLFPHLTVYRNIAYGLGNGKGRTAQERQRIEAMLELTGISELAGRYPHELSGGQQQRVALARALAPDPEL 159
Cdd:cd03258 82 RRIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKV 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1067578656 160 ILLDEPFSALDEQLRRQIREDMIAALRANGKSAVFVSHDREEALQYADRIAVMKQGRILQTASPHELYRQP 230
Cdd:cd03258 162 LLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFANP 232
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
5-225 |
4.35e-61 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 194.62 E-value: 4.35e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 5 LHIGHLSKSFQNTPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPD---SGEISLSGKTIfsknTNLPVRERR 81
Cdd:COG4136 2 LSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRL----TALPAEQRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 82 LGYLVQEGVLFPHLTVYRNIAYGLGNGKGRtAQERQRIEAMLELTGISELAGRYPHELSGGQQQRVALARALAPDPELIL 161
Cdd:COG4136 78 IGILFQDDLLFPHLSVGENLAFALPPTIGR-AQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1067578656 162 LDEPFSALDEQLRRQIREDMIAALRANGKSAVFVSHDREEALQyadriavmkQGRILQTASPHE 225
Cdd:COG4136 157 LDEPFSKLDAALRAQFREFVFEQIRQRGIPALLVTHDEEDAPA---------AGRVLDLGNWQH 211
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
3-238 |
5.16e-61 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 196.05 E-value: 5.16e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 3 AALHIGHLSKSFQN-TPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIfsknTNLPVRE-- 79
Cdd:COG3638 1 PMLELRNLSKRYPGgTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDV----TALRGRAlr 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 80 ---RRLGYLVQEGVLFPHLTVYRNIAYGLGNGKGR--------TAQERQRIEAMLELTGISELAGRYPHELSGGQQQRVA 148
Cdd:COG3638 77 rlrRRIGMIFQQFNLVPRLSVLTNVLAGRLGRTSTwrsllglfPPEDRERALEALERVGLADKAYQRADQLSGGQQQRVA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 149 LARALAPDPELILLDEPFSALDEQLRRQIREDMIAALRANGKSAVFVSHDREEALQYADRIAVMKQGRILqtaspheLYR 228
Cdd:COG3638 157 IARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRVV-------FDG 229
|
250
....*....|
gi 1067578656 229 QPADLDAALF 238
Cdd:COG3638 230 PPAELTDAVL 239
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
22-295 |
1.01e-59 |
|
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: 196.10 E-value: 1.01e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 22 DISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIFS--KNTNLPVRERRLGYLVQEGVLFPHLTVYR 99
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDsrKGIFLPPEKRRIGYVFQEARLFPHLSVRG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 100 NIAYGLGngKGRTAQERQRIEAMLELTGISELAGRYPHELSGGQQQRVALARALAPDPELILLDEPFSALDEQLRRQIRE 179
Cdd:TIGR02142 95 NLRYGMK--RARPSERRISFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILP 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 180 DMIAALRANGKSAVFVSHDREEALQYADRIAVMKQGRILQTASPHELYRQPaDLDAALFIGEGIVFPAAL----NADGTA 255
Cdd:TIGR02142 173 YLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASP-DLPWLAREDQGSLIEGVVaehdQHYGLT 251
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1067578656 256 DCRL--GRLPV-QSGAPAGTRGTLLIRPEQFSLHPHSAPAASI 295
Cdd:TIGR02142 252 ALRLggGHLWVpENLGPTGARLRLRVPARDVSLALQKPEATSI 294
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
9-217 |
1.62e-59 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 191.03 E-value: 1.62e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 9 HLSKSFQN-TPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIfsknTNLPVRE-----RRL 82
Cdd:COG2884 6 NVSKRYPGgREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDL----SRLKRREipylrRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 83 GYLVQEGVLFPHLTVYRNIAYGLG-NGKGRtAQERQRIEAMLELTGISELAGRYPHELSGGQQQRVALARALAPDPELIL 161
Cdd:COG2884 82 GVVFQDFRLLPDRTVYENVALPLRvTGKSR-KEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1067578656 162 LDEPFSALDEQLRRQIREdMIAALRANGKSAVFVSHDREEALQYADRIAVMKQGRI 217
Cdd:COG2884 161 ADEPTGNLDPETSWEIME-LLEEINRRGTTVLIATHDLELVDRMPKRVLELEDGRL 215
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
11-230 |
2.13e-59 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 191.46 E-value: 2.13e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 11 SKSFQNTPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIFSKNTNlpVRERRL--GYLVQE 88
Cdd:PRK09493 8 SKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVD--ERLIRQeaGMVFQQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 89 GVLFPHLTVYRNIAYGLGNGKGRTAQE-RQRIEAMLELTGISELAGRYPHELSGGQQQRVALARALAPDPELILLDEPFS 167
Cdd:PRK09493 86 FYLFPHLTALENVMFGPLRVRGASKEEaEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTS 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1067578656 168 ALDEQLRRQIREDMiAALRANGKSAVFVSHDREEALQYADRIAVMKQGRILQTASPHELYRQP 230
Cdd:PRK09493 166 ALDPELRHEVLKVM-QDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNP 227
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
11-314 |
1.07e-58 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 193.71 E-value: 1.07e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 11 SKSFQNTPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIfsknTNLPVRERRLGYLVQEGV 90
Cdd:PRK11000 10 TKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRM----NDVPPAERGVGMVFQSYA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 91 LFPHLTVYRNIAYGLGNGKGRTAQERQRIEAMLELTGISELAGRYPHELSGGQQQRVALARALAPDPELILLDEPFSALD 170
Cdd:PRK11000 86 LYPHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLD 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 171 EQLRRQIREDmIAAL-RANGKSAVFVSHDREEALQYADRIAVMKQGRILQTASPHELYRQPADLDAALFIGEG-----IV 244
Cdd:PRK11000 166 AALRVQMRIE-ISRLhKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPANRFVAGFIGSPkmnflPV 244
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1067578656 245 FPAALNADG----TADCRLGRLPVQS-GAPAGTRGTLLIRPEQfsLHPHSAPAASIHAVVLKTTPKARHTEISLR 314
Cdd:PRK11000 245 KVTATAIEQvqveLPNRQQVWLPVEGrGVQVGANMSLGIRPEH--LLPSDIADVTLEGEVQVVEQLGNETQIHIQ 317
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
5-217 |
6.35e-58 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 186.56 E-value: 6.35e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 5 LHIGHLSKSFQNTPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIfsknTNLPVRE--RRL 82
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPL----SAMPPPEwrRQV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 83 GYLVQEGVLFPHlTVYRNIAYGLGNGKGRTaqERQRIEAMLELTGISE-LAGRYPHELSGGQQQRVALARALAPDPELIL 161
Cdd:COG4619 77 AYVPQEPALWGG-TVRDNLPFPFQLRERKF--DRERALELLERLGLPPdILDKPVERLSGGERQRLALIRALLLQPDVLL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1067578656 162 LDEPFSALDEQLRRQIrEDMIAALRAN-GKSAVFVSHDREEALQYADRIAVMKQGRI 217
Cdd:COG4619 154 LDEPTSALDPENTRRV-EELLREYLAEeGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
5-231 |
1.03e-57 |
|
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: 186.87 E-value: 1.03e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 5 LHIGHLSKSFQNTPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIfsknTNLPVRER-RLG 83
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDI----TGLPPHEIaRLG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 84 yLV---QEGVLFPHLTVYRNIAYGLGNGKGRT----------AQERQRIEAMLELTGISELAGRYPHELSGGQQQRVALA 150
Cdd:cd03219 77 -IGrtfQIPRLFPELTVLENVMVAAQARTGSGlllararreeREARERAEELLERVGLADLADRPAGELSYGQQRRLEIA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 151 RALAPDPELILLDEPFSALDEQLRRQIREdMIAALRANGKSAVFVSHDREEALQYADRIAVMKQGRILQTASPHELYRQP 230
Cdd:cd03219 156 RALATDPKLLLLDEPAAGLNPEETEELAE-LIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRNNP 234
|
.
gi 1067578656 231 A 231
Cdd:cd03219 235 R 235
|
|
| ABC_choXWV_ATP |
TIGR03415 |
choline ABC transporter, ATP-binding protein; Members of this protein family are the ... |
21-239 |
3.58e-57 |
|
choline ABC transporter, ATP-binding protein; Members of this protein family are the ATP-binding subunit of a three-protein transporter. This family belongs, more broadly, to the family of proline and glycine-betaine transporters, but members have been identified by direct characterization and by bioinformatic means as choline transporters. Many species have several closely-related members of this family, probably with variable abilities to act additionally on related quaternary amines. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 188317 [Multi-domain] Cd Length: 382 Bit Score: 190.37 E-value: 3.58e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 21 NDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIFSKNTNLPV------RERRLGYLVQEGVLFPH 94
Cdd:TIGR03415 41 HNASLDIEEGEICVLMGLSGSGKSTLLRAVNGLNPVSRGSVLVKDGDGSVDVANCDAatlrrlRTHRVSMVFQQFALLPW 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 95 LTVYRNIAYGL---GNGKgrtAQERQRIEAMLELTGISELAGRYPHELSGGQQQRVALARALAPDPELILLDEPFSALDE 171
Cdd:TIGR03415 121 RTVEENVAFGLemqGMPK---AERRKRVDEQLELVGLAQWADRKPGELSGGMQQRVGLARAFATEAPILLMDEPFSALDP 197
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1067578656 172 QLRRQIREDMIAALRANGKSAVFVSHDREEALQYADRIAVMKQGRILQTASPHELYRQPADLDAALFI 239
Cdd:TIGR03415 198 LIRTQLQDELLELQSKLKKTIVFVSHDLDEALKIGNRIAIMEGGRIIQHGTPEEIVLNPANDYVADFV 265
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
5-231 |
1.18e-56 |
|
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: 186.80 E-value: 1.18e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 5 LHIGHLSKSFQ----NTPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQP---DSGEISLSGKTI--FSKNTNL 75
Cdd:COG0444 2 LEVRNLKVYFPtrrgVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLlkLSEKELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 76 PVRERRLGYLVQE--GVLFPHLTVYRNIAYGLGNGKGRTAQE-RQRIEAMLELTGIS---ELAGRYPHELSGGQQQRVAL 149
Cdd:COG0444 82 KIRGREIQMIFQDpmTSLNPVMTVGDQIAEPLRIHGGLSKAEaRERAIELLERVGLPdpeRRLDRYPHELSGGMRQRVMI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 150 ARALAPDPELILLDEPFSALDEQLRRQIrEDMIAALRAN-GKSAVFVSHDREEALQYADRIAVMKQGRILQTASPHELYR 228
Cdd:COG0444 162 ARALALEPKLLIADEPTTALDVTIQAQI-LNLLKDLQRElGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGPVEELFE 240
|
...
gi 1067578656 229 QPA 231
Cdd:COG0444 241 NPR 243
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
9-215 |
2.47e-56 |
|
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: 182.73 E-value: 2.47e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 9 HLSKSFQNTPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIFSKNtnlpvreRRLGYLVQE 88
Cdd:cd03235 4 DLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKER-------KRIGYVPQR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 89 GVL---FPhLTVYRNIAYGL----GNGKGRTAQERQRIEAMLELTGISELAGRYPHELSGGQQQRVALARALAPDPELIL 161
Cdd:cd03235 77 RSIdrdFP-ISVRDVVLMGLyghkGLFRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1067578656 162 LDEPFSALDEQLRRQIREdMIAALRANGKSAVFVSHDREEALQYADRIAVMKQG 215
Cdd:cd03235 156 LDEPFAGVDPKTQEDIYE-LLRELRREGMTILVVTHDLGLVLEYFDRVLLLNRT 208
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
9-218 |
5.01e-56 |
|
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: 180.71 E-value: 5.01e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 9 HLSKSFQNTPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIfsknTNLPVRE--RRLGYLV 86
Cdd:cd03214 4 NLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDL----ASLSPKElaRKIAYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 87 QegvlfphltvyrniayglgngkgrtaqerqrieaMLELTGISELAGRYPHELSGGQQQRVALARALAPDPELILLDEPF 166
Cdd:cd03214 80 Q----------------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPT 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1067578656 167 SALDeqLRRQIR-EDMIAAL-RANGKSAVFVSHDREEALQYADRIAVMKQGRIL 218
Cdd:cd03214 126 SHLD--IAHQIElLELLRRLaRERGKTVVMVLHDLNLAARYADRVILLKDGRIV 177
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
10-226 |
9.87e-56 |
|
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: 181.61 E-value: 9.87e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 10 LSKSFQNTPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGF-----EQPDSGEISLSGKTIFSKNTNLPVRERRLGY 84
Cdd:cd03260 6 LNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLndlipGAPDEGEVLLDGKDIYDLDVDVLELRRRVGM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 85 LVQEGVLFPhLTVYRNIAYGLG-NGKGRTAQERQRIEAMLELTGISELAGR--YPHELSGGQQQRVALARALAPDPELIL 161
Cdd:cd03260 86 VFQKPNPFP-GSIYDNVAYGLRlHGIKLKEELDERVEEALRKAALWDEVKDrlHALGLSGGQQQRLCLARALANEPEVLL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1067578656 162 LDEPFSALDEQLRRQIrEDMIAALRANgKSAVFVSHDREEALQYADRIAVMKQGRILQTASPHEL 226
Cdd:cd03260 165 LDEPTSALDPISTAKI-EELIAELKKE-YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
9-230 |
1.25e-55 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 184.90 E-value: 1.25e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 9 HLSKSF----QNTPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIfsknTNLPVRE----- 79
Cdd:COG1135 6 NLSKTFptkgGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDL----TALSERElraar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 80 RRLGYLVQEGVLFPHLTVYRNIAYGL-GNGKGRtAQERQRIEAMLELTGISELAGRYPHELSGGQQQRVALARALAPDPE 158
Cdd:COG1135 82 RKIGMIFQHFNLLSSRTVAENVALPLeIAGVPK-AEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPK 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1067578656 159 LILLDEPFSALDEQ-------LRRQIREDMiaalranGKSAVFVSHDREEALQYADRIAVMKQGRILQTASPHELYRQP 230
Cdd:COG1135 161 VLLCDEATSALDPEttrsildLLKDINREL-------GLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVLDVFANP 232
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
9-233 |
1.36e-55 |
|
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: 182.65 E-value: 1.36e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 9 HLSKSFQ-NTP----VLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIFSKN-TNL-PVReRR 81
Cdd:TIGR04521 5 NVSYIYQpGTPfekkALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKkKKLkDLR-KK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 82 LGYLVQ--EGVLFpHLTVYRNIAYGLGNgKGRTAQE-RQRIEAMLELTGISE-LAGRYPHELSGGQQQRVALARALAPDP 157
Cdd:TIGR04521 84 VGLVFQfpEHQLF-EETVYKDIAFGPKN-LGLSEEEaEERVKEALELVGLDEeYLERSPFELSGGQMRRVAIAGVLAMEP 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1067578656 158 ELILLDEPFSALDEQLRRQIReDMIAAL-RANGKSAVFVSHDREEALQYADRIAVMKQGRILQTASPHELYRQPADL 233
Cdd:TIGR04521 162 EVLILDEPTAGLDPKGRKEIL-DLFKRLhKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVFSDVDEL 237
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
5-226 |
2.20e-54 |
|
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: 178.53 E-value: 2.20e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 5 LHIGHLSKSFQN-TPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIfsknTNLPVRE---- 79
Cdd:cd03256 1 IEVENLSKTYPNgKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDI----NKLKGKAlrql 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 80 -RRLGYLVQEGVLFPHLTVYRNIAYG-LGN-GKGR------TAQERQRIEAMLELTGISELAGRYPHELSGGQQQRVALA 150
Cdd:cd03256 77 rRQIGMIFQQFNLIERLSVLENVLSGrLGRrSTWRslfglfPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1067578656 151 RALAPDPELILLDEPFSALDEQLRRQIREDMIAALRANGKSAVFVSHDREEALQYADRIAVMKQGRILQTASPHEL 226
Cdd:cd03256 157 RALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAEL 232
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-231 |
8.09e-54 |
|
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: 177.54 E-value: 8.09e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 1 MTAALHIGHLSKSFQNTPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIfsknTNLPVRER 80
Cdd:COG0411 1 SDPLLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDI----TGLPPHRI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 81 -RLGyLV---QEGVLFPHLTVYRNIAYGLGNGKGRT---------------AQERQRIEAMLELTGISELAGRYPHELSG 141
Cdd:COG0411 77 aRLG-IArtfQNPRLFPELTVLENVLVAAHARLGRGllaallrlprarreeREARERAEELLERVGLADRADEPAGNLSY 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 142 GQQQRVALARALAPDPELILLDEPFSALDEQLRRQIReDMIAALRAN-GKSAVFVSHDREEALQYADRIAVMKQGRILQT 220
Cdd:COG0411 156 GQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELA-ELIRRLRDErGITILLIEHDMDLVMGLADRIVVLDFGRVIAE 234
|
250
....*....|.
gi 1067578656 221 ASPHELYRQPA 231
Cdd:COG0411 235 GTPAEVRADPR 245
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
5-226 |
2.72e-52 |
|
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: 172.30 E-value: 2.72e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 5 LHIGHLSKSFQN--TPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGktiFSKNTNLPVRERRL 82
Cdd:cd03263 1 LQIRNLTKTYKKgtKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYING---YSIRTDRKAARQSL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 83 GYLVQEGVLFPHLTVYRNIA-YGLGNGKGRTaQERQRIEAMLELTGISELAGRYPHELSGGQQQRVALARALAPDPELIL 161
Cdd:cd03263 78 GYCPQFDALFDELTVREHLRfYARLKGLPKS-EIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1067578656 162 LDEPFSALDEQLRRQIReDMIAALRANgKSAVFVSHDREEALQYADRIAVMKQGRILQTASPHEL 226
Cdd:cd03263 157 LDEPTSGLDPASRRAIW-DLILEVRKG-RSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQEL 219
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
20-231 |
1.36e-51 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 174.15 E-value: 1.36e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 20 LNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIF--SKNTNLPVReRRLGYLVQE--GVLFPHL 95
Cdd:COG4608 34 VDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITglSGRELRPLR-RRMQMVFQDpyASLNPRM 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 96 TVYRNIAYGLG-NGKGRTAQERQRIEAMLELTGIS-ELAGRYPHELSGGQQQRVALARALAPDPELILLDEPFSALDEQL 173
Cdd:COG4608 113 TVGDIIAEPLRiHGLASKAERRERVAELLELVGLRpEHADRYPHEFSGGQRQRIGIARALALNPKLIVCDEPVSALDVSI 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1067578656 174 RRQI-------REDMiaalranGKSAVFVSHD----ReealQYADRIAVMKQGRILQTASPHELYRQPA 231
Cdd:COG4608 193 QAQVlnlledlQDEL-------GLTYLFISHDlsvvR----HISDRVAVMYLGKIVEIAPRDELYARPL 250
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
3-202 |
1.84e-51 |
|
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: 169.97 E-value: 1.84e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 3 AALHIGHLSKSFQNTPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIfskNTNLPVRERRL 82
Cdd:COG4133 1 MMLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPI---RDAREDYRRRL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 83 GYLVQEGVLFPHLTVYRNIAYGLGNGKGRTAQErqRIEAMLELTGISELAGRYPHELSGGQQQRVALARALAPDPELILL 162
Cdd:COG4133 78 AYLGHADGLKPELTVRENLRFWAALYGLRADRE--AIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1067578656 163 DEPFSALDEQLRRQIrEDMIAALRANGKSAVFVSHDREEA 202
Cdd:COG4133 156 DEPFTALDAAGVALL-AELIAAHLARGGAVLLTTHQPLEL 194
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
5-225 |
2.23e-51 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 171.45 E-value: 2.23e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 5 LHIGHLSKSFQNTPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIfsknTNLPVRE--RRL 82
Cdd:COG4559 2 LEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPL----AAWSPWElaRRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 83 GYLVQEGVL-FPhLTVYRNIAYGLGNGKGRTAQERQRIEAMLELTGISELAGRYPHELSGGQQQRVALARALA------- 154
Cdd:COG4559 78 AVLPQHSSLaFP-FTVEEVVALGRAPHGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLAqlwepvd 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1067578656 155 PDPELILLDEPFSALDeqLRRQIREDMIAALRANGKSAVF-VSHDREEALQYADRIAVMKQGRILQTASPHE 225
Cdd:COG4559 157 GGPRWLFLDEPTSALD--LAHQHAVLRLARQLARRGGGVVaVLHDLNLAAQYADRILLLHQGRLVAQGTPEE 226
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
5-238 |
4.50e-51 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 170.58 E-value: 4.50e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 5 LHIGHLSKSFQNTPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIfsknTNLPVRE--RRL 82
Cdd:PRK11231 3 LRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPI----SMLSSRQlaRRL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 83 GYLVQ-----EGVlfphlTVYRNIAYGLG---NGKGRTAQE-RQRIEAMLELTGISELAGRYPHELSGGQQQRVALARAL 153
Cdd:PRK11231 79 ALLPQhhltpEGI-----TVRELVAYGRSpwlSLWGRLSAEdNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 154 APDPELILLDEPFSALDeqLRRQIR-EDMIAALRANGKSAVFVSHDREEALQYADRIAVMKQGRILQTASPHE-----LY 227
Cdd:PRK11231 154 AQDTPVVLLDEPTTYLD--INHQVElMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEvmtpgLL 231
|
250
....*....|.
gi 1067578656 228 RQPADLDAALF 238
Cdd:PRK11231 232 RTVFDVEAEIH 242
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-229 |
5.06e-51 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 171.83 E-value: 5.06e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 4 ALHIGHLSKSFQNTPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIfskntNLPVReRRLG 83
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPL-----DPEDR-RRIG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 84 YLVQEGVLFPHLTVYRNIAYgLGNGKGRTAQE-RQRIEAMLELTGISELAGRYPHELSGGQQQRVALARALAPDPELILL 162
Cdd:COG4152 75 YLPEERGLYPKMKVGEQLVY-LARLKGLSKAEaKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLIL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1067578656 163 DEPFSALD----EQLRRQIREdmiaaLRANGKSAVFVSHDREEALQYADRIAVMKQGRILQTASPHELYRQ 229
Cdd:COG4152 154 DEPFSGLDpvnvELLKDVIRE-----LAAKGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEIRRQ 219
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
4-223 |
9.76e-51 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 169.50 E-value: 9.76e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 4 ALHIGHLSKSFQNTPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIfskntNLPVRERrlG 83
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPV-----EGPGAER--G 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 84 YLVQEGVLFPHLTVYRNIAYGLGNGKGRTAQERQRIEAMLELTGISELAGRYPHELSGGQQQRVALARALAPDPELILLD 163
Cdd:PRK11248 74 VVFQNEGLLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLD 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1067578656 164 EPFSALDEQLRRQIREDMIAALRANGKSAVFVSHDREEALQYADRIAVMK--QGRILQTASP 223
Cdd:PRK11248 154 EPFGALDAFTREQMQTLLLKLWQETGKQVLLITHDIEEAVFMATELVLLSpgPGRVVERLPL 215
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
3-225 |
9.79e-51 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 169.57 E-value: 9.79e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 3 AALHIGHLSKSFQNTPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIfsknTNLPVRE--R 80
Cdd:PRK13548 1 AMLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPL----ADWSPAElaR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 81 RLGYLVQEGVL-FPhLTVYRNIAYGLGNGKGRTAQERQRIEAMLELTGISELAGRYPHELSGGQQQRVALARALA----- 154
Cdd:PRK13548 77 RRAVLPQHSSLsFP-FTVEEVVAMGRAPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAqlwep 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1067578656 155 -PDPELILLDEPFSALDeqLRRQIREDMIAALRA--NGKSAVFVSHDREEALQYADRIAVMKQGRILQTASPHE 225
Cdd:PRK13548 156 dGPPRWLLLDEPTSALD--LAHQHHVLRLARQLAheRGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAE 227
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
9-209 |
1.70e-50 |
|
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: 167.41 E-value: 1.70e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 9 HLSKSFQNTPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIFSKNTNLPVRERR--LGYLV 86
Cdd:TIGR03608 3 NISKKFGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLNSKKASKFRRekLGYLF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 87 QEGVLFPHLTVYRNIAYGLGNGKGRTAQERQRIEAMLELTGISELAGRYPHELSGGQQQRVALARALAPDPELILLDEPF 166
Cdd:TIGR03608 83 QNFALIENETVEENLDLGLKYKKLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLILADEPT 162
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1067578656 167 SALDEQLRRQIReDMIAALRANGKSAVFVSHDREEALQyADRI 209
Cdd:TIGR03608 163 GSLDPKNRDEVL-DLLLELNDEGKTIIIVTHDPEVAKQ-ADRV 203
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
13-217 |
2.76e-50 |
|
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: 166.90 E-value: 2.76e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 13 SFQNTPVlnDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIfsknTNLPVRERRLGYLVQEGVLF 92
Cdd:cd03298 9 SYGEQPM--HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDV----TAAPPADRPVSMLFQENNLF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 93 PHLTVYRNIAYGLGNGKGRTAQERQRIEAMLELTGISELAGRYPHELSGGQQQRVALARALAPDPELILLDEPFSALDEQ 172
Cdd:cd03298 83 AHLTVEQNVGLGLSPGLKLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPA 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1067578656 173 LRRQIrEDMIAALRANGKSAV-FVSHDREEALQYADRIAVMKQGRI 217
Cdd:cd03298 163 LRAEM-LDLVLDLHAETKMTVlMVTHQPEDAKRLAQRVVFLDNGRI 207
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
2-230 |
4.70e-50 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 168.06 E-value: 4.70e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 2 TAALHIGHLSKSFQNTPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTI---FSKNTNLPVR 78
Cdd:COG4598 6 PPALEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIrlkPDRDGELVPA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 79 ER--------RLGYLVQEGVLFPHLTVYRNIAYG----LGNGKgrtAQERQRIEAMLELTGISELAGRYPHELSGGQQQR 146
Cdd:COG4598 86 DRrqlqrirtRLGMVFQSFNLWSHMTVLENVIEApvhvLGRPK---AEAIERAEALLAKVGLADKRDAYPAHLSGGQQQR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 147 VALARALAPDPELILLDEPFSALD-----EQLRrqiredMIAALRANGKSAVFVSHDREEALQYADRIAVMKQGRILQTA 221
Cdd:COG4598 163 AAIARALAMEPEVMLFDEPTSALDpelvgEVLK------VMRDLAEEGRTMLVVTHEMGFARDVSSHVVFLHQGRIEEQG 236
|
....*....
gi 1067578656 222 SPHELYRQP 230
Cdd:COG4598 237 PPAEVFGNP 245
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
5-227 |
5.06e-50 |
|
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: 167.48 E-value: 5.06e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 5 LHIGHLSKSFQN-TPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIfsknTNLPVRE---- 79
Cdd:TIGR02315 2 LEVENLSKVYPNgKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDI----TKLRGKKlrkl 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 80 -RRLGYLVQEGVLFPHLTVYRNIAYGLGNGKGR--------TAQERQRIEAMLELTGISELAGRYPHELSGGQQQRVALA 150
Cdd:TIGR02315 78 rRRIGMIFQHYNLIERLTVLENVLHGRLGYKPTwrsllgrfSEEDKERALSALERVGLADKAYQRADQLSGGQQQRVAIA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1067578656 151 RALAPDPELILLDEPFSALDEQLRRQIREDMIAALRANGKSAVFVSHDREEALQYADRIAVMKQGRILQTASPHELY 227
Cdd:TIGR02315 158 RALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSELD 234
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
15-226 |
1.10e-49 |
|
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: 176.56 E-value: 1.10e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 15 QNTPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIfsKNTNLPVRERRLGYLVQEGVLFpH 94
Cdd:COG2274 486 DSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDL--RQIDPASLRRQIGVVLQDVFLF-S 562
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 95 LTVYRNIAYglgngkGRTAQERQRIEAMLELTGISELAGRYPH-----------ELSGGQQQRVALARALAPDPELILLD 163
Cdd:COG2274 563 GTIRENITL------GDPDATDEEIIEAARLAGLHDFIEALPMgydtvvgeggsNLSGGQRQRLAIARALLRNPRILILD 636
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1067578656 164 EPFSALDEQLRRQIredmIAALR--ANGKSAVFVSHdREEALQYADRIAVMKQGRILQTASPHEL 226
Cdd:COG2274 637 EATSALDAETEAII----LENLRrlLKGRTVIIIAH-RLSTIRLADRIIVLDKGRIVEDGTHEEL 696
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
20-167 |
1.17e-49 |
|
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: 163.20 E-value: 1.17e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 20 LNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIFSKntNLPVRERRLGYLVQEGVLFPHLTVYR 99
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDD--ERKSLRKEIGYVFQDPQLFPRLTVRE 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1067578656 100 NIAYGLGNGKGRTAQERQRIEAMLELTGISELA----GRYPHELSGGQQQRVALARALAPDPELILLDEPFS 167
Cdd:pfam00005 79 NLRLGLLLKGLSKREKDARAEEALEKLGLGDLAdrpvGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
9-231 |
2.42e-49 |
|
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: 165.41 E-value: 2.42e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 9 HLSKSFQNTPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIfsknTNLPVRERR---LGYL 85
Cdd:cd03218 5 NLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDI----TKLPMHKRArlgIGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 86 VQEGVLFPHLTVYRNIAYGLGNGKGRTAQERQRIEAMLELTGISELAGRYPHELSGGQQQRVALARALAPDPELILLDEP 165
Cdd:cd03218 81 PQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1067578656 166 FSALDEQLRRQIREdMIAALRANGKSAVFVSHDREEALQYADRIAVMKQGRILQTASPHELYRQPA 231
Cdd:cd03218 161 FAGVDPIAVQDIQK-IIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANEL 225
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
9-216 |
4.92e-49 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 162.03 E-value: 4.92e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 9 HLSKSFQNTPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIFSKNtnLPVRERRLGYLVQe 88
Cdd:cd00267 4 NLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLP--LEELRRRIGYVPQ- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 89 gvlfphltvyrniayglgngkgrtaqerqrieamleltgiselagrypheLSGGQQQRVALARALAPDPELILLDEPFSA 168
Cdd:cd00267 81 --------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSG 110
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1067578656 169 LDEQLRRQIREdMIAALRANGKSAVFVSHDREEALQYADRIAVMKQGR 216
Cdd:cd00267 111 LDPASRERLLE-LLRELAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-226 |
1.20e-48 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 170.58 E-value: 1.20e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 1 MTAALHIGHLSKSFQNTPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIFSKNtnlPVRER 80
Cdd:COG1129 1 AEPLLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRS---PRDAQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 81 RLG-YLV-QEGVLFPHLTVYRNIAygLGNGKGR-----TAQERQRIEAMLELTGISELAGRYPHELSGGQQQRVALARAL 153
Cdd:COG1129 78 AAGiAIIhQELNLVPNLSVAENIF--LGREPRRgglidWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARAL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1067578656 154 APDPELILLDEPFSALD----EQLRRQIREdmiaaLRANGKSAVFVSHDREEALQYADRIAVMKQGRILQTASPHEL 226
Cdd:COG1129 156 SRDARVLILDEPTASLTerevERLFRIIRR-----LKAQGVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVAEL 227
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
24-239 |
1.12e-47 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 160.90 E-value: 1.12e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 24 SLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTifskNTNLPVRERRLGYLVQEGVLFPHLTVYRNIAY 103
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQD----HTTTPPSRRPVSMLFQENNLFSHLTVAQNIGL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 104 GLGNGKGRTAQERQRIEAMLELTGISELAGRYPHELSGGQQQRVALARALAPDPELILLDEPFSALDEQLRRQIREDMIA 183
Cdd:PRK10771 95 GLNPGLKLNAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLVSQ 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1067578656 184 ALRANGKSAVFVSHDREEALQYADRIAVMKQGRILQTASPHELYRQPADLDAALFI 239
Cdd:PRK10771 175 VCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELLSGKASASALLGI 230
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
3-230 |
1.19e-47 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 161.46 E-value: 1.19e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 3 AALHIGHLSKSFQNTPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTI-----FSKNTNLpV 77
Cdd:PRK11264 2 SAIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIdtarsLSQQKGL-I 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 78 RERR--LGYLVQEGVLFPHLTVYRNIAYGLGNGKGRTAQER-QRIEAMLELTGISELAGRYPHELSGGQQQRVALARALA 154
Cdd:PRK11264 81 RQLRqhVGFVFQNFNLFPHRTVLENIIEGPVIVKGEPKEEAtARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1067578656 155 PDPELILLDEPFSALDEQLRRQIReDMIAALRANGKSAVFVSHDREEALQYADRIAVMKQGRILQTASPHELYRQP 230
Cdd:PRK11264 161 MRPEVILFDEPTSALDPELVGEVL-NTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADP 235
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
20-215 |
1.93e-47 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 160.32 E-value: 1.93e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 20 LNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIfskntNLPVRERRLgyLVQEGVLFPHLTVYR 99
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQI-----TEPGPDRMV--VFQNYSLLPWLTVRE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 100 NIAYGLG--NGKGRTAQERQRIEAMLELTGISELAGRYPHELSGGQQQRVALARALAPDPELILLDEPFSALDEQLRRQI 177
Cdd:TIGR01184 74 NIALAVDrvLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNL 153
|
170 180 190
....*....|....*....|....*....|....*...
gi 1067578656 178 REDMIAALRANGKSAVFVSHDREEALQYADRIAVMKQG 215
Cdd:TIGR01184 154 QEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
24-219 |
2.12e-47 |
|
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: 159.64 E-value: 2.12e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 24 SLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIfsknTNLPVRERRLGYLVQEGVLFPHLTVYRNIAY 103
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSH----TGLAPYQRPVSMLFQENNLFAHLTVRQNIGL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 104 GLGNGKGRTAQERQRIEAMLELTGISELAGRYPHELSGGQQQRVALARALAPDPELILLDEPFSALDEQLRRQIREDMIA 183
Cdd:TIGR01277 94 GLHPGLKLNAEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALVKQ 173
|
170 180 190
....*....|....*....|....*....|....*.
gi 1067578656 184 ALRANGKSAVFVSHDREEALQYADRIAVMKQGRILQ 219
Cdd:TIGR01277 174 LCSERQRTLLMVTHHLSDARAIASQIAVVSQGKIKV 209
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
5-217 |
2.61e-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: 159.37 E-value: 2.61e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 5 LHIGHLSKSFQNTPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIfskntnLPVRERRLGY 84
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPL------DIAARNRIGY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 85 LVQEGVLFPHLTVYRNIAYgLGNGKGRTAQE-RQRIEAMLELTGISELAGRYPHELSGGQQQRVALARALAPDPELILLD 163
Cdd:cd03269 75 LPEERGLYPKMKVIDQLVY-LAQLKGLKKEEaRRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILD 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1067578656 164 EPFSALDEqLRRQIREDMIAALRANGKSAVFVSHDREEALQYADRIAVMKQGRI 217
Cdd:cd03269 154 EPFSGLDP-VNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRA 206
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
5-230 |
2.87e-47 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 160.19 E-value: 2.87e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 5 LHIGHLSKSFQNTPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIfsknTNLPVRER-RLG 83
Cdd:COG1137 4 LEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDI----THLPMHKRaRLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 84 --YLVQEGVLFPHLTVYRNIAYGL-GNGKGRTAQErQRIEAMLELTGISELAGRYPHELSGGQQQRVALARALAPDPELI 160
Cdd:COG1137 80 igYLPQEASIFRKLTVEDNILAVLeLRKLSKKERE-ERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKFI 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1067578656 161 LLDEPFSALD----EQLRRqiredMIAALRANGKSaVFVS-HDREEALQYADRIAVMKQGRILQTASPHELYRQP 230
Cdd:COG1137 159 LLDEPFAGVDpiavADIQK-----IIRHLKERGIG-VLITdHNVRETLGICDRAYIISEGKVLAEGTPEEILNNP 227
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
5-216 |
1.03e-46 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 156.39 E-value: 1.03e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 5 LHIGHLSKSFQNT--PVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIfsKNTNLPVRERRL 82
Cdd:cd03228 1 IEFKNVSFSYPGRpkPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDL--RDLDLESLRKNI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 83 GYLVQEGVLFpHLTVYRNIayglgngkgrtaqerqrieamleltgiselagrypheLSGGQQQRVALARALAPDPELILL 162
Cdd:cd03228 79 AYVPQDPFLF-SGTIRENI-------------------------------------LSGGQRQRIAIARALLRDPPILIL 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1067578656 163 DEPFSALDEQLRRQIREDMIAALRanGKSAVFVSHdREEALQYADRIAVMKQGR 216
Cdd:cd03228 121 DEATSALDPETEALILEALRALAK--GKTVIVIAH-RLSTIRDADRIIVLDDGR 171
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
2-221 |
1.35e-46 |
|
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: 157.98 E-value: 1.35e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 2 TAALHIGHLSKSFQNT----PVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIFSKNTN--L 75
Cdd:COG4181 6 APIIELRGLTKTVGTGagelTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDarA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 76 PVRERRLGYLVQEGVLFPHLTVYRNIAYGL---GNgkgrtAQERQRIEAMLELTGISELAGRYPHELSGGQQQRVALARA 152
Cdd:COG4181 86 RLRARHVGFVFQSFQLLPTLTALENVMLPLelaGR-----RDARARARALLERVGLGHRLDHYPAQLSGGEQQRVALARA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1067578656 153 LAPDPELILLDEPFSALDEQLRRQIREDMIAALRANGKSAVFVSHDREEALQyADRIAVMKQGRILQTA 221
Cdd:COG4181 161 FATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAAR-CDRVLRLRAGRLVEDT 228
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
17-226 |
1.66e-46 |
|
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: 157.60 E-value: 1.66e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 17 TPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIfsknTNLPVRER-RLGY-LVQEG-VLFP 93
Cdd:cd03224 13 SQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDI----TGLPPHERaRAGIgYVPEGrRIFP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 94 HLTVYRNIAYGLGNGKGRTAQErqRIEAMLEL-TGISELAGRYPHELSGGQQQRVALARALAPDPELILLDEPFSALDEQ 172
Cdd:cd03224 89 ELTVEENLLLGAYARRRAKRKA--RLERVYELfPRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLAPK 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1067578656 173 LRRQIrEDMIAALRANGKSAVFVSHDREEALQYADRIAVMKQGRILQTASPHEL 226
Cdd:cd03224 167 IVEEI-FEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAEL 219
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-232 |
2.84e-46 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 157.89 E-value: 2.84e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 1 MTAALHIGHLSKSFQNTPVLNDISLSLDPGEILFIIGASGCGKTTLLRCL-------AGFEQpdSGEISLSGKTIFSKNT 73
Cdd:COG1117 8 LEPKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLnrmndliPGARV--EGEILLDGEDIYDPDV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 74 NLP-VReRRLGYLVQEGVLFPHlTVYRNIAYGLG-NGKGRTAQERQRIEAMLELTGI-SELAGR---YPHELSGGQQQRV 147
Cdd:COG1117 86 DVVeLR-RRVGMVFQKPNPFPK-SIYDNVAYGLRlHGIKSKSELDEIVEESLRKAALwDEVKDRlkkSALGLSGGQQQRL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 148 ALARALAPDPELILLDEPFSALDEQLRRQIrEDMIAALRANgKSAVFVSHDREEALQYADRIAVMKQGRILQTASPHELY 227
Cdd:COG1117 164 CIARALAVEPEVLLMDEPTSALDPISTAKI-EELILELKKD-YTIVIVTHNMQQAARVSDYTAFFYLGELVEFGPTEQIF 241
|
....*
gi 1067578656 228 RQPAD 232
Cdd:COG1117 242 TNPKD 246
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
7-226 |
3.34e-46 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 157.55 E-value: 3.34e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 7 IGHLSKSFQNTPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIfsKNTNLPVRERRLGYLV 86
Cdd:COG4604 4 IKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDV--ATTPSRELAKRLAILR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 87 QEGVLFPHLTVYRNIAYG-LGNGKGR-TAQERQRIEAMLELTGISELAGRYPHELSGGQQQRVALARALAPDPELILLDE 164
Cdd:COG4604 82 QENHINSRLTVRELVAFGrFPYSKGRlTAEDREIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQDTDYVLLDE 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1067578656 165 PFSALDEQLRRQiredMIAALR--AN--GKSAVFVSHDREEALQYADRIAVMKQGRILQTASPHEL 226
Cdd:COG4604 162 PLNNLDMKHSVQ----MMKLLRrlADelGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEI 223
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
16-235 |
3.40e-46 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 159.03 E-value: 3.40e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 16 NTP----VLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIFS--KNTNLPVRERRLGYLVQ-- 87
Cdd:PRK13634 15 KTPferrALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAgkKNKKLKPLRKKVGIVFQfp 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 88 EGVLFPHlTVYRNIAYGLGNGKGRTAQERQRIEAMLELTGISE-LAGRYPHELSGGQQQRVALARALAPDPELILLDEPF 166
Cdd:PRK13634 95 EHQLFEE-TVEKDICFGPMNFGVSEEDAKQKAREMIELVGLPEeLLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPT 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 167 SALDEQLRRQIREdMIAAL-RANGKSAVFVSHDREEALQYADRIAVMKQGRILQTASPHELYRQPADLDA 235
Cdd:PRK13634 174 AGLDPKGRKEMME-MFYKLhKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADPDELEA 242
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
9-216 |
3.47e-46 |
|
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC transporter ATP-binding protein family. This protein, and its permease partner FtsX, localize to the division site. In a number of species, the ftsEX gene pair is located next to FtsY, the signal recognition particle-docking protein. [Cellular processes, Cell division]
Pssm-ID: 131721 [Multi-domain] Cd Length: 214 Bit Score: 156.64 E-value: 3.47e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 9 HLSKSFQ-NTPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIFS-KNTNLPVRERRLGYLV 86
Cdd:TIGR02673 6 NVSKAYPgGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRlRGRQLPLLRRRIGVVF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 87 QEGVLFPHLTVYRNIAYGLgNGKGRTAQE-RQRIEAMLELTGISELAGRYPHELSGGQQQRVALARALAPDPELILLDEP 165
Cdd:TIGR02673 86 QDFRLLPDRTVYENVALPL-EVRGKKEREiQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPPLLLADEP 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1067578656 166 FSALDEQLRRQIReDMIAALRANGKSAVFVSHDREEALQYADRIAVMKQGR 216
Cdd:TIGR02673 165 TGNLDPDLSERIL-DLLKRLNKRGTTVIVATHDLSLVDRVAHRVIILDDGR 214
|
|
| ABC_ATP_DarD |
NF038007 |
darobactin export ABC transporter ATP-binding protein; |
9-217 |
1.09e-45 |
|
darobactin export ABC transporter ATP-binding protein;
Pssm-ID: 411600 [Multi-domain] Cd Length: 218 Bit Score: 155.26 E-value: 1.09e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 9 HLSKSFQnTPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTI--FSKNTNLPVRERRLGYLV 86
Cdd:NF038007 11 YITKTIK-TKVLNHLNFSVEKGDFVSIMGPSGSGKSTLLNIIGMFDSLDSGSLTLAGKEVtnLSYSQKIILRRELIGYIF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 87 QEGVLFPHLTVYRNIAYGLgngKGRTAQERQRIEAM---LELTGISELAGRYPHELSGGQQQRVALARALAPDPELILLD 163
Cdd:NF038007 90 QSFNLIPHLSIFDNVALPL---KYRGVAKKERIERVnqvLNLFGIDNRRNHKPMQLSGGQQQRVAIARAMVSNPALLLAD 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1067578656 164 EPFSALDEQLRRQIREDMiAALRANGKSAVFVSHDrEEALQYADRIAVMKQGRI 217
Cdd:NF038007 167 EPTGNLDSKNARAVLQQL-KYINQKGTTIIMVTHS-DEASTYGNRIINMKDGKL 218
|
|
| 3a0107s01c2 |
TIGR00972 |
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein ... |
4-232 |
2.64e-45 |
|
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: 155.15 E-value: 2.64e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 4 ALHIGHLSKSFQNTPVLNDISLSLDPGEILFIIGASGCGKTTLLRCL-----AGFEQPDSGEISLSGKTIFSKNTNLPVR 78
Cdd:TIGR00972 1 AIEIENLNLFYGEKEALKNINLDIPKNQVTALIGPSGCGKSTLLRSLnrmndLVPGVRIEGKVLFDGQDIYDKKIDVVEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 79 ERRLGYLVQEGVLFPhLTVYRNIAYGL-GNGKGRTAQERQRIEAMLELTGI-SELAGR---YPHELSGGQQQRVALARAL 153
Cdd:TIGR00972 81 RRRVGMVFQKPNPFP-MSIYDNIAYGPrLHGIKDKKELDEIVEESLKKAALwDEVKDRlhdSALGLSGGQQQRLCIARAL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1067578656 154 APDPELILLDEPFSALDEQLRRQIrEDMIAALRANgKSAVFVSHDREEALQYADRIAVMKQGRILQTASPHELYRQPAD 232
Cdd:TIGR00972 160 AVEPEVLLLDEPTSALDPIATGKI-EELIQELKKK-YTIVIVTHNMQQAARISDRTAFFYDGELVEYGPTEQIFTNPKE 236
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
20-230 |
4.54e-45 |
|
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: 161.78 E-value: 4.54e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 20 LNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFeQPDSGEISLSGKTI--FSKNTNLPVReRRLGYLVQE--GVLFPHL 95
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTLGLALLRL-IPSEGEIRFDGQDLdgLSRRALRPLR-RRMQVVFQDpfGSLSPRM 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 96 TVYRNIAYGLG-NGKGRTAQER-QRIEAMLELTGIS-ELAGRYPHELSGGQQQRVALARALAPDPELILLDEPFSALDEQ 172
Cdd:COG4172 380 TVGQIIAEGLRvHGPGLSAAERrARVAEALEEVGLDpAARHRYPHEFSGGQRQRIAIARALILEPKLLVLDEPTSALDVS 459
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1067578656 173 LRRQIReDMIAAL-RANGKSAVFVSHDRE--EALqyADRIAVMKQGRILQTASPHELYRQP 230
Cdd:COG4172 460 VQAQIL-DLLRDLqREHGLAYLFISHDLAvvRAL--AHRVMVMKDGKVVEQGPTEQVFDAP 517
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
4-230 |
5.07e-45 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 154.40 E-value: 5.07e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 4 ALHIGHLSKSFQNTPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTI-FSKNTNLP-VRE-- 79
Cdd:COG4161 2 SIQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFdFSQKPSEKaIRLlr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 80 RRLGYLVQEGVLFPHLTVYRNIAYG----LGNGKgrtAQERQRIEAMLELTGISELAGRYPHELSGGQQQRVALARALAP 155
Cdd:COG4161 82 QKVGMVFQQYNLWPHLTVMENLIEApckvLGLSK---EQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMM 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1067578656 156 DPELILLDEPFSALDEQLRRQIREdMIAALRANGKSAVFVSHDREEALQYADRIAVMKQGRILQTASpHELYRQP 230
Cdd:COG4161 159 EPQVLLFDEPTAALDPEITAQVVE-IIRELSQTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQGD-ASHFTQP 231
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
9-277 |
1.43e-44 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 156.11 E-value: 1.43e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 9 HLSKSFQ----NTPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIfsknTNLPVRE----R 80
Cdd:PRK11153 6 NISKVFPqggrTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDL----TALSEKElrkaR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 81 RlgylvQEGVLFPHL------TVYRNIAYGLGNGKGRTAQERQRIEAMLELTGISELAGRYPHELSGGQQQRVALARALA 154
Cdd:PRK11153 82 R-----QIGMIFQHFnllssrTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 155 PDPELILLDEPFSALDEQLRRQIReDMIAAL-RANGKSAVFVSHDREEALQYADRIAVMKQGRILQTASPHELYRQPADL 233
Cdd:PRK11153 157 SNPKVLLCDEATSALDPATTRSIL-ELLKDInRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHPKHP 235
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1067578656 234 DAALFIGEGIvfpaalnADGTADCRLGRLPVQsgaPAGTRGTLL 277
Cdd:PRK11153 236 LTREFIQSTL-------HLDLPEDYLARLQAE---PTTGSGPLL 269
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
15-229 |
1.65e-44 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 160.69 E-value: 1.65e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 15 QNTPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIfsKNTNLPVRERRLGYLVQEGVLFpH 94
Cdd:COG4988 348 GGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDL--SDLDPASWRRQIAWVPQNPYLF-A 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 95 LTVYRNIAyglgngKGRTAQERQRIEAMLELTGISELAGRYPHE-----------LSGGQQQRVALARALAPDPELILLD 163
Cdd:COG4988 425 GTIRENLR------LGRPDASDEELEAALEAAGLDEFVAALPDGldtplgeggrgLSGGQAQRLALARALLRDAPLLLLD 498
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1067578656 164 EPFSALDEQLRRQIredmIAALR--ANGKSAVFVSHdREEALQYADRIAVMKQGRILQTASPHELYRQ 229
Cdd:COG4988 499 EPTAHLDAETEAEI----LQALRrlAKGRTVILITH-RLALLAQADRILVLDDGRIVEQGTHEELLAK 561
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
18-237 |
2.16e-44 |
|
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: 152.44 E-value: 2.16e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 18 PVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIfsknTNLPVRER-RLGY-LVQEG-VLFPH 94
Cdd:COG0410 17 HVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDI----TGLPPHRIaRLGIgYVPEGrRIFPS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 95 LTVYRNIAYGLGNGKGRtAQERQRIEAMLEL-----TGISELAGRypheLSGGQQQRVALARALAPDPELILLDEPFSAL 169
Cdd:COG0410 93 LTVEENLLLGAYARRDR-AEVRADLERVYELfprlkERRRQRAGT----LSGGEQQMLAIGRALMSRPKLLLLDEPSLGL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1067578656 170 DEQLRRQIrEDMIAALRANGKSAVFVSHDREEALQYADRIAVMKQGRILQTASPHELYRQPADLDAAL 237
Cdd:COG0410 168 APLIVEEI-FEIIRRLNREGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLADPEVREAYL 234
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
9-233 |
2.89e-44 |
|
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: 152.97 E-value: 2.89e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 9 HLSKSFQNT--PVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIFSKNTNLPVReRRLGYLV 86
Cdd:TIGR04520 5 NVSFSYPESekPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLDEENLWEIR-KKVGMVF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 87 QEgvlfPH-----LTVYRNIAYGLGNgKGRTAQE-RQRIEAMLELTGISELAGRYPHELSGGQQQRVALARALAPDPELI 160
Cdd:TIGR04520 84 QN----PDnqfvgATVEDDVAFGLEN-LGVPREEmRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLAMRPDII 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1067578656 161 LLDEPFSALDEQLRRQIREDMIAALRANGKSAVFVSHDREEALQyADRIAVMKQGRILQTASPHELYRQPADL 233
Cdd:TIGR04520 159 ILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEAVL-ADRVIVMNKGKIVAEGTPREIFSQVELL 230
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
22-217 |
3.29e-44 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 155.42 E-value: 3.29e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 22 DISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIF--SKNTNLPVRERRLGYLVQEGVLFPHLTVYR 99
Cdd:PRK11144 16 TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFdaEKGICLPPEKRRIGYVFQDARLFPHYKVRG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 100 NIAYGLgngkgrTAQERQRIEAMLELTGISELAGRYPHELSGGQQQRVALARALAPDPELILLDEPFSALD--------- 170
Cdd:PRK11144 96 NLRYGM------AKSMVAQFDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDlprkrellp 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1067578656 171 --EQLRRQIREDMIaalrangksavFVSHDREEALQYADRIAVMKQGRI 217
Cdd:PRK11144 170 ylERLAREINIPIL-----------YVSHSLDEILRLADRVVVLEQGKV 207
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
4-220 |
8.49e-44 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 151.32 E-value: 8.49e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 4 ALHIGHLSKSFQNTPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTI-FSKNTNLP-VRE-- 79
Cdd:PRK11124 2 SIQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFdFSKTPSDKaIRElr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 80 RRLGYLVQEGVLFPHLTVYRNIAYG----LGNGKgrtAQERQRIEAMLELTGISELAGRYPHELSGGQQQRVALARALAP 155
Cdd:PRK11124 82 RNVGMVFQQYNLWPHLTVQQNLIEApcrvLGLSK---DQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMM 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1067578656 156 DPELILLDEPFSALDEQLRRQIrEDMIAALRANGKSAVFVSHDREEALQYADRIAVMKQGRILQT 220
Cdd:PRK11124 159 EPQVLLFDEPTAALDPEITAQI-VSIIRELAETGITQVIVTHEVEVARKTASRVVYMENGHIVEQ 222
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
16-229 |
1.55e-43 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 158.02 E-value: 1.55e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 16 NTPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIfsknTNLPVRE--RRLGYLVQEGVLFp 93
Cdd:COG1132 352 DRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDI----RDLTLESlrRQIGVVPQDTFLF- 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 94 HLTVYRNIAYglgngkGRTAQERQRIEAMLELTGISELAGRYPH-----------ELSGGQQQRVALARALAPDPELILL 162
Cdd:COG1132 427 SGTIRENIRY------GRPDATDEEVEEAAKAAQAHEFIEALPDgydtvvgergvNLSGGQRQRIAIARALLKDPPILIL 500
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1067578656 163 DEPFSALDEQLRRQIREdMIAALRAnGKSAVFVSHdREEALQYADRIAVMKQGRILQTASPHELYRQ 229
Cdd:COG1132 501 DEATSALDTETEALIQE-ALERLMK-GRTTIVIAH-RLSTIRNADRILVLDDGRIVEQGTHEELLAR 564
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
6-217 |
1.67e-43 |
|
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: 149.33 E-value: 1.67e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 6 HIGHLSKSF-QNTPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIFSKntnlpVRERRLGY 84
Cdd:cd03226 1 RIENISFSYkKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAK-----ERRKSIGY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 85 LVQE--GVLFPHlTVYRNIAYGLGNgkgrTAQERQRIEAMLELTGISELAGRYPHELSGGQQQRVALARALAPDPELILL 162
Cdd:cd03226 76 VMQDvdYQLFTD-SVREELLLGLKE----LDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIF 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1067578656 163 DEPFSALD----EQLRRQIREdmiaaLRANGKSAVFVSHDREEALQYADRIAVMKQGRI 217
Cdd:cd03226 151 DEPTSGLDyknmERVGELIRE-----LAAQGKAVIVITHDYEFLAKVCDRVLLLANGAI 204
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
9-217 |
3.78e-43 |
|
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: 146.80 E-value: 3.78e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 9 HLSKSFQNTPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIFSKNtnlPVRERRLG-YLVq 87
Cdd:cd03216 5 GITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFAS---PRDARRAGiAMV- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 88 egvlfphltvyrniayglgngkgrtaqerqrieamleltgiselagrypHELSGGQQQRVALARALAPDPELILLDEPFS 167
Cdd:cd03216 81 -------------------------------------------------YQLSVGERQMVEIARALARNARLLILDEPTA 111
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1067578656 168 ALDEQLRRQIREdMIAALRANGKSAVFVSHDREEALQYADRIAVMKQGRI 217
Cdd:cd03216 112 ALTPAEVERLFK-VIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRV 160
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
20-232 |
4.55e-43 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 153.65 E-value: 4.55e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 20 LNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTI--FSKNTNLPVRERRLGYLVQEGVLFPHLTV 97
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIakISDAELREVRRKKIAMVFQSFALMPHMTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 98 YRNIAYGLGNGKGRTAQERQRIEAMLELTGISELAGRYPHELSGGQQQRVALARALAPDPELILLDEPFSALDEQLRRQI 177
Cdd:PRK10070 124 LDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEM 203
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1067578656 178 REDMIAALRANGKSAVFVSHDREEALQYADRIAVMKQGRILQTASPHELYRQPAD 232
Cdd:PRK10070 204 QDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPAN 258
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-248 |
7.37e-43 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 155.18 E-value: 7.37e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 1 MTAALHIGHLSKSFQNTPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIFSKNtnlPVRER 80
Cdd:COG3845 2 MPPALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRS---PRDAI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 81 RLG-YLV-QEGVLFPHLTVYRNIAYGLGNGKG---RTAQERQRIEamleltgisELAGRYP---------HELSGGQQQR 146
Cdd:COG3845 79 ALGiGMVhQHFMLVPNLTVAENIVLGLEPTKGgrlDRKAARARIR---------ELSERYGldvdpdakvEDLSVGEQQR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 147 VALARALAPDPELILLDEPFSALDEQlrrQIRE--DMIAALRANGKSAVFVSHDREEALQYADRIAVMKQGRILQTASPH 224
Cdd:COG3845 150 VEILKALYRGARILILDEPTAVLTPQ---EADElfEILRRLAAEGKSIIFITHKLREVMAIADRVTVLRRGKVVGTVDTA 226
|
250 260
....*....|....*....|....
gi 1067578656 225 ELyrQPADLdAALFIGEGIVFPAA 248
Cdd:COG3845 227 ET--SEEEL-AELMVGREVLLRVE 247
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
5-218 |
7.39e-43 |
|
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: 147.75 E-value: 7.39e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 5 LHIGHLSKSFQNTPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKtIFSKNTNLPvreRRLGY 84
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGK-SYQKNIEAL---RRIGA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 85 LVQEGVLFPHLTVYRNIAYgLGNGKGRtaqERQRIEAMLELTGISELAGRYPHELSGGQQQRVALARALAPDPELILLDE 164
Cdd:cd03268 77 LIEAPGFYPNLTARENLRL-LARLLGI---RKKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDE 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1067578656 165 PFSALDEQLRRQIREdMIAALRANGKSAVFVSHDREEALQYADRIAVMKQGRIL 218
Cdd:cd03268 153 PTNGLDPDGIKELRE-LILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKLI 205
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
15-217 |
1.02e-42 |
|
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: 147.74 E-value: 1.02e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 15 QNTPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIfsKNTNLPVRERRLGYLVQEGVLFpH 94
Cdd:cd03245 15 QEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDI--RQLDPADLRRNIGYVPQDVTLF-Y 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 95 LTVYRNIAYGLGNGkgrtaqERQRIEAMLELTGISELAGRYPH-----------ELSGGQQQRVALARALAPDPELILLD 163
Cdd:cd03245 92 GTLRDNITLGAPLA------DDERILRAAELAGVTDFVNKHPNgldlqigergrGLSGGQRQAVALARALLNDPPILLLD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1067578656 164 EPFSALDEQLRRQIREDMIAALRanGKSAVFVSHdREEALQYADRIAVMKQGRI 217
Cdd:cd03245 166 EPTSAMDMNSEERLKERLRQLLG--DKTLIIITH-RPSLLDLVDRIIVMDSGRI 216
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-231 |
3.78e-42 |
|
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: 153.69 E-value: 3.78e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 1 MTAALHIGHLSKSFQN----TPVLNDISLSLDPGEILFIIGASGCGKT----TLLRCLAGFEQPDSGEISLSGKTIFSkn 72
Cdd:COG4172 3 SMPLLSVEDLSVAFGQgggtVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLG-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 73 tnLP------VRERRLGYLVQEGV--LFPHLTVYRNIAYGLGNGKGRTAQE-RQRIEAMLELTGISELAGR---YPHELS 140
Cdd:COG4172 81 --LSerelrrIRGNRIAMIFQEPMtsLNPLHTIGKQIAEVLRLHRGLSGAAaRARALELLERVGIPDPERRldaYPHQLS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 141 GGQQQRVALARALAPDPELILLDEPFSALDEQLRRQIReDMIAALRA-NGKSAVFVSHD----ReealQYADRIAVMKQG 215
Cdd:COG4172 159 GGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQIL-DLLKDLQReLGMALLLITHDlgvvR----RFADRVAVMRQG 233
|
250
....*....|....*.
gi 1067578656 216 RILQTASPHELYRQPA 231
Cdd:COG4172 234 EIVEQGPTAELFAAPQ 249
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
15-231 |
6.62e-42 |
|
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: 153.38 E-value: 6.62e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 15 QNTPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIfsKNTNLPVRERRLGYLVQEGVLFpH 94
Cdd:COG4987 346 AGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDL--RDLDEDDLRRRIAVVPQRPHLF-D 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 95 LTVYRNIAygLGNGkgrTAQERQrIEAMLELTGISELAGRYPH-----------ELSGGQQQRVALARALAPDPELILLD 163
Cdd:COG4987 423 TTLRENLR--LARP---DATDEE-LWAALERVGLGDWLAALPDgldtwlgeggrRLSGGERRRLALARALLRDAPILLLD 496
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1067578656 164 EPFSALDEQLRRQIREDMIAALRanGKSAVFVSHdREEALQYADRIAVMKQGRILQTASPHELYRQPA 231
Cdd:COG4987 497 EPTEGLDAATEQALLADLLEALA--GRTVLLITH-RLAGLERMDRILVLEDGRIVEQGTHEELLAQNG 561
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
5-217 |
1.02e-41 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 146.36 E-value: 1.02e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 5 LHIGHLSKSFQNTPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEIsLSGKTIFSKntnlpVRER-RLg 83
Cdd:PRK11247 13 LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL-LAGTAPLAE-----AREDtRL- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 84 yLVQEGVLFPHLTVYRNIAYGLGnGKGRTAQERQrieamLELTGISELAGRYPHELSGGQQQRVALARALAPDPELILLD 163
Cdd:PRK11247 86 -MFQDARLLPWKKVIDNVGLGLK-GQWRDAALQA-----LAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLD 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1067578656 164 EPFSALDeQLRRQIREDMIAAL-RANGKSAVFVSHDREEALQYADRIAVMKQGRI 217
Cdd:PRK11247 159 EPLGALD-ALTRIEMQDLIESLwQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
5-230 |
1.41e-41 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 145.88 E-value: 1.41e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 5 LHIGHLSKSFQNTPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTI------------FSKN 72
Cdd:PRK10619 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTInlvrdkdgqlkvADKN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 73 tNLPVRERRLGYLVQEGVLFPHLTVYRNIAYGLGNGKGRTAQE-RQRIEAMLELTGISELA-GRYPHELSGGQQQRVALA 150
Cdd:PRK10619 86 -QLRLLRTRLTMVFQHFNLWSHMTVLENVMEAPIQVLGLSKQEaRERAVKYLAKVGIDERAqGKYPVHLSGGQQQRVSIA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 151 RALAPDPELILLDEPFSALDEQLRRQIREDMiAALRANGKSAVFVSHDREEALQYADRIAVMKQGRILQTASPHELYRQP 230
Cdd:PRK10619 165 RALAMEPEVLLFDEPTSALDPELVGEVLRIM-QQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGNP 243
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
5-219 |
1.54e-41 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 144.26 E-value: 1.54e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 5 LHIGHLSKSFQNTPVLNDISLSLDPGeILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIFSKNTNLpvrERRLGY 84
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKL---RRRIGY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 85 LVQEGVLFPHLTVYRNIAYgLGNGKG-RTAQERQRIEAMLELTGISELAGRYPHELSGGQQQRVALARALAPDPELILLD 163
Cdd:cd03264 77 LPQEFGVYPNFTVREFLDY-IAWLKGiPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1067578656 164 EPFSALDEQLRRQIREdMIAALRANgKSAVFVSHDREEALQYADRIAVMKQGRILQ 219
Cdd:cd03264 156 EPTAGLDPEERIRFRN-LLSELGED-RIVILSTHIVEDVESLCNQVAVLNKGKLVF 209
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
15-217 |
2.84e-41 |
|
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: 151.82 E-value: 2.84e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 15 QNTPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIFSKNtnlpvRE---RRLGYLVQEGVL 91
Cdd:COG4618 343 SKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWD-----REelgRHIGYLPQDVEL 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 92 FPHlTVYRNIAyglgngkgRTAQ-ERQRIEAMLELTGISELAGRYP-----------HELSGGQQQRVALARALAPDPEL 159
Cdd:COG4618 418 FDG-TIAENIA--------RFGDaDPEKVVAAAKLAGVHEMILRLPdgydtrigeggARLSGGQRQRIGLARALYGDPRL 488
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1067578656 160 ILLDEPFSALDEQLRRQIREdMIAALRANGKSAVFVSHdREEALQYADRIAVMKQGRI 217
Cdd:COG4618 489 VVLDEPNSNLDDEGEAALAA-AIRALKARGATVVVITH-RPSLLAAVDKLLVLRDGRV 544
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
9-226 |
2.87e-41 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 144.05 E-value: 2.87e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 9 HLSKSFQNTPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIFSKNTNlpVReRRLGYLVQE 88
Cdd:cd03265 5 NLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPRE--VR-RRIGIVFQD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 89 GVLFPHLTVYRNIA-----YGLGNgkgrtAQERQRIEAMLELTGISELAGRYPHELSGGQQQRVALARALAPDPELILLD 163
Cdd:cd03265 82 LSVDDELTGWENLYiharlYGVPG-----AERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLD 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1067578656 164 EPFSALDEQLRRQIREDMIAALRANGKSAVFVSHDREEALQYADRIAVMKQGRILQTASPHEL 226
Cdd:cd03265 157 EPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
5-231 |
3.80e-41 |
|
nickel import ATP-binding protein NikE; This family represents the NikE 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. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 144.95 E-value: 3.80e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 5 LHIGHLSKSF---------QNTPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIFSKNTNL 75
Cdd:TIGR02769 3 LEVRDVTHTYrtgglfgakQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 76 PVRERRLGYLVQE---GVLFPHLTVYRNIAYGLGNGKGRTAQERQ-RIEAMLELTGI-SELAGRYPHELSGGQQQRVALA 150
Cdd:TIGR02769 83 RRAFRRDVQLVFQdspSAVNPRMTVRQIIGEPLRHLTSLDESEQKaRIAELLDMVGLrSEDADKLPRQLSGGQLQRINIA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 151 RALAPDPELILLDEPFSALDEQLRRQIREDMIAALRANGKSAVFVSHDREEALQYADRIAVMKQGRILQTASPHEL--YR 228
Cdd:TIGR02769 163 RALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIVEECDVAQLlsFK 242
|
...
gi 1067578656 229 QPA 231
Cdd:TIGR02769 243 HPA 245
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
16-217 |
6.19e-41 |
|
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: 141.58 E-value: 6.19e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 16 NTPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIFSKNTNLpvRERRLGYLVQEGVLFPHl 95
Cdd:cd03246 14 EPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNE--LGDHVGYLPQDDELFSG- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 96 TVYRNIayglgngkgrtaqerqrieamleltgiselagrypheLSGGQQQRVALARALAPDPELILLDEPFSALDEQLRR 175
Cdd:cd03246 91 SIAENI-------------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGER 133
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1067578656 176 QIrEDMIAALRANGKSAVFVSHdREEALQYADRIAVMKQGRI 217
Cdd:cd03246 134 AL-NQAIAALKAAGATRIVIAH-RPETLASADRILVLEDGRV 173
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
16-217 |
7.51e-41 |
|
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: 142.55 E-value: 7.51e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 16 NTPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIFS-KNTNLPVRERRLGYLVQEGVLFPH 94
Cdd:cd03292 13 GTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDlRGRAIPYLRRKIGVVFQDFRLLPD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 95 LTVYRNIAYGL--GNGKGRTAQERqrIEAMLELTGISELAGRYPHELSGGQQQRVALARALAPDPELILLDEPFSALDEQ 172
Cdd:cd03292 93 RNVYENVAFALevTGVPPREIRKR--VPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPD 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1067578656 173 LRRQIReDMIAALRANGKSAVFVSHDREEALQYADRIAVMKQGRI 217
Cdd:cd03292 171 TTWEIM-NLLKKINKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
5-251 |
7.75e-41 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 144.39 E-value: 7.75e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 5 LHIGHLSKSFQNT--PVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIfSKNTNLPVReRRL 82
Cdd:PRK13635 6 IRVEHISFRYPDAatYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVL-SEETVWDVR-RQV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 83 GYLVQE-GVLFPHLTVYRNIAYGLGN-GKGRTaQERQRIEAMLELTGISELAGRYPHELSGGQQQRVALARALAPDPELI 160
Cdd:PRK13635 84 GMVFQNpDNQFVGATVQDDVAFGLENiGVPRE-EMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDII 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 161 LLDEPFSALDEQLRRQIREdMIAALRANGKSAVF-VSHDREEALQyADRIAVMKQGRILQTASPHELYRQPADLDAalfI 239
Cdd:PRK13635 163 ILDEATSMLDPRGRREVLE-TVRQLKEQKGITVLsITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEIFKSGHMLQE---I 237
|
250
....*....|..
gi 1067578656 240 GEGIVFPAALNA 251
Cdd:PRK13635 238 GLDVPFSVKLKE 249
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
1-230 |
2.04e-40 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 143.05 E-value: 2.04e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 1 MTAALHIGHLSKSF---------QNTPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIFSK 71
Cdd:COG4167 1 MSALLEVRNLSKTFkyrtglfrrQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 72 NTnlPVRERRLGYLVQ--EGVLFPHLTVYRNIAYGLGNGKGRTAQER-QRIEAMLELTGIS-ELAGRYPHELSGGQQQRV 147
Cdd:COG4167 81 DY--KYRCKHIRMIFQdpNTSLNPRLNIGQILEEPLRLNTDLTAEEReERIFATLRLVGLLpEHANFYPHMLSSGQKQRV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 148 ALARALAPDPELILLDEPFSALDEQLRRQIREDMIAALRANGKSAVFVSHDREEALQYADRIAVMKQGRILQTASPHELY 227
Cdd:COG4167 159 ALARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKHISDKVLVMHQGEVVEYGKTAEVF 238
|
...
gi 1067578656 228 RQP 230
Cdd:COG4167 239 ANP 241
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
5-218 |
3.74e-40 |
|
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: 140.97 E-value: 3.74e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 5 LHIGHLSKSFQNTP----VLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGktiFSKNTNLPVRER 80
Cdd:cd03266 2 ITADALTKRFRDVKktvqAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDG---FDVVKEPAEARR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 81 RLGYLVQEGVLFPHLTVYRNIAY--GLGNGKGRTAQerQRIEAMLELTGISELAGRYPHELSGGQQQRVALARALAPDPE 158
Cdd:cd03266 79 RLGFVSDSTGLYDRLTARENLEYfaGLYGLKGDELT--ARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 159 LILLDEPFSALDEQLRRQIREdMIAALRANGKSAVFVSHDREEALQYADRIAVMKQGRIL 218
Cdd:cd03266 157 VLLLDEPTTGLDVMATRALRE-FIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVV 215
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
18-226 |
5.81e-40 |
|
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: 140.83 E-value: 5.81e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 18 PVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIfsKNTNLPVRERRLGYLVQEGVLFpHLTV 97
Cdd:cd03253 15 PVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDI--REVTLDSLRRAIGVVPQDTVLF-NDTI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 98 YRNIAYGLGNgkgrtAQERQRIEAMlELTGISELAGRYPH-----------ELSGGQQQRVALARALAPDPELILLDEPF 166
Cdd:cd03253 92 GYNIRYGRPD-----ATDEEVIEAA-KAAQIHDKIMRFPDgydtivgerglKLSGGEKQRVAIARAILKNPPILLLDEAT 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 167 SALDEQLRRQIREDMIAAlrANGKSAVFVSHdREEALQYADRIAVMKQGRILQTASPHEL 226
Cdd:cd03253 166 SALDTHTEREIQAALRDV--SKGRTTIVIAH-RLSTIVNADKIIVLKDGRIVERGTHEEL 222
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
16-229 |
8.97e-40 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 140.37 E-value: 8.97e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 16 NTPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIfsKNTNLPVRERRLGYLVQEGVLFPhL 95
Cdd:cd03249 15 DVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDI--RDLNLRWLRSQIGLVSQEPVLFD-G 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 96 TVYRNIAYGLGNgkgRTAQERQRIEAMLELT--------GISELAGRYPHELSGGQQQRVALARALAPDPELILLDEPFS 167
Cdd:cd03249 92 TIAENIRYGKPD---ATDEEVEEAAKKANIHdfimslpdGYDTLVGERGSQLSGGQKQRIAIARALLRNPKILLLDEATS 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1067578656 168 ALDEQLRRQIREDMIAALRanGKSAVFVSHdREEALQYADRIAVMKQGRILQTASPHELYRQ 229
Cdd:cd03249 169 ALDAESEKLVQEALDRAMK--GRTTIVIAH-RLSTIRNADLIAVLQNGQVVEQGTHDELMAQ 227
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
15-218 |
1.47e-39 |
|
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: 148.48 E-value: 1.47e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 15 QNTPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIfsknTNLPVRERR--LGYLVQEGVLF 92
Cdd:TIGR03375 476 QETPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDI----RQIDPADLRrnIGYVPQDPRLF 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 93 pHLTVYRNIAYGlgngkgRTAQERQRIEAMLELTGISELAGRYPH-----------ELSGGQQQRVALARALAPDPELIL 161
Cdd:TIGR03375 552 -YGTLRDNIALG------APYADDEEILRAAELAGVTEFVRRHPDgldmqigergrSLSGGQRQAVALARALLRDPPILL 624
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1067578656 162 LDEPFSALDEQLRRQIREDMIAALRanGKSAVFVSHdREEALQYADRIAVMKQGRIL 218
Cdd:TIGR03375 625 LDEPTSAMDNRSEERFKDRLKRWLA--GKTLVLVTH-RTSLLDLVDRIIVMDNGRIV 678
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
2-218 |
3.39e-39 |
|
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: 139.45 E-value: 3.39e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 2 TAALHIGHLSKSFQNTPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSG-EISLSGKTIFSKNtnlpVRE- 79
Cdd:COG1119 1 DPLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRGGED----VWEl 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 80 -RRLGYLVQEGVLF--PHLTVYRNIAYGLGNGKGR----TAQERQRIEAMLELTGISELAGRYPHELSGGQQQRVALARA 152
Cdd:COG1119 77 rKRIGLVSPALQLRfpRDETVLDVVLSGFFDSIGLyrepTDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIARA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1067578656 153 LAPDPELILLDEPFSALDEQLRRQIREdMIAALRANGKSA-VFVSHDREEALQYADRIAVMKQGRIL 218
Cdd:COG1119 157 LVKDPELLILDEPTAGLDLGARELLLA-LLDKLAAEGAPTlVLVTHHVEEIPPGITHVLLLKDGRVV 222
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
19-217 |
7.24e-39 |
|
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: 136.41 E-value: 7.24e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 19 VLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIfsknTNLPVRERR---LGYL----VQEGvL 91
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPV----TRRSPRDAIragIAYVpedrKREG-L 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 92 FPHLTVYRNIAyglgngkgrtaqerqrieamleltgISELagrypheLSGGQQQRVALARALAPDPELILLDEPFSALDE 171
Cdd:cd03215 90 VLDLSVAENIA-------------------------LSSL-------LSGGNQQKVVLARWLARDPRVLILDEPTRGVDV 137
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1067578656 172 QLRRQIREdMIAALRANGKSAVFVSHDREEALQYADRIAVMKQGRI 217
Cdd:cd03215 138 GAKAEIYR-LIRELADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
2-226 |
1.93e-38 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 137.81 E-value: 1.93e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 2 TAALHIGHLSKSFQN--TPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIFSKNtnlpVRE 79
Cdd:PRK13632 5 SVMIKVENVSFSYPNseNNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKEN----LKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 80 RR--LGYLVQE-GVLFPHLTVYRNIAYGLGNGKGRTAQERQRIEAMLELTGISELAGRYPHELSGGQQQRVALARALAPD 156
Cdd:PRK13632 81 IRkkIGIIFQNpDNQFIGATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALN 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1067578656 157 PELILLDEPFSALDEQLRRQIREdMIAALRANGKSAVF-VSHDREEALQyADRIAVMKQGRILQTASPHEL 226
Cdd:PRK13632 161 PEIIIFDESTSMLDPKGKREIKK-IMVDLRKTRKKTLIsITHDMDEAIL-ADKVIVFSEGKLIAQGKPKEI 229
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
20-229 |
2.39e-38 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 138.26 E-value: 2.39e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 20 LNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIFSKNTNLPVRERRLGYLVQ--EGVLFPHlTV 97
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKLSDIRKKVGLVFQypEYQLFEE-TI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 98 YRNIAYGLGNgKGRTAQE-RQRIEAMLELTGIS--ELAGRYPHELSGGQQQRVALARALAPDPELILLDEPFSALDEQLR 174
Cdd:PRK13637 102 EKDIAFGPIN-LGLSEEEiENRVKRAMNIVGLDyeDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGR 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1067578656 175 RQIREDMIAALRANGKSAVFVSHDREEALQYADRIAVMKQGRILQTASPHELYRQ 229
Cdd:PRK13637 181 DEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVFKE 235
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
18-212 |
2.54e-38 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 135.05 E-value: 2.54e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 18 PVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKtifskntnlpvreRRLGYLVQEGVL---FPh 94
Cdd:NF040873 6 PVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGG-------------ARVAYVPQRSEVpdsLP- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 95 LTVYRNIAYGLGNGKGR----TAQERQRIEAMLELTGISELAGRYPHELSGGQQQRVALARALAPDPELILLDEPFSALD 170
Cdd:NF040873 72 LTVRDLVAMGRWARRGLwrrlTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLD 151
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1067578656 171 EQLRRQIReDMIAALRANGKSAVFVSHDREEALQyADRIAVM 212
Cdd:NF040873 152 AESRERII-ALLAEEHARGATVVVVTHDLELVRR-ADPCVLL 191
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-234 |
5.26e-38 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 137.17 E-value: 5.26e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 1 MTAALHIGHLS---KSFQNTPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIFSKNtnlpV 77
Cdd:PRK13650 1 MSNIIEVKNLTfkyKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEEN----V 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 78 RERR--LGYLVQE-GVLFPHLTVYRNIAYGLGNgKGRTAQE-RQRIEAMLELTGISELAGRYPHELSGGQQQRVALARAL 153
Cdd:PRK13650 77 WDIRhkIGMVFQNpDNQFVGATVEDDVAFGLEN-KGIPHEEmKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 154 APDPELILLDEPFSALDEQLR-------RQIREDmiaalraNGKSAVFVSHDREE-ALqyADRIAVMKQGRILQTASPHE 225
Cdd:PRK13650 156 AMRPKIIILDEATSMLDPEGRleliktiKGIRDD-------YQMTVISITHDLDEvAL--SDRVLVMKNGQVESTSTPRE 226
|
....*....
gi 1067578656 226 LYRQPADLD 234
Cdd:PRK13650 227 LFSRGNDLL 235
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
15-218 |
5.67e-38 |
|
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: 142.49 E-value: 5.67e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 15 QNTPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIfsKNTNLPVRERRLGYLVQEGVLFPH 94
Cdd:TIGR01842 329 GKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADL--KQWDRETFGKHIGYLPQDVELFPG 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 95 lTVYRNIAYglgngKGRTAQERQRIEAMlELTGISELAGRYPH-----------ELSGGQQQRVALARALAPDPELILLD 163
Cdd:TIGR01842 407 -TVAENIAR-----FGENADPEKIIEAA-KLAGVHELILRLPDgydtvigpggaTLSGGQRQRIALARALYGDPKLVVLD 479
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1067578656 164 EPFSALDEQLRRQIREDMIaALRANGKSAVFVSHdREEALQYADRIAVMKQGRIL 218
Cdd:TIGR01842 480 EPNSNLDEEGEQALANAIK-ALKARGITVVVITH-RPSLLGCVDKILVLQDGRIA 532
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
5-221 |
1.33e-37 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 135.58 E-value: 1.33e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 5 LHIGHLSKSFQNTP---------VLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIFSKNTNL 75
Cdd:PRK10419 4 LNVSGLSHHYAHGGlsgkhqhqtVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 76 PVRERRLGYLV-QE--GVLFPHLTVYRNIAYGLGNGKGRTAQERQ-RIEAMLELTGIS-ELAGRYPHELSGGQQQRVALA 150
Cdd:PRK10419 84 RKAFRRDIQMVfQDsiSAVNPRKTVREIIREPLRHLLSLDKAERLaRASEMLRAVDLDdSVLDKRPPQLSGGQLQRVCLA 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1067578656 151 RALAPDPELILLDEPFSALDEQLRRQIReDMIAALRANGKSA-VFVSHDREEALQYADRIAVMKQGRILQTA 221
Cdd:PRK10419 164 RALAVEPKLLILDEAVSNLDLVLQAGVI-RLLKKLQQQFGTAcLFITHDLRLVERFCQRVMVMDNGQIVETQ 234
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
5-219 |
4.71e-37 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 133.40 E-value: 4.71e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 5 LHIGHLSKSFQN----TPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTI--FSKNTNLPVR 78
Cdd:PRK11629 6 LQCDNLCKRYQEgsvqTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMskLSSAAKAELR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 79 ERRLGYLVQEGVLFPHLTVYRNIAYGLGNGKGRTAQERQRIEAMLELTGISELAGRYPHELSGGQQQRVALARALAPDPE 158
Cdd:PRK11629 86 NQKLGFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPR 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1067578656 159 LILLDEPFSALDEQLRRQIREDMIAALRANGKSAVFVSHDreeaLQYADRIA---VMKQGRILQ 219
Cdd:PRK11629 166 LVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHD----LQLAKRMSrqlEMRDGRLTA 225
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-216 |
1.14e-36 |
|
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: 132.17 E-value: 1.14e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 1 MTAALHIGHLSKSF----QNT---PVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEI------------ 61
Cdd:COG4778 1 MTTLLEVENLSKTFtlhlQGGkrlPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSIlvrhdggwvdla 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 62 SLSGKTIfskntnLPVRERRLGYLVQegvlF----PHLTVYRNIAYGLGNGKGRTAQERQRIEAMLELTGISE-LAGRYP 136
Cdd:COG4778 81 QASPREI------LALRRRTIGYVSQ----FlrviPRVSALDVVAEPLLERGVDREEARARARELLARLNLPErLWDLPP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 137 HELSGGQQQRVALARALAPDPELILLDEPFSALDEQLRRQIREdMIAALRANGKSAVFVSHDREEALQYADRIAVMKQGR 216
Cdd:COG4778 151 ATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVE-LIEEAKARGTAIIGIFHDEEVREAVADRVVDVTPFS 229
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-231 |
2.68e-36 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 131.82 E-value: 2.68e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 1 MTAA-LHIGHLSKSFQNTPVLNDISLSLDPGEILFIIGASGCGKTTLLRCL--AGFEQPD---SGEISLSGKTIFSKNTN 74
Cdd:PRK14239 1 MTEPiLQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDLNPEvtiTGSIVYNGHNIYSPRTD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 75 LPVRERRLGYLVQEGVLFPhLTVYRNIAYGLG-NGkgrtAQERQRIEAMLE--LTGIS---ELAGRYpHE----LSGGQQ 144
Cdd:PRK14239 81 TVDLRKEIGMVFQQPNPFP-MSIYENVVYGLRlKG----IKDKQVLDEAVEksLKGASiwdEVKDRL-HDsalgLSGGQQ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 145 QRVALARALAPDPELILLDEPFSALDEQLRRQIrEDMIAALRaNGKSAVFVSHDREEALQYADRIAVMKQGRILQTASPH 224
Cdd:PRK14239 155 QRVCIARVLATSPKIILLDEPTSALDPISAGKI-EETLLGLK-DDYTMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTK 232
|
....*..
gi 1067578656 225 ELYRQPA 231
Cdd:PRK14239 233 QMFMNPK 239
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1-237 |
3.27e-36 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 138.70 E-value: 3.27e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 1 MTAALHIGHLSKSFQN----TPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIFSKNTNLP 76
Cdd:PRK10535 1 MTALLELKDIRRSYPSgeeqVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 77 VRERR--LGYLVQEGVLFPHLTVYRNI---AYGLGNGKgrtAQERQRIEAMLELTGISELAGRYPHELSGGQQQRVALAR 151
Cdd:PRK10535 81 AQLRRehFGFIFQRYHLLSHLTAAQNVevpAVYAGLER---KQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIAR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 152 ALAPDPELILLDEPFSALDEQLRRQIREdMIAALRANGKSAVFVSHDREEALQyADRIAVMKQGRILQTaSPHELYRQPA 231
Cdd:PRK10535 158 ALMNGGQVILADEPTGALDSHSGEEVMA-ILHQLRDRGHTVIIVTHDPQVAAQ-AERVIEIRDGEIVRN-PPAQEKVNVA 234
|
....*.
gi 1067578656 232 DLDAAL 237
Cdd:PRK10535 235 GGTEPV 240
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
5-220 |
7.57e-36 |
|
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: 129.95 E-value: 7.57e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 5 LHIGHLSKSFQNTPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIFSKNTNLPVReRRLGY 84
Cdd:TIGR03410 1 LEVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERAR-AGIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 85 LVQEGVLFPHLTVYRNIAYGLGNGKGRtaqERQRIEAMLELTGI-SELAGRYPHELSGGQQQRVALARALAPDPELILLD 163
Cdd:TIGR03410 80 VPQGREIFPRLTVEENLLTGLAALPRR---SRKIPDEIYELFPVlKEMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLD 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1067578656 164 EPFSALDEQLRRQIrEDMIAALRANGKSAVFVS-HDREEALQYADRIAVMKQGRILQT 220
Cdd:TIGR03410 157 EPTEGIQPSIIKDI-GRVIRRLRAEGGMAILLVeQYLDFARELADRYYVMERGRVVAS 213
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
18-217 |
1.04e-35 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 135.53 E-value: 1.04e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 18 PVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIFSKNTNLPVReRRLGYL----VQEGvLFP 93
Cdd:COG1129 266 GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDAIR-AGIAYVpedrKGEG-LVL 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 94 HLTVYRNIAygLGN----GKG---RTAQERQRIEAMLELTGIselagRYPH------ELSGGQQQRVALARALAPDPELI 160
Cdd:COG1129 344 DLSIRENIT--LASldrlSRGgllDRRRERALAEEYIKRLRI-----KTPSpeqpvgNLSGGNQQKVVLAKWLATDPKVL 416
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1067578656 161 LLDEPFSALDEQLRRQIREdMIAALRANGKSAVFVSHDREEALQYADRIAVMKQGRI 217
Cdd:COG1129 417 ILDEPTRGIDVGAKAEIYR-LIRELAAEGKAVIVISSELPELLGLSDRILVMREGRI 472
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
20-230 |
1.49e-35 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 132.01 E-value: 1.49e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 20 LNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIFSKNtnlPVRERRLGYLVQ------EGVLFP 93
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKAD---PEAQKLLRQKIQivfqnpYGSLNP 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 94 HLTVYRNIAYGLG-NGKGRTAQERQRIEAMLELTGI-SELAGRYPHELSGGQQQRVALARALAPDPELILLDEPFSALDE 171
Cdd:PRK11308 108 RKKVGQILEEPLLiNTSLSAAERREKALAMMAKVGLrPEHYDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALDV 187
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1067578656 172 QLRRQIREDMIAALRANGKSAVFVSHDREEALQYADRIAVMKQGRILQTASPHELYRQP 230
Cdd:PRK11308 188 SVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFNNP 246
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-226 |
1.71e-35 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 131.08 E-value: 1.71e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 1 MTAALHIGHLSKSFQNTPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIFSKNtnlPVRER 80
Cdd:PRK13537 4 SVAPIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRA---RHARQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 81 RLGYLVQEGVLFPHLTVYRNIA-----YGLGngkgrTAQERQRIEAMLELTGISELAGRYPHELSGGQQQRVALARALAP 155
Cdd:PRK13537 81 RVGVVPQFDNLDPDFTVRENLLvfgryFGLS-----AAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVN 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1067578656 156 DPELILLDEPFSALDEQLRRQIREDMiAALRANGKSAVFVSHDREEALQYADRIAVMKQGRILQTASPHEL 226
Cdd:PRK13537 156 DPDVLVLDEPTTGLDPQARHLMWERL-RSLLARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHAL 225
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
19-229 |
4.45e-35 |
|
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: 128.37 E-value: 4.45e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 19 VLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIFSKNTNLpvRERRLGYLVQEGVLFpHLTVY 98
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAW--LRRQVGVVLQENVLF-NRSIR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 99 RNIAYGlgngkgRTAQERQRIEAMLELTG----ISEL-------AGRYPHELSGGQQQRVALARALAPDPELILLDEPFS 167
Cdd:cd03252 94 DNIALA------DPGMSMERVIEAAKLAGahdfISELpegydtiVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATS 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1067578656 168 ALDEQLRRQIREDMIAALRanGKSAVFVSHdREEALQYADRIAVMKQGRILQTASPHELYRQ 229
Cdd:cd03252 168 ALDYESEHAIMRNMHDICA--GRTVIIIAH-RLSTVKNADRIIVMEKGRIVEQGSHDELLAE 226
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
9-200 |
4.61e-35 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 134.04 E-value: 4.61e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 9 HLSKSFQNTPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTifskntnlpvrerRLGYLVQE 88
Cdd:COG0488 3 NLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGL-------------RIGYLPQE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 89 GVLFPHLTVYRNIAYGLG---------------NGKGRTAQERQ-----------------RIEAMLELTGISELAGRYP 136
Cdd:COG0488 70 PPLDDDLTVLDTVLDGDAelraleaeleeleakLAEPDEDLERLaelqeefealggweaeaRAEEILSGLGFPEEDLDRP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1067578656 137 -HELSGGQQQRVALARALAPDPELILLDEPFSALDeqlrrqirEDMIAALR---ANGKSAV-FVSHDRE 200
Cdd:COG0488 150 vSELSGGWRRRVALARALLSEPDLLLLDEPTNHLD--------LESIEWLEeflKNYPGTVlVVSHDRY 210
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
16-271 |
9.11e-35 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 128.34 E-value: 9.11e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 16 NTPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTI--FSKNTNLPVReRRLGYLVQEGVLFP 93
Cdd:PRK11831 19 NRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIpaMSRSRLYTVR-KRMSMLFQSGALFT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 94 HLTVYRNIAYGLGNGKGRTAQERQRIEAM-LELTGISELAGRYPHELSGGQQQRVALARALAPDPELILLDEPFSALDEq 172
Cdd:PRK11831 98 DMNVFDNVAYPLREHTQLPAPLLHSTVMMkLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDP- 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 173 LRRQIREDMIAAL-RANGKSAVFVSHDREEALQYADRIAVMKQGRILQTASPHELyRQPADLDAALFIgegivfpaalna 251
Cdd:PRK11831 177 ITMGVLVKLISELnSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQAL-QANPDPRVRQFL------------ 243
|
250 260
....*....|....*....|
gi 1067578656 252 DGTADCrlgrlPVQSGAPAG 271
Cdd:PRK11831 244 DGIADG-----PVPFRYPAG 258
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
17-229 |
9.42e-35 |
|
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: 127.35 E-value: 9.42e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 17 TPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIfsKNTNLPVRERRLGYLVQEGVLFpHLT 96
Cdd:cd03251 15 PPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDV--RDYTLASLRRQIGLVSQDVFLF-NDT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 97 VYRNIAYGlgngkgRTAQERQRIEAMLELTGISELAGRYPH-----------ELSGGQQQRVALARALAPDPELILLDEP 165
Cdd:cd03251 92 VAENIAYG------RPGATREEVEEAARAANAHEFIMELPEgydtvigergvKLSGGQRQRIAIARALLKDPPILILDEA 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1067578656 166 FSALDEQLRRQIREDMIAALRanGKSAVFVSHdREEALQYADRIAVMKQGRILQTASPHELYRQ 229
Cdd:cd03251 166 TSALDTESERLVQAALERLMK--NRTTFVIAH-RLSTIENADRIVVLEDGKIVERGTHEELLAQ 226
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
9-217 |
1.14e-34 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 132.88 E-value: 1.14e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 9 HLSKSFQNTPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLsGKTIfskntnlpvrerRLGYLVQE 88
Cdd:COG0488 320 GLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETV------------KIGYFDQH 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 89 G-VLFPHLTVYRNIAYGLGNGKGRTAqeRQRIEAMLeLTGisELAGRYPHELSGGQQQRVALARALAPDPELILLDEPFS 167
Cdd:COG0488 387 QeELDPDKTVLDELRDGAPGGTEQEV--RGYLGRFL-FSG--DDAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEPTN 461
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1067578656 168 ALDEQLRRQIrEDmiaALRA-NGkSAVFVSHDRE--EALqyADRIAVMKQGRI 217
Cdd:COG0488 462 HLDIETLEAL-EE---ALDDfPG-TVLLVSHDRYflDRV--ATRILEFEDGGV 507
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
16-226 |
3.50e-34 |
|
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: 125.42 E-value: 3.50e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 16 NTPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIfsKNTNLPVRERRLGYLVQEGVLFPHl 95
Cdd:cd03254 15 KKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDI--RDISRKSLRSMIGVVLQDTFLFSG- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 96 TVYRNIAYglgngkGRTAQERQRIEAMLELTGISELAGRYP-----------HELSGGQQQRVALARALAPDPELILLDE 164
Cdd:cd03254 92 TIMENIRL------GRPNATDEEVIEAAKEAGAHDFIMKLPngydtvlgengGNLSQGERQLLAIARAMLRDPKILILDE 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1067578656 165 PFSALDEQLRRQIREDMIAALraNGKSAVFVSHdREEALQYADRIAVMKQGRILQTASPHEL 226
Cdd:cd03254 166 ATSNIDTETEKLIQEALEKLM--KGRTSIIIAH-RLSTIKNADKILVLDDGKIIEEGTHDEL 224
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
20-230 |
6.19e-34 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 126.48 E-value: 6.19e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 20 LNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIFSK--NTNLPVRERRLGYLVQ--EGVLFPHl 95
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPEtgNKNLKKLRKKVSLVFQfpEAQLFEN- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 96 TVYRNIAYGLGNgKGRTAQErQRIEAM--LELTGISE-LAGRYPHELSGGQQQRVALARALAPDPELILLDEPFSALDEQ 172
Cdd:PRK13641 102 TVLKDVEFGPKN-FGFSEDE-AKEKALkwLKKVGLSEdLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPE 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1067578656 173 LRRQIREDMIAALRAnGKSAVFVSHDREEALQYADRIAVMKQGRILQTASPHELYRQP 230
Cdd:PRK13641 180 GRKEMMQLFKDYQKA-GHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDK 236
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
3-226 |
1.01e-33 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 124.62 E-value: 1.01e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 3 AALHIGHLSKSFQNTPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIfsknTNLPVRERR- 81
Cdd:PRK10895 2 ATLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDI----SLLPLHARAr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 82 --LGYLVQEGVLFPHLTVYRNIAYGLGNGKGRTAQERQ-RIEAMLELTGISELAGRYPHELSGGQQQRVALARALAPDPE 158
Cdd:PRK10895 78 rgIGYLPQEASIFRRLSVYDNLMAVLQIRDDLSAEQREdRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPK 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1067578656 159 LILLDEPFSALDEQLRRQIREdMIAALRANGKSAVFVSHDREEALQYADRIAVMKQGRILQTASPHEL 226
Cdd:PRK10895 158 FILLDEPFAGVDPISVIDIKR-IIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEI 224
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
15-229 |
1.49e-33 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 125.66 E-value: 1.49e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 15 QNTP----VLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIFSKNTN---LPVReRRLGYLVQ 87
Cdd:PRK13646 14 KGTPyehqAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDkyiRPVR-KRIGMVFQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 88 --EGVLFPHlTVYRNIAYGLGNGKGRTAQERQRIEAMLELTGIS-ELAGRYPHELSGGQQQRVALARALAPDPELILLDE 164
Cdd:PRK13646 93 fpESQLFED-TVEREIIFGPKNFKMNLDEVKNYAHRLLMDLGFSrDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDE 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1067578656 165 PFSALDEQLRRQIREdMIAALRA-NGKSAVFVSHDREEALQYADRIAVMKQGRILQTASPHELYRQ 229
Cdd:PRK13646 172 PTAGLDPQSKRQVMR-LLKSLQTdENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFKD 236
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-229 |
2.65e-33 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 123.65 E-value: 2.65e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 1 MTAALHIGHLSKSFQ-----------------NTP-----VLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDS 58
Cdd:COG1134 1 MSSMIEVENVSKSYRlyhepsrslkelllrrrRTRreefwALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 59 GEISLSGktifskntnlpvrerRLGYLVQEGVLF-PHLTVYRNI-----AYGLgngkgRTAQERQRIEAMLELTGIsela 132
Cdd:COG1134 81 GRVEVNG---------------RVSALLELGAGFhPELTGRENIylngrLLGL-----SRKEIDEKFDEIVEFAEL---- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 133 GRYPHE----LSGGQQQRVALARALAPDPELILLDEPFSALDEQLRRQIReDMIAALRANGKSAVFVSHDREEALQYADR 208
Cdd:COG1134 137 GDFIDQpvktYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCL-ARIRELRESGRTVIFVSHSMGAVRRLCDR 215
|
250 260
....*....|....*....|....
gi 1067578656 209 IAVMKQGRILQTASPHE---LYRQ 229
Cdd:COG1134 216 AIWLEKGRLVMDGDPEEviaAYEA 239
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1-226 |
3.31e-33 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 128.63 E-value: 3.31e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 1 MTAALHIGHLSKSFQNTPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIFSKNtnlPVRER 80
Cdd:PRK15439 8 APPLLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLT---PAKAH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 81 RLG-YLV-QEGVLFPHLTVYRNIAYGLgngkGRTAQERQRIEAMLELTGIS----ELAGryphELSGGQQQRVALARALA 154
Cdd:PRK15439 85 QLGiYLVpQEPLLFPNLSVKENILFGL----PKRQASMQKMKQLLAALGCQldldSSAG----SLEVADRQIVEILRGLM 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1067578656 155 PDPELILLDEPFSALD----EQLRRQIRedmiaALRANGKSAVFVSHDREEALQYADRIAVMKQGRILQTASPHEL 226
Cdd:PRK15439 157 RDSRILILDEPTASLTpaetERLFSRIR-----ELLAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTADL 227
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
17-212 |
6.02e-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: 128.17 E-value: 6.02e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 17 TPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIfsKNTNLPVRERRLGYLVQEGVLFPHlT 96
Cdd:TIGR02857 335 RPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPL--ADADADSWRDQIAWVPQHPFLFAG-T 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 97 VYRNIAYGLGNGKGRTAQERQRIEAMLELT-----GISELAGRYPHELSGGQQQRVALARALAPDPELILLDEPFSALDE 171
Cdd:TIGR02857 412 IAENIRLARPDASDAEIREALERAGLDEFVaalpqGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDA 491
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1067578656 172 QLRRQIREDMIAAlrANGKSAVFVSHDREEALQyADRIAVM 212
Cdd:TIGR02857 492 ETEAEVLEALRAL--AQGRTVLLVTHRLALAAL-ADRIVVL 529
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
17-236 |
2.10e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 122.11 E-value: 2.10e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 17 TPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTI-FSKNTNLPVReRRLGYLVQ--EGVLF- 92
Cdd:PRK13639 15 TEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIkYDKKSLLEVR-KTVGIVFQnpDDQLFa 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 93 PhlTVYRNIAYGLGNGKGRTAQERQRIEAMLELTGISELAGRYPHELSGGQQQRVALARALAPDPELILLDEPFSALDEQ 172
Cdd:PRK13639 94 P--TVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPM 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1067578656 173 LRRQIREdMIAALRANGKSAVFVSHDREEALQYADRIAVMKQGRILQTASPHELYRQPADLDAA 236
Cdd:PRK13639 172 GASQIMK-LLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDIETIRKA 234
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
4-226 |
2.79e-32 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 125.91 E-value: 2.79e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 4 ALHIGHLS-KSFQNTPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIfsknTNLPVRERR- 81
Cdd:COG3845 257 VLEVENLSvRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDI----TGLSPRERRr 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 82 --LGYLVQE----GvLFPHLTVYRNIA-----------YGLGNGKGRTAQERQRIEAM-LELTGISELAGRypheLSGGQ 143
Cdd:COG3845 333 lgVAYIPEDrlgrG-LVPDMSVAENLIlgryrrppfsrGGFLDRKAIRAFAEELIEEFdVRTPGPDTPARS----LSGGN 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 144 QQRVALARALAPDPELILLDEPFSALD----EQLRRQIREdmiaaLRANGKSAVFVSHDREEALQYADRIAVMKQGRILQ 219
Cdd:COG3845 408 QQKVILARELSRDPKLLIAAQPTRGLDvgaiEFIHQRLLE-----LRDAGAAVLLISEDLDEILALSDRIAVMYEGRIVG 482
|
....*..
gi 1067578656 220 TASPHEL 226
Cdd:COG3845 483 EVPAAEA 489
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
5-217 |
2.90e-32 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 121.35 E-value: 2.90e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 5 LHIGHLSKSF-QNTP----VLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIfsknTNLPV-- 77
Cdd:COG1101 2 LELKNLSKTFnPGTVnekrALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDV----TKLPEyk 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 78 RERRLGYLVQEGVL--FPHLTVYRNIAYGLGNGKGR------TAQERQRIEAMLELTGISeLAGRYPHE---LSGGQQQR 146
Cdd:COG1101 78 RAKYIGRVFQDPMMgtAPSMTIEENLALAYRRGKRRglrrglTKKRRELFRELLATLGLG-LENRLDTKvglLSGGQRQA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1067578656 147 VALARALAPDPELILLDEPFSALD--------EQLRRQIREDMIAALrangksavFVSHDREEALQYADRIAVMKQGRI 217
Cdd:COG1101 157 LSLLMATLTKPKLLLLDEHTAALDpktaalvlELTEKIVEENNLTTL--------MVTHNMEQALDYGNRLIMMHEGRI 227
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
21-230 |
3.14e-32 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 122.89 E-value: 3.14e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 21 NDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIfSKNTNLPVRERR--LGYLVQEGV--LFPHLT 96
Cdd:PRK15079 38 DGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDL-LGMKDDEWRAVRsdIQMIFQDPLasLNPRMT 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 97 VYRNIAYGLgngkgRT------AQE-RQRIEAMLELTGI-SELAGRYPHELSGGQQQRVALARALAPDPELILLDEPFSA 168
Cdd:PRK15079 117 IGEIIAEPL-----RTyhpklsRQEvKDRVKAMMLKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSA 191
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1067578656 169 LDEQLRRQIREDMIAALRANGKSAVFVSHDREEALQYADRIAVMKQGRILQTASPHELYRQP 230
Cdd:PRK15079 192 LDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNP 253
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
11-216 |
5.25e-32 |
|
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: 119.11 E-value: 5.25e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 11 SKSFQNTPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGktifskntnlpvrerRLGYLVQEGV 90
Cdd:cd03250 12 SGEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG---------------SIAYVSQEPW 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 91 LFPhLTVYRNIAYGLgngkgRTAQERQR--IEA--------MLE---LT-----GISelagrypheLSGGQQQRVALARA 152
Cdd:cd03250 77 IQN-GTIRENILFGK-----PFDEERYEkvIKAcalepdleILPdgdLTeigekGIN---------LSGGQKQRISLARA 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1067578656 153 LAPDPELILLDEPFSALDEQLRRQIREDMIAALRANGKSAVFVSHdREEALQYADRIAVMKQGR 216
Cdd:cd03250 142 VYSDADIYLLDDPLSAVDAHVGRHIFENCILGLLLNNKTRILVTH-QLQLLPHADQIVVLDNGR 204
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
4-252 |
5.74e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 121.06 E-value: 5.74e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 4 ALHIGHLSKSFQNT--PVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGE---ISLSGKTIFSKnTNLPVR 78
Cdd:PRK13640 5 IVEFKHVSFTYPDSkkPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPnskITVDGITLTAK-TVWDIR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 79 ERrLGYLVQE-GVLFPHLTVYRNIAYGLGNgKGRTAQERQRIEA-MLELTGISELAGRYPHELSGGQQQRVALARALAPD 156
Cdd:PRK13640 84 EK-VGIVFQNpDNQFVGATVGDDVAFGLEN-RAVPRPEMIKIVRdVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 157 PELILLDEPFSALDEQLRRQIREDMIAALRANGKSAVFVSHDREEALQyADRIAVMKQGRILQTASPHELYRQP-----A 231
Cdd:PRK13640 162 PKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEANM-ADQVLVLDDGKLLAQGSPVEIFSKVemlkeI 240
|
250 260
....*....|....*....|....*...
gi 1067578656 232 DLDAALF-------IGEGIVFPAALNAD 252
Cdd:PRK13640 241 GLDIPFVyklknklKEKGISVPQEINTE 268
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
5-272 |
7.35e-32 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 123.41 E-value: 7.35e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 5 LHIGHLSKSFQNTPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIfsknTNLPVRE--RRL 82
Cdd:PRK09536 4 IDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDV----EALSARAasRRV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 83 GYLVQEGVLFPHLTVYRNIAYG----LGNGKGRTAQERQRIEAMLELTGISELAGRYPHELSGGQQQRVALARALAPDPE 158
Cdd:PRK09536 80 ASVPQDTSLSFEFDVRQVVEMGrtphRSRFDTWTETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 159 LILLDEPFSALDeqLRRQIRE-DMIAALRANGKSAVFVSHDREEALQYADRIAVMKQGRILQTASPHELYRQP---ADLD 234
Cdd:PRK09536 160 VLLLDEPTASLD--INHQVRTlELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVLTADtlrAAFD 237
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1067578656 235 AALFIGEGIVFPAAL-----NADGTADCRLGRLPV-QSGAPAGT 272
Cdd:PRK09536 238 ARTAVGTDPATGAPTvtplpDPDRTEAAADTRVHVvGGGQPAAR 281
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
20-229 |
7.64e-32 |
|
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: 125.30 E-value: 7.64e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 20 LNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIFSKNTNLPVRER-----RLGYLVQEGVLFPH 94
Cdd:TIGR03269 300 VDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRVGDEWVDMTKPGPDGRgrakrYIGILHQEYDLYPH 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 95 LTVYRNI--AYGLgngkgRTAQERQRIEAM--LELTGISE-----LAGRYPHELSGGQQQRVALARALAPDPELILLDEP 165
Cdd:TIGR03269 380 RTVLDNLteAIGL-----ELPDELARMKAVitLKMVGFDEekaeeILDKYPDELSEGERHRVALAQVLIKEPRIVILDEP 454
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1067578656 166 FSALDEQLRRQIREDMIAALRANGKSAVFVSHDREEALQYADRIAVMKQGRILQTASPHELYRQ 229
Cdd:TIGR03269 455 TGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEEIVEE 518
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-226 |
1.37e-31 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 121.48 E-value: 1.37e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 2 TAALHIGHLSKSFQNTPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIfskntnlPVRER- 80
Cdd:PRK13536 39 TVAIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPV-------PARARl 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 81 ---RLGYLVQEGVLFPHLTVYRN-IAYGLGNGKgRTAQERQRIEAMLELTGISELAGRYPHELSGGQQQRVALARALAPD 156
Cdd:PRK13536 112 araRIGVVPQFDNLDLEFTVRENlLVFGRYFGM-STREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALIND 190
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 157 PELILLDEPFSALDEQLRRQIREDMiAALRANGKSAVFVSHDREEALQYADRIAVMKQGRILQTASPHEL 226
Cdd:PRK13536 191 PQLLILDEPTTGLDPHARHLIWERL-RSLLARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHAL 259
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
2-209 |
1.50e-31 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 118.66 E-value: 1.50e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 2 TAALHIGHLSKSFQNTPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIfsknTNLPVRERR 81
Cdd:PRK10247 5 SPLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDI----STLKPEIYR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 82 --LGYLVQEGVLFPHlTVYRNIA--YGLGNgkgrTAQERQRIEAMLELTGISE-LAGRYPHELSGGQQQRVALARALAPD 156
Cdd:PRK10247 81 qqVSYCAQTPTLFGD-TVYDNLIfpWQIRN----QQPDPAIFLDDLERFALPDtILTKNIAELSGGEKQRISLIRNLQFM 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1067578656 157 PELILLDEPFSALDEQLRRQIREDMIAALRANGKSAVFVSHDREEaLQYADRI 209
Cdd:PRK10247 156 PKVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDE-INHADKV 207
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
19-217 |
3.01e-31 |
|
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: 117.63 E-value: 3.01e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 19 VLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGktifskntnlpvrerRLGYLVQEGVLF-PHLTV 97
Cdd:cd03220 37 ALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG---------------RVSSLLGLGGGFnPELTG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 98 YRNIAYglgNG--KGRTAQE-RQRIEAMLELTGIselaGRYPHE----LSGGQQQRVALARALAPDPELILLDEPFSALD 170
Cdd:cd03220 102 RENIYL---NGrlLGLSRKEiDEKIDEIIEFSEL----GDFIDLpvktYSSGMKARLAFAIATALEPDILLIDEVLAVGD 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1067578656 171 EQLRRQIREdMIAALRANGKSAVFVSHDREEALQYADRIAVMKQGRI 217
Cdd:cd03220 175 AAFQEKCQR-RLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKI 220
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
17-227 |
4.23e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 118.80 E-value: 4.23e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 17 TPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTI-FSKNTNLPVRERrLGYLVQ--EGVLFP 93
Cdd:PRK13636 19 THALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIdYSRKGLMKLRES-VGMVFQdpDNQLFS 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 94 hLTVYRNIAYGLGNGKGRTAQERQRIEAMLELTGISELAGRYPHELSGGQQQRVALARALAPDPELILLDEPFSALDEQL 173
Cdd:PRK13636 98 -ASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMG 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1067578656 174 RRQIREDMIAALRANGKSAVFVSHDREEALQYADRIAVMKQGRILQTASPHELY 227
Cdd:PRK13636 177 VSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVF 230
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
10-225 |
5.07e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 119.04 E-value: 5.07e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 10 LSKSF-QNTP----VLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEIS---------------------- 62
Cdd:PRK13651 8 IVKIFnKKLPtelkALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEwifkdeknkkktkekekvlekl 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 63 LSGKTIFSKNTNLPVRERRLGYLVQ--EGVLFPHlTVYRNIAYG---LGNGKgrtAQERQRIEAMLELTGISE-LAGRYP 136
Cdd:PRK13651 88 VIQKTRFKKIKKIKEIRRRVGVVFQfaEYQLFEQ-TIEKDIIFGpvsMGVSK---EEAKKRAAKYIELVGLDEsYLQRSP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 137 HELSGGQQQRVALARALAPDPELILLDEPFSALDEQLRRQIREdMIAALRANGKSAVFVSHDREEALQYADRIAVMKQGR 216
Cdd:PRK13651 164 FELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILE-IFDNLNKQGKTIILVTHDLDNVLEWTKRTIFFKDGK 242
|
....*....
gi 1067578656 217 ILQTASPHE 225
Cdd:PRK13651 243 IIKDGDTYD 251
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-230 |
6.69e-31 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 117.64 E-value: 6.69e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 1 MTAALHIGHLSKSFQNTPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGF-----EQPDSGEISLSGKTIFSKNTNl 75
Cdd:PRK14267 1 MKFAIETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLlelneEARVEGEVRLFGRNIYSPDVD- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 76 PVRERR-LGYLVQEGVLFPHLTVYRNIAYGLG-NGKGRTAQE-RQRIEAMLELTGI-SELAGR---YPHELSGGQQQRVA 148
Cdd:PRK14267 80 PIEVRReVGMVFQYPNPFPHLTIYDNVAIGVKlNGLVKSKKElDERVEWALKKAALwDEVKDRlndYPSNLSGGQRQRLV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 149 LARALAPDPELILLDEPFSALDEQLRRQIrEDMIAALRaNGKSAVFVSHDREEALQYADRIAVMKQGRILQTASPHELYR 228
Cdd:PRK14267 160 IARALAMKPKILLMDEPTANIDPVGTAKI-EELLFELK-KEYTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFE 237
|
..
gi 1067578656 229 QP 230
Cdd:PRK14267 238 NP 239
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1-226 |
7.54e-31 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 117.81 E-value: 7.54e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 1 MTAALHIGHLSKSFQNTPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDS---GEISLSGKTIfSKNTNLP- 76
Cdd:PRK09984 1 MQTIIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKsagSHIELLGRTV-QREGRLAr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 77 -VRERR--LGYLVQEGVLFPHLTVYRNIAYG-LGNG-------KGRTAQERQRIEAMLELTGISELAGRYPHELSGGQQQ 145
Cdd:PRK09984 80 dIRKSRanTGYIFQQFNLVNRLSVLENVLIGaLGSTpfwrtcfSWFTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 146 RVALARALAPDPELILLDEPFSALDEQLRRQIREDMIAALRANGKSAVFVSHDREEALQYADRIAVMKQGRILQTASPHE 225
Cdd:PRK09984 160 RVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQQ 239
|
.
gi 1067578656 226 L 226
Cdd:PRK09984 240 F 240
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
7-223 |
1.02e-30 |
|
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: 123.59 E-value: 1.02e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 7 IGHLSKSFQ--NTPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIfskNTNLPVRERRLGY 84
Cdd:TIGR01257 931 VKNLVKIFEpsGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI---ETNLDAVRQSLGM 1007
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 85 LVQEGVLFPHLTVYRNIAYgLGNGKGRTAQERQ-RIEAMLELTGISELAGRYPHELSGGQQQRVALARALAPDPELILLD 163
Cdd:TIGR01257 1008 CPQHNILFHHLTVAEHILF-YAQLKGRSWEEAQlEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLD 1086
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 164 EPFSALDEQLRRQIReDMIAALRAnGKSAVFVSHDREEALQYADRIAVMKQGRILQTASP 223
Cdd:TIGR01257 1087 EPTSGVDPYSRRSIW-DLLLKYRS-GRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTP 1144
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
5-231 |
1.13e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 118.80 E-value: 1.13e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 5 LHIGHLSKSF-QNTP----VLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISL-----SGKTIFSKNTN 74
Cdd:PRK13631 22 LRVKNLYCVFdEKQEnelvALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVgdiyiGDKKNNHELIT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 75 LPV-----RERRLGYLVQEGVLFPHL-----TVYRNIAYG---LGNGKGRTaqeRQRIEAMLELTGISE-LAGRYPHELS 140
Cdd:PRK13631 102 NPYskkikNFKELRRRVSMVFQFPEYqlfkdTIEKDIMFGpvaLGVKKSEA---KKLAKFYLNKMGLDDsYLERSPFGLS 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 141 GGQQQRVALARALAPDPELILLDEPFSALDEQLRRQIReDMIAALRANGKSAVFVSHDREEALQYADRIAVMKQGRILQT 220
Cdd:PRK13631 179 GGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMM-QLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKT 257
|
250
....*....|.
gi 1067578656 221 ASPHELYRQPA 231
Cdd:PRK13631 258 GTPYEIFTDQH 268
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
9-217 |
1.43e-30 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 115.74 E-value: 1.43e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 9 HLSKSF-QNTPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIFS-KNTNLPVRERRLGYLV 86
Cdd:PRK10908 6 HVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRlKNREVPFLRRQIGMIF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 87 QEGVLFPHLTVYRNIAYGLGNGKGRTAQERQRIEAMLELTGISELAGRYPHELSGGQQQRVALARALAPDPELILLDEPF 166
Cdd:PRK10908 86 QDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPT 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1067578656 167 SALDEQLRRQIREdMIAALRANGKSAVFVSHDREEALQYADRIAVMKQGRI 217
Cdd:PRK10908 166 GNLDDALSEGILR-LFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
18-226 |
1.66e-30 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 121.75 E-value: 1.66e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 18 PVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIfsKNTNLPVRERRLGYLVQEGVLFPHlTV 97
Cdd:TIGR02203 346 PALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDL--ADYTLASLRRQVALVSQDVVLFND-TI 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 98 YRNIAYGLGNGKGRtaqerQRIEAMLELTGISELAGRYPH-----------ELSGGQQQRVALARALAPDPELILLDEPF 166
Cdd:TIGR02203 423 ANNIAYGRTEQADR-----AEIERALAAAYAQDFVDKLPLgldtpigengvLLSGGQRQRLAIARALLKDAPILILDEAT 497
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1067578656 167 SALDEQLRRQIRedmiAALRA--NGKSAVFVSHdREEALQYADRIAVMKQGRILQTASPHEL 226
Cdd:TIGR02203 498 SALDNESERLVQ----AALERlmQGRTTLVIAH-RLSTIEKADRIVVMDDGRIVERGTHNEL 554
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
18-229 |
3.22e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 116.38 E-value: 3.22e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 18 PVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIFSKNTNLPVRERR--LGYLVQ--EGVLFP 93
Cdd:PRK13649 21 RALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNKDIKQIRkkVGLVFQfpESQLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 94 HlTVYRNIAYGLGNgKGRTAQERQRI-EAMLELTGISE-LAGRYPHELSGGQQQRVALARALAPDPELILLDEPFSALDE 171
Cdd:PRK13649 101 E-TVLKDVAFGPQN-FGVSQEEAEALaREKLALVGISEsLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDP 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1067578656 172 QLRRQIReDMIAALRANGKSAVFVSHDREEALQYADRIAVMKQGRILQTASPHELYRQ 229
Cdd:PRK13649 179 KGRKELM-TLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIFQD 235
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
16-229 |
3.47e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 116.76 E-value: 3.47e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 16 NTP----VLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIFSKNTNL---PVReRRLGYLVQ- 87
Cdd:PRK13643 14 NSPfasrALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKeikPVR-KKVGVVFQf 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 88 -EGVLFPHlTVYRNIAYGLGNgKGRTAQERQRIEA-MLELTGIS-ELAGRYPHELSGGQQQRVALARALAPDPELILLDE 164
Cdd:PRK13643 93 pESQLFEE-TVLKDVAFGPQN-FGIPKEKAEKIAAeKLEMVGLAdEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDE 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1067578656 165 PFSALDEQLRRQIREdMIAALRANGKSAVFVSHDREEALQYADRIAVMKQGRILQTASPHELYRQ 229
Cdd:PRK13643 171 PTAGLDPKARIEMMQ-LFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQE 234
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
17-223 |
3.88e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 115.99 E-value: 3.88e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 17 TPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIfSKNTNLPVReRRLGYLVQE--GVLFPh 94
Cdd:PRK13647 18 TKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREV-NAENEKWVR-SKVGLVFQDpdDQVFS- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 95 LTVYRNIAYGLGNGKGRTAQERQRIEAMLELTGISELAGRYPHELSGGQQQRVALARALAPDPELILLDEPFSALDEQLR 174
Cdd:PRK13647 95 STVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQ 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1067578656 175 RQIREdMIAALRANGKSAVFVSHDREEALQYADRIAVMKQGRILQTASP 223
Cdd:PRK13647 175 ETLME-ILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDK 222
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
17-218 |
6.27e-30 |
|
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: 113.03 E-value: 6.27e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 17 TPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAG--FEQPDSGEISLSGKTIFSKNTNlpvreRRLGYLVQEGVLFPH 94
Cdd:cd03213 22 KQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGrrTGLGVSGEVLINGRPLDKRSFR-----KIIGYVPQDDILHPT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 95 LTVYRNIAYglgngkgrTAQERQrieamleltgiselagrypheLSGGQQQRVALARALAPDPELILLDEPFSALDEQLR 174
Cdd:cd03213 97 LTVRETLMF--------AAKLRG---------------------LSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSA 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1067578656 175 RQIREdMIAALRANGKSAVFVSHD-REEALQYADRIAVMKQGRIL 218
Cdd:cd03213 148 LQVMS-LLRRLADTGRTIICSIHQpSSEIFELFDKLLLLSQGRVI 191
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
5-226 |
7.29e-30 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 120.61 E-value: 7.29e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 5 LHIGHLSKSFQ-NTPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIfsKNTNLPVRERRLG 83
Cdd:TIGR01193 474 IVINDVSYSYGyGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSL--KDIDRHTLRQFIN 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 84 YLVQEGVLFPHlTVYRNIAygLGNGKGRTAQE----------RQRIEAMLE--LTGISELAGryphELSGGQQQRVALAR 151
Cdd:TIGR01193 552 YLPQEPYIFSG-SILENLL--LGAKENVSQDEiwaaceiaeiKDDIENMPLgyQTELSEEGS----SISGGQKQRIALAR 624
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1067578656 152 ALAPDPELILLDEPFSALDEQLRRQIREDMiaaLRANGKSAVFVSHdREEALQYADRIAVMKQGRILQTASPHEL 226
Cdd:TIGR01193 625 ALLTDSKVLILDESTSNLDTITEKKIVNNL---LNLQDKTIIFVAH-RLSVAKQSDKIIVLDHGKIIEQGSHDEL 695
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
16-230 |
1.00e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 114.90 E-value: 1.00e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 16 NTPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIFSKNtnlpVRERR--LGYLVQ---EGV 90
Cdd:PRK13652 16 SKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKEN----IREVRkfVGLVFQnpdDQI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 91 LFPhlTVYRNIAYGLGNGKGRTAQERQRIEAMLELTGISELAGRYPHELSGGQQQRVALARALAPDPELILLDEPFSALD 170
Cdd:PRK13652 92 FSP--TVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLD 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 171 EQLRRQIREDMIAALRANGKSAVFVSHDREEALQYADRIAVMKQGRILQTASPHELYRQP 230
Cdd:PRK13652 170 PQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
22-230 |
2.04e-29 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 118.80 E-value: 2.04e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 22 DISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTI--FSKNTNLPVReRRLGYLVQE--GVLFPHLTV 97
Cdd:PRK10261 342 KVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIdtLSPGKLQALR-RDIQFIFQDpyASLDPRQTV 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 98 YRNI-----AYGLGNGKgrtaQERQRIEAMLELTGI-SELAGRYPHELSGGQQQRVALARALAPDPELILLDEPFSALDE 171
Cdd:PRK10261 421 GDSImeplrVHGLLPGK----AAAARVAWLLERVGLlPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDV 496
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1067578656 172 QLRRQIREDMIAALRANGKSAVFVSHDREEALQYADRIAVMKQGRILQTASPHELYRQP 230
Cdd:PRK10261 497 SIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENP 555
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
21-241 |
2.71e-29 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 113.16 E-value: 2.71e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 21 NDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIfsknTNLPVRE-RRLGyLV---QEGVLFPHLT 96
Cdd:PRK11300 22 NNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHI----EGLPGHQiARMG-VVrtfQHVRLFREMT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 97 V--------YRNIAYGLGNGKGRTAQERQR-IEAM------LELTGISELAGRYPHELSGGQQQRVALARALAPDPELIL 161
Cdd:PRK11300 97 VienllvaqHQQLKTGLFSGLLKTPAFRRAeSEALdraatwLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILM 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 162 LDEPFSALDEQLRRQIREdMIAALRAN-GKSAVFVSHDREEALQYADRIAVMKQGRILQTASPHELYRQPADLDAALfiG 240
Cdd:PRK11300 177 LDEPAAGLNPKETKELDE-LIAELRNEhNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEIRNNPDVIKAYL--G 253
|
.
gi 1067578656 241 E 241
Cdd:PRK11300 254 E 254
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
17-231 |
2.96e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 113.54 E-value: 2.96e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 17 TPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTI--FSKntnLPVRERRLGYLVQE-GVLFP 93
Cdd:PRK13644 15 TPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTgdFSK---LQGIRKLVGIVFQNpETQFV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 94 HLTVYRNIAYGLGNGKGRTAQERQRIEAMLELTGISELAGRYPHELSGGQQQRVALARALAPDPELILLDEPFSALDEQL 173
Cdd:PRK13644 92 GRTVEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDS 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1067578656 174 RRQIREDmIAALRANGKSAVFVSHDREEaLQYADRIAVMKQGRILQTASPHELYRQPA 231
Cdd:PRK13644 172 GIAVLER-IKKLHEKGKTIVYITHNLEE-LHDADRIIVMDRGKIVLEGEPENVLSDVS 227
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
19-231 |
3.39e-29 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 117.88 E-value: 3.39e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 19 VLNDISLSLDPGEILFIIGASGCGKTT----LLRCLAGfeqpdSGEISLSGKTI--FSKNTNLPVReRRLGYLVQE--GV 90
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLINS-----QGEIWFDGQPLhnLNRRQLLPVR-HRIQVVFQDpnSS 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 91 LFPHLTVYRNIAYGLG-NGKGRTAQERQR--IEAMLELTGISELAGRYPHELSGGQQQRVALARALAPDPELILLDEPFS 167
Cdd:PRK15134 375 LNPRLNVLQIIEEGLRvHQPTLSAAQREQqvIAVMEEVGLDPETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTS 454
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1067578656 168 ALDEQLRRQIREDMIAALRANGKSAVFVSHDREEALQYADRIAVMKQGRILQTASPHELYRQPA 231
Cdd:PRK15134 455 SLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERVFAAPQ 518
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
5-217 |
5.93e-29 |
|
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: 110.10 E-value: 5.93e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 5 LHIGHLSKSF--QNTPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIFSKNTNLpvrERRL 82
Cdd:cd03247 1 LSINNVSFSYpeQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKAL---SSLI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 83 GYLVQEgvlfPHL---TVYRNIayglgngkgrtaqerqrieamleltgiselaGRyphELSGGQQQRVALARALAPDPEL 159
Cdd:cd03247 78 SVLNQR----PYLfdtTLRNNL-------------------------------GR---RFSGGERQRLALARILLQDAPI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1067578656 160 ILLDEPFSALDEQLRRQIREDMIAALRanGKSAVFVSHdREEALQYADRIAVMKQGRI 217
Cdd:cd03247 120 VLLDEPTVGLDPITERQLLSLIFEVLK--DKTLIWITH-HLTGIEHMDKILFLENGKI 174
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1-220 |
5.94e-29 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 116.55 E-value: 5.94e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 1 MTAALHIGHLSKSFQNTPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIFSKNTNLPVrER 80
Cdd:PRK11288 1 SSPYLSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAAL-AA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 81 RLGYLVQEGVLFPHLTVYRNIAYG-LGNGKGRTAQERQRIEAMLELTGISE-LAGRYP-HELSGGQQQRVALARALAPDP 157
Cdd:PRK11288 80 GVAIIYQELHLVPEMTVAENLYLGqLPHKGGIVNRRLLNYEAREQLEHLGVdIDPDTPlKYLSIGQRQMVEIAKALARNA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1067578656 158 ELILLDEPFSALD----EQLRRQIREdmiaaLRANGKSAVFVSHDREEALQYADRIAVMKQGRILQT 220
Cdd:PRK11288 160 RVIAFDEPTSSLSareiEQLFRVIRE-----LRAEGRVILYVSHRMEEIFALCDAITVFKDGRYVAT 221
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
15-229 |
2.28e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 111.33 E-value: 2.28e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 15 QNTPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIFSKNTNLPVRERrlgylvqEGVLFPH 94
Cdd:PRK13633 21 TEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLWDIRNK-------AGMVFQN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 95 -------LTVYRNIAYGLGNgKGRTAQE-RQRIEAMLELTGISELAGRYPHELSGGQQQRVALARALAPDPELILLDEPF 166
Cdd:PRK13633 94 pdnqivaTIVEEDVAFGPEN-LGIPPEEiRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPT 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1067578656 167 SALDEQLRRQIREDMIAALRANGKSAVFVSHDREEALQyADRIAVMKQGRILQTASPHELYRQ 229
Cdd:PRK13633 173 AMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIFKE 234
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
20-225 |
2.36e-28 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 110.70 E-value: 2.36e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 20 LNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFeQPDSGEISLSGKTIfsknTNLPVRE--RRLGYLVQEGVLFPHLTV 97
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGL-LPGQGEILLNGRPL----SDWSAAElaRHRAYLSQQQSPPFAMPV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 98 YRNIAYGLGnGKGRTAQERQRIEAMLELTGISELAGRYPHELSGGQQQRVALARALA-------PDPELILLDEPFSALD 170
Cdd:COG4138 87 FQYLALHQP-AGASSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLqvwptinPEGQLLLLDEPMNSLD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1067578656 171 eqLRRQIRED-MIAALRANGKSAVFVSHDREEALQYADRIAVMKQGRILQTASPHE 225
Cdd:COG4138 166 --VAQQAALDrLLRELCQQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAE 219
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
5-232 |
2.61e-28 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 110.91 E-value: 2.61e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 5 LHIGHLSKSFQNTPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTI-FSKNT----NLPVRe 79
Cdd:PRK14246 11 FNISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLyFGKDIfqidAIKLR- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 80 RRLGYLVQEGVLFPHLTVYRNIAYGLGNGKGRTAQERQRI-EAMLELTGI-SELAGRY---PHELSGGQQQRVALARALA 154
Cdd:PRK14246 90 KEVGMVFQQPNPFPHLSIYDNIAYPLKSHGIKEKREIKKIvEECLRKVGLwKEVYDRLnspASQLSGGQQQRLTIARALA 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1067578656 155 PDPELILLDEPFSALDeQLRRQIREDMIAALRaNGKSAVFVSHDREEALQYADRIAVMKQGRILQTASPHELYRQPAD 232
Cdd:PRK14246 170 LKPKVLLMDEPTSMID-IVNSQAIEKLITELK-NEIAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKN 245
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
20-250 |
3.21e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 110.61 E-value: 3.21e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 20 LNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIfsKNTNLPVRERRLGYLVQE-GVLFPHLTVY 98
Cdd:PRK13648 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAI--TDDNFEKLRKHIGIVFQNpDNQFVGSIVK 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 99 RNIAYGLGNGKGRTAQERQRIEAMLELTGISELAGRYPHELSGGQQQRVALARALAPDPELILLDEPFSALDEQLRRQIR 178
Cdd:PRK13648 103 YDVAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLL 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1067578656 179 eDMIAALRANGKSAVF-VSHDREEALQyADRIAVMKQGRILQTASPHELYRqpaDLDAALFIGEGIVFPAALN 250
Cdd:PRK13648 183 -DLVRKVKSEHNITIIsITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIFD---HAEELTRIGLDLPFPIKIN 250
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
15-209 |
5.25e-28 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 114.52 E-value: 5.25e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 15 QNTPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISL--SGKTIFskntnLPVRerrlGYLvqegvlf 92
Cdd:COG4178 374 DGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARpaGARVLF-----LPQR----PYL------- 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 93 PHLTVYRNIAYGlgngKGRTAQERQRIEAMLELTGISELAGRY------PHELSGGQQQRVALARALAPDPELILLDEPF 166
Cdd:COG4178 438 PLGTLREALLYP----ATAEAFSDAELREALEAVGLGHLAERLdeeadwDQVLSLGEQQRLAFARLLLHKPDWLFLDEAT 513
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1067578656 167 SALDEQLRRQiredMIAALRANGKSAVFVS--HdREEALQYADRI 209
Cdd:COG4178 514 SALDEENEAA----LYQLLREELPGTTVISvgH-RSTLAAFHDRV 553
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
15-198 |
6.01e-28 |
|
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: 113.99 E-value: 6.01e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 15 QNTPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIFSKNTNLPvrERRLGYLVQEGVLFpH 94
Cdd:TIGR02868 346 GAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEV--RRRVSVCAQDAHLF-D 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 95 LTVYRNIAYGLGNGKGrtaqerQRIEAMLELTGISELAGRYPH-----------ELSGGQQQRVALARALAPDPELILLD 163
Cdd:TIGR02868 423 TTVRENLRLARPDATD------EELWAALERVGLADWLRALPDgldtvlgeggaRLSGGERQRLALARALLADAPILLLD 496
|
170 180 190
....*....|....*....|....*....|....*
gi 1067578656 164 EPFSALDEQLRRQIREDMIAALRanGKSAVFVSHD 198
Cdd:TIGR02868 497 EPTEHLDAETADELLEDLLAALS--GRTVVLITHH 529
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
16-217 |
1.15e-27 |
|
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: 108.33 E-value: 1.15e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 16 NTPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIFS-KNTNLpvrERRLGYLVQEGVLFPH 94
Cdd:cd03248 26 DTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQyEHKYL---HSKVSLVGQEPVLFAR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 95 lTVYRNIAYGLGNGK-GRTAQERQRIEA----MLELTGISELAGRYPHELSGGQQQRVALARALAPDPELILLDEPFSAL 169
Cdd:cd03248 103 -SLQDNIAYGLQSCSfECVKEAAQKAHAhsfiSELASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSAL 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1067578656 170 DEQLRRQIREdmiAALRANGKSAVFVSHDREEALQYADRIAVMKQGRI 217
Cdd:cd03248 182 DAESEQQVQQ---ALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
16-230 |
1.23e-27 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 114.05 E-value: 1.23e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 16 NTPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKtifskntnlPVRE-------RRLGYLVQE 88
Cdd:TIGR00958 493 DVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGV---------PLVQydhhylhRQVALVGQE 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 89 GVLFPHlTVYRNIAYGLgngkgrTAQERQRIEAMLELTG----ISELAGRYPHE-------LSGGQQQRVALARALAPDP 157
Cdd:TIGR00958 564 PVLFSG-SVRENIAYGL------TDTPDEEIMAAAKAANahdfIMEFPNGYDTEvgekgsqLSGGQKQRIAIARALVRKP 636
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1067578656 158 ELILLDEPFSALDEQLRRQIREDMIAAlranGKSAVFVSHdREEALQYADRIAVMKQGRILQTASPHELYRQP 230
Cdd:TIGR00958 637 RVLILDEATSALDAECEQLLQESRSRA----SRTVLLIAH-RLSTVERADQILVLKKGSVVEMGTHKQLMEDQ 704
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
5-216 |
1.87e-27 |
|
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: 105.22 E-value: 1.87e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 5 LHIGHLSKSFQNTPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTifskntnlpvrerRLGY 84
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTV-------------KIGY 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 85 LVQegvlfphltvyrniayglgngkgrtaqerqrieamleltgiselagrypheLSGGQQQRVALARALAPDPELILLDE 164
Cdd:cd03221 68 FEQ---------------------------------------------------LSGGEKMRLALAKLLLENPNLLLLDE 96
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1067578656 165 PFSALDEQLRRQIREdmiaALRANGKSAVFVSHDREEALQYADRIAVMKQGR 216
Cdd:cd03221 97 PTNHLDLESIEALEE----ALKEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-232 |
2.45e-27 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 108.20 E-value: 2.45e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 1 MTAALHIGHLSKSFQNTPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDS-----GEISLSGKTIFSKNTNL 75
Cdd:PRK14258 4 LIPAIKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNIYERRVNL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 76 PVRERRLGYLVQEGVLFPhLTVYRNIAYGLGNGKGRTAQERQRI-EAMLELTGISELAGRYPH----ELSGGQQQRVALA 150
Cdd:PRK14258 84 NRLRRQVSMVHPKPNLFP-MSVYDNVAYGVKIVGWRPKLEIDDIvESALKDADLWDEIKHKIHksalDLSGGQQQRLCIA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 151 RALAPDPELILLDEPFSALDEQLRRQIrEDMIAALRANGK-SAVFVSHDREEALQYADRIAVMKQ-----GRILQTASPH 224
Cdd:PRK14258 163 RALAVKPKVLLMDEPCFGLDPIASMKV-ESLIQSLRLRSElTMVIVSHNLHQVSRLSDFTAFFKGnenriGQLVEFGLTK 241
|
....*...
gi 1067578656 225 ELYRQPAD 232
Cdd:PRK14258 242 KIFNSPHD 249
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
3-230 |
2.51e-27 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 108.08 E-value: 2.51e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 3 AALHIGHLSKSFQNTPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGF-----EQPDSGEISLSGKTIFskntNLPV 77
Cdd:PRK14247 2 NKIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQDIF----KMDV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 78 RE--RRLGYLVQEGVLFPHLTVYRNIAYGLG-NGKGRTAQE-RQRIEAMLELTGI-SELAGRY---PHELSGGQQQRVAL 149
Cdd:PRK14247 78 IElrRRVQMVFQIPNPIPNLSIFENVALGLKlNRLVKSKKElQERVRWALEKAQLwDEVKDRLdapAGKLSGGQQQRLCI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 150 ARALAPDPELILLDEPFSALD-------EQLRRQIREDMiaalrangkSAVFVSHDREEALQYADRIAVMKQGRILQTAS 222
Cdd:PRK14247 158 ARALAFQPEVLLADEPTANLDpentakiESLFLELKKDM---------TIVLVTHFPQQAARISDYVAFLYKGQIVEWGP 228
|
....*...
gi 1067578656 223 PHELYRQP 230
Cdd:PRK14247 229 TREVFTNP 236
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
22-197 |
3.34e-27 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 106.04 E-value: 3.34e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 22 DISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIFSkntnlpVRE---RRLGYLVQEGVLFPHLTVY 98
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRR------QRDeyhQDLLYLGHQPGIKTELTAL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 99 RNIAYglgNGKGRTAQERQRIEAMLELTGiseLAGR--YP-HELSGGQQQRVALARALAPDPELILLDEPFSALDEQLRR 175
Cdd:PRK13538 93 ENLRF---YQRLHGPGDDEALWEALAQVG---LAGFedVPvRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGVA 166
|
170 180
....*....|....*....|..
gi 1067578656 176 QIrEDMIAALRANGKSAVFVSH 197
Cdd:PRK13538 167 RL-EALLAQHAEQGGMVILTTH 187
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
9-240 |
3.82e-27 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 108.26 E-value: 3.82e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 9 HLSKSFQNTPVLNDISLSLDPGEILFIIGASGCGKTTLLRCL-------AGFEQpdSGEISLSGKTIFSKNTNLPVReRR 81
Cdd:PRK14271 26 NLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLnrmndkvSGYRY--SGDVLLGGRSIFNYRDVLEFR-RR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 82 LGYLVQEGVLFPhLTVYRNIAYGLGNGKGRTAQE-RQRIEAMLELTG----ISELAGRYPHELSGGQQQRVALARALAPD 156
Cdd:PRK14271 103 VGMLFQRPNPFP-MSIMDNVLAGVRAHKLVPRKEfRGVAQARLTEVGlwdaVKDRLSDSPFRLSGGQQQLLCLARTLAVN 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 157 PELILLDEPFSALDEQLRRQIrEDMIAALrANGKSAVFVSHDREEALQYADRIAVMKQGRILQTASPHELYRQPADLDAA 236
Cdd:PRK14271 182 PEVLLLDEPTSALDPTTTEKI-EEFIRSL-ADRLTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKHAETA 259
|
....
gi 1067578656 237 LFIG 240
Cdd:PRK14271 260 RYVA 263
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-218 |
6.67e-27 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 106.50 E-value: 6.67e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 1 MTAALHIGHLSKSFQNTPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIFSKNTNLPVRER 80
Cdd:PRK11614 2 EKVMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMREA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 81 RLgyLVQEG-VLFPHLTVYRNIAYGlGNGKGRTaQERQRIEAMLEL-TGISELAGRYPHELSGGQQQRVALARALAPDPE 158
Cdd:PRK11614 82 VA--IVPEGrRVFSRMTVEENLAMG-GFFAERD-QFQERIKWVYELfPRLHERRIQRAGTMSGGEQQMLAIGRALMSQPR 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 159 LILLDEPFSALDEQLRRQIReDMIAALRANGKSAVFVSHDREEALQYADRIAVMKQGRIL 218
Cdd:PRK11614 158 LLLLDEPSLGLAPIIIQQIF-DTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHVV 216
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
5-202 |
7.14e-27 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 106.02 E-value: 7.14e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 5 LHIGHLSKSF----QNTPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIFSKNTN--LPVR 78
Cdd:PRK10584 7 VEVHHLKKSVgqgeHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEarAKLR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 79 ERRLGYLVQEGVLFPHLTVYRNIAY-GLGNGKgRTAQERQRIEAMLELTGISELAGRYPHELSGGQQQRVALARALAPDP 157
Cdd:PRK10584 87 AKHVGFVFQSFMLIPTLNALENVELpALLRGE-SSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRP 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1067578656 158 ELILLDEPFSALDEQLRRQIREDMIAALRANGKSAVFVSHDREEA 202
Cdd:PRK10584 166 DVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLA 210
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
20-252 |
7.29e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 107.49 E-value: 7.29e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 20 LNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIFSKNT-NLpvrERRLGYLVQE-GVLFPHLTV 97
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVwNL---RRKIGMVFQNpDNQFVGATV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 98 YRNIAYGLGNGKGRTAQERQRIEAMLELTGISELAGRYPHELSGGQQQRVALARALAPDPELILLDEPFSALDEQLRRQI 177
Cdd:PRK13642 100 EDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEI 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1067578656 178 REDMIAALRANGKSAVFVSHDREEALQyADRIAVMKQGRILQTASPHELYRQPADLdaaLFIGEGIVFPAALNAD 252
Cdd:PRK13642 180 MRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELFATSEDM---VEIGLDVPFSSNLMKD 250
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-229 |
7.91e-27 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 106.55 E-value: 7.91e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 1 MTAALHIGHLSKSFQNTPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIFSKNTN-LPVRE 79
Cdd:PRK11701 3 DQPLLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYaLSEAE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 80 RRL------GYLVQ---EGvLFPHLTVYRNIAYGL--------GNGKGRTAQERQRIEamLELTGISELagryPHELSGG 142
Cdd:PRK11701 83 RRRllrtewGFVHQhprDG-LRMQVSAGGNIGERLmavgarhyGDIRATAGDWLERVE--IDAARIDDL----PTTFSGG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 143 QQQRVALARALAPDPELILLDEPFSALDEQLrrQIR-EDMIAALRAN-GKSAVFVSHDREEALQYADRIAVMKQGRILQT 220
Cdd:PRK11701 156 MQQRLQIARNLVTHPRLVFMDEPTGGLDVSV--QARlLDLLRGLVRElGLAVVIVTHDLAVARLLAHRLLVMKQGRVVES 233
|
250
....*....|....*.
gi 1067578656 221 A-------SPHELYRQ 229
Cdd:PRK11701 234 GltdqvldDPQHPYTQ 249
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
5-229 |
1.08e-26 |
|
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: 106.07 E-value: 1.08e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 5 LHIGHLSKSFQNTPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKT-IFSKNTNLPVRERRLG 83
Cdd:TIGR02323 4 LQVSGLSKSYGGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMRSgAELELYQLSEAERRRL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 84 YLVQEGVLFPH------LTVY-------RNIAYGLGN-GKGRTAQERQRIEAMLELTGISELagryPHELSGGQQQRVAL 149
Cdd:TIGR02323 84 MRTEWGFVHQNprdglrMRVSaganigeRLMAIGARHyGNIRATAQDWLEEVEIDPTRIDDL----PRAFSGGMQQRLQI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 150 ARALAPDPELILLDEPFSALDEQLRRQIREDMIAALRANGKSAVFVSHDREEALQYADRIAVMKQGRILQTA-------S 222
Cdd:TIGR02323 160 ARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRVVESGltdqvldD 239
|
....*..
gi 1067578656 223 PHELYRQ 229
Cdd:TIGR02323 240 PQHPYTQ 246
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
15-226 |
1.21e-26 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 110.68 E-value: 1.21e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 15 QNTPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTI--FSKnTNLpvreRRLGYLVQEGV-L 91
Cdd:PRK11160 351 QPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIadYSE-AAL----RQAISVVSQRVhL 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 92 FPHlTVYRNIAYGLGNgkgrtAQERQRIEaMLELTGISELA-------------GRyphELSGGQQQRVALARALAPDPE 158
Cdd:PRK11160 426 FSA-TLRDNLLLAAPN-----ASDEALIE-VLQQVGLEKLLeddkglnawlgegGR---QLSGGEQRRLGIARALLHDAP 495
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 159 LILLDEPFSALDEQLRRQIredmIAALR--ANGKSAVFVSHdREEALQYADRIAVMKQGRILQTASPHEL 226
Cdd:PRK11160 496 LLLLDEPTEGLDAETERQI----LELLAehAQNKTVLMITH-RLTGLEQFDRICVMDNGQIIEQGTHQEL 560
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
2-231 |
1.31e-26 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 110.18 E-value: 1.31e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 2 TAALHIGHLSKSFQNT----PVLNDISLSLDPGEILFIIGASGCGKT-TLLRCLAGFEQPD----SGEISLSGKTIF--S 70
Cdd:PRK15134 3 QPLLAIENLSVAFRQQqtvrTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPvvypSGDIRFHGESLLhaS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 71 KNTNLPVRERRLGYLVQEGV--LFPHLTVYRNIAYGLGNGKG-RTAQERQRIEAMLELTGISELAGR---YPHELSGGQQ 144
Cdd:PRK15134 83 EQTLRGVRGNKIAMIFQEPMvsLNPLHTLEKQLYEVLSLHRGmRREAARGEILNCLDRVGIRQAAKRltdYPHQLSGGER 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 145 QRVALARALAPDPELILLDEPFSALDEQLRRQIREDMIAALRANGKSAVFVSHDREEALQYADRIAVMKQGRILQTASPH 224
Cdd:PRK15134 163 QRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAA 242
|
....*..
gi 1067578656 225 ELYRQPA 231
Cdd:PRK15134 243 TLFSAPT 249
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
19-218 |
1.55e-26 |
|
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: 105.05 E-value: 1.55e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 19 VLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPD---SGEISLSGKTIfSKNTNLpvreRRLGYLVQEGVLFPHL 95
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGgttSGQILFNGQPR-KPDQFQ----KCVAYVRQDDILLPGL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 96 TVYRNIAYGLGNGKGRTAQERQRiEAMLELTGISELA-----GRYPHELSGGQQQRVALARALAPDPELILLDEPFSALD 170
Cdd:cd03234 97 TVRETLTYTAILRLPRKSSDAIR-KKRVEDVLLRDLAltrigGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLD 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1067578656 171 EQLRRQIredmIAALR--ANGKSAVFVS-HD-REEALQYADRIAVMKQGRIL 218
Cdd:cd03234 176 SFTALNL----VSTLSqlARRNRIVILTiHQpRSDLFRLFDRILLLSSGEIV 223
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
14-218 |
3.41e-26 |
|
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: 104.34 E-value: 3.41e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 14 FQNTPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGktifskntNLPVrERRLGYLVQEGVLF- 92
Cdd:cd03267 31 YREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAG--------LVPW-KRRKKFLRRIGVVFg 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 93 ---------PHLTVYRNIA--YGLgnGKGRTAQERQRIEAMLELTGISELAGRyphELSGGQQQRVALARALAPDPELIL 161
Cdd:cd03267 102 qktqlwwdlPVIDSFYLLAaiYDL--PPARFKKRLDELSELLDLEELLDTPVR---QLSLGQRMRAEIAAALLHEPEILF 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1067578656 162 LDEPFSALDEQLRRQIREDMIAALRANGKSAVFVSHDREEALQYADRIAVMKQGRIL 218
Cdd:cd03267 177 LDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLL 233
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
13-230 |
5.55e-26 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 108.78 E-value: 5.55e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 13 SFQNTPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFeQPDSGEISLSGktIFSKNTNLPVRERRLGYLVQEGVLF 92
Cdd:PRK11174 359 SPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGF-LPYQGSLKING--IELRELDPESWRKHLSWVGQNPQLP 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 93 pHLTVYRNIAygLGNGkgrTAQErQRIEAMLELTGISELAGRYPH-----------ELSGGQQQRVALARALAPDPELIL 161
Cdd:PRK11174 436 -HGTLRDNVL--LGNP---DASD-EQLQQALENAWVSEFLPLLPQgldtpigdqaaGLSVGQAQRLALARALLQPCQLLL 508
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1067578656 162 LDEPFSALDEQLRRQIREDMIAAlrANGKSAVFVSHdREEALQYADRIAVMKQGRILQTASPHELYRQP 230
Cdd:PRK11174 509 LDEPTASLDAHSEQLVMQALNAA--SRRQTTLMVTH-QLEDLAQWDQIWVMQDGQIVQQGDYAELSQAG 574
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
10-210 |
6.70e-26 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 104.48 E-value: 6.70e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 10 LSKSFQNTPVLNDISLSLDPGEILFIIGASGCGKTTLLRC-------LAGFEQpdSGEISLSGKTIFSKNTNlPVR-ERR 81
Cdd:PRK14243 16 LNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCfnrlndlIPGFRV--EGKVTFHGKNLYAPDVD-PVEvRRR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 82 LGYLVQEGVLFPHlTVYRNIAYGLG-NG-KG----------RTAQERQRIEAMLELTGISelagrypheLSGGQQQRVAL 149
Cdd:PRK14243 93 IGMVFQKPNPFPK-SIYDNIAYGARiNGyKGdmdelverslRQAALWDEVKDKLKQSGLS---------LSGGQQQRLCI 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1067578656 150 ARALAPDPELILLDEPFSALDEQLRRQIrEDMIAALRANgKSAVFVSHDREEALQYADRIA 210
Cdd:PRK14243 163 ARAIAVQPEVILMDEPCSALDPISTLRI-EELMHELKEQ-YTIIIVTHNMQQAARVSDMTA 221
|
|
| FbpC_C_terminal |
pfam17845 |
FbpC C-terminal regulatory nucleotide binding domain; Most functional ABC transporters are ... |
295-349 |
1.19e-25 |
|
FbpC C-terminal regulatory nucleotide binding domain; Most functional ABC transporters are composed of at least four sub-units: two trans-membrane (TM) domains where the transport process takes place and two cytoplasmic nucleotide binding domains (NBDs) providing the energy required for active transport. This entry is one of the two NBDs found at the the C-terminal domain of FbpC, ferric iron uptake transporter, from the Neisseria gonorrhoeae. The C-terminal regulatory domain adopts two OB-folds per monomer. These are similar in topology to those seen in the NBD (nucleotide binding domain) from the maltose uptake ABC transporter, MalK. However, FbpC does not open as far as MalK when ATP is removed from their respective closed structures. This difference was suggested to be due to the substantial domain swap in the regulatory domain of FbpC.
Pssm-ID: 407710 Cd Length: 55 Bit Score: 97.36 E-value: 1.19e-25
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1067578656 295 IHAVVLKTTPKARHTEISLRAGQTVLTLNLPSAPTLSDGISAVLHLDGPALFFPG 349
Cdd:pfam17845 1 IHAVVLKTTPKARHTEISLRGGQTVLTLNLPSAPTLSDGISAVLHLDGPALFFPG 55
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
14-236 |
2.28e-25 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 103.16 E-value: 2.28e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 14 FQNTPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTI-FSKNTNLPVRERRLGYLVQEGVLF 92
Cdd:PRK13638 11 YQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLdYSKRGLLALRQQVATVFQDPEQQI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 93 PHLTVYRNIAYGLGNGKGRTAQERQRIEAMLELTGiselAGRYPHE----LSGGQQQRVALARALAPDPELILLDEPFSA 168
Cdd:PRK13638 91 FYTDIDSDIAFSLRNLGVPEAEITRRVDEALTLVD----AQHFRHQpiqcLSHGQKKRVAIAGALVLQARYLLLDEPTAG 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1067578656 169 LDEQLRRQiredMIAALR---ANGKSAVFVSHDREEALQYADRIAVMKQGRILQTASPHELYRQPADLDAA 236
Cdd:PRK13638 167 LDPAGRTQ----MIAIIRrivAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVFACTEAMEQA 233
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-220 |
2.44e-25 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 106.55 E-value: 2.44e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 1 MTAALHIGHLSKSFQNTPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFeQPD---SGEISLSGKTIFSKNtnlpV 77
Cdd:PRK13549 2 MEYLLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGV-YPHgtyEGEIIFEGEELQASN----I 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 78 RE-RRLGYLV--QEGVLFPHLTVYRNIAygLGN---GKGRTAQER--QRIEAMLELTGISELAGRYPHELSGGQQQRVAL 149
Cdd:PRK13549 77 RDtERAGIAIihQELALVKELSVLENIF--LGNeitPGGIMDYDAmyLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEI 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1067578656 150 ARALAPDPELILLDEPFSALDEQlRRQIREDMIAALRANGKSAVFVSHDREEALQYADRIAVMKQGRILQT 220
Cdd:PRK13549 155 AKALNKQARLLILDEPTASLTES-ETAVLLDIIRDLKAHGIACIYISHKLNEVKAISDTICVIRDGRHIGT 224
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-215 |
5.25e-25 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 105.64 E-value: 5.25e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 1 MTAALHIGHLSKSFQNTPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTiFSKNTNLPVRER 80
Cdd:PRK09700 2 ATPYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNIN-YNKLDHKLAAQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 81 RLGYLVQEGVLFPHLTVYRNIAYG-------LGNGKGRTAQERQRIEAMLELTGISELAGRYPHELSGGQQQRVALARAL 153
Cdd:PRK09700 81 GIGIIYQELSVIDELTVLENLYIGrhltkkvCGVNIIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1067578656 154 APDPELILLDEPFSALD----EQLRRQIREdmiaaLRANGKSAVFVSHDREEALQYADRIAVMKQG 215
Cdd:PRK09700 161 MLDAKVIIMDEPTSSLTnkevDYLFLIMNQ-----LRKEGTAIVYISHKLAEIRRICDRYTVMKDG 221
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
5-252 |
5.59e-25 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 101.79 E-value: 5.59e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 5 LHIGHLSKSF---------QNTPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIfsKNTNL 75
Cdd:PRK15112 5 LEVRNLSKTFryrtgwfrrQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPL--HFGDY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 76 PVRERRLGYLVQE--GVLFPHLTVYRNIAYGLGNGKGRTAQER-QRIEAMLELTGI-SELAGRYPHELSGGQQQRVALAR 151
Cdd:PRK15112 83 SYRSQRIRMIFQDpsTSLNPRQRISQILDFPLRLNTDLEPEQReKQIIETLRQVGLlPDHASYYPHMLAPGQKQRLGLAR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 152 ALAPDPELILLDEPFSALDEQLRRQIREDMIAALRANGKSAVFVSHDREEALQYADRIAVMKQGRILQTASPHELYRQPA 231
Cdd:PRK15112 163 ALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVLASPL 242
|
250 260
....*....|....*....|..
gi 1067578656 232 -DLDAALFIGEgivFPAALNAD 252
Cdd:PRK15112 243 hELTKRLIAGH---FGEALTAD 261
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
18-229 |
1.11e-24 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 104.90 E-value: 1.11e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 18 PVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIfSKNTNLPVReRRLGYLVQEGVLFpHLTV 97
Cdd:COG5265 372 PILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDI-RDVTQASLR-AAIGIVPQDTVLF-NDTI 448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 98 YRNIAYGlgngkgRTAQERQRIEAMLELTGISELAGRYPH-----------ELSGGQQQRVALARALAPDPELILLDEPF 166
Cdd:COG5265 449 AYNIAYG------RPDASEEEVEAAARAAQIHDFIESLPDgydtrvgerglKLSGGEKQRVAIARTLLKNPPILIFDEAT 522
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1067578656 167 SALDEQLRRQIRedmiAALR--ANGKSAVFVSHdREEALQYADRIAVMKQGRILQTASPHELYRQ 229
Cdd:COG5265 523 SALDSRTERAIQ----AALRevARGRTTLVIAH-RLSTIVDADEILVLEAGRIVERGTHAELLAQ 582
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
2-226 |
1.60e-24 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 100.83 E-value: 1.60e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 2 TAALHIGHLSKSFQNTPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTI---FSKNTnlpvr 78
Cdd:PRK10253 5 VARLRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIqhyASKEV----- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 79 ERRLGYLVQEGVLFPHLTVYRNIAYGLGNGKGRTAQERQRIE----AMLELTGISELAGRYPHELSGGQQQRVALARALA 154
Cdd:PRK10253 80 ARRIGLLAQNATTPGDITVQELVARGRYPHQPLFTRWRKEDEeavtKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1067578656 155 PDPELILLDEPFSALDEQLRRQIREDMIAALRANGKSAVFVSHDREEALQYADRIAVMKQGRILQTASPHEL 226
Cdd:PRK10253 160 QETAIMLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEI 231
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
5-226 |
1.89e-24 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 99.76 E-value: 1.89e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 5 LHIGHLSKSFQNTPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFE--QPDSGEISLSGKTIfsknTNLPVRER-R 81
Cdd:COG0396 1 LEIKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPkyEVTSGSILLDGEDI----LELSPDERaR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 82 LG--YLVQEGVLFPHLTVYR--NIAYGLGNGKGRTAQE-RQRIEAMLELTGISE-LAGRYPHE-LSGGQQQRVALARALA 154
Cdd:COG0396 77 AGifLAFQYPVEIPGVSVSNflRTALNARRGEELSAREfLKLLKEKMKELGLDEdFLDRYVNEgFSGGEKKRNEILQMLL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1067578656 155 PDPELILLDEPFSALD-EQLRrqIREDMIAALRANGKSAVFVSHdREEALQY--ADRIAVMKQGRILQTASPhEL 226
Cdd:COG0396 157 LEPKLAILDETDSGLDiDALR--IVAEGVNKLRSPDRGILIITH-YQRILDYikPDFVHVLVDGRIVKSGGK-EL 227
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
1-237 |
2.25e-24 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 100.34 E-value: 2.25e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 1 MTAALHIGHLSKSFQNT-PVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISlsgktIFSKNTNLPVRE 79
Cdd:PRK15056 3 QQAGIVVNDVTVTWRNGhTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKIS-----ILGQPTRQALQK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 80 RRLGYLVQEGVL---FPHLT--VYRNIAYG-LGNGKGRTAQERQRIEAMLELTGISELAGRYPHELSGGQQQRVALARAL 153
Cdd:PRK15056 78 NLVAYVPQSEEVdwsFPVLVedVVMMGRYGhMGWLRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 154 APDPELILLDEPFSALDEQLRRQIReDMIAALRANGKSAVFVSHDREEALQYADrIAVMKQGRILqTASPHELYRQPADL 233
Cdd:PRK15056 158 AQQGQVILLDEPFTGVDVKTEARII-SLLRELRDEGKTMLVSTHNLGSVTEFCD-YTVMVKGTVL-ASGPTETTFTAENL 234
|
....
gi 1067578656 234 DAAL 237
Cdd:PRK15056 235 ELAF 238
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
17-197 |
3.84e-24 |
|
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: 97.81 E-value: 3.84e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 17 TPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIfskNTNLPVRERRLGYLVQEGVLFPHLT 96
Cdd:TIGR01189 13 RMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPL---AEQRDEPHENILYLGHLPGLKPELS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 97 VYRNIAYGLGNGKGrtaqERQRIEAMLELTGISELAGRYPHELSGGQQQRVALARALAPDPELILLDEPFSALDEQLRRQ 176
Cdd:TIGR01189 90 ALENLHFWAAIHGG----AQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVAL 165
|
170 180
....*....|....*....|.
gi 1067578656 177 IREDMIAALrANGKSAVFVSH 197
Cdd:TIGR01189 166 LAGLLRAHL-ARGGIVLLTTH 185
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
5-226 |
4.66e-24 |
|
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: 102.96 E-value: 4.66e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 5 LHIGHLSKSFQNTPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQ--PDSGEI--------------------- 61
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQyePTSGRIiyhvalcekcgyverpskvge 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 62 --SLSGKTIFSKNTNL-----PVRE---RRLGYLVQEG-VLFPHLTVYRNIAYGLgNGKGRTAQERqrIEAMLELTGISE 130
Cdd:TIGR03269 81 pcPVCGGTLEPEEVDFwnlsdKLRRrirKRIAIMLQRTfALYGDDTVLDNVLEAL-EEIGYEGKEA--VGRAVDLIEMVQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 131 LAGRYPH---ELSGGQQQRVALARALAPDPELILLDEPFSALDEQLRRQIREDMIAALRANGKSAVFVSHDREEALQYAD 207
Cdd:TIGR03269 158 LSHRITHiarDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDLSD 237
|
250
....*....|....*....
gi 1067578656 208 RIAVMKQGRILQTASPHEL 226
Cdd:TIGR03269 238 KAIWLENGEIKEEGTPDEV 256
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
21-219 |
5.01e-24 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 102.56 E-value: 5.01e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 21 NDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIfSKNTNLPVRERRLGYLVQ---EGVLFPHLTV 97
Cdd:PRK09700 280 RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDI-SPRSPLDAVKKGMAYITEsrrDNGFFPNFSI 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 98 YRNIA-------------YGLGNGK--GRTAQErQRIEAMLELTGISELAGryphELSGGQQQRVALARALAPDPELILL 162
Cdd:PRK09700 359 AQNMAisrslkdggykgaMGLFHEVdeQRTAEN-QRELLALKCHSVNQNIT----ELSGGNQQKVLISKWLCCCPEVIIF 433
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1067578656 163 DEPFSALDEQLRRQIREDMiAALRANGKSAVFVSHDREEALQYADRIAVMKQGRILQ 219
Cdd:PRK09700 434 DEPTRGIDVGAKAEIYKVM-RQLADDGKVILMVSSELPEIITVCDRIAVFCEGRLTQ 489
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
5-220 |
7.98e-24 |
|
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: 102.21 E-value: 7.98e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 5 LHIGHLSKSFQNTPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDS--GEISLSGKTIFSKNtnlpVRE-RR 81
Cdd:TIGR02633 2 LEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTwdGEIYWSGSPLKASN----IRDtER 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 82 LGYLV--QEGVLFPHLTVYRNIAYG----LGNGKGRTAQERQRIEAMLELTGISEL-AGRYPHELSGGQQQRVALARALA 154
Cdd:TIGR02633 78 AGIVIihQELTLVPELSVAENIFLGneitLPGGRMAYNAMYLRAKNLLRELQLDADnVTRPVGDYGGGQQQLVEIAKALN 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1067578656 155 PDPELILLDEPFSALDEQlRRQIREDMIAALRANGKSAVFVSHDREEALQYADRIAVMKQGRILQT 220
Cdd:TIGR02633 158 KQARLLILDEPSSSLTEK-ETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQHVAT 222
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
19-230 |
9.10e-24 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 98.71 E-value: 9.10e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 19 VLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIFSKNTNLPVRErrLGYLVQEGVLFPHLTVY 98
Cdd:PRK10575 26 LLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARK--VAYLPQQLPAAEGMTVR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 99 RNIA---YGLGNGKGRTAQE-RQRIEAMLELTGISELAGRYPHELSGGQQQRVALARALAPDPELILLDEPFSALDeqLR 174
Cdd:PRK10575 104 ELVAigrYPWHGALGRFGAAdREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALD--IA 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 175 RQIreDMIAAL----RANGKSAVFVSHDREEALQYADRIAVMKQGRILQTASPHELYRQP 230
Cdd:PRK10575 182 HQV--DVLALVhrlsQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRGE 239
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
15-230 |
9.18e-24 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 102.10 E-value: 9.18e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 15 QNTPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIfsKNTNLPVRERRLGYLVQEGVLFPH 94
Cdd:PRK10789 326 TDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPL--TKLQLDSWRSRLAVVSQTPFLFSD 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 95 lTVYRNIAYGlgngkgRTAQERQRIEAMLELTGISELAGRYPH-----------ELSGGQQQRVALARALAPDPELILLD 163
Cdd:PRK10789 404 -TVANNIALG------RPDATQQEIEHVARLASVHDDILRLPQgydtevgergvMLSGGQKQRISIARALLLNAEILILD 476
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1067578656 164 EPFSALDEQLRRQIREDmiaaLRANGKS-AVFVSHDREEALQYADRIAVMKQGRILQTASPHELYRQP 230
Cdd:PRK10789 477 DALSAVDGRTEHQILHN----LRQWGEGrTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQS 540
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
20-227 |
1.34e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 98.54 E-value: 1.34e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 20 LNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTI---FSKNTNLPVRERRLGYLVQ--EGVLFPH 94
Cdd:PRK13645 27 LNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIpanLKKIKEVKRLRKEIGLVFQfpEYQLFQE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 95 lTVYRNIAYGLGNGKGRTAQERQRIEAMLELTGI-SELAGRYPHELSGGQQQRVALARALAPDPELILLDEPFSALDEQL 173
Cdd:PRK13645 107 -TIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLpEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKG 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1067578656 174 rrqiREDMIAA-LRAN---GKSAVFVSHDREEALQYADRIAVMKQGRILQTASPHELY 227
Cdd:PRK13645 186 ----EEDFINLfERLNkeyKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIF 239
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
4-239 |
1.90e-23 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 101.74 E-value: 1.90e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 4 ALHIGHLSKSFQNTPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIFSKntnlpvRER--- 80
Cdd:NF033858 1 VARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMADA------RHRrav 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 81 --RLGYLVQeGV---LFPHLTVYRNIA-----YGLGngkgrtAQER-QRIEAMLELTGISELAGRYPHELSGGQQQRVAL 149
Cdd:NF033858 75 cpRIAYMPQ-GLgknLYPTLSVFENLDffgrlFGQD------AAERrRRIDELLRATGLAPFADRPAGKLSGGMKQKLGL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 150 ARALAPDPELILLDEPFSALDEQLRRQIREdMIAALRAN--GKSAVFVSHDREEALQYaDRIAVMKQGRILQTASPHELY 227
Cdd:NF033858 148 CCALIHDPDLLILDEPTTGVDPLSRRQFWE-LIDRIRAErpGMSVLVATAYMEEAERF-DWLVAMDAGRVLATGTPAELL 225
|
250
....*....|....
gi 1067578656 228 RQ--PADLDAAlFI 239
Cdd:NF033858 226 ARtgADTLEAA-FI 238
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
9-210 |
2.35e-23 |
|
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: 100.78 E-value: 2.35e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 9 HLSKSFQNTPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLsGKTIfskntnlpvrerRLGYLVQE 88
Cdd:TIGR03719 327 NLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETV------------KLAYVDQS 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 89 -GVLFPHLTVYRNIAYG-----LGNgkgRTAQERQRIEAmLELTGISE--LAGryphELSGGQQQRVALARALAPDPELI 160
Cdd:TIGR03719 394 rDALDPNKTVWEEISGGldiikLGK---REIPSRAYVGR-FNFKGSDQqkKVG----QLSGGERNRVHLAKTLKSGGNVL 465
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1067578656 161 LLDEPFSALD-EQLRRQirEDmiaALRANGKSAVFVSHDReealQYADRIA 210
Cdd:TIGR03719 466 LLDEPTNDLDvETLRAL--EE---ALLNFAGCAVVISHDR----WFLDRIA 507
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1-261 |
2.61e-23 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 100.46 E-value: 2.61e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 1 MTAALHIGHLSKSFQNTPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIfskNTNLP--VR 78
Cdd:PRK10762 1 MQALLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEV---TFNGPksSQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 79 ERRLGYLVQEGVLFPHLTVYRNIAYG--LGNGKGRTAQERQRIEA--MLELTGISELAGRYPHELSGGQQQRVALARALA 154
Cdd:PRK10762 78 EAGIGIIHQELNLIPQLTIAENIFLGreFVNRFGRIDWKKMYAEAdkLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 155 PDPELILLDEPFSAL----DEQLRRQIREdmiaaLRANGKSAVFVSHDREEALQYADRIAVMKQGRilqtasphelyrqp 230
Cdd:PRK10762 158 FESKVIIMDEPTDALtdteTESLFRVIRE-----LKSQGRGIVYISHRLKEIFEICDDVTVFRDGQ-------------- 218
|
250 260 270
....*....|....*....|....*....|.
gi 1067578656 231 adldaalFIGEGIVfpAALNADGTADCRLGR 261
Cdd:PRK10762 219 -------FIAEREV--ADLTEDSLIEMMVGR 240
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
9-240 |
2.94e-23 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 100.97 E-value: 2.94e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 9 HLSKSFQN-TPVlNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIFSKNtnLPVReRRLGYLVQ 87
Cdd:NF033858 271 GLTMRFGDfTAV-DHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDAGD--IATR-RRVGYMSQ 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 88 EGVLFPHLTVYRNIA-----YGLGngkgrTAQERQRIEAMLELTGISELAGRYPHELSGGQQQRVALARALAPDPELILL 162
Cdd:NF033858 347 AFSLYGELTVRQNLElharlFHLP-----AAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLIL 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 163 DEPFSALDEQLRRQIREDMIAALRaNGKSAVFVS-HDREEAlQYADRIAVMKQGRILQTASPHELY--RQPADLDAAlFI 239
Cdd:NF033858 422 DEPTSGVDPVARDMFWRLLIELSR-EDGVTIFIStHFMNEA-ERCDRISLMHAGRVLASDTPAALVaaRGAATLEEA-FI 498
|
.
gi 1067578656 240 G 240
Cdd:NF033858 499 A 499
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
23-230 |
3.55e-23 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 96.54 E-value: 3.55e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 23 ISLSLDPGEILFIIGASGCGKTTLLRCLAGFeQPDSGEISLSGKTIfsknTNLPVRE--RRLGYLVQEGVLFPHLTVYRN 100
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGL-LPGSGSIQFAGQPL----EAWSAAElaRHRAYLSQQQTPPFAMPVFQY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 101 IAYGLGNGkGRTAQERQRIEAMLELTGISELAGRYPHELSGGQQQRVALA-------RALAPDPELILLDEPFSALD--E 171
Cdd:PRK03695 90 LTLHQPDK-TRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAavvlqvwPDINPAGQLLLLDEPMNSLDvaQ 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1067578656 172 Q--LRRQIREdmiaaLRANGKSAVFVSHDREEALQYADRIAVMKQGRILQTASPHELYRQP 230
Cdd:PRK03695 169 QaaLDRLLSE-----LCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVLTPE 224
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
16-229 |
3.94e-23 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 100.48 E-value: 3.94e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 16 NTPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIfskntnlpvRERRLGYL------VQEG 89
Cdd:PRK11176 355 EVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDL---------RDYTLASLrnqvalVSQN 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 90 VlfpHL---TVYRNIAYGlgngkgRTAQ-ERQRIEAMLELTGISELAGRYPH-----------ELSGGQQQRVALARALA 154
Cdd:PRK11176 426 V---HLfndTIANNIAYA------RTEQySREQIEEAARMAYAMDFINKMDNgldtvigengvLLSGGQRQRIAIARALL 496
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1067578656 155 PDPELILLDEPFSALDEQLRRQIREdMIAALRANgKSAVFVSHdREEALQYADRIAVMKQGRILQTASPHELYRQ 229
Cdd:PRK11176 497 RDSPILILDEATSALDTESERAIQA-ALDELQKN-RTSLVIAH-RLSTIEKADEILVVEDGEIVERGTHAELLAQ 568
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
8-235 |
6.30e-23 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 99.35 E-value: 6.30e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 8 GHLSKSFQNTPVLN----------DISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIfsknTNLPV 77
Cdd:PRK15439 257 GNRRQQAAGAPVLTvedltgegfrNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEI----NALST 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 78 RERRLGYLV------QEGVLFPHLTVYRNIAYGLGNGKG---RTAQERQRIEAMLELTGIselagRYPHE------LSGG 142
Cdd:PRK15439 333 AQRLARGLVylpedrQSSGLYLDAPLAWNVCALTHNRRGfwiKPARENAVLERYRRALNI-----KFNHAeqaartLSGG 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 143 QQQRVALARALAPDPELILLDEPFSALDEQLRRQIReDMIAALRANGKSAVFVSHDREEALQYADRIAVMKQGRIlqtas 222
Cdd:PRK15439 408 NQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIY-QLIRSIAAQNVAVLFISSDLEEIEQMADRVLVMHQGEI----- 481
|
250
....*....|...
gi 1067578656 223 PHELYRQPADLDA 235
Cdd:PRK15439 482 SGALTGAAINVDT 494
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
5-229 |
6.89e-23 |
|
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: 94.52 E-value: 6.89e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 5 LHIGHLSKSFQNTPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFE--QPDSGEISLSGKTIfsknTNLPVRER-R 81
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKGEDI----TDLPPEERaR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 82 LGYLV--QEGVLFPHLTV---YRNIAYGlgngkgrtaqerqrieamleltgiselagrypheLSGGQQQRVALARALAPD 156
Cdd:cd03217 77 LGIFLafQYPPEIPGVKNadfLRYVNEG----------------------------------FSGGEKKRNEILQLLLLE 122
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1067578656 157 PELILLDEPFSALD-EQLRrqIREDMIAALRANGKSAVFVSHdREEALQY--ADRIAVMKQGRILQTASPhELYRQ 229
Cdd:cd03217 123 PDLAILDEPDSGLDiDALR--LVAEVINKLREEGKSVLIITH-YQRLLDYikPDRVHVLYDGRIVKSGDK-ELALE 194
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
6-237 |
7.19e-23 |
|
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: 96.46 E-value: 7.19e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 6 HIGHLSKSFQN-----TPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIFSKntnlpvrer 80
Cdd:cd03291 34 SSDDNNLFFSNlclvgAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGRISFSS--------- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 81 rlgylvQEGVLFPHlTVYRNIAYGLgngkgrtAQERQRIEAMLELTGISELAGRYPHE-----------LSGGQQQRVAL 149
Cdd:cd03291 105 ------QFSWIMPG-TIKENIIFGV-------SYDEYRYKSVVKACQLEEDITKFPEKdntvlgeggitLSGGQRARISL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 150 ARALAPDPELILLDEPFSALDEQLRRQIREDMIAALRANgKSAVFVShDREEALQYADRIAVMKQGRILQTASPHELYRQ 229
Cdd:cd03291 171 ARAVYKDADLYLLDSPFGYLDVFTEKEIFESCVCKLMAN-KTRILVT-SKMEHLKKADKILILHEGSSYFYGTFSELQSL 248
|
....*...
gi 1067578656 230 PADLDAAL 237
Cdd:cd03291 249 RPDFSSKL 256
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
16-215 |
1.42e-22 |
|
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: 94.32 E-value: 1.42e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 16 NTPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIFSKNTNLPVRERR--LGYLVQEGVLFp 93
Cdd:cd03290 13 GLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRNRysVAYAAQKPWLL- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 94 HLTVYRNIAYGlgngkgrTAQERQRIEAMLELTGISELAGRYPH-----------ELSGGQQQRVALARALAPDPELILL 162
Cdd:cd03290 92 NATVEENITFG-------SPFNKQRYKAVTDACSLQPDIDLLPFgdqteigergiNLSGGQRQRICVARALYQNTNIVFL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1067578656 163 DEPFSALDEQLRRQI-REDMIAALRANGKSAVFVSHdREEALQYADRIAVMKQG 215
Cdd:cd03290 165 DDPFSALDIHLSDHLmQEGILKFLQDDKRTLVLVTH-KLQYLPHADWIIAMKDG 217
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
18-197 |
2.44e-22 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 93.01 E-value: 2.44e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 18 PVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIfsknTNLPVRERrLGYLVQEGVLFPHLTV 97
Cdd:PRK13539 16 VLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDI----DDPDVAEA-CHYLGHRNAMKPALTV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 98 YRNIA-----YGlgngkgrtaQERQRIEAMLELTGISELAGRYPHELSGGQQQRVALARALAPDPELILLDEPFSALDEQ 172
Cdd:PRK13539 91 AENLEfwaafLG---------GEELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAA 161
|
170 180
....*....|....*....|....*
gi 1067578656 173 LRRQIrEDMIAALRANGKSAVFVSH 197
Cdd:PRK13539 162 AVALF-AELIRAHLAQGGIVIAATH 185
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
15-231 |
3.23e-22 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 97.62 E-value: 3.23e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 15 QNTPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIFSKNTNL------------PVRERRL 82
Cdd:PRK10261 27 QKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRRRSRQVielseqsaaqmrHVRGADM 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 83 GYLVQEGV--LFPHLTVYRNIAYGL----GNGKGRTAQERQRieaMLELTGISE---LAGRYPHELSGGQQQRVALARAL 153
Cdd:PRK10261 107 AMIFQEPMtsLNPVFTVGEQIAESIrlhqGASREEAMVEAKR---MLDQVRIPEaqtILSRYPHQLSGGMRQRVMIAMAL 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1067578656 154 APDPELILLDEPFSALDEQLRRQIREdMIAALRANGKSAV-FVSHDREEALQYADRIAVMKQGRILQTASPHELYRQPA 231
Cdd:PRK10261 184 SCRPAVLIADEPTTALDVTIQAQILQ-LIKVLQKEMSMGViFITHDMGVVAEIADRVLVMYQGEAVETGSVEQIFHAPQ 261
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
18-217 |
3.38e-22 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 97.38 E-value: 3.38e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 18 PVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIfskNTNLP----------VRERR------ 81
Cdd:PRK10762 266 PGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEV---VTRSPqdglangivyISEDRkrdglv 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 82 LGYLVQEGVLFPHLTVYRNIAYGLgngkgRTAQERQRIEAMLELTGIselagRYPH------ELSGGQQQRVALARALAP 155
Cdd:PRK10762 343 LGMSVKENMSLTALRYFSRAGGSL-----KHADEQQAVSDFIRLFNI-----KTPSmeqaigLLSGGNQQKVAIARGLMT 412
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1067578656 156 DPELILLDEPFSALDEQLRRQIReDMIAALRANGKSAVFVSHDREEALQYADRIAVMKQGRI 217
Cdd:PRK10762 413 RPKVLILDEPTRGVDVGAKKEIY-QLINQFKAEGLSIILVSSEMPEVLGMSDRILVMHEGRI 473
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
2-215 |
9.43e-22 |
|
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: 97.01 E-value: 9.43e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 2 TAALHIGHLSKSFQNT--PVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIFsknTNLPVRE 79
Cdd:TIGR01257 1935 TDILRLNELTKVYSGTssPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSIL---TNISDVH 2011
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 80 RRLGYLVQEGVLFPHLTvYRNIAYGLGNGKGRTAQERQRIEAM-LELTGISELAGRYPHELSGGQQQRVALARALAPDPE 158
Cdd:TIGR01257 2012 QNMGYCPQFDAIDDLLT-GREHLYLYARLRGVPAEEIEKVANWsIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPP 2090
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1067578656 159 LILLDEPFSALDEQLRRQIREDMIAALRaNGKSAVFVSHDREEALQYADRIAVMKQG 215
Cdd:TIGR01257 2091 LVLLDEPTTGMDPQARRMLWNTIVSIIR-EGRAVVLTSHSMEECEALCTRLAIMVKG 2146
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
20-218 |
1.09e-21 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 94.00 E-value: 1.09e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 20 LNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTifskntnlPVRERRlGYLVQEGV-------LF 92
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYV--------PFKRRK-EFARRIGVvfgqrsqLW 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 93 PHLTVY------RNIaYGLGNgkgrtAQERQRIEAMLELTGISELAGRYPHELSGGQQQRVALARALAPDPELILLDEPF 166
Cdd:COG4586 109 WDLPAIdsfrllKAI-YRIPD-----AEYKKRLDELVELLDLGELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPT 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1067578656 167 SALDEQLRRQIREdMIAALRANGKSAVFV-SHDRE--EALqyADRIAVMKQGRIL 218
Cdd:COG4586 183 IGLDVVSKEAIRE-FLKEYNRERGTTILLtSHDMDdiEAL--CDRVIVIDHGRII 234
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
20-239 |
1.10e-21 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 96.27 E-value: 1.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 20 LNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPD---SGEISLSGKTIfskntNLPVRERRLGYLVQEGVLFPHLT 96
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGMPI-----DAKEMRAISAYVQQDDLFIPTLT 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 97 VYRNIAYG----LGNgKGRTAQERQRIEAMLELTGISELA-------GRYpHELSGGQQQRVALARALAPDPELILLDEP 165
Cdd:TIGR00955 116 VREHLMFQahlrMPR-RVTKKEKRERVDEVLQALGLRKCAntrigvpGRV-KGLSGGERKRLAFASELLTDPPLLFCDEP 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 166 FSALDEQLRRQIredmIAALRA---NGKSAVFVSHD-REEALQYADRIAVMKQGRILQTASPHEL--------YRQPADL 233
Cdd:TIGR00955 194 TSGLDSFMAYSV----VQVLKGlaqKGKTIICTIHQpSSELFELFDKIILMAEGRVAYLGSPDQAvpffsdlgHPCPENY 269
|
....*.
gi 1067578656 234 DAALFI 239
Cdd:TIGR00955 270 NPADFY 275
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
3-230 |
1.35e-21 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 93.65 E-value: 1.35e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 3 AALHIGHLSKSF--QNTP--VLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFeqpdsgeISLSGKTI-----FSKN- 72
Cdd:PRK11022 2 ALLNVDKLSVHFgdESAPfrAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGL-------IDYPGRVMaekleFNGQd 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 73 -TNLPVRERR------LGYLVQEGV--LFPHLTVYRNIAYGL-----GNGKGRtaqeRQRIEAMLELTGISELAGR---Y 135
Cdd:PRK11022 75 lQRISEKERRnlvgaeVAMIFQDPMtsLNPCYTVGFQIMEAIkvhqgGNKKTR----RQRAIDLLNQVGIPDPASRldvY 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 136 PHELSGGQQQRVALARALAPDPELILLDEPFSALDEQLRRQIREDMIAALRANGKSAVFVSHDREEALQYADRIAVMKQG 215
Cdd:PRK11022 151 PHQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAG 230
|
250
....*....|....*
gi 1067578656 216 RILQTASPHELYRQP 230
Cdd:PRK11022 231 QVVETGKAHDIFRAP 245
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
21-237 |
1.81e-21 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 94.98 E-value: 1.81e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 21 NDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIFSKNTNLPVR-------ERRlgylVQEGVlFP 93
Cdd:PRK11288 270 EPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRDAIRagimlcpEDR----KAEGI-IP 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 94 HLTVYRNI----------AYGLGNGKGRTAQERQRIEAMLELTGISELAGRYpheLSGGQQQRVALARALAPDPELILLD 163
Cdd:PRK11288 345 VHSVADNInisarrhhlrAGCLINNRWEAENADRFIRSLNIKTPSREQLIMN---LSGGNQQKAILGRWLSEDMKVILLD 421
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1067578656 164 EPFSALDEQLRRQIReDMIAALRANGKSAVFVSHDREEALQYADRIAVMKQGRILQtasphELYRQPADLDAAL 237
Cdd:PRK11288 422 EPTRGIDVGAKHEIY-NVIYELAAQGVAVLFVSSDLPEVLGVADRIVVMREGRIAG-----ELAREQATERQAL 489
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
13-237 |
2.22e-21 |
|
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: 95.75 E-value: 2.22e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 13 SFQNTPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIFSKNTNLpvrerrlgylvqegvLF 92
Cdd:TIGR01271 435 SLYVTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGRISFSPQTSW---------------IM 499
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 93 PHlTVYRNIAYGLgngkgrtAQERQRIEAMLELTGISELAGRYPHE-----------LSGGQQQRVALARALAPDPELIL 161
Cdd:TIGR01271 500 PG-TIKDNIIFGL-------SYDEYRYTSVIKACQLEEDIALFPEKdktvlgeggitLSGGQRARISLARAVYKDADLYL 571
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1067578656 162 LDEPFSALDEQLRRQIREDMIAALRANgKSAVFVShDREEALQYADRIAVMKQGRILQTASPHELYRQPADLDAAL 237
Cdd:TIGR01271 572 LDSPFTHLDVVTEKEIFESCLCKLMSN-KTRILVT-SKLEHLKKADKILLLHEGVCYFYGTFSELQAKRPDFSSLL 645
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
5-199 |
2.42e-21 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 90.39 E-value: 2.42e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 5 LHIGHLSKSFQNTPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIfskNTNLPVRERRLGY 84
Cdd:PRK13540 2 LDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSI---KKDLCTYQKQLCF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 85 LVQEGVLFPHLTVYRNIAYGLgngkgRTAQERQRIEAMLELTGISELAGRYPHELSGGQQQRVALARALAPDPELILLDE 164
Cdd:PRK13540 79 VGHRSGINPYLTLRENCLYDI-----HFSPGAVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDE 153
|
170 180 190
....*....|....*....|....*....|....*
gi 1067578656 165 PFSALDEQLRRQIREDmIAALRANGKSAVFVSHDR 199
Cdd:PRK13540 154 PLVALDELSLLTIITK-IQEHRAKGGAVLLTSHQD 187
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
5-228 |
2.88e-21 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 91.81 E-value: 2.88e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 5 LHIGHLSKSFQNTPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGfEQPDS---------GEISLSGKTIFSKNTNL 75
Cdd:PRK13547 2 LTADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAG-DLTGGgaprgarvtGDVTLNGEPLAAIDAPR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 76 PVR---------ERRLGYLVQEGVL---FPHLTvyrniayglgNGKGRTAQERQRIEAMLELTGISELAGRYPHELSGGQ 143
Cdd:PRK13547 81 LARlravlpqaaQPAFAFSAREIVLlgrYPHAR----------RAGALTHRDGEIAWQALALAGATALVGRDVTTLSGGE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 144 QQRVALARALA---------PDPELILLDEPFSALDEQLRRQIREDMIAALRANGKSAVFVSHDREEALQYADRIAVMKQ 214
Cdd:PRK13547 151 LARVQFARVLAqlwpphdaaQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLAD 230
|
250
....*....|....
gi 1067578656 215 GRILQTASPHELYR 228
Cdd:PRK13547 231 GAIVAHGAPADVLT 244
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
23-226 |
5.98e-21 |
|
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: 93.71 E-value: 5.98e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 23 ISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIFSKNtnlpvRE--RRLGYLV-QEGVLFPHLtvyr 99
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADN-----REayRQLFSAVfSDFHLFDRL---- 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 100 niaYGLGNgkgrtAQERQRIEAMLELTGISEL----AGRY-PHELSGGQQQRVALARALAPDPELILLDEPFSALDEQLR 174
Cdd:COG4615 422 ---LGLDG-----EADPARARELLERLELDHKvsveDGRFsTTDLSQGQRKRLALLVALLEDRPILVFDEWAADQDPEFR 493
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1067578656 175 RQIREDMIAALRANGKSAVFVSHDReealQY---ADRIAVMKQGRILQTASPHEL 226
Cdd:COG4615 494 RVFYTELLPELKARGKTVIAISHDD----RYfdlADRVLKMDYGKLVELTGPAAL 544
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
19-197 |
7.31e-21 |
|
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: 89.09 E-value: 7.31e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 19 VLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIfskNTNLPVRERRLGYLVQEGVLFPHLTVY 98
Cdd:cd03231 15 LFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPL---DFQRDSIARGLLYLGHAPGIKTTLSVL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 99 RNIAYglgngkGRTAQERQRIEAMLELTGISELAGRYPHELSGGQQQRVALARALAPDPELILLDEPFSALDEQLRRQIR 178
Cdd:cd03231 92 ENLRF------WHADHSDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFA 165
|
170
....*....|....*....
gi 1067578656 179 EDMiAALRANGKSAVFVSH 197
Cdd:cd03231 166 EAM-AGHCARGGMVVLTTH 183
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-198 |
8.41e-21 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 90.17 E-value: 8.41e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 1 MTAALHIGHLSKSFQNTPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTifskntnlpvrer 80
Cdd:PRK09544 1 MTSLVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKL------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 81 RLGYLVQEGVLFPH--LTVYRNIAYGLGNGKGRTAQERQRIEAmleltgiSELAGRYPHELSGGQQQRVALARALAPDPE 158
Cdd:PRK09544 68 RIGYVPQKLYLDTTlpLTVNRFLRLRPGTKKEDILPALKRVQA-------GHLIDAPMQKLSGGETQRVLLARALLNRPQ 140
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1067578656 159 LILLDEPFSALDEQLRRQIReDMIAALRANGKSAVF-VSHD 198
Cdd:PRK09544 141 LLVLDEPTQGVDVNGQVALY-DLIDQLRRELDCAVLmVSHD 180
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
9-210 |
1.78e-20 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 92.49 E-value: 1.78e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 9 HLSKSFQNTPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLsGKTIfskntnlpvrerRLGYLVQE 88
Cdd:PRK11819 329 NLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GETV------------KLAYVDQS 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 89 -GVLFPHLTVYRNIAYG-----LG-------------NGKGRTAQERqrieamleltgiselAGryphELSGGQQQRVAL 149
Cdd:PRK11819 396 rDALDPNKTVWEEISGGldiikVGnreipsrayvgrfNFKGGDQQKK---------------VG----VLSGGERNRLHL 456
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1067578656 150 ARALAPDPELILLDEPFSALD-EQLRRQirEDmiaALRANGKSAVFVSHDReealQYADRIA 210
Cdd:PRK11819 457 AKTLKQGGNVLLLDEPTNDLDvETLRAL--EE---ALLEFPGCAVVISHDR----WFLDRIA 509
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
15-209 |
4.95e-20 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 85.67 E-value: 4.95e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 15 QNTPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISL--SGKTIFskntnLPVRerrlGYLVQeGVLf 92
Cdd:cd03223 12 DGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMpeGEDLLF-----LPQR----PYLPL-GTL- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 93 phltvyrniayglgngkgrtaqeRQRIeamleltgiselagRYP--HELSGGQQQRVALARALAPDPELILLDEPFSALD 170
Cdd:cd03223 81 -----------------------REQL--------------IYPwdDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALD 123
|
170 180 190
....*....|....*....|....*....|....*....
gi 1067578656 171 EQLRRQIREdmiaALRANGKSAVFVSHdREEALQYADRI 209
Cdd:cd03223 124 EESEDRLYQ----LLKELGITVISVGH-RPSLWKFHDRV 157
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
20-217 |
6.30e-20 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 90.80 E-value: 6.30e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 20 LNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIFSKNtnlPVRERRLGYLVQEGV-LFPHLTvy 98
Cdd:PRK10522 339 VGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQ---PEDYRKLFSAVFTDFhLFDQLL-- 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 99 rniayglgnGKGRTAQERQRIEAMLELTGISE----LAGRYPH-ELSGGQQQRVALARALAPDPELILLDEPFSALDEQL 173
Cdd:PRK10522 414 ---------GPEGKPANPALVEKWLERLKMAHklelEDGRISNlKLSKGQKKRLALLLALAEERDILLLDEWAADQDPHF 484
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1067578656 174 RRQIREDMIAALRANGKSAVFVSHDrEEALQYADRIAVMKQGRI 217
Cdd:PRK10522 485 RREFYQVLLPLLQEMGKTIFAISHD-DHYFIHADRLLEMRNGQL 527
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
9-226 |
1.16e-19 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 90.02 E-value: 1.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 9 HLSKSFQNT-PVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIfsKNTNLPVRERRLGYLVQ 87
Cdd:PRK13657 339 DVSFSYDNSrQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDI--RTVTRASLRRNIAVVFQ 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 88 EGVLFPhltvyRNIAYGLGNGKG-------RTAQERQRIEAMLE--LTGISELAGRYPHELSGGQQQRVALARALAPDPE 158
Cdd:PRK13657 417 DAGLFN-----RSIEDNIRVGRPdatdeemRAAAERAQAHDFIErkPDGYDTVVGERGRQLSGGERQRLAIARALLKDPP 491
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1067578656 159 LILLDEPFSALDEQLRRQIREdMIAALRANgkSAVFVSHDREEALQYADRIAVMKQGRILQTASPHEL 226
Cdd:PRK13657 492 ILILDEATSALDVETEAKVKA-ALDELMKG--RTTFIIAHRLSTVRNADRILVFDNGRVVESGSFDEL 556
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
21-231 |
1.46e-19 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 87.86 E-value: 1.46e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 21 NDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPD---SGEISLSGKTIFskntNLPvrERRLGYLVQEGV------- 90
Cdd:PRK09473 33 NDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANgriGGSATFNGREIL----NLP--EKELNKLRAEQIsmifqdp 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 91 ---LFPHLTVYRNIAYGL----GNGKGRTAQERQRieaMLELTGISELAGR---YPHELSGGQQQRVALARALAPDPELI 160
Cdd:PRK09473 107 mtsLNPYMRVGEQLMEVLmlhkGMSKAEAFEESVR---MLDAVKMPEARKRmkmYPHEFSGGMRQRVMIAMALLCRPKLL 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1067578656 161 LLDEPFSALDEQLRRQIREDMIAALRANGKSAVFVSHDREEALQYADRIAVMKQGRILQTASPHELYRQPA 231
Cdd:PRK09473 184 IADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARDVFYQPS 254
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
6-170 |
1.99e-19 |
|
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: 89.22 E-value: 1.99e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 6 HIGHLSKSFQ-NTPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLS-GKTIfskntnlpvrerrlG 83
Cdd:TIGR03719 6 TMNRVSKVVPpKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQpGIKV--------------G 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 84 YLVQEGVLFPHLTVYRNIAYGLGNGKG--------------------RTAQERQRIEAMLELTGISEL---------AGR 134
Cdd:TIGR03719 72 YLPQEPQLDPTKTVRENVEEGVAEIKDaldrfneisakyaepdadfdKLAAEQAELQEIIDAADAWDLdsqleiamdALR 151
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1067578656 135 YP------HELSGGQQQRVALARALAPDPELILLDEPFSALD 170
Cdd:TIGR03719 152 CPpwdadvTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLD 193
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
11-218 |
2.15e-19 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 89.55 E-value: 2.15e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 11 SKSFQNTPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDsgeiSLSGKTIfsKNTNLPVRE--RRLGYLVQE 88
Cdd:PLN03211 75 TRQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGN----NFTGTIL--ANNRKPTKQilKRTGFVTQD 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 89 GVLFPHLTVYRNIAYG--LGNGKGRTAQERQRI-EAMLELTGISE-----LAGRYPHELSGGQQQRVALARALAPDPELI 160
Cdd:PLN03211 149 DILYPHLTVRETLVFCslLRLPKSLTKQEKILVaESVISELGLTKcentiIGNSFIRGISGGERKRVSIAHEMLINPSLL 228
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1067578656 161 LLDEPFSALDEQLRRQIREDMiAALRANGKSAVFVSHD-REEALQYADRIAVMKQGRIL 218
Cdd:PLN03211 229 ILDEPTSGLDATAAYRLVLTL-GSLAQKGKTIVTSMHQpSSRVYQMFDSVLVLSEGRCL 286
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
4-217 |
3.00e-19 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 88.80 E-value: 3.00e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 4 ALHIGHLSKSFQNTPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISlsgktiFSKNTNlpvrerrLG 83
Cdd:PRK15064 319 ALEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVK------WSENAN-------IG 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 84 YLVQEGV--------LFPHLTVYRniayglgngkgRTAQERQRIEAML-ELTGISELAGRYPHELSGGQQQRVALARALA 154
Cdd:PRK15064 386 YYAQDHAydfendltLFDWMSQWR-----------QEGDDEQAVRGTLgRLLFSQDDIKKSVKVLSGGEKGRMLFGKLMM 454
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1067578656 155 PDPELILLDEPFSALD-EQLrrqirEDMIAALRANGKSAVFVSHDREEALQYADRIAVMKQGRI 217
Cdd:PRK15064 455 QKPNVLVMDEPTNHMDmESI-----ESLNMALEKYEGTLIFVSHDREFVSSLATRIIEITPDGV 513
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
11-220 |
3.21e-19 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 88.31 E-value: 3.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 11 SKSFQNTPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAG------FEqpdsGEISLSGKTIFSKNTNlpvRERRLGY 84
Cdd:NF040905 8 TKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGvyphgsYE----GEILFDGEVCRFKDIR---DSEALGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 85 LV--QEGVLFPHLTVYRNIAygLGNGKGRT-----AQERQRIEAMLELTGISELAGRYPHELSGGQQQRVALARALAPDP 157
Cdd:NF040905 81 VIihQELALIPYLSIAENIF--LGNERAKRgvidwNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDV 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1067578656 158 ELILLDEPFSALDEQLRRQIReDMIAALRANGKSAVFVSHDREEALQYADRIAVMKQGRILQT 220
Cdd:NF040905 159 KLLILDEPTAALNEEDSAALL-DLLLELKAQGITSIIISHKLNEIRRVADSITVLRDGRTIET 220
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
20-211 |
3.67e-19 |
|
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: 85.54 E-value: 3.67e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 20 LNDISLSLDPG-----EILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIFSKNTNLPVRerrlgylvQEGvlfph 94
Cdd:cd03237 10 LGEFTLEVEGGsisesEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSYKPQYIKAD--------YEG----- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 95 lTVyRNIAYGLGNGKGRTAQERQRIEAMLELTGISElagRYPHELSGGQQQRVALARALAPDPELILLDEPFSALD-EQl 173
Cdd:cd03237 77 -TV-RDLLSSITKDFYTHPYFKTEIAKPLQIEQILD---REVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDvEQ- 150
|
170 180 190
....*....|....*....|....*....|....*....
gi 1067578656 174 rRQIREDMIAALRANGKSAVFV-SHDREEALQYADRIAV 211
Cdd:cd03237 151 -RLMASKVIRRFAENNEKTAFVvEHDIIMIDYLADRLIV 188
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
10-193 |
4.17e-19 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 84.52 E-value: 4.17e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 10 LSKSFQNTPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIFSKNtnlpvRERRLGYLVQEG 89
Cdd:PRK13543 17 LAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGD-----RSRFMAYLGHLP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 90 VLFPHLTVYRNIAYgLGNGKGRTAQerQRIEAMLELTGISELAGRYPHELSGGQQQRVALARA-LAPDPeLILLDEPFSA 168
Cdd:PRK13543 92 GLKADLSTLENLHF-LCGLHGRRAK--QMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLwLSPAP-LWLLDEPYAN 167
|
170 180
....*....|....*....|....*
gi 1067578656 169 LDEQLRRQIREDMIAALRANGKSAV 193
Cdd:PRK13543 168 LDLEGITLVNRMISAHLRGGGAALV 192
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
20-237 |
5.38e-19 |
|
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: 87.96 E-value: 5.38e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 20 LNDISLSLDPGEILFIIGASGCGKTTLLRCLAG-FEQPDSGEISLSGKTIFSKNtnlPVRERRLGY-LVQE-----GVLf 92
Cdd:TIGR02633 276 VDDVSFSLRRGEILGVAGLVGAGRTELVQALFGaYPGKFEGNVFINGKPVDIRN---PAQAIRAGIaMVPEdrkrhGIV- 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 93 PHLTVYRNIAYGLGN---GKGR--TAQERQRIEAmleltGISELAGRYPH------ELSGGQQQRVALARALAPDPELIL 161
Cdd:TIGR02633 352 PILGVGKNITLSVLKsfcFKMRidAAAELQIIGS-----AIQRLKVKTASpflpigRLSGGNQQKAVLAKMLLTNPRVLI 426
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1067578656 162 LDEPFSALDEQLRRQIREdMIAALRANGKSAVFVSHDREEALQYADRIAVMKQGRILQTASPHELyRQPADLDAAL 237
Cdd:TIGR02633 427 LDEPTRGVDVGAKYEIYK-LINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGKLKGDFVNHAL-TQEQVLAAAL 500
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
17-204 |
5.86e-19 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 84.24 E-value: 5.86e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 17 TPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFE--QPDSGEISLSGKTIfskNTNLPVRERrlgylvqegvlfph 94
Cdd:COG2401 43 RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDVPDNQF---GREASLIDA-------------- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 95 ltVYRniayglgngKGRTAQERQRIEAMleltGISE--LAGRYPHELSGGQQQRVALARALAPDPELILLDEPFSALDEQ 172
Cdd:COG2401 106 --IGR---------KGDFKDAVELLNAV----GLSDavLWLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQ 170
|
170 180 190
....*....|....*....|....*....|....
gi 1067578656 173 LRRQIREDMIAALRANGKSAVFVSH--DREEALQ 204
Cdd:COG2401 171 TAKRVARNLQKLARRAGITLVVATHhyDVIDDLQ 204
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
18-231 |
8.45e-19 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 84.37 E-value: 8.45e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 18 PVLNDISLSLDPGEILFIIGASGCGKTtlLRCLA-------GFEQPdSGEISLSGKTIFSKNtnlpVRERRLGYLVQEG- 89
Cdd:PRK10418 17 PLVHGVSLTLQRGRVLALVGGSGSGKS--LTCAAalgilpaGVRQT-AGRVLLDGKPVAPCA----LRGRKIATIMQNPr 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 90 VLFPHLTVYRNIAYGLGNGKGRTAQERQRIEAMlELTGISE---LAGRYPHELSGGQQQRVALARALAPDPELILLDEPF 166
Cdd:PRK10418 90 SAFNPLHTMHTHARETCLALGKPADDATLTAAL-EAVGLENaarVLKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPT 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1067578656 167 SALDEQLRRQIREDMIAALRANGKSAVFVSHDREEALQYADRIAVMKQGRILQTASPHELYRQPA 231
Cdd:PRK10418 169 TDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPK 233
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
18-223 |
1.12e-18 |
|
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: 83.23 E-value: 1.12e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 18 PVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIfsKNTNLPVRERRLGYLVQEGVLFPHlTV 97
Cdd:cd03369 22 PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDI--STIPLEDLRSSLTIIPQDPTLFSG-TI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 98 YRNI-AYGlgngkgrtAQERQRIEAMLELTGISElagryphELSGGQQQRVALARALAPDPELILLDEPFSALDEQ---- 172
Cdd:cd03369 99 RSNLdPFD--------EYSDEEIYGALRVSEGGL-------NLSQGQRQLLCLARALLKRPRVLVLDEATASIDYAtdal 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1067578656 173 LRRQIREDMiaalraNGKSAVFVSHDREEALQYaDRIAVMKQGRILQTASP 223
Cdd:cd03369 164 IQKTIREEF------TNSTILTIAHRLRTIIDY-DKILVMDAGEVKEYDHP 207
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
5-217 |
4.57e-18 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 85.17 E-value: 4.57e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 5 LHIGHLSKsfQNTPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIFSKNTN--------LP 76
Cdd:PRK10982 251 LEVRNLTS--LRQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANeainhgfaLV 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 77 VRERR----LGYL-VQEGVLFPHLTVYRNiAYGLGNGKGRTAQERQRIEAM-LELTGISELAGryphELSGGQQQRVALA 150
Cdd:PRK10982 329 TEERRstgiYAYLdIGFNSLISNIRNYKN-KVGLLDNSRMKSDTQWVIDSMrVKTPGHRTQIG----SLSGGNQQKVIIG 403
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1067578656 151 RALAPDPELILLDEPFSALDEQLRRQIREdMIAALRANGKSAVFVSHDREEALQYADRIAVMKQGRI 217
Cdd:PRK10982 404 RWLLTQPEILMLDEPTRGIDVGAKFEIYQ-LIAELAKKDKGIIIISSEMPELLGITDRILVMSNGLV 469
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
18-223 |
4.69e-18 |
|
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: 81.77 E-value: 4.69e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 18 PVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIfsknTNLPVRE--RRLGYLVQEGVLFPHl 95
Cdd:cd03244 18 PVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDI----SKIGLHDlrSRISIIPQDPVLFSG- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 96 TVYRNIA-YGLgngkgrtAQERQRIEAmLELTG----ISELAGRYPHE-------LSGGQQQRVALARALAPDPELILLD 163
Cdd:cd03244 93 TIRSNLDpFGE-------YSDEELWQA-LERVGlkefVESLPGGLDTVveeggenLSVGQRQLLCLARALLRKSKILVLD 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1067578656 164 EPFSALDEQLRRQIREdmiaALRANGKSA--VFVSHdREEALQYADRIAVMKQGRILQTASP 223
Cdd:cd03244 165 EATASVDPETDALIQK----TIREAFKDCtvLTIAH-RLDTIIDSDRILVLDKGRVVEFDSP 221
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
10-220 |
5.61e-18 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 84.78 E-value: 5.61e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 10 LSKSFQNTPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIFSKNTNLPVrERRLGYLVQEG 89
Cdd:PRK10982 4 ISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEAL-ENGISMVHQEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 90 VLFPHLTVYRNIAYGLGNGKGRTAQER---QRIEAMLELTGISELAGRYPHELSGGQQQRVALARALAPDPELILLDEPF 166
Cdd:PRK10982 83 NLVLQRSVMDNMWLGRYPTKGMFVDQDkmyRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPT 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1067578656 167 SALDEQLRRQIREdMIAALRANGKSAVFVSHDREEALQYADRIAVMKQGRILQT 220
Cdd:PRK10982 163 SSLTEKEVNHLFT-IIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQWIAT 215
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
20-198 |
8.34e-18 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 84.47 E-value: 8.34e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 20 LNDISLSLDPGEI-----LFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIF-----SKNTNLPVRErrlgYLVQEG 89
Cdd:PRK13409 350 LGDFSLEVEGGEIyegevIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELKISYkpqyiKPDYDGTVED----LLRSIT 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 90 VLFPHLTVYRNIAYGLGngkgrtaqerqrIEAMLEltgiselagRYPHELSGGQQQRVALARALAPDPELILLDEPFSAL 169
Cdd:PRK13409 426 DDLGSSYYKSEIIKPLQ------------LERLLD---------KNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHL 484
|
170 180 190
....*....|....*....|....*....|....*..
gi 1067578656 170 D-EQ-------LRRQIREdmiaalraNGKSAVFVSHD 198
Cdd:PRK13409 485 DvEQrlavakaIRRIAEE--------REATALVVDHD 513
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
19-217 |
9.59e-18 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 84.21 E-value: 9.59e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 19 VLNDISLSLDPGEILFIIGASGCGKTTLLRCLAG-FEQPDSGEISLSGKTIFSKNtnlPVRERRLGY-LVQE-----GVL 91
Cdd:PRK13549 277 RVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGaYPGRWEGEIFIDGKPVKIRN---PQQAIAQGIaMVPEdrkrdGIV 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 92 fPHLTVYRNIAYG-LGNGKGRTaqerqRIEAMLELTGISE----LAGRYPH------ELSGGQQQRVALARALAPDPELI 160
Cdd:PRK13549 354 -PVMGVGKNITLAaLDRFTGGS-----RIDDAAELKTILEsiqrLKVKTASpelaiaRLSGGNQQKAVLAKCLLLNPKIL 427
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1067578656 161 LLDEPFSALDEQLRRQIREdMIAALRANGKSAVFVSHDREEALQYADRIAVMKQGRI 217
Cdd:PRK13549 428 ILDEPTRGIDVGAKYEIYK-LINQLVQQGVAIIVISSELPEVLGLSDRVLVMHEGKL 483
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
5-227 |
3.75e-17 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 82.69 E-value: 3.75e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 5 LHIGHLSksFQNTPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGfEQP-DSGEISLSGKTIFSKNTNLPVRERR-- 81
Cdd:PRK11147 6 IHGAWLS--FSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNG-EVLlDDGRIIYEQDLIVARLQQDPPRNVEgt 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 82 -LGYlVQEGV--LFPHLTVYRNIAYGLGN-------GKGRTAQER----------QRIEAMLELTGIS---ELAgryphE 138
Cdd:PRK11147 83 vYDF-VAEGIeeQAEYLKRYHDISHLVETdpseknlNELAKLQEQldhhnlwqleNRINEVLAQLGLDpdaALS-----S 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 139 LSGGQQQRVALARALAPDPELILLDEPFSALD-------EQLrrqiredmiaaLRANGKSAVFVSHDREEALQYADRIAV 211
Cdd:PRK11147 157 LSGGWLRKAALGRALVSNPDVLLLDEPTNHLDietiewlEGF-----------LKTFQGSIIFISHDRSFIRNMATRIVD 225
|
250
....*....|....*.
gi 1067578656 212 MKQGRILQTASPHELY 227
Cdd:PRK11147 226 LDRGKLVSYPGNYDQY 241
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
18-226 |
4.03e-17 |
|
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: 83.07 E-value: 4.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 18 PVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIFskntnLPVRERRLGYLVQEGVLFphltv 97
Cdd:TIGR00957 652 PTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSVAY-----VPQQAWIQNDSLRENILF----- 721
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 98 yrniayglgngkGRTAQE---RQRIEAMLELTGISELAGRYPHE-------LSGGQQQRVALARALAPDPELILLDEPFS 167
Cdd:TIGR00957 722 ------------GKALNEkyyQQVLEACALLPDLEILPSGDRTEigekgvnLSGGQKQRVSLARAVYSNADIYLFDDPLS 789
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 168 ALDEQLRRQIREDMIAALRA-NGKSAVFVSHDReEALQYADRIAVMKQGRILQTASPHEL 226
Cdd:TIGR00957 790 AVDAHVGKHIFEHVIGPEGVlKNKTRILVTHGI-SYLPQVDVIIVMSGGKISEMGSYQEL 848
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
13-202 |
7.82e-17 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 81.21 E-value: 7.82e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 13 SFQNTPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAG-FEQPDSGEISL------SGKTIFSKntnlpvrERRLGYL 85
Cdd:PRK10938 269 SYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGdHPQGYSNDLTLfgrrrgSGETIWDI-------KKHIGYV 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 86 VQEgvlfPHL-----TVYRN-IAYGLGNGKG--RTAQERQRIEAM--LELTGISELAGRYP-HELSGGQQQRVALARALA 154
Cdd:PRK10938 342 SSS----LHLdyrvsTSVRNvILSGFFDSIGiyQAVSDRQQKLAQqwLDILGIDKRTADAPfHSLSWGQQRLALIVRALV 417
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1067578656 155 PDPELILLDEPFSALDEqLRRQIREDMIAALRANGKSA-VFVSHDREEA 202
Cdd:PRK10938 418 KHPTLLILDEPLQGLDP-LNRQLVRRFVDVLISEGETQlLFVSHHAEDA 465
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
20-198 |
9.00e-17 |
|
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: 81.37 E-value: 9.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 20 LNDISLSLDPG-----EILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIF-----SKNTNLPVRErrlgYLvqEG 89
Cdd:COG1245 351 YGGFSLEVEGGeiregEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLKISYkpqyiSPDYDGTVEE----FL--RS 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 90 VLFPHLT---VYRNIAYGLGngkgrtaqerqrIEAMLEltgiselagRYPHELSGGQQQRVALARALAPDPELILLDEPF 166
Cdd:COG1245 425 ANTDDFGssyYKTEIIKPLG------------LEKLLD---------KNVKDLSGGELQRVAIAACLSRDADLYLLDEPS 483
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1067578656 167 SALD-EQ-------LRRQIREdmiaalraNGKSAVFVSHD 198
Cdd:COG1245 484 AHLDvEQrlavakaIRRFAEN--------RGKTAMVVDHD 515
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
10-170 |
9.05e-17 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 81.32 E-value: 9.05e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 10 LSKSF-QNTPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLS-GKTIfskntnlpvrerrlGYLVQ 87
Cdd:PRK11819 12 VSKVVpPKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPApGIKV--------------GYLPQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 88 EGVLFPHLTVYRNIAYGLGNGKG--------------------RTAQERQRIEAMLELTGISEL---------AGRYPH- 137
Cdd:PRK11819 78 EPQLDPEKTVRENVEEGVAEVKAaldrfneiyaayaepdadfdALAAEQGELQEIIDAADAWDLdsqleiamdALRCPPw 157
|
170 180 190
....*....|....*....|....*....|....*...
gi 1067578656 138 -----ELSGGQQQRVALARALAPDPELILLDEPFSALD 170
Cdd:PRK11819 158 dakvtKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLD 195
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
3-286 |
9.66e-17 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 79.95 E-value: 9.66e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 3 AALHIGHLSKSFQnTP-----VLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFeQPDSGEIS-----LSGKTIfskn 72
Cdd:COG4170 2 PLLDIRNLTIEID-TPqgrvkAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGI-TKDNWHVTadrfrWNGIDL---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 73 TNLPVRERR------LGYLVQE--GVLFPHLTVYRNIAYGLGNG--KG----RTAQERQRIEAMLELTGI---SELAGRY 135
Cdd:COG4170 76 LKLSPRERRkiigreIAMIFQEpsSCLDPSAKIGDQLIEAIPSWtfKGkwwqRFKWRKKRAIELLHRVGIkdhKDIMNSY 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 136 PHELSGGQQQRVALARALAPDPELILLDEPFSALDEQLRRQI-RedMIAAL-RANGKSAVFVSHDREEALQYADRIAVMK 213
Cdd:COG4170 156 PHELTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIfR--LLARLnQLQGTSILLISHDLESISQWADTITVLY 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 214 QGRILQTASPHELYRQP------ADLDAALFIGEGIVFPAALNA-DGTA--------DCRLG-RLP------VQsgAPAG 271
Cdd:COG4170 234 CGQTVESGPTEQILKSPhhpytkALLRSMPDFRQPLPHKSRLNTlPGSIpplqhlpiGCRLGpRCPyaqkkcVE--TPRL 311
|
330
....*....|....*
gi 1067578656 272 TRgtllIRPEQFSLH 286
Cdd:COG4170 312 RK----IKGHEFACH 322
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
5-230 |
3.51e-16 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 78.31 E-value: 3.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 5 LHIGHLSKSFQNT--PV--LNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQpDSGEISlSGKTIFSKNT--NLPVR 78
Cdd:PRK15093 4 LDIRNLTIEFKTSdgWVkaVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTK-DNWRVT-ADRMRFDDIDllRLSPR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 79 ERR------LGYLVQE--GVLFPHLTVYRNIAYGLGNG--KGRTAQ-----ERQRIEaMLELTGISE---LAGRYPHELS 140
Cdd:PRK15093 82 ERRklvghnVSMIFQEpqSCLDPSERVGRQLMQNIPGWtyKGRWWQrfgwrKRRAIE-LLHRVGIKDhkdAMRSFPYELT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 141 GGQQQRVALARALAPDPELILLDEPFSALDEQLRRQIREDMIAALRANGKSAVFVSHDREEALQYADRIAVMKQGRILQT 220
Cdd:PRK15093 161 EGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTVET 240
|
250
....*....|
gi 1067578656 221 ASPHELYRQP 230
Cdd:PRK15093 241 APSKELVTTP 250
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
11-217 |
3.86e-16 |
|
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: 75.76 E-value: 3.86e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 11 SKSFQNTPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEqpdSGEISLSGKTIFSKNTNLPVRERRLG---YLVQ 87
Cdd:cd03233 14 GKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRT---EGNVSVEGDIHYNGIPYKEFAEKYPGeiiYVSE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 88 EGVLFPHLTVyrniayglgngkgrtaqeRQRIEAMLELTGiselaGRYPHELSGGQQQRVALARALAPDPELILLDEPFS 167
Cdd:cd03233 91 EDVHFPTLTV------------------RETLDFALRCKG-----NEFVRGISGGERKRVSIAEALVSRASVLCWDNSTR 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1067578656 168 ALDEqlrrQIREDMIAALRANG---KSAVFVS--HDREEALQYADRIAVMKQGRI 217
Cdd:cd03233 148 GLDS----STALEILKCIRTMAdvlKTTTFVSlyQASDEIYDLFDKVLVLYEGRQ 198
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
15-172 |
9.24e-16 |
|
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: 74.59 E-value: 9.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 15 QNTPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPD--SGEISLSGKtifSKNTNLPvreRRLGYLVQEGVLF 92
Cdd:cd03232 18 GKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAGviTGEILINGR---PLDKNFQ---RSTGYVEQQDVHS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 93 PHLTVYrniayglgngkgrtaqERQRIEAMLEltgiselagryphELSGGQQQRVALARALAPDPELILLDEPFSALDEQ 172
Cdd:cd03232 92 PNLTVR----------------EALRFSALLR-------------GLSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQ 142
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
16-225 |
2.64e-15 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 77.38 E-value: 2.64e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 16 NTPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGF------------------------EQPD-------------- 57
Cdd:PTZ00265 1180 NVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFydlkndhhivfknehtndmtneqdYQGDeeqnvgmknvnefs 1259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 58 ----------------SGEISLSGKTIFSKNtnlpVRERR--LGYLVQEGVLFpHLTVYRNIAYGLGNGKGRTAQERQRI 119
Cdd:PTZ00265 1260 ltkeggsgedstvfknSGKILLDGVDICDYN----LKDLRnlFSIVSQEPMLF-NMSIYENIKFGKEDATREDVKRACKF 1334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 120 EAMLELtgISEL-------AGRYPHELSGGQQQRVALARALAPDPELILLDEPFSALDEQLRRQIREDMIAALRANGKSA 192
Cdd:PTZ00265 1335 AAIDEF--IESLpnkydtnVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTI 1412
|
250 260 270
....*....|....*....|....*....|....*..
gi 1067578656 193 VFVSHdREEALQYADRIAVM----KQGRILQTASPHE 225
Cdd:PTZ00265 1413 ITIAH-RIASIKRSDKIVVFnnpdRTGSFVQAHGTHE 1448
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
5-222 |
3.96e-15 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 74.29 E-value: 3.96e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 5 LHIGHLSKSFQNTPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGfeQPD----SGEISLSGKTIfsknTNLPVRER 80
Cdd:CHL00131 8 LEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG--HPAykilEGDILFKGESI----LDLEPEER 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 81 -RLGYLV--QEGVLFPHLTV--YRNIAYglgNGKgRTAQERQRIEAMLELTGISE---LAGRYPHEL--------SGGQQ 144
Cdd:CHL00131 82 aHLGIFLafQYPIEIPGVSNadFLRLAY---NSK-RKFQGLPELDPLEFLEIINEklkLVGMDPSFLsrnvnegfSGGEK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 145 QRVALARALAPDPELILLDEPFSALDEQLRRQIREDmIAALRANGKSAVFVSHdREEALQY--ADRIAVMKQGRILQTAS 222
Cdd:CHL00131 158 KRNEILQMALLDSELAILDETDSGLDIDALKIIAEG-INKLMTSENSIILITH-YQRLLDYikPDYVHVMQNGKIIKTGD 235
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
16-206 |
9.08e-15 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 71.83 E-value: 9.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 16 NTPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEislsgktIFSKNTNL-PVRERRLGYLVQEGVLFPH 94
Cdd:PRK13541 12 EQKNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGN-------IYYKNCNInNIAKPYCTYIGHNLGLKLE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 95 LTVYRNIAYGlgngkGRTAQERQRIEAMLELTGISELAGRYPHELSGGQQQRVALARALAPDPELILLDEPFSALDEQlR 174
Cdd:PRK13541 85 MTVFENLKFW-----SEIYNSAETLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKE-N 158
|
170 180 190
....*....|....*....|....*....|..
gi 1067578656 175 RQIREDMIaALRANGKSAVFVSHDREEALQYA 206
Cdd:PRK13541 159 RDLLNNLI-VMKANSGGIVLLSSHLESSIKSA 189
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
14-217 |
1.34e-14 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 75.20 E-value: 1.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 14 FQNTP--VLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEIslsgktifskntnlpVRERRLGYLVQEGVL 91
Cdd:PTZ00243 668 FELEPkvLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV---------------WAERSIAYVPQQAWI 732
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 92 FpHLTVYRNIAYGLGNGKGRTAQERQ--RIEAMLEL--TGISELAGRYPHELSGGQQQRVALARALAPDPELILLDEPFS 167
Cdd:PTZ00243 733 M-NATVRGNILFFDEEDAARLADAVRvsQLEADLAQlgGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLS 811
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1067578656 168 ALDEQLRRQIREDMI-AALRanGKSAVFVSHdREEALQYADRIAVMKQGRI 217
Cdd:PTZ00243 812 ALDAHVGERVVEECFlGALA--GKTRVLATH-QVHVVPRADYVVALGDGRV 859
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
18-226 |
3.77e-14 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 74.00 E-value: 3.77e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 18 PVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGfEQPdsgeiSLSGKTIFSKNTnlpvrerrLGYLVQEGVLFpHLTV 97
Cdd:PLN03130 631 PTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLG-ELP-----PRSDASVVIRGT--------VAYVPQVSWIF-NATV 695
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 98 YRNIAYGLgngkgrtAQERQRIEAMLELTGISE----LAGRYPHE-------LSGGQQQRVALARALAPDPELILLDEPF 166
Cdd:PLN03130 696 RDNILFGS-------PFDPERYERAIDVTALQHdldlLPGGDLTEigergvnISGGQKQRVSMARAVYSNSDVYIFDDPL 768
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1067578656 167 SALDEQLRRQIREDMIA-ALRanGKSAVFVShDREEALQYADRIAVMKQGRILQTASPHEL 226
Cdd:PLN03130 769 SALDAHVGRQVFDKCIKdELR--GKTRVLVT-NQLHFLSQVDRIILVHEGMIKEEGTYEEL 826
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
18-228 |
4.36e-14 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 73.47 E-value: 4.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 18 PVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGfeqpdsgEISlsgktiFSKNTNLPVRERrLGYLVQEGVLFpHLTV 97
Cdd:PLN03232 631 PTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLG-------ELS------HAETSSVVIRGS-VAYVPQVSWIF-NATV 695
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 98 YRNIAYGlgngkgrTAQERQRIEAMLELTGISE----LAGRYPHEL-------SGGQQQRVALARALAPDPELILLDEPF 166
Cdd:PLN03232 696 RENILFG-------SDFESERYWRAIDVTALQHdldlLPGRDLTEIgergvniSGGQKQRVSMARAVYSNSDIYIFDDPL 768
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1067578656 167 SALDEQLRRQIREDMIA-ALRanGKSAVFVShDREEALQYADRIAVMKQGRILQTASPHELYR 228
Cdd:PLN03232 769 SALDAHVAHQVFDSCMKdELK--GKTRVLVT-NQLHFLPLMDRIILVSEGMIKEEGTFAELSK 828
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
5-212 |
6.55e-14 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 72.35 E-value: 6.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 5 LHIGHLSKSFQNTPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSgktiFSKNTNLPVRErrLGY 84
Cdd:PRK10938 4 LQISQGTFRLSDTKTLQLPSLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQ----FSHITRLSFEQ--LQK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 85 LVQEgvlfphlTVYRNIAYGLGNGK---GRTAQE--------RQRIEAMLELTGISELAGRYPHELSGGQQQRVALARAL 153
Cdd:PRK10938 78 LVSD-------EWQRNNTDMLSPGEddtGRTTAEiiqdevkdPARCEQLAQQFGITALLDRRFKYLSTGETRKTLLCQAL 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1067578656 154 APDPELILLDEPFSALDEQLRRQIREdMIAALRANGKSAVFVSHDREEALQYADRIAVM 212
Cdd:PRK10938 151 MSEPDLLILDEPFDGLDVASRQQLAE-LLASLHQSGITLVLVLNRFDEIPDFVQFAGVL 208
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
19-226 |
6.95e-13 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 69.81 E-value: 6.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 19 VLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIFSKNtnlpVRE--RRLGYLVQEGVLFPHlT 96
Cdd:PTZ00243 1325 VLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYG----LRElrRQFSMIPQDPVLFDG-T 1399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 97 VYRNI-------------AYGLGNGKGRTAQERQRIEAMLeLTGISelagryphELSGGQQQRVALARA-LAPDPELILL 162
Cdd:PTZ00243 1400 VRQNVdpfleassaevwaALELVGLRERVASESEGIDSRV-LEGGS--------NYSVGQRQLMCMARAlLKKGSGFILM 1470
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1067578656 163 DEPFSALDEQLRRQIREDMIAALRANgkSAVFVSHDREEALQYaDRIAVMKQGRILQTASPHEL 226
Cdd:PTZ00243 1471 DEATANIDPALDRQIQATVMSAFSAY--TVITIAHRLHTVAQY-DKIIVMDHGAVAEMGSPREL 1531
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
7-226 |
7.91e-13 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 69.36 E-value: 7.91e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 7 IGHLSKSFQN-TPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIFSkntnLPVRERRLGY- 84
Cdd:PRK10790 343 IDNVSFAYRDdNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSS----LSHSVLRQGVa 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 85 LVQEGVLFPHLTVYRNIAYglgngkGRTAQERQRIEAmLELTGISELAGRYP-----------HELSGGQQQRVALARAL 153
Cdd:PRK10790 419 MVQQDPVVLADTFLANVTL------GRDISEEQVWQA-LETVQLAELARSLPdglytplgeqgNNLSVGQKQLLALARVL 491
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1067578656 154 APDPELILLDEPFSALDEQLRRQIREdMIAALRANgKSAVFVSHdREEALQYADRIAVMKQGRILQTASPHEL 226
Cdd:PRK10790 492 VQTPQILILDEATANIDSGTEQAIQQ-ALAAVREH-TTLVVIAH-RLSTIVEADTILVLHRGQAVEQGTHQQL 561
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
116-303 |
8.37e-13 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 68.61 E-value: 8.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 116 RQRIEAMLELTGISELAGRYPHELSGGQQQRVALARALAPDPELILLDEPFSALDEQLRRQIREDMIAALRaNGKSAVFV 195
Cdd:NF000106 122 RARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVR-DGATVLLT 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 196 SHDREEALQYADRIAVMKQGRILQTASPHELYRQ------------PADLDAALfigeGIVFPAALN--ADGTADCRLG- 260
Cdd:NF000106 201 TQYMEEAEQLAHELTVIDRGRVIADGKVDELKTKvggrtlqirpahAAELDRMV----GAIAQAGLDgiAGATADHEDGv 276
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1067578656 261 -RLPV----QSGAPAGTRGTllirpEQFSLHPHSAPAASIHAVVLKTT 303
Cdd:NF000106 277 vNVPIvsdeQLSAVVGMLGE-----RGFTISGHQHPSAQL*EVFLAIT 319
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
5-199 |
1.09e-12 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 69.04 E-value: 1.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 5 LHIGHLSKSFQNTPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSgKTIfskntnlpvrerRLGY 84
Cdd:PRK10636 313 LKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLA-KGI------------KLGY 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 85 LVQEGVLF--------PHLTvyrniayglgngkgRTAQerQRIEAMLE--LTG-------ISELAGRYphelSGGQQQRV 147
Cdd:PRK10636 380 FAQHQLEFlradesplQHLA--------------RLAP--QELEQKLRdyLGGfgfqgdkVTEETRRF----SGGEKARL 439
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1067578656 148 ALARALAPDPELILLDEPFSALDEQLRRQIREDMI---AALrangksaVFVSHDR 199
Cdd:PRK10636 440 VLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIdfeGAL-------VVVSHDR 487
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
15-212 |
3.68e-12 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 67.75 E-value: 3.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 15 QNTPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIFsKNTNLPVRERRLGYLVQEGVLFPH 94
Cdd:PTZ00265 396 KDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDSHNL-KDINLKWWRSKIGVVSQDPLLFSN 474
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 95 lTVYRNIAYGLGNGKGRTAQERQ------------------RIEAMLELTGISE-------------------------- 130
Cdd:PTZ00265 475 -SIKNNIKYSLYSLKDLEALSNYynedgndsqenknkrnscRAKCAGDLNDMSNttdsneliemrknyqtikdsevvdvs 553
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 131 ------------------LAGRYPHELSGGQQQRVALARALAPDPELILLDEPFSALDEQLRRQIREdMIAALRANGKSA 192
Cdd:PTZ00265 554 kkvlihdfvsalpdkyetLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQK-TINNLKGNENRI 632
|
250 260
....*....|....*....|
gi 1067578656 193 VFVSHDREEALQYADRIAVM 212
Cdd:PTZ00265 633 TIIIAHRLSTIRYANTIFVL 652
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
18-226 |
5.63e-12 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 67.31 E-value: 5.63e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 18 PVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIfSKNTNLPVReRRLGYLVQEGVLFPHlTV 97
Cdd:PLN03232 1250 PVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDV-AKFGLTDLR-RVLSIIPQSPVLFSG-TV 1326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 98 YRNI-AYGLGNGKGR-TAQERQRIEAMLELT--GISELAGRYPHELSGGQQQRVALARALAPDPELILLDEPFSALDEQ- 172
Cdd:PLN03232 1327 RFNIdPFSEHNDADLwEALERAHIKDVIDRNpfGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRt 1406
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1067578656 173 ---LRRQIREDMIAAlrangkSAVFVSHdREEALQYADRIAVMKQGRILQTASPHEL 226
Cdd:PLN03232 1407 dslIQRTIREEFKSC------TMLVIAH-RLNTIIDCDKILVLSSGQVLEYDSPQEL 1456
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
29-198 |
2.02e-11 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 64.83 E-value: 2.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 29 PGEILFIIGASGCGKTTLLRCLAG--------FEQPDSGEISL---SGKTIFSKNTNLPVRERRLGYLVQEGVLFPHLTv 97
Cdd:PRK13409 98 EGKVTGILGPNGIGKTTAVKILSGelipnlgdYEEEPSWDEVLkrfRGTELQNYFKKLYNGEIKVVHKPQYVDLIPKVF- 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 98 yrniayglgNGKGR----TAQERQRIEAMLELTGISELAGRYPHELSGGQQQRVALARALAPDPELILLDEPFSALDeql 173
Cdd:PRK13409 177 ---------KGKVRellkKVDERGKLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLD--- 244
|
170 180
....*....|....*....|....*....
gi 1067578656 174 rrqIREDMIAA--LR--ANGKSAVFVSHD 198
Cdd:PRK13409 245 ---IRQRLNVArlIRelAEGKYVLVVEHD 270
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
19-172 |
2.36e-11 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 65.13 E-value: 2.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 19 VLNDISLSLDPGEILFIIGASGCGKTTLLRCLAgfEQPDSGEISlSGKTIfsknTNLPVR----ERRLGYLVQEGVLFPH 94
Cdd:TIGR00956 778 ILNNVDGWVKPGTLTALMGASGAGKTTLLNVLA--ERVTTGVIT-GGDRL----VNGRPLdssfQRSIGYVQQQDLHLPT 850
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 95 LTVYRNIAYG--LGNGKGRTAQERQR-IEAMLELTGISELA----GRYPHELSGGQQQRVALARALAPDPELIL-LDEPF 166
Cdd:TIGR00956 851 STVRESLRFSayLRQPKSVSKSEKMEyVEEVIKLLEMESYAdavvGVPGEGLNVEQRKRLTIGVELVAKPKLLLfLDEPT 930
|
....*.
gi 1067578656 167 SALDEQ 172
Cdd:TIGR00956 931 SGLDSQ 936
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
19-217 |
2.83e-11 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 64.43 E-value: 2.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 19 VLNDISLSLDPGEILFIIGASGCGKTTLLRCLAG--FEQPDSGEISLSGKTIFSKNTNLPVR-------ERRLGY-LVQE 88
Cdd:NF040905 275 VVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFGrsYGRNISGTVFKDGKEVDVSTVSDAIDaglayvtEDRKGYgLNLI 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 89 GvlfphlTVYRNI-AYGLG----------NGKGRTAQE---RQRIEAmlelTGISELAGRypheLSGGQQQRVALARALA 154
Cdd:NF040905 355 D------DIKRNItLANLGkvsrrgvideNEEIKVAEEyrkKMNIKT----PSVFQKVGN----LSGGNQQKVVLSKWLF 420
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1067578656 155 PDPELILLDEPFSALDEQLRRQIREdMIAALRANGKSAVFVSHDREEALQYADRIAVMKQGRI 217
Cdd:NF040905 421 TDPDVLILDEPTRGIDVGAKYEIYT-IINELAAEGKGVIVISSELPELLGMCDRIYVMNEGRI 482
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
29-201 |
3.42e-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: 60.85 E-value: 3.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 29 PGEILFIIGASGCGKTTLLRCLAGFEQPDsgeislsGKTIFSKNTNlpvrerrlgylvqegvlfphltvyrniayglgng 108
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPP-------GGGVIYIDGE---------------------------------- 39
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 109 kgrtaqerqRIEAMLELTGISELAGRYPHELSGGQQQRVALARALAPDPELILLDEPFSALDEQLRRQIREDMIAAL--- 185
Cdd:smart00382 40 ---------DILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLlll 110
|
170
....*....|....*...
gi 1067578656 186 --RANGKSAVFVSHDREE 201
Cdd:smart00382 111 lkSEKNLTVILTTNDEKD 128
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
20-209 |
3.57e-11 |
|
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: 61.18 E-value: 3.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 20 LNDISLSLDPGEILFIIGASGCGKTTLlrCLAGFEQpdSGEISL-SGKTIFSKNtnLPVRERRLGYLvqegvlfphltvy 98
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTL--VNEGLYA--SGKARLiSFLPKFSRN--KLIFIDQLQFL------------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 99 rnIAYGLGngkgrtaqerqrieaMLELtgiselaGRYPHELSGGQQQRVALARALA--PDPELILLDEPFSALDEQLRRQ 176
Cdd:cd03238 72 --IDVGLG---------------YLTL-------GQKLSTLSGGELQRVKLASELFsePPGTLFILDEPSTGLHQQDINQ 127
|
170 180 190
....*....|....*....|....*....|...
gi 1067578656 177 IREdMIAALRANGKSAVFVSHDrEEALQYADRI 209
Cdd:cd03238 128 LLE-VIKGLIDLGNTVILIEHN-LDVLSSADWI 158
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
29-198 |
6.79e-11 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 63.26 E-value: 6.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 29 PGEILFIIGASGCGKTTLLRCLAGFEQPDSGEIS-----------LSGKTIFSkntnlpvrerrlgYL--VQEGvlfpHL 95
Cdd:COG1245 98 KGKVTGILGPNGIGKSTALKILSGELKPNLGDYDeepswdevlkrFRGTELQD-------------YFkkLANG----EI 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 96 TVYRNIAY-----GLGNGKGRT----AQERQRIEAMLELTGISELAGRYPHELSGGQQQRVALARALAPDPELILLDEPF 166
Cdd:COG1245 161 KVAHKPQYvdlipKVFKGTVREllekVDERGKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPS 240
|
170 180 190
....*....|....*....|....*....|....*.
gi 1067578656 167 SALD--EQLR--RQIREdmiaaLRANGKSAVFVSHD 198
Cdd:COG1245 241 SYLDiyQRLNvaRLIRE-----LAEEGKYVLVVEHD 271
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
20-200 |
1.50e-10 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 62.28 E-value: 1.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 20 LNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSgktifsknTNLPVrerrlGYLVQ-EGVLFPHLTVY 98
Cdd:PRK11147 335 VKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCG--------TKLEV-----AYFDQhRAELDPEKTVM 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 99 RNIAYG----LGNGKGRtaqerqRIEAMLELTGISELAGRYP-HELSGGQQQRVALARALAPDPELILLDEPFSALD-EQ 172
Cdd:PRK11147 402 DNLAEGkqevMVNGRPR------HVLGYLQDFLFHPKRAMTPvKALSGGERNRLLLARLFLKPSNLLILDEPTNDLDvET 475
|
170 180
....*....|....*....|....*...
gi 1067578656 173 LrrQIREDMIAALRAngkSAVFVSHDRE 200
Cdd:PRK11147 476 L--ELLEELLDSYQG---TVLLVSHDRQ 498
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
30-211 |
2.31e-10 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 59.12 E-value: 2.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 30 GEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIFSKNtnlpvrerrlgylvqegvlfphltvyrniayglgngk 109
Cdd:cd03222 25 GEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITPVYKP------------------------------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 110 grtaqerQRIEamleltgiselagrypheLSGGQQQRVALARALAPDPELILLDEPFSALDEQLRRQIREDMIAALRANG 189
Cdd:cd03222 68 -------QYID------------------LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGK 122
|
170 180
....*....|....*....|..
gi 1067578656 190 KSAVFVSHDREEALQYADRIAV 211
Cdd:cd03222 123 KTALVVEHDLAVLDYLSDRIHV 144
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
36-199 |
2.89e-10 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 61.45 E-value: 2.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 36 IGASGCGKTTLLRCLAGFEQPDSGEISLSGKTifskntnlpvrerRLGYLVQEGVLFPHLTVYRNIAYG---LGNGKgrt 112
Cdd:PRK15064 33 IGANGCGKSTFMKILGGDLEPSAGNVSLDPNE-------------RLGKLRQDQFAFEEFTVLDTVIMGhteLWEVK--- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 113 aQERQRIEAMLELT---GI--SELAGRYP------------------------H-----ELSGGQQQRVALARALAPDPE 158
Cdd:PRK15064 97 -QERDRIYALPEMSeedGMkvADLEVKFAemdgytaearagelllgvgipeeqHyglmsEVAPGWKLRVLLAQALFSNPD 175
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1067578656 159 LILLDEPFSALDEQlrrQIR--EDMiaaLRANGKSAVFVSHDR 199
Cdd:PRK15064 176 ILLLDEPTNNLDIN---TIRwlEDV---LNERNSTMIIISHDR 212
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
18-217 |
4.67e-10 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 61.03 E-value: 4.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 18 PVL-NDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKT---IFSKN--TNLPVRERRLGYLVQegvL 91
Cdd:PLN03073 522 PLLfKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSAKVrmaVFSQHhvDGLDLSSNPLLYMMR---C 598
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 92 FPHLTvyrniayglgngkgrtaqeRQRIEAMLELTGIS-ELAGRYPHELSGGQQQRVALARALAPDPELILLDEPFSALD 170
Cdd:PLN03073 599 FPGVP-------------------EQKLRAHLGSFGVTgNLALQPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLD 659
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1067578656 171 eqlrRQIREDMIAALRANGKSAVFVSHDREEALQYADRIAVMKQGRI 217
Cdd:PLN03073 660 ----LDAVEALIQGLVLFQGGVLMVSHDEHLISGSVDELWVVSEGKV 702
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
11-256 |
1.17e-09 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 59.74 E-value: 1.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 11 SKSFQntpVLNDISLSLDPGEILFIIGASGCGKTTLLRCLA----GFEQPDSGEISLSGktiFSKNTNLPVRERRLGYLV 86
Cdd:TIGR00956 71 TKTFD---ILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIAsntdGFHIGVEGVITYDG---ITPEEIKKHYRGDVVYNA 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 87 QEGVLFPHLTVYRNIAY-----GLGN-GKGRTAQERQRIEAMLELT--GIS-----ELAGRYPHELSGGQQQRVALARAL 153
Cdd:TIGR00956 145 ETDVHFPHLTVGETLDFaarckTPQNrPDGVSREEYAKHIADVYMAtyGLShtrntKVGNDFVRGVSGGERKRVSIAEAS 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 154 APDPELILLDEPFSALDEQLRRQIredmIAALRANG---KSAVFVS--HDREEALQYADRIAVMKQGRIlqtaspheLYR 228
Cdd:TIGR00956 225 LGGAKIQCWDNATRGLDSATALEF----IRALKTSAnilDTTPLVAiyQCSQDAYELFDKVIVLYEGYQ--------IYF 292
|
250 260
....*....|....*....|....*...
gi 1067578656 229 QPADLDAALFIGEGIVFPaalNADGTAD 256
Cdd:TIGR00956 293 GPADKAKQYFEKMGFKCP---DRQTTAD 317
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
29-198 |
1.41e-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: 57.76 E-value: 1.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 29 PGEILFIIGASGCGKTTLLRCLAGFEQPDSGEislsgktiFSKNTNLP--VRERR-------LGYLVQEGVLFPHLTVYR 99
Cdd:cd03236 25 EGQVLGLVGPNGIGKSTALKILAGKLKPNLGK--------FDDPPDWDeiLDEFRgselqnyFTKLLEGDVKVIVKPQYV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 100 NIAYGLGNGKGR----TAQERQRIEAMLELTGISELAGRYPHELSGGQQQRVALARALAPDPELILLDEPFSALDEQLR- 174
Cdd:cd03236 97 DLIPKAVKGKVGellkKKDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRl 176
|
170 180
....*....|....*....|....*..
gi 1067578656 175 ---RQIREdmiaaLRANGKSAVFVSHD 198
Cdd:cd03236 177 naaRLIRE-----LAEDDNYVLVVEHD 198
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
20-197 |
1.43e-09 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 59.13 E-value: 1.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 20 LNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIFskntnlpvrerrlgYLVQEGvLFPHLTVYR 99
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAAL--------------IAISSG-LNGQLTGIE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 100 NIAYGlGNGKGRTAQERQRI-EAMLELTGISELAGRYPHELSGGQQQRVALARALAPDPELILLDEPFSALDEQLRRQIR 178
Cdd:PRK13545 105 NIELK-GLMMGLTKEKIKEIiPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKCL 183
|
170
....*....|....*....
gi 1067578656 179 EDMiAALRANGKSAVFVSH 197
Cdd:PRK13545 184 DKM-NEFKEQGKTIFFISH 201
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
19-229 |
1.56e-09 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 59.57 E-value: 1.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 19 VLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIfsKNTNLPVRERRLGYLVQEGVLFPHlTVY 98
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNI--AKIGLHDLRFKITIIPQDPVLFSG-SLR 1377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 99 RNIayglgNGKGRTAQERqrIEAMLEL----TGISELAGRYPHE-------LSGGQQQRVALARALAPDPELILLDEPFS 167
Cdd:TIGR00957 1378 MNL-----DPFSQYSDEE--VWWALELahlkTFVSALPDKLDHEcaeggenLSVGQRQLVCLARALLRKTKILVLDEATA 1450
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1067578656 168 ALDEQLRRQIRedmiAALRANGK--SAVFVSHDREEALQYAdRIAVMKQGRILQTASPHELYRQ 229
Cdd:TIGR00957 1451 AVDLETDNLIQ----STIRTQFEdcTVLTIAHRLNTIMDYT-RVIVLDKGEVAEFGAPSNLLQQ 1509
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
5-220 |
1.68e-09 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 57.49 E-value: 1.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 5 LHIGHLSKSFQNTPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFE--QPDSGEISLSGKTIFSKNTnlpvrERRL 82
Cdd:PRK09580 2 LSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLELSP-----EDRA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 83 GYLV----QEGVLFPHLTVYRNIAYGLGNGKGRTAQE-------RQRIEAMLELTGISE-LAGRYPHE-LSGGQQQRVAL 149
Cdd:PRK09580 77 GEGIfmafQYPVEIPGVSNQFFLQTALNAVRSYRGQEpldrfdfQDLMEEKIALLKMPEdLLTRSVNVgFSGGEKKRNDI 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1067578656 150 ARALAPDPELILLDEPFSALD-EQLRrqIREDMIAALRANGKSAVFVSHdREEALQY--ADRIAVMKQGRILQT 220
Cdd:PRK09580 157 LQMAVLEPELCILDESDSGLDiDALK--IVADGVNSLRDGKRSFIIVTH-YQRILDYikPDYVHVLYQGRIVKS 227
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
17-237 |
8.90e-09 |
|
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: 55.63 E-value: 8.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 17 TPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDsGEISLSGktiFSKNTnLPVRERR--LGYLVQEGVLFPH 94
Cdd:cd03289 17 NAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GDIQIDG---VSWNS-VPLQKWRkaFGVIPQKVFIFSG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 95 lTVYRNI-AYGLGNGkgrtaqerQRIEAMLELTGISELAGRYPHE-----------LSGGQQQRVALARALAPDPELILL 162
Cdd:cd03289 92 -TFRKNLdPYGKWSD--------EEIWKVAEEVGLKSVIEQFPGQldfvlvdggcvLSHGHKQLMCLARSVLSKAKILLL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1067578656 163 DEPFSALDEQLRRQIREDMIAALranGKSAVFVSHDREEALQYADRIAVMKQGRILQTASPHELYRQPADLDAAL 237
Cdd:cd03289 163 DEPSAHLDPITYQVIRKTLKQAF---ADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEKSHFKQAI 234
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
19-170 |
1.50e-08 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 56.39 E-value: 1.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 19 VLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPD--SGEISLSGktiFSKNTNLPVRERrlGYLVQEGVLFPHLT 96
Cdd:PLN03140 895 LLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTGGyiEGDIRISG---FPKKQETFARIS--GYCEQNDIHSPQVT 969
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 97 VYRNIAYG--LGNGKGRTAQERQR-IEAMLEL----------TGISELAGrypheLSGGQQQRVALARALAPDPELILLD 163
Cdd:PLN03140 970 VRESLIYSafLRLPKEVSKEEKMMfVDEVMELveldnlkdaiVGLPGVTG-----LSTEQRKRLTIAVELVANPSIIFMD 1044
|
....*..
gi 1067578656 164 EPFSALD 170
Cdd:PLN03140 1045 EPTSGLD 1051
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
4-217 |
1.84e-08 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 54.82 E-value: 1.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 4 ALHIGHLSKSFQntpVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGK-TIFSKNTNLPVRerrl 82
Cdd:PRK13546 27 ALIPKHKNKTFF---ALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEvSVIAISAGLSGQ---- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 83 gylvqegvlfphLTVYRNIAYG---LGngkgrtaQERQRIEAML-ELTGISELaGRYPHE----LSGGQQQRVALARALA 154
Cdd:PRK13546 100 ------------LTGIENIEFKmlcMG-------FKRKEIKAMTpKIIEFSEL-GEFIYQpvkkYSSGMRAKLGFSINIT 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1067578656 155 PDPELILLDEPFSALDeQLRRQIREDMIAALRANGKSAVFVSHDREEALQYADRIAVMKQGRI 217
Cdd:PRK13546 160 VNPDILVIDEALSVGD-QTFAQKCLDKIYEFKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKL 221
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
28-209 |
2.54e-08 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 53.38 E-value: 2.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 28 DPGEILF------IIGASGCGKTTLLRCL-------------AGFEQPD---SGEISLSGKTIFSKNTNLPVRERRlgyl 85
Cdd:cd03240 14 ERSEIEFfspltlIVGQNGAGKTTIIEALkyaltgelppnskGGAHDPKlirEGEVRAQVKLAFENANGKKYTITR---- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 86 vqegvlfpHLTVYRNIAYglgngkgrTAQERQRIEAMLELtgiselaGRypheLSGGQQQ------RVALARALAPDPEL 159
Cdd:cd03240 90 --------SLAILENVIF--------CHQGESNWPLLDMR-------GR----CSGGEKVlasliiRLALAETFGSNCGI 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1067578656 160 ILLDEPFSALD-EQLRRQIREDMIAALRANGKSAVFVSHDrEEALQYADRI 209
Cdd:cd03240 143 LALDEPTTNLDeENIEESLAEIIEERKSQKNFQLIVITHD-EELVDAADHI 192
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
4-213 |
3.76e-08 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 52.36 E-value: 3.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 4 ALHIGHlsksFQNTPVLNDISLSldPGEILFIIGASGCGKTTLLRCLagfeqpdsgeislsgktifskntnlpvrerrlG 83
Cdd:cd03227 1 KIVLGR----FPSYFVPNDVTFG--EGSLTIITGPNGSGKSTILDAI--------------------------------G 42
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 84 YLVqeGVLFPHLTVYRNIAYGLgngkgrtaqerqrIEAMLELTGISELagrypHELSGGQQQRVALARALA-----PDPe 158
Cdd:cd03227 43 LAL--GGAQSATRRRSGVKAGC-------------IVAAVSAELIFTR-----LQLSGGEKELSALALILAlaslkPRP- 101
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1067578656 159 LILLDEPFSALDEQlRRQIREDMIAALRANGKSAVFVSHDrEEALQYADRIAVMK 213
Cdd:cd03227 102 LYILDEIDRGLDPR-DGQALAEAILEHLVKGAQVIVITHL-PELAELADKLIHIK 154
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
18-226 |
6.80e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 54.36 E-value: 6.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 18 PVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIfSKNTNLPVReRRLGYLVQEGVLFP---- 93
Cdd:PLN03130 1253 PVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDI-SKFGLMDLR-KVLGIIPQAPVLFSgtvr 1330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 94 ---------------------HLT-VYRNiayglgNGKGRTAQerqrieamleltgISElAGrypHELSGGQQQRVALAR 151
Cdd:PLN03130 1331 fnldpfnehndadlwesleraHLKdVIRR------NSLGLDAE-------------VSE-AG---ENFSVGQRQLLSLAR 1387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 152 ALAPDPELILLDEPFSALDEQ----LRRQIRED------MIAALRANgksavfvshdreeALQYADRIAVMKQGRILQTA 221
Cdd:PLN03130 1388 ALLRRSKILVLDEATAAVDVRtdalIQKTIREEfksctmLIIAHRLN-------------TIIDCDRILVLDAGRVVEFD 1454
|
....*
gi 1067578656 222 SPHEL 226
Cdd:PLN03130 1455 TPENL 1459
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
5-237 |
6.10e-07 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 49.91 E-value: 6.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 5 LHIGHLSKSFQNT--PVLNDISLSLDPGEILFIIGASGCGKTTLlrCLAGFEQPD--SGEISLSGKTIfsknTNLPVR-- 78
Cdd:cd03288 20 IKIHDLCVRYENNlkPVLKHVKAYIKPGQKVGICGRTGSGKSSL--SLAFFRMVDifDGKIVIDGIDI----SKLPLHtl 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 79 ERRLGYLVQEGVLFPHltvyrNIAYGLGNGKGRTaqeRQRIEAMLELTGISELAGRYPHEL-----------SGGQQQRV 147
Cdd:cd03288 94 RSRLSIILQDPILFSG-----SIRFNLDPECKCT---DDRLWEALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLF 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 148 ALARALAPDPELILLDEPFSALDEQLRRQIREDMIAALRanGKSAVFVSHdREEALQYADRIAVMKQGRILQTASPHELY 227
Cdd:cd03288 166 CLARAFVRKSSILIMDEATASIDMATENILQKVVMTAFA--DRTVVTIAH-RVSTILDADLVLVLSRGILVECDTPENLL 242
|
250
....*....|
gi 1067578656 228 RQPADLDAAL 237
Cdd:cd03288 243 AQEDGVFASL 252
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
19-237 |
6.41e-07 |
|
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: 51.45 E-value: 6.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 19 VLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDsGEISLSGktIFSKNTNLPVRERRLGYLVQEGVLFPHlTVY 98
Cdd:TIGR01271 1234 VLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTE-GEIQIDG--VSWNSVTLQTWRKAFGVIPQKVFIFSG-TFR 1309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 99 RNIayglgngkgrTAQER---QRIEAMLELTGISELAGRYPHE-----------LSGGQQQRVALARALAPDPELILLDE 164
Cdd:TIGR01271 1310 KNL----------DPYEQwsdEEIWKVAEEVGLKSVIEQFPDKldfvlvdggyvLSNGHKQLMCLARSILSKAKILLLDE 1379
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1067578656 165 PFSALDEQLRRQIREDMIAALranGKSAVFVSHDREEALQYADRIAVMKQGRILQTASPHELYRQPADLDAAL 237
Cdd:TIGR01271 1380 PSAHLDPVTLQIIRKTLKQSF---SNCTVILSEHRVEALLECQQFLVIEGSSVKQYDSIQKLLNETSLFKQAM 1449
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
14-169 |
1.17e-06 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 50.13 E-value: 1.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 14 FQNTPV--------LNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEIslsgkTIFSKNTNLPVRER---RL 82
Cdd:TIGR00954 454 FENIPLvtpngdvlIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRL-----TKPAKGKLFYVPQRpymTL 528
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 83 GYLvQEGVLFPHlTVYRNIAYGLGNgkgrtaqerQRIEAMLELTGISELAGR---------YPHELSGGQQQRVALARAL 153
Cdd:TIGR00954 529 GTL-RDQIIYPD-SSEDMKRRGLSD---------KDLEQILDNVQLTHILEReggwsavqdWMDVLSGGEKQRIAMARLF 597
|
170
....*....|....*.
gi 1067578656 154 APDPELILLDEPFSAL 169
Cdd:TIGR00954 598 YHKPQFAILDECTSAV 613
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
5-170 |
1.28e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 50.24 E-value: 1.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 5 LHIGHLSKSFQNTPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLA--------------GFEQPDSGEISLSGKTIFS 70
Cdd:PLN03073 178 IHMENFSISVGGRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRYMAmhaidgipkncqilHVEQEVVGDDTTALQCVLN 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 71 KN---TNLPVRERRLgYLVQEGVLFPHLTVYRNIAYGLGNGKGRTAQERQRIEAMLE--------------LTGIS---E 130
Cdd:PLN03073 258 TDierTQLLEEEAQL-VAQQRELEFETETGKGKGANKDGVDKDAVSQRLEEIYKRLElidaytaearaasiLAGLSftpE 336
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1067578656 131 LAGRYPHELSGGQQQRVALARALAPDPELILLDEPFSALD 170
Cdd:PLN03073 337 MQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLD 376
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
19-214 |
3.99e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 48.63 E-value: 3.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 19 VLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIFS-KNTNLPVRER-RLGYLVQEGVLFPHLT 96
Cdd:PRK10636 16 LLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNWQLAwVNQETPALPQpALEYVIDGDREYRQLE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 97 VYRNIA--------YGLGNGKGRTAQE---RQRIEAMLELTGISELAGRYP-HELSGGQQQRVALARALAPDPELILLDE 164
Cdd:PRK10636 96 AQLHDAnerndghaIATIHGKLDAIDAwtiRSRAASLLHGLGFSNEQLERPvSDFSGGWRMRLNLAQALICRSDLLLLDE 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1067578656 165 PFSALDeqlrrqirEDMIAALRANGKS----AVFVSHDREEALQYADRIAVMKQ 214
Cdd:PRK10636 176 PTNHLD--------LDAVIWLEKWLKSyqgtLILISHDRDFLDPIVDKIIHIEQ 221
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
20-209 |
1.14e-05 |
|
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: 45.71 E-value: 1.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 20 LNDISLSLDPGEILFIIGASGCGKTTLL---------------------RCLAGFEQPD-------SGEISLSGKTIfSK 71
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSSLAfdtiyaegqrryveslsayarQFLGQMDKPDvdsieglSPAIAIDQKTT-SR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 72 NT-------------------NLPVRERrLGYLVQEGVlfPHLTVYRNIAyglgngkgrtaqerqrieamleltgisela 132
Cdd:cd03270 90 NPrstvgtvteiydylrllfaRVGIRER-LGFLVDVGL--GYLTLSRSAP------------------------------ 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1067578656 133 gryphELSGGQQQRVALARALAPDPELIL--LDEPFSALDEQLRRQIREdMIAALRANGKSAVFVSHDrEEALQYADRI 209
Cdd:cd03270 137 -----TLSGGEAQRIRLATQIGSGLTGVLyvLDEPSIGLHPRDNDRLIE-TLKRLRDLGNTVLVVEHD-EDTIRAADHV 208
|
|
| SbcC_Walker_B |
pfam13558 |
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from ... |
138-187 |
1.64e-05 |
|
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from eukaryotes and the prokaryotic homolog SbcCD complex subunit C. RAD50-ATPase forms a complex with Mre11-nuclease that detects and processes diverse and obstructed DNA ends. This domain is separated of the Walker A domain by a long coiled-coil domain and forms the nucleotide-binding domain (NBD) when the coiled coils fold back on themselves and bring together Walker A and B domains. Two RAD50-NBDs forms heterotetramers with a Mre11 nuclease dimer that assemble as catalytic head module that binds and cleaves DNA in an ATP-dependent reaction. Through secondary structural analysis, it has been suggested that there is a wide structural conservation in the Rad50/SMC protein family as seen in structural similarities between RAD50's hook and ABC-ATPase MukB's elbow region.
Pssm-ID: 463921 [Multi-domain] Cd Length: 90 Bit Score: 42.99 E-value: 1.64e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1067578656 138 ELSGGQQQR---VALARALA----------PDPELILLDEPFSALDEQLRRQiredMIAALRA 187
Cdd:pfam13558 32 GLSGGEKQLlayLPLAAALAaqygsaegrpPAPRLVFLDEAFAKLDEENIRT----ALELLRA 90
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
116-235 |
2.25e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 46.36 E-value: 2.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 116 RQRIEAMLELtGISELA-GRYPHELSGGQQQRVALARALApdPELI----LLDEPFSALDEQLRRQIReDMIAALRANGK 190
Cdd:PRK00635 454 KSRLSILIDL-GLPYLTpERALATLSGGEQERTALAKHLG--AELIgityILDEPSIGLHPQDTHKLI-NVIKKLRDQGN 529
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1067578656 191 SAVFVSHDrEEALQYADRI------AVMKQGRILQTASPHELYRQPADLDA 235
Cdd:PRK00635 530 TVLLVEHD-EQMISLADRIidigpgAGIFGGEVLFNGSPREFLAKSDSLTA 579
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
26-213 |
3.65e-05 |
|
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini.
Pssm-ID: 213246 [Multi-domain] Cd Length: 213 Bit Score: 44.18 E-value: 3.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 26 SLDPGEILFIIGASGCGKTTLLrclagfeqpDSGEISLSGKTIFSKNTNlpvrerRLGYLVQEGVLFPHLTVY---RNIA 102
Cdd:cd03279 24 GLDNNGLFLICGPTGAGKSTIL---------DAITYALYGKTPRYGRQE------NLRSVFAPGEDTAEVSFTfqlGGKK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 103 YGLGNGKGRTAQERQRIeAMLELTGISELAGRYPHELSGGQQQRVALARALAPDP----------ELILLDEPFSALDEQ 172
Cdd:cd03279 89 YRVERSRGLDYDQFTRI-VLLPQGEFDRFLARPVSTLSGGETFLASLSLALALSEvlqnrggarlEALFIDEGFGTLDPE 167
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1067578656 173 LRRQIrEDMIAALRANGKSAVFVSHDREEALQYADRIAVMK 213
Cdd:cd03279 168 ALEAV-ATALELIRTENRMVGVISHVEELKERIPQRLEVIK 207
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
12-198 |
4.80e-05 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 43.85 E-value: 4.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 12 KSFQNTPVLNdislsLDPGEILfIIGASGCGKTTLLR--CLAGFEQPDSG-------------------EISLSGKTI-- 68
Cdd:COG0419 11 RSYRDTETID-----FDDGLNL-IVGPNGAGKSTILEaiRYALYGKARSRsklrsdlinvgseeasvelEFEHGGKRYri 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 69 ------FSKNTNLPVRERR--LGYLVQegvlfphLTVYRNIAYGLGNGKGRTAQERQRIEAMLELTG--ISELAGRYP-H 137
Cdd:COG0419 85 errqgeFAEFLEAKPSERKeaLKRLLG-------LEIYEELKERLKELEEALESALEELAELQKLKQeiLAQLSGLDPiE 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1067578656 138 ELSGGQQQRVALARALApdpelILLDepFSALDEQLRRQiredMIAALRangkSAVFVSHD 198
Cdd:COG0419 158 TLSGGERLRLALADLLS-----LILD--FGSLDEERLER----LLDALE----ELAIITHV 203
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
139-209 |
3.43e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.74 E-value: 3.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 139 LSGGQqqRVALARA--------LAPDPELILLDEPFSALDEQLRRQIREDMIAALRangK--SAVFVSHDrEEALQYADR 208
Cdd:PRK03918 789 LSGGE--RIALGLAfrlalslyLAGNIPLLILDEPTPFLDEERRRKLVDIMERYLR---KipQVIIVSHD-EELKDAADY 862
|
.
gi 1067578656 209 I 209
Cdd:PRK03918 863 V 863
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
139-241 |
9.51e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 41.15 E-value: 9.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 139 LSGGQQQRVALARALApdPELI----LLDEPFSALDEQLRRQIREDMIaALRANGKSAVFVSHDrEEALQYADRI----- 209
Cdd:TIGR00630 489 LSGGEAQRIRLATQIG--SGLTgvlyVLDEPSIGLHQRDNRRLINTLK-RLRDLGNTLIVVEHD-EDTIRAADYVidigp 564
|
90 100 110
....*....|....*....|....*....|...
gi 1067578656 210 -AVMKQGRILQTASPHELYRQPADLDAALFIGE 241
Cdd:TIGR00630 565 gAGEHGGEVVASGTPEEILANPDSLTGQYLSGR 597
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
32-106 |
1.86e-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: 39.68 E-value: 1.86e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1067578656 32 ILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIFSKNTNLPVRERRLGYLVQEGVLFPHLTVYRNIAYGLG 106
Cdd:pfam13304 1 INVLIGPNGSGKSNLLEALRFLADFDALVIGLTDERSRNGGIGGIPSLLNGIDPKEPIEFEISEFLEDGVRYRYG 75
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
139-200 |
2.65e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 39.88 E-value: 2.65e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 139 LSGGQQQ------RVALARALAPDPELILLDEPFSALDEQLRRQIREDMIAALRANG--KSAVFVSHDRE 200
Cdd:PRK01156 802 LSGGEKTavafalRVAVAQFLNNDKSLLIMDEPTAFLDEDRRTNLKDIIEYSLKDSSdiPQVIMISHHRE 871
|
|
| ABC_SMC3_euk |
cd03272 |
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ... |
138-209 |
6.04e-03 |
|
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of chromosomes (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: 213239 [Multi-domain] Cd Length: 243 Bit Score: 37.62 E-value: 6.04e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1067578656 138 ELSGGQQQRVALARALA-----PDPeLILLDEPFSALDEQLRRQIrEDMIAALranGKSAVFVSHD-REEALQYADRI 209
Cdd:cd03272 158 QLSGGQKSLVALALIFAiqkcdPAP-FYLFDEIDAALDAQYRTAV-ANMIKEL---SDGAQFITTTfRPELLEVADKF 230
|
|
| EutP |
COG4917 |
Ethanolamine utilization protein EutP, contains a P-loop NTPase domain [Amino acid transport ... |
33-56 |
8.30e-03 |
|
Ethanolamine utilization protein EutP, contains a P-loop NTPase domain [Amino acid transport and metabolism];
Pssm-ID: 443945 [Multi-domain] Cd Length: 145 Bit Score: 36.32 E-value: 8.30e-03
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
139-227 |
8.57e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 38.27 E-value: 8.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578656 139 LSGGQQQRVALARAL--AP-DPELILLDEPFSALDEQLRRQIREdMIAALRANGKSAVFVSHDrEEALQYADRIAVM--- 212
Cdd:PRK00635 1700 LSLSEKIAIKIAKFLylPPkHPTLFLLDEIATSLDNQQKSALLV-QLRTLVSLGHSVIYIDHD-PALLKQADYLIEMgpg 1777
|
90
....*....|....*...
gi 1067578656 213 --KQ-GRILQTASPHELY 227
Cdd:PRK00635 1778 sgKTgGKILFSGPPKDIS 1795
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
25-51 |
9.47e-03 |
|
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily represents an ancient group of ATPases belonging to the ASCE (for additional strand, catalytic E) division of the P-loop NTPase fold. The ASCE division also includes ABC, RecA-like, VirD4-like, PilT-like, and SF1/2 helicases. Members of the AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. The AAA+ proteins contain several distinct features in addition to the conserved alpha-beta-alpha core domain structure and the Walker A and B motifs of the P-loop NTPases.
Pssm-ID: 99707 [Multi-domain] Cd Length: 151 Bit Score: 36.36 E-value: 9.47e-03
10 20
....*....|....*....|....*..
gi 1067578656 25 LSLDPGEILFIIGASGCGKTTLLRCLA 51
Cdd:cd00009 14 LELPPPKNLLLYGPPGTGKTTLARAIA 40
|
|
|