|
Name |
Accession |
Description |
Interval |
E-value |
| ABC_choXWV_ATP |
TIGR03415 |
choline ABC transporter, ATP-binding protein; Members of this protein family are the ... |
4-344 |
0e+00 |
|
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: 594.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 4 VNFNNVSIIFGDRPETALAMVDQGKSRDEIGAATGLVLGVADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGD 83
Cdd:TIGR03415 1 IRFKNVDIVFGDQPDEALALLDQGKTREEILDRTGLVLGVHNASLDIEEGEICVLMGLSGSGKSTLLRAVNGLNPVSRGS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 84 VAVSTTTGPVNPYRCNAKALRDLRTHTVSMVFQQFALLPWRTVAENVGFGLELAGMPEAERKLRVGEQLELVNLTKWAGR 163
Cdd:TIGR03415 81 VLVKDGDGSVDVANCDAATLRRLRTHRVSMVFQQFALLPWRTVEENVAFGLEMQGMPKAERRKRVDEQLELVGLAQWADR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 164 KVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDPLIRTRLQDELLEFQRRLKKTILFVSHDLDEAFRIGNRIAIMEG 243
Cdd:TIGR03415 161 KPGELSGGMQQRVGLARAFATEAPILLMDEPFSALDPLIRTQLQDELLELQSKLKKTIVFVSHDLDEALKIGNRIAIMEG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 244 GRIIQCGTPHDIVKNPADQYVADFVQNLNPINMLTAADVMQP--------------------------GLGQTAAGMSVS 297
Cdd:TIGR03415 241 GRIIQHGTPEEIVLNPANDYVADFVAHTNPLNVLTARDLMRPlttlekvdgewcvskrydtwlktadkQVRRAAAGLPVA 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2087760999 298 ATA---------------RAATPLIDVLDALARQPGSIGIVENGAIVGTISAQDIVAGLTRH 344
Cdd:TIGR03415 321 AWAaeqevesleklptviNPDTPMRDVLAARHRTGGAILLVENGRIVGVIGDQNIYHALLGH 382
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
1-342 |
0e+00 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 532.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 1 MTAVNFNNVSIIFGDRPETALAMVDQGKSRDEIGAATGLVLGVADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVV 80
Cdd:COG4175 1 MPKIEVRNLYKIFGKRPERALKLLDQGKSKDEILEKTGQTVGVNDASFDVEEGEIFVIMGLSGSGKSTLVRCLNRLIEPT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 81 RGDVAVSTttgpVNPYRCNAKALRDLRTHTVSMVFQQFALLPWRTVAENVGFGLELAGMPEAERKLRVGEQLELVNLTKW 160
Cdd:COG4175 81 AGEVLIDG----EDITKLSKKELRELRRKKMSMVFQHFALLPHRTVLENVAFGLEIQGVPKAERRERAREALELVGLAGW 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 161 AGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDPLIRTRLQDELLEFQRRLKKTILFVSHDLDEAFRIGNRIAI 240
Cdd:COG4175 157 EDSYPDELSGGMQQRVGLARALATDPDILLMDEAFSALDPLIRREMQDELLELQAKLKKTIVFITHDLDEALRLGDRIAI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 241 MEGGRIIQCGTPHDIVKNPADQYVADFVQNLNPINMLTAADVMQPGLGQTAAGMSVSA---------------------- 298
Cdd:COG4175 237 MKDGRIVQIGTPEEILTNPANDYVADFVEDVDRSKVLTAGSVMRPPEAVVSEKDGPRValrrmreegisslyvvdrdrrl 316
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2087760999 299 ----------------------------TARAATPLIDVLDALARQPGSIGIV-ENGAIVGTISAQDIVAGLT 342
Cdd:COG4175 317 lgvvtaddaleavkgekdleeilltdvpTVSPDTPLRDLLPLVAESPYPLAVVdEDGRLLGVISRGSLLAALA 389
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
7-275 |
5.26e-134 |
|
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: 382.38 E-value: 5.26e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 7 NNVSIIFGDRPETALAMVDQGKSRDEIGAATGLVLGVADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAV 86
Cdd:cd03294 4 KGLYKIFGKNPQKAFKLLAKGKSKEEILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 87 STTtgPVNpyRCNAKALRDLRTHTVSMVFQQFALLPWRTVAENVGFGLELAGMPEAERKLRVGEQLELVNLTKWAGRKVN 166
Cdd:cd03294 84 DGQ--DIA--AMSRKELRELRRKKISMVFQSFALLPHRTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 167 ELSGGMQQRVGLARAFATGAPILLMDEPFSALDPLIRTRLQDELLEFQRRLKKTILFVSHDLDEAFRIGNRIAIMEGGRI 246
Cdd:cd03294 160 ELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRL 239
|
250 260
....*....|....*....|....*....
gi 2087760999 247 IQCGTPHDIVKNPADQYVADFVQNLNPIN 275
Cdd:cd03294 240 VQVGTPEEILTNPANDYVREFFRGVDRAK 268
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
43-341 |
4.50e-97 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 290.07 E-value: 4.50e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 43 VADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAV---STTTgpVNPYRcnakaLRdlRthtvSM--VFQQ 117
Cdd:COG1125 18 VDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIdgeDIRD--LDPVE-----LR--R----RIgyVIQQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 118 FALLPWRTVAENVGFGLELAGMPEAERKLRVGEQLELVNL--TKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPF 195
Cdd:COG1125 85 IGLFPHMTVAENIATVPRLLGWDKERIRARVDELLELVGLdpEEYRDRYPHELSGGQQQRVGVARALAADPPILLMDEPF 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 196 SALDPLIRTRLQDELLEFQRRLKKTILFVSHDLDEAFRIGNRIAIMEGGRIIQCGTPHDIVKNPADQYVADFV---QNLN 272
Cdd:COG1125 165 GALDPITREQLQDELLRLQRELGKTIVFVTHDIDEALKLGDRIAVMREGRIVQYDTPEEILANPANDFVADFVgadRGLR 244
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2087760999 273 PINMLTAADVMQPGLgqtaagmsvsATARAATPLIDVLDALARQPGSIGIV--ENGAIVGTISAQDIVAGL 341
Cdd:COG1125 245 RLSLLRVEDLMLPEP----------PTVSPDASLREALSLMLERGVDWLLVvdEDGRPLGWLTLEDLLRAL 305
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
36-284 |
2.55e-90 |
|
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: 274.81 E-value: 2.55e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 36 ATGLVLGVADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTttgpVNPYRCNAKALRDLRTHTVSMVF 115
Cdd:TIGR01186 2 KTGGKKGVNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEPTAGQIFIDG----ENIMKQSPVELREVRRKKIGMVF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 116 QQFALLPWRTVAENVGFGLELAGMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPF 195
Cdd:TIGR01186 78 QQFALFPHMTILQNTSLGPELLGWPEQERKEKALELLKLVGLEEYEHRYPDELSGGMQQRVGLARALAAEPDILLMDEAF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 196 SALDPLIRTRLQDELLEFQRRLKKTILFVSHDLDEAFRIGNRIAIMEGGRIIQCGTPHDIVKNPADQYVADFVQNLNPIN 275
Cdd:TIGR01186 158 SALDPLIRDSMQDELKKLQATLQKTIVFITHDLDEAIRIGDRIVIMKAGEIVQVGTPDEILRNPANEYVEEFIGKVDLSQ 237
|
....*....
gi 2087760999 276 MLTAADVMQ 284
Cdd:TIGR01186 238 VFDAERIAQ 246
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-305 |
3.45e-90 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 274.28 E-value: 3.45e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 1 MTAVNFNNVSIIFGDrpetalamvdqgksrdeigaatglVLGVADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVV 80
Cdd:COG3842 3 MPALELENVSKRYGD------------------------VTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPD 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 81 RGDVAVS--TTTGpVNPYRcnakalRDlrthtVSMVFQQFALLPWRTVAENVGFGLELAGMPEAERKLRVGEQLELVNLT 158
Cdd:COG3842 59 SGRILLDgrDVTG-LPPEK------RN-----VGMVFQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLE 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 159 KWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDPLIRTRLQDELLEFQRRLKKTILFVSHDLDEAFRIGNRI 238
Cdd:COG3842 127 GLADRYPHQLSGGQQQRVALARALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRI 206
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2087760999 239 AIMEGGRIIQCGTPHDIVKNPADQYVADFVqnlNPINMLTAADVMQPGLGQTAAGMSVSATARAATP 305
Cdd:COG3842 207 AVMNDGRIEQVGTPEEIYERPATRFVADFI---GEANLLPGTVLGDEGGGVRTGGRTLEVPADAGLA 270
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
43-247 |
9.19e-85 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 256.94 E-value: 9.19e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 43 VADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAV--STTTGPvnpyrcnakalrdlrTHTVSMVFQQFAL 120
Cdd:COG1116 27 LDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVdgKPVTGP---------------GPDRGVVFQEPAL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 121 LPWRTVAENVGFGLELAGMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDP 200
Cdd:COG1116 92 LPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPEVLLMDEPFGALDA 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2087760999 201 LIRTRLQDELLEFQRRLKKTILFVSHDLDEAFRIGNRIAIMEG--GRII 247
Cdd:COG1116 172 LTRERLQDELLRLWQETGKTVLFVTHDVDEAVFLADRVVVLSArpGRIV 220
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
8-292 |
2.36e-84 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 261.12 E-value: 2.36e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 8 NVSIIFGDRPETALAMVDQGKSRDEIGAATGLVLGVADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVS 87
Cdd:PRK10070 9 NLYKIFGEHPQRAFKYIEQGLSKEQILEKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLID 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 88 TttgpVNPYRCNAKALRDLRTHTVSMVFQQFALLPWRTVAENVGFGLELAGMPEAERKLRVGEQLELVNLTKWAGRKVNE 167
Cdd:PRK10070 89 G----VDIAKISDAELREVRRKKIAMVFQSFALMPHMTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 168 LSGGMQQRVGLARAFATGAPILLMDEPFSALDPLIRTRLQDELLEFQRRLKKTILFVSHDLDEAFRIGNRIAIMEGGRII 247
Cdd:PRK10070 165 LSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVV 244
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 2087760999 248 QCGTPHDIVKNPADQYVADFVQNLNPINMLTAADVMQ----------PGLGQTAA 292
Cdd:PRK10070 245 QVGTPDEILNNPANDYVRTFFRGVDISQVFSAKDIARrtpnglirktPGFGPRSA 299
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
38-250 |
9.70e-81 |
|
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: 245.12 E-value: 9.70e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 38 GLVLGVADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTTT-GPVNPYRcnakalRDlrthtVSMVFQ 116
Cdd:cd03259 11 GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDvTGVPPER------RN-----IGMVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 117 QFALLPWRTVAENVGFGLELAGMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFS 196
Cdd:cd03259 80 DYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLS 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2087760999 197 ALDPLIRTRLQDELLEFQRRLKKTILFVSHDLDEAFRIGNRIAIMEGGRIIQCG 250
Cdd:cd03259 160 ALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
43-269 |
3.11e-80 |
|
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: 244.90 E-value: 3.11e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 43 VADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVS-TTTGPVNPYRcnakalrdLRTHtVSMVFQQFALL 121
Cdd:cd03295 17 VNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDgEDIREQDPVE--------LRRK-IGYVIQQIGLF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 122 PWRTVAENVGFGLELAGMPEAERKLRVGEQLELVNL--TKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALD 199
Cdd:cd03295 88 PHMTVEENIALVPKLLKWPKEKIRERADELLALVGLdpAEFADRYPHELSGGQQQRVGVARALAADPPLLLMDEPFGALD 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 200 PLIRTRLQDELLEFQRRLKKTILFVSHDLDEAFRIGNRIAIMEGGRIIQCGTPHDIVKNPADQYVADFVQ 269
Cdd:cd03295 168 PITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDFVAEFVG 237
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-322 |
8.35e-80 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 247.68 E-value: 8.35e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 1 MTAVNFNNVSIIFGDRPetalamvdqgksrdeigaatglvlGVADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVV 80
Cdd:COG3839 1 MASLELENVSKSYGGVE------------------------ALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPT 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 81 RGDVA----VSTTTGPVNpyrcnakalRDlrthtVSMVFQQFALLPWRTVAENVGFGLELAGMPEAERKLRVGEQLELVN 156
Cdd:COG3839 57 SGEILiggrDVTDLPPKD---------RN-----IAMVFQSYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLG 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 157 LTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDPLIRTRLQDELLEFQRRLKKTILFVSHDLDEAFRIGN 236
Cdd:COG3839 123 LEDLLDRKPKQLSGGQRQRVALGRALVREPKVFLLDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLAD 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 237 RIAIMEGGRIIQCGTPHDIVKNPADQYVADFVQNlNPINMLTaADVMQPGLgqTAAGMSVsataraatPLIDVLDALARQ 316
Cdd:COG3839 203 RIAVMNDGRIQQVGTPEELYDRPANLFVAGFIGS-PPMNLLP-GTVEGGGV--RLGGVRL--------PLPAALAAAAGG 270
|
....*.
gi 2087760999 317 PGSIGI 322
Cdd:COG3839 271 EVTLGI 276
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
34-248 |
1.46e-78 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 239.68 E-value: 1.46e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 34 GAATGLVLGVADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTTtgPVNPyrcnakalrdlRTHTVSM 113
Cdd:cd03293 11 GGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGE--PVTG-----------PGPDRGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 114 VFQQFALLPWRTVAENVGFGLELAGMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDE 193
Cdd:cd03293 78 VFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDE 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2087760999 194 PFSALDPLIRTRLQDELLEFQRRLKKTILFVSHDLDEAFRIGNRIAIMEG--GRIIQ 248
Cdd:cd03293 158 PFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLSArpGRIVA 214
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
43-268 |
4.88e-73 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 230.03 E-value: 4.88e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 43 VADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTttgpvnpyrcnakalRDLRTHT------VSMVFQ 116
Cdd:COG1118 18 LDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNG---------------RDLFTNLpprerrVGFVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 117 QFALLPWRTVAENVGFGLELAGMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFS 196
Cdd:COG1118 83 HYALFPHMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLLLDEPFG 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2087760999 197 ALDPLIRTRLQDELLEFQRRLKKTILFVSHDLDEAFRIGNRIAIMEGGRIIQCGTPHDIVKNPADQYVADFV 268
Cdd:COG1118 163 ALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDRPATPFVARFL 234
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
41-268 |
2.51e-69 |
|
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: 216.72 E-value: 2.51e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 41 LGVADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVstttgpvnpyrcNAKALRDLRTHT--VSMVFQQF 118
Cdd:cd03300 14 VALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILL------------DGKDITNLPPHKrpVNTVFQNY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 119 ALLPWRTVAENVGFGLELAGMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSAL 198
Cdd:cd03300 82 ALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGAL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 199 DPLIRTRLQDELLEFQRRLKKTILFVSHDLDEAFRIGNRIAIMEGGRIIQCGTPHDIVKNPADQYVADFV 268
Cdd:cd03300 162 DLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPANRFVADFI 231
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
30-272 |
2.12e-66 |
|
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: 212.97 E-value: 2.12e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 30 RDEIGAATGLvlgvADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVS---TTTGPVnpyrcnakALRDL 106
Cdd:TIGR03265 11 RKRFGAFTAL----KDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGgrdITRLPP--------QKRDY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 107 rthtvSMVFQQFALLPWRTVAENVGFGLELAGMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGA 186
Cdd:TIGR03265 79 -----GIVFQSYALFPNLTVADNIAYGLKNRGMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALATSP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 187 PILLMDEPFSALDPLIRTRLQDELLEFQRRLKKTILFVSHDLDEAFRIGNRIAIMEGGRIIQCGTPHDIVKNPADQYVAD 266
Cdd:TIGR03265 154 GLLLLDEPLSALDARVREHLRTEIRQLQRRLGVTTIMVTHDQEEALSMADRIVVMNHGVIEQVGTPQEIYRHPATPFVAD 233
|
....*.
gi 2087760999 267 FVQNLN 272
Cdd:TIGR03265 234 FVGEVN 239
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
45-268 |
4.60e-66 |
|
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: 208.29 E-value: 4.60e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 45 DASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVstttGPVNPYRCNAKALRDLRTHtVSMVFQQFALLPWR 124
Cdd:COG1127 23 GVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILV----DGQDITGLSEKELYELRRR-IGMLFQGGALFDSL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 125 TVAENVGFGL-ELAGMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDPlIR 203
Cdd:COG1127 98 TVFENVAFPLrEHTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDPEILLYDEPTAGLDP-IT 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2087760999 204 TRLQDEL-LEFQRRLKKTILFVSHDLDEAFRIGNRIAIMEGGRIIQCGTPHDIVKNPaDQYVADFV 268
Cdd:COG1127 177 SAVIDELiRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLASD-DPWVRQFL 241
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
34-269 |
9.08e-63 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 203.39 E-value: 9.08e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 34 GAATGLVLGVADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVS---TTTgpvnpyrCNAKALRDLRtHT 110
Cdd:COG1135 12 PTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDgvdLTA-------LSERELRAAR-RK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 111 VSMVFQQFALLPWRTVAENVGFGLELAGMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILL 190
Cdd:COG1135 84 IGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPKVLL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 191 MDEPFSALDP------LirtrlqdELL-EFQRRLKKTILFVSHDLDEAFRIGNRIAIMEGGRIIQCGTPHDIVKNPADQY 263
Cdd:COG1135 164 CDEATSALDPettrsiL-------DLLkDINRELGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVLDVFANPQSEL 236
|
....*.
gi 2087760999 264 VADFVQ 269
Cdd:COG1135 237 TRRFLP 242
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
4-259 |
1.33e-62 |
|
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: 199.34 E-value: 1.33e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 4 VNFNNVSIIFGDRPETALAmvdqgksrdeigaatglvlgVADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGD 83
Cdd:cd03258 2 IELKNVSKVFGDTGGKVTA--------------------LKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGS 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 84 VAVSTTtgpvNPYRCNAKALRDLRTHtVSMVFQQFALLPWRTVAENVGFGLELAGMPEAERKLRVGEQLELVNLTKWAGR 163
Cdd:cd03258 62 VLVDGT----DLTLLSGKELRKARRR-IGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADA 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 164 KVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDPLIRTRLQDELLEFQRRLKKTILFVSHDLDEAFRIGNRIAIMEG 243
Cdd:cd03258 137 YPAQLSGGQKQRVGIARALANNPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEK 216
|
250
....*....|....*.
gi 2087760999 244 GRIIQCGTPHDIVKNP 259
Cdd:cd03258 217 GEVVEEGTVEEVFANP 232
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-248 |
6.11e-61 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 196.24 E-value: 6.11e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 1 MTAVNFNNVSIIFGDRPETALAMvdqgksrdeigaatglvlgvADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVV 80
Cdd:COG4525 1 MSMLTVRHVSVRYPGGGQPQPAL--------------------QDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPS 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 81 RGDVAVS--TTTGPvnpyrcnaKALRdlrthtvSMVFQQFALLPWRTVAENVGFGLELAGMPEAERKLRVGEQLELVNLT 158
Cdd:COG4525 61 SGEITLDgvPVTGP--------GADR-------GVVFQKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLA 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 159 KWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDPLIRTRLQDELLEFQRRLKKTILFVSHDLDEAFRIGNRI 238
Cdd:COG4525 126 DFARRRIWQLSGGMRQRVGIARALAADPRFLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHSVEEALFLATRL 205
|
250
....*....|..
gi 2087760999 239 AIMEG--GRIIQ 248
Cdd:COG4525 206 VVMSPgpGRIVE 217
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
43-263 |
1.44e-60 |
|
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: 202.44 E-value: 1.44e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 43 VADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVstttGPVNPYRCNAKALRDLRTHtVSMVFQ--QFAL 120
Cdd:COG1123 281 VDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILF----DGKDLTKLSRRSLRELRRR-VQMVFQdpYSSL 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 121 LPWRTVAENVGFGLELAG-MPEAERKLRVGEQLELVNL-TKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSAL 198
Cdd:COG1123 356 NPRMTVGDIIAEPLRLHGlLSRAERRERVAELLERVGLpPDLADRYPHELSGGQRQRVAIARALALEPKLLILDEPTSAL 435
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2087760999 199 DPLIRTRLQDELLEFQRRLKKTILFVSHDLDEAFRIGNRIAIMEGGRIIQCGTPHDIVKNPADQY 263
Cdd:COG1123 436 DVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVFANPQHPY 500
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
43-255 |
3.41e-60 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 193.36 E-value: 3.41e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 43 VADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVStttGpVNPYRCNAKALRDlrthtVSMVFQQFALLP 122
Cdd:COG1131 16 LDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVL---G-EDVARDPAEVRRR-----IGYVPQEPALYP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 123 WRTVAENVGFGLELAGMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDPLI 202
Cdd:COG1131 87 DLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTSGLDPEA 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2087760999 203 RTRLQDELLEFQRRlKKTILFVSHDLDEAFRIGNRIAIMEGGRIIQCGTPHDI 255
Cdd:COG1131 167 RRELWELLRELAAE-GKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDEL 218
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
45-259 |
4.99e-60 |
|
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: 192.55 E-value: 4.99e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 45 DASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVstttgpvNPYRCNAKALRDLRTHtVSMVFQQ-----FA 119
Cdd:COG1122 19 DVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLV-------DGKDITKKNLRELRRK-VGLVFQNpddqlFA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 120 llpwRTVAENVGFGLELAGMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALD 199
Cdd:COG1122 91 ----PTVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLD 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 200 PLIRTRLQDELLEFQRRlKKTILFVSHDLDEAFRIGNRIAIMEGGRIIQCGTPHDIVKNP 259
Cdd:COG1122 167 PRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDY 225
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
58-278 |
6.41e-60 |
|
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: 195.40 E-value: 6.41e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 58 LMGLSGSGKSTLLRAVNGLAPVVRGDVAVS-TTTGPVNPYRcnakalrdlrtHTVSMVFQQFALLPWRTVAENVGFGLEL 136
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDgEDVTNVPPHL-----------RHINMVFQSYALFPHMTVEENVAFGLKM 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 137 AGMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDPLIRTRLQDELLEFQRR 216
Cdd:TIGR01187 70 RKVPRAEIKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQ 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2087760999 217 LKKTILFVSHDLDEAFRIGNRIAIMEGGRIIQCGTPHDIVKNPADQYVADFVQNLNPINMLT 278
Cdd:TIGR01187 150 LGITFVFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFVARFIGEINVFEATV 211
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
45-267 |
1.22e-59 |
|
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: 191.95 E-value: 1.22e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 45 DASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTttgpVNPYRCNAKALRDLRTHtVSMVFQQFALLPWR 124
Cdd:cd03261 18 GVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDG----EDISGLSEAELYRLRRR-MGMLFQSGALFDSL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 125 TVAENVGFGL-ELAGMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDPLIR 203
Cdd:cd03261 93 TVFENVAFPLrEHTRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLYDEPTAGLDPIAS 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2087760999 204 TRLQDELLEFQRRLKKTILFVSHDLDEAFRIGNRIAIMEGGRIIQCGTPHDIvKNPADQYVADF 267
Cdd:cd03261 173 GVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEEL-RASDDPLVRQF 235
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
45-246 |
2.69e-59 |
|
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: 190.39 E-value: 2.69e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 45 DASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTTtgpvNPYRCNAKALRDLRTHTVSMVFQQFALLPWR 124
Cdd:cd03255 22 GVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGT----DISKLSEKELAAFRRRHIGFVFQSFNLLPDL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 125 TVAENVGFGLELAGMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDPLIRT 204
Cdd:cd03255 98 TALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPKIILADEPTGNLDSETGK 177
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2087760999 205 RLQDELLEFQRRLKKTILFVSHDLDEAfRIGNRIAIMEGGRI 246
Cdd:cd03255 178 EVMELLRELNKEAGTTIVVVTHDPELA-EYADRIIELRDGKI 218
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
45-272 |
1.87e-58 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 193.24 E-value: 1.87e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 45 DASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVS--TTTGpVNPYRcnakalRDLRThtvsmVFQQFALLP 122
Cdd:PRK09452 32 NLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDgqDITH-VPAEN------RHVNT-----VFQSYALFP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 123 WRTVAENVGFGLELAGMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDPLI 202
Cdd:PRK09452 100 HMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALDYKL 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 203 RTRLQDELLEFQRRLKKTILFVSHDLDEAFRIGNRIAIMEGGRIIQCGTPHDIVKNPADQYVADFVQNLN 272
Cdd:PRK09452 180 RKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNLFVARFIGEIN 249
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
45-247 |
7.34e-58 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 186.79 E-value: 7.34e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 45 DASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVstttGPVNPYRCNAKALRDLRTHTVSMVFQQFALLPWR 124
Cdd:COG1136 26 GVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLI----DGQDISSLSERELARLRRRHIGFVFQFFNLLPEL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 125 TVAENVGFGLELAGMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDPLIRT 204
Cdd:COG1136 102 TALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNRPKLILADEPTGNLDSKTGE 181
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2087760999 205 RLQDELLEFQRRLKKTILFVSHDLdEAFRIGNRIAIMEGGRII 247
Cdd:COG1136 182 EVLELLRELNRELGTTIVMVTHDP-ELAARADRVIRLRDGRIV 223
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
43-272 |
7.79e-57 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 189.28 E-value: 7.79e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 43 VADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVS-TTTGPVNPYRcnakalrdlrtHTVSMVFQQFALL 121
Cdd:PRK11607 35 VDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDgVDLSHVPPYQ-----------RPINMMFQSYALF 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 122 PWRTVAENVGFGLELAGMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDPL 201
Cdd:PRK11607 104 PHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKK 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2087760999 202 IRTRLQDELLEFQRRLKKTILFVSHDLDEAFRIGNRIAIMEGGRIIQCGTPHDIVKNPADQYVADFVQNLN 272
Cdd:PRK11607 184 LRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAEFIGSVN 254
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
38-250 |
1.06e-56 |
|
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: 183.61 E-value: 1.06e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 38 GLVLGVADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVS----TTTGPvnpyrcnakALRDlrthtVSM 113
Cdd:cd03301 11 GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGgrdvTDLPP---------KDRD-----IAM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 114 VFQQFALLPWRTVAENVGFGLELAGMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDE 193
Cdd:cd03301 77 VFQNYALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2087760999 194 PFSALDPLIRTRLQDELLEFQRRLKKTILFVSHDLDEAFRIGNRIAIMEGGRIIQCG 250
Cdd:cd03301 157 PLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
45-245 |
3.47e-56 |
|
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: 180.85 E-value: 3.47e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 45 DASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTTtgPVNPYRCNAKALRDlrthTVSMVFQQFALLPWR 124
Cdd:cd03229 18 DVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGE--DLTDLEDELPPLRR----RIGMVFQDFALFPHL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 125 TVAENVGFGLelagmpeaerklrvgeqlelvnltkwagrkvnelSGGMQQRVGLARAFATGAPILLMDEPFSALDPLIRT 204
Cdd:cd03229 92 TVLENIALGL----------------------------------SGGQQQRVALARALAMDPDVLLLDEPTSALDPITRR 137
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2087760999 205 RLQDELLEFQRRLKKTILFVSHDLDEAFRIGNRIAIMEGGR 245
Cdd:cd03229 138 EVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
45-268 |
1.84e-55 |
|
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: 181.38 E-value: 1.84e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 45 DASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTTTGpvnpyrcnakALRDLRTHTVSMVFQQFALLPWR 124
Cdd:cd03296 20 DVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDA----------TDVPVQERNVGFVFQHYALFRHM 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 125 TVAENVGFGLEL----AGMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDP 200
Cdd:cd03296 90 TVFDNVAFGLRVkprsERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLDEPFGALDA 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2087760999 201 LIRTRLQDELLEFQRRLKKTILFVSHDLDEAFRIGNRIAIMEGGRIIQCGTPHDIVKNPADQYVADFV 268
Cdd:cd03296 170 KVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPASPFVYSFL 237
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
45-268 |
2.90e-55 |
|
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: 180.61 E-value: 2.90e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 45 DASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVavstttgpvnpyRCNAKALRDL--RTHTVSMVFQQFALLP 122
Cdd:cd03299 17 NVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKI------------LLNGKDITNLppEKRDISYVPQNYALFP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 123 WRTVAENVGFGLELAGMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDPLI 202
Cdd:cd03299 85 HMTVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRT 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2087760999 203 RTRLQDELLEFQRRLKKTILFVSHDLDEAFRIGNRIAIMEGGRIIQCGTPHDIVKNPADQYVADFV 268
Cdd:cd03299 165 KEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPKNEFVAEFL 230
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
47-269 |
2.03e-54 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 178.65 E-value: 2.03e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 47 SLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTTtgPVNPyrcNAKALRDLRTHtVSMVFQQFALLPWRTV 126
Cdd:COG1126 21 SLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGE--DLTD---SKKDINKLRRK-VGMVFQQFNLFPHLTV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 127 AENVGFGLELA-GMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDPlirtR 205
Cdd:COG1126 95 LENVTLAPIKVkKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKVMLFDEPTSALDP----E 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2087760999 206 LQDELLEFQRRLKK---TILFVSHDLDEAFRIGNRIAIMEGGRIIQCGTPHDIVKNPADQYVADFVQ 269
Cdd:COG1126 171 LVGEVLDVMRDLAKegmTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFENPQHERTRAFLS 237
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
34-269 |
7.55e-54 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 180.38 E-value: 7.55e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 34 GAATGLVLGVADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVstttGPVNPYRCNAKALRDLRtHTVSM 113
Cdd:PRK11153 12 PQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLV----DGQDLTALSEKELRKAR-RQIGM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 114 VFQQFALLPWRTVAENVGFGLELAGMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDE 193
Cdd:PRK11153 87 IFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPKVLLCDE 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2087760999 194 PFSALDPLIrTRLQDELL-EFQRRLKKTILFVSHDLDEAFRIGNRIAIMEGGRIIQCGTPHDIVKNPADQYVADFVQ 269
Cdd:PRK11153 167 ATSALDPAT-TRSILELLkDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHPKHPLTREFIQ 242
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
43-250 |
1.57e-53 |
|
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: 175.77 E-value: 1.57e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 43 VADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTTtgPVNPyrcNAKALRDLRTHTVSMVFQ--QFAL 120
Cdd:cd03257 21 LDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGK--DLLK---LSRRLRKIRRKEIQMVFQdpMSSL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 121 LPWRTVAENVGFGLELAGMP--EAERKLRVGEQLELVNLTK-WAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSA 197
Cdd:cd03257 96 NPRMTIGEQIAEPLRIHGKLskKEARKEAVLLLLVGVGLPEeVLNRYPHELSGGQRQRVAIARALALNPKLLIADEPTSA 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2087760999 198 LDPLIRTRLQDELLEFQRRLKKTILFVSHDLDEAFRIGNRIAIMEGGRIIQCG 250
Cdd:cd03257 176 LDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
45-267 |
1.67e-53 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 179.53 E-value: 1.67e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 45 DASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRG-------DVAVSTTTGpvnpyrcnakalRDlrthtVSMVFQQ 117
Cdd:PRK11432 24 NLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGqifidgeDVTHRSIQQ------------RD-----ICMVFQS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 118 FALLPWRTVAENVGFGLELAGMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSA 197
Cdd:PRK11432 87 YALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSN 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 198 LDPLIRTRLQDELLEFQRRLKKTILFVSHDLDEAFRIGNRIAIMEGGRIIQCGTPHDIVKNPADQYVADF 267
Cdd:PRK11432 167 LDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPASRFMASF 236
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
6-245 |
4.52e-53 |
|
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: 174.19 E-value: 4.52e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 6 FNNVSIIFGDRPETALamvdqgksrDEIgaatglvlgvadaSLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVA 85
Cdd:cd03225 2 LKNLSFSYPDGARPAL---------DDI-------------SLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVL 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 86 VstttgpvNPYRCNAKALRDLRTHtVSMVFQ----QFALLpwrTVAENVGFGLELAGMPEAERKLRVGEQLELVNLTKWA 161
Cdd:cd03225 60 V-------DGKDLTKLSLKELRRK-VGLVFQnpddQFFGP---TVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLR 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 162 GRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDPLIRTRLQDELLEFQRRlKKTILFVSHDLDEAFRIGNRIAIM 241
Cdd:cd03225 129 DRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVL 207
|
....
gi 2087760999 242 EGGR 245
Cdd:cd03225 208 EDGK 211
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
45-272 |
1.72e-52 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 177.20 E-value: 1.72e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 45 DASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTTtgpvNPYRCNAkalRDLRthtVSMVFQQFALLPWR 124
Cdd:PRK10851 20 DISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGT----DVSRLHA---RDRK---VGFVFQHYALFRHM 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 125 TVAENVGFGLELagMPEAER------KLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSAL 198
Cdd:PRK10851 90 TVFDNIAFGLTV--LPRRERpnaaaiKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGAL 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2087760999 199 DPLIRTRLQDELLEFQRRLKKTILFVSHDLDEAFRIGNRIAIMEGGRIIQCGTPHDIVKNPADQYVADFVQNLN 272
Cdd:PRK10851 168 DAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREPATRFVLEFMGEVN 241
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
33-260 |
8.46e-52 |
|
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: 179.33 E-value: 8.46e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 33 IGAATGLVLGVADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAP---VVRGDVAVSTttgpvnpyRCNAKALRDLRTH 109
Cdd:COG1123 12 VRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPhggRISGEVLLDG--------RDLLELSEALRGR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 110 TVSMVFQQF--ALLPWrTVAENVGFGLELAGMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAP 187
Cdd:COG1123 84 RIGMVFQDPmtQLNPV-TVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPD 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2087760999 188 ILLMDEPFSALDPLIRTRLQDELLEFQRRLKKTILFVSHDLDEAFRIGNRIAIMEGGRIIQCGTPHDIVKNPA 260
Cdd:COG1123 163 LLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAPQ 235
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
46-267 |
9.13e-52 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 171.48 E-value: 9.13e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 46 ASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVS----TTTGPvnpyrcnakALRdlrthTVSMVFQQFALL 121
Cdd:COG3840 18 FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNgqdlTALPP---------AER-----PVSMLFQENNLF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 122 PWRTVAENVGFGLELAGMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDPL 201
Cdd:COG3840 84 PHLTVAQNIGLGLRPGLKLTAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDPA 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2087760999 202 IRTRLQDELLEFQRRLKKTILFVSHDLDEAFRIGNRIAIMEGGRIIQCGTPHDIVKNPADQYVADF 267
Cdd:COG3840 164 LRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPPALAAY 229
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
43-269 |
3.82e-51 |
|
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: 170.37 E-value: 3.82e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 43 VADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTTtgPVNPyrcnaKALRDLRtHTVSMVFQQF--AL 120
Cdd:COG1124 21 LKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGR--PVTR-----RRRKAFR-RRVQMVFQDPyaSL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 121 LPWRTVAENVGFGLELAGMPEAERklRVGEQLELVNLTK-WAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALD 199
Cdd:COG1124 93 HPRHTVDRILAEPLRIHGLPDREE--RIAELLEQVGLPPsFLDRYPHQLSGGQRQRVAIARALILEPELLLLDEPTSALD 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 200 PLIRTRLQDELLEFQRRLKKTILFVSHDLDEAFRIGNRIAIMEGGRIIQCGTPHDIVKNPADQYVADFVQ 269
Cdd:COG1124 171 VSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAGPKHPYTRELLA 240
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
4-269 |
7.86e-50 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 166.81 E-value: 7.86e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 4 VNFNNVSIIFGDRPetalamvdqgksrdeigaatglVLgvADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGD 83
Cdd:PRK09493 2 IEFKNVSKHFGPTQ----------------------VL--HNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGD 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 84 VAVS--TTTGPvnpyrcnAKALRDLRTHTvSMVFQQFALLPWRTVAENVGFG-LELAGMPEAERKLRVGEQLELVNLTKW 160
Cdd:PRK09493 58 LIVDglKVNDP-------KVDERLIRQEA-GMVFQQFYLFPHLTALENVMFGpLRVRGASKEEAEKQARELLAKVGLAER 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 161 AGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDPlirtRLQDELLEFQRRLKK---TILFVSHDLDEAFRIGNR 237
Cdd:PRK09493 130 AHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTSALDP----ELRHEVLKVMQDLAEegmTMVIVTHEIGFAEKVASR 205
|
250 260 270
....*....|....*....|....*....|..
gi 2087760999 238 IAIMEGGRIIQCGTPHDIVKNPADQYVADFVQ 269
Cdd:PRK09493 206 LIFIDKGRIAEDGDPQVLIKNPPSQRLQEFLQ 237
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
40-255 |
1.29e-49 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 166.39 E-value: 1.29e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 40 VLGVADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVstttGPVNPYRCNAKALRDLRTHtVSMVFQQFA 119
Cdd:COG3638 16 TPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILV----DGQDVTALRGRALRRLRRR-IGMIFQQFN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 120 LLPWRTVAENVgfgleLAGM--------------PEAERkLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATG 185
Cdd:COG3638 91 LVPRLSVLTNV-----LAGRlgrtstwrsllglfPPEDR-ERALEALERVGLADKAYQRADQLSGGQQQRVAIARALVQE 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 186 APILLMDEPFSALDPLIRTRLQDELLEFQRRLKKTILFVSHDLDEAFRIGNRIAIMEGGRIIQCGTPHDI 255
Cdd:COG3638 165 PKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRVVFDGPPAEL 234
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
45-250 |
1.92e-49 |
|
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: 164.78 E-value: 1.92e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 45 DASLTIEEgEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTTtgpvnPYRCNAKALrDLRTHT--VSMVFQQFALLP 122
Cdd:cd03297 16 KIDFDLNE-EVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGT-----VLFDSRKKI-NLPPQQrkIGLVFQQYALFP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 123 WRTVAENVGFGLElaGMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDPLI 202
Cdd:cd03297 89 HLNVRENLAFGLK--RKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRAL 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2087760999 203 RTRLQDELLEFQRRLKKTILFVSHDLDEAFRIGNRIAIMEGGRIIQCG 250
Cdd:cd03297 167 RLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
45-246 |
4.57e-48 |
|
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: 161.16 E-value: 4.57e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 45 DASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTTtgPVNPyrcNAKALRDLRTHtVSMVFQQFALLPWR 124
Cdd:cd03262 18 GIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGL--KLTD---DKKNINELRQK-VGMVFQQFNLFPHL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 125 TVAENVGFGL-ELAGMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDPlir 203
Cdd:cd03262 92 TVLENITLAPiKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFDEPTSALDP--- 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2087760999 204 tRLQDELLEFQRRLKK---TILFVSHDLDEAFRIGNRIAIMEGGRI 246
Cdd:cd03262 169 -ELVGEVLDVMKDLAEegmTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
45-268 |
5.65e-48 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 165.59 E-value: 5.65e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 45 DASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTTtgpvnpyRCNAKALRDlrtHTVSMVFQQFALLPWR 124
Cdd:PRK11000 21 DINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEK-------RMNDVPPAE---RGVGMVFQSYALYPHL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 125 TVAENVGFGLELAGMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDPLIRT 204
Cdd:PRK11000 91 SVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRV 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2087760999 205 RLQDELLEFQRRLKKTILFVSHDLDEAFRIGNRIAIMEGGRIIQCGTPHDIVKNPADQYVADFV 268
Cdd:PRK11000 171 QMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPANRFVAGFI 234
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
47-322 |
5.79e-48 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 165.40 E-value: 5.79e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 47 SLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTTtgPVN---PyrcnakALRDlrthtVSMVFQQFALLPW 123
Cdd:PRK11650 24 DLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGR--VVNeleP------ADRD-----IAMVFQNYALYPH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 124 RTVAENVGFGLELAGMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDPLIR 203
Cdd:PRK11650 91 MSVRENMAYGLKIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDAKLR 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 204 TRLQDELLEFQRRLKKTILFVSHDLDEAFRIGNRIAIMEGGRIIQCGTPHDIVKNPADQYVADFVQNlNPINMLTAAdvm 283
Cdd:PRK11650 171 VQMRLEIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGGVAEQIGTPVEVYEKPASTFVASFIGS-PAMNLLDGR--- 246
|
250 260 270
....*....|....*....|....*....|....*....
gi 2087760999 284 qpglgQTAAGMSVSATARAATPLIDVLDALARQPGSIGI 322
Cdd:PRK11650 247 -----VSADGAAFELAGGIALPLGGGYRQYAGRKLTLGI 280
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
38-255 |
6.73e-48 |
|
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: 161.95 E-value: 6.73e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 38 GLVLGVADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTttgpVNPYRCNAKALRDLrthtvSMVFQQ 117
Cdd:COG4555 12 GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDG----EDVRKEPREARRQI-----GVLPDE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 118 FALLPWRTVAENVGFGLELAGMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSA 197
Cdd:COG4555 83 RGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTNG 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2087760999 198 LDPLIRTRLQDELLEFqRRLKKTILFVSHDLDEAFRIGNRIAIMEGGRIIQCGTPHDI 255
Cdd:COG4555 163 LDVMARRLLREILRAL-KKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDEL 219
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
43-256 |
7.83e-48 |
|
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: 161.75 E-value: 7.83e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 43 VADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVavstttgpvnpyRCNAKALRDLRTH----TVSMVFQQF 118
Cdd:COG1120 17 LDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEV------------LLDGRDLASLSRRelarRIAYVPQEP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 119 ALlPWR-TVAENVGFG----LELAGMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDE 193
Cdd:COG1120 85 PA-PFGlTVRELVALGryphLGLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLLLDE 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2087760999 194 PFSALDPlirtRLQDELLEFQRRL----KKTILFVSHDLDEAFRIGNRIAIMEGGRIIQCGTPHDIV 256
Cdd:COG1120 164 PTSHLDL----AHQLEVLELLRRLarerGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEVL 226
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
45-255 |
8.66e-48 |
|
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: 161.58 E-value: 8.66e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 45 DASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTTtgPVNPYRcnAKALRDLRTHtVSMVFQQFALLPWR 124
Cdd:cd03256 19 DVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGT--DINKLK--GKALRQLRRQ-IGMIFQQFNLIERL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 125 TVAENVGFGL--------ELAGMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFS 196
Cdd:cd03256 94 SVLENVLSGRlgrrstwrSLFGLFPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIARALMQQPKLILADEPVA 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2087760999 197 ALDPLIRTRLQDELLEFQRRLKKTILFVSHDLDEAFRIGNRIAIMEGGRIIQCGTPHDI 255
Cdd:cd03256 174 SLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAEL 232
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
43-260 |
5.13e-47 |
|
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: 161.76 E-value: 5.13e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 43 VADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAP---VVRGDVAVstttGPVNPYRCNAKALRDLRTHTVSMVFQ--Q 117
Cdd:COG0444 21 VDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPppgITSGEILF----DGEDLLKLSEKELRKIRGREIQMIFQdpM 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 118 FALLPWRTVAENVGFGLEL-AGMPEAERKLRVGEQLELVNLTKWAGRKVN---ELSGGMQQRVGLARAFATGAPILLMDE 193
Cdd:COG0444 97 TSLNPVMTVGDQIAEPLRIhGGLSKAEARERAIELLERVGLPDPERRLDRyphELSGGMRQRVMIARALALEPKLLIADE 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2087760999 194 PFSALDPLIRTRLQDELLEFQRRLKKTILFVSHDLDEAFRIGNRIAIMEGGRIIQCGTPHDIVKNPA 260
Cdd:COG0444 177 PTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGPVEELFENPR 243
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
4-247 |
1.03e-46 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 157.91 E-value: 1.03e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 4 VNFNNVSIIFGDRPEtALAmvdqgksrdeigaatglvlgvaDASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGD 83
Cdd:COG2884 2 IRFENVSKRYPGGRE-ALS----------------------DVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQ 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 84 VAVstttGPVNPYRCNAKALRDLRTHtVSMVFQQFALLPWRTVAENVGFGLELAGMPEAERKLRVGEQLELVNLTKWAGR 163
Cdd:COG2884 59 VLV----NGQDLSRLKRREIPYLRRR-IGVVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKA 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 164 KVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDPLIRTRLQDELLEFQRRlKKTILFVSHDLDEAFRIGNRIAIMEG 243
Cdd:COG2884 134 LPHELSGGEQQRVAIARALVNRPELLLADEPTGNLDPETSWEIMELLEEINRR-GTTVLIATHDLELVDRMPKRVLELED 212
|
....
gi 2087760999 244 GRII 247
Cdd:COG2884 213 GRLV 216
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
44-231 |
3.91e-46 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 157.55 E-value: 3.91e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 44 ADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAV--STTTGPvnpyrcnaKALRdlrthtvSMVFQQFALL 121
Cdd:PRK11248 18 EDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLdgKPVEGP--------GAER-------GVVFQNEGLL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 122 PWRTVAENVGFGLELAGMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDPL 201
Cdd:PRK11248 83 PWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAF 162
|
170 180 190
....*....|....*....|....*....|
gi 2087760999 202 IRTRLQDELLEFQRRLKKTILFVSHDLDEA 231
Cdd:PRK11248 163 TREQMQTLLLKLWQETGKQVLLITHDIEEA 192
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
45-255 |
2.31e-45 |
|
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: 154.65 E-value: 2.31e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 45 DASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGdvavSTTTGPVNPYRCNAKALRD----LRThTVSMVFQQFAL 120
Cdd:cd03260 18 DISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPG----APDEGEVLLDGKDIYDLDVdvleLRR-RVGMVFQKPNP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 121 LPwRTVAENVGFGLELAGM-PEAERKLRVGEQLELVNLTKWAGRKVN--ELSGGMQQRVGLARAFATGAPILLMDEPFSA 197
Cdd:cd03260 93 FP-GSIYDNVAYGLRLHGIkLKEELDERVEEALRKAALWDEVKDRLHalGLSGGQQQRLCLARALANEPEVLLLDEPTSA 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 198 LDPlIRTRLQDELLefqRRLKK--TILFVSHDLDEAFRIGNRIAIMEGGRIIQCGTPHDI 255
Cdd:cd03260 172 LDP-ISTAKIEELI---AELKKeyTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
45-244 |
2.73e-45 |
|
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: 154.55 E-value: 2.73e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 45 DASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVS----TTTGPVNpyrcnakalrdlrthtvSMVFQQFAL 120
Cdd:TIGR01184 3 GVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEgkqiTEPGPDR-----------------MVVFQNYSL 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 121 LPWRTVAENVGFGLE--LAGMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSAL 198
Cdd:TIGR01184 66 LPWLTVRENIALAVDrvLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGAL 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2087760999 199 DPLIRTRLQDELLEFQRRLKKTILFVSHDLDEAFRIGNRIAIMEGG 244
Cdd:TIGR01184 146 DALTRGNLQEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
45-260 |
1.59e-44 |
|
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: 156.41 E-value: 1.59e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 45 DASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTTTgpvnpyRCNAKALRDLRTH--TVSMVFQQFALLP 122
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEV------LQDSARGIFLPPHrrRIGYVFQEARLFP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 123 WRTVAENVGFGLELAgmPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDpli 202
Cdd:COG4148 91 HLSVRGNLLYGRKRA--PRAERRISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALD--- 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2087760999 203 rTRLQDELLEFQRRLKKT----ILFVSHDLDEAFRIGNRIAIMEGGRIIQCGTPHDIVKNPA 260
Cdd:COG4148 166 -LARKAEILPYLERLRDEldipILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRPD 226
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
45-259 |
8.20e-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 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: 152.22 E-value: 8.20e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 45 DASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVstttGPVNPYRCNAKALRDLRtHTVSMVFQQ-----FA 119
Cdd:TIGR04521 23 DVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTI----DGRDITAKKKKKLKDLR-KKVGLVFQFpehqlFE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 120 llpwRTVAENVGFGLELAGMPEAERKLRVGEQLELVNLT-KWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSAL 198
Cdd:TIGR04521 98 ----ETVYKDIAFGPKNLGLSEEEAEERVKEALELVGLDeEYLERSPFELSGGQMRRVAIAGVLAMEPEVLILDEPTAGL 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2087760999 199 DPLIRTRLQDELLEFQRRLKKTILFVSHDLDEAFRIGNRIAIMEGGRIIQCGTPHDIVKNP 259
Cdd:TIGR04521 174 DPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVFSDV 234
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
42-255 |
3.15e-43 |
|
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: 149.76 E-value: 3.15e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 42 GVADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTTtgpvNPYRCNAKALRDLRTHTvSMVFQQFALL 121
Cdd:TIGR02315 17 ALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGT----DITKLRGKKLRKLRRRI-GMIFQHYNLI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 122 PWRTVAENV--------GFGLELAGMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDE 193
Cdd:TIGR02315 92 ERLTVLENVlhgrlgykPTWRSLLGRFSEEDKERALSALERVGLADKAYQRADQLSGGQQQRVAIARALAQQPDLILADE 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2087760999 194 PFSALDPLIRTRLQDELLEFQRRLKKTILFVSHDLDEAFRIGNRIAIMEGGRIIQCGTPHDI 255
Cdd:TIGR02315 172 PIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSEL 233
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
43-252 |
3.47e-43 |
|
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: 148.81 E-value: 3.47e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 43 VADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAV---STTTGPVNPYRCnakalrdlrthtVSMVFQQFA 119
Cdd:cd03263 18 VDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYIngySIRTDRKAARQS------------LGYCPQFDA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 120 LLPWRTVAENVGFGLELAGMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALD 199
Cdd:cd03263 86 LFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2087760999 200 PLIRTRLQDELLEFQRrlKKTILFVSHDLDEAFRIGNRIAIMEGGRIIQCGTP 252
Cdd:cd03263 166 PASRRAIWDLILEVRK--GRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSP 216
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-255 |
1.02e-41 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 145.62 E-value: 1.02e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 1 MTAVNFNNVSIIFGDRPetalamvdqgksrdeigaatglVLgvADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVV 80
Cdd:COG1121 4 MPAIELENLTVSYGGRP----------------------VL--EDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPT 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 81 RGDVavstttgpvnpyRCNAKALRDLRtHTVSMVFQQFALlPWR---TVAENVGFGL----ELAGMPEAERKLRVGEQLE 153
Cdd:COG1121 60 SGTV------------RLFGKPPRRAR-RRIGYVPQRAEV-DWDfpiTVRDVVLMGRygrrGLFRRPSRADREAVDEALE 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 154 LVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDPLIRTRLQDeLLEFQRRLKKTILFVSHDLDEAFR 233
Cdd:COG1121 126 RVGLEDLADRPIGELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYE-LLRELRREGKTILVVTHDLGAVRE 204
|
250 260
....*....|....*....|..
gi 2087760999 234 IGNRIAIMEgGRIIQCGTPHDI 255
Cdd:COG1121 205 YFDRVLLLN-RGLVAHGPPEEV 225
|
|
| 3a0107s01c2 |
TIGR00972 |
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein ... |
45-268 |
1.94e-41 |
|
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: 145.13 E-value: 1.94e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 45 DASLTIEEGEILVLMGLSGSGKSTLLRAVN---GLAPVVRGDVAVSTTTGPVNPYRCNAKALRdlrtHTVSMVFQQFALL 121
Cdd:TIGR00972 19 NINLDIPKNQVTALIGPSGCGKSTLLRSLNrmnDLVPGVRIEGKVLFDGQDIYDKKIDVVELR----RRVGMVFQKPNPF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 122 PwRTVAENVGFGLELAGM-PEAERKLRVGEQLELVNLtkWAGRK------VNELSGGMQQRVGLARAFATGAPILLMDEP 194
Cdd:TIGR00972 95 P-MSIYDNIAYGPRLHGIkDKKELDEIVEESLKKAAL--WDEVKdrlhdsALGLSGGQQQRLCIARALAVEPEVLLLDEP 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2087760999 195 FSALDPlIRTRlqdELLEFQRRLKK--TILFVSHDLDEAFRIGNRIAIMEGGRIIQCGTPHDIVKNPADQYVADFV 268
Cdd:TIGR00972 172 TSALDP-IATG---KIEELIQELKKkyTIVIVTHNMQQAARISDRTAFFYDGELVEYGPTEQIFTNPKEKRTEDYI 243
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
45-246 |
1.09e-40 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 141.88 E-value: 1.09e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 45 DASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVavstttgpvnpyRCNAKALRDLRTHT----VSMVFQQFAL 120
Cdd:COG4619 18 PVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEI------------YLDGKPLSAMPPPEwrrqVAYVPQEPAL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 121 lpWR-TVAENVGFGLELAGMPEAERKLRvgEQLELVNLTKWA-GRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSAL 198
Cdd:COG4619 86 --WGgTVRDNLPFPFQLRERKFDRERAL--ELLERLGLPPDIlDKPVERLSGGERQRLALIRALLLQPDVLLLDEPTSAL 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2087760999 199 DPLIRTRLQDELLEFQRRLKKTILFVSHDLDEAFRIGNRIAIMEGGRI 246
Cdd:COG4619 162 DPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
45-246 |
1.21e-40 |
|
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: 140.61 E-value: 1.21e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 45 DASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVStttGpVNPYRCNAKALRDlrthtVSMVFQQFALLPWR 124
Cdd:cd03230 18 DISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVL---G-KDIKKEPEEVKRR-----IGYLPEEPSLYENL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 125 TVAENVgfglelagmpeaerklrvgeqlelvnltkwagrkvnELSGGMQQRVGLARAFATGAPILLMDEPFSALDPLIRT 204
Cdd:cd03230 89 TVRENL------------------------------------KLSGGMKQRLALAQALLHDPELLILDEPTSGLDPESRR 132
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2087760999 205 RLQDELLEFQRRlKKTILFVSHDLDEAFRIGNRIAIMEGGRI 246
Cdd:cd03230 133 EFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
45-245 |
2.39e-40 |
|
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: 141.23 E-value: 2.39e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 45 DASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTTtgPVNPYRCNAKALrdLRTHtVSMVFQQFALLPWR 124
Cdd:TIGR02673 20 DVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGE--DVNRLRGRQLPL--LRRR-IGVVFQDFRLLPDR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 125 TVAENVGFGLELAGMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDPLIRT 204
Cdd:TIGR02673 95 TVYENVALPLEVRGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPPLLLADEPTGNLDPDLSE 174
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2087760999 205 RLQDELLEFQRRlKKTILFVSHDLDEAFRIGNRIAIMEGGR 245
Cdd:TIGR02673 175 RILDLLKRLNKR-GTTVIVATHDLSLVDRVAHRVIILDDGR 214
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
43-250 |
5.53e-40 |
|
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: 139.11 E-value: 5.53e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 43 VADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVstttgpvnpyrcNAKALRDLrthtvsmvfqqfallP 122
Cdd:cd03214 15 LDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILL------------DGKDLASL---------------S 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 123 WRTVAENVGFglelagMPEAerklrvgeqLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDPli 202
Cdd:cd03214 68 PKELARKIAY------VPQA---------LELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDI-- 130
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2087760999 203 rtRLQDELLEFQRRLK----KTILFVSHDLDEAFRIGNRIAIMEGGRIIQCG 250
Cdd:cd03214 131 --AHQIELLELLRRLArergKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
45-268 |
6.29e-40 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 141.33 E-value: 6.29e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 45 DASLTIEEGEILVLMGLSGSGKSTLLRAVNG---LAPVVR--GDVAV------STTTGPVnpyrcnakalrDLRTHtVSM 113
Cdd:COG1117 29 DINLDIPENKVTALIGPSGCGKSTLLRCLNRmndLIPGARveGEILLdgediyDPDVDVV-----------ELRRR-VGM 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 114 VFQQFALLPWrTVAENVGFGLELAGM-PEAERKLRVGEQLELVNLtkWagrkvNE-----------LSGGMQQRVGLARA 181
Cdd:COG1117 97 VFQKPNPFPK-SIYDNVAYGLRLHGIkSKSELDEIVEESLRKAAL--W-----DEvkdrlkksalgLSGGQQQRLCIARA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 182 FATGAPILLMDEPFSALDPlIRTRLQDELLefqRRLKK--TILFVSHDLDEAFRIGNRIAIMEGGRIIQCGTPHDIVKNP 259
Cdd:COG1117 169 LAVEPEVLLMDEPTSALDP-ISTAKIEELI---LELKKdyTIVIVTHNMQQAARVSDYTAFFYLGELVEFGPTEQIFTNP 244
|
....*....
gi 2087760999 260 ADQYVADFV 268
Cdd:COG1117 245 KDKRTEDYI 253
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
43-257 |
9.78e-40 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 141.69 E-value: 9.78e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 43 VADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTTTgpvnpyrCNAKALRDLRTHtVSMVFQ----QF 118
Cdd:PRK13635 23 LKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMV-------LSEETVWDVRRQ-VGMVFQnpdnQF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 119 AllpWRTVAENVGFGLELAGMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSAL 198
Cdd:PRK13635 95 V---GATVQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSML 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2087760999 199 DPLIRtrlqDELLEFQRRLKK----TILFVSHDLDEAFRiGNRIAIMEGGRIIQCGTPHDIVK 257
Cdd:PRK13635 172 DPRGR----REVLETVRQLKEqkgiTVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEIFK 229
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
45-267 |
4.19e-39 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 138.99 E-value: 4.19e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 45 DASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAV-------STTTGPvnpyrcnaKALRDLRtHTVSMVFQQ 117
Cdd:PRK11124 20 DITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIagnhfdfSKTPSD--------KAIRELR-RNVGMVFQQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 118 FALLPWRTVAENVgfgLE----LAGMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDE 193
Cdd:PRK11124 91 YNLWPHLTVQQNL---IEapcrVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDE 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2087760999 194 PFSALDPLIRTRLQDELLEFQrRLKKTILFVSHDLDEAFRIGNRIAIMEGGRIIQCGTpHDIVKNPADQYVADF 267
Cdd:PRK11124 168 PTAALDPEITAQIVSIIRELA-ETGITQVIVTHEVEVARKTASRVVYMENGHIVEQGD-ASCFTQPQTEAFKNY 239
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
45-258 |
7.64e-39 |
|
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: 138.72 E-value: 7.64e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 45 DASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTTTgpvnpyRCNAKALRDLRTHtVSMVFQ----QF-- 118
Cdd:TIGR04520 20 NVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLD------TLDEENLWEIRKK-VGMVFQnpdnQFvg 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 119 AllpwrTVAENVGFGLELAGMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSAL 198
Cdd:TIGR04520 93 A-----TVEDDVAFGLENLGVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLAMRPDIIILDEATSML 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 199 DPLIRTRLQDELLEFQRRLKKTILFVSHDLDEAFRiGNRIAIMEGGRIIQCGTPHDIVKN 258
Cdd:TIGR04520 168 DPKGRKEVLETIRKLNKEEGITVISITHDMEEAVL-ADRVIVMNKGKIVAEGTPREIFSQ 226
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
45-196 |
2.23e-38 |
|
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: 133.93 E-value: 2.23e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 45 DASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVStttGPVNPYRCnakaLRDLRTHtVSMVFQQFALLPWR 124
Cdd:pfam00005 3 NVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLD---GQDLTDDE----RKSLRKE-IGYVFQDPQLFPRL 74
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2087760999 125 TVAENVGFGLELAGMPEAERKLRVGEQLELVNLTKWAGRKV----NELSGGMQQRVGLARAFATGAPILLMDEPFS 196
Cdd:pfam00005 75 TVRENLRLGLLLKGLSKREKDARAEEALEKLGLGDLADRPVgerpGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
45-268 |
3.02e-38 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 136.83 E-value: 3.02e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 45 DASLTIEEGEILVLMGLSGSGKSTLLRAVN---GLAPVVrgdvavsTTTGPVNpYrcNAKALRDLRTHTVS------MVF 115
Cdd:PRK14239 23 SVSLDFYPNEITALIGPSGSGKSTLLRSINrmnDLNPEV-------TITGSIV-Y--NGHNIYSPRTDTVDlrkeigMVF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 116 QQFALLPWrTVAENVGFGLELAGMPEAERKLRVGEQlELVNLTKWAGRK------VNELSGGMQQRVGLARAFATGAPIL 189
Cdd:PRK14239 93 QQPNPFPM-SIYENVVYGLRLKGIKDKQVLDEAVEK-SLKGASIWDEVKdrlhdsALGLSGGQQQRVCIARVLATSPKII 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2087760999 190 LMDEPFSALDPLIRTRLQDELLEFQRrlKKTILFVSHDLDEAFRIGNRIAIMEGGRIIQCGTPHDIVKNPADQYVADFV 268
Cdd:PRK14239 171 LLDEPTSALDPISAGKIEETLLGLKD--DYTMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQMFMNPKHKETEDYI 247
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
45-267 |
8.58e-38 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 135.53 E-value: 8.58e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 45 DASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVST-----TTGPvnpyrcNAKALRDLRtHTVSMVFQQFA 119
Cdd:COG4161 20 DINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGhqfdfSQKP------SEKAIRLLR-QKVGMVFQQYN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 120 LLPWRTVAENVgfgLE----LAGMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPF 195
Cdd:COG4161 93 LWPHLTVMENL---IEapckVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPT 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2087760999 196 SALDPLIrtrlQDELLEFQRRLKKT-I--LFVSHDLDEAFRIGNRIAIMEGGRIIQCGTpHDIVKNPADQYVADF 267
Cdd:COG4161 170 AALDPEI----TAQVVEIIRELSQTgItqVIVTHEVEFARKVASQVVYMEKGRIIEQGD-ASHFTQPQTEAFAHY 239
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
34-263 |
1.81e-37 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 136.79 E-value: 1.81e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 34 GAATGLVLGVADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVavstTTGPVNPYRCNAKALRDLRTHtVSM 113
Cdd:COG4608 25 GRTVGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEI----LFDGQDITGLSGRELRPLRRR-MQM 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 114 VFQQ-FALL-PWRTVAENVGFGLELAGM-PEAERKLRVGEQLELVNL-TKWAGRKVNELSGGMQQRVGLARAFATGAPIL 189
Cdd:COG4608 100 VFQDpYASLnPRMTVGDIIAEPLRIHGLaSKAERRERVAELLELVGLrPEHADRYPHEFSGGQRQRIGIARALALNPKLI 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2087760999 190 LMDEPFSALDPLIRTRLQDELLEFQRRLKKTILFVSHDLDEAFRIGNRIAIMEGGRIIQCGTPHDIVKNPADQY 263
Cdd:COG4608 180 VCDEPVSALDVSIQAQVLNLLEDLQDELGLTYLFISHDLSVVRHISDRVAVMYLGKIVEIAPRDELYARPLHPY 253
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
43-260 |
2.95e-37 |
|
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: 134.40 E-value: 2.95e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 43 VADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAV--STTTGpVNPYRCNAKALRdlRThtvsmvFQQFAL 120
Cdd:COG0411 20 VDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFdgRDITG-LPPHRIARLGIA--RT------FQNPRL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 121 LPWRTVAENV---------------GFGLELAGMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATG 185
Cdd:COG0411 91 FPELTVLENVlvaaharlgrgllaaLLRLPRARREEREARERAEELLERVGLADRADEPAGNLSYGQQRRLEIARALATE 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2087760999 186 APILLMDEPFSALDPLIRTRLQDELLEFQRRLKKTILFVSHDLDEAFRIGNRIAIMEGGRIIQCGTPHDIVKNPA 260
Cdd:COG0411 171 PKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGTPAEVRADPR 245
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
47-250 |
7.96e-37 |
|
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: 131.85 E-value: 7.96e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 47 SLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDV---AVSTTTGPVnpyrcnakALRdlrthTVSMVFQQFALLPW 123
Cdd:cd03298 18 DLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVlinGVDVTAAPP--------ADR-----PVSMLFQENNLFAH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 124 RTVAENVGFGLELAGMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDPLIR 203
Cdd:cd03298 85 LTVEQNVGLGLSPGLKLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALR 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2087760999 204 TRLQDELLEFQRRLKKTILFVSHDLDEAFRIGNRIAIMEGGRIIQCG 250
Cdd:cd03298 165 AEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
45-245 |
1.02e-36 |
|
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: 130.06 E-value: 1.02e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 45 DASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVstttgpvNPYRCNAKALRDLRTHtVSMVFQqfallpwr 124
Cdd:cd00267 17 NVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILI-------DGKDIAKLPLEELRRR-IGYVPQ-------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 125 tvaenvgfglelagmpeaerklrvgeqlelvnltkwagrkvneLSGGMQQRVGLARAFATGAPILLMDEPFSALDPLIRT 204
Cdd:cd00267 81 -------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRE 117
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2087760999 205 RLQDELLEFQRRlKKTILFVSHDLDEAFRIGNRIAIMEGGR 245
Cdd:cd00267 118 RLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
45-238 |
1.57e-35 |
|
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: 128.50 E-value: 1.57e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 45 DASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTTTGPvnpyRCNAKALRDLRTHTVSMVFQQFALLPWR 124
Cdd:TIGR03608 16 DLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETP----PLNSKKASKFRREKLGYLFQNFALIENE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 125 TVAENVGFGLELAGMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDPliRT 204
Cdd:TIGR03608 92 TVEENLDLGLKYKKLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLILADEPTGSLDP--KN 169
|
170 180 190
....*....|....*....|....*....|....*..
gi 2087760999 205 RlqDELLEFQRRLK---KTILFVSHDLdEAFRIGNRI 238
Cdd:TIGR03608 170 R--DEVLDLLLELNdegKTIIIVTHDP-EVAKQADRV 203
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
43-260 |
1.77e-35 |
|
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: 129.09 E-value: 1.77e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 43 VADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVA---VSTTTGPvnPYRCNAKALRdlRThtvsmvFQQFA 119
Cdd:cd03219 16 LDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLfdgEDITGLP--PHEIARLGIG--RT------FQIPR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 120 LLPWRTVAENV--------GFGLELAGMPEAERKLR--VGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPIL 189
Cdd:cd03219 86 LFPELTVLENVmvaaqartGSGLLLARARREEREARerAEELLERVGLADLADRPAGELSYGQQRRLEIARALATDPKLL 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2087760999 190 LMDEPFSALDPlirtRLQDELLEFQRRLKK---TILFVSHDLDEAFRIGNRIAIMEGGRIIQCGTPHDIVKNPA 260
Cdd:cd03219 166 LLDEPAAGLNP----EETEELAELIRELRErgiTVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRNNPR 235
|
|
| PhnK |
COG4107 |
ABC-type phosphonate transport system, ATPase component PhnK [Inorganic ion transport and ... |
34-250 |
1.86e-35 |
|
ABC-type phosphonate transport system, ATPase component PhnK [Inorganic ion transport and metabolism];
Pssm-ID: 443283 [Multi-domain] Cd Length: 262 Bit Score: 129.93 E-value: 1.86e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 34 GAATGLVLGVADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTT-TGPVNPYRCNAKALRDLRTHTVS 112
Cdd:COG4107 19 GPGCGTVVACRDVSFDLYPGEVLGIVGESGSGKSTLLKCLYFDLAPTSGSVYYRDRdGGPRDLFALSEAERRRLRRTDWG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 113 MVFQQ--FALLPWRTVAENVGFGLELAGMPEAER-KLRVGEQLELVNLTkwAGRKVNE---LSGGMQQRVGLARAFATGA 186
Cdd:COG4107 99 MVYQNprDGLRMDVSAGGNIAERLMAAGERHYGDiRARALEWLERVEIP--LERIDDLprtFSGGMQQRVQIARALVTNP 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2087760999 187 PILLMDEPFSALDPLIRTRLQDELLEFQRRLKKTILFVSHDLDEAFRIGNRIAIMEGGRIIQCG 250
Cdd:COG4107 177 RLLFLDEPTTGLDVSVQARLLDLIRRLQRELGLSMIVVTHDLGVIRLLADRTMVMKNGRVVESG 240
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
47-231 |
3.49e-35 |
|
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: 127.21 E-value: 3.49e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 47 SLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTTtgpvnpyrcNAKALRDLRTHTVSMVFQQFALLPWRTV 126
Cdd:COG4133 22 SFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGE---------PIRDAREDYRRRLAYLGHADGLKPELTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 127 AENVGFGLELAGMPEAERklRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDPLIRTRL 206
Cdd:COG4133 93 RENLRFWAALYGLRADRE--AIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGVALL 170
|
170 180
....*....|....*....|....*
gi 2087760999 207 QDELLEFQRRlKKTILFVSHDLDEA 231
Cdd:COG4133 171 AELIAAHLAR-GGAVLLTTHQPLEL 194
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
43-263 |
4.11e-35 |
|
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. NikD and NikE are homologous. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131817 [Multi-domain] Cd Length: 230 Bit Score: 127.87 E-value: 4.11e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 43 VADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAP----VVRGDVAVSTTtgPVNPYRcnakalrdLRTHTVSMVFQ-- 116
Cdd:TIGR02770 2 VQDLNLSLKRGEVLALVGESGSGKSLTCLAILGLLPpgltQTSGEILLDGR--PLLPLS--------IRGRHIATIMQnp 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 117 QFALLPWRTVAENVGFGLELAGMPEAERKLRVGEQLELVNLTKwaGRKV-----NELSGGMQQRVGLARAFATGAPILLM 191
Cdd:TIGR02770 72 RTAFNPLFTMGNHAIETLRSLGKLSKQARALILEALEAVGLPD--PEEVlkkypFQLSGGMLQRVMIALALLLEPPFLIA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2087760999 192 DEPFSALDPLIRTRLQDELLEFQRRLKKTILFVSHDLDEAFRIGNRIAIMEGGRIIQCGTPHDIVKNPADQY 263
Cdd:TIGR02770 150 DEPTTDLDVVNQARVLKLLRELRQLFGTGILLITHDLGVVARIADEVAVMDDGRIVERGTVKEIFYNPKHET 221
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
47-262 |
1.15e-34 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 127.01 E-value: 1.15e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 47 SLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTttgpvNPYRCNAKALRdlrthTVSMVFQQFALLPWRTV 126
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNG-----QDHTTTPPSRR-----PVSMLFQENNLFSHLTV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 127 AENVGFGLELAGMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDPLIRT-- 204
Cdd:PRK10771 89 AQNIGLGLNPGLKLNAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQem 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2087760999 205 -RLQDELLEfQRRLkkTILFVSHDLDEAFRIGNRIAIMEGGRIIQCGTPHDIVKNPADQ 262
Cdd:PRK10771 169 lTLVSQVCQ-ERQL--TLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELLSGKASA 224
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
45-265 |
1.50e-34 |
|
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: 129.85 E-value: 1.50e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 45 DASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTTTgpvnpyRCNAKALRDLRTH--TVSMVFQQFALLP 122
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRT------LFDSRKGIFLPPEkrRIGYVFQEARLFP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 123 WRTVAENVGFGLELAgMPEaERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDpli 202
Cdd:TIGR02142 89 HLSVRGNLRYGMKRA-RPS-ERRISFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALD--- 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2087760999 203 rTRLQDELLEFQRRLKKT----ILFVSHDLDEAFRIGNRIAIMEGGRIIQCGTPHDIVKNPADQYVA 265
Cdd:TIGR02142 164 -DPRKYEILPYLERLHAEfgipILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPDLPWLA 229
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
45-258 |
1.72e-34 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 127.86 E-value: 1.72e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 45 DASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVstttGPVNPYRCNAKaLRDLRTHtVSMVFQ--QFALLP 122
Cdd:PRK13637 25 NVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIII----DGVDITDKKVK-LSDIRKK-VGLVFQypEYQLFE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 123 wRTVAENVGFGLELAGMPEAERKLRVGEQLELVNLT--KWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDP 200
Cdd:PRK13637 99 -ETIEKDIAFGPINLGLSEEEIENRVKRAMNIVGLDyeDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDP 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2087760999 201 LIRTRLQDELLEFQRRLKKTILFVSHDLDEAFRIGNRIAIMEGGRIIQCGTPHDIVKN 258
Cdd:PRK13637 178 KGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVFKE 235
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
45-248 |
1.74e-34 |
|
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: 126.39 E-value: 1.74e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 45 DASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTTtgPVNPYRCNAKALrdLRTHTVSMVFQQFALLPWR 124
Cdd:COG4181 30 GISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQ--DLFALDEDARAR--LRARHVGFVFQSFQLLPTL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 125 TVAENVGFGLELAGMPEAERKLRvgEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDPLIRT 204
Cdd:COG4181 106 TALENVMLPLELAGRRDARARAR--ALLERVGLGHRLDHYPAQLSGGEQQRVALARAFATEPAILFADEPTGNLDAATGE 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2087760999 205 RLQDELLEFQRRLKKTILFVSHDLDEAFRIGnRIAIMEGGRIIQ 248
Cdd:COG4181 184 QIIDLLFELNRERGTTLVLVTHDPALAARCD-RVLRLRAGRLVE 226
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
45-257 |
1.94e-34 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 132.06 E-value: 1.94e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 45 DASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVStttG-PVNPyrcnaKALRDLRTHTVSMVFQQFALLPW 123
Cdd:COG1129 22 GVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLD---GePVRF-----RSPRDAQAAGIAIIHQELNLVPN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 124 RTVAENVGFGLELAGMP---EAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDP 200
Cdd:COG1129 94 LSVAENIFLGREPRRGGlidWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRDARVLILDEPTASLTE 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2087760999 201 lirtRLQDELLEFQRRLKK---TILFVSHDLDEAFRIGNRIAIMEGGRIIQCG-----TPHDIVK 257
Cdd:COG1129 174 ----REVERLFRIIRRLKAqgvAIIYISHRLDEVFEIADRVTVLRDGRLVGTGpvaelTEDELVR 234
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
40-246 |
3.48e-34 |
|
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: 125.21 E-value: 3.48e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 40 VLGVADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTTtgPVNPYRCNAKALrdLRTHtVSMVFQQFA 119
Cdd:cd03292 14 TAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQ--DVSDLRGRAIPY--LRRK-IGVVFQDFR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 120 LLPWRTVAENVGFGLELAGMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALD 199
Cdd:cd03292 89 LLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLD 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2087760999 200 PLIRTRLQDELLEFQRRlKKTILFVSHDLDEAFRIGNRIAIMEGGRI 246
Cdd:cd03292 169 PDTTWEIMNLLKKINKA-GTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
38-252 |
4.28e-34 |
|
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: 125.17 E-value: 4.28e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 38 GLVLGVADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGdvavsttTGPVNPY--RCNAKALRdlrtHTVSMVF 115
Cdd:cd03265 11 GDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSG-------RATVAGHdvVREPREVR----RRIGIVF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 116 QQFALLPWRTVAENVGFGLELAGMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPF 195
Cdd:cd03265 80 QDLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPT 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2087760999 196 SALDPLIRTRLQDELLEFQRRLKKTILFVSHDLDEAFRIGNRIAIMEGGRIIQCGTP 252
Cdd:cd03265 160 IGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTP 216
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
41-261 |
5.78e-34 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 126.67 E-value: 5.78e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 41 LGVADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTTTgpVNPYRcNAKALRDLRTHtVSMVFQqF-- 118
Cdd:PRK13634 21 RALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERV--ITAGK-KNKKLKPLRKK-VGIVFQ-Fpe 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 119 ALLPWRTVAENVGFGLELAGMPEAERKLRVGEQLELVNLT-KWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSA 197
Cdd:PRK13634 96 HQLFEETVEKDICFGPMNFGVSEEDAKQKAREMIELVGLPeELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAG 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2087760999 198 LDPLIRTRLQDELLEFQRRLKKTILFVSHDLDEAFRIGNRIAIMEGGRIIQCGTPHDIVKNPAD 261
Cdd:PRK13634 176 LDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADPDE 239
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
45-244 |
8.04e-34 |
|
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: 124.18 E-value: 8.04e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 45 DASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVstttgpvnpyrcNAKALRDLRtHTVSMVfQQFALLPWR 124
Cdd:cd03235 17 DVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRV------------FGKPLEKER-KRIGYV-PQRRSIDRD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 125 ---TVAENVGFGL----ELAGMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSA 197
Cdd:cd03235 83 fpiSVRDVVLMGLyghkGLFRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAG 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2087760999 198 LDPLIRTRLQdELLEFQRRLKKTILFVSHDLDEAFRIGNRIAIMEGG 244
Cdd:cd03235 163 VDPKTQEDIY-ELLRELRREGMTILVVTHDLGLVLEYFDRVLLLNRT 208
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
43-254 |
9.06e-34 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 123.75 E-value: 9.06e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 43 VADASLTIEEGEILVLMGLSGSGKSTLLRAVNG-LAPVVrgdvavsTTTGPVnpyRCNAKALRDLRTHT--VSMVFQQFA 119
Cdd:COG4136 17 LAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGtLSPAF-------SASGEV---LLNGRRLTALPAEQrrIGILFQDDL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 120 LLPWRTVAENVGFGLElAGMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALD 199
Cdd:COG4136 87 LFPHLSVGENLAFALP-PTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKLD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2087760999 200 PLIRTRLQDELLEFQRRLKKTILFVSHDLDEAfrignriaiMEGGRIIQCGTPHD 254
Cdd:COG4136 166 AALRAQFREFVFEQIRQRGIPALLVTHDEEDA---------PAAGRVLDLGNWQH 211
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
48-269 |
2.50e-33 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 123.71 E-value: 2.50e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 48 LTIEEGEILVLMGLSGSGKSTLLRAVNGL----APVVR-GDVAVSTTtgpvNPYRCNAKALRDLRTHtVSMVFQQFALLP 122
Cdd:PRK11264 24 LEVKPGEVVAIIGPSGSGKTTLLRCINLLeqpeAGTIRvGDITIDTA----RSLSQQKGLIRQLRQH-VGFVFQNFNLFP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 123 WRTVAENVGFG-LELAGMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDPl 201
Cdd:PRK11264 99 HRTVLENIIEGpVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPEVILFDEPTSALDP- 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2087760999 202 irtRLQDELLEFQRRL---KKTILFVSHDLDEAFRIGNRIAIMEGGRIIQCGTPHDIVKNPADQYVADFVQ 269
Cdd:PRK11264 178 ---ELVGEVLNTIRQLaqeKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADPQQPRTRQFLE 245
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
38-250 |
2.71e-33 |
|
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: 122.39 E-value: 2.71e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 38 GLVLGVADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVstttgpvnpyrcNAKALRDLRTHTVSMVFQQ 117
Cdd:cd03269 11 GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLF------------DGKPLDIAARNRIGYLPEE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 118 FALLPWRTVAENVGFGLELAGMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSA 197
Cdd:cd03269 79 RGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSG 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2087760999 198 LDPLIRTRLQDELLEfQRRLKKTILFVSHDLDEAFRIGNRIAIMEGGRIIQCG 250
Cdd:cd03269 159 LDPVNVELLKDVIRE-LARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
47-259 |
4.35e-33 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 123.37 E-value: 4.35e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 47 SLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVS------TTTGPVNPYRCNAKALRDLRTHtVSMVFQQFAL 120
Cdd:COG4598 28 SLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGgeeirlKPDRDGELVPADRRQLQRIRTR-LGMVFQSFNL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 121 LPWRTVAENVGFG-LELAGMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALD 199
Cdd:COG4598 107 WSHMTVLENVIEApVHVLGRPKAEAIERAEALLAKVGLADKRDAYPAHLSGGQQQRAAIARALAMEPEVMLFDEPTSALD 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2087760999 200 PlirtRLQDELLEFQRRLK---KTILFVSHDLDEAFRIGNRIAIMEGGRIIQCGTPHDIVKNP 259
Cdd:COG4598 187 P----ELVGEVLKVMRDLAeegRTMLVVTHEMGFARDVSSHVVFLHQGRIEEQGPPAEVFGNP 245
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
43-263 |
5.49e-33 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 128.26 E-value: 5.49e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 43 VADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPvVRGDVAVSTTtgPVNPYrcNAKALRDLRTHtVSMVFQQ-FALL 121
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIP-SEGEIRFDGQ--DLDGL--SRRALRPLRRR-MQVVFQDpFGSL 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 122 -PWRTVAENVGFGLEL--AGMPEAERKLRVGEQLELVNLTK-WAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSA 197
Cdd:COG4172 376 sPRMTVGQIIAEGLRVhgPGLSAAERRARVAEALEEVGLDPaARHRYPHEFSGGQRQRIAIARALILEPKLLVLDEPTSA 455
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2087760999 198 LDPLIRTRLQDELLEFQRRLKKTILFVSHDLDEAFRIGNRIAIMEGGRIIQCGTPHDIVKNPADQY 263
Cdd:COG4172 456 LDVSVQAQILDLLRDLQREHGLAYLFISHDLAVVRALAHRVMVMKDGKVVEQGPTEQVFDAPQHPY 521
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
43-254 |
6.56e-33 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 122.92 E-value: 6.56e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 43 VADASLTIEEGEILVLMGLSGSGKSTLLRAVNG-LAPvvrgdvavstTTGPVnpyRCNAKALRDLRTHTVSM---VFQQF 118
Cdd:COG4559 17 LDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGeLTP----------SSGEV---RLNGRPLAAWSPWELARrraVLPQH 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 119 ALL--PWrTVAENVGFGLELAGMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFA-------TGAPIL 189
Cdd:COG4559 84 SSLafPF-TVEEVVALGRAPHGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLAqlwepvdGGPRWL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2087760999 190 LMDEPFSALDPlirtRLQDELLEFQRRLKK---TILFVSHDLDEAFRIGNRIAIMEGGRIIQCGTPHD 254
Cdd:COG4559 163 FLDEPTSALDL----AHQHAVLRLARQLARrggGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPEE 226
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
4-245 |
9.80e-33 |
|
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: 119.80 E-value: 9.80e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 4 VNFNNVSIIFGDRPETALAmvdqgksrdeigaatglvlgvaDASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGD 83
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLK----------------------DVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGE 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 84 VAVSTTtgPVNPYrcnakALRDLRTHtVSMVFQQFALLPwRTVAENVgfglelagmpeaerklrvgeqlelvnltkwagr 163
Cdd:cd03228 59 ILIDGV--DLRDL-----DLESLRKN-IAYVPQDPFLFS-GTIRENI--------------------------------- 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 164 kvneLSGGMQQRVGLARAFATGAPILLMDEPFSALDPLIRTRLQDELLEFQRrlKKTILFVSHDLdEAFRIGNRIAIMEG 243
Cdd:cd03228 97 ----LSGGQRQRIAIARALLRDPPILILDEATSALDPETEALILEALRALAK--GKTVIVIAHRL-STIRDADRIIVLDD 169
|
..
gi 2087760999 244 GR 245
Cdd:cd03228 170 GR 171
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
43-255 |
1.96e-32 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 122.52 E-value: 1.96e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 43 VADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLapvvrgdvaVSTTTGPVnpyRCNAKALRDLrthtvsmVFQQFALLP 122
Cdd:COG4152 17 VDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGI---------LAPDSGEV---LWDGEPLDPE-------DRRRIGYLP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 123 -WR------TVAENVGFGLELAGMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFAtGAP-ILLMDEP 194
Cdd:COG4152 78 eERglypkmKVGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALL-HDPeLLILDEP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2087760999 195 FSALDPLIRTRLQDELLEFQRRlKKTILFVSHDLDEAFRIGNRIAIMEGGRIIQCGTPHDI 255
Cdd:COG4152 157 FSGLDPVNVELLKDVIRELAAK-GTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEI 216
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
33-263 |
5.98e-32 |
|
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: 125.57 E-value: 5.98e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 33 IGAATGLVLGVADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVvrgdvAVSTTTGPV-----NPYRCNAKALRDLR 107
Cdd:COG4172 16 FGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLLPD-----PAAHPSGSIlfdgqDLLGLSERELRRIR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 108 THTVSMVFQQ--FALLPWRTVAENVGFGLEL-AGMPEAERKLRVGEQLELVNLTKwAGRKVN----ELSGGMQQRVGLAR 180
Cdd:COG4172 91 GNRIAMIFQEpmTSLNPLHTIGKQIAEVLRLhRGLSGAAARARALELLERVGIPD-PERRLDayphQLSGGQRQRVMIAM 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 181 AFATGAPILLMDEPFSALDPLIRTRLQDELLEFQRRLKKTILFVSHDLDEAFRIGNRIAIMEGGRIIQCGTPHDIVKNPA 260
Cdd:COG4172 170 ALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFADRVAVMRQGEIVEQGPTAELFAAPQ 249
|
...
gi 2087760999 261 DQY 263
Cdd:COG4172 250 HPY 252
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
43-252 |
1.97e-31 |
|
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin resistance ABC transporter, ATP binding subunit in bacteria and archaea. This model is restricted in its scope to preferentially recognize the ATP binding subunit associated with effux of the drug, daunorubicin. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. In eukaryotes proteins of similar function include p-gyco proteins, multidrug resistance protein etc. [Transport and binding proteins, Other]
Pssm-ID: 130256 [Multi-domain] Cd Length: 302 Bit Score: 120.19 E-value: 1.97e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 43 VADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGdvavsttTGPVNPYRCNAKAlRDLRtHTVSMVFQQFALLP 122
Cdd:TIGR01188 9 VDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSG-------TARVAGYDVVREP-RKVR-RSIGIVPQYASVDE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 123 WRTVAENVGFGLELAGMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDPLI 202
Cdd:TIGR01188 80 DLTGRENLEMMGRLYGLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPRT 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2087760999 203 RTRLQDELLEFqRRLKKTILFVSHDLDEAFRIGNRIAIMEGGRIIQCGTP 252
Cdd:TIGR01188 160 RRAIWDYIRAL-KEEGVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTP 208
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
43-268 |
2.00e-31 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 118.86 E-value: 2.00e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 43 VADASLTIEEGEILVLMGLSGSGKSTLLRAVNGL-----APVVRGDVAVSTTtgpvNPYRCNAKALRdlrtHTVSMVFQQ 117
Cdd:PRK14247 19 LDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQ----DIFKMDVIELR----RRVQMVFQI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 118 FALLPWRTVAENVGFGLELAGMPEAERKL--RVGEQLELVNLTKWAGRKVN----ELSGGMQQRVGLARAFATGAPILLM 191
Cdd:PRK14247 91 PNPIPNLSIFENVALGLKLNRLVKSKKELqeRVRWALEKAQLWDEVKDRLDapagKLSGGQQQRLCIARALAFQPEVLLA 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2087760999 192 DEPFSALDPLIRTRLQDELLEFQRRLkkTILFVSHDLDEAFRIGNRIAIMEGGRIIQCGTPHDIVKNPADQYVADFV 268
Cdd:PRK14247 171 DEPTANLDPENTAKIESLFLELKKDM--TIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTNPRHELTEKYV 245
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-255 |
1.03e-30 |
|
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: 116.72 E-value: 1.03e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 1 MTAVNFNNVSIIFGDRPetalamvdqgksrdeigaatglVLGvaDASLTIEEGEILVLMGLSGSGKSTLLRAVNG-LAPV 79
Cdd:COG1119 1 DPLLELRNVTVRRGGKT----------------------ILD--DISWTVKPGEHWAILGPNGAGKSTLLSLITGdLPPT 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 80 VRGDVAV-STTTGPVNpyrcnakaLRDLRTHT--VSMVFQQFalLPWRTVAENV---GF--GLELAGMPEAERKLRVGEQ 151
Cdd:COG1119 57 YGNDVRLfGERRGGED--------VWELRKRIglVSPALQLR--FPRDETVLDVvlsGFfdSIGLYREPTDEQRERAREL 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 152 LELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDPLIRTRLQDELLEFQRRLKKTILFVSHDLDEA 231
Cdd:COG1119 127 LELLGLAHLADRPFGTLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEI 206
|
250 260
....*....|....*....|....
gi 2087760999 232 FRIGNRIAIMEGGRIIQCGTPHDI 255
Cdd:COG1119 207 PPGITHVLLLKDGRVVAAGPKEEV 230
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
45-255 |
1.30e-30 |
|
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: 115.61 E-value: 1.30e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 45 DASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVstttgpvnpyrcNAKALRDLRTHT-----VSMVFQQFA 119
Cdd:cd03224 18 GVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRF------------DGRDITGLPPHEraragIGYVPEGRR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 120 LLPWRTVAENvgfgLELAGM--PEAERKLRVGEQLELV-NLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFS 196
Cdd:cd03224 86 IFPELTVEEN----LLLGAYarRRAKRKARLERVYELFpRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSE 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2087760999 197 ALDPLIRTRLQDELLEFqRRLKKTILFVSHDLDEAFRIGNRIAIMEGGRIIQCGTPHDI 255
Cdd:cd03224 162 GLAPKIVEEIFEAIREL-RDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAEL 219
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
48-246 |
1.33e-30 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 116.70 E-value: 1.33e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 48 LTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTTtgPVnpyrcnAKALRDLRthtvsMVFQQFALLPWRTVA 127
Cdd:PRK11247 33 LHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTA--PL------AEAREDTR-----LMFQDARLLPWKKVI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 128 ENVGFGLELAGMPEAErklrvgEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDPLIRTRLQ 207
Cdd:PRK11247 100 DNVGLGLKGQWRDAAL------QALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRIEMQ 173
|
170 180 190
....*....|....*....|....*....|....*....
gi 2087760999 208 DELLEFQRRLKKTILFVSHDLDEAFRIGNRIAIMEGGRI 246
Cdd:PRK11247 174 DLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
47-269 |
2.31e-30 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 116.22 E-value: 2.31e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 47 SLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVST--------TTGPVNPYrcNAKALRDLRTHtVSMVFQQF 118
Cdd:PRK10619 25 SLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGqtinlvrdKDGQLKVA--DKNQLRLLRTR-LTMVFQHF 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 119 ALLPWRTVAENVGFG-LELAGMPEAERKLRVGEQLELVNLTKWA-GRKVNELSGGMQQRVGLARAFATGAPILLMDEPFS 196
Cdd:PRK10619 102 NLWSHMTVLENVMEApIQVLGLSKQEARERAVKYLAKVGIDERAqGKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTS 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2087760999 197 ALDPlirtRLQDELLEFQRRLK---KTILFVSHDLDEAFRIGNRIAIMEGGRIIQCGTPHDIVKNPADQYVADFVQ 269
Cdd:PRK10619 182 ALDP----ELVGEVLRIMQQLAeegKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGNPQSPRLQQFLK 253
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
45-248 |
3.35e-30 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 115.94 E-value: 3.35e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 45 DASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTTtgPVNPY-RCNAKALRdlrtHTVSMVFQQF--ALL 121
Cdd:PRK10419 30 NVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGE--PLAKLnRAQRKAFR----RDIQMVFQDSisAVN 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 122 PWRTVAENVGFGLE-LAGMPEAERKLRVGEQLELVNLT-KWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALD 199
Cdd:PRK10419 104 PRKTVREIIREPLRhLLSLDKAERLARASEMLRAVDLDdSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLD 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2087760999 200 PLIRTRLQDELLEFQRRLKKTILFVSHDLDEAFRIGNRIAIMEGGRIIQ 248
Cdd:PRK10419 184 LVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVE 232
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
45-255 |
3.92e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 115.98 E-value: 3.92e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 45 DASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTTtgpvnpyRCNAKALRDLRtHTVSMVFQ----QFAl 120
Cdd:PRK13650 25 DVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGD-------LLTEENVWDIR-HKIGMVFQnpdnQFV- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 121 lpWRTVAENVGFGLELAGMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDP 200
Cdd:PRK13650 96 --GATVEDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDP 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2087760999 201 LIRTRLQDELLEFQRRLKKTILFVSHDLDEAfRIGNRIAIMEGGRIIQCGTPHDI 255
Cdd:PRK13650 174 EGRLELIKTIKGIRDDYQMTVISITHDLDEV-ALSDRVLVMKNGQVESTSTPREL 227
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
45-270 |
5.20e-30 |
|
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: 120.71 E-value: 5.20e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 45 DASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVstttgpvNPYRCNAKALRDLRTHtVSMVFQQFALLPwR 124
Cdd:COG2274 493 NISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILI-------DGIDLRQIDPASLRRQ-IGVVLQDVFLFS-G 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 125 TVAENVGFGLELAGMPEAERKLRVGEQLELVN-LTKWAGRKVNE----LSGGMQQRVGLARAFATGAPILLMDEPFSALD 199
Cdd:COG2274 564 TIRENITLGDPDATDEEIIEAARLAGLHDFIEaLPMGYDTVVGEggsnLSGGQRQRLAIARALLRNPRILILDEATSALD 643
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2087760999 200 PLIRTRLQDELLEFQRrlKKTILFVSHDLdEAFRIGNRIAIMEGGRIIQCGTPHDIVKnpADQYVADFVQN 270
Cdd:COG2274 644 AETEAIILENLRRLLK--GRTVIIIAHRL-STIRLADRIIVLDKGRIVEDGTHEELLA--RKGLYAELVQQ 709
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
45-258 |
5.50e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 115.88 E-value: 5.50e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 45 DASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTTTGPVNPYRCnaKALRDLRTHtVSMVFQ--QFALLP 122
Cdd:PRK13645 29 NTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPANLKKI--KEVKRLRKE-IGLVFQfpEYQLFQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 123 wRTVAENVGFGLELAGMPEAERKLRVGEQLELVNLTK-WAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDPL 201
Cdd:PRK13645 106 -ETIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLPEdYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPK 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2087760999 202 IRTRLQDELLEFQRRLKKTILFVSHDLDEAFRIGNRIAIMEGGRIIQCGTPHDIVKN 258
Cdd:PRK13645 185 GEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFSN 241
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
38-256 |
5.58e-30 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 119.91 E-value: 5.58e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 38 GLVLGVADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVS--------TTTGPVNPYRCnakalrdlrTH 109
Cdd:TIGR03269 295 GVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRvgdewvdmTKPGPDGRGRA---------KR 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 110 TVSMVFQQFALLPWRTVAENV--GFGLELagmPEAERKLRVGEQLELVNLTKWAGRKV-----NELSGGMQQRVGLARAF 182
Cdd:TIGR03269 366 YIGILHQEYDLYPHRTVLDNLteAIGLEL---PDELARMKAVITLKMVGFDEEKAEEIldkypDELSEGERHRVALAQVL 442
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2087760999 183 ATGAPILLMDEPFSALDPLIRTRLQDELLEFQRRLKKTILFVSHDLDEAFRIGNRIAIMEGGRIIQCGTPHDIV 256
Cdd:TIGR03269 443 IKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEEIV 516
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
45-252 |
5.83e-30 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 114.87 E-value: 5.83e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 45 DASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVavstttgpvnpyRCNAKALRDLRTHTVSM---VFQQFALL 121
Cdd:PRK13548 20 DVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEV------------RLNGRPLADWSPAELARrraVLPQHSSL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 122 --PWrTVAENVGFGLELAGMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFA------TGAPILLMDE 193
Cdd:PRK13548 88 sfPF-TVEEVVAMGRAPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAqlwepdGPPRWLLLDE 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2087760999 194 PFSALDPlirtRLQDELLEFQRRLKK----TILFVSHDLDEAFRIGNRIAIMEGGRIIQCGTP 252
Cdd:PRK13548 167 PTSALDL----AHQHHVLRLARQLAHerglAVIVVLHDLNLAARYADRIVLLHQGRLVADGTP 225
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
43-258 |
8.00e-30 |
|
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: 119.48 E-value: 8.00e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 43 VADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVstttgpvnpyrcNAKALRDLRTHTVsmvFQQFALLP 122
Cdd:COG4988 353 LDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILI------------NGVDLSDLDPASW---RRQIAWVP 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 123 WR------TVAENVGFGLELAGMPEAERKLRvgeqleLVNLTKWAGR-------KVNE----LSGGMQQRVGLARAFATG 185
Cdd:COG4988 418 QNpylfagTIRENLRLGRPDASDEELEAALE------AAGLDEFVAAlpdgldtPLGEggrgLSGGQAQRLALARALLRD 491
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2087760999 186 APILLMDEPFSALDPLIRTRLQDELLEFQRRlkKTILFVSHDLDEAfRIGNRIAIMEGGRIIQCGTPHDIVKN 258
Cdd:COG4988 492 APLLLLDEPTAHLDAETEAEILQALRRLAKG--RTVILITHRLALL-AQADRILVLDDGRIVEQGTHEELLAK 561
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
34-250 |
1.16e-29 |
|
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: 113.23 E-value: 1.16e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 34 GAATGLVLGVADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLapvVRGDVAVSTTTGpVNPYRCNAKALRDLrthtvSM 113
Cdd:cd03266 12 RDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGL---LEPDAGFATVDG-FDVVKEPAEARRRL-----GF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 114 VFQQFALLPWRTVAENVGFGLELAGMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDE 193
Cdd:cd03266 83 VSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDE 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2087760999 194 PFSALDpLIRTRLQDELLEFQRRLKKTILFVSHDLDEAFRIGNRIAIMEGGRIIQCG 250
Cdd:cd03266 163 PTTGLD-VMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
43-260 |
1.47e-29 |
|
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: 119.10 E-value: 1.47e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 43 VADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVstttGPVNPYRCNAKALRDLrthtVSMVFQQFALLP 122
Cdd:COG4987 351 LDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITL----GGVDLRDLDEDDLRRR----IAVVPQRPHLFD 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 123 wRTVAENvgfgLELAGmPEA-ERKLRvgEQLELVNLTKW--------------AGRKvneLSGGMQQRVGLARAFATGAP 187
Cdd:COG4987 423 -TTLREN----LRLAR-PDAtDEELW--AALERVGLGDWlaalpdgldtwlgeGGRR---LSGGERRRLALARALLRDAP 491
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2087760999 188 ILLMDEPFSALDPLIRTRLQDELLEFQRRlkKTILFVSHDLDEAFRIgNRIAIMEGGRIIQCGTPHDIVKNPA 260
Cdd:COG4987 492 ILLLDEPTEGLDAATEQALLADLLEALAG--RTVLLITHRLAGLERM-DRILVLEDGRIVEQGTHEELLAQNG 561
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
41-258 |
1.70e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 114.41 E-value: 1.70e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 41 LGVADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVStttgpvNPYRCNAKALRDLRThTVSMVFQ---- 116
Cdd:PRK13633 24 LALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVD------GLDTSDEENLWDIRN-KAGMVFQnpdn 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 117 QfalLPWRTVAENVGFGLELAGMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFS 196
Cdd:PRK13633 97 Q---IVATIVEEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTA 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2087760999 197 ALDPLIRTRLQDELLEFQRRLKKTILFVSHDLDEAFRiGNRIAIMEGGRIIQCGTPHDIVKN 258
Cdd:PRK13633 174 MLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIFKE 234
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
45-247 |
2.64e-29 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 117.82 E-value: 2.64e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 45 DASLTIEEGEILVLMGLSGSGKSTLLRAVNGL-AP-----VVRG-DVAVStttgpvNPyrcnakalRDLRTHTVSMVFQQ 117
Cdd:COG3845 23 DVSLTVRPGEIHALLGENGAGKSTLMKILYGLyQPdsgeiLIDGkPVRIR------SP--------RDAIALGIGMVHQH 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 118 FALLPWRTVAENVGFGLE-----LAGMPEAERKLR-VGEQLEL-VNLTkwagRKVNELSGGMQQRVGLARAFATGAPILL 190
Cdd:COG3845 89 FMLVPNLTVAENIVLGLEptkggRLDRKAARARIReLSERYGLdVDPD----AKVEDLSVGEQQRVEILKALYRGARILI 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2087760999 191 MDEPFSALDPlirtrlQ--DELLEFQRRLK---KTILFVSHDLDEAFRIGNRIAIMEGGRII 247
Cdd:COG3845 165 LDEPTAVLTP------QeaDELFEILRRLAaegKSIIFITHKLREVMAIADRVTVLRRGKVV 220
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
45-258 |
6.08e-29 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 117.19 E-value: 6.08e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 45 DASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTTtgPVNPYRcnakaLRDLRTHtVSMVFQQFALLPwR 124
Cdd:COG1132 358 DISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGV--DIRDLT-----LESLRRQ-IGVVPQDTFLFS-G 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 125 TVAENVGFGLELAGMPEAERKLRvgeqleLVNLTKWA-----------GRKVNELSGGMQQRVGLARAFATGAPILLMDE 193
Cdd:COG1132 429 TIRENIRYGRPDATDEEVEEAAK------AAQAHEFIealpdgydtvvGERGVNLSGGQRQRIAIARALLKDPPILILDE 502
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2087760999 194 PFSALDPLIRTRLQDELLEFQRRlkKTILFVSHDLdEAFRIGNRIAIMEGGRIIQCGTPHDIVKN 258
Cdd:COG1132 503 ATSALDTETEALIQEALERLMKG--RTTIVIAHRL-STIRNADRILVLDDGRIVEQGTHEELLAR 564
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
43-255 |
8.76e-29 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 112.03 E-value: 8.76e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 43 VADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVstttgpvnpyrcNAKALRDLRTHTVSmvfQQFALLP 122
Cdd:PRK11231 18 LNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFL------------GDKPISMLSSRQLA---RRLALLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 123 WR-------TVAENVGFG----LELAGMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLM 191
Cdd:PRK11231 83 QHhltpegiTVRELVAYGrspwLSLWGRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2087760999 192 DEPFSALDplirTRLQDELLEFQRRLK---KTILFVSHDLDEAFRIGNRIAIMEGGRIIQCGTPHDI 255
Cdd:PRK11231 163 DEPTTYLD----INHQVELMRLMRELNtqgKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEV 225
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
45-258 |
1.16e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 112.01 E-value: 1.16e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 45 DASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTTTgpvnpyrCNAKALRDLRTHtVSMVFQ----QFAL 120
Cdd:PRK13632 27 NVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGIT-------ISKENLKEIRKK-IGIIFQnpdnQFIG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 121 LpwrTVAENVGFGLELAGMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDP 200
Cdd:PRK13632 99 A---TVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFDESTSMLDP 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2087760999 201 LIRTRLQDELLEFQRRLKKTILFVSHDLDEAFrIGNRIAIMEGGRIIQCGTPHDIVKN 258
Cdd:PRK13632 176 KGKREIKKIMVDLRKTRKKTLISITHDMDEAI-LADKVIVFSEGKLIAQGKPKEILNN 232
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
44-268 |
1.19e-28 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 111.78 E-value: 1.19e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 44 ADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTTtgpvnpyrcNAKALRDLRTHTV----SMVFQQFA 119
Cdd:PRK11831 24 DNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGE---------NIPAMSRSRLYTVrkrmSMLFQSGA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 120 LLPWRTVAENVGFGL-ELAGMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSAL 198
Cdd:PRK11831 95 LFTDMNVFDNVAYPLrEHTQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQ 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 199 DPLIRTRLQDELLEFQRRLKKTILFVSHDLDEAFRIGNRIAIMEGGRIIQCGTPHDIVKNPaDQYVADFV 268
Cdd:PRK11831 175 DPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQANP-DPRVRQFL 243
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
48-253 |
1.40e-28 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 111.64 E-value: 1.40e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 48 LTIEEGEILVLMGLSGSGKSTLLRAVNGLapvVRGDVAVSTTTGPV-NPYRCNAKALRDLR---THTvSMVFQQFALLPW 123
Cdd:PRK09984 25 LNIHHGEMVALLGPSGSGKSTLLRHLSGL---ITGDKSAGSHIELLgRTVQREGRLARDIRksrANT-GYIFQQFNLVNR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 124 RTVAENVGFGlELAGMP---------EAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEP 194
Cdd:PRK09984 101 LSVLENVLIG-ALGSTPfwrtcfswfTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVILADEP 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2087760999 195 FSALDPLIRTRLQDELLEFQRRLKKTILFVSHDLDEAFRIGNRIAIMEGGRIIQCGTPH 253
Cdd:PRK09984 180 IASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQ 238
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
43-247 |
1.59e-28 |
|
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: 110.00 E-value: 1.59e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 43 VADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTttgpvNPYRCNAKALRdlrtHTVSMVFQQfALLP 122
Cdd:cd03268 16 LDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDG-----KSYQKNIEALR----RIGALIEAP-GFYP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 123 WRTVAENVGFGLELAGMPEAerklRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDPL- 201
Cdd:cd03268 86 NLTARENLRLLARLLGIRKK----RIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPDg 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2087760999 202 IRtrlqdELLEFQRRLKK---TILFVSHDLDEAFRIGNRIAIMEGGRII 247
Cdd:cd03268 162 IK-----ELRELILSLRDqgiTVLISSHLLSEIQKVADRIGIINKGKLI 205
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
45-247 |
2.13e-28 |
|
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: 108.28 E-value: 2.13e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 45 DASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTTtgPVNPyrcnaKALRDLRTHTVSMVFQqfallpwr 124
Cdd:cd03216 18 GVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGK--EVSF-----ASPRDARRAGIAMVYQ-------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 125 tvaenvgfglelagmpeaerklrvgeqlelvnltkwagrkvneLSGGMQQRVGLARAFATGAPILLMDEPFSALDPlirt 204
Cdd:cd03216 83 -------------------------------------------LSVGERQMVEIARALARNARLLILDEPTAALTP---- 115
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2087760999 205 RLQDELLEFQRRLKK---TILFVSHDLDEAFRIGNRIAIMEGGRII 247
Cdd:cd03216 116 AEVERLFKVIRRLRAqgvAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
45-231 |
3.29e-28 |
|
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 130234 [Multi-domain] Cd Length: 190 Bit Score: 108.66 E-value: 3.29e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 45 DASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTTtgpvnPYRCNAKALRDLRTHtVSMVFQQ-----FA 119
Cdd:TIGR01166 10 GLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGE-----PLDYSRKGLLERRQR-VGLVFQDpddqlFA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 120 llpwRTVAENVGFGLELAGMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALD 199
Cdd:TIGR01166 84 ----ADVDQDVAFGPLNLGLSEAEVERRVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAGLD 159
|
170 180 190
....*....|....*....|....*....|....*
gi 2087760999 200 PLIRTRLQDELlefqRRLK---KTILFVSHDLDEA 231
Cdd:TIGR01166 160 PAGREQMLAIL----RRLRaegMTVVISTHDVDLA 190
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
45-250 |
3.35e-28 |
|
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: 109.20 E-value: 3.35e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 45 DASLTIEEGeILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTTTGPVNPyrcnakalRDLRTHtVSMVFQQFALLPWR 124
Cdd:cd03264 18 GVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQP--------QKLRRR-IGYLPQEFGVYPNF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 125 TVAENVGFGLELAGMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDPLIRT 204
Cdd:cd03264 88 TVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDPEERI 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2087760999 205 RLQDELLEFQRrlKKTILFVSHDLDEAFRIGNRIAIMEGGRIIQCG 250
Cdd:cd03264 168 RFRNLLSELGE--DRIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
3-259 |
4.60e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 110.69 E-value: 4.60e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 3 AVNFNNVSIIFGdrPETALamvdQGKSRDEIgaatglvlgvadaSLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRG 82
Cdd:PRK13641 2 SIKFENVDYIYS--PGTPM----EKKGLDNI-------------SFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSG 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 83 DVAVSTTTgpVNPYRCNaKALRDLRTHtVSMVFQqF--ALLPWRTVAENVGFGLELAGMPEAERKLRVGEQLELVNL-TK 159
Cdd:PRK13641 63 TITIAGYH--ITPETGN-KNLKKLRKK-VSLVFQ-FpeAQLFENTVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLsED 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 160 WAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDPLIRTRLQDELLEFQRRlKKTILFVSHDLDEAFRIGNRIA 239
Cdd:PRK13641 138 LISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKA-GHTVILVTHNMDDVAEYADDVL 216
|
250 260
....*....|....*....|
gi 2087760999 240 IMEGGRIIQCGTPHDIVKNP 259
Cdd:PRK13641 217 VLEHGKLIKHASPKEIFSDK 236
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
45-257 |
4.62e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 110.98 E-value: 4.62e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 45 DASLTIEEGEILVLMGLSGSGKSTLLRAVNGL-----APVVRGDVAVSTTTgpvnpyrcNAKALRDLRThTVSMVFQ-QF 118
Cdd:PRK13643 24 DIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLlqpteGKVTVGDIVVSSTS--------KQKEIKPVRK-KVGVVFQfPE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 119 ALLPWRTVAENVGFGLELAGMPEAERKLRVGEQLELVNLTK--WAgRKVNELSGGMQQRVGLARAFATGAPILLMDEPFS 196
Cdd:PRK13643 95 SQLFEETVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLADefWE-KSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTA 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2087760999 197 ALDPLIRTRLQdELLEFQRRLKKTILFVSHDLDEAFRIGNRIAIMEGGRIIQCGTPHDIVK 257
Cdd:PRK13643 174 GLDPKARIEMM-QLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQ 233
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
24-268 |
5.17e-28 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 109.75 E-value: 5.17e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 24 VDQGKSRDEIGAATGLVLGVADASL------TIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVStttGPV---- 93
Cdd:PRK14246 1 MEAGKSAEDVFNISRLYLYINDKAIlkditiKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVD---GKVlyfg 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 94 -NPYRCNAKALRDlrthTVSMVFQQFALLPWRTVAENVGFGLELAGMPEA-ERKLRVGEQLELVNLTKWAGRKVN----E 167
Cdd:PRK14246 78 kDIFQIDAIKLRK----EVGMVFQQPNPFPHLSIYDNIAYPLKSHGIKEKrEIKKIVEECLRKVGLWKEVYDRLNspasQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 168 LSGGMQQRVGLARAFATGAPILLMDEPFSALDPLIRTRLQDELLEFQRRLkkTILFVSHDLDEAFRIGNRIAIMEGGRII 247
Cdd:PRK14246 154 LSGGQQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNEI--AIVIVSHNPQQVARVADYVAFLYNGELV 231
|
250 260
....*....|....*....|.
gi 2087760999 248 QCGTPHDIVKNPADQYVADFV 268
Cdd:PRK14246 232 EWGSSNEIFTSPKNELTEKYV 252
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
45-257 |
5.27e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 110.23 E-value: 5.27e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 45 DASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVstttgpvNPYRCNAKALRDLRTHtVSMVFQ----QFAl 120
Cdd:PRK13648 27 DVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFY-------NNQAITDDNFEKLRKH-IGIVFQnpdnQFV- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 121 lpWRTVAENVGFGLELAGMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDP 200
Cdd:PRK13648 98 --GSIVKYDVAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDP 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2087760999 201 LIRTrlqdELLEFQRRLKK----TILFVSHDLDEAFRiGNRIAIMEGGRIIQCGTPHDIVK 257
Cdd:PRK13648 176 DARQ----NLLDLVRKVKSehniTIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIFD 231
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
45-260 |
8.87e-28 |
|
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: 108.53 E-value: 8.87e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 45 DASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVavstttgpvnpyRCNAKALRDLRTHT-----VSMVFQQ-- 117
Cdd:COG0410 21 GVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSI------------RFDGEDITGLPPHRiarlgIGYVPEGrr 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 118 -FALLpwrTVAENvgfgLELAGMPEAERKlRVGEQLELV-----NLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLM 191
Cdd:COG0410 89 iFPSL---TVEEN----LLLGAYARRDRA-EVRADLERVyelfpRLKERRRQRAGTLSGGEQQMLAIGRALMSRPKLLLL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2087760999 192 DEPFSALDPLIRtrlqDELLEFQRRLKK---TILFVSHDLDEAFRIGNRIAIMEGGRIIQCGTPHDIVKNPA 260
Cdd:COG0410 161 DEPSLGLAPLIV----EEIFEIIRRLNRegvTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLADPE 228
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
43-270 |
9.46e-28 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 109.16 E-value: 9.46e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 43 VADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVstttgpvnpyrcNAKAL----RDLRTHTVSMVFQ-- 116
Cdd:COG4167 29 VKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILI------------NGHKLeygdYKYRCKHIRMIFQdp 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 117 QFALLPWRTVAENVGFGLELA-GMPEAERKLRVGEQLELVNL-TKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEP 194
Cdd:COG4167 97 NTSLNPRLNIGQILEEPLRLNtDLTAEEREERIFATLRLVGLlPEHANFYPHMLSSGQKQRVALARALILQPKIIIADEA 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2087760999 195 FSALDPLIRTRLQDELLEFQRRLKKTILFVSHDLDEAFRIGNRIAIMEGGRIIQCGTPHDIVKNPADQYVADFVQN 270
Cdd:COG4167 177 LAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKHISDKVLVMHQGEVVEYGKTAEVFANPQHEVTKRLIES 252
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
45-243 |
1.18e-27 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 108.36 E-value: 1.18e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 45 DASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTTtgPVNPYRCNAKAlrDLRTHTVSMVFQQFALLPWR 124
Cdd:PRK11629 27 NVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQ--PMSKLSSAAKA--ELRNQKLGFIYQFHHLLPDF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 125 TVAENVGFGLELAGMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDPLIRT 204
Cdd:PRK11629 103 TALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNAD 182
|
170 180 190
....*....|....*....|....*....|....*....
gi 2087760999 205 RLQDELLEFQRRLKKTILFVSHDLDEAFRIGNRIAIMEG 243
Cdd:PRK11629 183 SIFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQLEMRDG 221
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
47-259 |
1.40e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 109.01 E-value: 1.40e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 47 SLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTttgpvNPYRCNAKALRDLRtHTVSMVFQQ-----FAll 121
Cdd:PRK13639 22 NFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKG-----EPIKYDKKSLLEVR-KTVGIVFQNpddqlFA-- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 122 PwrTVAENVGFGLELAGMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDPL 201
Cdd:PRK13639 94 P--TVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPM 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2087760999 202 IRTRLQDELLEFQRRlKKTILFVSHDLDEAFRIGNRIAIMEGGRIIQCGTPHDIVKNP 259
Cdd:PRK13639 172 GASQIMKLLYDLNKE-GITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDI 228
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
47-261 |
1.56e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 109.03 E-value: 1.56e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 47 SLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTTtgpvnpyRCNAKALRDLRtHTVSMVFQ----QFAllp 122
Cdd:PRK13642 27 SFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGE-------LLTAENVWNLR-RKIGMVFQnpdnQFV--- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 123 WRTVAENVGFGLELAGMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDPLI 202
Cdd:PRK13642 96 GATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTG 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2087760999 203 RTRLQDELLEFQRRLKKTILFVSHDLDEAFRiGNRIAIMEGGRIIQCGTPHDIVKNPAD 261
Cdd:PRK13642 176 RQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELFATSED 233
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
3-259 |
1.62e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 109.12 E-value: 1.62e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 3 AVNFNNVSIIFGDRPETAlamvdqgksrdeigaatglvlgVADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLapVVRG 82
Cdd:PRK13640 5 IVEFKHVSFTYPDSKKPA----------------------LNDISFSIPRGSWTALIGHNGSGKSTISKLINGL--LLPD 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 83 DVAVSTTTgpVNPYRCNAKALRDLRtHTVSMVFQ----QFAllpWRTVAENVGFGLELAGMPEAERKLRVGEQLELVNLT 158
Cdd:PRK13640 61 DNPNSKIT--VDGITLTAKTVWDIR-EKVGIVFQnpdnQFV---GATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGML 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 159 KWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDPLIRTRLQDELLEFQRRLKKTILFVSHDLDEAfRIGNRI 238
Cdd:PRK13640 135 DYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEA-NMADQV 213
|
250 260
....*....|....*....|.
gi 2087760999 239 AIMEGGRIIQCGTPHDIVKNP 259
Cdd:PRK13640 214 LVLDDGKLLAQGSPVEIFSKV 234
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
43-268 |
1.67e-27 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 108.59 E-value: 1.67e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 43 VADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPV---VRGDVAVSTTTGPVNPYRCNAKALRdlrtHTVSMVFQQFA 119
Cdd:PRK14258 23 LEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELeseVRVEGRVEFFNQNIYERRVNLNRLR----RQVSMVHPKPN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 120 LLPwRTVAENVGFGLELAGM-PEAERKLRVGEQLELVNLTKWAGRKVN----ELSGGMQQRVGLARAFATGAPILLMDEP 194
Cdd:PRK14258 99 LFP-MSVYDNVAYGVKIVGWrPKLEIDDIVESALKDADLWDEIKHKIHksalDLSGGQQQRLCIARALAVKPKVLLMDEP 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2087760999 195 FSALDPLIRTRLQDELLEFQRRLKKTILFVSHDLDEAFRIGNRIAIMEG-----GRIIQCGTPHDIVKNPADQYVADFV 268
Cdd:PRK14258 178 CFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGnenriGQLVEFGLTKKIFNSPHDSRTREYV 256
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
43-247 |
1.78e-27 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 106.96 E-value: 1.78e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 43 VADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVstttgpvnpyrCNAKALRDLRTHTVSMVFQ----QF 118
Cdd:cd03226 16 LDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILL-----------NGKPIKAKERRKSIGYVMQdvdyQL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 119 ALlpwRTVAENVGFGLELAGmpeaERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSAL 198
Cdd:cd03226 85 FT---DSVREELLLGLKELD----AGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2087760999 199 DPLIRTRLQDELLEFQRRlKKTILFVSHDLDEAFRIGNRIAIMEGGRII 247
Cdd:cd03226 158 DYKNMERVGELIRELAAQ-GKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
43-268 |
4.82e-27 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 107.24 E-value: 4.82e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 43 VADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPV-----VRGDVAVSTttgpVNPYRCNAKALRDLRThtVSMVFQQ 117
Cdd:PRK14267 20 IKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELneearVEGEVRLFG----RNIYSPDVDPIEVRRE--VGMVFQY 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 118 FALLPWRTVAENVGFGLELAGMpeaerklrVGEQLELVNLTKWAGRKV--------------NELSGGMQQRVGLARAFA 183
Cdd:PRK14267 94 PNPFPHLTIYDNVAIGVKLNGL--------VKSKKELDERVEWALKKAalwdevkdrlndypSNLSGGQRQRLVIARALA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 184 TGAPILLMDEPFSALDPLIRTRLQDELLEFQRRLkkTILFVSHDLDEAFRIGNRIAIMEGGRIIQCGTPHDIVKNPADQY 263
Cdd:PRK14267 166 MKPKILLMDEPTANIDPVGTAKIEELLFELKKEY--TIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENPEHEL 243
|
....*
gi 2087760999 264 VADFV 268
Cdd:PRK14267 244 TEKYV 248
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
48-243 |
5.79e-27 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 106.40 E-value: 5.79e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 48 LTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTTtgpvNPYRCNAKALRDLRTHTVSMVFQQFALLPWRTVA 127
Cdd:PRK10584 31 LVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQ----PLHQMDEEARAKLRAKHVGFVFQSFMLIPTLNAL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 128 ENVGFGLELAGMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDPLIRTRLQ 207
Cdd:PRK10584 107 ENVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIA 186
|
170 180 190
....*....|....*....|....*....|....*.
gi 2087760999 208 DELLEFQRRLKKTILFVSHDLDEAFRIGNRIAIMEG 243
Cdd:PRK10584 187 DLLFSLNREHGTTLILVTHDLQLAARCDRRLRLVNG 222
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
47-264 |
2.66e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 105.84 E-value: 2.66e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 47 SLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTTTGpvnpyrCNAKALRDLRThTVSMVFQ----QFAllp 122
Cdd:PRK13644 22 NLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDT------GDFSKLQGIRK-LVGIVFQnpetQFV--- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 123 WRTVAENVGFGLELAGMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDPLI 202
Cdd:PRK13644 92 GRTVEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDS 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2087760999 203 RTRLQDELLEFQRRlKKTILFVSHDLDEaFRIGNRIAIMEGGRIIQCGTPHDIVKNPADQYV 264
Cdd:PRK13644 172 GIAVLERIKKLHEK-GKTIVYITHNLEE-LHDADRIIVMDRGKIVLEGEPENVLSDVSLQTL 231
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
47-252 |
3.24e-26 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 110.10 E-value: 3.24e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 47 SLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTttgpvNPYRCNAKALRdlrtHTVSMVFQQFALLPWRTV 126
Cdd:TIGR01257 950 NITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGG-----KDIETNLDAVR----QSLGMCPQHNILFHHLTV 1020
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 127 AENVGFGLELAGMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDPLIRTRL 206
Cdd:TIGR01257 1021 AEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSI 1100
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2087760999 207 QDELLEFqrRLKKTILFVSHDLDEAFRIGNRIAIMEGGRIIQCGTP 252
Cdd:TIGR01257 1101 WDLLLKY--RSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTP 1144
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
38-268 |
4.09e-26 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 104.86 E-value: 4.09e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 38 GLVLGVADASLTIEEGEILVLMGLSGSGKSTLLRA---VNGLAPVVRGDVAVSTTTGPVNPYRCNAKALRdlrtHTVSMV 114
Cdd:PRK14243 21 GSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCfnrLNDLIPGFRVEGKVTFHGKNLYAPDVDPVEVR----RRIGMV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 115 FQQFALLPwRTVAENVGFGLELAG----MPE-AERKLRvgeQLELVNLTKwagRKVNE----LSGGMQQRVGLARAFATG 185
Cdd:PRK14243 97 FQKPNPFP-KSIYDNIAYGARINGykgdMDElVERSLR---QAALWDEVK---DKLKQsglsLSGGQQQRLCIARAIAVQ 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 186 APILLMDEPFSALDPLIRTRLQDELLEFQRRLkkTILFVSHDLDEAFRIGNRIAIM-----EG----GRIIQCGTPHDIV 256
Cdd:PRK14243 170 PEVILMDEPCSALDPISTLRIEELMHELKEQY--TIIIVTHNMQQAARVSDMTAFFnveltEGggryGYLVEFDRTEKIF 247
|
250
....*....|..
gi 2087760999 257 KNPADQYVADFV 268
Cdd:PRK14243 248 NSPQQQATRDYV 259
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-257 |
5.65e-26 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 104.01 E-value: 5.65e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 1 MT-AVNFNNVSIIF--GDRPETAL--AMVDQGKSRDEIgaatglVLGVADASLTIEEGEILVLMGLSGSGKSTLLRAVNG 75
Cdd:COG1134 1 MSsMIEVENVSKSYrlYHEPSRSLkeLLLRRRRTRREE------FWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 76 LAPVVRGDVAVstttgpvnpyRCNAKALRDLrthtvSMVFQQFAllpwrTVAENVGFGLELAGMPEAERKLRVGEQLELV 155
Cdd:COG1134 75 ILEPTSGRVEV----------NGRVSALLEL-----GAGFHPEL-----TGRENIYLNGRLLGLSRKEIDEKFDEIVEFA 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 156 NLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDPLIRTRLQDELLEFQRRlKKTILFVSHDLDEAFRIG 235
Cdd:COG1134 135 ELGDFIDQPVKTYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRES-GRTVIFVSHSMGAVRRLC 213
|
250 260
....*....|....*....|..
gi 2087760999 236 NRIAIMEGGRIIQCGTPHDIVK 257
Cdd:COG1134 214 DRAIWLEKGRLVMDGDPEEVIA 235
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-257 |
7.66e-26 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 105.68 E-value: 7.66e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 1 MTAVNFNNVSIIFGDRPEtalamvdqgksrdeigaatglvlgVADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVV 80
Cdd:PRK13536 39 TVAIDLAGVSKSYGDKAV------------------------VNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 81 RGDVAVsttTGPVNPYRCNAKALRdlrthtVSMVFQQFALLPWRTVAENVGFGLELAGMPEAERKLRVGEQLELVNLTKW 160
Cdd:PRK13536 95 AGKITV---LGVPVPARARLARAR------IGVVPQFDNLDLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESK 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 161 AGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDP----LIRTRLQDELlefqrRLKKTILFVSHDLDEAFRIGN 236
Cdd:PRK13536 166 ADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPharhLIWERLRSLL-----ARGKTILLTTHFMEEAERLCD 240
|
250 260
....*....|....*....|.
gi 2087760999 237 RIAIMEGGRIIQCGTPHDIVK 257
Cdd:PRK13536 241 RLCVLEAGRKIAEGRPHALID 261
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
43-260 |
8.31e-26 |
|
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: 103.39 E-value: 8.31e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 43 VADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVA---VSTTTGPVnpYRcnaKALRDLrthtvSMVFQQFA 119
Cdd:cd03218 16 VNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILldgQDITKLPM--HK---RARLGI-----GYLPQEAS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 120 LLPWRTVAENVGFGLELAGMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALD 199
Cdd:cd03218 86 IFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVD 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2087760999 200 PLIRTRLQdELLEFQRRLKKTILFVSHDLDEAFRIGNRIAIMEGGRIIQCGTPHDIVKNPA 260
Cdd:cd03218 166 PIAVQDIQ-KIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANEL 225
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
31-246 |
1.38e-25 |
|
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: 101.35 E-value: 1.38e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 31 DEIGAATGLVLG--VADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVStttGpvNPYRcnAKALRDLRT 108
Cdd:cd03215 2 EPVLEVRGLSVKgaVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLD---G--KPVT--RRSPRDAIR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 109 HTVSMV---FQQFALLPWRTVAENVGFGlelagmpeaerklrvgeqlelvnltkwagrkvNELSGGMQQRVGLARAFATG 185
Cdd:cd03215 75 AGIAYVpedRKREGLVLDLSVAENIALS--------------------------------SLLSGGNQQKVVLARWLARD 122
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2087760999 186 APILLMDEPFSALDPLIRTRLQDELLEFqRRLKKTILFVSHDLDEAFRIGNRIAIMEGGRI 246
Cdd:cd03215 123 PRVLILDEPTRGVDVGAKAEIYRLIREL-ADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
40-250 |
1.62e-25 |
|
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: 102.35 E-value: 1.62e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 40 VLGVADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLapvVRGDvavSTTTGPVnpyRCNAKAL-RDLRTHTVSMVFQQF 118
Cdd:cd03234 20 ARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGR---VEGG---GTTSGQI---LFNGQPRkPDQFQKCVAYVRQDD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 119 ALLPWRTVAENVGFGLELAG---MPEAERKLRVG-EQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEP 194
Cdd:cd03234 91 ILLPGLTVRETLTYTAILRLprkSSDAIRKKRVEdVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEP 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2087760999 195 FSALDPLIRTRLQDELLEFQRRLKKTILFVSHDLDEAFRIGNRIAIMEGGRIIQCG 250
Cdd:cd03234 171 TSGLDSFTALNLVSTLSQLARRNRIVILTIHQPRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
43-256 |
1.87e-25 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 104.12 E-value: 1.87e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 43 VADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGdvAVSTTTGPVnPYRCNAKALRdlrthtVSMVFQQFALLP 122
Cdd:PRK13537 23 VDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAG--SISLCGEPV-PSRARHARQR------VGVVPQFDNLDP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 123 WRTVAENVGFGLELAGMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDPLI 202
Cdd:PRK13537 94 DFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQA 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2087760999 203 RTRLQDELLEFQRRlKKTILFVSHDLDEAFRIGNRIAIMEGGRIIQCGTPHDIV 256
Cdd:PRK13537 174 RHLMWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALI 226
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
43-263 |
3.96e-25 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 103.63 E-value: 3.96e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 43 VADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTTtgpvNPYRCNAKALRDLRTHtVSMVFQQ--FAL 120
Cdd:PRK15079 37 VDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGK----DLLGMKDDEWRAVRSD-IQMIFQDplASL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 121 LPWRTVAENVGFGLEL--AGMPEAERKLRVGEQLELVNL-TKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSA 197
Cdd:PRK15079 112 NPRMTIGEIIAEPLRTyhPKLSRQEVKDRVKAMMLKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSA 191
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2087760999 198 LDPLIRTRLQDELLEFQRRLKKTILFVSHDLDEAFRIGNRIAIMEGGRIIQCGTPHDIVKNPADQY 263
Cdd:PRK15079 192 LDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNPLHPY 257
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
45-278 |
4.05e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 103.24 E-value: 4.05e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 45 DASLTIEEGEILVLMGLSGSGKSTLLRAVNGL-------------------APVVRGDVAVSTTTGPvnPYRCNAKALRD 105
Cdd:PRK13651 25 NVSVEINQGEFIAIIGQTGSGKTTFIEHLNALllpdtgtiewifkdeknkkKTKEKEKVLEKLVIQK--TRFKKIKKIKE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 106 LRTHtVSMVFQqFA--LLPWRTVAENVGFGLELAGMPEAERKLRVGEQLELVNL-TKWAGRKVNELSGGMQQRVGLARAF 182
Cdd:PRK13651 103 IRRR-VGVVFQ-FAeyQLFEQTIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLdESYLQRSPFELSGGQKRRVALAGIL 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 183 ATGAPILLMDEPFSALDPlirtRLQDELLEFQRRLK---KTILFVSHDLDEAFRIGNRIAIMEGGRIIQCGTPHDIVKNp 259
Cdd:PRK13651 181 AMEPDFLVFDEPTAGLDP----QGVKEILEIFDNLNkqgKTIILVTHDLDNVLEWTKRTIFFKDGKIIKDGDTYDILSD- 255
|
250
....*....|....*....
gi 2087760999 260 aDQYVADfvQNLNPINMLT 278
Cdd:PRK13651 256 -NKFLIE--NNMEPPKLLN 271
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
43-260 |
6.79e-25 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 101.31 E-value: 6.79e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 43 VADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAP----VVRGDVAVSTTtgPVNPyrcnakalRDLRTHTVSMVFQ-- 116
Cdd:PRK10418 19 VHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPagvrQTAGRVLLDGK--PVAP--------CALRGRKIATIMQnp 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 117 QFALLPWRTVAENVGFGLELAGMPEAERKLRvgEQLELVNLTKwAGRKVN----ELSGGMQQRVGLARAFATGAPILLMD 192
Cdd:PRK10418 89 RSAFNPLHTMHTHARETCLALGKPADDATLT--AALEAVGLEN-AARVLKlypfEMSGGMLQRMMIALALLCEAPFIIAD 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2087760999 193 EPFSALDPLIRTRLQDELLEFQRRLKKTILFVSHDLDEAFRIGNRIAIMEGGRIIQCGTPHDIVKNPA 260
Cdd:PRK10418 166 EPTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPK 233
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
43-233 |
8.13e-25 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 99.23 E-value: 8.13e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 43 VADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTTTgpvnpyrcnakalrdlrthTVSMVFQQFALlP 122
Cdd:NF040873 8 LHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGA-------------------RVAYVPQRSEV-P 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 123 WR---TVAENVGFGL----ELAGMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPF 195
Cdd:NF040873 68 DSlplTVRDLVAMGRwarrGLWRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPT 147
|
170 180 190
....*....|....*....|....*....|....*...
gi 2087760999 196 SALDPLIRTRLqDELLEFQRRLKKTILFVSHDLDEAFR 233
Cdd:NF040873 148 TGLDAESRERI-IALLAEEHARGATVVVVTHDLELVRR 184
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
43-259 |
9.14e-25 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 103.77 E-value: 9.14e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 43 VADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLapvvrgdvaVSTTTGPVnpyRCNAKALRDLRTHTVSmvfQQFALLP 122
Cdd:PRK09536 19 LDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGT---------LTPTAGTV---LVAGDDVEALSARAAS---RRVASVP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 123 WRT-------VAENVGFGL-----ELAGMPEAERKLrVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILL 190
Cdd:PRK09536 84 QDTslsfefdVRQVVEMGRtphrsRFDTWTETDRAA-VERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2087760999 191 MDEPFSALD--PLIRTrlqdelLEFQRRL---KKTILFVSHDLDEAFRIGNRIAIMEGGRIIQCGTPHDIVKNP 259
Cdd:PRK09536 163 LDEPTASLDinHQVRT------LELVRRLvddGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVLTAD 230
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
45-255 |
1.06e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 101.36 E-value: 1.06e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 45 DASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAV---STTTGPVNpyrcnaKALRDLRTHtVSMVFqQFA-- 119
Cdd:PRK13649 25 DVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVddtLITSTSKN------KDIKQIRKK-VGLVF-QFPes 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 120 LLPWRTVAENVGFGLELAGMPEAERKLRVGEQLELVNLTK-WAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSAL 198
Cdd:PRK13649 97 QLFEETVLKDVAFGPQNFGVSQEEAEALAREKLALVGISEsLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 199 DPLIRTrlqdELLEFQRRLKK---TILFVSHDLDEAFRIGNRIAIMEGGRIIQCGTPHDI 255
Cdd:PRK13649 177 DPKGRK----ELMTLFKKLHQsgmTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDI 232
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
4-250 |
1.92e-24 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 99.14 E-value: 1.92e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 4 VNFNNVSIIF--GDRPETALAMVDQGKSRDEIGAatglVLGVADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVR 81
Cdd:cd03220 1 IELENVSKSYptYKGGSSSLKKLGILGRKGEVGE----FWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 82 GDVavsTTTGPVnpyrcnakalrdlrthtVSMVFQQFALLPWRTVAENVGFGLELAGMPEAERKLRVGEQLELVNLTKWA 161
Cdd:cd03220 77 GTV---TVRGRV-----------------SSLLGLGGGFNPELTGRENIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFI 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 162 GRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDPLIRTRLQDELLEFQRRlKKTILFVSHDLDEAFRIGNRIAIM 241
Cdd:cd03220 137 DLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQ-GKTVILVSHDPSSIKRLCDRALVL 215
|
....*....
gi 2087760999 242 EGGRIIQCG 250
Cdd:cd03220 216 EKGKIRFDG 224
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1-263 |
2.20e-24 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 101.36 E-value: 2.20e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 1 MTAVNFNNVSIIFGDRpETALAMVDQgksrdeigaatglvlgvadASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVV 80
Cdd:PRK11022 1 MALLNVDKLSVHFGDE-SAPFRAVDR-------------------ISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDYP 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 81 RGDVAVSTTTGPVNPYRCNAKALRDLRTHTVSMVFQQ--FALLPWRTVAENVGFGLEL-AGMPEAERKLRVGEQLELVNL 157
Cdd:PRK11022 61 GRVMAEKLEFNGQDLQRISEKERRNLVGAEVAMIFQDpmTSLNPCYTVGFQIMEAIKVhQGGNKKTRRQRAIDLLNQVGI 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 158 TKWAGR---KVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDPLIRTRLQDELLEFQRRLKKTILFVSHDLDEAFRI 234
Cdd:PRK11022 141 PDPASRldvYPHQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEA 220
|
250 260
....*....|....*....|....*....
gi 2087760999 235 GNRIAIMEGGRIIQCGTPHDIVKNPADQY 263
Cdd:PRK11022 221 AHKIIVMYAGQVVETGKAHDIFRAPRHPY 249
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
29-260 |
2.50e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 101.08 E-value: 2.50e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 29 SRDEIGAATGL-----------VLGVADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAV----------- 86
Cdd:PRK13631 17 SDDIILRVKNLycvfdekqeneLVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVgdiyigdkknn 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 87 STTTGPVNPYRC-NAKALRdlrtHTVSMVFQ--QFALLPwRTVAENVGFGLELAGMPEAERKLRVGEQLELVNL-TKWAG 162
Cdd:PRK13631 97 HELITNPYSKKIkNFKELR----RRVSMVFQfpEYQLFK-DTIEKDIMFGPVALGVKKSEAKKLAKFYLNKMGLdDSYLE 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 163 RKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDPLIRTRLQDELLEFQRRlKKTILFVSHDLDEAFRIGNRIAIME 242
Cdd:PRK13631 172 RSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKAN-NKTVFVITHTMEHVLEVADEVIVMD 250
|
250
....*....|....*...
gi 2087760999 243 GGRIIQCGTPHDIVKNPA 260
Cdd:PRK13631 251 KGKILKTGTPYEIFTDQH 268
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
42-245 |
3.24e-24 |
|
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: 98.66 E-value: 3.24e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 42 GVADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTTTGPVNPYRCNAKALRDLRTHTVSMVFQQFALL 121
Cdd:COG4778 26 VLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDGGWVDLAQASPREILALRRRTIGYVSQFLRVI 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 122 PwRT-----VAEnvgfGLELAGMPEAERKLRVGEQLELVNLTK--WagrkvnEL-----SGGMQQRVGLARAFATGAPIL 189
Cdd:COG4778 106 P-RVsaldvVAE----PLLERGVDREEARARARELLARLNLPErlW------DLppatfSGGEQQRVNIARGFIADPPLL 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2087760999 190 LMDEPFSALDPLIRTRLQDELLEFQRRlKKTILFVSHDLDEAFRIGNRIAIMEGGR 245
Cdd:COG4778 175 LLDEPTASLDAANRAVVVELIEEAKAR-GTAIIGIFHDEEVREAVADRVVDVTPFS 229
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
47-252 |
3.75e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 99.81 E-value: 3.75e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 47 SLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTTTgpvnpyrCNAKALRDLRTHtVSMVFQQ-----FALl 121
Cdd:PRK13647 25 SLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGRE-------VNAENEKWVRSK-VGLVFQDpddqvFSS- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 122 pwrTVAENVGFGLELAGMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDPl 201
Cdd:PRK13647 96 ---TVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDP- 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2087760999 202 irtRLQDELLEFQRRLK---KTILFVSHDLDEAFRIGNRIAIMEGGRIIQCGTP 252
Cdd:PRK13647 172 ---RGQETLMEILDRLHnqgKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDK 222
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
3-228 |
6.23e-24 |
|
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: 102.36 E-value: 6.23e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 3 AVNFNNVSIIFGDRPEtalamvdqgksrdeigaatglvlGVADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRG 82
Cdd:TIGR02857 321 SLEFSGVSVAYPGRRP-----------------------ALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEG 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 83 DVAVstttGPVNPYRCNAKALRDlrthTVSMVFQQFALLPwRTVAENVGFG------------LELAGMPEAERKLRVGE 150
Cdd:TIGR02857 378 SIAV----NGVPLADADADSWRD----QIAWVPQHPFLFA-GTIAENIRLArpdasdaeireaLERAGLDEFVAALPQGL 448
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2087760999 151 QLELvnltkwaGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDPLIRTRLQDELLEFQRRlkKTILFVSHDL 228
Cdd:TIGR02857 449 DTPI-------GEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQG--RTVLLVTHRL 517
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
43-259 |
1.67e-23 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 97.02 E-value: 1.67e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 43 VADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVavstttgpvnpyRCNAKALRDLRTHtvsmvfqQFAL-- 120
Cdd:COG1137 19 VKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRI------------FLDGEDITHLPMH-------KRARlg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 121 ---LP-----WR--TVAENVGFGLELAGMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILL 190
Cdd:COG1137 80 igyLPqeasiFRklTVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKFIL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2087760999 191 MDEPFSALDPLIRTRLQDELlefqRRLKKT---ILFVSHDLDEAFRIGNRIAIMEGGRIIQCGTPHDIVKNP 259
Cdd:COG1137 160 LDEPFAGVDPIAVADIQKII----RHLKERgigVLITDHNVRETLGICDRAYIISEGKVLAEGTPEEILNNP 227
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
33-263 |
8.58e-23 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 96.96 E-value: 8.58e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 33 IGAATGLVLGVADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRG-------DVAVstttgpvnpyrcNAKALRD 105
Cdd:PRK11308 21 LFKPERLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGelyyqgqDLLK------------ADPEAQK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 106 LRTHTVSMVFQQ-FALL-PWRTVAENVGFGLEL-AGMPEAERKLRVGEQLELVNL-TKWAGRKVNELSGGMQQRVGLARA 181
Cdd:PRK11308 89 LLRQKIQIVFQNpYGSLnPRKKVGQILEEPLLInTSLSAAERREKALAMMAKVGLrPEHYDRYPHMFSGGQRQRIAIARA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 182 FATGAPILLMDEPFSALDPLIRTRLQDELLEFQRRLKKTILFVSHDLDEAFRIGNRIAIMEGGRIIQCGTPHDIVKNPAD 261
Cdd:PRK11308 169 LMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFNNPRH 248
|
..
gi 2087760999 262 QY 263
Cdd:PRK11308 249 PY 250
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
45-245 |
1.30e-22 |
|
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: 93.69 E-value: 1.30e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 45 DASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTTtgpvnpyrcnakalrdlrthtVSMVFQQfallPW- 123
Cdd:cd03250 23 DINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS---------------------IAYVSQE----PWi 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 124 --RTVAENVGFGLELagmpEAERKLRV---------GEQLELVNLTKWAGRKVNeLSGGMQQRVGLARAFATGAPILLMD 192
Cdd:cd03250 78 qnGTIRENILFGKPF----DEERYEKVikacalepdLEILPDGDLTEIGEKGIN-LSGGQKQRISLARAVYSDADIYLLD 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2087760999 193 EPFSALDPLIRTRLQDELLEFQRRLKKTILFVSHDLdEAFRIGNRIAIMEGGR 245
Cdd:cd03250 153 DPLSAVDAHVGRHIFENCILGLLLNNKTRILVTHQL-QLLPHADQIVVLDNGR 204
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
43-255 |
1.49e-22 |
|
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: 98.64 E-value: 1.49e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 43 VADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTTtgPVNPYRcnakaLRDLRTHtVSMVFQQFALLP 122
Cdd:TIGR02203 348 LDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGH--DLADYT-----LASLRRQ-VALVSQDVVLFN 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 123 wRTVAENVGFG-LELAGMPEAERKLRVGEQLELVN-----LTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFS 196
Cdd:TIGR02203 420 -DTIANNIAYGrTEQADRAEIERALAAAYAQDFVDklplgLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATS 498
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2087760999 197 ALDPLIRTRLQDELLEFQRrlKKTILFVSHDLdEAFRIGNRIAIMEGGRIIQCGTPHDI 255
Cdd:TIGR02203 499 ALDNESERLVQAALERLMQ--GRTTLVIAHRL-STIEKADRIVVMDDGRIVERGTHNEL 554
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
43-256 |
3.08e-22 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 93.99 E-value: 3.08e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 43 VADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVA-----VSTTtgpvnPYRCNAKALRDLR--THTVSmvf 115
Cdd:COG4604 17 LDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLvdgldVATT-----PSRELAKRLAILRqeNHINS--- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 116 qqfallpwR-TVAENVGFGle--laGMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMD 192
Cdd:COG4604 89 --------RlTVRELVAFGrfpyskGRLTAEDREIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQDTDYVLLD 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2087760999 193 EPFSALDP--------LIRtRLQDEllefqrrLKKTILFVSHDLDEAFRIGNRIAIMEGGRIIQCGTPHDIV 256
Cdd:COG4604 161 EPLNNLDMkhsvqmmkLLR-RLADE-------LGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEII 224
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
43-267 |
9.24e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 93.31 E-value: 9.24e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 43 VADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTTTgpvNPYRCNAKALRDLRtHTVSMVFQqF--AL 120
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDIT---ITHKTKDKYIRPVR-KRIGMVFQ-FpeSQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 121 LPWRTVAENVGFGLELAGMPEAERK-------LRVGEQLELVNLTKWagrkvnELSGGMQQRVGLARAFATGAPILLMDE 193
Cdd:PRK13646 98 LFEDTVEREIIFGPKNFKMNLDEVKnyahrllMDLGFSRDVMSQSPF------QMSGGQMRKIAIVSILAMNPDIIVLDE 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2087760999 194 PFSALDPLIRTRLQDELLEFQRRLKKTILFVSHDLDEAFRIGNRIAIMEGGRIIQCGTPHDIVKNpaDQYVADF 267
Cdd:PRK13646 172 PTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFKD--KKKLADW 243
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
45-247 |
1.13e-21 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 95.95 E-value: 1.13e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 45 DASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTTtgpvNPYRCNAKALRDLRTHTVSMVFQQFALLPWR 124
Cdd:PRK10535 26 GISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQ----DVATLDADALAQLRREHFGFIFQRYHLLSHL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 125 TVAENVGFGLELAGMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDplirT 204
Cdd:PRK10535 102 TAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALD----S 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2087760999 205 RLQDELLEFQRRLKK---TILFVSHDLDEAFRiGNRIAIMEGGRII 247
Cdd:PRK10535 178 HSGEEVMAILHQLRDrghTVIIVTHDPQVAAQ-AERVIEIRDGEIV 222
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
45-255 |
1.30e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 92.99 E-value: 1.30e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 45 DASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTttgpvNPYRCNAKALRDLRtHTVSMVFQQ-----FA 119
Cdd:PRK13636 24 GININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDG-----KPIDYSRKGLMKLR-ESVGMVFQDpdnqlFS 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 120 llpwRTVAENVGFGLELAGMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALD 199
Cdd:PRK13636 98 ----ASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLD 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2087760999 200 PLIRTRLQDELLEFQRRLKKTILFVSHDLDEAFRIGNRIAIMEGGRIIQCGTPHDI 255
Cdd:PRK13636 174 PMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEV 229
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
45-256 |
1.52e-21 |
|
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: 95.25 E-value: 1.52e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 45 DASLTIEEGEILVLMGLSGSGKSTL---LRAVNGLAPV---VRGDVAVSTTTGPVNP----------------------Y 96
Cdd:TIGR03269 18 NISFTIEEGEVLGILGRSGAGKSVLmhvLRGMDQYEPTsgrIIYHVALCEKCGYVERpskvgepcpvcggtlepeevdfW 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 97 RCNAKALRDLRTHTVSMVFQQFALLPWRTVAENVGFGLELAGMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRV 176
Cdd:TIGR03269 98 NLSDKLRRRIRKRIAIMLQRTFALYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEMVQLSHRITHIARDLSGGEKQRV 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 177 GLARAFATGAPILLMDEPFSALDPLIRTRLQDELLEFQRRLKKTILFVSHDLDEAFRIGNRIAIMEGGRIIQCGTPHDIV 256
Cdd:TIGR03269 178 VLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDLSDKAIWLENGEIKEEGTPDEVV 257
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
40-263 |
1.62e-21 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 95.69 E-value: 1.62e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 40 VLGVADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTTTGPVNPyrcnAKALRDLRtHTVSMVFQQ-- 117
Cdd:PRK10261 337 VHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLS----PGKLQALR-RDIQFIFQDpy 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 118 FALLPWRTVAENVGFGLELAGMPEAER-KLRVGEQLELVNLT-KWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPF 195
Cdd:PRK10261 412 ASLDPRQTVGDSIMEPLRVHGLLPGKAaAARVAWLLERVGLLpEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAV 491
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2087760999 196 SALDPLIRTRLQDELLEFQRRLKKTILFVSHDLDEAFRIGNRIAIMEGGRIIQCGTPHDIVKNPADQY 263
Cdd:PRK10261 492 SALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENPQHPY 559
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
42-263 |
5.31e-21 |
|
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: 90.66 E-value: 5.31e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 42 GVADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTTTGPVNPYRCNAKALRDLRTHTvsmvfqqfall 121
Cdd:TIGR02323 18 GCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMRSGAELELYQLSEAERRRLMRT----------- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 122 PWRTVAENVGFGLEL---AGMPEAERKLRVGEQ------------LELVNLTkwAGR---KVNELSGGMQQRVGLARAFA 183
Cdd:TIGR02323 87 EWGFVHQNPRDGLRMrvsAGANIGERLMAIGARhygnirataqdwLEEVEID--PTRiddLPRAFSGGMQQRLQIARNLV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 184 TGAPILLMDEPFSALDPLIRTRLQDELLEFQRRLKKTILFVSHDLDEAFRIGNRIAIMEGGRIIQCGTPHDIVKNPADQY 263
Cdd:TIGR02323 165 TRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRVVESGLTDQVLDDPQHPY 244
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
38-250 |
5.42e-21 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 90.76 E-value: 5.42e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 38 GLVLGVADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAvstttgpvnpYRCNAKALRDLRTHTVSmvfQQ 117
Cdd:PRK11701 17 GPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVH----------YRMRDGQLRDLYALSEA---ER 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 118 FALL--PWRTVAENVGFGLEL---AGMPEAERKLRVGEQ------------LELVNLtkwAGRKVNEL----SGGMQQRV 176
Cdd:PRK11701 84 RRLLrtEWGFVHQHPRDGLRMqvsAGGNIGERLMAVGARhygdiratagdwLERVEI---DAARIDDLpttfSGGMQQRL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2087760999 177 GLARAFATGAPILLMDEPFSALDPLIRTRLQDELLEFQRRLKKTILFVSHDLDEAFRIGNRIAIMEGGRIIQCG 250
Cdd:PRK11701 161 QIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVVESG 234
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
40-302 |
5.69e-21 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 93.44 E-value: 5.69e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 40 VLGVADASLTIEEGEILVLMGLSGSGKSTLLRAVNGL-AP-----VVRGDVAVSTTTgpvnpyrcnakalRDLRTHTVSM 113
Cdd:PRK11288 17 VKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNyQPdagsiLIDGQEMRFAST-------------TAALAAGVAI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 114 VFQQFALLPWRTVAENvgfgLELAGMPEA-----ERKL--RVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGA 186
Cdd:PRK11288 84 IYQELHLVPEMTVAEN----LYLGQLPHKggivnRRLLnyEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 187 PILLMDEPFSALDplirTRLQDELLEFQRRLK---KTILFVSHDLDEAFRIGNRIAIMEGGRIIQcgTPHDIVKNPADQY 263
Cdd:PRK11288 160 RVIAFDEPTSSLS----AREIEQLFRVIRELRaegRVILYVSHRMEEIFALCDAITVFKDGRYVA--TFDDMAQVDRDQL 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 2087760999 264 VADFV-QNLNPI----------NMLTAADVMQPGLGQTaagmsVSATARA 302
Cdd:PRK11288 234 VQAMVgREIGDIygyrprplgeVRLRLDGLKGPGLREP-----ISFSVRA 278
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
38-263 |
8.61e-21 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 91.32 E-value: 8.61e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 38 GLVLGVADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLApVVRGDVAVSTTTGPVNPYRCNAKALRDLRTHTVSMVFQQ 117
Cdd:PRK09473 27 GDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLL-AANGRIGGSATFNGREILNLPEKELNKLRAEQISMIFQD 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 118 --FALLPWRTVAENVGFGLEL-AGMPEAERKLRVGEQLELVNLTKwAGRKVN----ELSGGMQQRVGLARAFATGAPILL 190
Cdd:PRK09473 106 pmTSLNPYMRVGEQLMEVLMLhKGMSKAEAFEESVRMLDAVKMPE-ARKRMKmyphEFSGGMRQRVMIAMALLCRPKLLI 184
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2087760999 191 MDEPFSALDPLIRTRLQDELLEFQRRLKKTILFVSHDLDEAFRIGNRIAIMEGGRIIQCGTPHDIVKNPADQY 263
Cdd:PRK09473 185 ADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARDVFYQPSHPY 257
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
42-247 |
3.08e-20 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 91.23 E-value: 3.08e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 42 GVADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTTtgPVNPyRCNAKALRdlrtHTVSMV---FQQF 118
Cdd:COG1129 267 VVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGK--PVRI-RSPRDAIR----AGIAYVpedRKGE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 119 ALLPWRTVAENVGfgleLAGMPEAERKLRVGEQLELVNLTKWAGR----------KVNELSGGMQQRVGLARAFATGAPI 188
Cdd:COG1129 340 GLVLDLSIRENIT----LASLDRLSRGGLLDRRRERALAEEYIKRlriktpspeqPVGNLSGGNQQKVVLAKWLATDPKV 415
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2087760999 189 LLMDEPFSALDplIRTRlqDELLEFQRRLK---KTILFVSHDLDEAFRIGNRIAIMEGGRII 247
Cdd:COG1129 416 LILDEPTRGID--VGAK--AEIYRLIRELAaegKAVIVISSELPELLGLSDRILVMREGRIV 473
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
47-206 |
3.22e-20 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 87.24 E-value: 3.22e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 47 SLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAV--STTTGPVNPYRCNAKALRDlrthtvsmvfqqfALLPWR 124
Cdd:PRK13539 22 SFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLdgGDIDDPDVAEACHYLGHRN-------------AMKPAL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 125 TVAENVGFGLELAGMPEaerkLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDP---- 200
Cdd:PRK13539 89 TVAENLEFWAAFLGGEE----LDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAaava 164
|
170
....*....|
gi 2087760999 201 ----LIRTRL 206
Cdd:PRK13539 165 lfaeLIRAHL 174
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
45-250 |
4.02e-20 |
|
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: 86.84 E-value: 4.02e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 45 DASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPV--VRGDVAVSTTTGPVNPYRCnakalrdlrthTVSMVFQQFALLP 122
Cdd:cd03213 27 NVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGlgVSGEVLINGRPLDKRSFRK-----------IIGYVPQDDILHP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 123 WRTVAENVGFGLELAGmpeaerklrvgeqlelvnltkwagrkvneLSGGMQQRVGLARAFATGAPILLMDEPFSALDPli 202
Cdd:cd03213 96 TLTVRETLMFAAKLRG-----------------------------LSGGERKRVSIALELVSNPSLLFLDEPTSGLDS-- 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2087760999 203 RTRLQdeLLEFQRRLK---KTILFVSHDL-DEAFRIGNRIAIMEGGRIIQCG 250
Cdd:cd03213 145 SSALQ--VMSLLRRLAdtgRTIICSIHQPsSEIFELFDKLLLLSQGRVIYFG 194
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
4-246 |
4.72e-20 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 87.53 E-value: 4.72e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 4 VNFNNVSIIFGDRPETalamvdqgksrdeigaatgLVLgvADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGD 83
Cdd:cd03248 12 VKFQNVTFAYPTRPDT-------------------LVL--QDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 84 VAVSTTtgPVNPYrcNAKALRDlrthTVSMVFQQFALLPwRTVAENVGFGL---ELAGMPEAERKLRVGEQLELVNLTKW 160
Cdd:cd03248 71 VLLDGK--PISQY--EHKYLHS----KVSLVGQEPVLFA-RSLQDNIAYGLqscSFECVKEAAQKAHAHSFISELASGYD 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 161 --AGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDPLIRTRLQDELLEFQRRlkKTILFVSHDLDEAFRiGNRI 238
Cdd:cd03248 142 teVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAESEQQVQQALYDWPER--RTVLVIAHRLSTVER-ADQI 218
|
....*...
gi 2087760999 239 AIMEGGRI 246
Cdd:cd03248 219 LVLDGGRI 226
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
47-200 |
5.75e-20 |
|
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: 86.26 E-value: 5.75e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 47 SLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTTTGPvnpyrcnakALRDLRTHTVSMVFQQFALLPWRTV 126
Cdd:TIGR01189 20 SFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLA---------EQRDEPHENILYLGHLPGLKPELSA 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2087760999 127 AENVGFGLELAGmpeaERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDP 200
Cdd:TIGR01189 91 LENLHFWAAIHG----GAQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDK 160
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
45-247 |
6.00e-20 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 89.55 E-value: 6.00e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 45 DASLTIEEGEILVLMGLSGSGKSTLLRAVNGL-AP-----VVRGDVAVSTTTG---PVNPYRcnakalrdlrthtVSMVF 115
Cdd:PRK11144 16 TVNLTLPAQGITAIFGRSGAGKTSLINAISGLtRPqkgriVLNGRVLFDAEKGiclPPEKRR-------------IGYVF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 116 QQFALLPWRTVAENVGFGLElAGMPEAERKLrvgeqLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPF 195
Cdd:PRK11144 83 QDARLFPHYKVRGNLRYGMA-KSMVAQFDKI-----VALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2087760999 196 SALDpLIRTRlqdELLEFQRRLKKT----ILFVSHDLDEAFRIGNRIAIMEGGRII 247
Cdd:PRK11144 157 ASLD-LPRKR---ELLPYLERLAREinipILYVSHSLDEILRLADRVVVLEQGKVK 208
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
56-259 |
6.94e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 87.94 E-value: 6.94e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 56 LVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTTtgPVNpyrcnAKALRDLRtHTVSMVFQQ-----FAllpwRTVAENV 130
Cdd:PRK13652 33 IAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGE--PIT-----KENIREVR-KFVGLVFQNpddqiFS----PTVEQDI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 131 GFGLELAGMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDPLIRtrlqDEL 210
Cdd:PRK13652 101 AFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGV----KEL 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2087760999 211 LEFQRRLKK----TILFVSHDLDEAFRIGNRIAIMEGGRIIQCGTPHDIVKNP 259
Cdd:PRK13652 177 IDFLNDLPEtygmTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
39-247 |
7.63e-20 |
|
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: 87.00 E-value: 7.63e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 39 LVLGVADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVStttGPVnPYRCNAKALRDLrthtvSMVFQQF 118
Cdd:cd03267 33 EVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVA---GLV-PWKRRKKFLRRI-----GVVFGQK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 119 ALLPWR-TVAENVGFGLELAGMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSA 197
Cdd:cd03267 104 TQLWWDlPVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIG 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2087760999 198 LDPLIRTRLQDELLEFQRRLKKTILFVSHDLDEAFRIGNRIAIMEGGRII 247
Cdd:cd03267 184 LDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLL 233
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
35-272 |
7.73e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 87.84 E-value: 7.73e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 35 AATGLVLGVA------DASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGdvavstttgpvnpYRCNAKALRDLRT 108
Cdd:PRK14271 23 AAVNLTLGFAgktvldQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSG-------------YRYSGDVLLGGRS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 109 -----------HTVSMVFQQFALLPwRTVAENVGFGLElAGMPEAERKLRVGEQLELVNLTKWAGRKVN------ELSGG 171
Cdd:PRK14271 90 ifnyrdvlefrRRVGMLFQRPNPFP-MSIMDNVLAGVR-AHKLVPRKEFRGVAQARLTEVGLWDAVKDRlsdspfRLSGG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 172 MQQRVGLARAFATGAPILLMDEPFSALDPLIRTRLQDELLEFQRRLkkTILFVSHDLDEAFRIGNRIAIMEGGRIIQCGT 251
Cdd:PRK14271 168 QQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRL--TVIIVTHNLAQAARISDRAALFFDGRLVEEGP 245
|
250 260
....*....|....*....|.
gi 2087760999 252 PHDIVKNPADQYVADFVQNLN 272
Cdd:PRK14271 246 TEQLFSSPKHAETARYVAGLS 266
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
43-247 |
7.87e-20 |
|
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 represents the family of all lantibiotics related to gallidermin, including epidermin, mutatin, and nisin. This protein family describes the ATP-binding subunit of a gallidermin/epidermin class lantibiotic protection transporter. It is largely restricted to gallidermin-family lantibiotic biosynthesis and export cassettes, but also occurs in orphan transporter cassettes in species that lack candidate lantibiotic precursor and synthetase genes.
Pssm-ID: 163452 [Multi-domain] Cd Length: 223 Bit Score: 86.68 E-value: 7.87e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 43 VADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLapvvrgdvaVSTTTGPV--NPYRCNAKALRDlrthtVSMVFQQFAL 120
Cdd:TIGR03740 16 VNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGI---------LRPTSGEIifDGHPWTRKDLHK-----IGSLIESPPL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 121 LPWRTVAENVGFGLELAGMPEAerklRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDP 200
Cdd:TIGR03740 82 YENLTARENLKVHTTLLGLPDS----RIDEVLNIVDLTNTGKKKAKQFSLGMKQRLGIAIALLNHPKLLILDEPTNGLDP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2087760999 201 L-IRtrlqdELLEFQRRLKK---TILFVSHDLDEAFRIGNRIAIMEGGRII 247
Cdd:TIGR03740 158 IgIQ-----ELRELIRSFPEqgiTVILSSHILSEVQQLADHIGIISEGVLG 203
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
43-263 |
8.94e-20 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 90.15 E-value: 8.94e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 43 VADASLTIEEGEILVLMGLSGSGKSTLLRAVNGL---APVV--RGDVAVSTTTgpvnPYRCNAKALRDLRTHTVSMVFQQ 117
Cdd:PRK15134 25 VNDVSLQIEAGETLALVGESGSGKSVTALSILRLlpsPPVVypSGDIRFHGES----LLHASEQTLRGVRGNKIAMIFQE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 118 --FALLPWRTVAENVGFGLEL-AGMPEAERKLRVGEQLELVNLTKWAGRKVN---ELSGGMQQRVGLARAFATGAPILLM 191
Cdd:PRK15134 101 pmVSLNPLHTLEKQLYEVLSLhRGMRREAARGEILNCLDRVGIRQAAKRLTDyphQLSGGERQRVMIAMALLTRPELLIA 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2087760999 192 DEPFSALDPLIRTRLQDELLEFQRRLKKTILFVSHDLDEAFRIGNRIAIMEGGRIIQCGTPHDIVKNPADQY 263
Cdd:PRK15134 181 DEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAATLFSAPTHPY 252
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
47-259 |
9.76e-20 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 87.54 E-value: 9.76e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 47 SLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTTtgPVNPYrcNAKALrdlrTHTVSMVFQQFALLPWRTV 126
Cdd:PRK10575 31 SLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQ--PLESW--SSKAF----ARKVAYLPQQLPAAEGMTV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 127 AENVGFGLE----LAGMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDpli 202
Cdd:PRK10575 103 RELVAIGRYpwhgALGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALD--- 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2087760999 203 rTRLQDELLEFQRRLKK----TILFVSHDLDEAFRIGNRIAIMEGGRIIQCGTPHDIVKNP 259
Cdd:PRK10575 180 -IAHQVDVLALVHRLSQerglTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRGE 239
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
45-251 |
1.75e-19 |
|
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: 86.13 E-value: 1.75e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 45 DASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTTTgpVNPYrcnakALRDLRTHtVSMVFQQfALLPWR 124
Cdd:cd03251 20 DISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHD--VRDY-----TLASLRRQ-IGLVSQD-VFLFND 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 125 TVAENVGFGLELAGMPEAERKLRVGEQLELVNL------TKWAGRKVNeLSGGMQQRVGLARAFATGAPILLMDEPFSAL 198
Cdd:cd03251 91 TVAENIAYGRPGATREEVEEAARAANAHEFIMElpegydTVIGERGVK-LSGGQRQRIAIARALLKDPPILILDEATSAL 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2087760999 199 DPLIRTRLQDELLEFQRRlkKTILFVSHDLdEAFRIGNRIAIMEGGRIIQCGT 251
Cdd:cd03251 170 DTESERLVQAALERLMKN--RTTFVIAHRL-STIENADRIVVLEDGKIVERGT 219
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
38-259 |
3.26e-19 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 85.81 E-value: 3.26e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 38 GLVLGVADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVavstttgpvnpyRCNAKALRDLRTHTVS---MV 114
Cdd:PRK11300 16 GGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTI------------LLRGQHIEGLPGHQIArmgVV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 115 --FQQFALLPWRTVAEN--------VGFGLeLAGM--------PEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRV 176
Cdd:PRK11300 84 rtFQHVRLFREMTVIENllvaqhqqLKTGL-FSGLlktpafrrAESEALDRAATWLERVGLLEHANRQAGNLAYGQQRRL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 177 GLARAFATGAPILLMDEPFSALDPLIRTRLQDELLEFQRRLKKTILFVSHDLDEAFRIGNRIAIMEGGRIIQCGTPHDIV 256
Cdd:PRK11300 163 EIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEIR 242
|
...
gi 2087760999 257 KNP 259
Cdd:PRK11300 243 NNP 245
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
45-254 |
3.66e-19 |
|
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: 85.23 E-value: 3.66e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 45 DASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVstttgpvNPYRCNAKALRDLRTHtVSMVFQQFALLPwR 124
Cdd:cd03252 20 NISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLV-------DGHDLALADPAWLRRQ-VGVVLQENVLFN-R 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 125 TVAENVGFGLELAGMPEAERKLRVGEQLELV-NLTKWAGRKVNE----LSGGMQQRVGLARAFATGAPILLMDEPFSALD 199
Cdd:cd03252 91 SIRDNIALADPGMSMERVIEAAKLAGAHDFIsELPEGYDTIVGEqgagLSGGQRQRIAIARALIHNPRILIFDEATSALD 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2087760999 200 PLIRTRLQDELlefQRRLK-KTILFVSHDLdEAFRIGNRIAIMEGGRIIQCGTpHD 254
Cdd:cd03252 171 YESEHAIMRNM---HDICAgRTVIIIAHRL-STVKNADRIIVMEKGRIVEQGS-HD 221
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
32-247 |
3.99e-19 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 88.06 E-value: 3.99e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 32 EIGAATGLVLGVADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPV--VRGDVAVSTTTgpvnpyrCNAKALRDLRTH 109
Cdd:PRK13549 10 NITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHgtYEGEIIFEGEE-------LQASNIRDTERA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 110 TVSMVFQQFALLPWRTVAENVGFGLEL--AG-MPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGA 186
Cdd:PRK13549 83 GIAIIHQELALVKELSVLENIFLGNEItpGGiMDYDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQA 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2087760999 187 PILLMDEPFSALdplirTRLQDE-LLEFQRRLKK---TILFVSHDLDEAFRIGNRIAIMEGGRII 247
Cdd:PRK13549 163 RLLILDEPTASL-----TESETAvLLDIIRDLKAhgiACIYISHKLNEVKAISDTICVIRDGRHI 222
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
43-247 |
4.47e-19 |
|
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: 84.56 E-value: 4.47e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 43 VADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTT-TGPVNPyrcnakalRDLRTHtVSMVFQQFALL 121
Cdd:cd03245 20 LDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTdIRQLDP--------ADLRRN-IGYVPQDVTLF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 122 pWRTVAENVGFGLELAgmpEAERKLRVgeqLELVNLTKWAGR-------KVNE----LSGGMQQRVGLARAFATGAPILL 190
Cdd:cd03245 91 -YGTLRDNITLGAPLA---DDERILRA---AELAGVTDFVNKhpngldlQIGErgrgLSGGQRQAVALARALLNDPPILL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2087760999 191 MDEPFSALDPLIRTRLQDELLEFQRrlKKTILFVSHDLdEAFRIGNRIAIMEGGRII 247
Cdd:cd03245 164 LDEPTSAMDMNSEERLKERLRQLLG--DKTLIIITHRP-SLLDLVDRIIVMDSGRIV 217
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
6-247 |
6.09e-19 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 87.81 E-value: 6.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 6 FNNVSIIFGDRPetalamvdqgksrdeigaatglVLgvADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVA 85
Cdd:COG0488 1 LENLSKSFGGRP----------------------LL--DDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVS 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 86 VStttgpvnpyrcnakalRDLRthtVSMVFQQFALLPWRTVAENVGFGLE-----LAGMPEAERKL--------RVGE-Q 151
Cdd:COG0488 57 IP----------------KGLR---IGYLPQEPPLDDDLTVLDTVLDGDAelralEAELEELEAKLaepdedleRLAElQ 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 152 LELVNLTKWA-------------------GRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDplIRTR--LQDEL 210
Cdd:COG0488 118 EEFEALGGWEaearaeeilsglgfpeedlDRPVSELSGGWRRRVALARALLSEPDLLLLDEPTNHLD--LESIewLEEFL 195
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 2087760999 211 LEFqrrlKKTILFVSHD---LDeafRIGNRIAIMEGGRII 247
Cdd:COG0488 196 KNY----PGTVLVVSHDryfLD---RVATRILELDRGKLT 228
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
47-250 |
6.70e-19 |
|
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: 83.13 E-value: 6.70e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 47 SLTIEEGEILVLMGLSGSGKSTLLRAVNGlapvvrgdvAVSTTTGPVNPYRCNAKALRDLRTHTVSmVFQQFALLPWRTV 126
Cdd:cd03247 22 SLELKQGEKIALLGRSGSGKSTLLQLLTG---------DLKPQQGEITLDGVPVSDLEKALSSLIS-VLNQRPYLFDTTL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 127 AENVGfglelagmpeaerklrvgeqlelvnltkwagrkvNELSGGMQQRVGLARAFATGAPILLMDEPFSALDPLIRTRL 206
Cdd:cd03247 92 RNNLG----------------------------------RRFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQL 137
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2087760999 207 QDELLEFQRrlKKTILFVSHDLD--EAFrigNRIAIMEGGRIIQCG 250
Cdd:cd03247 138 LSLIFEVLK--DKTLIWITHHLTgiEHM---DKILFLENGKIIMQG 178
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
53-246 |
7.20e-19 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 84.16 E-value: 7.20e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 53 GEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTTtgpvNPYRCNAKALRDLRTHtVSMVFQQFALLPWRTVAENVGF 132
Cdd:PRK10908 28 GEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGH----DITRLKNREVPFLRRQ-IGMIFQDHHLLMDRTVYDNVAI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 133 GLELAGMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDPLIRTRLQDELLE 212
Cdd:PRK10908 103 PLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSEGILRLFEE 182
|
170 180 190
....*....|....*....|....*....|....
gi 2087760999 213 FQrRLKKTILFVSHDLDEAFRIGNRIAIMEGGRI 246
Cdd:PRK10908 183 FN-RVGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
43-246 |
7.28e-19 |
|
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: 82.65 E-value: 7.28e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 43 VADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTTtgPVNPYrcnakALRDLRTHtVSMVFQQFALLP 122
Cdd:cd03246 18 LRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGA--DISQW-----DPNELGDH-VGYLPQDDELFS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 123 wRTVAENVgfglelagmpeaerklrvgeqlelvnltkwagrkvneLSGGMQQRVGLARAFaTGAP-ILLMDEPFSALDPL 201
Cdd:cd03246 90 -GSIAENI-------------------------------------LSGGQRQRLGLARAL-YGNPrILVLDEPNSHLDVE 130
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2087760999 202 IRTRLQDELLEFQRRlKKTILFVSHDLdEAFRIGNRIAIMEGGRI 246
Cdd:cd03246 131 GERALNQAIAALKAA-GATRIVIAHRP-ETLASADRILVLEDGRV 173
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
47-258 |
8.28e-19 |
|
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: 84.13 E-value: 8.28e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 47 SLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVavstttgPVNPYRCNAKALRDLRTHtVSMVFQQFALLPwRTV 126
Cdd:cd03249 23 SLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEI-------LLDGVDIRDLNLRWLRSQ-IGLVSQEPVLFD-GTI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 127 AENVGFGLELAGMPEAERKLRVGEQLELVnlTKW-------AGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALD 199
Cdd:cd03249 94 AENIRYGKPDATDEEVEEAAKKANIHDFI--MSLpdgydtlVGERGSQLSGGQKQRIAIARALLRNPKILLLDEATSALD 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2087760999 200 PLIRTRLQDELLEFqrRLKKTILFVSHDLdEAFRIGNRIAIMEGGRIIQCGTPHDIVKN 258
Cdd:cd03249 172 AESEKLVQEALDRA--MKGRTTIVIAHRL-STIRNADLIAVLQNGQVVEQGTHDELMAQ 227
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
45-267 |
9.53e-19 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 84.48 E-value: 9.53e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 45 DASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVavsTTTGPVNPYRCNAKALRDLrthtvsmvfqqfallpwr 124
Cdd:PRK13546 42 DISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKV---DRNGEVSVIAISAGLSGQL------------------ 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 125 TVAENVGFGLELAGMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDPLIRT 204
Cdd:PRK13546 101 TGIENIEFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQ 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2087760999 205 RLQDELLEFQRRlKKTILFVSHDLDEAFRIGNRIAIMEGGRIIQCGTPHDIVKNpADQYVADF 267
Cdd:PRK13546 181 KCLDKIYEFKEQ-NKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDVLPK-YEAFLNDF 241
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
29-257 |
1.02e-18 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 87.15 E-value: 1.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 29 SRDEIGAATGLVLGVADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTTTGPVNPYRCNAKAlrdlrt 108
Cdd:PRK09700 7 SMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQL------ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 109 hTVSMVFQQFALLPWRTVAENVGFGLELA----GMP---EAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARA 181
Cdd:PRK09700 81 -GIGIIYQELSVIDELTVLENLYIGRHLTkkvcGVNiidWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 182 FATGAPILLMDEPFSALDplirTRLQDELLEFQRRLK---KTILFVSHDLDEAFRIGNRIAIMEGG-----RIIQCGTPH 253
Cdd:PRK09700 160 LMLDAKVIIMDEPTSSLT----NKEVDYLFLIMNQLRkegTAIVYISHKLAEIRRICDRYTVMKDGssvcsGMVSDVSND 235
|
....
gi 2087760999 254 DIVK 257
Cdd:PRK09700 236 DIVR 239
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
43-226 |
1.03e-18 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 87.17 E-value: 1.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 43 VADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAvstttgpvnpyrcnakalrdlRTHTVSMVFqqfalLP 122
Cdd:COG4178 379 LEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIA---------------------RPAGARVLF-----LP 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 123 WR------TVAENVGFGLELAGMPEAErklrVGEQLELVNLTKWAGRkVNE-------LSGGMQQRVGLARAFATGAPIL 189
Cdd:COG4178 433 QRpylplgTLREALLYPATAEAFSDAE----LREALEAVGLGHLAER-LDEeadwdqvLSLGEQQRLAFARLLLHKPDWL 507
|
170 180 190
....*....|....*....|....*....|....*....
gi 2087760999 190 LMDEPFSALDPlirtRLQDELLE-FQRRLKK-TILFVSH 226
Cdd:COG4178 508 FLDEATSALDE----ENEAALYQlLREELPGtTVISVGH 542
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
50-264 |
2.01e-18 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 86.25 E-value: 2.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 50 IEEGEILVLMGLSGSGKSTLLravNGLAPVVRGDVAVSTTTgPVNPYRCNAKALRdlrthTVSMVFQQFAL-LPWRTVAE 128
Cdd:TIGR00955 48 AKPGELLAVMGSSGAGKTTLM---NALAFRSPKGVKGSGSV-LLNGMPIDAKEMR-----AISAYVQQDDLfIPTLTVRE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 129 NVGFGLEL---AGMPEAERKLRVGEQLELVNLTKWA------GRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALD 199
Cdd:TIGR00955 119 HLMFQAHLrmpRRVTKKEKRERVDEVLQALGLRKCAntrigvPGRVKGLSGGERKRLAFASELLTDPPLLFCDEPTSGLD 198
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2087760999 200 PLIRTRLQDELLEFQRRLKKTILFVSHDLDEAFRIGNRIAIMEGGRIIQCGTPHDIVK-------------NPADQYV 264
Cdd:TIGR00955 199 SFMAYSVVQVLKGLAQKGKTIICTIHQPSSELFELFDKIILMAEGRVAYLGSPDQAVPffsdlghpcpenyNPADFYV 276
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
45-271 |
2.24e-18 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 86.03 E-value: 2.24e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 45 DASLTIEEGEILVLMGLSGSGKSTLL----RAVNglapVVRGDVAVSTTtgPVNPYrcNAKALRDlrthTVSMVFQQFAL 120
Cdd:PRK11160 358 GLSLQIKAGEKVALLGRTGCGKSTLLqlltRAWD----PQQGEILLNGQ--PIADY--SEAALRQ----AISVVSQRVHL 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 121 LPwRTVAENvgfgLELAGmPEA--ERKLRVGEQLELVNLTK-------WAGRKVNELSGGMQQRVGLARAFATGAPILLM 191
Cdd:PRK11160 426 FS-ATLRDN----LLLAA-PNAsdEALIEVLQQVGLEKLLEddkglnaWLGEGGRQLSGGEQRRLGIARALLHDAPLLLL 499
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 192 DEPFSALDPLIRTRLQDELLEFQRrlKKTILFVSHDLD--EAFrigNRIAIMEGGRIIQCGTPHDIVKNpaDQYVADFVQ 269
Cdd:PRK11160 500 DEPTEGLDAETERQILELLAEHAQ--NKTVLMITHRLTglEQF---DRICVMDNGQIIEQGTHQELLAQ--QGRYYQLKQ 572
|
..
gi 2087760999 270 NL 271
Cdd:PRK11160 573 RL 574
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
32-273 |
2.55e-18 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 84.57 E-value: 2.55e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 32 EIGAATGLVLGVADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAP---VVRGDvavSTTTGPVNPYRCNAKALRDLRT 108
Cdd:COG4170 12 EIDTPQGRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKdnwHVTAD---RFRWNGIDLLKLSPRERRKIIG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 109 HTVSMVFQ--QFALLPwrtvAENVGFGLELAgMPEAE-----------RKLRVGEQLELVNLTKWagRKV-----NELSG 170
Cdd:COG4170 89 REIAMIFQepSSCLDP----SAKIGDQLIEA-IPSWTfkgkwwqrfkwRKKRAIELLHRVGIKDH--KDImnsypHELTE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 171 GMQQRVGLARAFATGAPILLMDEPFSALDPLirTRLQD-ELLEFQRRLKKT-ILFVSHDLDEAFRIGNRIAIMEGGRIIQ 248
Cdd:COG4170 162 GECQKVMIAMAIANQPRLLIADEPTNAMEST--TQAQIfRLLARLNQLQGTsILLISHDLESISQWADTITVLYCGQTVE 239
|
250 260 270
....*....|....*....|....*....|..
gi 2087760999 249 CGTPHDIVKNPADQY-------VADFVQNLNP 273
Cdd:COG4170 240 SGPTEQILKSPHHPYtkallrsMPDFRQPLPH 271
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
40-263 |
4.05e-18 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 85.29 E-value: 4.05e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 40 VLGVADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVavstTTGPVNPYRCN----------AKALRDLRTH 109
Cdd:PRK10261 29 IAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLV----QCDKMLLRRRSrqvielseqsAAQMRHVRGA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 110 TVSMVFQQ--FALLPWRTVAENV--------GFGLELAgMPEAERKLrvgEQLELVNLTKWAGRKVNELSGGMQQRVGLA 179
Cdd:PRK10261 105 DMAMIFQEpmTSLNPVFTVGEQIaesirlhqGASREEA-MVEAKRML---DQVRIPEAQTILSRYPHQLSGGMRQRVMIA 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 180 RAFATGAPILLMDEPFSALDPLIRTRLQDELLEFQRRLKKTILFVSHDLDEAFRIGNRIAIMEGGRIIQCGTPHDIVKNP 259
Cdd:PRK10261 181 MALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQIFHAP 260
|
....
gi 2087760999 260 ADQY 263
Cdd:PRK10261 261 QHPY 264
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
43-258 |
4.18e-18 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 82.25 E-value: 4.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 43 VADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTTTGPVNPYrcNAKALRDlrthtVSMVFQQFALLP 122
Cdd:PRK10895 19 VEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPL--HARARRG-----IGYLPQEASIFR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 123 WRTVAENVGFGLEL-AGMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDPL 201
Cdd:PRK10895 92 RLSVYDNLMAVLQIrDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPI 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2087760999 202 IRTRLQdELLEFQRRLKKTILFVSHDLDEAFRIGNRIAIMEGGRIIQCGTPHDIVKN 258
Cdd:PRK10895 172 SVIDIK-RIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQD 227
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
58-255 |
4.49e-18 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 82.75 E-value: 4.49e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 58 LMGLSGSGKSTLLRAVNGLAPVVRGdvAVSTTTGPVNPYRCNAKALRdlrtHTVSMVFQQFALLPWRT-VAENVGFGLEL 136
Cdd:PRK13638 32 LVGANGCGKSTLFMNLSGLLRPQKG--AVLWQGKPLDYSKRGLLALR----QQVATVFQDPEQQIFYTdIDSDIAFSLRN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 137 AGMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDPLIRTrlqdELLEFQRR 216
Cdd:PRK13638 106 LGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRT----QMIAIIRR 181
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2087760999 217 L---KKTILFVSHDLDEAFRIGNRIAIMEGGRIIQCGTPHDI 255
Cdd:PRK13638 182 IvaqGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEV 223
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
45-228 |
8.43e-18 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 82.24 E-value: 8.43e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 45 DASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTTtgPVNpyrcnakalRDLRTHTVSMVFQQ------F 118
Cdd:PRK15056 25 DASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQ--PTR---------QALQKNLVAYVPQSeevdwsF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 119 ALLPWRTVAENVGFGLELAGMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSAL 198
Cdd:PRK15056 94 PVLVEDVVMMGRYGHMGWLRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGV 173
|
170 180 190
....*....|....*....|....*....|
gi 2087760999 199 DPLIRTRLQDELLEFqRRLKKTILFVSHDL 228
Cdd:PRK15056 174 DVKTEARIISLLREL-RDEGKTMLVSTHNL 202
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
38-247 |
1.38e-17 |
|
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: 83.72 E-value: 1.38e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 38 GLVLGVADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTTTGPVnpyrcNAKALRDLRTHTVSMVFQQ 117
Cdd:TIGR02633 12 GGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTWDGEIYWSGSPL-----KASNIRDTERAGIVIIHQE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 118 FALLPWRTVAENVGFGLEL----AGMPEAERKLRVGEQLELVNLTKW-AGRKVNELSGGMQQRVGLARAFATGAPILLMD 192
Cdd:TIGR02633 87 LTLVPELSVAENIFLGNEItlpgGRMAYNAMYLRAKNLLRELQLDADnVTRPVGDYGGGQQQLVEIAKALNKQARLLILD 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2087760999 193 EPFSALdplirTRLQDE-LLEFQRRLKK---TILFVSHDLDEAFRIGNRIAIMEGGRII 247
Cdd:TIGR02633 167 EPSSSL-----TEKETEiLLDIIRDLKAhgvACVYISHKLNEVKAVCDTICVIRDGQHV 220
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
32-263 |
1.88e-17 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 82.16 E-value: 1.88e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 32 EIGAATGLVLGVADASLTIEEGEILVLMGLSGSGKSTLLRAVNGlapVVRGDVAVSTTT---GPVNPYRCNAKALRDLRT 108
Cdd:PRK15093 12 EFKTSDGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICG---VTKDNWRVTADRmrfDDIDLLRLSPRERRKLVG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 109 HTVSMVFQ--QFALLPwrtvAENVGFGLeLAGMPEAE-----------RKLRVGEQLELVNLT--KWAGRKVN-ELSGGM 172
Cdd:PRK15093 89 HNVSMIFQepQSCLDP----SERVGRQL-MQNIPGWTykgrwwqrfgwRKRRAIELLHRVGIKdhKDAMRSFPyELTEGE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 173 QQRVGLARAFATGAPILLMDEPFSALDPLIRTRLQDELLEFQRRLKKTILFVSHDLDEAFRIGNRIAIMEGGRIIQCGTP 252
Cdd:PRK15093 164 CQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTVETAPS 243
|
250
....*....|.
gi 2087760999 253 HDIVKNPADQY 263
Cdd:PRK15093 244 KELVTTPHHPY 254
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
37-259 |
2.95e-17 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 80.60 E-value: 2.95e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 37 TGL-----VLGVADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTTTGPVNPYRcnakalrdLRTHTV 111
Cdd:PRK15112 18 TGWfrrqtVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYS--------YRSQRI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 112 SMVFQ--QFALLPWRTVAENVGFGLEL-AGMPEAERKLRVGEQLELVNL-TKWAGRKVNELSGGMQQRVGLARAFATGAP 187
Cdd:PRK15112 90 RMIFQdpSTSLNPRQRISQILDFPLRLnTDLEPEQREKQIIETLRQVGLlPDHASYYPHMLAPGQKQRLGLARALILRPK 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2087760999 188 ILLMDEPFSALDPLIRTRLQDELLEFQRRLKKTILFVSHDLDEAFRIGNRIAIMEGGRIIQCGTPHDIVKNP 259
Cdd:PRK15112 170 VIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVLASP 241
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
47-255 |
3.71e-17 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 79.88 E-value: 3.71e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 47 SLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPvVRGDVAVSTTtgPVNpyRCNAKALRDLRthtvSMVFQQFALLPWRTV 126
Cdd:COG4138 16 SAQVNAGELIHLIGPNGAGKSTLLARMAGLLP-GQGEILLNGR--PLS--DWSAAELARHR----AYLSQQQSPPFAMPV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 127 AENVGFGLElAGMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAF--------ATGApILLMDEPFSAL 198
Cdd:COG4138 87 FQYLALHQP-AGASSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLlqvwptinPEGQ-LLLLDEPMNSL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2087760999 199 DplIRTRLQ-DELLEFQRRLKKTILFVSHDLDEAFRIGNRIAIMEGGRIIQCGTPHDI 255
Cdd:COG4138 165 D--VAQQAAlDRLLRELCQQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEV 220
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
45-253 |
3.97e-17 |
|
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: 79.19 E-value: 3.97e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 45 DASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTTtgPVNPYrcNAKALRDLrthtVSMVFQQFALLPwR 124
Cdd:cd03254 21 DINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGI--DIRDI--SRKSLRSM----IGVVLQDTFLFS-G 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 125 TVAENVGFGLELAGMPEAERKLR-VGEQLELVNLTK----WAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALD 199
Cdd:cd03254 92 TIMENIRLGRPNATDEEVIEAAKeAGAHDFIMKLPNgydtVLGENGGNLSQGERQLLAIARAMLRDPKILILDEATSNID 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2087760999 200 PLIRTRLQDELLEFQRrlKKTILFVSHDLDeAFRIGNRIAIMEGGRIIQCGTPH 253
Cdd:cd03254 172 TETEKLIQEALEKLMK--GRTSIIIAHRLS-TIKNADKILVLDDGKIIEEGTHD 222
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
42-251 |
4.10e-17 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 82.32 E-value: 4.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 42 GVADASLTIEEGEILVLMGLSGSGKSTLL----RAVNGLAPVVRGD-VAVSTTTgpvnpyrcnakaLRDLRtHTVSMVFQ 116
Cdd:PRK13657 350 GVEDVSFEAKPGQTVAIVGPTGAGKSTLInllqRVFDPQSGRILIDgTDIRTVT------------RASLR-RNIAVVFQ 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 117 QfALLPWRTVAENVGFGLELAGMPEAERKLRVGEQLELV-----NLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLM 191
Cdd:PRK13657 417 D-AGLFNRSIEDNIRVGRPDATDEEMRAAAERAQAHDFIerkpdGYDTVVGERGRQLSGGERQRLAIARALLKDPPILIL 495
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 192 DEPFSALDPLIRTRLQDELLEFQRrlKKTILFVSHDLdEAFRIGNRIAIMEGGRIIQCGT 251
Cdd:PRK13657 496 DEATSALDVETEAKVKAALDELMK--GRTTFIIAHRL-STVRNADRILVFDNGRVVESGS 552
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
43-257 |
4.47e-17 |
|
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: 82.10 E-value: 4.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 43 VADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVavstttgpvnpyRCNAKALR-----DLRTHtVSMVFQQ 117
Cdd:COG4618 348 LRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSV------------RLDGADLSqwdreELGRH-IGYLPQD 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 118 FALLPwRTVAENVG-FG----------LELAGMPEAERKL------RVGEqlelvnltkwAGRKvneLSGGMQQRVGLAR 180
Cdd:COG4618 415 VELFD-GTIAENIArFGdadpekvvaaAKLAGVHEMILRLpdgydtRIGE----------GGAR---LSGGQRQRIGLAR 480
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2087760999 181 AFAtGAP-ILLMDEPFSALDPLIRTRLQDELLEFQRRlKKTILFVSHDLdEAFRIGNRIAIMEGGRIIQCGTPHDIVK 257
Cdd:COG4618 481 ALY-GDPrLVVLDEPNSNLDDEGEAALAAAIRALKAR-GATVVVITHRP-SLLAAVDKLLVLRDGRVQAFGPRDEVLA 555
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
45-257 |
1.08e-16 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 79.10 E-value: 1.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 45 DASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAP--------VVRGDVAVSTttgpvNPYRC-NAKALRDLRTHTVSMVF 115
Cdd:PRK13547 19 DLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTgggaprgaRVTGDVTLNG-----EPLAAiDAPRLARLRAVLPQAAQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 116 QQFALlpwrTVAENVGFGLELAGMPEAERKLRVGE----QLELVNLTKWAGRKVNELSGGMQQRVGLARAFA-------- 183
Cdd:PRK13547 94 PAFAF----SAREIVLLGRYPHARRAGALTHRDGEiawqALALAGATALVGRDVTTLSGGELARVQFARVLAqlwpphda 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2087760999 184 -TGAPILLMDEPFSALDPLIRTRLQDELLEFQRRLKKTILFVSHDLDEAFRIGNRIAIMEGGRIIQCGTPHDIVK 257
Cdd:PRK13547 170 aQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPADVLT 244
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
4-245 |
1.21e-16 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 75.56 E-value: 1.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 4 VNFNNVSIIFGDRPetalamvdqgksrdeigaatglVLgvADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGD 83
Cdd:cd03221 1 IELENLSKTYGGKL----------------------LL--KDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGI 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 84 VAVSTTTGPVnpyrcnakalrdlrthtvsmVFQQfallpwrtvaenvgfglelagmpeaerklrvgeqlelvnltkwagr 163
Cdd:cd03221 57 VTWGSTVKIG--------------------YFEQ---------------------------------------------- 70
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 164 kvneLSGGMQQRVGLARAFATGAPILLMDEPFSALDPLIRTRLQDELLEFQRrlkkTILFVSHdlDEAF--RIGNRIAIM 241
Cdd:cd03221 71 ----LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEEALKEYPG----TVILVSH--DRYFldQVATKIIEL 140
|
....
gi 2087760999 242 EGGR 245
Cdd:cd03221 141 EDGK 144
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
40-247 |
1.54e-16 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 80.46 E-value: 1.54e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 40 VLGVADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVstttGPVNPYRCNAKALRDLRTHTVSMVFQQFA 119
Cdd:COG3845 271 VPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRL----DGEDITGLSPRERRRLGVAYIPEDRLGRG 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 120 LLPWRTVAENvgFGLELAGMPEAERK--LRVGEqlelvnLTKWAGRKVNE--------------LSGGMQQRVGLARAFA 183
Cdd:COG3845 347 LVPDMSVAEN--LILGRYRRPPFSRGgfLDRKA------IRAFAEELIEEfdvrtpgpdtparsLSGGNQQKVILARELS 418
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2087760999 184 TGAPILLMDEPFSALDP----LIRTRLQDellefQRRLKKTILFVSHDLDEAFRIGNRIAIMEGGRII 247
Cdd:COG3845 419 RDPKLLIAAQPTRGLDVgaieFIHQRLLE-----LRDAGAAVLLISEDLDEILALSDRIAVMYEGRIV 481
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
31-230 |
2.20e-16 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 77.06 E-value: 2.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 31 DEIGAATGLVLGVADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDV---AVSTTTGPVNPYRcnakalrdlr 107
Cdd:PRK10247 11 QNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLlfeGEDISTLKPEIYR---------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 108 tHTVSMVFQQFALLPwRTVAENVGFGLELAGM-PEAERKLRVGEQLELVN--LTKwagrKVNELSGGMQQRVGLARAFAT 184
Cdd:PRK10247 81 -QQVSYCAQTPTLFG-DTVYDNLIFPWQIRNQqPDPAIFLDDLERFALPDtiLTK----NIAELSGGEKQRISLIRNLQF 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2087760999 185 GAPILLMDEPFSALDPLIRTRLQDELLEFQRRLKKTILFVSHDLDE 230
Cdd:PRK10247 155 MPKVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDE 200
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
45-253 |
2.26e-16 |
|
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: 77.27 E-value: 2.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 45 DASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTttgpvnpyrcnakalRDLRTHTVSMVFQQFALLPWR 124
Cdd:cd03253 19 DVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDG---------------QDIREVTLDSLRRAIGVVPQD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 125 TV------AENVGFGLELAG---MPEAERKLRVGEqlELVNLTKWAGRKVNE----LSGGMQQRVGLARAFATGAPILLM 191
Cdd:cd03253 84 TVlfndtiGYNIRYGRPDATdeeVIEAAKAAQIHD--KIMRFPDGYDTIVGErglkLSGGEKQRVAIARAILKNPPILLL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2087760999 192 DEPFSALDPLIRTRLQDELLEFQRRlkKTILFVSHDLDEafrIGN--RIAIMEGGRIIQCGTPH 253
Cdd:cd03253 162 DEATSALDTHTEREIQAALRDVSKG--RTTIVIAHRLST---IVNadKIIVLKDGRIVERGTHE 220
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
43-228 |
2.32e-16 |
|
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: 76.99 E-value: 2.32e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 43 VADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTttgpVNPYRCNAKALRDLRTHTVSMVFQQfallP 122
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSN----KNESEPSFEATRSRNRYSVAYAAQK----P 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 123 W---RTVAENVGFG-----------LELAGMPEAERKLRVGEQLELvnltkwAGRKVNeLSGGMQQRVGLARAFATGAPI 188
Cdd:cd03290 89 WllnATVEENITFGspfnkqrykavTDACSLQPDIDLLPFGDQTEI------GERGIN-LSGGQRQRICVARALYQNTNI 161
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2087760999 189 LLMDEPFSALDPLIRTRL-QDELLEFQRRLKKTILFVSHDL 228
Cdd:cd03290 162 VFLDDPFSALDIHLSDHLmQEGILKFLQDDKRTLVLVTHKL 202
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
47-247 |
2.98e-16 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 77.43 E-value: 2.98e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 47 SLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAV---STTTGPVnpYRcnakalrdlRTHTVSMVFQQfallPW 123
Cdd:COG1101 26 NLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIdgkDVTKLPE--YK---------RAKYIGRVFQD----PM 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 124 R------TVAENvgfgLELAGMPEAERKLRVG----------EQLELVNLtkwaG---R---KVNELSGGmqQRVGLARA 181
Cdd:COG1101 91 MgtapsmTIEEN----LALAYRRGKRRGLRRGltkkrrelfrELLATLGL----GlenRldtKVGLLSGG--QRQALSLL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2087760999 182 FATGAP--ILLMDEPFSALDPliRTrlQDELLEFQRRL----KKTILFVSHDLDEAFRIGNRIAIMEGGRII 247
Cdd:COG1101 161 MATLTKpkLLLLDEHTAALDP--KT--AALVLELTEKIveenNLTTLMVTHNMEQALDYGNRLIMMHEGRII 228
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
45-247 |
4.46e-16 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 78.95 E-value: 4.46e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 45 DASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVStttgpvnpyrcnakalrdlrtHTVSMVF--QQFALL- 121
Cdd:COG0488 333 DLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLG---------------------ETVKIGYfdQHQEELd 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 122 PWRTVAENVGfglelAGMPEA-ERKLR--------VGEQlelvnltkwAGRKVNELSGGMQQRVGLARAFATGAPILLMD 192
Cdd:COG0488 392 PDKTVLDELR-----DGAPGGtEQEVRgylgrflfSGDD---------AFKPVGVLSGGEKARLALAKLLLSPPNVLLLD 457
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2087760999 193 EPFSALDPLIRTRLQDELLEFqrrlKKTILFVSHD---LDeafRIGNRIAIMEGGRII 247
Cdd:COG0488 458 EPTNHLDIETLEALEEALDDF----PGTVLLVSHDryfLD---RVATRILEFEDGGVR 508
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
47-199 |
5.82e-16 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 75.61 E-value: 5.82e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 47 SLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVavstttgpvnpyRCNAKALRDLRTHtvsmvFQQfALL----- 121
Cdd:PRK13538 21 SFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEV------------LWQGEPIRRQRDE-----YHQ-DLLylghq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 122 ----PWRTVAENVGFGLELAGMPEAERklrVGEQLELVNLtkwAGRK---VNELSGGMQQRVGLARAFATGAPILLMDEP 194
Cdd:PRK13538 83 pgikTELTALENLRFYQRLHGPGDDEA---LWEALAQVGL---AGFEdvpVRQLSAGQQRRVALARLWLTRAPLWILDEP 156
|
....*
gi 2087760999 195 FSALD 199
Cdd:PRK13538 157 FTAID 161
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
43-257 |
5.91e-16 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 79.01 E-value: 5.91e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 43 VADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVsttTG-PVNPyrcnakalRDLRT-HTVSMVFQQFAL 120
Cdd:NF033858 282 VDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWL---FGqPVDA--------GDIATrRRVGYMSQAFSL 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 121 LPWRTVAENvgfgLEL-A---GMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFS 196
Cdd:NF033858 351 YGELTVRQN----LELhArlfHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTS 426
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2087760999 197 ALDPLIRTRLQDELLEFQRRLKKTIlFVS-HDLDEAFRIgNRIAIMEGGRIIQCGTPHDIVK 257
Cdd:NF033858 427 GVDPVARDMFWRLLIELSREDGVTI-FIStHFMNEAERC-DRISLMHAGRVLASDTPAALVA 486
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
47-259 |
1.17e-15 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 75.35 E-value: 1.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 47 SLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVvRGDVAVstttgpvnpyrcNAKALRDLRTHTVSM------------- 113
Cdd:PRK03695 16 SAEVRAGEILHLVGPNGAGKSTLLARMAGLLPG-SGSIQF------------AGQPLEAWSAAELARhraylsqqqtppf 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 114 ---VFQQFAL-LPwrtvaenvgfglelAGMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAP-- 187
Cdd:PRK03695 83 ampVFQYLTLhQP--------------DKTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVLQVWPdi 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2087760999 188 -----ILLMDEPFSALDPLIRTRLqDELLEFQRRLKKTILFVSHDLDEAFRIGNRIAIMEGGRIIQCGTPHDIVKNP 259
Cdd:PRK03695 149 npagqLLLLDEPMNSLDVAQQAAL-DRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVLTPE 224
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
45-228 |
1.36e-15 |
|
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: 77.79 E-value: 1.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 45 DASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTTtgPVNPYRCNAKALRdlrthtVSmVFQQFALLPWR 124
Cdd:TIGR02868 353 GVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGV--PVSSLDQDEVRRR------VS-VCAQDAHLFDT 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 125 TVAENVGFGLELAGMPEAERKL-RVGEQLELVNLTKWAGRKVNE----LSGGMQQRVGLARAFATGAPILLMDEPFSALD 199
Cdd:TIGR02868 424 TVRENLRLARPDATDEELWAALeRVGLADWLRALPDGLDTVLGEggarLSGGERQRLALARALLADAPILLLDEPTEHLD 503
|
170 180
....*....|....*....|....*....
gi 2087760999 200 PLIRTRLQDELLEFQRRlkKTILFVSHDL 228
Cdd:TIGR02868 504 AETADELLEDLLAALSG--RTVVLITHHL 530
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
45-229 |
3.35e-15 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 73.84 E-value: 3.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 45 DASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTTTGPVNPyrcnAKALRDlrthtvsmvfqqfALLPWR 124
Cdd:COG2401 48 DLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVDVPDNQFGR----EASLID-------------AIGRKG 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 125 TVAENVGFgLELAGMPEAerklrvgeQLELvnltkwagRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDPLIRT 204
Cdd:COG2401 111 DFKDAVEL-LNAVGLSDA--------VLWL--------RRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAK 173
|
170 180
....*....|....*....|....*
gi 2087760999 205 RLQDELLEFQRRLKKTILFVSHDLD 229
Cdd:COG2401 174 RVARNLQKLARRAGITLVVATHHYD 198
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
40-248 |
4.56e-15 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 75.98 E-value: 4.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 40 VLGVADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAP--------VVRGDVavstttgpvnpyrCNAKALRDLRTHTV 111
Cdd:NF040905 14 VKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPhgsyegeiLFDGEV-------------CRFKDIRDSEALGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 112 SMVFQQFALLPWRTVAENVGFGLELA--GM---PEAERKLRvgEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGA 186
Cdd:NF040905 81 VIIHQELALIPYLSIAENIFLGNERAkrGVidwNETNRRAR--ELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDV 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2087760999 187 PILLMDEPFSALDPLIRTRLQDELLEFQRRLKKTILfVSHDLDEAFRIGNRIAIMEGGRIIQ 248
Cdd:NF040905 159 KLLILDEPTAALNEEDSAALLDLLLELKAQGITSII-ISHKLNEIRRVADSITVLRDGRTIE 219
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
21-199 |
5.77e-15 |
|
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: 72.53 E-value: 5.77e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 21 LAMVDQGKSRDEIGAATGLvlgvadaSLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVavSTTTGPVNpyrcna 100
Cdd:cd03231 1 LEADELTCERDGRALFSGL-------SFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRV--LLNGGPLD------ 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 101 kALRDLRTHTVSMVFQQFALLPWRTVAENVGFGLELAGMPEAErklrvgEQLELVNLTKWAGRKVNELSGGMQQRVGLAR 180
Cdd:cd03231 66 -FQRDSIARGLLYLGHAPGIKTTLSVLENLRFWHADHSDEQVE------EALARVGLNGFEDRPVAQLSAGQQRRVALAR 138
|
170
....*....|....*....
gi 2087760999 181 AFATGAPILLMDEPFSALD 199
Cdd:cd03231 139 LLLSGRPLWILDEPTTALD 157
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
45-247 |
8.36e-15 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 75.15 E-value: 8.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 45 DASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTTtgPVNpYRCNAKALRdlrtHTVSMVFQQFALLPWR 124
Cdd:PRK10982 16 NVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGK--EID-FKSSKEALE----NGISMVHQELNLVLQR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 125 TVAENVGFG-LELAGMPEAERKL-----RVGEQLEL-VNLTKwagrKVNELSGGMQQRVGLARAFATGAPILLMDEPFSA 197
Cdd:PRK10982 89 SVMDNMWLGrYPTKGMFVDQDKMyrdtkAIFDELDIdIDPRA----KVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSS 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2087760999 198 LDplirTRLQDELLEFQRRLKKT---ILFVSHDLDEAFRIGNRIAIMEGGRII 247
Cdd:PRK10982 165 LT----EKEVNHLFTIIRKLKERgcgIVYISHKMEEIFQLCDEITILRDGQWI 213
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
45-251 |
1.22e-14 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 74.67 E-value: 1.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 45 DASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTTTgpVNPYRcnakaLRDLRTHtVSMVFQQFALLPwR 124
Cdd:PRK11176 361 NINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHD--LRDYT-----LASLRNQ-VALVSQNVHLFN-D 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 125 TVAENVGFGL-ELAGMPEAERKLRVGEQLELVN-----LTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSAL 198
Cdd:PRK11176 432 TIANNIAYARtEQYSREQIEEAARMAYAMDFINkmdngLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSAL 511
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2087760999 199 DPLIRTRLQDELLEFQRrlKKTILFVSHDL------DEafrignrIAIMEGGRIIQCGT 251
Cdd:PRK11176 512 DTESERAIQAALDELQK--NRTSLVIAHRLstiekaDE-------ILVVEDGEIVERGT 561
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
43-263 |
1.60e-14 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 74.36 E-value: 1.60e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 43 VADASLTIEEGEILVLMGLSGSGKST----LLRAVNGlapvvRGDVAVSTTtgPVnpYRCNAKALRDLRtHTVSMVFQ-- 116
Cdd:PRK15134 302 VKNISFTLRPGETLGLVGESGSGKSTtglaLLRLINS-----QGEIWFDGQ--PL--HNLNRRQLLPVR-HRIQVVFQdp 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 117 QFALLPWRTVAENVGFGLEL--AGMPEAERKLRVGEQLELVNL---TKWagRKVNELSGGMQQRVGLARAFATGAPILLM 191
Cdd:PRK15134 372 NSSLNPRLNVLQIIEEGLRVhqPTLSAAQREQQVIAVMEEVGLdpeTRH--RYPAEFSGGQRQRIAIARALILKPSLIIL 449
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2087760999 192 DEPFSALDPLIRTRLQDELLEFQRRLKKTILFVSHDLDEAFRIGNRIAIMEGGRIIQCGTPHDIVKNPADQY 263
Cdd:PRK15134 450 DEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERVFAAPQQEY 521
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
8-246 |
2.29e-14 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 73.79 E-value: 2.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 8 NVSIIFGDRPEtalamvDQGKSRDEIGAATGLVLGvADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVS 87
Cdd:PRK11288 241 EIGDIYGYRPR------PLGEVRLRLDGLKGPGLR-EPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLD 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 88 tttGPVNPYRCNAKALRdlrthtVSMVF-----QQFALLPWRTVAENVG---------FGLELAGMPEAE------RKLR 147
Cdd:PRK11288 314 ---GKPIDIRSPRDAIR------AGIMLcpedrKAEGIIPVHSVADNINisarrhhlrAGCLINNRWEAEnadrfiRSLN 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 148 VGeqlelvnlTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDPLIRTRLQDELLEFQRRlKKTILFVSHD 227
Cdd:PRK11288 385 IK--------TPSREQLIMNLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYELAAQ-GVAVLFVSSD 455
|
250
....*....|....*....
gi 2087760999 228 LDEAFRIGNRIAIMEGGRI 246
Cdd:PRK11288 456 LPEVLGVADRIVVMREGRI 474
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
50-274 |
2.45e-14 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 74.28 E-value: 2.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 50 IEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTTTGPVNpyrcnakalrdlrthtVSMVFQQFALLPWRTVAEN 129
Cdd:TIGR01257 1962 VRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTN----------------ISDVHQNMGYCPQFDAIDD 2025
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 130 VGFGLE-------LAGMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDPLI 202
Cdd:TIGR01257 2026 LLTGREhlylyarLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQA 2105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 203 RTRLQDELLEFQRRlKKTILFVSHDLDEAFRIGNRIAIMEGGRIIQCGTPHDIVKNPADQYVA---------DFVQNLNP 273
Cdd:TIGR01257 2106 RRMLWNTIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGTIQHLKSKFGDGYIVtmkikspkdDLLPDLNP 2184
|
.
gi 2087760999 274 I 274
Cdd:TIGR01257 2185 V 2185
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
43-226 |
4.60e-14 |
|
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: 69.10 E-value: 4.60e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 43 VADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTTTG----PVNPYrCNAKALRDLrthtvsmvfqqf 118
Cdd:cd03223 17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEGEDllflPQRPY-LPLGTLREQ------------ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 119 ALLPWRTVaenvgfglelagmpeaerklrvgeqlelvnltkwagrkvneLSGGMQQRVGLARAFATGAPILLMDEPFSAL 198
Cdd:cd03223 84 LIYPWDDV-----------------------------------------LSGGEQQRLAFARLLLHKPKFVFLDEATSAL 122
|
170 180
....*....|....*....|....*...
gi 2087760999 199 DPlirtRLQDELLEFQRRLKKTILFVSH 226
Cdd:cd03223 123 DE----ESEDRLYQLLKELGITVISVGH 146
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
47-259 |
4.81e-14 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 72.96 E-value: 4.81e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 47 SLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVvRGDVAVstttgpvnpyrcNAKALRDL-----RTHtVSMVFQQfALL 121
Cdd:PRK11174 370 NFTLPAGQRIALVGPSGAGKTSLLNALLGFLPY-QGSLKI------------NGIELRELdpeswRKH-LSWVGQN-PQL 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 122 PWRTVAENVGFG------------LELAGMPEAERKL------RVGEQlelvnltkwAGRkvneLSGGMQQRVGLARAFA 183
Cdd:PRK11174 435 PHGTLRDNVLLGnpdasdeqlqqaLENAWVSEFLPLLpqgldtPIGDQ---------AAG----LSVGQAQRLALARALL 501
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2087760999 184 TGAPILLMDEPFSALDPLIRTRLQDELLEFQRRlkKTILFVSHDLDEAFRIgNRIAIMEGGRIIQCGTPHDIVKNP 259
Cdd:PRK11174 502 QPCQLLLLDEPTASLDAHSEQLVMQALNAASRR--QTTLMVTHQLEDLAQW-DQIWVMQDGQIVQQGDYAELSQAG 574
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
47-248 |
6.19e-14 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 72.70 E-value: 6.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 47 SLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTTtgPVnpyrcNAKALRDLRTHtVSMVFQQFALlpWRTV 126
Cdd:PRK10522 343 NLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGK--PV-----TAEQPEDYRKL-FSAVFTDFHL--FDQL 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 127 AENVGFGLELAGMPEAERKLRVGEQLELVNltkwaGRKVN-ELSGGMQQRVGLARAFATGAPILLMDEPFSALDPLIRTR 205
Cdd:PRK10522 413 LGPEGKPANPALVEKWLERLKMAHKLELED-----GRISNlKLSKGQKKRLALLLALAEERDILLLDEWAADQDPHFRRE 487
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2087760999 206 LQDELLEFQRRLKKTILFVSHDlDEAFRIGNRIAIMEGGRIIQ 248
Cdd:PRK10522 488 FYQVLLPLLQEMGKTIFAISHD-DHYFIHADRLLEMRNGQLSE 529
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
40-247 |
7.16e-14 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 72.34 E-value: 7.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 40 VLGVADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVA----VSTTTGPvnpyrcnakalRDLRTHTVSMVF 115
Cdd:PRK10762 17 VKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILylgkEVTFNGP-----------KSSQEAGIGIIH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 116 QQFALLPWRTVAENVGFGLELAG---------MPEAERKLrvgeqLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGA 186
Cdd:PRK10762 86 QELNLIPQLTIAENIFLGREFVNrfgridwkkMYAEADKL-----LARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFES 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2087760999 187 PILLMDEPFSALdplirTRLQDE-LLEFQRRLKKT---ILFVSHDLDEAFRIGNRIAIMEGGRII 247
Cdd:PRK10762 161 KVIIMDEPTDAL-----TDTETEsLFRVIRELKSQgrgIVYISHRLKEIFEICDDVTVFRDGQFI 220
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
45-256 |
7.95e-14 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 70.40 E-value: 7.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 45 DASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTTTgpVNPYRCNAKALRdlrthtVSMVFQQFALLPWR 124
Cdd:PRK10253 25 NLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEH--IQHYASKEVARR------IGLLAQNATTPGDI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 125 TVAENVGFG----LELAGMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDP 200
Cdd:PRK10253 97 TVQELVARGryphQPLFTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDI 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2087760999 201 LIRTRLQDELLEFQRRLKKTILFVSHDLDEAFRIGNRIAIMEGGRIIQCGTPHDIV 256
Cdd:PRK10253 177 SHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIV 232
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
43-248 |
3.57e-13 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 70.20 E-value: 3.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 43 VADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVS-TTTGPVNPYRCNAKALRdlrthTVSMVFQQFALL 121
Cdd:PRK09700 279 VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNgKDISPRSPLDAVKKGMA-----YITESRRDNGFF 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 122 PWRTVAENVGFG--LELAGM--------PEAERKLrVGEQLELVNLtKWAG--RKVNELSGGMQQRVGLARAFATGAPIL 189
Cdd:PRK09700 354 PNFSIAQNMAISrsLKDGGYkgamglfhEVDEQRT-AENQRELLAL-KCHSvnQNITELSGGNQQKVLISKWLCCCPEVI 431
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2087760999 190 LMDEPFSALDPLIRTrlqdELLEFQRRLK---KTILFVSHDLDEAFRIGNRIAIMEGGRIIQ 248
Cdd:PRK09700 432 IFDEPTRGIDVGAKA----EIYKVMRQLAddgKVILMVSSELPEIITVCDRIAVFCEGRLTQ 489
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
43-284 |
4.09e-13 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 68.96 E-value: 4.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 43 VADASLTIEEGEILVLMGLSGSGKSTLLRAVNG-LAPvvrgdvavstTTGPV-----NPYRcNAKALRdlrtHTVSMVFQ 116
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGiLVP----------TSGEVrvlgyVPFK-RRKEFA----RRIGVVFG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 117 QFALLPWR-TVAENvgFGL--ELAGMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDE 193
Cdd:COG4586 103 QRSQLWWDlPAIDS--FRLlkAIYRIPDAEYKKRLDELVELLDLGELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDE 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 194 PFSALDPLIRTRLQDELLEFQRRLKKTILFVSHDLDEAFRIGNRIAIMEGGRIIQCGTPHDIVKN--PADQYVADFVQNL 271
Cdd:COG4586 181 PTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEALCDRVIVIDHGRIIYDGSLEELKERfgPYKTIVLELAEPV 260
|
250
....*....|...
gi 2087760999 272 NPINMLTAADVMQ 284
Cdd:COG4586 261 PPLELPRGGEVIE 273
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
47-316 |
6.90e-13 |
|
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: 69.97 E-value: 6.90e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 47 SLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTTtgpvnpyrcnakalrdlrthtVSMVFQQfALLPWRTV 126
Cdd:TIGR00957 658 TFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS---------------------VAYVPQQ-AWIQNDSL 715
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 127 AENVGFGLEL------------AGMPEAErKLRVGEQLELvnltkwaGRKVNELSGGMQQRVGLARAFATGAPILLMDEP 194
Cdd:TIGR00957 716 RENILFGKALnekyyqqvleacALLPDLE-ILPSGDRTEI-------GEKGVNLSGGQKQRVSLARAVYSNADIYLFDDP 787
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 195 FSALDPLIRTRLQDELLEFQRRLK-KTILFVSHDLDEAFRIgNRIAIMEGGRIIQCGTPHDIVKNpaDQYVADFVQNLnp 273
Cdd:TIGR00957 788 LSAVDAHVGKHIFEHVIGPEGVLKnKTRILVTHGISYLPQV-DVIIVMSGGKISEMGSYQELLQR--DGAFAEFLRTY-- 862
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 2087760999 274 inmltaADVMQPGLGQTAAGMSVSATARAATPLID---VLDALARQ 316
Cdd:TIGR00957 863 ------APDEQQGHLEDSWTALVSGEGKEAKLIENgmlVTDVVGKQ 902
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
45-252 |
7.18e-13 |
|
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: 67.13 E-value: 7.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 45 DASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVA---VSTTTGPvnpyrcnakaLRDLRTHtVSMVFQQFALL 121
Cdd:cd03244 22 NISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILidgVDISKIG----------LHDLRSR-ISIIPQDPVLF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 122 PwRTVAENVG-FG----------LELAGMPEAERKLRVGEQLELvnltkwAGRKVNeLSGGMQQRVGLARAFATGAPILL 190
Cdd:cd03244 91 S-GTIRSNLDpFGeysdeelwqaLERVGLKEFVESLPGGLDTVV------EEGGEN-LSVGQRQLLCLARALLRKSKILV 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2087760999 191 MDEPFSALDP--------LIRTRLQDellefqrrlkKTILFVSH------DLDeafrignRIAIMEGGRIIQCGTP 252
Cdd:cd03244 163 LDEATASVDPetdaliqkTIREAFKD----------CTVLTIAHrldtiiDSD-------RILVLDKGRVVEFDSP 221
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
45-259 |
1.20e-12 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 68.98 E-value: 1.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 45 DASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTTtgPVNPYRCnakalRDLRTHTVSMvfQQFALLPWR 124
Cdd:TIGR00958 499 GLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGV--PLVQYDH-----HYLHRQVALV--GQEPVLFSG 569
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 125 TVAENVGFGLELAGMPEAERKLRVGEQLELV-NLTKW----AGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALD 199
Cdd:TIGR00958 570 SVRENIAYGLTDTPDEEIMAAAKAANAHDFImEFPNGydteVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALD 649
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 200 PLIRTRLQdELLEFQRRlkkTILFVSHDLDEAfRIGNRIAIMEGGRIIQCGTPHDIVKNP 259
Cdd:TIGR00958 650 AECEQLLQ-ESRSRASR---TVLLIAHRLSTV-ERADQILVLKKGSVVEMGTHKQLMEDQ 704
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
47-255 |
1.93e-12 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 68.15 E-value: 1.93e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 47 SLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVS-TTTGPVNPyrcnAKAlrdlrtHT--VSMVFQQFALLPW 123
Cdd:PRK15439 31 DFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGgNPCARLTP----AKA------HQlgIYLVPQEPLLFPN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 124 RTVAENVGFGleLAGMPEAERKLrvgEQL--EL---VNLTKWAGrkvnELSGGMQQRVGLARAFATGAPILLMDEPFSAL 198
Cdd:PRK15439 101 LSVKENILFG--LPKRQASMQKM---KQLlaALgcqLDLDSSAG----SLEVADRQIVEILRGLMRDSRILILDEPTASL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2087760999 199 DPLIRTRLQDELLEFQrRLKKTILFVSHDLDEAFRIGNRIAIMEGGRIIQCGTPHDI 255
Cdd:PRK15439 172 TPAETERLFSRIRELL-AQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTADL 227
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
29-260 |
2.13e-12 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 66.06 E-value: 2.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 29 SRDEIGAATGLVLGVADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVavsTTTGPVNPYRCNAKALRDlrt 108
Cdd:PRK11614 7 SFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRI---VFDGKDITDWQTAKIMRE--- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 109 hTVSMVFQQFALLPWRTVAENVGFGLELAGMPEAERKLRVGEQLeLVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPI 188
Cdd:PRK11614 81 -AVAIVPEGRRVFSRMTVEENLAMGGFFAERDQFQERIKWVYEL-FPRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2087760999 189 LLMDEPFSALDPLIRTRLQDELLEFqRRLKKTILFVSHDLDEAFRIGNRIAIMEGGRIIQCGTPHDIVKNPA 260
Cdd:PRK11614 159 LLLDEPSLGLAPIIIQQIFDTIEQL-REQGMTIFLVEQNANQALKLADRGYVLENGHVVLEDTGDALLANEA 229
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
50-200 |
2.14e-12 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 65.64 E-value: 2.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 50 IEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTTTgpvnpyrcnakALRDLRTHTVSMVFQQFALLPWRTVAEN 129
Cdd:PRK13543 34 VDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKT-----------ATRGDRSRFMAYLGHLPGLKADLSTLEN 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2087760999 130 VGFgleLAGMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDP 200
Cdd:PRK13543 103 LHF---LCGLHGRRAKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDL 170
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1-227 |
2.40e-12 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 68.05 E-value: 2.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 1 MTAVNFNNVSIIFGDRPetalaMVDqgksrdeigaatglvlgvaDASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAP-- 78
Cdd:PRK11147 1 MSLISIHGAWLSFSDAP-----LLD-------------------NAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLld 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 79 ----VVRGDVAVS--------TTTGPVNPYRCN-----AKALRdlRTHTVSmvfQQFALLPWRTVaenvgfgleLAGMPE 141
Cdd:PRK11147 57 dgriIYEQDLIVArlqqdpprNVEGTVYDFVAEgieeqAEYLK--RYHDIS---HLVETDPSEKN---------LNELAK 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 142 AERKL----------RVGEQLELVNLTkwAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDPLIRTRLQDELL 211
Cdd:PRK11147 123 LQEQLdhhnlwqlenRINEVLAQLGLD--PDAALSSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLK 200
|
250
....*....|....*.
gi 2087760999 212 EFQrrlkKTILFVSHD 227
Cdd:PRK11147 201 TFQ----GSIIFISHD 212
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
130-250 |
3.76e-12 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 66.68 E-value: 3.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 130 VGFGLELAgmpEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDPLIRTRLQDE 209
Cdd:NF000106 110 IGR*LDLS---RKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDE 186
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 2087760999 210 LLEFQRRlKKTILFVSHDLDEAFRIGNRIAIMEGGRIIQCG 250
Cdd:NF000106 187 VRSMVRD-GATVLLTTQYMEEAEQLAHELTVIDRGRVIADG 226
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
43-293 |
6.84e-12 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 66.92 E-value: 6.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 43 VADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAP-------VVRGDVAVStttgPVNPYRCNAkalrdlrthtvsmvf 115
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELShaetssvVIRGSVAYV----PQVSWIFNA--------------- 693
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 116 qqfallpwrTVAENVGFGLELagmpEAERKLR------VGEQLELV---NLTKWAGRKVNeLSGGMQQRVGLARAFATGA 186
Cdd:PLN03232 694 ---------TVRENILFGSDF----ESERYWRaidvtaLQHDLDLLpgrDLTEIGERGVN-ISGGQKQRVSMARAVYSNS 759
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 187 PILLMDEPFSALDPLIRTRLQDELLEFQRRlKKTILFVSHDLdEAFRIGNRIAIMEGGRIIQCGTPHDIVKN-------- 258
Cdd:PLN03232 760 DIYIFDDPLSALDAHVAHQVFDSCMKDELK-GKTRVLVTNQL-HFLPLMDRIILVSEGMIKEEGTFAELSKSgslfkklm 837
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 2087760999 259 ------PADQYVADFVQNLNPINMLTAADVMQPGLGQTAAG 293
Cdd:PLN03232 838 enagkmDATQEVNTNDENILKLGPTVTIDVSERNLGSTKQG 878
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
24-246 |
7.22e-12 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 66.18 E-value: 7.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 24 VDQGKSRDEIGAATGLvlGVADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTTtgPVNPyRCNAKAL 103
Cdd:PRK10762 251 KAPGEVRLKVDNLSGP--GVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGH--EVVT-RSPQDGL 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 104 RDLRTHtVSMVFQQFALLPWRTVAENVG------FGLELAGMPEAERKLRVGEQLELVNL-TKWAGRKVNELSGGMQQRV 176
Cdd:PRK10762 326 ANGIVY-ISEDRKRDGLVLGMSVKENMSltalryFSRAGGSLKHADEQQAVSDFIRLFNIkTPSMEQAIGLLSGGNQQKV 404
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2087760999 177 GLARAFATGAPILLMDEPfsaldplirTRLQD-----ELLEFQRRLKK---TILFVSHDLDEAFRIGNRIAIMEGGRI 246
Cdd:PRK10762 405 AIARGLMTRPKVLILDEP---------TRGVDvgakkEIYQLINQFKAeglSIILVSSEMPEVLGMSDRILVMHEGRI 473
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-228 |
1.35e-11 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 63.98 E-value: 1.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 1 MTAVNFNNVSIIFGDRPetalamvdqgksrdeigaatglVLgvADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLapvv 80
Cdd:PRK09544 2 TSLVSLENVSVSFGQRR----------------------VL--SDVSLELKPGKILTLLGPNGAGKSTLVRVVLGL---- 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 81 rgdvaVSTTTGPVNpyrcNAKALRdlrthtVSMVFQQFALLPwrTVAENVGFGLELAGmpeAERKLRVGEQLELVNLTKW 160
Cdd:PRK09544 54 -----VAPDEGVIK----RNGKLR------IGYVPQKLYLDT--TLPLTVNRFLRLRP---GTKKEDILPALKRVQAGHL 113
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2087760999 161 AGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDPLIRTRLQDELLEFQRRLKKTILFVSHDL 228
Cdd:PRK09544 114 IDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDL 181
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
45-247 |
2.59e-11 |
|
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: 62.28 E-value: 2.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 45 DASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPV---VRGDVAVSTTTGPVNPYRCnakalrdlrTHTVSMVFQQ---F 118
Cdd:cd03233 25 DFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGnvsVEGDIHYNGIPYKEFAEKY---------PGEIIYVSEEdvhF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 119 ALLpwrTVAENVGFGLELAGmpeaerklrvgeqlelvnltkwaGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSAL 198
Cdd:cd03233 96 PTL---TVRETLDFALRCKG-----------------------NEFVRGISGGERKRVSIAEALVSRASVLCWDNSTRGL 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2087760999 199 DPLIRTRLQDELLEFQRRLKKTILF-VSHDLDEAFRIGNRIAIMEGGRII 247
Cdd:cd03233 150 DSSTALEILKCIRTMADVLKTTTFVsLYQASDEIYDLFDKVLVLYEGRQI 199
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
45-259 |
1.01e-10 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 62.81 E-value: 1.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 45 DASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVavstttgpvnpyRCNAKALRDLRTHTVS---MVFQQFALL 121
Cdd:PRK10789 333 NVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDI------------RFHDIPLTKLQLDSWRsrlAVVSQTPFL 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 122 PWRTVAENVGFGLELAGMPEAERKLRVGEQLE-LVNLTKWAGRKVNE----LSGGMQQRVGLARAFATGAPILLMDEPFS 196
Cdd:PRK10789 401 FSDTVANNIALGRPDATQQEIEHVARLASVHDdILRLPQGYDTEVGErgvmLSGGQKQRISIARALLLNAEILILDDALS 480
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2087760999 197 ALDplirTRLQDELLEFQRRL--KKTILFVSHDLdEAFRIGNRIAIMEGGRIIQCGTPHDIVKNP 259
Cdd:PRK10789 481 AVD----GRTEHQILHNLRQWgeGRTVIISAHRL-SALTEASEILVMQHGHIAQRGNHDQLAQQS 540
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
49-243 |
1.09e-10 |
|
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: 61.27 E-value: 1.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 49 TIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTTTGPVNPYRCNAK---ALRDLrthtVSMVFQQFALLP-WR 124
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSYKPQYIKADyegTVRDL----LSSITKDFYTHPyFK 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 125 TvaenvgfglelagmpEAERKLRVGEQLElvnltkwagRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDPLIRT 204
Cdd:cd03237 97 T---------------EIAKPLQIEQILD---------REVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRL 152
|
170 180 190
....*....|....*....|....*....|....*....
gi 2087760999 205 RLQDELLEFQRRLKKTILFVSHDLDEAFRIGNRIAIMEG 243
Cdd:cd03237 153 MASKVIRRFAENNEKTAFVVEHDIIMIDYLADRLIVFEG 191
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
47-276 |
1.73e-10 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 62.22 E-value: 1.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 47 SLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTTTgpvnpyrcnakalrdlrthtvSMVFQQFALLPWRTV 126
Cdd:PRK13545 44 SFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSA---------------------ALIAISSGLNGQLTG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 127 AENVGFGLELAGMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDPLIRTRL 206
Cdd:PRK13545 103 IENIELKGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKC 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 207 QDELLEFQRRlKKTILFVSHDLDEAFRIGNRIAIMEGGRIIQCGTPHDIVknpaDQYvADFVQNLNPINM 276
Cdd:PRK13545 183 LDKMNEFKEQ-GKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEVV----DHY-DEFLKKYNQMSV 246
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
48-258 |
1.80e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 62.45 E-value: 1.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 48 LTIEEGEILVLMGLSGSGKSTLLRAVNG-LAPVVRGDVAVSTTTGPVNpyrcnakalrdlrthTVSMVFQQfallpwrTV 126
Cdd:PLN03130 638 LDVPVGSLVAIVGSTGEGKTSLISAMLGeLPPRSDASVVIRGTVAYVP---------------QVSWIFNA-------TV 695
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 127 AENVGFGLELAGmPEAERKLRVGE---QLELV---NLTKWAGRKVNeLSGGMQQRVGLARAFATGAPILLMDEPFSALDP 200
Cdd:PLN03130 696 RDNILFGSPFDP-ERYERAIDVTAlqhDLDLLpggDLTEIGERGVN-ISGGQKQRVSMARAVYSNSDVYIFDDPLSALDA 773
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2087760999 201 LIRTRLQDELLEFQRRlKKTILFVSHDLDEAFRIgNRIAIMEGGRIIQCGTPHDIVKN 258
Cdd:PLN03130 774 HVGRQVFDKCIKDELR-GKTRVLVTNQLHFLSQV-DRIILVHEGMIKEEGTYEELSNN 829
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
45-254 |
2.21e-10 |
|
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: 61.76 E-value: 2.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 45 DASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVStttGpvnpyrcnakalRDLRTHTVSMVFQQFALLPWR 124
Cdd:COG5265 376 GVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILID---G------------QDIRDVTQASLRAAIGIVPQD 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 125 TV------AENVGFGLELAGMPEAERKLR------------------VGEQlelvnltkwaGRKvneLSGGMQQRVGLAR 180
Cdd:COG5265 441 TVlfndtiAYNIAYGRPDASEEEVEAAARaaqihdfieslpdgydtrVGER----------GLK---LSGGEKQRVAIAR 507
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 181 AFATGAPILLMDEPFSALDPLIRTRLQDELLEFQRRlkKTILFVSH------DLDEafrignrIAIMEGGRIIQCGTpHD 254
Cdd:COG5265 508 TLLKNPPILIFDEATSALDSRTERAIQAALREVARG--RTTLVIAHrlstivDADE-------ILVLEAGRIVERGT-HA 577
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
47-247 |
2.85e-10 |
|
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: 61.35 E-value: 2.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 47 SLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTTtgPVnpyrcNAKALRDLRTHtVSMVFQQFALLPwrtv 126
Cdd:COG4615 352 DLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQ--PV-----TADNREAYRQL-FSAVFSDFHLFD---- 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 127 aenvgfglELAGMPEAERKLRVGEQLELVNLtkwaGRKV---------NELSGGMQQRVGLARAFATGAPILLMDEPFSA 197
Cdd:COG4615 420 --------RLLGLDGEADPARARELLERLEL----DHKVsvedgrfstTDLSQGQRKRLALLVALLEDRPILVFDEWAAD 487
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2087760999 198 LDPLIRTRLQDELLEFQRRLKKTILFVSHDlDEAFRIGNRIAIMEGGRII 247
Cdd:COG4615 488 QDPEFRRVFYTELLPELKARGKTVIAISHD-DRYFDLADRVLKMDYGKLV 536
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
45-252 |
4.87e-10 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 58.31 E-value: 4.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 45 DASLTIEEGEILVLMGLSGSGKSTLLRAVNGLA--PVVRGDVAVstttgpvnpyrcNAKALRDLRTHtvsmvfqqfallp 122
Cdd:cd03217 18 GVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILF------------KGEDITDLPPE------------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 123 wrtvaENVGFGLELA-GMPEAERKLRVGEQLelvnltkwagRKVNE-LSGGMQQRVGLARAFATGAPILLMDEPFSALDp 200
Cdd:cd03217 73 -----ERARLGIFLAfQYPPEIPGVKNADFL----------RYVNEgFSGGEKKRNEILQLLLLEPDLAILDEPDSGLD- 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2087760999 201 LIRTRLQDELLEFQRRLKKTILFVSHD---LDeaFRIGNRIAIMEGGRIIQCGTP 252
Cdd:cd03217 137 IDALRLVAEVINKLREEGKSVLIITHYqrlLD--YIKPDRVHVLYDGRIVKSGDK 189
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
38-255 |
9.39e-10 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 60.14 E-value: 9.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 38 GLVLGVADASLTIEEGEILVLMGLSGSGKSTLL------RAV-NGLAPVVRGDVAvstttgpvnpyrcNAKALRDLRTHT 110
Cdd:NF033858 12 GKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLsliagaRKIqQGRVEVLGGDMA-------------DARHRRAVCPRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 111 VSMVfQQFA--LLPWRTVAENVGFGLELAGMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPI 188
Cdd:NF033858 79 AYMP-QGLGknLYPTLSVFENLDFFGRLFGQDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCALIHDPDL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 189 LLMDEPFSALDPLIRTR---LQDELLefQRRLKKTILFVSHDLDEAFRIgNRIAIMEGGRIIQCGTPHDI 255
Cdd:NF033858 158 LILDEPTTGVDPLSRRQfweLIDRIR--AERPGMSVLVATAYMEEAERF-DWLVAMDAGRVLATGTPAEL 224
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
51-228 |
1.44e-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: 1.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 51 EEGEILVLMGLSGSGKSTLLRAVNG-LAPVVRGDVAVSTTTGPVNPYRCNA--KALRDLRTHTVSMVF--QQFALLPwRT 125
Cdd:cd03236 24 REGQVLGLVGPNGIGKSTALKILAGkLKPNLGKFDDPPDWDEILDEFRGSElqNYFTKLLEGDVKVIVkpQYVDLIP-KA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 126 VAENVGFGLELAGmpEAERKLRVGEQLELVNLTKwagRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDplIRTR 205
Cdd:cd03236 103 VKGKVGELLKKKD--ERGKLDELVDQLELRHVLD---RNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLD--IKQR 175
|
170 180
....*....|....*....|....*.
gi 2087760999 206 LQDELLefQRRL---KKTILFVSHDL 228
Cdd:cd03236 176 LNAARL--IRELaedDNYVLVVEHDL 199
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
47-226 |
1.45e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 57.27 E-value: 1.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 47 SLTIEEGEILVLMGLSGSGKSTLLRAVNGLapvvrgdvaVSTTTGPVNPYRCNAKalRDLRTHTVSMVF--QQFALLPWR 124
Cdd:PRK13540 21 SFHLPAGGLLHLKGSNGAGKTTLLKLIAGL---------LNPEKGEILFERQSIK--KDLCTYQKQLCFvgHRSGINPYL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 125 TVAENVGFGLELAGMpeaerKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDPL--- 201
Cdd:PRK13540 90 TLRENCLYDIHFSPG-----AVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELsll 164
|
170 180
....*....|....*....|....*.
gi 2087760999 202 -IRTRLQDellefQRRLKKTILFVSH 226
Cdd:PRK13540 165 tIITKIQE-----HRAKGGAVLLTSH 185
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
42-246 |
2.76e-09 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 58.14 E-value: 2.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 42 GVADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVS-TTTGPVNPYRCNAKALRDL-RTHTVSMVFQQfA 119
Cdd:PRK15439 278 GFRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNgKEINALSTAQRLARGLVYLpEDRQSSGLYLD-A 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 120 LLPWRTVA---ENVGFGLElagmPEAERklRVGEQLELVNLTKWAG--RKVNELSGGMQQRVGLARAFATGAPILLMDEP 194
Cdd:PRK15439 357 PLAWNVCAlthNRRGFWIK----PAREN--AVLERYRRALNIKFNHaeQAARTLSGGNQQKVLIAKCLEASPQLLIVDEP 430
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2087760999 195 FSALDPLIRTRLQDELlefqRRLKK---TILFVSHDLDEAFRIGNRIAIMEGGRI 246
Cdd:PRK15439 431 TRGVDVSARNDIYQLI----RSIAAqnvAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
45-259 |
1.79e-08 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 56.33 E-value: 1.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 45 DASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVavstttgpvnpyrcnakalrdLRTHTVSMVFQQfallPW- 123
Cdd:PTZ00243 678 DVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV---------------------WAERSIAYVPQQ----AWi 732
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 124 --RTVAENVGFGLElagmpeaERKLRVGE-----QLE--LVNL-----TKWAGRKVNeLSGGMQQRVGLARAFATGAPIL 189
Cdd:PTZ00243 733 mnATVRGNILFFDE-------EDAARLADavrvsQLEadLAQLgggleTEIGEKGVN-LSGGQKARVSLARAVYANRDVY 804
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2087760999 190 LMDEPFSALDPLIRTRLQDELleFQRRLK-KTILFVSHDLDEAFRiGNRIAIMEGGRIIQCGTPHDIVKNP 259
Cdd:PTZ00243 805 LLDDPLSALDAHVGERVVEEC--FLGALAgKTRVLATHQVHVVPR-ADYVVALGDGRVEFSGSSADFMRTS 872
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
45-243 |
1.93e-08 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 55.71 E-value: 1.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 45 DASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTTTgpvnpyrcnakalrdlrthTVSMVFQQF-ALLPW 123
Cdd:TIGR03719 340 DLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETV-------------------KLAYVDQSRdALDPN 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 124 RTVAENVGFGLELagmpeaerkLRVGEQLelVNLTKWAGR----------KVNELSGGMQQRVGLARAFATGAPILLMDE 193
Cdd:TIGR03719 401 KTVWEEISGGLDI---------IKLGKRE--IPSRAYVGRfnfkgsdqqkKVGQLSGGERNRVHLAKTLKSGGNVLLLDE 469
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2087760999 194 PFSALDplIRT--RLQDELLEFqrrlKKTILFVSHD---LDeafRIGNRIAIMEG 243
Cdd:TIGR03719 470 PTNDLD--VETlrALEEALLNF----AGCAVVISHDrwfLD---RIATHILAFEG 515
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
53-254 |
3.13e-08 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 55.27 E-value: 3.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 53 GEILVLMGLSGSGKSTLLRAvnglapvVRGDVAVSTTTGPV--NPYRCNAKALRdlRThtvSMVFQQFALLPWRTVAENV 130
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNA-------LAGRIQGNNFTGTIlaNNRKPTKQILK--RT---GFVTQDDILYPHLTVRETL 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 131 GFgLELAGMPEA---ERKLRVGEQL--ELvNLTKWAGRKVNE-----LSGGMQQRVGLARAFATGAPILLMDEPFSALDP 200
Cdd:PLN03211 162 VF-CSLLRLPKSltkQEKILVAESVisEL-GLTKCENTIIGNsfirgISGGERKRVSIAHEMLINPSLLILDEPTSGLDA 239
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2087760999 201 LIRTRLQDELLEFQRRLKKTILFVSHDLDEAFRIGNRIAIMEGGRIIQCGTPHD 254
Cdd:PLN03211 240 TAAYRLVLTLGSLAQKGKTIVTSMHQPSSRVYQMFDSVLVLSEGRCLFFGKGSD 293
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
103-254 |
6.79e-08 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 54.26 E-value: 6.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 103 LRDLRtHTVSMVFQQFALLPwRTVAENVGFGLELAGMPEAERKLRVGEQLELVNL--TKW---AGRKVNELSGGMQQRVG 177
Cdd:PTZ00265 1291 LKDLR-NLFSIVSQEPMLFN-MSIYENIKFGKEDATREDVKRACKFAAIDEFIESlpNKYdtnVGPYGKSLSGGQKQRIA 1368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 178 LARAFATGAPILLMDEPFSALDPLIRTRLQDELLEFQRRLKKTILFVSHDLDEAFRiGNRIAIMEG----GRIIQCGTPH 253
Cdd:PTZ00265 1369 IARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASIKR-SDKIVVFNNpdrtGSFVQAHGTH 1447
|
.
gi 2087760999 254 D 254
Cdd:PTZ00265 1448 E 1448
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
43-246 |
7.56e-08 |
|
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: 53.68 E-value: 7.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 43 VADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPvVRGDVAVSTTTGPVNPYRCnAKALRdlrtHTVSMV---FQQFA 119
Cdd:TIGR02633 276 VDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYP-GKFEGNVFINGKPVDIRNP-AQAIR----AGIAMVpedRKRHG 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 120 LLPWRTVAENVgfglELAGMPEAERKLRVGEQLELVNLTKWAGR----------KVNELSGGMQQRVGLARAFATGAPIL 189
Cdd:TIGR02633 350 IVPILGVGKNI----TLSVLKSFCFKMRIDAAAELQIIGSAIQRlkvktaspflPIGRLSGGNQQKAVLAKMLLTNPRVL 425
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2087760999 190 LMDEPFSALDPLIRTRLQDELLEFQRRlKKTILFVSHDLDEAFRIGNRIAIMEGGRI 246
Cdd:TIGR02633 426 ILDEPTRGVDVGAKYEIYKLINQLAQE-GVAIIVVSSELAEVLGLSDRVLVIGEGKL 481
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
38-259 |
1.03e-07 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 54.01 E-value: 1.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 38 GLVLGVADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAvstttgpVNPYRCNAKALRDLRthtvsmvfQQ 117
Cdd:PTZ00243 1321 GLPLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIR-------VNGREIGAYGLRELR--------RQ 1385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 118 FALLPWR------TVAENVGFGLELAgmpEAErklrVGEQLELVNLTkwaGRKVNE--------LSGGMQQRVG------ 177
Cdd:PTZ00243 1386 FSMIPQDpvlfdgTVRQNVDPFLEAS---SAE----VWAALELVGLR---ERVASEsegidsrvLEGGSNYSVGqrqlmc 1455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 178 LARA-FATGAPILLMDEPFSALDPLIRTRLQDELLE-FQrrlKKTILFVSHDLDEAFRIgNRIAIMEGGRIIQCGTPHDI 255
Cdd:PTZ00243 1456 MARAlLKKGSGFILMDEATANIDPALDRQIQATVMSaFS---AYTVITIAHRLHTVAQY-DKIIVMDHGAVAEMGSPREL 1531
|
....
gi 2087760999 256 VKNP 259
Cdd:PTZ00243 1532 VMNR 1535
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
45-251 |
1.08e-07 |
|
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: 52.55 E-value: 1.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 45 DASLTIEEGEILVLMGLSGSGKSTLLRAVNG-LAPvvrgdvavstTTGPVNpyrcnakalrdlrtHTVSMVF-QQFALLP 122
Cdd:cd03291 55 NINLKIEKGEMLAITGSTGSGKTSLLMLILGeLEP----------SEGKIK--------------HSGRISFsSQFSWIM 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 123 WRTVAENVGFGLELagmpEAERKLRVGE--QLElVNLTKWA-------GRKVNELSGGMQQRVGLARAFATGAPILLMDE 193
Cdd:cd03291 111 PGTIKENIIFGVSY----DEYRYKSVVKacQLE-EDITKFPekdntvlGEGGITLSGGQRARISLARAVYKDADLYLLDS 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2087760999 194 PFSALDPLIRTRLQDELLeFQRRLKKTILFVSHDLdEAFRIGNRIAIMEGGRIIQCGT 251
Cdd:cd03291 186 PFGYLDVFTEKEIFESCV-CKLMANKTRILVTSKM-EHLKKADKILILHEGSSYFYGT 241
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
49-228 |
1.79e-07 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 52.86 E-value: 1.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 49 TIEEGEILVLMGLSGSGKSTLLRAVNG-LAPVVrGDVAVSTTTGPV-NPYRCNA-----KALRD--LRthtVSMVFQQFA 119
Cdd:COG1245 95 VPKKGKVTGILGPNGIGKSTALKILSGeLKPNL-GDYDEEPSWDEVlKRFRGTElqdyfKKLANgeIK---VAHKPQYVD 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 120 LLPwRTVAENVGFGLELAGmpeaERKlRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALD 199
Cdd:COG1245 171 LIP-KVFKGTVRELLEKVD----ERG-KLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLD 244
|
170 180 190
....*....|....*....|....*....|....
gi 2087760999 200 plIRTRLQ-----DELLEfqrrLKKTILFVSHDL 228
Cdd:COG1245 245 --IYQRLNvarliRELAE----EGKYVLVVEHDL 272
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
150-228 |
2.13e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 52.50 E-value: 2.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 150 EQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDplIRTRLQ-----DELLEfqrrlKKTILFV 224
Cdd:PRK13409 195 EVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLD--IRQRLNvarliRELAE-----GKYVLVV 267
|
....
gi 2087760999 225 SHDL 228
Cdd:PRK13409 268 EHDL 271
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
167-243 |
1.12e-06 |
|
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: 48.34 E-value: 1.12e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2087760999 167 ELSGGMQQRVGLARAFATGAPILLMDEPFSALDPLIRTRLQDELLEFQRRLKKTILFVSHDLDEAFRIGNRIAIMEG 243
Cdd:cd03222 71 DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTALVVEHDLAVLDYLSDRIHVFEG 147
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
45-199 |
1.16e-06 |
|
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: 50.68 E-value: 1.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 45 DASLTIEEGEILVLMGLSGSGKSTLLRAVNG-LAPvvrgdvavstTTGPVNpyrcnakalrdlrtHTVSMVFQ-QFALLP 122
Cdd:TIGR01271 444 NISFKLEKGQLLAVAGSTGSGKSSLLMMIMGeLEP----------SEGKIK--------------HSGRISFSpQTSWIM 499
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 123 WRTVAENVGFGLELagmpEAERKLRVGE--QLElVNLTKWA-------GRKVNELSGGMQQRVGLARAFATGAPILLMDE 193
Cdd:TIGR01271 500 PGTIKDNIIFGLSY----DEYRYTSVIKacQLE-EDIALFPekdktvlGEGGITLSGGQRARISLARAVYKDADLYLLDS 574
|
....*.
gi 2087760999 194 PFSALD 199
Cdd:TIGR01271 575 PFTHLD 580
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
43-246 |
1.25e-06 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 49.93 E-value: 1.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 43 VADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAP-VVRGDVAVSTTtgPVNPYRCnAKALRdlrtHTVSMV---FQQF 118
Cdd:PRK13549 278 VDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPgRWEGEIFIDGK--PVKIRNP-QQAIA----QGIAMVpedRKRD 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 119 ALLPWRTVAENVgfglELAGMPEAERKLRVGEQLELVNLTKWAGR----------KVNELSGGMQQRVGLARAFATGAPI 188
Cdd:PRK13549 351 GIVPVMGVGKNI----TLAALDRFTGGSRIDDAAELKTILESIQRlkvktaspelAIARLSGGNQQKAVLAKCLLLNPKI 426
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2087760999 189 LLMDEPfsaldplirTRLQD-----ELLEFQRRLKK---TILFVSHDLDEAFRIGNRIAIMEGGRI 246
Cdd:PRK13549 427 LILDEP---------TRGIDvgakyEIYKLINQLVQqgvAIIVISSELPEVLGLSDRVLVMHEGKL 483
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
45-229 |
1.54e-06 |
|
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: 47.70 E-value: 1.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 45 DASLTIEEGEILVLMGLSGSGKSTLLRAvnGLAPVVRGDVAVSTTTGPVNPyrcnakalrdlrthtVSMVFQQFALLpwr 124
Cdd:cd03238 13 NLDVSIPLNVLVVVTGVSGSGKSTLVNE--GLYASGKARLISFLPKFSRNK---------------LIFIDQLQFLI--- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 125 tvaeNVGFG-LELagmpeaerklrvgeqlelvnltkwaGRKVNELSGGMQQRVGLARAFATGAP--ILLMDEPFSALDPL 201
Cdd:cd03238 73 ----DVGLGyLTL-------------------------GQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQ 123
|
170 180
....*....|....*....|....*...
gi 2087760999 202 IRTRLQDELLEFqRRLKKTILFVSHDLD 229
Cdd:cd03238 124 DINQLLEVIKGL-IDLGNTVILIEHNLD 150
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
43-227 |
1.58e-06 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 49.95 E-value: 1.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 43 VADASLTIEEGEILVLMGLSGSGKSTLLRAVNG-LAPvvrgdvavstTTGPVnpyRCNakalrdlrTHTVSMVFQQF--A 119
Cdd:PRK11147 335 VKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGqLQA----------DSGRI---HCG--------TKLEVAYFDQHraE 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 120 LLPWRTVAENVgfglelagmpeAErklrvGEQLELVNltkwaGRK--------------------VNELSGGMQQRVGLA 179
Cdd:PRK11147 394 LDPEKTVMDNL-----------AE-----GKQEVMVN-----GRPrhvlgylqdflfhpkramtpVKALSGGERNRLLLA 452
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2087760999 180 RAFATGAPILLMDEPFSALDplIRT-RLQDELL-EFQrrlkKTILFVSHD 227
Cdd:PRK11147 453 RLFLKPSNLLILDEPTNDLD--VETlELLEELLdSYQ----GTVLLVSHD 496
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
47-248 |
1.64e-06 |
|
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: 49.08 E-value: 1.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 47 SLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVvRGDV---AVSTTTGPVNPYRcNAKALRDLRTHTVSMVFQQfALLP- 122
Cdd:cd03289 24 SFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNT-EGDIqidGVSWNSVPLQKWR-KAFGVIPQKVFIFSGTFRK-NLDPy 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 123 --------WRtVAENVGFGLELAGMPEaerklrvgeQLELVNLTkwaGRKVneLSGGMQQRVGLARAFATGAPILLMDEP 194
Cdd:cd03289 101 gkwsdeeiWK-VAEEVGLKSVIEQFPG---------QLDFVLVD---GGCV--LSHGHKQLMCLARSVLSKAKILLLDEP 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2087760999 195 FSALDPL----IRTRLQdellefQRRLKKTILFVSHDLdEAFRIGNRIAIMEGGRIIQ 248
Cdd:cd03289 166 SAHLDPItyqvIRKTLK------QAFADCTVILSEHRI-EAMLECQRFLVIEENKVRQ 216
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
58-231 |
1.89e-06 |
|
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: 49.55 E-value: 1.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 58 LMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTTTgpvnpyrcnakalrdlrthTVSMVFQQFALLPWRTVAENVGFGL-EL 136
Cdd:TIGR03719 36 VLGLNGAGKSTLLRIMAGVDKDFNGEARPQPGI-------------------KVGYLPQEPQLDPTKTVRENVEEGVaEI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 137 AGM-------------PEAERKLRVGEQLELVNLTKWAG---------------------RKVNELSGGMQQRVGLARAF 182
Cdd:TIGR03719 97 KDAldrfneisakyaePDADFDKLAAEQAELQEIIDAADawdldsqleiamdalrcppwdADVTKLSGGERRRVALCRLL 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2087760999 183 ATGAPILLMDEPFSALDPLIRTRLQDELLEFqrrlKKTILFVSHD---LDEA 231
Cdd:TIGR03719 177 LSKPDMLLLDEPTNHLDAESVAWLERHLQEY----PGTVVAVTHDryfLDNV 224
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
45-250 |
2.21e-06 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 48.02 E-value: 2.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 45 DASLTIEEGEILVLMGLSGSGKSTL----------LRAVNGLAPVVRG--------DV----------AVSTTTGPVNPy 96
Cdd:cd03270 13 NVDVDIPRNKLVVITGVSGSGKSSLafdtiyaegqRRYVESLSAYARQflgqmdkpDVdsieglspaiAIDQKTTSRNP- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 97 rcnakalrdlRTH--TVSMVFQQFALLPWRtvaenVGFGLELAGMpeaerkLRVGeqLELVNLTkwagRKVNELSGGMQQ 174
Cdd:cd03270 92 ----------RSTvgTVTEIYDYLRLLFAR-----VGIRERLGFL------VDVG--LGYLTLS----RSAPTLSGGEAQ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 175 RVGLARAFATG--APILLMDEPFSALDPlirtRLQDELLEFQRRLKK---TILFVSHDLDeAFRIGNRI------AIMEG 243
Cdd:cd03270 145 RIRLATQIGSGltGVLYVLDEPSIGLHP----RDNDRLIETLKRLRDlgnTVLVVEHDED-TIRAADHVidigpgAGVHG 219
|
....*..
gi 2087760999 244 GRIIQCG 250
Cdd:cd03270 220 GEIVAQG 226
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
48-251 |
2.66e-06 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 48.10 E-value: 2.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 48 LTIEEGEILVLMGLSGSGKSTllravngLAPVVRGDVAVSTTTGPVnpyRCNAKALRDL----RTHT-VSMVFQQFALLP 122
Cdd:CHL00131 28 LSINKGEIHAIMGPNGSGKST-------LSKVIAGHPAYKILEGDI---LFKGESILDLepeeRAHLgIFLAFQYPIEIP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 123 WRTvaeNVGFgLELA--------GMPEAErKLR----VGEQLELVNLT-KWAGRKVNE-LSGGMQQRVGLARaFATGAPI 188
Cdd:CHL00131 98 GVS---NADF-LRLAynskrkfqGLPELD-PLEfleiINEKLKLVGMDpSFLSRNVNEgFSGGEKKRNEILQ-MALLDSE 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2087760999 189 L-LMDEPFSALDpLIRTRLQDELLEFQRRLKKTILFVSHD---LDeaFRIGNRIAIMEGGRIIQCGT 251
Cdd:CHL00131 172 LaILDETDSGLD-IDALKIIAEGINKLMTSENSIILITHYqrlLD--YIKPDYVHVMQNGKIIKTGD 235
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
162-259 |
2.91e-06 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 49.24 E-value: 2.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 162 GRKVNELSGGMQQRVGLARAFATG--APILLMDEPFSALDP-----LIRT--RLQDellefqrrLKKTILFVSHDlDEAF 232
Cdd:TIGR00630 483 SRAAGTLSGGEAQRIRLATQIGSGltGVLYVLDEPSIGLHQrdnrrLINTlkRLRD--------LGNTLIVVEHD-EDTI 553
|
90 100 110
....*....|....*....|....*....|...
gi 2087760999 233 RIGNRI------AIMEGGRIIQCGTPHDIVKNP 259
Cdd:TIGR00630 554 RAADYVidigpgAGEHGGEVVASGTPEEILANP 586
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
43-246 |
3.15e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 48.57 E-value: 3.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 43 VADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTTTgpVNpyrcNAKALRDLRtHTVSMVFQQ----- 117
Cdd:PRK10982 264 IRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKK--IN----NHNANEAIN-HGFALVTEErrstg 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 118 -FALLPwrtvaenVGFGLELAGMPEAERKLRVGEQLELVNLTKWA-----------GRKVNELSGGMQQRVGLARAFATG 185
Cdd:PRK10982 337 iYAYLD-------IGFNSLISNIRNYKNKVGLLDNSRMKSDTQWVidsmrvktpghRTQIGSLSGGNQQKVIIGRWLLTQ 409
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2087760999 186 APILLMDEPFSALDPLIRTRLQDELLEFQRRlKKTILFVSHDLDEAFRIGNRIAIMEGGRI 246
Cdd:PRK10982 410 PEILMLDEPTRGIDVGAKFEIYQLIAELAKK-DKGIIIISSEMPELLGITDRILVMSNGLV 469
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
47-229 |
4.99e-06 |
|
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: 46.20 E-value: 4.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 47 SLTIEEGEILVLMGLSGSGKSTLLRAVnGLAPVVRGDVAVSTTTGPVNPYRCnakalrdlrthTVSMVFQQFallpwrtv 126
Cdd:cd03227 15 DVTFGEGSLTIITGPNGSGKSTILDAI-GLALGGAQSATRRRSGVKAGCIVA-----------AVSAELIFT-------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 127 aenvgfglelagmpeaerklrvgeqlelvnltkwagrkVNELSGGMQQRVGLARAFA----TGAPILLMDEPFSALDPLI 202
Cdd:cd03227 75 --------------------------------------RLQLSGGEKELSALALILAlaslKPRPLYILDEIDRGLDPRD 116
|
170 180
....*....|....*....|....*..
gi 2087760999 203 RTRLQDELLEfQRRLKKTILFVSHDLD 229
Cdd:cd03227 117 GQALAEAILE-HLVKGAQVIVITHLPE 142
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
38-257 |
6.47e-06 |
|
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: 48.02 E-value: 6.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 38 GLVLGVADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTttgpVNPYRCnakALRDLRTHtVSMVFQQ 117
Cdd:TIGR00957 1297 DLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDG----LNIAKI---GLHDLRFK-ITIIPQD 1368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 118 FALL---------PWRTVA-ENVGFGLELAGMpeaerKLRVGEQLELVNLTKWAGRKvnELSGGMQQRVGLARAFATGAP 187
Cdd:TIGR00957 1369 PVLFsgslrmnldPFSQYSdEEVWWALELAHL-----KTFVSALPDKLDHECAEGGE--NLSVGQRQLVCLARALLRKTK 1441
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2087760999 188 ILLMDEPFSALD--------PLIRTRLQDellefqrrlkKTILFVSHDLDEAFRIgNRIAIMEGGRIIQCGTPHDIVK 257
Cdd:TIGR00957 1442 ILVLDEATAAVDletdnliqSTIRTQFED----------CTVLTIAHRLNTIMDY-TRVIVLDKGEVAEFGAPSNLLQ 1508
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
45-251 |
8.12e-06 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 47.41 E-value: 8.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 45 DASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTTtgPVNPYrcNAKALRDlrthTVSMVfQQFALLPWR 124
Cdd:PRK10790 359 NINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGR--PLSSL--SHSVLRQ----GVAMV-QQDPVVLAD 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 125 TVAENVGFGLELAgmpEAerklRVGEQLELVNLTKWA-----------GRKVNELSGGMQQRVGLARAFATGAPILLMDE 193
Cdd:PRK10790 430 TFLANVTLGRDIS---EE----QVWQALETVQLAELArslpdglytplGEQGNNLSVGQKQLLALARVLVQTPQILILDE 502
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2087760999 194 PFSALDPLIRTRLQDELLEFqrRLKKTILFVSHDLD---EAfrigNRIAIMEGGRIIQCGT 251
Cdd:PRK10790 503 ATANIDSGTEQAIQQALAAV--REHTTLVVIAHRLStivEA----DTILVLHRGQAVEQGT 557
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
53-227 |
8.87e-06 |
|
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: 45.06 E-value: 8.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 53 GEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVavstttgpvnpYRCNAKALRdlrthtvsmvfqqfallpwrtvaenvgf 132
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGV-----------IYIDGEDIL---------------------------- 42
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 133 glelagmpeaerklrvgEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDPLIRTRLQDE--- 209
Cdd:smart00382 43 -----------------EEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLeel 105
|
170 180
....*....|....*....|
gi 2087760999 210 --LLEFQRRLKKTILFVSHD 227
Cdd:smart00382 106 rlLLLLKSEKNLTVILTTND 125
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
45-241 |
9.83e-06 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 47.72 E-value: 9.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 45 DASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVS--------------TTTGPV--------NPYRCNAK- 101
Cdd:PTZ00265 403 DLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINdshnlkdinlkwwrSKIGVVsqdpllfsNSIKNNIKy 482
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 102 ---ALRDLRTHTVSM---VFQQFALLPWRTVAENVGFG--------LELAGMPEAERKLRVGEQLELVNLTK-------- 159
Cdd:PTZ00265 483 slySLKDLEALSNYYnedGNDSQENKNKRNSCRAKCAGdlndmsntTDSNELIEMRKNYQTIKDSEVVDVSKkvlihdfv 562
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 160 ---------WAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDPLIRTRLQDELLEFQRRLKKTILFVSHDLdE 230
Cdd:PTZ00265 563 salpdkyetLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAHRL-S 641
|
250
....*....|.
gi 2087760999 231 AFRIGNRIAIM 241
Cdd:PTZ00265 642 TIRYANTIFVL 652
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
4-243 |
1.21e-05 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 47.04 E-value: 1.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 4 VNFNNVSIIFGDRpetalamvdqgksrdeigaatglVLgVADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGD 83
Cdd:PRK11819 325 IEAENLSKSFGDR-----------------------LL-IDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGT 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 84 VAVstttGPvnpyrcnakalrdlrthTVSMVF-QQF--ALLPWRTVAENVGFGLELagmpeaerkLRVGeQLElVNLTKW 160
Cdd:PRK11819 381 IKI----GE-----------------TVKLAYvDQSrdALDPNKTVWEEISGGLDI---------IKVG-NRE-IPSRAY 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 161 AGR----------KVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDplIRT--RLQDELLEFqrrlKKTILFVSHD- 227
Cdd:PRK11819 429 VGRfnfkggdqqkKVGVLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLD--VETlrALEEALLEF----PGCAVVISHDr 502
|
250
....*....|....*...
gi 2087760999 228 --LDeafRIGNRIAIMEG 243
Cdd:PRK11819 503 wfLD---RIATHILAFEG 517
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
50-271 |
1.40e-05 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 47.03 E-value: 1.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 50 IEEGEILVLMGLSGSGKSTLLRAVNGlaPVVRGDVAVSTTTgpvnpyRCNAKALRDLRTHTVSMVF---QQFALLPWRTV 126
Cdd:TIGR00956 84 IKPGELTVVLGRPGSGCSTLLKTIAS--NTDGFHIGVEGVI------TYDGITPEEIKKHYRGDVVynaETDVHFPHLTV 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 127 AENVGF-------GLELAGMPEAERKLRVGE------QLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDE 193
Cdd:TIGR00956 156 GETLDFaarcktpQNRPDGVSREEYAKHIADvymatyGLSHTRNTKVGNDFVRGVSGGERKRVSIAEASLGGAKIQCWDN 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 194 PFSALDplirtrlQDELLEFQRRLK------KTILFVS--HDLDEAFRIGNRIAIMEGGRIIQCGtPHDIVKN------- 258
Cdd:TIGR00956 236 ATRGLD-------SATALEFIRALKtsanilDTTPLVAiyQCSQDAYELFDKVIVLYEGYQIYFG-PADKAKQyfekmgf 307
|
250
....*....|....*
gi 2087760999 259 --PADQYVADFVQNL 271
Cdd:TIGR00956 308 kcPDRQTTADFLTSL 322
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
140-231 |
1.60e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 46.55 E-value: 1.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 140 PEAERKLrVGEQLELVNLTKWAGRK-VNELSGGmQQRVGL-ARAFATGAPILLMDEPFSALDPLIRT---RLQDELL-EF 213
Cdd:PRK10938 374 SDRQQKL-AQQWLDILGIDKRTADApFHSLSWG-QQRLALiVRALVKHPTLLILDEPLQGLDPLNRQlvrRFVDVLIsEG 451
|
90
....*....|....*...
gi 2087760999 214 QRRLkktiLFVSHDLDEA 231
Cdd:PRK10938 452 ETQL----LFVSHHAEDA 465
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
163-270 |
1.74e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 46.75 E-value: 1.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 163 RKVNELSGGMQQRVGLARAFatGAPIL----LMDEPFSALDPlirtRLQDELLEFQRRLK---KTILFVSHD------LD 229
Cdd:PRK00635 472 RALATLSGGEQERTALAKHL--GAELIgityILDEPSIGLHP----QDTHKLINVIKKLRdqgNTVLLVEHDeqmislAD 545
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 2087760999 230 EAFRIGNRIAIMeGGRIIQCGTPHDIVKNpADQYVADFVQN 270
Cdd:PRK00635 546 RIIDIGPGAGIF-GGEVLFNGSPREFLAK-SDSLTAKYLRQ 584
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
49-228 |
2.10e-05 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 46.34 E-value: 2.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 49 TIEEGEILVLMGLSGSGKSTLLRAVNG-LAPV---VRGDVAVStttgpVNP-YrcnakaLRDLRTHTVSMVFqqfallpw 123
Cdd:PRK13409 361 EIYEGEVIGIVGPNGIGKTTFAKLLAGvLKPDegeVDPELKIS-----YKPqY------IKPDYDGTVEDLL-------- 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 124 RTVAENVG---FGLELAgmpeaeRKLRVGEQLElvnltkwagRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDP 200
Cdd:PRK13409 422 RSITDDLGssyYKSEII------KPLQLERLLD---------KNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDV 486
|
170 180
....*....|....*....|....*...
gi 2087760999 201 LIRTRLQDELLEFQRRLKKTILFVSHDL 228
Cdd:PRK13409 487 EQRLAVAKAIRRIAEEREATALVVDHDI 514
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
49-228 |
2.22e-05 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 46.32 E-value: 2.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 49 TIEEGEILVLMGLSGSGKSTLLRAVNG-LAP---VVRGDVAVS--------TTTGPVNPYrcnakaLRDLRTHTVSMVFq 116
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGvLKPdegEVDEDLKISykpqyispDYDGTVEEF------LRSANTDDFGSSY- 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 117 qfallpWRTvaenvgfglELAgmpeaeRKLRVGEQLElvnltkwagRKVNELSGGMQQRVGLARAFATGAPILLMDEPFS 196
Cdd:COG1245 435 ------YKT---------EII------KPLGLEKLLD---------KNVKDLSGGELQRVAIAACLSRDADLYLLDEPSA 484
|
170 180 190
....*....|....*....|....*....|....*.
gi 2087760999 197 ALDplIRTRLqdELLEFQRRL----KKTILFVSHDL 228
Cdd:COG1245 485 HLD--VEQRL--AVAKAIRRFaenrGKTAMVVDHDI 516
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
50-199 |
2.27e-05 |
|
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: 44.54 E-value: 2.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 50 IEEGEILVLMGLSGSGKSTLLR--AVNGLAPVVRGDVAVSTTTGPVNPYRcnakalrdlrthTVSMVFQQFALLPWRTVA 127
Cdd:cd03232 30 VKPGTLTALMGESGAGKTTLLDvlAGRKTAGVITGEILINGRPLDKNFQR------------STGYVEQQDVHSPNLTVR 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2087760999 128 ENVGFGLELAGMPEAERKlRVGEQLELVnltkwagrkvnelsggmqqrvglARAFatgapILLMDEPFSALD 199
Cdd:cd03232 98 EALRFSALLRGLSVEQRK-RLTIGVELA-----------------------AKPS-----ILFLDEPTSGLD 140
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
47-275 |
2.30e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 46.51 E-value: 2.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 47 SLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVstttgpvNPYRCNAKALRDLRtHTVSMVFQQFALLpwrtv 126
Cdd:PLN03232 1256 SFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMI-------DDCDVAKFGLTDLR-RVLSIIPQSPVLF----- 1322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 127 AENVGFGLElagmPEAERK-LRVGEQLELVNLTKWAGR-------KVNE----LSGGMQQRVGLARAFATGAPILLMDEP 194
Cdd:PLN03232 1323 SGTVRFNID----PFSEHNdADLWEALERAHIKDVIDRnpfgldaEVSEggenFSVGQRQLLSLARALLRRSKILVLDEA 1398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 195 FSALDPLIRTRLQDELLEFQRRLkkTILFVSHDLDEAFRIgNRIAIMEGGRIIQCGTPHDIVKNPADQYvADFVQNLNPI 274
Cdd:PLN03232 1399 TASVDVRTDSLIQRTIREEFKSC--TMLVIAHRLNTIIDC-DKILVLSSGQVLEYDSPQELLSRDTSAF-FRMVHSTGPA 1474
|
.
gi 2087760999 275 N 275
Cdd:PLN03232 1475 N 1475
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
3-257 |
2.77e-05 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 45.99 E-value: 2.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 3 AVNFNNVSIiFGDRPETalaMVDQGKSRDEIGaatgLVLGVADAsltIEEGEILVLMGLSGSGKSTLLRAVNG--LAPVV 80
Cdd:PLN03140 867 AMSFDDVNY-FVDMPAE---MKEQGVTEDRLQ----LLREVTGA---FRPGVLTALMGVSGAGKTTLMDVLAGrkTGGYI 935
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 81 RGDVAVS------TTTGPVNPYrCNAKalrDLRTHTV----SMVFQQFALLPWRTVAEnvgfglelagmpeaERKLRVGE 150
Cdd:PLN03140 936 EGDIRISgfpkkqETFARISGY-CEQN---DIHSPQVtvreSLIYSAFLRLPKEVSKE--------------EKMMFVDE 997
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 151 QLELVNLTKWAGR-----KVNELSGGMQQRVGLARAFATGAPILLMDEPFSALD---PLIRTRLQDELLEFQRRLKKTIL 222
Cdd:PLN03140 998 VMELVELDNLKDAivglpGVTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDaraAAIVMRTVRNTVDTGRTVVCTIH 1077
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 2087760999 223 FVSHDLDEAFrigNRIAIME-GGRIIQCGT----PHDIVK 257
Cdd:PLN03140 1078 QPSIDIFEAF---DELLLMKrGGQVIYSGPlgrnSHKIIE 1114
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
125-260 |
3.12e-05 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 45.79 E-value: 3.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 125 TVAENVGFgleLAGMPEAERKLR----VGeqLELVNLtkwaGRKVNELSGGMQQRVGLARAFA---TGAPILLMDEPFSA 197
Cdd:COG0178 789 TVEEALEF---FENIPKIARKLQtlqdVG--LGYIKL----GQPATTLSGGEAQRVKLASELSkrsTGKTLYILDEPTTG 859
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 198 L---DplIRTrlqdeLLE-FQRRLKK--TILFVSHDLD-------------EAfriGNRiaimeGGRIIQCGTPHDIVKN 258
Cdd:COG0178 860 LhfhD--IRK-----LLEvLHRLVDKgnTVVVIEHNLDviktadwiidlgpEG---GDG-----GGEIVAEGTPEEVAKV 924
|
..
gi 2087760999 259 PA 260
Cdd:COG0178 925 KA 926
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
45-199 |
7.98e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 42.94 E-value: 7.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 45 DASLTIEEGEILVLMGLSGSGKSTLLRAVNGLapvvrgdvaVSTTTGPVNPYRCNakaLRDLRTHTVSMVFQQFALLPWR 124
Cdd:PRK13541 18 DLSITFLPSAITYIKGANGCGKSSLLRMIAGI---------MQPSSGNIYYKNCN---INNIAKPYCTYIGHNLGLKLEM 85
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2087760999 125 TVAENVGFGLELAGMPEAerklrVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALD 199
Cdd:PRK13541 86 TVFENLKFWSEIYNSAET-----LYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLS 155
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
163-244 |
1.01e-04 |
|
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: 43.03 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 163 RKVNELSGGMQQRVGLARAFA--------TGAPI--LLMDEPFSALDPLIRTRLQdELLEFQRRLKKTILFVSHDLDEAF 232
Cdd:cd03279 119 RPVSTLSGGETFLASLSLALAlsevlqnrGGARLeaLFIDEGFGTLDPEALEAVA-TALELIRTENRMVGVISHVEELKE 197
|
90
....*....|..
gi 2087760999 233 RIGNRIAIMEGG 244
Cdd:cd03279 198 RIPQRLEVIKTP 209
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
166-252 |
3.20e-04 |
|
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: 41.24 E-value: 3.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 166 NELSGGMQQRVGLARAFATGAPILLMDEPFSALDPLIRTRLQDELLE-FQrrlKKTILFVSHDLDEAFRIgNRIAIMEGG 244
Cdd:cd03369 124 LNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDALIQKTIREeFT---NSTILTIAHRLRTIIDY-DKILVMDAG 199
|
....*...
gi 2087760999 245 RIIQCGTP 252
Cdd:cd03369 200 EVKEYDHP 207
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
43-226 |
3.40e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 42.54 E-value: 3.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 43 VADASLTIEEGEILVLMGLSGSGKSTLLR-----AVNGLAPV-----VRGDVAVSTTTGpvnpYRC--NAKALRDLRTHT 110
Cdd:PLN03073 193 IVDASVTLAFGRHYGLVGRNGTGKTTFLRymamhAIDGIPKNcqilhVEQEVVGDDTTA----LQCvlNTDIERTQLLEE 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 111 VSMVFQQFALLPWRTVAENVGFGLE--LAGMPEAERKLRVGEQLELVNL--------TKWAG---------RKVNELSGG 171
Cdd:PLN03073 269 EAQLVAQQRELEFETETGKGKGANKdgVDKDAVSQRLEEIYKRLELIDAytaearaaSILAGlsftpemqvKATKTFSGG 348
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2087760999 172 MQQRVGLARAFATGAPILLMDEPFSALDPLIRTRLQDELLEFqrrlKKTILFVSH 226
Cdd:PLN03073 349 WRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKW----PKTFIVVSH 399
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
53-199 |
4.23e-04 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 42.40 E-value: 4.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 53 GEILVLMGLSGSGKSTLLravNGLAPVVRGDVavsTTTGPVnpyRCNAKALRDLRTHTVSMVFQQFALLPWRTVAENVGF 132
Cdd:TIGR00956 789 GTLTALMGASGAGKTTLL---NVLAERVTTGV---ITGGDR---LVNGRPLDSSFQRSIGYVQQQDLHLPTSTVRESLRF 859
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2087760999 133 GLEL---AGMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGM--QQR------VGLArafATGAPILLMDEPFSALD 199
Cdd:TIGR00956 860 SAYLrqpKSVSKSEKMEYVEEVIKLLEMESYADAVVGVPGEGLnvEQRkrltigVELV---AKPKLLLFLDEPTSGLD 934
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
140-255 |
4.37e-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: 42.31 E-value: 4.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 140 PEAERKLR----VGeqLELVNLtkwaGRKVNELSGGMQQRVGLARAF---ATGAPILLMDEPFSALdplirtRLQD--EL 210
Cdd:TIGR00630 804 PSISRKLQtlcdVG--LGYIRL----GQPATTLSGGEAQRIKLAKELskrSTGRTLYILDEPTTGL------HFDDikKL 871
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 2087760999 211 LEFQRRLKK---TILFVSHDLD---EAFRI-------GNRiaimeGGRIIQCGTPHDI 255
Cdd:TIGR00630 872 LEVLQRLVDkgnTVVVIEHNLDvikTADYIidlgpegGDG-----GGTVVASGTPEEV 924
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
125-252 |
8.90e-04 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 40.29 E-value: 8.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 125 TVAENVGFgleLAGMPEAERKLRVGEQLELVNLTkwAGRKVNELSGGMQQRVGLARAF---ATGAPILLMDEPFSALdpl 201
Cdd:cd03271 132 TVEEALEF---FENIPKIARKLQTLCDVGLGYIK--LGQPATTLSGGEAQRIKLAKELskrSTGKTLYILDEPTTGL--- 203
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2087760999 202 irtRLQD--ELLEFQRRLKK---TILFVSHDLD-------------EAfriGNRiaimeGGRIIQCGTP 252
Cdd:cd03271 204 ---HFHDvkKLLEVLQRLVDkgnTVVVIEHNLDvikcadwiidlgpEG---GDG-----GGQVVASGTP 261
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
167-228 |
1.05e-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: 40.45 E-value: 1.05e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2087760999 167 ELSGGMQQ---RVGLARAFATGAPILLMDEPFSALDPLIRTRLQdELLEFQRRLKKTILFVSHDL 228
Cdd:pfam13304 236 ELSDGTKRllaLLAALLSALPKGGLLLIDEPESGLHPKLLRRLL-ELLKELSRNGAQLILTTHSP 299
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
168-237 |
1.51e-03 |
|
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: 39.13 E-value: 1.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 168 LSGGmQQ-------RVGLARAFATGAPILLMDEPFSALDP-LIRTRLQDeLLEFQRRLK-KTILFVSHD------LDEAF 232
Cdd:cd03240 116 CSGG-EKvlasliiRLALAETFGSNCGILALDEPTTNLDEeNIEESLAE-IIEERKSQKnFQLIVITHDeelvdaADHIY 193
|
....*
gi 2087760999 233 RIGNR 237
Cdd:cd03240 194 RVEKD 198
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
47-258 |
3.73e-03 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 39.34 E-value: 3.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 47 SLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVstttgpvNPYRCNAKALRDLRThtVSMVFQQFALLPWRTV 126
Cdd:PLN03130 1259 SFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILI-------DGCDISKFGLMDLRK--VLGIIPQAPVLFSGTV 1329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 127 AENVG-FG----------LELAGMPEAERKLRVGEQLELVNltkwAGRKvneLSGGMQQRVGLARAFATGAPILLMDEPF 195
Cdd:PLN03130 1330 RFNLDpFNehndadlwesLERAHLKDVIRRNSLGLDAEVSE----AGEN---FSVGQRQLLSLARALLRRSKILVLDEAT 1402
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2087760999 196 SALDplIRTrlqDELLefQRRLKK-----TILFVSHDLDEAFRIgNRIAIMEGGRIIQCGTPHDIVKN 258
Cdd:PLN03130 1403 AAVD--VRT---DALI--QKTIREefkscTMLIIAHRLNTIIDC-DRILVLDAGRVVEFDTPENLLSN 1462
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
164-247 |
4.72e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 38.62 E-value: 4.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 164 KVNELSGGMQQRVGLARAFATGAPILLMDEPfsaldplirTRLQD-----ELLEFQRRLK---KTILFVSHDLDEAFRIG 235
Cdd:NF040905 401 KVGNLSGGNQQKVVLSKWLFTDPDVLILDEP---------TRGIDvgakyEIYTIINELAaegKGVIVISSELPELLGMC 471
|
90
....*....|..
gi 2087760999 236 NRIAIMEGGRII 247
Cdd:NF040905 472 DRIYVMNEGRIT 483
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
163-242 |
4.82e-03 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 38.61 E-value: 4.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087760999 163 RKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDplirtrlQDELLEFQRRLKK---TILFVSHDLDEAFRIGNRIA 239
Cdd:PRK10636 145 RPVSDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLD-------LDAVIWLEKWLKSyqgTLILISHDRDFLDPIVDKII 217
|
...
gi 2087760999 240 IME 242
Cdd:PRK10636 218 HIE 220
|
|
| COG4639 |
COG4639 |
Predicted kinase [General function prediction only]; |
52-80 |
6.74e-03 |
|
Predicted kinase [General function prediction only];
Pssm-ID: 443677 [Multi-domain] Cd Length: 145 Bit Score: 36.73 E-value: 6.74e-03
10 20
....*....|....*....|....*....
gi 2087760999 52 EGEILVLMGLSGSGKSTLLRAVNGLAPVV 80
Cdd:COG4639 1 MLSLVVLIGLPGSGKSTFARRLFAPTEVV 29
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
44-73 |
9.68e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 38.10 E-value: 9.68e-03
10 20 30
....*....|....*....|....*....|
gi 2087760999 44 ADASLTIEEGeILVLMGLSGSGKSTLLRAV 73
Cdd:PRK02224 15 ADADLRLEDG-VTVIHGVNGSGKSSLLEAC 43
|
|
| |
