|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
1-400 |
0e+00 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 732.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 1 MAIKLEIKNLYKIFGEHPQRAFKYIEQGLSKEQILEKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEP 80
Cdd:PRK10070 1 MAIKLEIKNLYKIFGEHPQRAFKYIEQGLSKEQILEKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 81 TRGQVLIDGVDIAKISDAELREVRRKKIAMVFQSFALMPHMTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHS 160
Cdd:PRK10070 81 TRGQVLIDGVDIAKISDAELREVRRKKIAMVFQSFALMPHMTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 161 YPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQN 240
Cdd:PRK10070 161 YPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 241 GEVVQVGTPDEILNNPANDYVRTFFRGVDISQVFSAKDIARRTPNGLIRKTPGFGPRSALKLLQDEDREYGYVIERGNKF 320
Cdd:PRK10070 241 GEVVQVGTPDEILNNPANDYVRTFFRGVDISQVFSAKDIARRTPNGLIRKTPGFGPRSALKLLQDEDREYGYVIERGNKF 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 321 VGAVSIDSLKTALTQQQGLDAALIDAPLAVDAQTPLSELLSHVGQAPCAVPVVDEDQQYVGIISKGMLLRALDREGVNNG 400
Cdd:PRK10070 321 VGAVSIDSLKTALTQQQGLDAALIDAPLAVDAQTPLSELLSHVGQAPCAVPVVDEDQQYVGIISKGMLLRALDREGVNNG 400
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
3-393 |
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: 672.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 3 IKLEIKNLYKIFGEHPQRAFKYIEQGLSKEQILEKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTR 82
Cdd:COG4175 2 PKIEVRNLYKIFGKRPERALKLLDQGKSKDEILEKTGQTVGVNDASFDVEEGEIFVIMGLSGSGKSTLVRCLNRLIEPTA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 83 GQVLIDGVDIAKISDAELREVRRKKIAMVFQSFALMPHMTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYP 162
Cdd:COG4175 82 GEVLIDGEDITKLSKKELRELRRKKMSMVFQHFALLPHRTVLENVAFGLEIQGVPKAERRERAREALELVGLAGWEDSYP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 163 DELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGE 242
Cdd:COG4175 162 DELSGGMQQRVGLARALATDPDILLMDEAFSALDPLIRREMQDELLELQAKLKKTIVFITHDLDEALRLGDRIAIMKDGR 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 243 VVQVGTPDEILNNPANDYVRTFFRGVDISQVFSAKDIARRTPNGLIRKTpgfGPRSALKLLQDEDREYGYVIERGNKFVG 322
Cdd:COG4175 242 IVQIGTPEEILTNPANDYVADFVEDVDRSKVLTAGSVMRPPEAVVSEKD---GPRVALRRMREEGISSLYVVDRDRRLLG 318
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16130591 323 AVSIDSLKTALTQQQGLDAALIDAPLAVDAQTPLSELLSHVGQAPCAVPVVDEDQQYVGIISKGMLLRALD 393
Cdd:COG4175 319 VVTADDALEAVKGEKDLEEILLTDVPTVSPDTPLRDLLPLVAESPYPLAVVDEDGRLLGVISRGSLLAALA 389
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
36-396 |
0e+00 |
|
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: 596.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 36 EKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVRRKKIAMVFQSF 115
Cdd:TIGR01186 1 KKTGGKKGVNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEPTAGQIFIDGENIMKQSPVELREVRRKKIGMVFQQF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 116 ALMPHMTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSAL 195
Cdd:TIGR01186 81 ALFPHMTILQNTSLGPELLGWPEQERKEKALELLKLVGLEEYEHRYPDELSGGMQQRVGLARALAAEPDILLMDEAFSAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 196 DPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFFRGVDISQVFS 275
Cdd:TIGR01186 161 DPLIRDSMQDELKKLQATLQKTIVFITHDLDEAIRIGDRIVIMKAGEIVQVGTPDEILRNPANEYVEEFIGKVDLSQVFD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 276 AKDIARRTPNGLIRKTPGFGPRSALKLLQDEDREYGYVIERGNKFVGAVSIDSLKTALTQQQGLDAALIDAPLAVDAQTP 355
Cdd:TIGR01186 241 AERIAQRMNTGPITKTADKGPRSALQLMRDERVDSLYVVDRQNKLVGVVDVESIKQARKKAQGLQDVLIDDIYTVDAGTL 320
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 16130591 356 LSELLSHVGQAPCAVPVVDEDQQYVGIISKGMLLRALD--REG 396
Cdd:TIGR01186 321 LRETVRKVLKAGIKVPVVDEDQRLVGIVTRGSLVDALYdsREG 363
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
5-273 |
0e+00 |
|
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: 514.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 5 LEIKNLYKIFGEHPQRAFKYIEQGLSKEQILEKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQ 84
Cdd:cd03294 1 IKIKGLYKIFGKNPQKAFKLLAKGKSKEEILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 85 VLIDGVDIAKISDAELREVRRKKIAMVFQSFALMPHMTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDE 164
Cdd:cd03294 81 VLIDGQDIAAMSRKELRELRRKKISMVFQSFALLPHRTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 165 LSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVV 244
Cdd:cd03294 161 LSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLV 240
|
250 260
....*....|....*....|....*....
gi 16130591 245 QVGTPDEILNNPANDYVRTFFRGVDISQV 273
Cdd:cd03294 241 QVGTPEEILTNPANDYVREFFRGVDRAKV 269
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-265 |
4.92e-100 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 301.25 E-value: 4.92e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 1 MAIKLEIKNLYKIFGEHPqrafkyieqglskeqilektglslGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEP 80
Cdd:COG3842 2 AMPALELENVSKRYGDVT------------------------ALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETP 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 81 TRGQVLIDGVDIAKISdAELREvrrkkIAMVFQSFALMPHMTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHS 160
Cdd:COG3842 58 DSGRILLDGRDVTGLP-PEKRN-----VGMVFQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADR 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 161 YPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQN 240
Cdd:COG3842 132 YPHQLSGGQQQRVALARALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMND 211
|
250 260
....*....|....*....|....*
gi 16130591 241 GEVVQVGTPDEILNNPANDYVRTFF 265
Cdd:COG3842 212 GRIEQVGTPEEIYERPATRFVADFI 236
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
44-265 |
2.00e-98 |
|
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: 293.05 E-value: 2.00e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELRevrrKKIAMVFQSFALMPHMTV 123
Cdd:cd03295 17 VNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELR----RKIGYVIQQIGLFPHMTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 124 LDNTAFGMELAGINAEERREKALDALRQVGLE--NYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRT 201
Cdd:cd03295 93 EENIALVPKLLKWPKEKIRERADELLALVGLDpaEFADRYPHELSGGQQQRVGVARALAADPPLLLMDEPFGALDPITRD 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16130591 202 EMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFF 265
Cdd:cd03295 173 QLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDFVAEFV 236
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
5-247 |
2.89e-95 |
|
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: 284.03 E-value: 2.89e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 5 LEIKNLYKIFGEHPqrafkyieqglskeqilektglslGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQ 84
Cdd:cd03259 1 LELKGLSKTYGSVR------------------------ALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGE 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 85 VLIDGVDIAKisdaelREVRRKKIAMVFQSFALMPHMTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDE 164
Cdd:cd03259 57 ILIDGRDVTG------VPPERRNIGMVFQDYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHE 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 165 LSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVV 244
Cdd:cd03259 131 LSGGQQQRVALARALAREPSLLLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIV 210
|
...
gi 16130591 245 QVG 247
Cdd:cd03259 211 QVG 213
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-265 |
2.14e-94 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 286.58 E-value: 2.14e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 1 MAiKLEIKNLYKIFGEHPqrafkyieqglskeqilektglslGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEP 80
Cdd:COG3839 1 MA-SLELENVSKSYGGVE------------------------ALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDP 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 81 TRGQVLIDGVDIAKIsdaelrEVRRKKIAMVFQSFALMPHMTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHS 160
Cdd:COG3839 56 TSGEILIGGRDVTDL------PPKDRNIAMVFQSYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDR 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 161 YPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQN 240
Cdd:COG3839 130 KPKQLSGGQRQRVALGRALVREPKVFLLDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMND 209
|
250 260
....*....|....*....|....*
gi 16130591 241 GEVVQVGTPDEILNNPANDYVRTFF 265
Cdd:COG3839 210 GRIQQVGTPEELYDRPANLFVAGFI 234
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-249 |
2.02e-91 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 275.81 E-value: 2.02e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 1 MAIKLEIKNLYKIFGEHPQRAfkyieqglskeQILEktglslgvkDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEP 80
Cdd:COG1116 4 AAPALELRGVSKRFPTGGGGV-----------TALD---------DVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKP 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 81 TRGQVLIDGVDIAKISDaelrevrrkKIAMVFQSFALMPHMTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHS 160
Cdd:COG1116 64 TSGEVLVDGKPVTGPGP---------DRGVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDA 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 161 YPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQN 240
Cdd:COG1116 135 YPHQLSGGMRQRVAIARALANDPEVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFLADRVVVLSA 214
|
250
....*....|....
gi 16130591 241 G-----EVVQVGTP 249
Cdd:COG1116 215 RpgrivEEIDVDLP 228
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-265 |
1.90e-89 |
|
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: 269.93 E-value: 1.90e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 1 MAIKLEIKNLYKIFGEHPqrafkyieqglskeqILektglslgvKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEP 80
Cdd:COG1127 2 SEPMIEVRNLTKSFGDRV---------------VL---------DGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRP 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 81 TRGQVLIDGVDIAKISDAELREVRRKkIAMVFQSFALMPHMTVLDNTAFGM-ELAGINAEERREKALDALRQVGLENYAH 159
Cdd:COG1127 58 DSGEILVDGQDITGLSEKELYELRRR-IGMLFQGGALFDSLTVFENVAFPLrEHTDLSEAEIRELVLEKLELVGLPGAAD 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 160 SYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPlIRTEMQDELV-KLQAKHQRTIVFISHDLDEAMRIGDRIAIM 238
Cdd:COG1127 137 KMPSELSGGMRKRVALARALALDPEILLYDEPTAGLDP-ITSAVIDELIrELRDELGLTSVVVTHDLDSAFAIADRVAVL 215
|
250 260
....*....|....*....|....*..
gi 16130591 239 QNGEVVQVGTPDEILNNPaNDYVRTFF 265
Cdd:COG1127 216 ADGKIIAEGTPEELLASD-DPWVRQFL 241
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
5-238 |
4.21e-89 |
|
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: 268.57 E-value: 4.21e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 5 LEIKNLYKIFGeHPQRAFKyieqglskeqILEktglslgvkDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQ 84
Cdd:cd03293 1 LEVRNVSKTYG-GGGGAVT----------ALE---------DISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGE 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 85 VLIDGvdiakisdAELREVRRKkIAMVFQSFALMPHMTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDE 164
Cdd:cd03293 61 VLVDG--------EPVTGPGPD-RGYVFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQ 131
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16130591 165 LSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIM 238
Cdd:cd03293 132 LSGGMRQRVALARALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVL 205
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
5-268 |
7.09e-86 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 264.63 E-value: 7.09e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 5 LEIKNLYKIFgEHPQRAFKyieqglskeqilektglslGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQ 84
Cdd:COG1135 2 IELENLSKTF-PTKGGPVT-------------------ALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGS 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 85 VLIDGVDIAKISDAELREVRRKkIAMVFQSFALMPHMTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDE 164
Cdd:COG1135 62 VLVDGVDLTALSERELRAARRK-IGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 165 LSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVV 244
Cdd:COG1135 141 LSGGQKQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRICDRVAVLENGRIV 220
|
250 260
....*....|....*....|....
gi 16130591 245 QVGTPDEILNNPANDYVRTFFRGV 268
Cdd:COG1135 221 EQGPVLDVFANPQSELTRRFLPTV 244
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
5-263 |
1.15e-83 |
|
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: 264.46 E-value: 1.15e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 5 LEIKNLYKIFGEHPQRAFKyieqglskeqilektglslGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQ 84
Cdd:COG1123 261 LEVRNLSKRYPVRGKGGVR-------------------AVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGS 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 85 VLIDGVDIAKISDAELREVRRKkIAMVFQ--SFALMPHMTVLDNTAFGMELAGI-NAEERREKALDALRQVGL-ENYAHS 160
Cdd:COG1123 322 ILFDGKDLTKLSRRSLRELRRR-VQMVFQdpYSSLNPRMTVGDIIAEPLRLHGLlSRAERRERVAELLERVGLpPDLADR 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 161 YPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQN 240
Cdd:COG1123 401 YPHELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYD 480
|
250 260
....*....|....*....|...
gi 16130591 241 GEVVQVGTPDEILNNPANDYVRT 263
Cdd:COG1123 481 GRIVEDGPTEEVFANPQHPYTRA 503
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
44-287 |
4.55e-83 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 257.77 E-value: 4.55e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDiAKISdaelREVRRKKIAMVFQSFALMPHMTV 123
Cdd:COG1118 18 LDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRD-LFTN----LPPRERRVGFVFQHYALFPHMTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 124 LDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEM 203
Cdd:COG1118 93 AENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLLLDEPFGALDAKVRKEL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 204 QDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYV------RTFFRGVDISQVFSAK 277
Cdd:COG1118 173 RRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDRPATPFVarflgcVNVLRGRVIGGQLEAD 252
|
250
....*....|
gi 16130591 278 DIARRTPNGL 287
Cdd:COG1118 253 GLTLPVAEPL 262
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
5-268 |
1.45e-82 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 252.22 E-value: 1.45e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 5 LEIKNLYKIFGEHpqrafkyieqglskeQILektglslgvKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQ 84
Cdd:COG1126 2 IEIENLHKSFGDL---------------EVL---------KGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGT 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 85 VLIDGVDIAkISDAELREVRRKkIAMVFQSFALMPHMTVLDNTAFG-MELAGINAEERREKALDALRQVGLENYAHSYPD 163
Cdd:COG1126 58 ITVDGEDLT-DSKKDINKLRRK-VGMVFQQFNLFPHLTVLENVTLApIKVKKMSKAEAEERAMELLERVGLADKADAYPA 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 164 ELSGGMRQRVGLARALAINPDILLMDEAFSALDPlirtEMQDE----LVKLqAKHQRTIVFISHDLDEAMRIGDRIAIMQ 239
Cdd:COG1126 136 QLSGGQQQRVAIARALAMEPKVMLFDEPTSALDP----ELVGEvldvMRDL-AKEGMTMVVVTHEMGFAREVADRVVFMD 210
|
250 260
....*....|....*....|....*....
gi 16130591 240 NGEVVQVGTPDEILNNPANDYVRTFFRGV 268
Cdd:COG1126 211 GGRIVEEGPPEEFFENPQHERTRAFLSKV 239
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
32-264 |
9.67e-82 |
|
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: 250.23 E-value: 9.67e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 32 EQILEKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISdaelreVRRKKIAMV 111
Cdd:cd03300 4 ENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLP------PHKRPVNTV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 112 FQSFALMPHMTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEA 191
Cdd:cd03300 78 FQNYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEP 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16130591 192 FSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTF 264
Cdd:cd03300 158 LGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPANRFVADF 230
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
5-264 |
2.93e-80 |
|
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: 246.26 E-value: 2.93e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 5 LEIKNLYKIFGEHpqrafkyieqglskeQILektglslgvKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQ 84
Cdd:cd03261 1 IELRGLTKSFGGR---------------TVL---------KGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGE 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 85 VLIDGVDIAKISDAELREVRRKkIAMVFQSFALMPHMTVLDNTAFGM-ELAGINAEERREKALDALRQVGLENYAHSYPD 163
Cdd:cd03261 57 VLIDGEDISGLSEAELYRLRRR-MGMLFQSGALFDSLTVFENVAFPLrEHTRLSEEEIREIVLEKLEAVGLRGAEDLYPA 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 164 ELSGGMRQRVGLARALAINPDILLMDEAFSALDPlIRTEMQDELV-KLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGE 242
Cdd:cd03261 136 ELSGGMKKRVALARALALDPELLLYDEPTAGLDP-IASGVIDDLIrSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGK 214
|
250 260
....*....|....*....|..
gi 16130591 243 VVQVGTPDEILNNPaNDYVRTF 264
Cdd:cd03261 215 IVAEGTPEELRASD-DPLVRQF 235
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
5-256 |
9.25e-79 |
|
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: 242.49 E-value: 9.25e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 5 LEIKNLYKIFGEHPQRAfkyieqglskeqilektglsLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQ 84
Cdd:cd03258 2 IELKNVSKVFGDTGGKV--------------------TALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGS 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 85 VLIDGVDIAKISDAELREVRRKkIAMVFQSFALMPHMTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDE 164
Cdd:cd03258 62 VLVDGTDLTLLSGKELRKARRR-IGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 165 LSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVV 244
Cdd:cd03258 141 LSGGQKQRVGIARALANNPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVV 220
|
250
....*....|..
gi 16130591 245 QVGTPDEILNNP 256
Cdd:cd03258 221 EEGTVEEVFANP 232
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-244 |
8.52e-75 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 232.24 E-value: 8.52e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 1 MAIKLEIKNLYKIFGehpqrafkyieQGLSKEQILektglslgvKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEP 80
Cdd:COG1136 1 MSPLLELRNLTKSYG-----------TGEGEVTAL---------RGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRP 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 81 TRGQVLIDGVDIAKISDAELREVRRKKIAMVFQSFALMPHMTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHS 160
Cdd:COG1136 61 TSGEVLIDGQDISSLSERELARLRRRHIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDH 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 161 YPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLdEAMRIGDRIAIMQN 240
Cdd:COG1136 141 RPSQLSGGQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDP-ELAARADRVIRLRD 219
|
....
gi 16130591 241 GEVV 244
Cdd:COG1136 220 GRIV 223
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
5-243 |
9.69e-75 |
|
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: 231.61 E-value: 9.69e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 5 LEIKNLYKIFGehpqrafkyieQGLSKEQILektglslgvKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQ 84
Cdd:cd03255 1 IELKNLSKTYG-----------GGGEKVQAL---------KGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGE 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 85 VLIDGVDIAKISDAELREVRRKKIAMVFQSFALMPHMTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDE 164
Cdd:cd03255 61 VRVDGTDISKLSEKELAAFRRRHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSE 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16130591 165 LSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAmRIGDRIAIMQNGEV 243
Cdd:cd03255 141 LSGGQQQRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELA-EYADRIIELRDGKI 218
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
5-247 |
6.31e-74 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 229.45 E-value: 6.31e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 5 LEIKNLYKIFGEHPqrafkyieqglskeqilektglslGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQ 84
Cdd:cd03301 1 VELENVTKRFGNVT------------------------ALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGR 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 85 VLIDGVDIAKISDAElrevrrKKIAMVFQSFALMPHMTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDE 164
Cdd:cd03301 57 IYIGGRDVTDLPPKD------RDIAMVFQNYALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQ 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 165 LSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVV 244
Cdd:cd03301 131 LSGGQRQRVALGRAIVREPKVFLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQ 210
|
...
gi 16130591 245 QVG 247
Cdd:cd03301 211 QIG 213
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
5-242 |
1.34e-73 |
|
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: 227.46 E-value: 1.34e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 5 LEIKNLYKIFGEHpqrafkyieqglskeqilektglsLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQ 84
Cdd:cd03229 1 LELKNVSKRYGQK------------------------TVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGS 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 85 VLIDGVDIAKISDaeLREVRRKKIAMVFQSFALMPHMTVLDNTAFGmelaginaeerrekaldalrqvglenyahsypde 164
Cdd:cd03229 57 ILIDGEDLTDLED--ELPPLRRRIGMVFQDFALFPHLTVLENIALG---------------------------------- 100
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16130591 165 LSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGE 242
Cdd:cd03229 101 LSGGQQQRVALARALAMDPDVLLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
44-256 |
7.17e-73 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 227.22 E-value: 7.17e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKisdAELREVRRKkIAMVFQS-----FAlm 118
Cdd:COG1122 17 LDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITK---KNLRELRRK-VGLVFQNpddqlFA-- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 119 phMTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPL 198
Cdd:COG1122 91 --PTVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPR 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 16130591 199 IRTEMQDELVKLQAKHqRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNP 256
Cdd:COG1122 169 GRRELLELLKRLNKEG-KTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDY 225
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
43-289 |
1.02e-72 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 230.84 E-value: 1.02e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVRRKkIAMVFQSFALMPHMT 122
Cdd:PRK11153 20 ALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKARRQ-IGMIFQHFNLLSSRT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 123 VLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPlirtE 202
Cdd:PRK11153 99 VFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPKVLLCDEATSALDP----A 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 203 MQDELVKLQAKHQR----TIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFFR---GVDISQVFS 275
Cdd:PRK11153 175 TTRSILELLKDINRelglTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHPKHPLTREFIQstlHLDLPEDYL 254
|
250
....*....|....*.
gi 16130591 276 AKDIARRTPNG--LIR 289
Cdd:PRK11153 255 ARLQAEPTTGSgpLLR 270
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
44-257 |
3.24e-72 |
|
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: 228.78 E-value: 3.24e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEP---TRGQVLIDGVDIAKISDAELREVRRKKIAMVFQSF--ALM 118
Cdd:COG0444 21 VDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKELRKIRGREIQMIFQDPmtSLN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 119 PHMTVLDNTAFGMEL-AGINAEERREKALDALRQVGL---ENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSA 194
Cdd:COG0444 101 PVMTVGDQIAEPLRIhGGLSKAEARERAIELLERVGLpdpERRLDRYPHELSGGMRQRVMIARALALEPKLLIADEPTTA 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16130591 195 LDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPA 257
Cdd:COG0444 181 LDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGPVEELFENPR 243
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
5-254 |
2.86e-71 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 223.40 E-value: 2.86e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 5 LEIKNLYKIFGEHPqrafkyieqglskeqilektglslGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQ 84
Cdd:COG1131 1 IEVRGLTKRYGDKT------------------------ALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGE 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 85 VLIDGVDIAKisdaELREVRRKkIAMVFQSFALMPHMTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDE 164
Cdd:COG1131 57 VRVLGEDVAR----DPAEVRRR-IGYVPQEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGT 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 165 LSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLqAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVV 244
Cdd:COG1131 132 LSGGMKQRLGLALALLHDPELLILDEPTSGLDPEARRELWELLREL-AAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIV 210
|
250
....*....|
gi 16130591 245 QVGTPDEILN 254
Cdd:COG1131 211 ADGTPDELKA 220
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
5-247 |
5.05e-71 |
|
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: 222.38 E-value: 5.05e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 5 LEIKNLYKIFGEH--PQRAfkyieqglskeqilektglslgVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTR 82
Cdd:cd03257 2 LEVKNLSVSFPTGggSVKA----------------------LDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTS 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 83 GQVLIDGVDIAKISDaELREVRRKKIAMVFQ--SFALMPHMTVLDNTAFGMELAGIN--AEERREKALDALRQVGL-ENY 157
Cdd:cd03257 60 GSIIFDGKDLLKLSR-RLRKIRRKEIQMVFQdpMSSLNPRMTIGEQIAEPLRIHGKLskKEARKEAVLLLLVGVGLpEEV 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 158 AHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAI 237
Cdd:cd03257 139 LNRYPHELSGGQRQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAV 218
|
250
....*....|
gi 16130591 238 MQNGEVVQVG 247
Cdd:cd03257 219 MYAGKIVEEG 228
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1-264 |
1.14e-69 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 219.52 E-value: 1.14e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 1 MAIklEIKNLYKIFGEHPqrafkyieqglskeqilektglslGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEP 80
Cdd:cd03296 1 MSI--EVRNVSKRFGDFV------------------------ALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERP 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 81 TRGQVLIDGVDIAKISdaelreVRRKKIAMVFQSFALMPHMTVLDNTAFGMEL----AGINAEERREKALDALRQVGLEN 156
Cdd:cd03296 55 DSGTILFGGEDATDVP------VQERNVGFVFQHYALFRHMTVFDNVAFGLRVkprsERPPEAEIRAKVHELLKLVQLDW 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 157 YAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIA 236
Cdd:cd03296 129 LADRYPAQLSGGQRQRVALARALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVV 208
|
250 260
....*....|....*....|....*...
gi 16130591 237 IMQNGEVVQVGTPDEILNNPANDYVRTF 264
Cdd:cd03296 209 VMNKGRIEQVGTPDEVYDHPASPFVYSF 236
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
59-264 |
4.80e-69 |
|
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: 220.83 E-value: 4.80e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 59 IMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISdAELREvrrkkIAMVFQSFALMPHMTVLDNTAFGMELAGINA 138
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVP-PHLRH-----INMVFQSYALFPHMTVEENVAFGLKMRKVPR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 139 EERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTI 218
Cdd:TIGR01187 75 AEIKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITF 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 16130591 219 VFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTF 264
Cdd:TIGR01187 155 VFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFVARF 200
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
5-243 |
7.37e-69 |
|
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: 216.24 E-value: 7.37e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 5 LEIKNLYKIFGEHpqrafkyieqglskeQILektglslgvKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQ 84
Cdd:cd03262 1 IEIKNLHKSFGDF---------------HVL---------KGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGT 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 85 VLIDGVDIAKiSDAELREVRrKKIAMVFQSFALMPHMTVLDNTAFG-MELAGINAEERREKALDALRQVGLENYAHSYPD 163
Cdd:cd03262 57 IIIDGLKLTD-DKKNINELR-QKVGMVFQQFNLFPHLTVLENITLApIKVKGMSKAEAEERALELLEKVGLADKADAYPA 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 164 ELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLqAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEV 243
Cdd:cd03262 135 QLSGGQQQRVAIARALAMNPKVMLFDEPTSALDPELVGEVLDVMKDL-AEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
5-316 |
6.19e-68 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 219.43 E-value: 6.19e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 5 LEIKNLYKIFGEHpqrafkyieqglskeQILektglslgvKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQ 84
Cdd:PRK09452 15 VELRGISKSFDGK---------------EVI---------SNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 85 VLIDGVDIAKISdAELREVRrkkiaMVFQSFALMPHMTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDE 164
Cdd:PRK09452 71 IMLDGQDITHVP-AENRHVN-----TVFQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 165 LSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVV 244
Cdd:PRK09452 145 LSGGQQQRVAIARAVVNKPKVLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIE 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 245 QVGTPDEILNNPANDYVRTFfrgVDISQVFSAKDIARRTPNGL----------IRKTPGFGPRSALKLL----------- 303
Cdd:PRK09452 225 QDGTPREIYEEPKNLFVARF---IGEINIFDATVIERLDEQRVranvegrecnIYVNFAVEPGQKLHVLlrpedlrveei 301
|
330
....*....|....*.
gi 16130591 304 -QDEDREY--GYVIER 316
Cdd:PRK09452 302 nDDEHAEGliGYVRER 317
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
44-252 |
1.54e-67 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 214.15 E-value: 1.54e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVRRKkIAMVFQSFALMPHMTV 123
Cdd:COG3638 19 LDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRRLRRR-IGMIFQQFNLVPRLSV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 124 LDN--------TAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSAL 195
Cdd:COG3638 98 LTNvlagrlgrTSTWRSLLGLFPPEDRERALEALERVGLADKAYQRADQLSGGQQQRVAIARALVQEPKLILADEPVASL 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 16130591 196 DPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEI 252
Cdd:COG3638 178 DPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRVVFDGPPAEL 234
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
5-268 |
1.64e-67 |
|
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: 214.28 E-value: 1.64e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 5 LEIKNLYKIFGEHPQRafKYIeqglskeqilektglslgVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQ 84
Cdd:COG1124 2 LEVRNLSVSYGQGGRR--VPV------------------LKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGE 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 85 VLIDGVDIAKISDAElrevRRKKIAMVFQSF--ALMPHMTVLDNTAFGMELAGINAEERRekALDALRQVGL-ENYAHSY 161
Cdd:COG1124 62 VTFDGRPVTRRRRKA----FRRRVQMVFQDPyaSLHPRHTVDRILAEPLRIHGLPDREER--IAELLEQVGLpPSFLDRY 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 162 PDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNG 241
Cdd:COG1124 136 PHQLSGGQRQRVAIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNG 215
|
250 260
....*....|....*....|....*..
gi 16130591 242 EVVQVGTPDEILNNPANDYVRTFFRGV 268
Cdd:COG1124 216 RIVEELTVADLLAGPKHPYTRELLAAS 242
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
43-252 |
1.95e-66 |
|
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: 211.27 E-value: 1.95e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVRRKkIAMVFQSFALMPHMT 122
Cdd:cd03256 16 ALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLRRQ-IGMIFQQFNLIERLS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 123 VLDNTAFGM--------ELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSA 194
Cdd:cd03256 95 VLENVLSGRlgrrstwrSLFGLFPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIARALMQQPKLILADEPVAS 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 16130591 195 LDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEI 252
Cdd:cd03256 175 LDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAEL 232
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
44-262 |
5.08e-66 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 213.05 E-value: 5.08e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVRRKkIAMVFQ-SFA-LMPHM 121
Cdd:COG4608 34 VDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELRPLRRR-MQMVFQdPYAsLNPRM 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 122 TVLDNTAFGMELAGI-NAEERREKALDALRQVGL-ENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLI 199
Cdd:COG4608 113 TVGDIIAEPLRIHGLaSKAERRERVAELLELVGLrPEHADRYPHEFSGGQRQRIGIARALALNPKLIVCDEPVSALDVSI 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16130591 200 RTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVR 262
Cdd:COG4608 193 QAQVLNLLEDLQDELGLTYLFISHDLSVVRHISDRVAVMYLGKIVEIAPRDELYARPLHPYTQ 255
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
44-257 |
1.31e-65 |
|
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: 217.46 E-value: 1.31e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPT---RGQVLIDGVDIAKISDAelreVRRKKIAMVFQSF--ALM 118
Cdd:COG1123 22 VDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEA----LRGRRIGMVFQDPmtQLN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 119 PhMTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPL 198
Cdd:COG1123 98 P-VTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPDLLIADEPTTALDVT 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 16130591 199 IRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPA 257
Cdd:COG1123 177 TQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAPQ 235
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
45-238 |
9.51e-65 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 207.41 E-value: 9.51e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 45 KDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKiSDAElREVrrkkiamVFQSFALMPHMTVL 124
Cdd:COG4525 24 QDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTG-PGAD-RGV-------VFQKDALLPWLNVL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 125 DNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQ 204
Cdd:COG4525 95 DNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLLMDEPFGALDALTREQMQ 174
|
170 180 190
....*....|....*....|....*....|....
gi 16130591 205 DELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIM 238
Cdd:COG4525 175 ELLLDVWQRTGKGVFLITHSVEEALFLATRLVVM 208
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
35-264 |
1.13e-64 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 206.42 E-value: 1.13e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 35 LEKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDaelrevRRKKIAMVFQS 114
Cdd:cd03299 6 LSKDWKEFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPP------EKRDISYVPQN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 115 FALMPHMTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSA 194
Cdd:cd03299 80 YALFPHMTVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 195 LDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTF 264
Cdd:cd03299 160 LDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPKNEFVAEF 229
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
45-268 |
4.28e-64 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 205.33 E-value: 4.28e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 45 KDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIaKISDAELREVRRKKiAMVFQSFALMPHMTVL 124
Cdd:PRK09493 18 HNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKV-NDPKVDERLIRQEA-GMVFQQFYLFPHLTAL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 125 DNTAFG-MELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTE- 202
Cdd:PRK09493 96 ENVMFGpLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTSALDPELRHEv 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16130591 203 ---MQDelvklQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFFRGV 268
Cdd:PRK09493 176 lkvMQD-----LAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPPSQRLQEFLQHV 239
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
47-264 |
1.20e-63 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 203.45 E-value: 1.20e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 47 ASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAElrevrrKKIAMVFQSFALMPHMTVLDN 126
Cdd:COG3840 18 FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAE------RPVSMLFQENNLFPHLTVAQN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 127 TAFGMELAG-INAEERrEKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQD 205
Cdd:COG3840 92 IGLGLRPGLkLTAEQR-AQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDPALRQEMLD 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 16130591 206 ELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTF 264
Cdd:COG3840 171 LVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPPALAAY 229
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
44-252 |
5.86e-63 |
|
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: 201.64 E-value: 5.86e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIE-----PTRGQVLIDGVDIAKISDAELrEVRRKkIAMVFQSfALM 118
Cdd:cd03260 16 LKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIYDLDVDVL-ELRRR-VGMVFQK-PNP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 119 PHMTVLDNTAFGMELAGI-NAEERREKALDALRQVGLENYAH--SYPDELSGGMRQRVGLARALAINPDILLMDEAFSAL 195
Cdd:cd03260 93 FPGSIYDNVAYGLRLHGIkLKEELDERVEEALRKAALWDEVKdrLHALGLSGGQQQRLCLARALANEPEVLLLDEPTSAL 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 16130591 196 DPLIRTEMQDELVKLqaKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEI 252
Cdd:cd03260 173 DPISTAKIEELIAEL--KKEYTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
5-255 |
1.05e-62 |
|
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: 202.28 E-value: 1.05e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 5 LEIKNLYkifgehpqraFKYIEQglsKEQILektglslgvKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQ 84
Cdd:TIGR04520 1 IEVENVS----------FSYPES---EKPAL---------KNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGK 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 85 VLIDGVDIAkiSDAELREVRRKkIAMVFQSfalmPH-----MTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAH 159
Cdd:TIGR04520 59 VTVDGLDTL--DEENLWEIRKK-VGMVFQN----PDnqfvgATVEDDVAFGLENLGVPREEMRKRVDEALKLVGMEDFRD 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 160 SYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRiGDRIAIMQ 239
Cdd:TIGR04520 132 REPHLLSGGQKQRVAIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEAVL-ADRVIVMN 210
|
250
....*....|....*.
gi 16130591 240 NGEVVQVGTPDEILNN 255
Cdd:TIGR04520 211 KGKIVAEGTPREIFSQ 226
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
43-252 |
1.07e-62 |
|
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: 201.76 E-value: 1.07e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVRRKkIAMVFQSFALMPHMT 122
Cdd:TIGR02315 17 ALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKLRKLRRR-IGMIFQHYNLIERLT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 123 VLDN--------TAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSA 194
Cdd:TIGR02315 96 VLENvlhgrlgyKPTWRSLLGRFSEEDKERALSALERVGLADKAYQRADQLSGGQQQRVAIARALAQQPDLILADEPIAS 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 16130591 195 LDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEI 252
Cdd:TIGR02315 176 LDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSEL 233
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
34-254 |
1.08e-62 |
|
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: 201.81 E-value: 1.08e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 34 ILEKTGLSLG------VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAElrevRRKK 107
Cdd:COG1120 1 MLEAENLSVGyggrpvLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRE----LARR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 108 IAMVFQSFALMPHMTVLDNTAFG----MELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINP 183
Cdd:COG1120 77 IAYVPQEPPAPFGLTVRELVALGryphLGLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEP 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16130591 184 DILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILN 254
Cdd:COG1120 157 PLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEVLT 227
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
5-305 |
1.50e-62 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 205.45 E-value: 1.50e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 5 LEIKNLYKIF-GEHpqrafkyieqglskeqilektglslGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRG 83
Cdd:PRK11607 20 LEIRNLTKSFdGQH-------------------------AVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 84 QVLIDGVDIAKISDaelrevRRKKIAMVFQSFALMPHMTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPD 163
Cdd:PRK11607 75 QIMLDGVDLSHVPP------YQRPINMMFQSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPH 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 164 ELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEV 243
Cdd:PRK11607 149 QLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKF 228
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16130591 244 VQVGTPDEILNNPANDYVRTFFRGVDisqVFSAKdIARRTPNGLIRKTPGFgpRSALKLLQD 305
Cdd:PRK11607 229 VQIGEPEEIYEHPTTRYSAEFIGSVN---VFEGV-LKERQEDGLVIDSPGL--VHPLKVDAD 284
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
45-242 |
5.51e-62 |
|
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: 198.46 E-value: 5.51e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 45 KDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELRevrrKKIAMVFQSFA---LMPhm 121
Cdd:cd03225 18 DDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELR----RKVGLVFQNPDdqfFGP-- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 122 TVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRT 201
Cdd:cd03225 92 TVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDPAGRR 171
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 16130591 202 EMQDELVKLQAKHQrTIVFISHDLDEAMRIGDRIAIMQNGE 242
Cdd:cd03225 172 ELLELLKKLKAEGK-TIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1-264 |
2.19e-61 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 201.85 E-value: 2.19e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 1 MAIklEIKNLYKIFGehpqrafkyieqglsKEQILektglslgvKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEP 80
Cdd:PRK10851 1 MSI--EIANIKKSFG---------------RTQVL---------NDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQ 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 81 TRGQVLIDGVDIAKISdaelreVRRKKIAMVFQSFALMPHMTVLDNTAFGMEL----AGINAEERREKALDALRQVGLEN 156
Cdd:PRK10851 55 TSGHIRFHGTDVSRLH------ARDRKVGFVFQHYALFRHMTVFDNIAFGLTVlprrERPNAAAIKAKVTQLLEMVQLAH 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 157 YAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIA 236
Cdd:PRK10851 129 LADRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVV 208
|
250 260
....*....|....*....|....*...
gi 16130591 237 IMQNGEVVQVGTPDEILNNPANDYVRTF 264
Cdd:PRK10851 209 VMSQGNIEQAGTPDQVWREPATRFVLEF 236
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
27-247 |
6.06e-61 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 196.43 E-value: 6.06e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 27 QGLSKEQILEKTGLSlgvkDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVRRK 106
Cdd:COG2884 5 ENVSKRYPGGREALS----DVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 107 kIAMVFQSFALMPHMTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDIL 186
Cdd:COG2884 81 -IGVVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16130591 187 LMDEAFSALDPlirtEMQDELVKL-QAKHQR--TIVFISHDLDEAMRIGDRIAIMQNGEVVQVG 247
Cdd:COG2884 160 LADEPTGNLDP----ETSWEIMELlEEINRRgtTVLIATHDLELVDRMPKRVLELEDGRLVRDE 219
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
44-263 |
2.58e-60 |
|
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: 203.76 E-value: 2.58e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIePTRGQVLIDGVDIAKISDAELREVRRKkIAMVFQS-FA-LMPHM 121
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLI-PSEGEIRFDGQDLDGLSRRALRPLRRR-MQVVFQDpFGsLSPRM 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 122 TVLDNTAFGMEL--AGINAEERREKALDALRQVGL-ENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPL 198
Cdd:COG4172 380 TVGQIIAEGLRVhgPGLSAAERRARVAEALEEVGLdPAARHRYPHEFSGGQRQRIAIARALILEPKLLVLDEPTSALDVS 459
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16130591 199 IRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRT 263
Cdd:COG4172 460 VQAQILDLLRDLQREHGLAYLFISHDLAVVRALAHRVMVMKDGKVVEQGPTEQVFDAPQHPYTRA 524
|
|
| ABC_arch_GlcV |
NF040933 |
glucose ABC transporter ATP-binding protein GlcV; |
44-265 |
2.94e-60 |
|
glucose ABC transporter ATP-binding protein GlcV;
Pssm-ID: 468866 [Multi-domain] Cd Length: 357 Bit Score: 199.07 E-value: 2.94e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELrEVRRKKIAMVFQSFALMPHMTV 123
Cdd:NF040933 22 LDNVNLEIKSGEFFGILGPSGHGKTTFLRIIAGLEVPTDGEIYFDDKLVASPGKIIV-PPEDRNIGMVFQNWALYPNMTV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 124 LDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRtEM 203
Cdd:NF040933 101 FDNIAFPLKIKKVPKDEIEKKVKEVAEILGISEVLDRYPRELSGGQQQRVALARALVKNPQVLLLDEPFSNLDARIR-DS 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16130591 204 QDELVK-LQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFF 265
Cdd:NF040933 180 ARALVKkIQRELKITTIIVSHDPADIFSLADRAGVINNGKFQQVGKPEEIYDNPANIFVARLI 242
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
27-265 |
1.09e-57 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 188.53 E-value: 1.09e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 27 QGLSKeqileKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAelrevRRK 106
Cdd:COG4555 5 ENLSK-----KYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPRE-----ARR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 107 KIAMVFQSFALMPHMTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDIL 186
Cdd:COG4555 75 QIGVLPDERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16130591 187 LMDEAFSALDPLIRTEMQDELVKLqAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFF 265
Cdd:COG4555 155 LLDEPTNGLDVMARRLLREILRAL-KKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREEIGEENLEDAF 232
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
5-262 |
7.73e-57 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 187.35 E-value: 7.73e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 5 LEIKNLYKIFGEHpqrafkyieQGLSKEQILEktglslGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQ 84
Cdd:COG4167 5 LEVRNLSKTFKYR---------TGLFRRQQFE------AVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 85 VLIDGVDIAKISDAelreVRRKKIAMVFQ--SFALMPHMTV---LD-----NTAFgmelagiNAEERREKALDALRQVGL 154
Cdd:COG4167 70 ILINGHKLEYGDYK----YRCKHIRMIFQdpNTSLNPRLNIgqiLEeplrlNTDL-------TAEEREERIFATLRLVGL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 155 -ENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGD 233
Cdd:COG4167 139 lPEHANFYPHMLSSGQKQRVALARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKHISD 218
|
250 260
....*....|....*....|....*....
gi 16130591 234 RIAIMQNGEVVQVGTPDEILNNPANDYVR 262
Cdd:COG4167 219 KVLVMHQGEVVEYGKTAEVFANPQHEVTK 247
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
44-264 |
1.57e-56 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 189.16 E-value: 1.57e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKisdaelREVRRKKIAMVFQSFALMPHMTV 123
Cdd:PRK11432 22 IDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTH------RSIQQRDICMVFQSYALFPHMSL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 124 LDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEM 203
Cdd:PRK11432 96 GENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSM 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16130591 204 QDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTF 264
Cdd:PRK11432 176 REKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPASRFMASF 236
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
44-262 |
2.00e-56 |
|
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: 193.36 E-value: 2.00e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 44 VKDASLAIEEGEIFVIMGLSGSGKS----TMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVRRKKIAMVFQ--SFAL 117
Cdd:COG4172 26 VKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERELRRIRGNRIAMIFQepMTSL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 118 MPHMTVLDNTAFGMEL-AGINAEERREKALDALRQVGL---ENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFS 193
Cdd:COG4172 106 NPLHTIGKQIAEVLRLhRGLSGAAARARALELLERVGIpdpERRLDAYPHQLSGGQRQRVMIAMALANEPDLLIADEPTT 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16130591 194 ALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVR 262
Cdd:COG4172 186 ALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFADRVAVMRQGEIVEQGPTAELFAAPQHPYTR 254
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
2-267 |
5.34e-56 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 184.62 E-value: 5.34e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 2 AIKLEIKNLYKIFGEHpqrafkyieqglskeQILektglslgvKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPT 81
Cdd:COG4598 6 PPALEVRDLHKSFGDL---------------EVL---------KGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPD 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 82 RGQVLIDGVDIAKISD-------AELREVR--RKKIAMVFQSFALMPHMTVLDNTAFG-MELAGINAEERREKALDALRQ 151
Cdd:COG4598 62 SGEIRVGGEEIRLKPDrdgelvpADRRQLQriRTRLGMVFQSFNLWSHMTVLENVIEApVHVLGRPKAEAIERAEALLAK 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 152 VGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPlirtEMQDELVKLQ---AKHQRTIVFISHDLDEA 228
Cdd:COG4598 142 VGLADKRDAYPAHLSGGQQQRAAIARALAMEPEVMLFDEPTSALDP----ELVGEVLKVMrdlAEEGRTMLVVTHEMGFA 217
|
250 260 270
....*....|....*....|....*....|....*....
gi 16130591 229 MRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFFRG 267
Cdd:COG4598 218 RDVSSHVVFLHQGRIEEQGPPAEVFGNPKSERLRQFLSS 256
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
44-257 |
7.05e-56 |
|
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: 184.47 E-value: 7.05e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDaelREVRRKKIAMVFQSFALMPHMTV 123
Cdd:COG0411 20 VDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPP---HRIARLGIARTFQNPRLFPELTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 124 LDNTAFGME-------------LAGINAEER--REKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLM 188
Cdd:COG0411 97 LENVLVAAHarlgrgllaallrLPRARREEReaRERAEELLERVGLADRADEPAGNLSYGQQRRLEIARALATEPKLLLL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16130591 189 DEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPA 257
Cdd:COG0411 177 DEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGTPAEVRADPR 245
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
44-261 |
1.55e-55 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 183.70 E-value: 1.55e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIE--P---TRGQVLIDGVDI--AKISDAELRevrrKKIAMVFQS-- 114
Cdd:COG1117 27 LKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDliPgarVEGEILLDGEDIydPDVDVVELR----RRVGMVFQKpn 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 115 -FAlmphMTVLDNTAFGMELAGI-NAEERREKALDALRQVGLenyahsyPDE-----------LSGGMRQRVGLARALAI 181
Cdd:COG1117 103 pFP----KSIYDNVAYGLRLHGIkSKSELDEIVEESLRKAAL-------WDEvkdrlkksalgLSGGQQQRLCIARALAV 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 182 NPDILLMDEAFSALDPlIRTEMQDELVkLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPAN--- 258
Cdd:COG1117 172 EPEVLLMDEPTSALDP-ISTAKIEELI-LELKKDYTIVIVTHNMQQAARVSDYTAFFYLGELVEFGPTEQIFTNPKDkrt 249
|
....
gi 16130591 259 -DYV 261
Cdd:COG1117 250 eDYI 253
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
45-264 |
3.90e-55 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 186.00 E-value: 3.90e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 45 KDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAElrevrrKKIAMVFQSFALMPHMTVL 124
Cdd:PRK11000 20 KDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAE------RGVGMVFQSYALYPHLSVA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 125 DNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQ 204
Cdd:PRK11000 94 ENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRVQMR 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 205 DELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTF 264
Cdd:PRK11000 174 IEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPANRFVAGF 233
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
44-252 |
1.10e-53 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 179.44 E-value: 1.10e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVdiaKISDAELREVRRKkIAMVFQSfalmPH--- 120
Cdd:PRK13635 23 LKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGM---VLSEETVWDVRRQ-VGMVFQN----PDnqf 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 121 --MTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPL 198
Cdd:PRK13635 95 vgATVQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPR 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 16130591 199 IRTEMQDELVKLQAKHQRTIVFISHDLDEAMRiGDRIAIMQNGEVVQVGTPDEI 252
Cdd:PRK13635 175 GRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEI 227
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
44-257 |
1.32e-53 |
|
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: 177.63 E-value: 1.32e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDaelREVRRKKIAMVFQSFALMPHMTV 123
Cdd:cd03219 16 LDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPP---HEIARLGIGRTFQIPRLFPELTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 124 LDN----------TAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFS 193
Cdd:cd03219 93 LENvmvaaqartgSGLLLARARREEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALATDPKLLLLDEPAA 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16130591 194 ALDPLIRTEMQDELVKLqAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPA 257
Cdd:cd03219 173 GLNPEETEELAELIREL-RERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRNNPR 235
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
5-252 |
3.47e-53 |
|
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: 176.16 E-value: 3.47e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 5 LEIKNLYKIFGEHPQRAfkyieqglskeqilektglslgVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQ 84
Cdd:cd03263 1 LQIRNLTKTYKKGTKPA----------------------VDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGT 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 85 VLIDGVDIAKisdaELREVRRKkIAMVFQSFALMPHMTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDE 164
Cdd:cd03263 59 AYINGYSIRT----DRKAARQS-LGYCPQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRART 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 165 LSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLqaKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVV 244
Cdd:cd03263 134 LSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPASRRAIWDLILEV--RKGRSIILTTHSMDEAEALCDRIAIMSDGKLR 211
|
....*...
gi 16130591 245 QVGTPDEI 252
Cdd:cd03263 212 CIGSPQEL 219
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
5-243 |
1.34e-52 |
|
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: 172.97 E-value: 1.34e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 5 LEIKNLYKIFGEHPqrafkyieqglskeqilektglslGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQ 84
Cdd:cd03230 1 IEVRNLSKRYGKKT------------------------ALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGE 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 85 VLIDGVDIAKisdaELREVRRKkIAMVFQSFALMPHMTVLDNTafgmelaginaeerrekaldalrqvglenyahsypdE 164
Cdd:cd03230 57 IKVLGKDIKK----EPEEVKRR-IGYLPEEPSLYENLTVRENL------------------------------------K 95
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16130591 165 LSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLqAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEV 243
Cdd:cd03230 96 LSGGMKQRLALAQALLHDPELLILDEPTSGLDPESRREFWELLREL-KKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
45-243 |
1.36e-51 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 171.54 E-value: 1.36e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 45 KDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELRevrrKKIAMVFQSFALMPhMTVL 124
Cdd:COG4619 17 SPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWR----RQVAYVPQEPALWG-GTVR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 125 DNTAFGMELAGINAEerREKALDALRQVGL-ENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEM 203
Cdd:COG4619 92 DNLPFPFQLRERKFD--RERALELLERLGLpPDILDKPVERLSGGERQRLALIRALLLQPDVLLLDEPTSALDPENTRRV 169
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 16130591 204 QDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEV 243
Cdd:COG4619 170 EELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
45-251 |
2.35e-51 |
|
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: 171.85 E-value: 2.35e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 45 KDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVRRKKIAMVFQSFALMPHMTVL 124
Cdd:COG4181 29 KGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDARARLRARHVGFVFQSFQLLPTLTAL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 125 DNTAFGMELAGinAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQ 204
Cdd:COG4181 109 ENVMLPLELAG--RRDARARARALLERVGLGHRLDHYPAQLSGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQII 186
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 16130591 205 DELVKLQAKHQRTIVFISHDLDEAMRIgDRIAIMQNGEVVQVGTPDE 251
Cdd:COG4181 187 DLLFELNRERGTTLVLVTHDPALAARC-DRVLRLRAGRLVEDTAATA 232
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
44-255 |
5.23e-51 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 172.10 E-value: 5.23e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIakiSDAELREVRrKKIAMVFQSfalmPH--- 120
Cdd:PRK13632 25 LKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITI---SKENLKEIR-KKIGIIFQN----PDnqf 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 121 --MTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPL 198
Cdd:PRK13632 97 igATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFDESTSMLDPK 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 16130591 199 IRTEMQDELVKLQAKHQRTIVFISHDLDEAMrIGDRIAIMQNGEVVQVGTPDEILNN 255
Cdd:PRK13632 177 GKREIKKIMVDLRKTRKKTLISITHDMDEAI-LADKVIVFSEGKLIAQGKPKEILNN 232
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
44-254 |
1.84e-50 |
|
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: 180.42 E-value: 1.84e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELrevrRKKIAMVFQSFALMpHMTV 123
Cdd:COG2274 491 LDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASL----RRQIGVVLQDVFLF-SGTI 565
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 124 LDNTAFGMELAGInaeerrEKALDALRQVGLENYAHSYPD-----------ELSGGMRQRVGLARALAINPDILLMDEAF 192
Cdd:COG2274 566 RENITLGDPDATD------EEIIEAARLAGLHDFIEALPMgydtvvgeggsNLSGGQRQRLAIARALLRNPRILILDEAT 639
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16130591 193 SALDPLIRTEMQDELvkLQAKHQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEILN 254
Cdd:COG2274 640 SALDAETEAIILENL--RRLLKGRTVIIIAHRL-STIRLADRIIVLDKGRIVEDGTHEELLA 698
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
44-255 |
2.88e-50 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 178.05 E-value: 2.88e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELrevrRKKIAMVFQSFALMpHMTV 123
Cdd:COG1132 356 LKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESL----RRQIGVVPQDTFLF-SGTI 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 124 LDNTAFGmelagiNAEERREKALDALRQVGLENYAHSYPD-----------ELSGGMRQRVGLARALAINPDILLMDEAF 192
Cdd:COG1132 431 RENIRYG------RPDATDEEVEEAAKAAQAHEFIEALPDgydtvvgergvNLSGGQRQRIAIARALLKDPPILILDEAT 504
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16130591 193 SALDPliRTEM--QDELVKLqaKHQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEILNN 255
Cdd:COG1132 505 SALDT--ETEAliQEALERL--MKGRTTIVIAHRL-STIRNADRILVLDDGRIVEQGTHEELLAR 564
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
44-264 |
3.89e-50 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 172.34 E-value: 3.89e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAElrevrrKKIAMVFQSFALMPHMTV 123
Cdd:PRK11650 20 IKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPAD------RDIAMVFQNYALYPHMSV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 124 LDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEM 203
Cdd:PRK11650 94 RENMAYGLKIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDAKLRVQM 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16130591 204 QDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTF 264
Cdd:PRK11650 174 RLEIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGGVAEQIGTPVEVYEKPASTFVASF 234
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
44-256 |
5.54e-50 |
|
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: 168.41 E-value: 5.54e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELrevrrkkiaMVFQSFALMPHMTV 123
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRM---------VVFQNYSLLPWLTV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 124 LDNTAFGME--LAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRT 201
Cdd:TIGR01184 72 RENIALAVDrvLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRG 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 16130591 202 EMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGtpdEILNNP 256
Cdd:TIGR01184 152 NLQEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAANIG---QILEVP 203
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
46-289 |
1.47e-49 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 171.05 E-value: 1.47e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 46 DASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDG---VDIAKISDaelREVRRKKIAMVFQSFALMPHMT 122
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGevlQDSARGIF---LPPHRRRIGYVFQEARLFPHLS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 123 VLDNTAFGMELAGinAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTE 202
Cdd:COG4148 94 VRGNLLYGRKRAP--RAERRISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAE 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 203 MQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPAndyVRTFFRGVDISQVFSAKDIARR 282
Cdd:COG4148 172 ILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRPD---LLPLAGGEEAGSVLEATVAAHD 248
|
....*..
gi 16130591 283 TPNGLIR 289
Cdd:COG4148 249 PDYGLTR 255
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
32-252 |
1.60e-49 |
|
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: 166.78 E-value: 1.60e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 32 EQILEKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKisdaELREVRRKkIAMV 111
Cdd:cd03265 4 ENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR----EPREVRRR-IGIV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 112 FQSFALMPHMTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEA 191
Cdd:cd03265 79 FQDLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16130591 192 FSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEI 252
Cdd:cd03265 159 TIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
46-229 |
1.69e-49 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 167.95 E-value: 1.69e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 46 DASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISdAElREVrrkkiamVFQSFALMPHMTVLD 125
Cdd:PRK11248 19 DINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPG-AE-RGV-------VFQNEGLLPWRNVQD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 126 NTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQD 205
Cdd:PRK11248 90 NVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQMQT 169
|
170 180
....*....|....*....|....
gi 16130591 206 ELVKLQAKHQRTIVFISHDLDEAM 229
Cdd:PRK11248 170 LLLKLWQETGKQVLLITHDIEEAV 193
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
44-254 |
2.53e-49 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 166.80 E-value: 2.53e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKisdaelrevRRKKIAMVFQSFALMPH--M 121
Cdd:COG1121 22 LEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRR---------ARRRIGYVPQRAEVDWDfpI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 122 TVLDNTAFG----MELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDP 197
Cdd:COG1121 93 TVRDVVLMGrygrRGLFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDA 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 198 lirtEMQDELVKL---QAKHQRTIVFISHDLDEAMRIGDRIAIMqNGEVVQVGTPDEILN 254
Cdd:COG1121 173 ----ATEEALYELlreLRREGKTILVVTHDLGAVREYFDRVLLL-NRGLVAHGPPEEVLT 227
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
53-247 |
2.87e-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: 165.93 E-value: 2.87e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 53 EGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVRRKKIAMVFQSFALMPHMTVLDNTAFGME 132
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRKKINLPPQQRKIGLVFQQYALFPHLNVRENLAFGLK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 133 LAGINAEERREKALDALrqVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQA 212
Cdd:cd03297 102 RKRNREDRISVDELLDL--LGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELKQIKK 179
|
170 180 190
....*....|....*....|....*....|....*
gi 16130591 213 KHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVG 247
Cdd:cd03297 180 NLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
1-256 |
7.53e-49 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 165.57 E-value: 7.53e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 1 MAIKLeiKNLYKIFGEHpqrafkyieqglskeQILektglslgvKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEP 80
Cdd:COG4161 1 MSIQL--KNINCFYGSH---------------QAL---------FDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETP 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 81 TRGQVLIDGVDI---AKISDAELREVRRKkIAMVFQSFALMPHMTVLDN-TAFGMELAGINAEERREKALDALRQVGLEN 156
Cdd:COG4161 55 DSGQLNIAGHQFdfsQKPSEKAIRLLRQK-VGMVFQQYNLWPHLTVMENlIEAPCKVLGLSKEQAREKAMKLLARLRLTD 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 157 YAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQdELVKLQAKHQRTIVFISHDLDEAMRIGDRIA 236
Cdd:COG4161 134 KADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQVV-EIIRELSQTGITQVIVTHEVEFARKVASQVV 212
|
250 260
....*....|....*....|
gi 16130591 237 IMQNGEVVQVGTPdEILNNP 256
Cdd:COG4161 213 YMEKGRIIEQGDA-SHFTQP 231
|
|
| CBS_pair_ABC_Gly_Pro_assoc |
cd09831 |
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found associated with ... |
278-393 |
1.03e-48 |
|
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found associated with the glycine betaine/L-proline ABC transporter; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in association with the ABC transporter OpuCA. OpuCA is the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment but the function of the CBS domains in OpuCA remains unknown. In the related ABC transporter, OpuA, the tandem CBS domains have been shown to function as sensors for ionic strength, whereby they control the transport activity through an electronic switching mechanism. 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. They 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. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).
Pssm-ID: 341402 [Multi-domain] Cd Length: 116 Bit Score: 160.80 E-value: 1.03e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 278 DIARRTPNGLIRKTpGFGPRSALKLLQDEDREYGYVIERGNKFVGAVSIDSLKTALTQQ-QGLDAALIDAPLAVDAQTPL 356
Cdd:cd09831 1 DIARKTQVTVIEKT-GDGPRAALQLLREHDREYGYVVDKKRRFLGVVSVDSLRAALKENaQSLEDAFLTDVETVPADTSL 79
|
90 100 110
....*....|....*....|....*....|....*..
gi 16130591 357 SELLSHVGQAPCAVPVVDEDQQYVGIISKGMLLRALD 393
Cdd:cd09831 80 SDILGLVASAPCPLPVVDEDGRYLGVISKASLLETLD 116
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
35-247 |
2.07e-48 |
|
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: 163.43 E-value: 2.07e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 35 LEKTGLSLGVK--DASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKIsdaelrEVRRKKIAMVF 112
Cdd:cd03298 3 LDKIRFSYGEQpmHFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAA------PPADRPVSMLF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 113 QSFALMPHMTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAF 192
Cdd:cd03298 77 QENNLFAHLTVEQNVGLGLSPGLKLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPF 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 16130591 193 SALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVG 247
Cdd:cd03298 157 AALDPALRAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
44-247 |
4.63e-47 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 158.75 E-value: 4.63e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAElrevRRKKIAMVFQsfalmphmtv 123
Cdd:cd03214 15 LDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKE----LARKIAYVPQ---------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 124 ldntafgmelaginaeerrekaldALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEM 203
Cdd:cd03214 81 ------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQIEL 136
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 16130591 204 QDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVG 247
Cdd:cd03214 137 LELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| ectoine_ehuA |
TIGR03005 |
ectoine/hydroxyectoine ABC transporter, ATP-binding protein; Members of this family are the ... |
47-268 |
7.19e-47 |
|
ectoine/hydroxyectoine ABC transporter, ATP-binding protein; Members of this family are the ATP-binding protein of a conserved four gene ABC transporter operon found next to ectoine unilization operons and ectoine biosynthesis operons. Ectoine is a compatible solute that protects enzymes from high osmolarity. It is released by some species in response to hypoosmotic shock, and it is taken up by a number of bacteria as a compatible solute or for consumption. This family shows strong sequence similiarity to a number of amino acid ABC transporter ATP-binding proteins.
Pssm-ID: 132050 [Multi-domain] Cd Length: 252 Bit Score: 160.77 E-value: 7.19e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 47 ASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDI-------AKISDAELREVR--RKKIAMVFQSFAL 117
Cdd:TIGR03005 19 LNFSVAAGEKVALIGPSGSGKSTILRILMTLEPIDEGQIQVEGEQLyhmpgrnGPLVPADEKHLRqmRNKIGMVFQSFNL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 118 MPHMTVLDN-TAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALD 196
Cdd:TIGR03005 99 FPHKTVLDNvTEAPVLVLGMARAEAEKRAMELLDMVGLADKADHMPAQLSGGQQQRVAIARALAMRPKVMLFDEVTSALD 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16130591 197 PLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFFRGV 268
Cdd:TIGR03005 179 PELVGEVLNVIRRLASEHDLTMLLVTHEMGFAREFADRVCFFDKGRIVEQGKPDEIFRQPKEERTREFLSKV 250
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
48-262 |
1.14e-46 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 162.44 E-value: 1.14e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNrLIE-PTRGQVLIDGVDIAKiSDAELREVRRKKIAMVFQS-FA-LMPHMTV- 123
Cdd:PRK11308 35 SFTLERGKTLAVVGESGCGKSTLARLLT-MIEtPTGGELYYQGQDLLK-ADPEAQKLLRQKIQIVFQNpYGsLNPRKKVg 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 124 -------LDNTAfgmelagINAEERREKALDALRQVGL--ENYaHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSA 194
Cdd:PRK11308 113 qileeplLINTS-------LSAAERREKALAMMAKVGLrpEHY-DRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSA 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16130591 195 LDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVR 262
Cdd:PRK11308 185 LDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFNNPRHPYTQ 252
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
44-193 |
6.04e-46 |
|
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: 155.11 E-value: 6.04e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISdaelREVRRKKIAMVFQSFALMPHMTV 123
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDE----RKSLRKEIGYVFQDPQLFPRLTV 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16130591 124 LDNTAFGMELAGINAEERREKALDALRQVGLENYAH----SYPDELSGGMRQRVGLARALAINPDILLMDEAFS 193
Cdd:pfam00005 77 RENLRLGLLLKGLSKREKDARAEEALEKLGLGDLADrpvgERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
44-242 |
7.56e-46 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 155.23 E-value: 7.56e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELrevrRKKIAMVFQSFALMpHMTV 123
Cdd:cd03228 18 LKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESL----RKNIAYVPQDPFLF-SGTI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 124 LDNtafgmelagInaeerrekaldalrqvglenyahsypdeLSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEM 203
Cdd:cd03228 93 REN---------I----------------------------LSGGQRQRIAIARALLRDPPILILDEATSALDPETEALI 135
|
170 180 190
....*....|....*....|....*....|....*....
gi 16130591 204 QDELVKLqaKHQRTIVFISHDLdEAMRIGDRIAIMQNGE 242
Cdd:cd03228 136 LEALRAL--AKGKTVIVIAHRL-STIRDADRIIVLDDGR 171
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
44-247 |
1.20e-45 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 156.15 E-value: 1.20e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKisdaelrevRRKKIAMVFQSFAL---MPh 120
Cdd:cd03235 15 LEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEK---------ERKRIGYVPQRRSIdrdFP- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 121 MTVLDNTAFG----MELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALD 196
Cdd:cd03235 85 ISVRDVVLMGlyghKGLFRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAGVD 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 16130591 197 PlirtEMQDELVKL---QAKHQRTIVFISHDLDEAMRIGDRIAIMqNGEVVQVG 247
Cdd:cd03235 165 P----KTQEDIYELlreLRREGMTILVVTHDLGLVLEYFDRVLLL-NRTVVASG 213
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
46-250 |
1.30e-45 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 157.10 E-value: 1.30e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 46 DASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDG--VDIAK-ISDAELREVRRKkIAMVFQSFALMPHMT 122
Cdd:PRK11124 20 DITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGnhFDFSKtPSDKAIRELRRN-VGMVFQQYNLWPHLT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 123 VLDN-TAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRT 201
Cdd:PRK11124 99 VQQNlIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITA 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 16130591 202 EMQDELVKLQAKHQrTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPD 250
Cdd:PRK11124 179 QIVSIIRELAETGI-TQVIVTHEVEVARKTASRVVYMENGHIVEQGDAS 226
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
46-243 |
1.98e-45 |
|
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: 156.03 E-value: 1.98e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 46 DASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVRRKkIAMVFQSFALMPHMTVLD 125
Cdd:cd03292 19 GINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYLRRK-IGVVFQDFRLLPDRNVYE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 126 NTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQD 205
Cdd:cd03292 98 NVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTTWEIMN 177
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 16130591 206 ELVKLqakHQR--TIVFISHDLDEAMRIGDRIAIMQNGEV 243
Cdd:cd03292 178 LLKKI---NKAgtTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
44-242 |
2.07e-45 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 153.94 E-value: 2.07e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELRevrrKKIAMVFQsfalmphmtv 123
Cdd:cd00267 15 LDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELR----RRIGYVPQ---------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 124 ldntafgmelaginaeerrekaldalrqvglenyahsypdeLSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEM 203
Cdd:cd00267 81 -----------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERL 119
|
170 180 190
....*....|....*....|....*....|....*....
gi 16130591 204 QDELVKLqAKHQRTIVFISHDLDEAMRIGDRIAIMQNGE 242
Cdd:cd00267 120 LELLREL-AEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
44-255 |
3.55e-45 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 157.52 E-value: 3.55e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKiSDAELREVRrKKIAMVFQ--SFALMPHm 121
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITD-KKVKLSDIR-KKVGLVFQypEYQLFEE- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 122 TVLDNTAFGMELAGINAEERREKALDALRQVGL--ENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLI 199
Cdd:PRK13637 100 TIEKDIAFGPINLGLSEEEIENRVKRAMNIVGLdyEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKG 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 16130591 200 RTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNN 255
Cdd:PRK13637 180 RDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVFKE 235
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
44-252 |
6.78e-45 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 156.43 E-value: 6.78e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGvdiAKISDAELREVRRKkIAMVFQSfalmPH--- 120
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDG---DLLTEENVWDIRHK-IGMVFQN----PDnqf 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 121 --MTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPL 198
Cdd:PRK13650 95 vgATVEDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPE 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 16130591 199 IRTEMQDELVKLQAKHQRTIVFISHDLDEaMRIGDRIAIMQNGEVVQVGTPDEI 252
Cdd:PRK13650 175 GRLELIKTIKGIRDDYQMTVISITHDLDE-VALSDRVLVMKNGQVESTSTPREL 227
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
22-273 |
9.14e-45 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 156.02 E-value: 9.14e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 22 FKYIEQGLSKEQIlektglslGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDaeLR 101
Cdd:PRK13633 12 YKYESNEESTEKL--------ALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEEN--LW 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 102 EVRRKKiAMVFQSfalmPH-----MTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLA 176
Cdd:PRK13633 82 DIRNKA-GMVFQN----PDnqivaTIVEEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 177 RALAINPDILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRiGDRIAIMQNGEVVQVGTPDEILNNp 256
Cdd:PRK13633 157 GILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIFKE- 234
|
250
....*....|....*...
gi 16130591 257 andyVRTFFR-GVDISQV 273
Cdd:PRK13633 235 ----VEMMKKiGLDVPQV 248
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
4-267 |
2.31e-44 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 154.36 E-value: 2.31e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 4 KLEIKNLYKIFGEHpqrafkyieqglskeQILektglslgvKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRG 83
Cdd:PRK10619 5 KLNVIDLHKRYGEH---------------EVL---------KGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEG 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 84 QVLIDGVDIA---------KISDAELREVRRKKIAMVFQSFALMPHMTVLDNTAFG-MELAGINAEERREKALDALRQVG 153
Cdd:PRK10619 61 SIVVNGQTINlvrdkdgqlKVADKNQLRLLRTRLTMVFQHFNLWSHMTVLENVMEApIQVLGLSKQEARERAVKYLAKVG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 154 LENYAH-SYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLqAKHQRTIVFISHDLDEAMRIG 232
Cdd:PRK10619 141 IDERAQgKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQL-AEEGKTMVVVTHEMGFARHVS 219
|
250 260 270
....*....|....*....|....*....|....*
gi 16130591 233 DRIAIMQNGEVVQVGTPDEILNNPANDYVRTFFRG 267
Cdd:PRK10619 220 SHVIFLHQGKIEEEGAPEQLFGNPQSPRLQQFLKG 254
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
44-270 |
8.13e-44 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 155.25 E-value: 8.13e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVRrKKIAMVFQS--FALMPHM 121
Cdd:PRK15079 37 VDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRAVR-SDIQMIFQDplASLNPRM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 122 TVLDNTA-----FGMELAginAEERREKALDALRQVGL-ENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSAL 195
Cdd:PRK15079 116 TIGEIIAeplrtYHPKLS---RQEVKDRVKAMMLKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSAL 192
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16130591 196 DPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFFRGVDI 270
Cdd:PRK15079 193 DVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNPLHPYTKALMSAVPI 267
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
42-257 |
1.57e-43 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 153.25 E-value: 1.57e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 42 LGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLI-DGVDIAKISDAELREVRrKKIAMVFQsFAlmPH 120
Cdd:PRK13634 21 RALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIgERVITAGKKNKKLKPLR-KKVGIVFQ-FP--EH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 121 M----TVLDNTAFGMELAGINAEERREKALDALRQVGL-ENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSAL 195
Cdd:PRK13634 97 QlfeeTVEKDICFGPMNFGVSEEDAKQKAREMIELVGLpEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16130591 196 DPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPA 257
Cdd:PRK13634 177 DPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADPD 238
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
44-257 |
2.69e-43 |
|
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: 158.78 E-value: 2.69e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVrrkkIAMVFQSFALMpHMTV 123
Cdd:COG4987 351 LDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRR----IAVVPQRPHLF-DTTL 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 124 LDNTAfgmeLAGINAEErrEKALDALRQVGLENYAHSYPD-----------ELSGGMRQRVGLARALAINPDILLMDEAF 192
Cdd:COG4987 426 RENLR----LARPDATD--EELWAALERVGLGDWLAALPDgldtwlgeggrRLSGGERRRLALARALLRDAPILLLDEPT 499
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16130591 193 SALDPLIRTEMQDELvkLQAKHQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEILNNPA 257
Cdd:COG4987 500 EGLDAATEQALLADL--LEALAGRTVLLITHRL-AGLERMDRILVLEDGRIVEQGTHEELLAQNG 561
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
34-251 |
4.12e-43 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 149.55 E-value: 4.12e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 34 ILEKTGLSLG----VKDASLAIEEGEIFVIMGLSGSGKSTmvrLLNRLI---EP---TRGQVLIDGVDIAKISdaelreV 103
Cdd:COG4136 3 SLENLTITLGgrplLAPLSLTVAPGEILTLMGPSGSGKST---LLAAIAgtlSPafsASGEVLLNGRRLTALP------A 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 104 RRKKIAMVFQSFALMPHMTVLDNTAFGMElAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINP 183
Cdd:COG4136 74 EQRRIGILFQDDLLFPHLSVGENLAFALP-PTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEP 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16130591 184 DILLMDEAFSALDPLIRTEMQdELVKLQAKHQRTIV-FISHDLDEAmrigdriaiMQNGEVVQVGTPDE 251
Cdd:COG4136 153 RALLLDEPFSKLDAALRAQFR-EFVFEQIRQRGIPAlLVTHDEEDA---------PAAGRVLDLGNWQH 211
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
44-268 |
4.77e-43 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 150.76 E-value: 4.77e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIE-----PTRGQVLIDGVDIAKiSDAELREVRRKkIAMVFQSFALM 118
Cdd:PRK14267 20 IKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElneeaRVEGEVRLFGRNIYS-PDVDPIEVRRE-VGMVFQYPNPF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 119 PHMTVLDNTAFGMELAGI--NAEERREKALDALRQVGL----ENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAF 192
Cdd:PRK14267 98 PHLTIYDNVAIGVKLNGLvkSKKELDERVEWALKKAALwdevKDRLNDYPSNLSGGQRQRLVIARALAMKPKILLMDEPT 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16130591 193 SALDPLIRTEMQDELVKLqaKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFFRGV 268
Cdd:PRK14267 178 ANIDPVGTAKIEELLFEL--KKEYTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENPEHELTEKYVTGA 251
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
48-254 |
7.92e-43 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 149.73 E-value: 7.92e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAelrevrRKKIAMVFQSFALMPHMTVLDNT 127
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPS------RRPVSMLFQENNLFSHLTVAQNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 128 AFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDEL 207
Cdd:PRK10771 93 GLGLNPGLKLNAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLV 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 16130591 208 VKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILN 254
Cdd:PRK10771 173 SQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELLS 219
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
46-278 |
1.05e-42 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 152.96 E-value: 1.05e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 46 DASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVRRKKIAMVFQSFALMPHMTVLD 125
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKGIFLPPEKRRIGYVFQEARLFPHLSVRG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 126 NTAFGMELAgiNAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQD 205
Cdd:TIGR02142 95 NLRYGMKRA--RPSERRISFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILP 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16130591 206 ELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFFRGVDISQVFSAKD 278
Cdd:TIGR02142 173 YLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPDLPWLAREDQGSLIEGVVAEHD 245
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
45-243 |
1.10e-42 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 150.21 E-value: 1.10e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 45 KDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKIsdaelrevrRKKIAMVFQSFALMPHMTVL 124
Cdd:PRK11247 29 NQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEA---------REDTRLMFQDARLLPWKKVI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 125 DNTAFGmeLAGinaeERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQ 204
Cdd:PRK11247 100 DNVGLG--LKG----QWRDAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRIEMQ 173
|
170 180 190
....*....|....*....|....*....|....*....
gi 16130591 205 DELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEV 243
Cdd:PRK11247 174 DLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
49-266 |
2.03e-42 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 149.13 E-value: 2.03e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 49 LAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDI--AKISDAELREVR--RKKIAMVFQSFALMPHMTVL 124
Cdd:PRK11264 24 LEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIdtARSLSQQKGLIRqlRQHVGFVFQNFNLFPHRTVL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 125 DNTAFG-MELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEM 203
Cdd:PRK11264 104 ENIIEGpVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPEVILFDEPTSALDPELVGEV 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16130591 204 QDELVKLqAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFFR 266
Cdd:PRK11264 184 LNTIRQL-AQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADPQQPRTRQFLE 245
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
46-268 |
3.94e-42 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 148.76 E-value: 3.94e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 46 DASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVRrKKIAMVFQSFALMPHMTVLD 125
Cdd:PRK11831 25 NISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTVR-KRMSMLFQSGALFTDMNVFD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 126 NTAFGM-ELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLirteMQ 204
Cdd:PRK11831 104 NVAYPLrEHTQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDPI----TM 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16130591 205 DELVKL--QAKHQR--TIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPaNDYVRTFFRGV 268
Cdd:PRK11831 180 GVLVKLisELNSALgvTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQANP-DPRVRQFLDGI 246
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
44-255 |
7.55e-42 |
|
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: 154.53 E-value: 7.55e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELRevrrKKIAMVFQSFALmPHMTV 123
Cdd:COG4988 353 LDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWR----RQIAWVPQNPYL-FAGTI 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 124 LDNTAFGMELAGinaeerREKALDALRQVGLENYAHSYPDE-----------LSGGMRQRVGLARALAINPDILLMDEAF 192
Cdd:COG4988 428 RENLRLGRPDAS------DEELEAALEAAGLDEFVAALPDGldtplgeggrgLSGGQAQRLALARALLRDAPLLLLDEPT 501
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16130591 193 SALDPLIRTEMQDELvkLQAKHQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEILNN 255
Cdd:COG4988 502 AHLDAETEAEILQAL--RRLAKGRTVILITHRL-ALLAQADRILVLDDGRIVEQGTHEELLAK 561
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
20-253 |
7.57e-42 |
|
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: 154.19 E-value: 7.57e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 20 RAFKYIEQG--------LSKEQILEKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLI---- 87
Cdd:TIGR03269 268 EKECEVEVGepiikvrnVSKRYISVDRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgd 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 88 DGVDIAKISdAELREVRRKKIAMVFQSFALMPHMTVLDN--TAFGMELAginAEERREKALDALRQVGL-ENYAHS---- 160
Cdd:TIGR03269 348 EWVDMTKPG-PDGRGRAKRYIGILHQEYDLYPHRTVLDNltEAIGLELP---DELARMKAVITLKMVGFdEEKAEEildk 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 161 YPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQN 240
Cdd:TIGR03269 424 YPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRD 503
|
250
....*....|...
gi 16130591 241 GEVVQVGTPDEIL 253
Cdd:TIGR03269 504 GKIVKIGDPEEIV 516
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
5-252 |
1.04e-41 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 148.72 E-value: 1.04e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 5 LEIKNLYKIFGEHpqRAfkyieqglskeqilektglslgVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQ 84
Cdd:COG4152 2 LELKGLTKRFGDK--TA----------------------VDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGE 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 85 VLIDGVDIAkisdaelREVRRKkiamvfqsFALMPH-------MTVLDNTAFGMELAGINAEERREKALDALRQVGLENY 157
Cdd:COG4152 58 VLWDGEPLD-------PEDRRR--------IGYLPEerglypkMKVGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDR 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 158 AHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQAKhQRTIVFISHDLDEAMRIGDRIAI 237
Cdd:COG4152 123 ANKKVEELSKGNQQKVQLIAALLHDPELLILDEPFSGLDPVNVELLKDVIRELAAK-GTTVIFSSHQMELVEELCDRIVI 201
|
250
....*....|....*
gi 16130591 238 MQNGEVVQVGTPDEI 252
Cdd:COG4152 202 INKGRKVLSGSVDEI 216
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
25-267 |
1.83e-41 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 146.73 E-value: 1.83e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 25 IEQGLSKEQILEKTGLSLGV------KDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIE------PTRGQVLIDGVDI 92
Cdd:PRK14246 1 MEAGKSAEDVFNISRLYLYIndkailKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiydskiKVDGKVLYFGKDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 93 AKISDAELrevrRKKIAMVFQSFALMPHMTVLDNTAFGMELAGINAEERREKAL-DALRQVGLENYAH----SYPDELSG 167
Cdd:PRK14246 81 FQIDAIKL----RKEVGMVFQQPNPFPHLSIYDNIAYPLKSHGIKEKREIKKIVeECLRKVGLWKEVYdrlnSPASQLSG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 168 GMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLqaKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVG 247
Cdd:PRK14246 157 GQQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITEL--KNEIAIVIVSHNPQQVARVADYVAFLYNGELVEWG 234
|
250 260
....*....|....*....|
gi 16130591 248 TPDEILNNPANDYVRTFFRG 267
Cdd:PRK14246 235 SSNEIFTSPKNELTEKYVIG 254
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
5-262 |
1.95e-41 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 147.24 E-value: 1.95e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 5 LEIKNLYKifgehpqrAFKYiEQGLSKEQILEktglslGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQ 84
Cdd:PRK15112 5 LEVRNLSK--------TFRY-RTGWFRRQTVE------AVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 85 VLIDGVDIAkISDAELREVRrkkIAMVFQ--SFALMPHMTVLDNTAFGMEL-AGINAEERREKALDALRQVGL-ENYAHS 160
Cdd:PRK15112 70 LLIDDHPLH-FGDYSYRSQR---IRMIFQdpSTSLNPRQRISQILDFPLRLnTDLEPEQREKQIIETLRQVGLlPDHASY 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 161 YPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQN 240
Cdd:PRK15112 146 YPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQ 225
|
250 260
....*....|....*....|..
gi 16130591 241 GEVVQVGTPDEILNNPANDYVR 262
Cdd:PRK15112 226 GEVVERGSTADVLASPLHELTK 247
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
5-247 |
2.26e-41 |
|
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: 145.12 E-value: 2.26e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 5 LEIKNLYKIFGEHPqrafkyieqglskeqilektglslGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQ 84
Cdd:cd03269 1 LEVENVTKRFGRVT------------------------ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGE 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 85 VLIDG--VDIAKISD-AELREVRrkkiamvfqsfALMPHMTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSY 161
Cdd:cd03269 57 VLFDGkpLDIAARNRiGYLPEER-----------GLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKR 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 162 PDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQAKhQRTIVFISHDLDEAMRIGDRIAIMQNG 241
Cdd:cd03269 126 VEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVNVELLKDVIRELARA-GKTVILSTHQMELVEELCDRVLLLNKG 204
|
....*.
gi 16130591 242 EVVQVG 247
Cdd:cd03269 205 RAVLYG 210
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
44-267 |
2.51e-41 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 146.21 E-value: 2.51e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIE-----PTRGQVLIDGVDIAKISDAELRevrrKKIAMVFQSFALM 118
Cdd:PRK14247 19 LDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElypeaRVSGEVYLDGQDIFKMDVIELR----RRVQMVFQIPNPI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 119 PHMTVLDNTAFGMELAGI--NAEERREKALDALRQVGL----ENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAF 192
Cdd:PRK14247 95 PNLSIFENVALGLKLNRLvkSKKELQERVRWALEKAQLwdevKDRLDAPAGKLSGGQQQRLCIARALAFQPEVLLADEPT 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16130591 193 SALDPlIRTEMQDELVkLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFFRG 267
Cdd:PRK14247 175 ANLDP-ENTAKIESLF-LELKKDMTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTNPRHELTEKYVTG 247
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
44-252 |
4.74e-41 |
|
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin resistance ABC transporter, ATP binding subunit in bacteria and archaea. This model is restricted in its scope to preferentially recognize the ATP binding subunit associated with effux of the drug, daunorubicin. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. In eukaryotes proteins of similar function include p-gyco proteins, multidrug resistance protein etc. [Transport and binding proteins, Other]
Pssm-ID: 130256 [Multi-domain] Cd Length: 302 Bit Score: 147.15 E-value: 4.74e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKisdaELREVRRKkIAMVFQSFALMPHMTV 123
Cdd:TIGR01188 9 VDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVVR----EPRKVRRS-IGIVPQYASVDEDLTG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 124 LDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEM 203
Cdd:TIGR01188 84 RENLEMMGRLYGLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPRTRRAI 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 16130591 204 QDELVKLQaKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEI 252
Cdd:TIGR01188 164 WDYIRALK-EEGVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPEEL 211
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
44-254 |
6.88e-41 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 146.08 E-value: 6.88e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDI-AKISDAELREVRrKKIAMVFQsfalMPHMT 122
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITItHKTKDKYIRPVR-KRIGMVFQ----FPESQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 123 VLDNTA-----FGMELAGINAEERREKALDALRQVGLE-NYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALD 196
Cdd:PRK13646 98 LFEDTVereiiFGPKNFKMNLDEVKNYAHRLLMDLGFSrDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLD 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 16130591 197 PLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILN 254
Cdd:PRK13646 178 PQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFK 235
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
31-261 |
2.97e-40 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 143.38 E-value: 2.97e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 31 KEQILEKTGLSL------GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRL--IEP---TRGQVLIDGVDI--AKISD 97
Cdd:PRK14239 2 TEPILQVSDLSVyynkkkALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndLNPevtITGSIVYNGHNIysPRTDT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 98 AELRevrrKKIAMVFQSFALMPhMTVLDNTAFGMELAGINAEERREKALD-ALRQVGL----ENYAHSYPDELSGGMRQR 172
Cdd:PRK14239 82 VDLR----KEIGMVFQQPNPFP-MSIYENVVYGLRLKGIKDKQVLDEAVEkSLKGASIwdevKDRLHDSALGLSGGQQQR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 173 VGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLqaKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEI 252
Cdd:PRK14239 157 VCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGL--KDDYTMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQM 234
|
250
....*....|...
gi 16130591 253 LNNPAN----DYV 261
Cdd:PRK14239 235 FMNPKHketeDYI 247
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
44-245 |
4.01e-40 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 143.67 E-value: 4.01e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVRRKkIAMVFQSF--ALMPHM 121
Cdd:PRK10419 28 LNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQRKAFRRD-IQMVFQDSisAVNPRK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 122 TVLDNTAFGME-LAGINAEERREKALDALRQVGL-ENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLI 199
Cdd:PRK10419 107 TVREIIREPLRhLLSLDKAERLARASEMLRAVDLdDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVL 186
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 16130591 200 RTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQ 245
Cdd:PRK10419 187 QAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVE 232
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-252 |
6.11e-40 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 148.24 E-value: 6.11e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 1 MAIKLEIKNLYKIFGehpqrafkyieqglskeqilektglslGVK---DASLAIEEGEIFVIMGLSGSGKSTMVRLLNRL 77
Cdd:COG1129 1 AEPLLEMRGISKSFG---------------------------GVKaldGVSLELRPGEVHALLGENGAGKSTLMKILSGV 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 78 IEPTRGQVLIDG--VDIAKISDAElrevrRKKIAMVFQSFALMPHMTVLDNTAFGMELAG---INAEERREKALDALRQV 152
Cdd:COG1129 54 YQPDSGEILLDGepVRFRSPRDAQ-----AAGIAIIHQELNLVPNLSVAENIFLGREPRRgglIDWRAMRRRARELLARL 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 153 GLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDP--------LIRtemqdelvKLQAKHqRTIVFISHD 224
Cdd:COG1129 129 GLDIDPDTPVGDLSVAQQQLVEIARALSRDARVLILDEPTASLTEreverlfrIIR--------RLKAQG-VAIIYISHR 199
|
250 260 270
....*....|....*....|....*....|...
gi 16130591 225 LDEAMRIGDRIAIMQNGEVVQVG-----TPDEI 252
Cdd:COG1129 200 LDEVFEIADRVTVLRDGRLVGTGpvaelTEDEL 232
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
41-254 |
8.11e-40 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 142.97 E-value: 8.11e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 41 SLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGvdiAKISDAELREVRrKKIAMVFQSfalmPH 120
Cdd:PRK13648 22 SFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNN---QAITDDNFEKLR-KHIGIVFQN----PD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 121 -----MTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSAL 195
Cdd:PRK13648 94 nqfvgSIVKYDVAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSML 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 16130591 196 DPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRiGDRIAIMQNGEVVQVGTPDEILN 254
Cdd:PRK13648 174 DPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIFD 231
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
45-253 |
2.66e-39 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 140.37 E-value: 2.66e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 45 KDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISdaeLREVRRkKIAMVFQSFALMPhMTVL 124
Cdd:cd03249 20 KGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLN---LRWLRS-QIGLVSQEPVLFD-GTIA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 125 DNTAFGmeLAGINAEERREkaldALRQVGLENYAHSYPD-----------ELSGGMRQRVGLARALAINPDILLMDEAFS 193
Cdd:cd03249 95 ENIRYG--KPDATDEEVEE----AAKKANIHDFIMSLPDgydtlvgergsQLSGGQKQRIAIARALLRNPKILLLDEATS 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 194 ALDPLIRTEMQDELVKlqAKHQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEIL 253
Cdd:cd03249 169 ALDAESEKLVQEALDR--AMKGRTTIVIAHRL-STIRNADLIAVLQNGQVVEQGTHDELM 225
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
44-253 |
4.84e-39 |
|
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: 139.67 E-value: 4.84e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREvrrkKIAMVFQSFALMPHmTV 123
Cdd:cd03254 19 LKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRS----MIGVVLQDTFLFSG-TI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 124 LDNTAFGMELAginaeeRREKALDALRQVG-------LENYAHSYPDE----LSGGMRQRVGLARALAINPDILLMDEAF 192
Cdd:cd03254 94 MENIRLGRPNA------TDEEVIEAAKEAGahdfimkLPNGYDTVLGEnggnLSQGERQLLAIARAMLRDPKILILDEAT 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16130591 193 SALDPLIRTEMQDELVKLQakHQRTIVFISHDLDeAMRIGDRIAIMQNGEVVQVGTPDEIL 253
Cdd:cd03254 168 SNIDTETEKLIQEALEKLM--KGRTSIIIAHRLS-TIKNADKILVLDDGKIIEEGTHDELL 225
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
22-256 |
5.72e-39 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 141.12 E-value: 5.72e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 22 FKYIEQGLSKEQILEKTGLSlgvkDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDI-AKISDAEL 100
Cdd:PRK13641 5 FENVDYIYSPGTPMEKKGLD----NISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHItPETGNKNL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 101 REVRrKKIAMVFQ-SFALMPHMTVLDNTAFGMELAGINAEERREKALDALRQVGL-ENYAHSYPDELSGGMRQRVGLARA 178
Cdd:PRK13641 81 KKLR-KKVSLVFQfPEAQLFENTVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLsEDLISKSPFELSGGQMRRVAIAGV 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16130591 179 LAINPDILLMDEAFSALDPLIRTEMQDELVKLQaKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNP 256
Cdd:PRK13641 160 MAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQ-KAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDK 236
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
45-254 |
5.83e-39 |
|
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: 139.67 E-value: 5.83e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 45 KDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELrevrRKKIAMVFQSFALMpHMTVL 124
Cdd:cd03253 18 KDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSL----RRAIGVVPQDTVLF-NDTIG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 125 DNTAFGmelaGINAEErrEKALDALRQVGLENYAHSYPD-----------ELSGGMRQRVGLARALAINPDILLMDEAFS 193
Cdd:cd03253 93 YNIRYG----RPDATD--EEVIEAAKAAQIHDKIMRFPDgydtivgerglKLSGGEKQRVAIARAILKNPPILLLDEATS 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16130591 194 ALDPLIRTEMQDELVKLQAKhqRTIVFISHDLDEAMRiGDRIAIMQNGEVVQVGTPDEILN 254
Cdd:cd03253 167 ALDTHTEREIQAALRDVSKG--RTTIVIAHRLSTIVN-ADKIIVLKDGRIVERGTHEELLA 224
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
45-256 |
7.55e-39 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 140.60 E-value: 7.55e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 45 KDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIaKISDAELREVRrKKIAMVFQS-----FAlmP 119
Cdd:PRK13639 19 KGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPI-KYDKKSLLEVR-KTVGIVFQNpddqlFA--P 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 120 hmTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLI 199
Cdd:PRK13639 95 --TVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMG 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 16130591 200 RTEMQDELVKLQaKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNP 256
Cdd:PRK13639 173 ASQIMKLLYDLN-KEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDI 228
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
44-256 |
7.75e-39 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 140.71 E-value: 7.75e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEP---TRGQVLIDGVDIAKISDAELREvrrkKIAMVFQSfalmPH 120
Cdd:PRK13640 23 LNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPddnPNSKITVDGITLTAKTVWDIRE----KVGIVFQN----PD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 121 -----MTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSAL 195
Cdd:PRK13640 95 nqfvgATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSML 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16130591 196 DPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAmRIGDRIAIMQNGEVVQVGTPDEILNNP 256
Cdd:PRK13640 175 DPAGKEQILKLIRKLKKKNNLTVISITHDIDEA-NMADQVLVLDDGKLLAQGSPVEIFSKV 234
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-254 |
2.69e-38 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 137.91 E-value: 2.69e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 1 MAIKLEIKNLYKIF--GEHPQRAFKYIEQGLSKEQILEKTGLslgvKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLI 78
Cdd:COG1134 1 MSSMIEVENVSKSYrlYHEPSRSLKELLLRRRRTRREEFWAL----KDVSFEVERGESVGIIGRNGAGKSTLLKLIAGIL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 79 EPTRGQVLIDGvdiakisdaelrevrrkKIAMVFQ-SFALMPHMTVLDNTAFGMELAGINAEERREKaldaLRQV----G 153
Cdd:COG1134 77 EPTSGRVEVNG-----------------RVSALLElGAGFHPELTGRENIYLNGRLLGLSRKEIDEK----FDEIvefaE 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 154 LENYAH----SYpdelSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQaKHQRTIVFISHDLDEAM 229
Cdd:COG1134 136 LGDFIDqpvkTY----SSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELR-ESGRTVIFVSHSMGAVR 210
|
250 260
....*....|....*....|....*
gi 16130591 230 RIGDRIAIMQNGEVVQVGTPDEILN 254
Cdd:COG1134 211 RLCDRAIWLEKGRLVMDGDPEEVIA 235
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
44-245 |
3.65e-38 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 137.25 E-value: 3.65e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVRRKKIAMVFQSFALMPHMTV 123
Cdd:PRK11629 25 LHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAELRNQKLGFIYQFHHLLPDFTA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 124 LDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEM 203
Cdd:PRK11629 105 LENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADSI 184
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 16130591 204 QDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAiMQNGEVVQ 245
Cdd:PRK11629 185 FQLLGELNRLQGTAFLVVTHDLQLAKRMSRQLE-MRDGRLTA 225
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
44-276 |
4.83e-38 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 137.55 E-value: 4.83e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVRrkkiAMVFQ----SFALmp 119
Cdd:COG4559 17 LDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRR----AVLPQhsslAFPF-- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 120 hmTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAH-SYPdELSGGMRQRVGLARALA-------INPDILLMDEA 191
Cdd:COG4559 91 --TVEEVVALGRAPHGSSAAQDRQIVREALALVGLAHLAGrSYQ-TLSGGEQQRVQLARVLAqlwepvdGGPRWLFLDEP 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 192 FSALDPL--IRTeMQdeLVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPAndyvrtffrgvd 269
Cdd:COG4559 168 TSALDLAhqHAV-LR--LARQLARRGGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPEEVLTDEL------------ 232
|
....*..
gi 16130591 270 ISQVFSA 276
Cdd:COG4559 233 LERVYGA 239
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
5-228 |
5.83e-38 |
|
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: 136.07 E-value: 5.83e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 5 LEIKNLYKIFGEHPqrafkyieqglskeqILEktglslgvkDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQ 84
Cdd:COG4133 3 LEAENLSCRRGERL---------------LFS---------GLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGE 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 85 VLIDGVDIAKisdaeLREVRRKKIAMVFQSFALMPHMTVLDNTAFGMELAGINAeeRREKALDALRQVGLENYAHSYPDE 164
Cdd:COG4133 59 VLWNGEPIRD-----AREDYRRRLAYLGHADGLKPELTVRENLRFWAALYGLRA--DREAIDEALEAVGLAGLADLPVRQ 131
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16130591 165 LSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQdELVKLQAKHQRTIVFISHDLDEA 228
Cdd:COG4133 132 LSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGVALLA-ELIAAHLARGGAVLLTTHQPLEL 194
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
44-253 |
7.50e-38 |
|
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: 136.59 E-value: 7.50e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELrevrRKKIAMVFQSFALMpHMTV 123
Cdd:cd03251 18 LRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASL----RRQIGLVSQDVFLF-NDTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 124 LDNTAFGMElaginaEERREKALDALRQVGLENYAHSYPD-----------ELSGGMRQRVGLARALAINPDILLMDEAF 192
Cdd:cd03251 93 AENIAYGRP------GATREEVEEAARAANAHEFIMELPEgydtvigergvKLSGGQRQRIAIARALLKDPPILILDEAT 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16130591 193 SALDplIRTEM--QDELVKLQAkhQRTIVFISHDLDEAMRIgDRIAIMQNGEVVQVGTPDEIL 253
Cdd:cd03251 167 SALD--TESERlvQAALERLMK--NRTTFVIAHRLSTIENA-DRIVVLEDGKIVERGTHEELL 224
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
44-257 |
1.03e-37 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 137.43 E-value: 1.03e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISdaELREVRrKKIAMVFQSfalmPHM-- 121
Cdd:PRK13644 18 LENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFS--KLQGIR-KLVGIVFQN----PETqf 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 122 ---TVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPL 198
Cdd:PRK13644 91 vgrTVEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPD 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 16130591 199 IRTEMQDELVKLQAKhQRTIVFISHDLDEaMRIGDRIAIMQNGEVVQVGTPDEILNNPA 257
Cdd:PRK13644 171 SGIAVLERIKKLHEK-GKTIVYITHNLEE-LHDADRIIVMDRGKIVLEGEPENVLSDVS 227
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
44-255 |
1.38e-37 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 135.25 E-value: 1.38e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISdaeLREVRRKKIAMVFQSFALMPHMTV 123
Cdd:cd03224 16 LFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLP---PHERARAGIGYVPEGRRIFPELTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 124 LDNTAFGME-LAGINAEERREKALD---ALRQVgLENYAHSypdeLSGGMRQRVGLARALAINPDILLMDEAFSALDPLI 199
Cdd:cd03224 93 EENLLLGAYaRRRAKRKARLERVYElfpRLKER-RKQLAGT----LSGGEQQMLAIARALMSRPKLLLLDEPSEGLAPKI 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 16130591 200 RTEMQDELVKLqAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNN 255
Cdd:cd03224 168 VEEIFEAIREL-RDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELLAD 222
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-251 |
2.38e-37 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 141.32 E-value: 2.38e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 1 MAIKLEIKNLYKIFGehpqrafkyieqglskeqilektglslGV---KDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRL 77
Cdd:COG3845 2 MPPALELRGITKRFG---------------------------GVvanDDVSLTVRPGEIHALLGENGAGKSTLMKILYGL 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 78 IEPTRGQVLIDG--VDIAKISDAelrevRRKKIAMVFQSFALMPHMTVLDNTAFGME---LAGINAEERREKALDALRQV 152
Cdd:COG3845 55 YQPDSGEILIDGkpVRIRSPRDA-----IALGIGMVHQHFMLVPNLTVAENIVLGLEptkGGRLDRKAARARIRELSERY 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 153 GLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDP-----LIRTemqdeLVKLQAKhQRTIVFISHDLDE 227
Cdd:COG3845 130 GLDVDPDAKVEDLSVGEQQRVEILKALYRGARILILDEPTAVLTPqeadeLFEI-----LRRLAAE-GKSIIFITHKLRE 203
|
250 260
....*....|....*....|....
gi 16130591 228 AMRIGDRIAIMQNGEVVQVGTPDE 251
Cdd:COG3845 204 VMAIADRVTVLRRGKVVGTVDTAE 227
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
44-247 |
3.60e-37 |
|
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: 133.86 E-value: 3.60e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 44 VKDASLAIEEGeIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKisdaeLREVRRKKIAMVFQSFALMPHMTV 123
Cdd:cd03264 16 LDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLK-----QPQKLRRRIGYLPQEFGVYPNFTV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 124 LDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEM 203
Cdd:cd03264 90 REFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDPEERIRF 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 16130591 204 QDELVKLQAkhQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVG 247
Cdd:cd03264 170 RNLLSELGE--DRIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
39-267 |
5.35e-37 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 135.29 E-value: 5.35e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 39 GLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNR---LIEPTR--GQVLIDGVDIAKiSDAELREVRRKkIAMVFQ 113
Cdd:PRK14243 21 GSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRlndLIPGFRveGKVTFHGKNLYA-PDVDPVEVRRR-IGMVFQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 114 SFALMPHmTVLDNTAFGMELAGI--NAEERREKAL----------DALRQVGLEnyahsypdeLSGGMRQRVGLARALAI 181
Cdd:PRK14243 99 KPNPFPK-SIYDNIAYGARINGYkgDMDELVERSLrqaalwdevkDKLKQSGLS---------LSGGQQQRLCIARAIAV 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 182 NPDILLMDEAFSALDPlIRTEMQDELVKlQAKHQRTIVFISHDLDEAMRIGDRIAIM---------QNGEVVQVGTPDEI 252
Cdd:PRK14243 169 QPEVILMDEPCSALDP-ISTLRIEELMH-ELKEQYTIIIVTHNMQQAARVSDMTAFFnveltegggRYGYLVEFDRTEKI 246
|
250
....*....|....*
gi 16130591 253 LNNPANDYVRTFFRG 267
Cdd:PRK14243 247 FNSPQQQATRDYVSG 261
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
5-262 |
6.18e-37 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 140.61 E-value: 6.18e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 5 LEIKNLykifgehpQRAFKyIEQGLSKEQILEKTGLslgvKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIePTRGQ 84
Cdd:PRK15134 276 LDVEQL--------QVAFP-IRKGILKRTVDHNVVV----KNISFTLRPGETLGLVGESGSGKSTTGLALLRLI-NSQGE 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 85 VLIDGVDIAKISDAELREVRRKkIAMVFQ--SFALMPHMTVLDNTAFGMEL--AGINAEERREKALDALRQVGLE-NYAH 159
Cdd:PRK15134 342 IWFDGQPLHNLNRRQLLPVRHR-IQVVFQdpNSSLNPRLNVLQIIEEGLRVhqPTLSAAQREQQVIAVMEEVGLDpETRH 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 160 SYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQ 239
Cdd:PRK15134 421 RYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLR 500
|
250 260
....*....|....*....|...
gi 16130591 240 NGEVVQVGTPDEILNNPANDYVR 262
Cdd:PRK15134 501 QGEVVEQGDCERVFAAPQQEYTR 523
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
44-267 |
8.73e-37 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 134.00 E-value: 8.73e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISdaeLREVRRKKI------AMVFQsfal 117
Cdd:COG1137 19 VKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLP---MHKRARLGIgylpqeASIFR---- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 118 mpHMTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDP 197
Cdd:COG1137 92 --KLTVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKFILLDEPFAGVDP 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16130591 198 LIRTEMQDELVKLQakhQRTI-VFIS-HDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPAndyVRTFFRG 267
Cdd:COG1137 170 IAVADIQKIIRHLK---ERGIgVLITdHNVRETLGICDRAYIISEGKVLAEGTPEEILNNPL---VRKVYLG 235
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
44-254 |
1.31e-36 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 133.67 E-value: 1.31e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELRevrrKKIAMVFQSFALMPHMTV 123
Cdd:COG4604 17 LDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELA----KRLAILRQENHINSRLTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 124 LDNTAFG--------MElaginaEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSAL 195
Cdd:COG4604 93 RELVAFGrfpyskgrLT------AEDREIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQDTDYVLLDEPLNNL 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 16130591 196 DPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILN 254
Cdd:COG4604 167 DMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEIIT 225
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
44-253 |
3.57e-36 |
|
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: 132.22 E-value: 3.57e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELrevrRKKIAMVFQSFALMpHMTV 123
Cdd:cd03252 18 LDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWL----RRQVGVVLQENVLF-NRSI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 124 LDNTAF---GMELAGINAEERREKALDALRQV--GLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDpl 198
Cdd:cd03252 93 RDNIALadpGMSMERVIEAAKLAGAHDFISELpeGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATSALD-- 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 16130591 199 irteMQDELVKLQAKHQ----RTIVFISHDLDEAMRiGDRIAIMQNGEVVQVGTPDEIL 253
Cdd:cd03252 171 ----YESEHAIMRNMHDicagRTVIIIAHRLSTVKN-ADRIIVMEKGRIVEQGSHDELL 224
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
46-252 |
4.91e-36 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 132.95 E-value: 4.91e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 46 DASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAkiSDAELREVR--RKKIAMVFQsFA--LMPHM 121
Cdd:PRK13649 25 DVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLIT--STSKNKDIKqiRKKVGLVFQ-FPesQLFEE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 122 TVLDNTAFGMELAGINAEERREKALDALRQVGL-ENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIR 200
Cdd:PRK13649 102 TVLKDVAFGPQNFGVSQEEAEALAREKLALVGIsESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGR 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 16130591 201 TEMQDELVKLqakHQR--TIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEI 252
Cdd:PRK13649 182 KELMTLFKKL---HQSgmTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDI 232
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
44-247 |
1.17e-35 |
|
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: 130.18 E-value: 1.17e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKisdaELREVRRKkIAMVFQSFALMPHMTV 123
Cdd:cd03266 21 VDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVK----EPAEARRR-LGFVSDSTGLYDRLTA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 124 LDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEM 203
Cdd:cd03266 96 RENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRAL 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 16130591 204 QDELVKLQAKhQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVG 247
Cdd:cd03266 176 REFIRQLRAL-GKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
23-257 |
1.44e-35 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 133.05 E-value: 1.44e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 23 KYIEQGLSKEQILEKTGLS-----------LGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVD 91
Cdd:PRK13631 10 LKVPNPLSDDIILRVKNLYcvfdekqenelVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 92 IAKISDAELREVR------------RKKIAMVFQ--SFALMPHmTVLDNTAFGMELAGINAEERREKALDALRQVGL-EN 156
Cdd:PRK13631 90 IGDKKNNHELITNpyskkiknfkelRRRVSMVFQfpEYQLFKD-TIEKDIMFGPVALGVKKSEAKKLAKFYLNKMGLdDS 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 157 YAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDeLVKLQAKHQRTIVFISHDLDEAMRIGDRIA 236
Cdd:PRK13631 169 YLERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQ-LILDAKANNKTVFVITHTMEHVLEVADEVI 247
|
250 260
....*....|....*....|.
gi 16130591 237 IMQNGEVVQVGTPDEILNNPA 257
Cdd:PRK13631 248 VMDKGKILKTGTPYEIFTDQH 268
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
5-244 |
3.77e-35 |
|
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: 127.16 E-value: 3.77e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 5 LEIKNLYKIFGEHPqrafkyieqglskeqilektglslGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQ 84
Cdd:cd03216 1 LELRGITKRFGGVK------------------------ALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGE 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 85 VLIDG--VDIAKISDAelrevRRKKIAMVFQsfalmphmtvldntafgmelaginaeerrekaldalrqvglenyahsyp 162
Cdd:cd03216 57 ILVDGkeVSFASPRDA-----RRAGIAMVYQ------------------------------------------------- 82
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 163 deLSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQAKHqRTIVFISHDLDEAMRIGDRIAIMQNGE 242
Cdd:cd03216 83 --LSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFKVIRRLRAQG-VAVIFISHRLDEVFEIADRVTVLRDGR 159
|
..
gi 16130591 243 VV 244
Cdd:cd03216 160 VV 161
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
44-257 |
6.55e-35 |
|
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: 128.81 E-value: 6.55e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIakiSDAELREVRRKKIAMVFQSFALMPHMTV 123
Cdd:cd03218 16 VNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDI---TKLPMHKRARLGIGYLPQEASIFRKLTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 124 LDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEM 203
Cdd:cd03218 93 EENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVDPIAVQDI 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 16130591 204 QDELVKLQakhQRTI-VFIS-HDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPA 257
Cdd:cd03218 173 QKIIKILK---DRGIgVLITdHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANEL 225
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
44-284 |
6.74e-35 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 136.14 E-value: 6.74e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVRRKkIAMVFQS--FALMPHM 121
Cdd:PRK10261 340 VEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQALRRD-IQFIFQDpyASLDPRQ 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 122 TVLDNTAFGMELAGI-NAEERREKALDALRQVGLE-NYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLI 199
Cdd:PRK10261 419 TVGDSIMEPLRVHGLlPGKAAAARVAWLLERVGLLpEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSI 498
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 200 RTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFFRGVDISqvfsakDI 279
Cdd:PRK10261 499 RGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENPQHPYTRKLMAAVPVA------DP 572
|
....*
gi 16130591 280 ARRTP 284
Cdd:PRK10261 573 SRQRP 577
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
44-284 |
9.28e-35 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 135.37 E-value: 9.28e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDG----------VDIAKISDAELREVRRKKIAMVFQ 113
Cdd:PRK10261 32 VRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKmllrrrsrqvIELSEQSAAQMRHVRGADMAMIFQ 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 114 S--FALMPHMTVLDNTAFGMEL-AGINAEERREKALDALRQVGL---ENYAHSYPDELSGGMRQRVGLARALAINPDILL 187
Cdd:PRK10261 112 EpmTSLNPVFTVGEQIAESIRLhQGASREEAMVEAKRMLDQVRIpeaQTILSRYPHQLSGGMRQRVMIAMALSCRPAVLI 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 188 MDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFFRG 267
Cdd:PRK10261 192 ADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQIFHAPQHPYTRALLAA 271
|
250
....*....|....*..
gi 16130591 268 VDISQVFSAKDIARRTP 284
Cdd:PRK10261 272 VPQLGAMKGLDYPRRFP 288
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
48-253 |
2.02e-34 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 128.67 E-value: 2.02e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGvdiAKISDAELREVRRKkIAMVFQS-FALMPHMTVLDN 126
Cdd:PRK13642 27 SFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDG---ELLTAENVWNLRRK-IGMVFQNpDNQFVGATVEDD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 127 TAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDE 206
Cdd:PRK13642 103 VAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMRV 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 16130591 207 LVKLQAKHQRTIVFISHDLDEAMRiGDRIAIMQNGEVVQVGTPDEIL 253
Cdd:PRK13642 183 IHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELF 228
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
3-281 |
2.63e-34 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 129.05 E-value: 2.63e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 3 IKLEIKNLYKIFGEHPQRAFKYIeqglskeqilektglslgvKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTR 82
Cdd:PRK13651 1 MQIKVKNIVKIFNKKLPTELKAL-------------------DNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDT 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 83 GQVLIDGVDIAKISDAELREVR--------------------RKKIAMVFQsFA--LMPHMTVLDNTAFGMELAGINAEE 140
Cdd:PRK13651 62 GTIEWIFKDEKNKKKTKEKEKVleklviqktrfkkikkikeiRRRVGVVFQ-FAeyQLFEQTIEKDIIFGPVSMGVSKEE 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 141 RREKALDALRQVGL-ENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQaKHQRTIV 219
Cdd:PRK13651 141 AKKRAAKYIELVGLdESYLQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLN-KQGKTII 219
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16130591 220 FISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNN----------PAN--DYVRTFF-RGVDISQVFSAKDIAR 281
Cdd:PRK13651 220 LVTHDLDNVLEWTKRTIFFKDGKIIKDGDTYDILSDnkfliennmePPKllNFVNKLEkKGIDVPKVTSIEELAS 294
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
44-264 |
6.15e-34 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 127.08 E-value: 6.15e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEpTRGQVLIDG-VDIAKISDAELR---EVRRKKIAMVFQSFALMP 119
Cdd:PRK14258 23 LEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNE-LESEVRVEGrVEFFNQNIYERRvnlNRLRRQVSMVHPKPNLFP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 120 hMTVLDNTAFGMELAG----INAEERREKAL-DALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSA 194
Cdd:PRK14258 102 -MSVYDNVAYGVKIVGwrpkLEIDDIVESALkDADLWDEIKHKIHKSALDLSGGQQQRLCIARALAVKPKVLLMDEPCFG 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16130591 195 LDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQN-----GEVVQVGTPDEILNNPANDYVRTF 264
Cdd:PRK14258 181 LDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGnenriGQLVEFGLTKKIFNSPHDSRTREY 255
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
46-275 |
8.10e-34 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 127.54 E-value: 8.10e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 46 DASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDgvDIAKISDAELREVR--RKKIAMVFQ-SFALMPHMT 122
Cdd:PRK13643 24 DIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVG--DIVVSSTSKQKEIKpvRKKVGVVFQfPESQLFEET 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 123 VLDNTAFGMELAGINAEERREKALDALRQVGL-ENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRT 201
Cdd:PRK13643 102 VLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLaDEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKARI 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16130591 202 EMqdeLVKLQAKHQ--RTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPanDYVRTFFRGVDISQVFS 275
Cdd:PRK13643 182 EM---MQLFESIHQsgQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQEV--DFLKAHELGVPKATHFA 252
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
43-255 |
8.15e-34 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 127.43 E-value: 8.15e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDI-AKISdaELREVR--RKKIAMVFQ--SFAL 117
Cdd:PRK13645 26 ALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIpANLK--KIKEVKrlRKEIGLVFQfpEYQL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 118 MPHmTVLDNTAFGMELAGINAEERREKALDALRQVGL-ENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALD 196
Cdd:PRK13645 104 FQE-TIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLpEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLD 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 16130591 197 PLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNN 255
Cdd:PRK13645 183 PKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFSN 241
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
44-254 |
1.26e-33 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 126.04 E-value: 1.26e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAEL---REVRRKKIAMVFqSFalmph 120
Cdd:PRK13548 18 LDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELarrRAVLPQHSSLSF-PF----- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 121 mTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAH-SYPdELSGGMRQRVGLARALA------INPDILLMDEAFS 193
Cdd:PRK13548 92 -TVEEVVAMGRAPHGLSRAEDDALVAAALAQVDLAHLAGrDYP-QLSGGEQQRVQLARVLAqlwepdGPPRWLLLDEPTS 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16130591 194 ALDPL--IRTeMQdeLVK-LQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILN 254
Cdd:PRK13548 170 ALDLAhqHHV-LR--LARqLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAEVLT 230
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-241 |
1.78e-33 |
|
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: 124.85 E-value: 1.78e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 1 MAIKLEIKNLYKIFGEHpqrafkyiEQGlskeqilektGLSL-GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIE 79
Cdd:COG4778 1 MTTLLEVENLSKTFTLH--------LQG----------GKRLpVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYL 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 80 PTRGQVLID----GVDIAKISDAELREVRRKKIAMVFQSFALMPHMTVLDNTAFGMELAGINAEERREKALDALRQVGL- 154
Cdd:COG4778 63 PDSGSILVRhdggWVDLAQASPREILALRRRTIGYVSQFLRVIPRVSALDVVAEPLLERGVDREEARARARELLARLNLp 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 155 ENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDP--------LIRtemqdelvklQAKHQ-RTIVFISHDL 225
Cdd:COG4778 143 ERLWDLPPATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAanravvveLIE----------EAKARgTAIIGIFHDE 212
|
250
....*....|....*.
gi 16130591 226 DEAMRIGDRIAIMQNG 241
Cdd:COG4778 213 EVREAVADRVVDVTPF 228
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
44-266 |
1.81e-33 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 127.55 E-value: 1.81e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIE-PTR---GQVLIDGVDIAKISDAELREVRRKKIAMVFQS--FAL 117
Cdd:PRK11022 23 VDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDyPGRvmaEKLEFNGQDLQRISEKERRNLVGAEVAMIFQDpmTSL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 118 MPHMTVldntAFGMELA-----GINAEERREKALDALRQVGLENYAHS---YPDELSGGMRQRVGLARALAINPDILLMD 189
Cdd:PRK11022 103 NPCYTV----GFQIMEAikvhqGGNKKTRRQRAIDLLNQVGIPDPASRldvYPHQLSGGMSQRVMIAMAIACRPKLLIAD 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16130591 190 EAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFFR 266
Cdd:PRK11022 179 EPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDIFRAPRHPYTQALLR 255
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
44-244 |
6.84e-33 |
|
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: 122.71 E-value: 6.84e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAelrevrRKKIAMVFQSFALMPHMTV 123
Cdd:cd03268 16 LDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEA------LRRIGALIEAPGFYPNLTA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 124 LDNTAFGMELAGInaeeRREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEM 203
Cdd:cd03268 90 RENLRLLARLLGI----RKKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPDGIKEL 165
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 16130591 204 QDELVKLqAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVV 244
Cdd:cd03268 166 RELILSL-RDQGITVLISSHLLSEIQKVADRIGIINKGKLI 205
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
44-244 |
7.01e-33 |
|
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: 122.70 E-value: 7.01e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELrevrRKKIAMVFQSFALMpHMTV 123
Cdd:cd03245 20 LDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADL----RRNIGYVPQDVTLF-YGTL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 124 LDNTAFGMELaginAEERRekALDALRQVGLENYAHSYPD-----------ELSGGMRQRVGLARALAINPDILLMDEAF 192
Cdd:cd03245 95 RDNITLGAPL----ADDER--ILRAAELAGVTDFVNKHPNgldlqigergrGLSGGQRQAVALARALLNDPPILLLDEPT 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 16130591 193 SALDplIRTEMQ--DELVKLQAkhQRTIVFISHDLdEAMRIGDRIAIMQNGEVV 244
Cdd:cd03245 169 SAMD--MNSEERlkERLRQLLG--DKTLIIITHRP-SLLDLVDRIIVMDSGRIV 217
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
44-254 |
8.29e-33 |
|
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: 129.15 E-value: 8.29e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRL--IEPTRGQVLI----------------DG--------------VD 91
Cdd:TIGR03269 16 LKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIYhvalcekcgyverpskVGepcpvcggtlepeeVD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 92 IAKISDAELREVRrKKIAMVFQ-SFALMPHMTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMR 170
Cdd:TIGR03269 96 FWNLSDKLRRRIR-KRIAIMLQrTFALYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEMVQLSHRITHIARDLSGGEK 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 171 QRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPD 250
Cdd:TIGR03269 175 QRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDLSDKAIWLENGEIKEEGTPD 254
|
....
gi 16130591 251 EILN 254
Cdd:TIGR03269 255 EVVA 258
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
5-244 |
1.08e-32 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 123.66 E-value: 1.08e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 5 LEIKNLYKIFGehpqrafkyieqglsKEQILEKTGLslgvKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQ 84
Cdd:COG1101 2 LELKNLSKTFN---------------PGTVNEKRAL----DGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGS 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 85 VLIDGVDIAKISDAElrevRRKKIAMVFQSfALM---PHMTVLDNtafgMELA-----------GINAEERRE-KALDAL 149
Cdd:COG1101 63 ILIDGKDVTKLPEYK----RAKYIGRVFQD-PMMgtaPSMTIEEN----LALAyrrgkrrglrrGLTKKRRELfRELLAT 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 150 RQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPliRT-----EMQDELVKlqaKHQRTIVFISHD 224
Cdd:COG1101 134 LGLGLENRLDTKVGLLSGGQRQALSLLMATLTKPKLLLLDEHTAALDP--KTaalvlELTEKIVE---ENNLTTLMVTHN 208
|
250 260
....*....|....*....|
gi 16130591 225 LDEAMRIGDRIAIMQNGEVV 244
Cdd:COG1101 209 MEQALDYGNRLIMMHEGRII 228
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
43-253 |
1.68e-32 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 128.93 E-value: 1.68e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELrevrRKKIAMVFQSfALMPHMT 122
Cdd:PRK13657 350 GVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASL----RRNIAVVFQD-AGLFNRS 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 123 VLDNTAFGMELAgINAEER----REKALD--ALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALD 196
Cdd:PRK13657 425 IEDNIRVGRPDA-TDEEMRaaaeRAQAHDfiERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALD 503
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16130591 197 plIRTEmqdelVKLQA-----KHQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEIL 253
Cdd:PRK13657 504 --VETE-----AKVKAaldelMKGRTTFIIAHRL-STVRNADRILVFDNGRVVESGSFDELV 557
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
44-254 |
1.73e-32 |
|
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: 122.50 E-value: 1.73e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLI------DGVDIAKIsdaelrevrRKKIAMVFQSFA- 116
Cdd:COG1119 19 LDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNDVRlfgerrGGEDVWEL---------RKRIGLVSPALQl 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 117 -LMPHMTVLDntafgMELAGINA---------EERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDIL 186
Cdd:COG1119 90 rFPRDETVLD-----VVLSGFFDsiglyreptDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIARALVKDPELL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16130591 187 LMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILN 254
Cdd:COG1119 165 ILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRVVAAGPKEEVLT 232
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
44-257 |
2.07e-32 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 122.01 E-value: 2.07e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISdAElrEVRRKKIAMVFQSFALMPHMTV 123
Cdd:COG0410 19 LHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLP-PH--RIARLGIGYVPEGRRIFPSLTV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 124 LDNTAFGMELAGINAE--ERREKALD---ALRQvglenYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPL 198
Cdd:COG0410 96 EENLLLGAYARRDRAEvrADLERVYElfpRLKE-----RRRQRAGTLSGGEQQMLAIGRALMSRPKLLLLDEPSLGLAPL 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 16130591 199 IRTEMQDELVKLQAKHQrTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPA 257
Cdd:COG0410 171 IVEEIFEIIRRLNREGV-TILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLADPE 228
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
44-257 |
2.07e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 123.31 E-value: 2.07e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELRevrrKKIAMVFQS-----FAlm 118
Cdd:PRK13647 21 LKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVR----SKVGLVFQDpddqvFS-- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 119 phMTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPL 198
Cdd:PRK13647 95 --STVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPR 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 16130591 199 IRTEMQDELVKLQaKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPdEILNNPA 257
Cdd:PRK13647 173 GQETLMEILDRLH-NQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDK-SLLTDED 229
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
44-253 |
2.32e-32 |
|
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: 128.30 E-value: 2.32e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELRevrrKKIAMVFQSFALMPHmTV 123
Cdd:TIGR02203 348 LDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASLR----RQVALVSQDVVLFND-TI 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 124 LDNTAFGmELAGINAEERREKALDALRQ-------VGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALD 196
Cdd:TIGR02203 423 ANNIAYG-RTEQADRAEIERALAAAYAQdfvdklpLGLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALD 501
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 16130591 197 PLIRTEMQDELVKLQakHQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEIL 253
Cdd:TIGR02203 502 NESERLVQAALERLM--QGRTTLVIAHRL-STIEKADRIVVMDDGRIVERGTHNELL 555
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
45-254 |
2.56e-32 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 128.92 E-value: 2.56e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 45 KDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKIsdaELREVRRKkIAMVFQSFALMPHmTVL 124
Cdd:TIGR03797 470 DDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAGL---DVQAVRRQ-LGVVLQNGRLMSG-SIF 544
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 125 DNTAFGmelAGINAEErrekALDALRQVGLEN-------YAHSYPDE----LSGGMRQRVGLARALAINPDILLMDEAFS 193
Cdd:TIGR03797 545 ENIAGG---APLTLDE----AWEAARMAGLAEdirampmGMHTVISEgggtLSGGQRQRLLIARALVRKPRILLFDEATS 617
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16130591 194 ALDPLIRTEMQDELVKLQAkhqrTIVFISHDLDEAMRiGDRIAIMQNGEVVQVGTPDEILN 254
Cdd:TIGR03797 618 ALDNRTQAIVSESLERLKV----TRIVIAHRLSTIRN-ADRIYVLDAGRVVQQGTYDELMA 673
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
44-262 |
3.12e-32 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 127.51 E-value: 3.12e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 44 VKDASLAIEEGEIFVIMGLSGSGKS-TMVRLLNRLIEP----TRGQVLIDGVDIAKISDAELREVRRKKIAMVFQS--FA 116
Cdd:PRK15134 25 VNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPpvvyPSGDIRFHGESLLHASEQTLRGVRGNKIAMIFQEpmVS 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 117 LMPHMTVLDNTAFGMEL-AGINAEERREKALDALRQVGLENYA---HSYPDELSGGMRQRVGLARALAINPDILLMDEAF 192
Cdd:PRK15134 105 LNPLHTLEKQLYEVLSLhRGMRREAARGEILNCLDRVGIRQAAkrlTDYPHQLSGGERQRVMIAMALLTRPELLIADEPT 184
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 193 SALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVR 262
Cdd:PRK15134 185 TALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAATLFSAPTHPYTQ 254
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
45-244 |
5.70e-32 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 127.53 E-value: 5.70e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 45 KDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVRRKKIAMVFQSFALMPHMTVL 124
Cdd:PRK10535 25 KGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQLRREHFGFIFQRYHLLSHLTAA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 125 DNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQ 204
Cdd:PRK10535 105 QNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDSHSGEEVM 184
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 16130591 205 DELVKLQAKHQrTIVFISHDLDEAMRiGDRIAIMQNGEVV 244
Cdd:PRK10535 185 AILHQLRDRGH-TVIIVTHDPQVAAQ-AERVIEIRDGEIV 222
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
45-253 |
8.52e-32 |
|
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: 126.86 E-value: 8.52e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 45 KDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVrrkkIAMVfqsfalmPHMTVL 124
Cdd:COG5265 375 KGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAA----IGIV-------PQDTVL 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 125 DNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPD-----------ELSGGMRQRVGLARALAINPDILLMDEAFS 193
Cdd:COG5265 444 FNDTIAYNIAYGRPDASEEEVEAAARAAQIHDFIESLPDgydtrvgerglKLSGGEKQRVAIARTLLKNPPILIFDEATS 523
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16130591 194 ALDPliRTEM--QDELVKLqAKHQRTIVfISHDLDEAMRiGDRIAIMQNGEVVQVGTPDEIL 253
Cdd:COG5265 524 ALDS--RTERaiQAALREV-ARGRTTLV-IAHRLSTIVD-ADEILVLEAGRIVERGTHAELL 580
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
30-256 |
1.44e-31 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 120.48 E-value: 1.44e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 30 SKEQILEKTGLS------LGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDaelREV 103
Cdd:PRK11300 1 MSQPLLSVSGLMmrfgglLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPG---HQI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 104 RRKKIAMVFQSFALMPHMTVLDN----------TAFgmeLAGI-------NAE-ERREKALDALRQVGLENYAHSYPDEL 165
Cdd:PRK11300 78 ARMGVVRTFQHVRLFREMTVIENllvaqhqqlkTGL---FSGLlktpafrRAEsEALDRAATWLERVGLLEHANRQAGNL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 166 SGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQ 245
Cdd:PRK11300 155 AYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLA 234
|
250
....*....|.
gi 16130591 246 VGTPDEILNNP 256
Cdd:PRK11300 235 NGTPEEIRNNP 245
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
34-253 |
1.64e-31 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 120.12 E-value: 1.64e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 34 ILEKTGLSLG------VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELrevrRKK 107
Cdd:PRK11231 2 TLRTENLTVGygtkriLNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQL----ARR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 108 IAMVFQSFALMPHMTVLDNTAFG----MELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINP 183
Cdd:PRK11231 78 LALLPQHHLTPEGITVRELVAYGrspwLSLWGRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDT 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 184 DILLMDEAFSALDPLIRTEMQDELVKLQAKhQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEIL 253
Cdd:PRK11231 158 PVVLLDEPTTYLDINHQVELMRLMRELNTQ-GKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVM 226
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
59-256 |
2.36e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 120.29 E-value: 2.36e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 59 IMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKisdAELREVRrKKIAMVFQS-----FAlmphMTVLDNTAFGMEL 133
Cdd:PRK13652 35 VIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITK---ENIREVR-KFVGLVFQNpddqiFS----PTVEQDIAFGPIN 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 134 AGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQAK 213
Cdd:PRK13652 107 LGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPET 186
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 16130591 214 HQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNP 256
Cdd:PRK13652 187 YGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
44-244 |
3.15e-31 |
|
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: 118.13 E-value: 3.15e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAkisdaelREVRRKKIAMVFQsfalmpHM-- 121
Cdd:cd03226 16 LDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIK-------AKERRKSIGYVMQ------DVdy 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 122 -----TVLDNTAFGMElagiNAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALD 196
Cdd:cd03226 83 qlftdSVREELLLGLK----ELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLD 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 16130591 197 PlIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVV 244
Cdd:cd03226 159 Y-KNMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
23-235 |
2.01e-30 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 116.42 E-value: 2.01e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 23 KYIEQGLSKEQILekTGLSLGVKDAslaieegEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELRE 102
Cdd:PRK10584 14 KSVGQGEHELSIL--TGVELVVKRG-------ETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 103 VRRKKIAMVFQSFALMPHMTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAIN 182
Cdd:PRK10584 85 LRAKHVGFVFQSFMLIPTLNALENVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGR 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 16130591 183 PDILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRI 235
Cdd:PRK10584 165 PDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLAARCDRRL 217
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
45-256 |
3.74e-30 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 122.52 E-value: 3.74e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 45 KDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELrevrRKKIAMVFQSFALMPHmTVL 124
Cdd:TIGR00958 498 KGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYL----HRQVALVGQEPVLFSG-SVR 572
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 125 DNTAFGM---ELAGINAEERREKALDALrqVGLENYAHSYPDE----LSGGMRQRVGLARALAINPDILLMDEAFSALDp 197
Cdd:TIGR00958 573 ENIAYGLtdtPDEEIMAAAKAANAHDFI--MEFPNGYDTEVGEkgsqLSGGQKQRIAIARALVRKPRVLILDEATSALD- 649
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 16130591 198 lirTEMQDELVKLQAKHQRTIVFISHDLDEAMRiGDRIAIMQNGEVVQVGTPDEILNNP 256
Cdd:TIGR00958 650 ---AECEQLLQESRSRASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQLMEDQ 704
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
59-257 |
8.46e-30 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 118.05 E-value: 8.46e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 59 IMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGvdiAKISDAELR-----EVRRkkIAMVFQSFALMPHMTVLDNTAFGMel 133
Cdd:PRK11144 29 IFGRSGAGKTSLINAISGLTRPQKGRIVLNG---RVLFDAEKGiclppEKRR--IGYVFQDARLFPHYKVRGNLRYGM-- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 134 aginAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQAK 213
Cdd:PRK11144 102 ----AKSMVAQFDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLERLARE 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 16130591 214 HQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPA 257
Cdd:PRK11144 178 INIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVWASSA 221
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
5-247 |
1.36e-29 |
|
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: 114.17 E-value: 1.36e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 5 LEIKNLYKIFgehpqRAFKYIEQGLSKEQILEKTGLS---LGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPT 81
Cdd:cd03220 1 IELENVSKSY-----PTYKGGSSSLKKLGILGRKGEVgefWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 82 RGQVLIDGvdiaKISdaelrevrrkkiAMVFQSFALMPHMTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSY 161
Cdd:cd03220 76 SGTVTVRG----RVS------------SLLGLGGGFNPELTGRENIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLP 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 162 PDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQaKHQRTIVFISHDLDEAMRIGDRIAIMQNG 241
Cdd:cd03220 140 VKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELL-KQGKTVILVSHDPSSIKRLCDRALVLEKG 218
|
....*.
gi 16130591 242 EVVQVG 247
Cdd:cd03220 219 KIRFDG 224
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
32-243 |
2.59e-29 |
|
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: 112.14 E-value: 2.59e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 32 EQILEKTGLSLG--VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISdaeLREVRRKKIA 109
Cdd:cd03215 2 EPVLEVRGLSVKgaVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRS---PRDAIRAGIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 110 MV---FQSFALMPHMTVLDNTAFgmelaginaeerrekaldalrqvglenyahsyPDELSGGMRQRVGLARALAINPDIL 186
Cdd:cd03215 79 YVpedRKREGLVLDLSVAENIAL--------------------------------SSLLSGGNQQKVVLARWLARDPRVL 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 16130591 187 LMDEAFSALDPLIRTEMQDELVKLqAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEV 243
Cdd:cd03215 127 ILDEPTRGVDVGAKAEIYRLIREL-ADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
48-260 |
3.27e-29 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 115.77 E-value: 3.27e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEP----TRGQVLIDGVDIAKISDAELREVRRKKIAMVFQ--SFALMPHM 121
Cdd:COG4170 27 SLTLNEGEIRGLVGESGSGKSLIAKAICGITKDnwhvTADRFRWNGIDLLKLSPRERRKIIGREIAMIFQepSSCLDPSA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 122 TVLDNTAFGM---ELAGI---NAEERREKALDALRQVGLENYAH---SYPDELSGGMRQRVGLARALAINPDILLMDEAF 192
Cdd:COG4170 107 KIGDQLIEAIpswTFKGKwwqRFKWRKKRAIELLHRVGIKDHKDimnSYPHELTEGECQKVMIAMAIANQPRLLIADEPT 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16130591 193 SALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDY 260
Cdd:COG4170 187 NAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYCGQTVESGPTEQILKSPHHPY 254
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
44-243 |
9.81e-29 |
|
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: 110.38 E-value: 9.81e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELRevrrKKIAMVFQSFALMPHmTV 123
Cdd:cd03246 18 LRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELG----DHVGYLPQDDELFSG-SI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 124 LDNTafgmelaginaeerrekaldalrqvglenyahsypdeLSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEM 203
Cdd:cd03246 93 AENI-------------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERAL 135
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 16130591 204 QDELVKLQAKhQRTIVFISHDLdEAMRIGDRIAIMQNGEV 243
Cdd:cd03246 136 NQAIAALKAA-GATRIVIAHRP-ETLASADRILVLEDGRV 173
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
44-256 |
9.83e-29 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 116.09 E-value: 9.83e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELrevrRKKIAMVFQSFAL------ 117
Cdd:PRK09536 19 LDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAA----SRRVASVPQDTSLsfefdv 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 118 --------MPHMTVLDntafGMELAGINAEERrekaldALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMD 189
Cdd:PRK09536 95 rqvvemgrTPHRSRFD----TWTETDRAAVER------AMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLD 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16130591 190 EAFSALD--PLIRTEmqdELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNP 256
Cdd:PRK09536 165 EPTASLDinHQVRTL---ELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVLTAD 230
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
44-252 |
1.28e-28 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 118.30 E-value: 1.28e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIakisDAELREVRRKKIAMVfQSFALMPHMTV 123
Cdd:NF033858 282 VDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPV----DAGDIATRRRVGYMS-QAFSLYGELTV 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 124 LDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEM 203
Cdd:NF033858 357 RQNLELHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVARDMF 436
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 16130591 204 QDELVKLQAKHQRTIvFIS-HDLDEAMRIgDRIAIMQNGEVVQVGTPDEI 252
Cdd:NF033858 437 WRLLIELSREDGVTI-FIStHFMNEAERC-DRISLMHAGRVLASDTPAAL 484
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
39-260 |
1.45e-28 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 114.05 E-value: 1.45e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 39 GLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEP---TRGQVLIDGVDIAKISDAELREVRRKKIAMVFQS- 114
Cdd:PRK09473 27 GDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAAngrIGGSATFNGREILNLPEKELNKLRAEQISMIFQDp 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 115 -FALMPHMTVLDNTafgMEL----AGINAEERRE---KALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDIL 186
Cdd:PRK09473 107 mTSLNPYMRVGEQL---MEVlmlhKGMSKAEAFEesvRMLDAVKMPEARKRMKMYPHEFSGGMRQRVMIAMALLCRPKLL 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16130591 187 LMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDY 260
Cdd:PRK09473 184 IADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARDVFYQPSHPY 257
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
54-244 |
3.33e-28 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 110.35 E-value: 3.33e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 54 GEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVRRKkIAMVFQSFALMPHMTVLDNTAFGMEL 133
Cdd:PRK10908 28 GEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPFLRRQ-IGMIFQDHHLLMDRTVYDNVAIPLII 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 134 AGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDplirTEMQDELVKLQAK 213
Cdd:PRK10908 107 AGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLD----DALSEGILRLFEE 182
|
170 180 190
....*....|....*....|....*....|....
gi 16130591 214 HQR---TIVFISHDLDEAMRIGDRIAIMQNGEVV 244
Cdd:PRK10908 183 FNRvgvTVLMATHDIGLISRRSYRMLTLSDGHLH 216
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
44-225 |
3.36e-28 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 115.92 E-value: 3.36e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELRevrrkKIAMVFQSFALMPHMTV 123
Cdd:TIGR02868 351 LDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVR-----RRVSVCAQDAHLFDTTV 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 124 LDNTAFGmelagiNAEERREKALDALRQVGLENYAHSYPD-----------ELSGGMRQRVGLARALAINPDILLMDEAF 192
Cdd:TIGR02868 426 RENLRLA------RPDATDEELWAALERVGLADWLRALPDgldtvlgeggaRLSGGERQRLALARALLADAPILLLDEPT 499
|
170 180 190
....*....|....*....|....*....|...
gi 16130591 193 SALDPLIRTEMQDELvkLQAKHQRTIVFISHDL 225
Cdd:TIGR02868 500 EHLDAETADELLEDL--LAALSGRTVVLITHHL 530
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
39-249 |
5.83e-28 |
|
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: 109.51 E-value: 5.83e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 39 GLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELrevrRKKIAMVFQSFALM 118
Cdd:cd03244 15 NLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDL----RSRISIIPQDPVLF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 119 PHmTVLDNtafgMELAGINAEERREKALDalrQVGLENYAHSYPDEL-----------SGGMRQRVGLARALAINPDILL 187
Cdd:cd03244 91 SG-TIRSN----LDPFGEYSDEELWQALE---RVGLKEFVESLPGGLdtvveeggenlSVGQRQLLCLARALLRKSKILV 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 188 MDEAFSALDP--------LIRTEMQDelvklqakhqRTIVFISHDLDEAMRIgDRIAIMQNGEVVQVGTP 249
Cdd:cd03244 163 LDEATASVDPetdaliqkTIREAFKD----------CTVLTIAHRLDTIIDS-DRILVLDKGRVVEFDSP 221
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
44-254 |
1.21e-27 |
|
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: 114.46 E-value: 1.21e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVrrkkIAMVFQSFALMPHmTV 123
Cdd:COG4618 348 LRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRH----IGYLPQDVELFDG-TI 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 124 LDNTA-FGmelaginaEERREKALDALRQVGlenyAH----SYPD-----------ELSGGMRQRVGLARALAINPDILL 187
Cdd:COG4618 423 AENIArFG--------DADPEKVVAAAKLAG----VHemilRLPDgydtrigeggaRLSGGQRQRIGLARALYGDPRLVV 490
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16130591 188 MDEAFSALDP-----LIRTemqdelVKLQAKHQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEILN 254
Cdd:COG4618 491 LDEPNSNLDDegeaaLAAA------IRALKARGATVVVITHRP-SLLAAVDKLLVLRDGRVQAFGPRDEVLA 555
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
44-243 |
1.83e-27 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 108.33 E-value: 1.83e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGvdiAKISDAELREVRRkKIAMVFQSFALMPHmTV 123
Cdd:cd03248 30 LQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDG---KPISQYEHKYLHS-KVSLVGQEPVLFAR-SL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 124 LDNTAFGmeLAGINAEERREKALDALRQVGLENYAHSYPDE-------LSGGMRQRVGLARALAINPDILLMDEAFSALD 196
Cdd:cd03248 105 QDNIAYG--LQSCSFECVKEAAQKAHAHSFISELASGYDTEvgekgsqLSGGQKQRVAIARALIRNPQVLILDEATSALD 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 16130591 197 plIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRiGDRIAIMQNGEV 243
Cdd:cd03248 183 --AESEQQVQQALYDWPERRTVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
35-227 |
1.87e-27 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 108.26 E-value: 1.87e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 35 LEKTGLSLG----VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDaelrEVRRKKIAM 110
Cdd:PRK10247 10 LQNVGYLAGdakiLNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKP----EIYRQQVSY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 111 VFQSFALMPHmTVLDNTAFGMELAGINAEERreKALDALRQVGL-ENYAHSYPDELSGGMRQRVGLARALAINPDILLMD 189
Cdd:PRK10247 86 CAQTPTLFGD-TVYDNLIFPWQIRNQQPDPA--IFLDDLERFALpDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLD 162
|
170 180 190
....*....|....*....|....*....|....*...
gi 16130591 190 EAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDE 227
Cdd:PRK10247 163 EITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDE 200
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
59-268 |
2.39e-27 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 109.42 E-value: 2.39e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 59 IMGLSGSGKSTMVRLLNRLIEPTRG-----QVLIDGVDIAKISDaeLREVRRKkIAMVFQSFALMPhMTVLDNTafgmeL 133
Cdd:PRK14271 52 LMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIFNYRD--VLEFRRR-VGMLFQRPNPFP-MSIMDNV-----L 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 134 AGINA------EERREKALDALRQVGL----ENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPlIRTEM 203
Cdd:PRK14271 123 AGVRAhklvprKEFRGVAQARLTEVGLwdavKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDP-TTTEK 201
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16130591 204 QDELVKLQAKhQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFFRGV 268
Cdd:PRK14271 202 IEEFIRSLAD-RLTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKHAETARYVAGL 265
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
43-260 |
2.94e-27 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 108.86 E-value: 2.94e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDG-----VDIAKISDAELREVRRKKIAMVFQSFAL 117
Cdd:PRK11701 21 GCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMrdgqlRDLYALSEAERRRLLRTEWGFVHQHPRD 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 118 MPHMTVldntafgmeLAGINAEER------------REKALDALRQVGLE-NYAHSYPDELSGGMRQRVGLARALAINPD 184
Cdd:PRK11701 101 GLRMQV---------SAGGNIGERlmavgarhygdiRATAGDWLERVEIDaARIDDLPTTFSGGMQQRLQIARNLVTHPR 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16130591 185 ILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDY 260
Cdd:PRK11701 172 LVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVVESGLTDQVLDDPQHPY 247
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
45-255 |
4.67e-27 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 113.00 E-value: 4.67e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 45 KDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREvrrkKIAMVFQSFALMPHmTVL 124
Cdd:PRK11160 357 KGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQ----AISVVSQRVHLFSA-TLR 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 125 DNTAfgmeLAGINAEErrEKALDALRQVGLENYAHSypDE------------LSGGMRQRVGLARALAINPDILLMDEAF 192
Cdd:PRK11160 432 DNLL----LAAPNASD--EALIEVLQQVGLEKLLED--DKglnawlgeggrqLSGGEQRRLGIARALLHDAPLLLLDEPT 503
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16130591 193 SALDPliRTEMQdeLVKLQAKH--QRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEILNN 255
Cdd:PRK11160 504 EGLDA--ETERQ--ILELLAEHaqNKTVLMITHRL-TGLEQFDRICVMDNGQIIEQGTHQELLAQ 563
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
33-249 |
5.91e-27 |
|
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: 113.57 E-value: 5.91e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 33 QILEKTGLSlGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAElrevrRKKIAMVF 112
Cdd:TIGR01257 936 KIFEPSGRP-AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDAV-----RQSLGMCP 1009
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 113 QSFALMPHMTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAF 192
Cdd:TIGR01257 1010 QHNILFHHLTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPT 1089
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 16130591 193 SALDPLIRTEMQDELVKLQAKhqRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTP 249
Cdd:TIGR01257 1090 SGVDPYSRRSIWDLLLKYRSG--RTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTP 1144
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
43-238 |
6.25e-27 |
|
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: 112.38 E-value: 6.25e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELrevrRKKIAMVFQSfalmPHM- 121
Cdd:TIGR02857 337 ALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSW----RDQIAWVPQH----PFLf 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 122 --TVLDNTAFGmeLAGINAEERREkaldALRQVGLENYAHSYPD-----------ELSGGMRQRVGLARALAINPDILLM 188
Cdd:TIGR02857 409 agTIAENIRLA--RPDASDAEIRE----ALERAGLDEFVAALPQgldtpigeggaGLSGGQAQRLALARAFLRDAPLLLL 482
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 16130591 189 DEAFSALDPLIRTEMQDELvkLQAKHQRTIVFISHDLdEAMRIGDRIAIM 238
Cdd:TIGR02857 483 DEPTAHLDAETEAEVLEAL--RALAQGRTVLLVTHRL-ALAALADRIVVL 529
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
44-254 |
7.92e-27 |
|
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes a multidomain ABC transporter subunit that is one of three protein families associated with some regularity with a distinctive family of putative bacteriocins. It includes a bacteriocin-processing peptidase domain at the N-terminus. Model TIGR03793 describes a conserved propeptide region for this bacteriocin family, unusual because it shows obvious homology a region of the enzyme nitrile hydratase up to the classic Gly-Gly cleavage motif. This family is therefore predicted to be a subunit of a bacteriocin processing and export system characteristic to this system that we designate NHLM, Nitrile Hydratase Leader Microcin. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274788 [Multi-domain] Cd Length: 710 Bit Score: 112.73 E-value: 7.92e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISdaelREVRRKKIAMVFQSFALMpHMTV 123
Cdd:TIGR03796 495 IENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIPREEIP----REVLANSVAMVDQDIFLF-EGTV 569
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 124 LDNTAfgMELAGINAEERREKALDA------LRQVGleNYAHSYPD---ELSGGMRQRVGLARALAINPDILLMDEAFSA 194
Cdd:TIGR03796 570 RDNLT--LWDPTIPDADLVRACKDAaihdviTSRPG--GYDAELAEggaNLSGGQRQRLEIARALVRNPSILILDEATSA 645
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16130591 195 LDPlirtemQDELVKLQAKHQR--TIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEILN 254
Cdd:TIGR03796 646 LDP------ETEKIIDDNLRRRgcTCIIVAHRL-STIRDCDEIIVLERGKVVQRGTHEELWA 700
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
44-253 |
8.63e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 108.01 E-value: 8.63e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDG--VDIAKISDAELREvrrkKIAMVFQS-----FA 116
Cdd:PRK13636 22 LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGkpIDYSRKGLMKLRE----SVGMVFQDpdnqlFS 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 117 lmphMTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALD 196
Cdd:PRK13636 98 ----ASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLD 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 16130591 197 PLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEIL 253
Cdd:PRK13636 174 PMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVF 230
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
33-263 |
9.59e-27 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 107.09 E-value: 9.59e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 33 QILEKTGLSLG-----VKDASLAIEEGEIFVIMGLSGSGKS-TMVRLLNRL---IEPTRGQVLIDGVDIAkisdaeLREV 103
Cdd:PRK10418 3 QQIELRNIALQaaqplVHGVSLTLQRGRVLALVGGSGSGKSlTCAAALGILpagVRQTAGRVLLDGKPVA------PCAL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 104 RRKKIAMVFQS--FALMPHMTVLDNTAFGMELAGINAEERRekALDALRQVGLENYA---HSYPDELSGGMRQRVGLARA 178
Cdd:PRK10418 77 RGRKIATIMQNprSAFNPLHTMHTHARETCLALGKPADDAT--LTAALEAVGLENAArvlKLYPFEMSGGMLQRMMIALA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 179 LAINPDILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPAN 258
Cdd:PRK10418 155 LLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPKH 234
|
....*
gi 16130591 259 DYVRT 263
Cdd:PRK10418 235 AVTRS 239
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
29-253 |
2.25e-26 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 107.58 E-value: 2.25e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 29 LSKEQILEKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISdaelrEVRRKKI 108
Cdd:PRK13537 8 IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRA-----RHARQRV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 109 AMVFQSFALMPHMTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLM 188
Cdd:PRK13537 83 GVVPQFDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16130591 189 DEAFSALDPLIRTEMQDELVKLQAKhQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEIL 253
Cdd:PRK13537 163 DEPTTGLDPQARHLMWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALI 226
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
42-247 |
2.60e-26 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 105.43 E-value: 2.60e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 42 LGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEP---TRGQVLIDGVDIAkisdaelREVRRKKIAMVFQSFALM 118
Cdd:cd03234 21 RILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGggtTSGQILFNGQPRK-------PDQFQKCVAYVRQDDILL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 119 PHMTVLDNTAFGMELAG--INAEERREK--ALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSA 194
Cdd:cd03234 94 PGLTVRETLTYTAILRLprKSSDAIRKKrvEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSG 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 16130591 195 LDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVG 247
Cdd:cd03234 174 LDSFTALNLVSTLSQLARRNRIVILTIHQPRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
32-260 |
1.02e-25 |
|
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: 104.53 E-value: 1.02e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 32 EQILEKTGLS------LGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDG-----VDIAKISDAEL 100
Cdd:TIGR02323 1 KPLLQVSGLSksygggKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMrsgaeLELYQLSEAER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 101 REVRRKKIAMVFQSFALMPHMTVLDNTAFGMELAGINAEER---REKALDALRQVGLE-NYAHSYPDELSGGMRQRVGLA 176
Cdd:TIGR02323 81 RRLMRTEWGFVHQNPRDGLRMRVSAGANIGERLMAIGARHYgniRATAQDWLEEVEIDpTRIDDLPRAFSGGMQQRLQIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 177 RALAINPDILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNP 256
Cdd:TIGR02323 161 RNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRVVESGLTDQVLDDP 240
|
....
gi 16130591 257 ANDY 260
Cdd:TIGR02323 241 QHPY 244
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
44-254 |
1.39e-25 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 106.07 E-value: 1.39e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAkiSDAELRevrRKKIAMVFQSFALMPHMTV 123
Cdd:PRK13536 57 VNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVP--ARARLA---RARIGVVPQFDNLDLEFTV 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 124 LDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEM 203
Cdd:PRK13536 132 RENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLI 211
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 16130591 204 QDELVKLQAKhQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILN 254
Cdd:PRK13536 212 WERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHALID 261
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
48-256 |
1.65e-25 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 104.10 E-value: 1.65e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKI-SDAELREVrrkkiAMVFQSFALMPHMTVLDN 126
Cdd:PRK10575 31 SLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWsSKAFARKV-----AYLPQQLPAAEGMTVREL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 127 TAFGM-----ELAGINAEERrEKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRT 201
Cdd:PRK10575 106 VAIGRypwhgALGRFGAADR-EKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQV 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 16130591 202 EMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNP 256
Cdd:PRK10575 185 DVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRGE 239
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
49-266 |
2.17e-25 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 103.94 E-value: 2.17e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 49 LAIEEGEIFVIMGLSGSGKSTMVRLLNRLIE-----PTRGQVLIDGVDIAKISDAELREvRRKKIAMVFQSFALMPHMTV 123
Cdd:PRK09984 25 LNIHHGEMVALLGPSGSGKSTLLRHLSGLITgdksaGSHIELLGRTVQREGRLARDIRK-SRANTGYIFQQFNLVNRLSV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 124 LDN--------TAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSAL 195
Cdd:PRK09984 104 LENvligalgsTPFWRTCFSWFTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVILADEPIASL 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16130591 196 DPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFFR 266
Cdd:PRK09984 184 DPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQQFDNERFDHLYRSINR 254
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
34-252 |
4.03e-25 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 106.64 E-value: 4.03e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 34 ILEKTGLSLG--VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDG--VDIAKISDAelrevRRKKIA 109
Cdd:COG1129 256 VLEVEGLSVGgvVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGkpVRIRSPRDA-----IRAGIA 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 110 MV---FQSFALMPHMTVLDNTA---------FGMelagINAEERREKALDALRQVGLenyahSYPD------ELSGGMRQ 171
Cdd:COG1129 331 YVpedRKGEGLVLDLSIRENITlasldrlsrGGL----LDRRRERALAEEYIKRLRI-----KTPSpeqpvgNLSGGNQQ 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 172 RVGLARALAINPDILLMDE--------AfsaldpliRTEMQDELVKLqAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEV 243
Cdd:COG1129 402 KVVLAKWLATDPKVLILDEptrgidvgA--------KAEIYRLIREL-AAEGKAVIVISSELPELLGLSDRILVMREGRI 472
|
....*....
gi 16130591 244 VQVGTPDEI 252
Cdd:COG1129 473 VGELDREEA 481
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
44-255 |
5.56e-25 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 102.28 E-value: 5.56e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISdaeLREVRRKKIAMVFQSFALMPHMTV 123
Cdd:PRK10895 19 VEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLP---LHARARRGIGYLPQEASIFRRLSV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 124 LDNTAFGMEL-AGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTE 202
Cdd:PRK10895 96 YDNLMAVLQIrDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPISVID 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 16130591 203 MQDELVKLQaKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNN 255
Cdd:PRK10895 176 IKRIIEHLR-DSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQD 227
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
45-254 |
1.19e-24 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 105.87 E-value: 1.19e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 45 KDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREvrrkKIAMVFQSFALMpHMTVL 124
Cdd:PRK11176 360 RNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRN----QVALVSQNVHLF-NDTIA 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 125 DNTAFGME----LAGINAEERREKALDALRQV--GL-----ENYAhsypdELSGGMRQRVGLARALAINPDILLMDEAFS 193
Cdd:PRK11176 435 NNIAYARTeqysREQIEEAARMAYAMDFINKMdnGLdtvigENGV-----LLSGGQRQRIAIARALLRDSPILILDEATS 509
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16130591 194 ALDPLIRTEMQDELVKLQakHQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEILN 254
Cdd:PRK11176 510 ALDTESERAIQAALDELQ--KNRTSLVIAHRL-STIEKADEILVVEDGEIVERGTHAELLA 567
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
44-247 |
1.89e-24 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 99.16 E-value: 1.89e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLL-NRLIEP-TRGQVLIDGVDIAKISdaelrevRRKKIAMVFQSFALMPHM 121
Cdd:cd03213 25 LKNVSGKAKPGELTAIMGPSGAGKSTLLNALaGRRTGLgVSGEVLINGRPLDKRS-------FRKIIGYVPQDDILHPTL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 122 TVLDNTAFGMELAGInaeerrekaldalrqvglenyahsypdelSGGMRQRVGLARALAINPDILLMDEAFSALDP---- 197
Cdd:cd03213 98 TVRETLMFAAKLRGL-----------------------------SGGERKRVSIALELVSNPSLLFLDEPTSGLDSssal 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 16130591 198 -LIRTemqdeLVKLqAKHQRTIVFISHDL-DEAMRIGDRIAIMQNGEVVQVG 247
Cdd:cd03213 149 qVMSL-----LRRL-ADTGRTIICSIHQPsSEIFELFDKLLLLSQGRVIYFG 194
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
44-238 |
3.97e-24 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 98.46 E-value: 3.97e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVlidgvdiakisdaelREVRRKKIAMVFQSFAL---MPh 120
Cdd:NF040873 8 LHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTV---------------RRAGGARVAYVPQRSEVpdsLP- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 121 MTVLDNTAFGM-----ELAGINAEERREKAlDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSAL 195
Cdd:NF040873 72 LTVRDLVAMGRwarrgLWRRLTRDDRAAVD-DALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGL 150
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 16130591 196 DPLIRTEMqDELVKLQAKHQRTIVFISHDLDEAMRIgDRIAIM 238
Cdd:NF040873 151 DAESRERI-IALLAEEHARGATVVVVTHDLELVRRA-DPCVLL 191
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
44-268 |
9.91e-24 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 100.65 E-value: 9.91e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLL----NRLIEPTRGQVLIDGVDIAKISDAELREVRRKKIAMVFQSfalmP 119
Cdd:PRK15093 23 VDRVSMTLTEGEIRGLVGESGSGKSLIAKAIcgvtKDNWRVTADRMRFDDIDLLRLSPRERRKLVGHNVSMIFQE----P 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 120 HMTVLDNTAFGMELagINA--------------EERREKALDALRQVGLENY---AHSYPDELSGGMRQRVGLARALAIN 182
Cdd:PRK15093 99 QSCLDPSERVGRQL--MQNipgwtykgrwwqrfGWRKRRAIELLHRVGIKDHkdaMRSFPYELTEGECQKVMIAIALANQ 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 183 PDILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVR 262
Cdd:PRK15093 177 PRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTVETAPSKELVTTPHHPYTQ 256
|
....*.
gi 16130591 263 TFFRGV 268
Cdd:PRK15093 257 ALIRAI 262
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
29-253 |
1.04e-23 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 99.29 E-value: 1.04e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 29 LSKEQILEKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDaelREVRRKkI 108
Cdd:PRK10253 8 LRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYAS---KEVARR-I 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 109 AMVFQSFALMPHMTVLDNTAFG----MELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPD 184
Cdd:PRK10253 84 GLLAQNATTPGDITVQELVARGryphQPLFTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETA 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16130591 185 ILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEIL 253
Cdd:PRK10253 164 IMLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIV 232
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
22-247 |
3.21e-23 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 95.46 E-value: 3.21e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 22 FKYIEQglsKEQILektglslgvKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAelr 101
Cdd:cd03247 8 FSYPEQ---EQQVL---------KNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKA--- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 102 evRRKKIAMVFQSfalmPHM---TVLDNtafgmelaginaeerrekaldalrqVGLEnyahsypdeLSGGMRQRVGLARA 178
Cdd:cd03247 73 --LSSLISVLNQR----PYLfdtTLRNN-------------------------LGRR---------FSGGERQRLALARI 112
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16130591 179 LAINPDILLMDEAFSALDPliRTEMQDELVKLQAKHQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVG 247
Cdd:cd03247 113 LLQDAPIVLLDEPTVGLDP--ITERQLLSLIFEVLKDKTLIWITHHL-TGIEHMDKILFLENGKIIMQG 178
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
25-286 |
4.71e-23 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 100.63 E-value: 4.71e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 25 IEQGLSKEQILEKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVr 104
Cdd:PRK09700 2 ATPYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQL- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 105 rkKIAMVFQSFALMPHMTVLDNTAFGMELA----GINA---EERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLAR 177
Cdd:PRK09700 81 --GIGIIYQELSVIDELTVLENLYIGRHLTkkvcGVNIidwREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 178 ALAINPDILLMDEAFSALdplirteMQDELVKLQA------KHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDE 251
Cdd:PRK09700 159 TLMLDAKVIIMDEPTSSL-------TNKEVDYLFLimnqlrKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSD 231
|
250 260 270
....*....|....*....|....*....|....*
gi 16130591 252 IlnnpANDYVRTFFRGVDISQVFSAKDIARRTPNG 286
Cdd:PRK09700 232 V----SNDDIVRLMVGRELQNRFNAMKENVSNLAH 262
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
32-253 |
1.62e-22 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 96.23 E-value: 1.62e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 32 EQILEktGLSLgvkDASLAIEEGeifvIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDG--VDIAKISDAELREvrrkKIA 109
Cdd:PRK13638 14 EPVLK--GLNL---DFSLSPVTG----LVGANGCGKSTLFMNLSGLLRPQKGAVLWQGkpLDYSKRGLLALRQ----QVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 110 MVFQSFALMPHMTVLD-NTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLM 188
Cdd:PRK13638 81 TVFQDPEQQIFYTDIDsDIAFSLRNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16130591 189 DEAFSALDPLIRTEMQdELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEIL 253
Cdd:PRK13638 161 DEPTAGLDPAGRTQMI-AIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVF 224
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
32-252 |
2.79e-22 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 98.56 E-value: 2.79e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 32 EQILEKTGLSL-------GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISdaeLREVR 104
Cdd:COG3845 255 EVVLEVENLSVrddrgvpALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLS---PRERR 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 105 RKKIAMV---FQSFALMPHMTVLDNTAFG----MELAG---INAEERREKALDALRQ-----VGLENYAHSypdeLSGGM 169
Cdd:COG3845 332 RLGVAYIpedRLGRGLVPDMSVAENLILGryrrPPFSRggfLDRKAIRAFAEELIEEfdvrtPGPDTPARS----LSGGN 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 170 RQRVGLARALAINPDILLMDEAFSALDP----LIRtemqDELVKLQAKhQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQ 245
Cdd:COG3845 408 QQKVILARELSRDPKLLIAAQPTRGLDVgaieFIH----QRLLELRDA-GAAVLLISEDLDEILALSDRIAVMYEGRIVG 482
|
....*..
gi 16130591 246 VGTPDEI 252
Cdd:COG3845 483 EVPAAEA 489
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
5-244 |
5.58e-21 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 90.85 E-value: 5.58e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 5 LEIKNLYKIFGEHPQRA-FKYIEQGLSKEQILEKTGLslgvKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRG 83
Cdd:cd03267 1 IEVSNLSKSYRVYSKEPgLIGSLKSLFKRKYREVEAL----KGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 84 QVLIDGVDIAKISDAELRevrrkKIAMVF-------------QSFALMPHMTVLDNTAFGmelaginaeERREKALDALR 150
Cdd:cd03267 77 EVRVAGLVPWKRRKKFLR-----RIGVVFgqktqlwwdlpviDSFYLLAAIYDLPPARFK---------KRLDELSELLD 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 151 qvgLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMR 230
Cdd:cd03267 143 ---LEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEA 219
|
250
....*....|....
gi 16130591 231 IGDRIAIMQNGEVV 244
Cdd:cd03267 220 LARRVLVIDKGRLL 233
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
44-249 |
7.10e-21 |
|
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: 89.78 E-value: 7.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKIsdaELREVRRkkiamvfqSFALMPHMTV 123
Cdd:cd03369 24 LKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTI---PLEDLRS--------SLTIIPQDPT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 124 LDNTAFGMELAGINaEERREKALDALR-QVGLENyahsypdeLSGGMRQRVGLARALAINPDILLMDEAFSALD------ 196
Cdd:cd03369 93 LFSGTIRSNLDPFD-EYSDEEIYGALRvSEGGLN--------LSQGQRQLLCLARALLKRPRVLVLDEATASIDyatdal 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 16130591 197 --PLIRTEMQDElvklqakhqrTIVFISHDLDEAMRIgDRIAIMQNGEVVQVGTP 249
Cdd:cd03369 164 iqKTIREEFTNS----------TILTIAHRLRTIIDY-DKILVMDAGEVKEYDHP 207
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
36-242 |
1.76e-20 |
|
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: 88.68 E-value: 1.76e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 36 EKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTmvrLLNRLI---EPTRGQVLIDGvdiakisdaelrevrrkKIAMVF 112
Cdd:cd03250 13 GEQETSFTLKDINLEVPKGELVAIVGPVGSGKSS---LLSALLgelEKLSGSVSVPG-----------------SIAYVS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 113 QSFALMPhMTVLDNTAFGMELAginaEERREKALDA--LRQvGLENYAHSypDE---------LSGGMRQRVGLARALAI 181
Cdd:cd03250 73 QEPWIQN-GTIRENILFGKPFD----EERYEKVIKAcaLEP-DLEILPDG--DLteigekginLSGGQKQRISLARAVYS 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16130591 182 NPDILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLdEAMRIGDRIAIMQNGE 242
Cdd:cd03250 145 DADIYLLDDPLSAVDAHVGRHIFENCILGLLLNNKTRILVTHQL-QLLPHADQIVVLDNGR 204
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
48-253 |
1.87e-20 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 89.51 E-value: 1.87e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 48 SLAIEEGEIFVIMGLSGSGKSTmvrLLNRL--IEPTRGQVLIDGVDIAKISDAELREVRrkkiAMVFQSFALMPHMTVLD 125
Cdd:COG4138 16 SAQVNAGELIHLIGPNGAGKST---LLARMagLLPGQGEILLNGRPLSDWSAAELARHR----AYLSQQQSPPFAMPVFQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 126 NTAFGMElAGINAEERrEKALDAL-RQVGLENYAHSYPDELSGGMRQRVGLARAL-----AINPD--ILLMDEAFSALDp 197
Cdd:COG4138 89 YLALHQP-AGASSEAV-EQLLAQLaEALGLEDKLSRPLTQLSGGEWQRVRLAAVLlqvwpTINPEgqLLLLDEPMNSLD- 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 16130591 198 lIRTE-MQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEIL 253
Cdd:COG4138 166 -VAQQaALDRLLRELCQQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEVM 221
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
37-253 |
2.55e-20 |
|
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: 93.47 E-value: 2.55e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 37 KTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELRevrrkkiamvFQsFA 116
Cdd:TIGR00957 1295 REDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLR----------FK-IT 1363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 117 LMPHMTVLDNTAFGMELAGInAEERREKALDALRQVGLENYAHSYPDE-----------LSGGMRQRVGLARALAINPDI 185
Cdd:TIGR00957 1364 IIPQDPVLFSGSLRMNLDPF-SQYSDEEVWWALELAHLKTFVSALPDKldhecaeggenLSVGQRQLVCLARALLRKTKI 1442
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16130591 186 LLMDEAFSALD--------PLIRTEMQDelvklqakhqRTIVFISHDLDEAMRIgDRIAIMQNGEVVQVGTPDEIL 253
Cdd:TIGR00957 1443 LVLDEATAAVDletdnliqSTIRTQFED----------CTVLTIAHRLNTIMDY-TRVIVLDKGEVAEFGAPSNLL 1507
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
48-256 |
2.65e-20 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 92.99 E-value: 2.65e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 48 SLAIEEGEIFVIMGLSGSGKSTmvrLLNRLIE--PTRGQVLIDGVdiakisdaELREVR----RKKIAMVFQSfALMPHM 121
Cdd:PRK11174 370 NFTLPAGQRIALVGPSGAGKTS---LLNALLGflPYQGSLKINGI--------ELRELDpeswRKHLSWVGQN-PQLPHG 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 122 TVLDNTAfgmeLAGINAEErrEKALDALRQVGLENYAHSYPD-----------ELSGGMRQRVGLARALAINPDILLMDE 190
Cdd:PRK11174 438 TLRDNVL----LGNPDASD--EQLQQALENAWVSEFLPLLPQgldtpigdqaaGLSVGQAQRLALARALLQPCQLLLLDE 511
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16130591 191 AFSALDplIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIgDRIAIMQNGEVVQVGTPDEILNNP 256
Cdd:PRK11174 512 PTASLD--AHSEQLVMQALNAASRRQTTLMVTHQLEDLAQW-DQIWVMQDGQIVQQGDYAELSQAG 574
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
43-248 |
6.83e-20 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 91.14 E-value: 6.83e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 43 GVK---DASLAIEEGEIFVIMGLSGSGKSTMVRLLNRlIEPT---RGQVLIDGvdiAKISDAELREVRRKKIAMVFQSFA 116
Cdd:PRK13549 17 GVKaldNVSLKVRAGEIVSLCGENGAGKSTLMKVLSG-VYPHgtyEGEIIFEG---EELQASNIRDTERAGIAIIHQELA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 117 LMPHMTVLDNTAFGMEL--AGI---NAEERREKALdaLRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEA 191
Cdd:PRK13549 93 LVKELSVLENIFLGNEItpGGImdyDAMYLRAQKL--LAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQARLLILDEP 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16130591 192 FSALdplirTEMQDE----LVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEvvQVGT 248
Cdd:PRK13549 171 TASL-----TESETAvlldIIRDLKAHGIACIYISHKLNEVKAISDTICVIRDGR--HIGT 224
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
29-267 |
9.89e-20 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 87.24 E-value: 9.89e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 29 LSKEQILEKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDiakISDAELREVRRKKI 108
Cdd:PRK11614 6 LSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKD---ITDWQTAKIMREAV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 109 AMVFQSFALMPHMTVLDNTAFGMELAGINA-EERREKALDALRQvgLENYAHSYPDELSGGMRQRVGLARALAINPDILL 187
Cdd:PRK11614 83 AIVPEGRRVFSRMTVEENLAMGGFFAERDQfQERIKWVYELFPR--LHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 188 MDEAFSALDPLIRTEMQDELVKLQAKHQrTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILnnpANDYVRTFFRG 267
Cdd:PRK11614 161 LDEPSLGLAPIIIQQIFDTIEQLREQGM-TIFLVEQNANQALKLADRGYVLENGHVVLEDTGDALL---ANEAVRSAYLG 236
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
22-242 |
1.82e-19 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 90.03 E-value: 1.82e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 22 FKYIEQGLSkeqilektglslgVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIakisDAELR 101
Cdd:PRK10522 330 FAYQDNGFS-------------VGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPV----TAEQP 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 102 EVRRKKIAMVFQSFALMPHMTVLDNTAFGMELAginaeerrEKALDAL---RQVGLENYAHSYPDeLSGGMRQRVGLARA 178
Cdd:PRK10522 393 EDYRKLFSAVFTDFHLFDQLLGPEGKPANPALV--------EKWLERLkmaHKLELEDGRISNLK-LSKGQKKRLALLLA 463
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16130591 179 LAINPDILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDlDEAMRIGDRIAIMQNGE 242
Cdd:PRK10522 464 LAEERDILLLDEWAADQDPHFRREFYQVLLPLLQEMGKTIFAISHD-DHYFIHADRLLEMRNGQ 526
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
45-243 |
2.15e-19 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 89.74 E-value: 2.15e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 45 KDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDgvdiakisdaelrevRRKKIAMVFQSFALMPHMTVL 124
Cdd:COG0488 15 DDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIP---------------KGLRIGYLPQEPPLDDDLTVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 125 DN-------------------------TAFGMELA----------GINAEERREKALDALrqvGLENYAHSYP-DELSGG 168
Cdd:COG0488 80 DTvldgdaelraleaeleeleaklaepDEDLERLAelqeefealgGWEAEARAEEILSGL---GFPEEDLDRPvSELSGG 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16130591 169 MRQRVGLARALAINPDILLMDEAFSALDplirTEMQDELVKLQAKHQRTIVFISHD---LDeamRIGDRIAIMQNGEV 243
Cdd:COG0488 157 WRRRVALARALLSEPDLLLLDEPTNHLD----LESIEWLEEFLKNYPGTVLVVSHDryfLD---RVATRILELDRGKL 227
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
48-255 |
2.46e-19 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 90.57 E-value: 2.46e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVrrkkiamvfqsFALMPHMTVLDNT 127
Cdd:PLN03130 1259 SFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKV-----------LGIIPQAPVLFSG 1327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 128 AFGMELAGINAE------ERREKA--LDALRQ--VGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDp 197
Cdd:PLN03130 1328 TVRFNLDPFNEHndadlwESLERAhlKDVIRRnsLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVD- 1406
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16130591 198 lIRTemqDELVklqakhQRTI---------VFISHDLDEAMRIgDRIAIMQNGEVVQVGTPDEILNN 255
Cdd:PLN03130 1407 -VRT---DALI------QKTIreefksctmLIIAHRLNTIIDC-DRILVLDAGRVVEFDTPENLLSN 1462
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
48-197 |
3.90e-19 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 84.72 E-value: 3.90e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAkisdaELREVRRKKIAMVFQSFALMPHMTVLDNT 127
Cdd:TIGR01189 20 SFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLA-----EQRDEPHENILYLGHLPGLKPELSALENL 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 128 AFgmeLAGINAEERREkALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDP 197
Cdd:TIGR01189 95 HF---WAAIHGGAQRT-IEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDK 160
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
44-255 |
5.36e-19 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 87.06 E-value: 5.36e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKisdaelREVR-RKKIAMVF-QSFALMPHM 121
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPFK------RRKEfARRIGVVFgQRSQLWWDL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 122 TVLDNTAFGMELAGINAEERREKaLDALRQV-GLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIR 200
Cdd:COG4586 112 PAIDSFRLLKAIYRIPDAEYKKR-LDELVELlDLGELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSK 190
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 16130591 201 TEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNN 255
Cdd:COG4586 191 EAIREFLKEYNRERGTTILLTSHDMDDIEALCDRVIVIDHGRIIYDGSLEELKER 245
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
48-262 |
1.47e-18 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 88.11 E-value: 1.47e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVrrkkIAMVFQSFALMPHMTVLDNT 127
Cdd:PLN03232 1256 SFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRV----LSIIPQSPVLFSGTVRFNID 1331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 128 AF----------GMELAGI-NAEERREKALDALRQVGLENYahsypdelSGGMRQRVGLARALAINPDILLMDEAFSALD 196
Cdd:PLN03232 1332 PFsehndadlweALERAHIkDVIDRNPFGLDAEVSEGGENF--------SVGQRQLLSLARALLRRSKILVLDEATASVD 1403
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16130591 197 plIRTemqDELVKLQAKHQR---TIVFISHDLDEAMRIgDRIAIMQNGEVVQVGTPDEILNNPANDYVR 262
Cdd:PLN03232 1404 --VRT---DSLIQRTIREEFkscTMLVIAHRLNTIIDC-DKILVLSSGQVLEYDSPQELLSRDTSAFFR 1466
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
45-256 |
1.71e-18 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 87.46 E-value: 1.71e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 45 KDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELrevrRKKIAMVFQSFALMPHmTVL 124
Cdd:PRK10789 332 ENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSW----RSRLAVVSQTPFLFSD-TVA 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 125 DNTAFGMELAgiNAEERREKALDALRQVGLENYAHSYPDE-------LSGGMRQRVGLARALAINPDILLMDEAFSALDP 197
Cdd:PRK10789 407 NNIALGRPDA--TQQEIEHVARLASVHDDILRLPQGYDTEvgergvmLSGGQKQRISIARALLLNAEILILDDALSAVDG 484
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 16130591 198 liRTEMQDELVKLQAKHQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEILNNP 256
Cdd:PRK10789 485 --RTEHQILHNLRQWGEGRTVIISAHRL-SALTEASEILVMQHGHIAQRGNHDQLAQQS 540
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
45-295 |
3.67e-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: 3.67e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 45 KDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEP---TRGQVLIDGVDIakisdaELREVRRKKiAMVFQSFALMPHM 121
Cdd:TIGR00955 42 KNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKgvkGSGSVLLNGMPI------DAKEMRAIS-AYVQQDDLFIPTL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 122 TVLDNTAFGMEL---AGINAEERREKALDALRQVGLENYAHS---YPDE---LSGGMRQRVGLARALAINPDILLMDEAF 192
Cdd:TIGR00955 115 TVREHLMFQAHLrmpRRVTKKEKRERVDEVLQALGLRKCANTrigVPGRvkgLSGGERKRLAFASELLTDPPLLFCDEPT 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 193 SALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILN-------------NPAND 259
Cdd:TIGR00955 195 SGLDSFMAYSVVQVLKGLAQKGKTIICTIHQPSSELFELFDKIILMAEGRVAYLGSPDQAVPffsdlghpcpenyNPADF 274
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 16130591 260 YVRTfFRGVD------------ISQVFSAKDIAR---RTPNGLIRKTPGFG 295
Cdd:TIGR00955 275 YVQV-LAVIPgsenesreriekICDSFAVSDIGRdmlVNTNLWSGKAGGLV 324
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
29-250 |
4.87e-18 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 85.65 E-value: 4.87e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 29 LSKEQILEKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRlIEPT---RGQVLIDGvdiAKISDAELREVRR 105
Cdd:TIGR02633 2 LEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSG-VYPHgtwDGEIYWSG---SPLKASNIRDTER 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 106 KKIAMVFQSFALMPHMTVLDNTAFGMELA------GINAEERREKALdaLRQVGLENYAHSYP-DELSGGMRQRVGLARA 178
Cdd:TIGR02633 78 AGIVIIHQELTLVPELSVAENIFLGNEITlpggrmAYNAMYLRAKNL--LRELQLDADNVTRPvGDYGGGQQQLVEIAKA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16130591 179 LAINPDILLMDEAFSALDPLiRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEvvQVGTPD 250
Cdd:TIGR02633 156 LNKQARLLILDEPSSSLTEK-ETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQ--HVATKD 224
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
48-256 |
5.29e-18 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 82.67 E-value: 5.29e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 48 SLAIEEGEIFVIMGLSGSGKSTmvrLLNRL--IEPTRGQVLIDGVDIAKISDAELREVR-------RKKIAM-VFQSFAL 117
Cdd:PRK03695 16 SAEVRAGEILHLVGPNGAGKST---LLARMagLLPGSGSIQFAGQPLEAWSAAELARHRaylsqqqTPPFAMpVFQYLTL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 118 mpHMTVLDNTAFGmelaginaeerrEKALDAL-RQVGLENYAHSYPDELSGGMRQRVGLARAL-----AINPD--ILLMD 189
Cdd:PRK03695 93 --HQPDKTRTEAV------------ASALNEVaEALGLDDKLGRSVNQLSGGEWQRVRLAAVVlqvwpDINPAgqLLLLD 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16130591 190 EAFSALDPLIRTEMqDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNP 256
Cdd:PRK03695 159 EPMNSLDVAQQAAL-DRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVLTPE 224
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
43-245 |
5.64e-18 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 85.35 E-value: 5.64e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 43 GVK---DASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREvrrKKIAMVFQSFALMP 119
Cdd:PRK11288 16 GVKaldDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAALA---AGVAIIYQELHLVP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 120 HMTVLDN-------TAFGMelagINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAF 192
Cdd:PRK11288 93 EMTVAENlylgqlpHKGGI----VNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAFDEPT 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 193 SAL-----DPLIR--TEMQDElvklqakhQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQ 245
Cdd:PRK11288 169 SSLsareiEQLFRviRELRAE--------GRVILYVSHRMEEIFALCDAITVFKDGRYVA 220
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
48-196 |
6.88e-18 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 81.39 E-value: 6.88e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKisdaeLREVRRKKIAMVFQSFALMPHMTVLDNT 127
Cdd:PRK13538 21 SFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRR-----QRDEYHQDLLYLGHQPGIKTELTALENL 95
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16130591 128 AFGMELAGinaEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALD 196
Cdd:PRK13538 96 RFYQRLHG---PGDDEALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAID 161
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
45-252 |
6.97e-18 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 85.10 E-value: 6.97e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 45 KDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVrrkKIAMVFQSFALMPHMTVL 124
Cdd:PRK15439 28 KGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQL---GIYLVPQEPLLFPNLSVK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 125 DNTAFGmeLAGINAEERREKALdaLRQVGlenyAHSYPDELSGGM----RQRVGLARALAINPDILLMDEAFSALDPLIR 200
Cdd:PRK15439 105 ENILFG--LPKRQASMQKMKQL--LAALG----CQLDLDSSAGSLevadRQIVEILRGLMRDSRILILDEPTASLTPAET 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 16130591 201 TEMQDELVKLQAKHQrTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEI 252
Cdd:PRK15439 177 ERLFSRIRELLAQGV-GIVFISHKLPEIRQLADRISVMRDGTIALSGKTADL 227
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
48-196 |
7.11e-18 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 81.46 E-value: 7.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAkisDAELREVrrkkIAMVFQSFALMPHMTVLDNT 127
Cdd:PRK13539 22 SFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDID---DPDVAEA----CHYLGHRNAMKPALTVAENL 94
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16130591 128 AFGMELAGinaeERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALD 196
Cdd:PRK13539 95 EFWAAFLG----GEELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALD 159
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
83-254 |
7.18e-18 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 85.85 E-value: 7.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 83 GQVLIDGVDIAkisDAELREVRrKKIAMVFQSFALMpHMTVLDNTAFGMELAginaeeRREKALDALRQVGLENYAHSYP 162
Cdd:PTZ00265 1277 GKILLDGVDIC---DYNLKDLR-NLFSIVSQEPMLF-NMSIYENIKFGKEDA------TREDVKRACKFAAIDEFIESLP 1345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 163 DE-----------LSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRi 231
Cdd:PTZ00265 1346 NKydtnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASIKR- 1424
|
170 180
....*....|....*....|....*...
gi 16130591 232 GDRIAIMQN----GEVVQV-GTPDEILN 254
Cdd:PTZ00265 1425 SDKIVVFNNpdrtGSFVQAhGTHEELLS 1452
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
45-259 |
1.45e-17 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 85.08 E-value: 1.45e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 45 KDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDgvDIAKISDAELREvRRKKIAMVFQSFALMPHmTVL 124
Cdd:PTZ00265 402 KDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIIN--DSHNLKDINLKW-WRSKIGVVSQDPLLFSN-SIK 477
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 125 DNTAFGM-------------ELAGINAEERREK--------------------------------------ALDALRQVG 153
Cdd:PTZ00265 478 NNIKYSLyslkdlealsnyyNEDGNDSQENKNKrnscrakcagdlndmsnttdsneliemrknyqtikdseVVDVSKKVL 557
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 154 LENYAHSYPDE-----------LSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFIS 222
Cdd:PTZ00265 558 IHDFVSALPDKyetlvgsnaskLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIA 637
|
250 260 270
....*....|....*....|....*....|....*..
gi 16130591 223 HDLdEAMRIGDRIAIMQNGEVVQVGTPDEILNNPAND 259
Cdd:PTZ00265 638 HRL-STIRYANTIFVLSNRERGSTVDVDIIGEDPTKD 673
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
45-253 |
1.64e-17 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 84.38 E-value: 1.64e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 45 KDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELrevrRKKIAMVFQSFALMPHmTVL 124
Cdd:PRK10790 358 QNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVL----RQGVAMVQQDPVVLAD-TFL 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 125 DNTAFGMELAginaeerREKALDALRQVGLENYAHSYPD-----------ELSGGMRQRVGLARALAINPDILLMDEAFS 193
Cdd:PRK10790 433 ANVTLGRDIS-------EEQVWQALETVQLAELARSLPDglytplgeqgnNLSVGQKQLLALARVLVQTPQILILDEATA 505
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16130591 194 ALDPLIRTEMQDELVKLqaKHQRTIVFISHDLD---EAmrigDRIAIMQNGEVVQVGTPDEIL 253
Cdd:PRK10790 506 NIDSGTEQAIQQALAAV--REHTTLVVIAHRLStivEA----DTILVLHRGQAVEQGTHQQLL 562
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
44-253 |
2.20e-17 |
|
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: 79.88 E-value: 2.20e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 44 VKDASLAIEEGEIFVIMGLSGSGKSTmvrLLNRLI-----EPTRGQVLIDGVDIAkisDAELREVRRKKIAMVFQSfalm 118
Cdd:cd03217 16 LKGVNLTIKKGEVHALMGPNGSGKST---LAKTIMghpkyEVTEGEILFKGEDIT---DLPPEERARLGIFLAFQY---- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 119 PhmtvldntafgMELAGInaeerreKALDALRQVGlenyahsypDELSGGMRQRVGLARALAINPDILLMDEAFSALDpL 198
Cdd:cd03217 86 P-----------PEIPGV-------KNADFLRYVN---------EGFSGGEKKRNEILQLLLLEPDLAILDEPDSGLD-I 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 199 IRTEMQDELVKLQAKHQRTIVFISH-----DLDEAmrigDRIAIMQNGEVVQVGTPDEIL 253
Cdd:cd03217 138 DALRLVAEVINKLREEGKSVLIITHyqrllDYIKP----DRVHVLYDGRIVKSGDKELAL 193
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
1-253 |
2.81e-17 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 81.02 E-value: 2.81e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 1 MAIKLEIKNL---YKIFGEHPQRAfkyieqglsKEQIL--EKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLN 75
Cdd:PRK13546 1 MNVSVNIKNVtkeYRIYRTNKERM---------KDALIpkHKNKTFFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 76 RLIEPTRGQVLIDGvdiakisdaelrevrrkKIAMVFQSFALMPHMTVLDNTAFGMELAGINAEERREKALDALRQVGLE 155
Cdd:PRK13546 72 GSLSPTVGKVDRNG-----------------EVSVIAISAGLSGQLTGIENIEFKMLCMGFKRKEIKAMTPKIIEFSELG 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 156 NYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDpliRTEMQDELVKLQ--AKHQRTIVFISHDLDEAMRIGD 233
Cdd:PRK13546 135 EFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGD---QTFAQKCLDKIYefKEQNKTIFFVSHNLGQVRQFCT 211
|
250 260
....*....|....*....|
gi 16130591 234 RIAIMQNGEVVQVGTPDEIL 253
Cdd:PRK13546 212 KIAWIEGGKLKDYGELDDVL 231
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
44-223 |
2.98e-17 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 83.32 E-value: 2.98e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLI-DGVDIA------KISDAELREVrrkkiamvfqsfA 116
Cdd:COG4178 379 LEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARpAGARVLflpqrpYLPLGTLREA------------L 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 117 LMPHmtvlDNTAFGmelaginaeerREKALDALRQVGLENYAHSYPDE------LSGGMRQRVGLARALAINPDILLMDE 190
Cdd:COG4178 447 LYPA----TAEAFS-----------DAELREALEAVGLGHLAERLDEEadwdqvLSLGEQQRLAFARLLLHKPDWLFLDE 511
|
170 180 190
....*....|....*....|....*....|....*
gi 16130591 191 AFSALDPlirtEMQDELVKL--QAKHQRTIVFISH 223
Cdd:COG4178 512 ATSALDE----ENEAALYQLlrEELPGTTVISVGH 542
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
45-250 |
7.66e-17 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 79.34 E-value: 7.66e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 45 KDASLAIEEGEIFVIMGLSGSGKSTMVRLL--NRLIEPTRGQVLIDGVDiakISDAELREVRRKKIAMVFQSFALMPHMT 122
Cdd:COG0396 17 KGVNLTIKPGEVHAIMGPNGSGKSTLAKVLmgHPKYEVTSGSILLDGED---ILELSPDERARAGIFLAFQYPVEIPGVS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 123 VLD--NTAFG-MELAGINAEERREKALDALRQVGL-ENYAHSYPDE-LSGGMRQRVGLARALAINPDILLMDEAFSALD- 196
Cdd:COG0396 94 VSNflRTALNaRRGEELSAREFLKLLKEKMKELGLdEDFLDRYVNEgFSGGEKKRNEILQMLLLEPKLAILDETDSGLDi 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16130591 197 ----PLIRT--EMQDElvklqakhQRTIVFISH-----DLDEAmrigDRIAIMQNGEVVQVGTPD 250
Cdd:COG0396 174 dalrIVAEGvnKLRSP--------DRGILIITHyqrilDYIKP----DFVHVLVDGRIVKSGGKE 226
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
41-263 |
1.40e-16 |
|
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: 81.98 E-value: 1.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 41 SLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDI-AKISDaelrevrrkkiamVFQSFALMP 119
Cdd:TIGR01257 1952 SPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSIlTNISD-------------VHQNMGYCP 2018
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 120 HMTVLDNTAFGME-------LAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAF 192
Cdd:TIGR01257 2019 QFDAIDDLLTGREhlylyarLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPT 2098
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16130591 193 SALDPLIRTEMQDELVKLqAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRT 263
Cdd:TIGR01257 2099 TGMDPQARRMLWNTIVSI-IREGRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGTIQHLKSKFGDGYIVT 2168
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
47-244 |
1.73e-16 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 81.11 E-value: 1.73e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 47 ASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDG--VDIAKISDAelreVR---------RKKIAMVfqsf 115
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGkpIDIRSPRDA----IRagimlcpedRKAEGII---- 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 116 almPHMTVLDNTA---------FGMELaginaEERREKALdALRQVGLENYAHSYPDE----LSGGMRQRVGLARALAIN 182
Cdd:PRK11288 344 ---PVHSVADNINisarrhhlrAGCLI-----NNRWEAEN-ADRFIRSLNIKTPSREQlimnLSGGNQQKAILGRWLSED 414
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16130591 183 PDILLMDEAFSALDPLIRTEMQDELVKLqAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVV 244
Cdd:PRK11288 415 MKVILLDEPTRGIDVGAKHEIYNVIYEL-AAQGVAVLFVSSDLPEVLGVADRIVVMREGRIA 475
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
48-196 |
1.97e-16 |
|
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: 77.15 E-value: 1.97e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVdiakiSDAELREVRRKKIAMVFQSFALMPHMTVLDNT 127
Cdd:cd03231 20 SFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGG-----PLDFQRDSIARGLLYLGHAPGIKTTLSVLENL 94
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16130591 128 AFgmeLAGINAEERREKALDalrQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALD 196
Cdd:cd03231 95 RF---WHADHSDEQVEEALA---RVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALD 157
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
51-263 |
1.02e-15 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 76.49 E-value: 1.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 51 IEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREvrrkKIAMVFQS---------FALMPHM 121
Cdd:cd03288 44 IKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRS----RLSIILQDpilfsgsirFNLDPEC 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 122 TVLDNTAF-GMELAGI-NAEERREKALDALRQVGLENYahsypdelSGGMRQRVGLARALAINPDILLMDEAFSALDplI 199
Cdd:cd03288 120 KCTDDRLWeALEIAQLkNMVKSLPGGLDAVVTEGGENF--------SVGQRQLFCLARAFVRKSSILIMDEATASID--M 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16130591 200 RTEMQDELVKLQAKHQRTIVFISHDLDEAMRiGDRIAIMQNGEVVQVGTPDEIL---NNPANDYVRT 263
Cdd:cd03288 190 ATENILQKVVMTAFADRTVVTIAHRVSTILD-ADLVLVLSRGILVECDTPENLLaqeDGVFASLVRT 255
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
44-258 |
3.73e-15 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 74.92 E-value: 3.73e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKisdaelrEVRRKKIAMVFQS------FAL 117
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQ-------ALQKNLVAYVPQSeevdwsFPV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 118 MPHMTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDP 197
Cdd:PRK15056 96 LVEDVVMMGRYGHMGWLRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDV 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16130591 198 LIRTEMQDELVKLQAKhQRTIVFISHDLDEAMRIGDrIAIMQNGEVVQVGtPDEILNNPAN 258
Cdd:PRK15056 176 KTEARIISLLRELRDE-GKTMLVSTHNLGSVTEFCD-YTVMVKGTVLASG-PTETTFTAEN 233
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
32-246 |
3.76e-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: 3.76e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 32 EQILEKTGLSLGV------KDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDgvdiakisdaelrevrr 105
Cdd:COG2401 28 AIVLEAFGVELRVveryvlRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVD----------------- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 106 kkiamvfqsfalmphmtVLDNTaFGMELAGINAEERREKALDA---LRQVGLeNYAHSY---PDELSGGMRQRVGLARAL 179
Cdd:COG2401 91 -----------------VPDNQ-FGREASLIDAIGRKGDFKDAvelLNAVGL-SDAVLWlrrFKELSTGQKFRFRLALLL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16130591 180 AINPDILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISH--DLDEAMrIGDRIAIMQNGEVVQV 246
Cdd:COG2401 152 AERPKLLVIDEFCSHLDRQTAKRVARNLQKLARRAGITLVVATHhyDVIDDL-QPDLLIFVGYGGVPEE 219
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
44-252 |
3.82e-15 |
|
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: 75.28 E-value: 3.82e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGvdiakisdaelrevrrkKIAMVFQSFALMPHmTV 123
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG-----------------RISFSSQFSWIMPG-TI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 124 LDNTAFGmelagINAEERREKALdaLRQVGLENYAHSYPDE-----------LSGGMRQRVGLARALAINPDILLMDEAF 192
Cdd:cd03291 115 KENIIFG-----VSYDEYRYKSV--VKACQLEEDITKFPEKdntvlgeggitLSGGQRARISLARAVYKDADLYLLDSPF 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16130591 193 SALDPLIRTEMQDELV-KLQAKHQRTIVfisHDLDEAMRIGDRIAIMQNGEVVQVGTPDEI 252
Cdd:cd03291 188 GYLDVFTEKEIFESCVcKLMANKTRILV---TSKMEHLKKADKILILHEGSSYFYGTFSEL 245
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
43-245 |
5.17e-15 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 76.37 E-value: 5.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 43 GVK---DASLAIEEGEIFVIMGLSGSGKSTMVRLLNRlIEPT---RGQVLIDG--VDIAKISDAElrevrRKKIAMVFQS 114
Cdd:NF040905 13 GVKaldDVNLSVREGEIHALCGENGAGKSTLMKVLSG-VYPHgsyEGEILFDGevCRFKDIRDSE-----ALGIVIIHQE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 115 FALMPHMTVLDNTAFGMELAG---INAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEA 191
Cdd:NF040905 87 LALIPYLSIAENIFLGNERAKrgvIDWNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLILDEP 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 16130591 192 FSALDPLIRTEMQDELVKLQAkHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQ 245
Cdd:NF040905 167 TAALNEEDSAALLDLLLELKA-QGITSIIISHKLNEIRRVADSITVLRDGRTIE 219
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
48-250 |
6.63e-15 |
|
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: 76.38 E-value: 6.63e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIakisDAELREVRRKKIAMVFQSFALMPHmtvldnt 127
Cdd:COG4615 352 DLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPV----TADNREAYRQLFSAVFSDFHLFDR------- 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 128 afgmeLAGINAEERREKALDALRQ------VGLENYAHSYPDeLSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRT 201
Cdd:COG4615 421 -----LLGLDGEADPARARELLERleldhkVSVEDGRFSTTD-LSQGQRKRLALLVALLEDRPILVFDEWAADQDPEFRR 494
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 16130591 202 EMQDELV-KLQAKhQRTIVFISHDlDEAMRIGDRIAIMQNGEVVQVGTPD 250
Cdd:COG4615 495 VFYTELLpELKAR-GKTVIAISHD-DRYFDLADRVLKMDYGKLVELTGPA 542
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
48-255 |
6.84e-15 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 76.08 E-value: 6.84e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGvdiakisdaelrevrrkKIAMVFQSFALMPHMTVLDNT 127
Cdd:PRK13545 44 SFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKG-----------------SAALIAISSGLNGQLTGIENI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 128 AFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDEL 207
Cdd:PRK13545 107 ELKGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKCLDKM 186
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 16130591 208 VKLQAKhQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNN 255
Cdd:PRK13545 187 NEFKEQ-GKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEVVDH 233
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
44-253 |
1.27e-14 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 73.32 E-value: 1.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLL-NRLIEPT-------RGQVLIDGVDIAKIsDAELREVRRKKIAMVFQ-S 114
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALaGDLTGGGaprgarvTGDVTLNGEPLAAI-DAPRLARLRAVLPQAAQpA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 115 FALMPHMTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALA---------INPDI 185
Cdd:PRK13547 96 FAFSAREIVLLGRYPHARRAGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLAqlwpphdaaQPPRY 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16130591 186 LLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEIL 253
Cdd:PRK13547 176 LLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPADVL 243
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
7-253 |
2.44e-14 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 74.33 E-value: 2.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 7 IKNLYKIFGEHPQRAFKYIEQGLSKE-----QILEKTGLSLG------VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLN 75
Cdd:COG0488 283 IKALEKLEREEPPRRDKTVEIRFPPPerlgkKVLELEGLSKSygdktlLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLA 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 76 RLIEPTRGQVLIdGVDIakisdaelrevrrkKIAMVFQSFA-LMPHMTVLDntafgmELAGINAEERREKALDALRQVGL 154
Cdd:COG0488 363 GELEPDSGTVKL-GETV--------------KIGYFDQHQEeLDPDKTVLD------ELRDGAPGGTEQEVRGYLGRFLF 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 155 -ENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPlirtEMQDELVKLQAKHQRTIVFISHD---LDeamR 230
Cdd:COG0488 422 sGDDAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDI----ETLEALEEALDDFPGTVLLVSHDryfLD---R 494
|
250 260
....*....|....*....|....
gi 16130591 231 IGDRIAIMQNGEVVQ-VGTPDEIL 253
Cdd:COG0488 495 VATRILEFEDGGVREyPGGYDDYL 518
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
39-256 |
2.76e-14 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 74.82 E-value: 2.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 39 GLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISdaeLREVRRKkiamvfqsFALM 118
Cdd:PTZ00243 1321 GLPLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYG---LRELRRQ--------FSMI 1389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 119 PHMTVL-DNTA------F----------GMELAGINAEERRE-KALDALRQVGLENYahsypdelSGGMRQRVGLARA-L 179
Cdd:PTZ00243 1390 PQDPVLfDGTVrqnvdpFleassaevwaALELVGLRERVASEsEGIDSRVLEGGSNY--------SVGQRQLMCMARAlL 1461
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16130591 180 AINPDILLMDEAFSALDPLIRTEMQDELVKLQAKHqrTIVFISHDLDEAMRIgDRIAIMQNGEVVQVGTPDEILNNP 256
Cdd:PTZ00243 1462 KKGSGFILMDEATANIDPALDRQIQATVMSAFSAY--TVITIAHRLHTVAQY-DKIIVMDHGAVAEMGSPRELVMNR 1535
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
9-223 |
2.93e-14 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 74.53 E-value: 2.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 9 NLYKIFGeHPQRAFKyieqglSKEQILEKTGLSlGVKDAslaIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPT--RGQVL 86
Cdd:PLN03211 60 NIKRILG-HKPKISD------ETRQIQERTILN-GVTGM---ASPGEILAVLGPSGSGKSTLLNALAGRIQGNnfTGTIL 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 87 IDGVDIAKISdaelrevrRKKIAMVFQSFALMPHMTVLDNTAFGMELAGINAEERREKALDA---LRQVGL---EN--YA 158
Cdd:PLN03211 129 ANNRKPTKQI--------LKRTGFVTQDDILYPHLTVRETLVFCSLLRLPKSLTKQEKILVAesvISELGLtkcENtiIG 200
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16130591 159 HSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLqAKHQRTIVFISH 223
Cdd:PLN03211 201 NSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLTLGSL-AQKGKTIVTSMH 264
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
43-243 |
4.08e-14 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 73.55 E-value: 4.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAElrevrRKKIAMVF-----QSFAL 117
Cdd:PRK15439 278 GFRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQ-----RLARGLVYlpedrQSSGL 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 118 MPHMTVLDNT-AFGMELAGINAEERREKALdalrqvgLENYAH------SYPDE----LSGGMRQRVGLARALAINPDIL 186
Cdd:PRK15439 353 YLDAPLAWNVcALTHNRRGFWIKPARENAV-------LERYRRalnikfNHAEQaartLSGGNQQKVLIAKCLEASPQLL 425
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 16130591 187 LMDEAFSALDPLIRTEMQDeLVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEV 243
Cdd:PRK15439 426 IVDEPTRGVDVSARNDIYQ-LIRSIAAQNVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
39-235 |
5.06e-14 |
|
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: 71.29 E-value: 5.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 39 GLSLGVKDASlaIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIA----KIS---DAELREVRRKKIAMV 111
Cdd:cd03237 12 EFTLEVEGGS--ISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSykpqYIKadyEGTVRDLLSSITKDF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 112 -----FQSFALMPHMTvldntafgmelaginaeerrEKALDalRQVglenyahsypDELSGGMRQRVGLARALAINPDIL 186
Cdd:cd03237 90 ythpyFKTEIAKPLQI--------------------EQILD--REV----------PELSGGELQRVAIAACLSKDADIY 137
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 16130591 187 LMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRI 235
Cdd:cd03237 138 LLDEPSAYLDVEQRLMASKVIRRFAENNEKTAFVVEHDIIMIDYLADRL 186
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
44-241 |
5.51e-14 |
|
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: 70.44 E-value: 5.51e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVRRKKIAMVFQSFALMpHMTV 123
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRNRYSVAYAAQKPWLL-NATV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 124 LDNTAFGMELAginaEERREKALDALR-QVGLENYAHSYPDE-------LSGGMRQRVGLARALAINPDILLMDEAFSAL 195
Cdd:cd03290 96 EENITFGSPFN----KQRYKAVTDACSlQPDIDLLPFGDQTEigerginLSGGQRQRICVARALYQNTNIVFLDDPFSAL 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 16130591 196 DPLIRTE-MQDELVKLQAKHQRTIVFISHDLdEAMRIGDRIAIMQNG 241
Cdd:cd03290 172 DIHLSDHlMQEGILKFLQDDKRTLVLVTHKL-QYLPHADWIIAMKDG 217
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
44-254 |
6.59e-14 |
|
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: 73.79 E-value: 6.59e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGvdiakisdaelrevrrkKIAMVFQSFALMPHmTV 123
Cdd:TIGR01271 442 LKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG-----------------RISFSPQTSWIMPG-TI 503
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 124 LDNTAFGmelagINAEERREKALdaLRQVGLENYAHSYPDE-----------LSGGMRQRVGLARALAINPDILLMDEAF 192
Cdd:TIGR01271 504 KDNIIFG-----LSYDEYRYTSV--IKACQLEEDIALFPEKdktvlgeggitLSGGQRARISLARAVYKDADLYLLDSPF 576
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16130591 193 SALDPLIRTEMQDE-LVKLQAKHQRTIVfiSHDLdEAMRIGDRIAIMQNGEVVQVGTPDEILN 254
Cdd:TIGR01271 577 THLDVVTEKEIFEScLCKLMSNKTRILV--TSKL-EHLKKADKILLLHEGVCYFYGTFSELQA 636
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
35-256 |
1.73e-13 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 69.76 E-value: 1.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 35 LEKTGLSLG----VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVlidgvdiakISDAELRevrrkkIAM 110
Cdd:PRK09544 7 LENVSVSFGqrrvLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI---------KRNGKLR------IGY 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 111 VFQSFALMPHMTvLDNTAFGMELAGInaeeRREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDE 190
Cdd:PRK09544 72 VPQKLYLDTTLP-LTVNRFLRLRPGT----KKEDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDE 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16130591 191 AFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMqNGEVVQVGTPDEILNNP 256
Cdd:PRK09544 147 PTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCL-NHHICCSGTPEVVSLHP 211
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
45-242 |
2.05e-13 |
|
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: 67.09 E-value: 2.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 45 KDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQV-LIDGVDIAkisdaelrevrrkkiamvfqsfalmphmtv 123
Cdd:cd03221 17 KDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVtWGSTVKIG------------------------------ 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 124 ldntafgmelaginaeerrekaldalrqvglenyahsYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEM 203
Cdd:cd03221 67 -------------------------------------YFEQLSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEAL 109
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 16130591 204 QDELVklqaKHQRTIVFISHD---LDeamRIGDRIAIMQNGE 242
Cdd:cd03221 110 EEALK----EYPGTVILVSHDryfLD---QVATKIIELEDGK 144
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
51-197 |
2.16e-13 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 68.72 E-value: 2.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 51 IEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGvdiAKISDAElrevRRKKIAMVFQSFALMPHMTVLDNTAFg 130
Cdd:PRK13543 34 VDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDG---KTATRGD----RSRFMAYLGHLPGLKADLSTLENLHF- 105
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16130591 131 meLAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARaLAINPDIL-LMDEAFSALDP 197
Cdd:PRK13543 106 --LCGLHGRRAKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALAR-LWLSPAPLwLLDEPYANLDL 170
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
44-243 |
3.18e-13 |
|
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: 71.01 E-value: 3.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPT-RGQVLIDG--VDIAKISDAelrevRRKKIAMVFQS---FAL 117
Cdd:TIGR02633 276 VDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGkpVDIRNPAQA-----IRAGIAMVPEDrkrHGI 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 118 MPHMTVLDNTAFGM-----ELAGINAEERREKALDALRQVGLENYAHSYP-DELSGGMRQRVGLARALAINPDILLMDEA 191
Cdd:TIGR02633 351 VPILGVGKNITLSVlksfcFKMRIDAAAELQIIGSAIQRLKVKTASPFLPiGRLSGGNQQKAVLAKMLLTNPRVLILDEP 430
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 16130591 192 FSALDPLIRTEMQdELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEV 243
Cdd:TIGR02633 431 TRGVDVGAKYEIY-KLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGKL 481
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
44-223 |
5.57e-13 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 66.41 E-value: 5.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDgvdiakisdaelrevRRKKIAMVFQSfalmPHMTV 123
Cdd:cd03223 17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMP---------------EGEDLLFLPQR----PYLPL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 124 LdntafgmelaginaeerrekaldALRQVGLenyahsYP--DELSGGMRQRVGLARALAINPDILLMDEAFSALDPlirt 201
Cdd:cd03223 78 G-----------------------TLREQLI------YPwdDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDE---- 124
|
170 180
....*....|....*....|..
gi 16130591 202 EMQDELVKLQAKHQRTIVFISH 223
Cdd:cd03223 125 ESEDRLYQLLKELGITVISVGH 146
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
44-246 |
6.29e-13 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 70.20 E-value: 6.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 44 VKDASLAIEEGEIFVIMGLSGSGKStmvRLLNRL--IEPTR-GQVLIDGVDIAKISD--------AELREVRRKKiaMVF 112
Cdd:PRK09700 279 VRDISFSVCRGEILGFAGLVGSGRT---ELMNCLfgVDKRAgGEIRLNGKDISPRSPldavkkgmAYITESRRDN--GFF 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 113 QSFALMPHMTV---LDNTAFGMELAGINAEERREKALDALRQVGLEnyAHSYPD---ELSGGMRQRVGLARALAINPDIL 186
Cdd:PRK09700 354 PNFSIAQNMAIsrsLKDGGYKGAMGLFHEVDEQRTAENQRELLALK--CHSVNQnitELSGGNQQKVLISKWLCCCPEVI 431
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 187 LMDEAFSALDPLIRTEMQDELVKLqAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQV 246
Cdd:PRK09700 432 IFDEPTRGIDVGAKAEIYKVMRQL-ADDGKVILMVSSELPEIITVCDRIAVFCEGRLTQI 490
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
43-242 |
1.05e-12 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 69.26 E-value: 1.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 43 GVK---DASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGvdiAKISDAELREVRRKKIAMVFQSFALMP 119
Cdd:PRK10762 16 GVKalsGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLG---KEVTFNGPKSSQEAGIGIIHQELNLIP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 120 HMTVLDNTAFGME----LAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEafsAL 195
Cdd:PRK10762 93 QLTIAENIFLGREfvnrFGRIDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDE---PT 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 16130591 196 DPLIRTEMQdELVK----LQAKHqRTIVFISHDLDEAMRIGDRIAIMQNGE 242
Cdd:PRK10762 170 DALTDTETE-SLFRvireLKSQG-RGIVYISHRLKEIFEICDDVTVFRDGQ 218
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
44-309 |
1.19e-12 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 67.57 E-value: 1.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEpTRGQVLIDGVDIAKISDAELRevrrkkiamvfQSFALMPHMTV 123
Cdd:cd03289 20 LENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQKWR-----------KAFGVIPQKVF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 124 LDNTAFGMELAGiNAEERREKALDALRQVGLENYAHSYPDEL-----------SGGMRQRVGLARALAINPDILLMDEAF 192
Cdd:cd03289 88 IFSGTFRKNLDP-YGKWSDEEIWKVAEEVGLKSVIEQFPGQLdfvlvdggcvlSHGHKQLMCLARSVLSKAKILLLDEPS 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 193 SALDPLIRTEMQDELVklQAKHQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEILNNpandyvRTFFRGVdISQ 272
Cdd:cd03289 167 AHLDPITYQVIRKTLK--QAFADCTVILSEHRI-EAMLECQRFLVIEENKVRQYDSIQKLLNE------KSHFKQA-ISP 236
|
250 260 270
....*....|....*....|....*....|....*..
gi 16130591 273 VFSAKDIARRTPNGLIRKtpgfgPRSALKLLQDEDRE 309
Cdd:cd03289 237 SDRLKLFPRRNSSKSKRK-----PRPQIQALQEETEE 268
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
44-247 |
2.63e-12 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 68.65 E-value: 2.63e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLidgvdiakisdAElrevrrKKIAMVFQSFALMpHMTV 123
Cdd:PTZ00243 676 LRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVW-----------AE------RSIAYVPQQAWIM-NATV 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 124 LDNTAFgmelagiNAEERREKALDALR--QV---------GLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAF 192
Cdd:PTZ00243 738 RGNILF-------FDEEDAARLADAVRvsQLeadlaqlggGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPL 810
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 16130591 193 SALDPLIRTEMQDELVkLQAKHQRTIVFISHDLDEAMRiGDRIAIMQNGEVVQVG 247
Cdd:PTZ00243 811 SALDAHVGERVVEECF-LGALAGKTRVLATHQVHVVPR-ADYVVALGDGRVEFSG 863
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
46-253 |
3.26e-12 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 68.23 E-value: 3.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 46 DASLAIEEGEIFVIMGLSGSGKSTMVRLLN--RLIEptRGQVLIDGVDIAkisDAELREVRRKKIAMVFQSFA--LMPHM 121
Cdd:NF033858 19 DVSLDIPAGCMVGLIGPDGVGKSSLLSLIAgaRKIQ--QGRVEVLGGDMA---DARHRRAVCPRIAYMPQGLGknLYPTL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 122 TVLDNTAFGMELAGINAEERREKALDALRQVGLenyaHSYPD----ELSGGMRQRVGLARALAINPDILLMDEAFSALDP 197
Cdd:NF033858 94 SVFENLDFFGRLFGQDAAERRRRIDELLRATGL----APFADrpagKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDP 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 16130591 198 LIRTEMQDELVKLQAKHQRTIVFIS-HDLDEAMRIgDRIAIMQNGEVVQVGTPDEIL 253
Cdd:NF033858 170 LSRRQFWELIDRIRAERPGMSVLVAtAYMEEAERF-DWLVAMDAGRVLATGTPAELL 225
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
45-250 |
3.63e-12 |
|
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six proteins and believed to act in Fe-S cluster formation during oxidative stress. SufC forms a complex with SufB and SufD. SufC belongs to the ATP-binding cassette transporter family (pfam00005) but is no longer thought to be part of a transporter. The complex is reported as cytosolic () or associated with the membrane (). The SUF system also includes a cysteine desulfurase (SufS, enhanced by SufE) and a probable iron-sulfur cluster assembly scaffold protein, SufA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 273907 [Multi-domain] Cd Length: 243 Bit Score: 65.74 E-value: 3.63e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 45 KDASLAIEEGEIFVIMGLSGSGKSTMVRLL--NRLIEPTRGQVLIDGVDIAKIsdaELREVRRKKIAMVFQSFALMPHMT 122
Cdd:TIGR01978 17 KGVNLTVKKGEIHAIMGPNGSGKSTLSKTIagHPSYEVTSGTILFKGQDLLEL---EPDERARAGLFLAFQYPEEIPGVS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 123 VLD--NTAfgmelagINA--EERREKALDALRQVGL-----------ENYAHSYPDE-LSGGMRQRVGLARALAINPDIL 186
Cdd:TIGR01978 94 NLEflRSA-------LNArrSARGEEPLDLLDFEKLlkeklalldmdEEFLNRSVNEgFSGGEKKRNEILQMALLEPKLA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16130591 187 LMDEAFSALDPLIRTEMQDELVKLQAKHqRTIVFISHDLdeamRIGDRIA-----IMQNGEVVQVGTPD 250
Cdd:TIGR01978 167 ILDEIDSGLDIDALKIVAEGINRLREPD-RSFLIITHYQ----RLLNYIKpdyvhVLLDGRIVKSGDVE 230
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
48-264 |
6.38e-12 |
|
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: 67.66 E-value: 6.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGV-----DIAKISDAELRE-------VRRKKIAMVFQSF 115
Cdd:TIGR00957 658 TFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSvayvpQQAWIQNDSLREnilfgkaLNEKYYQQVLEAC 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 116 ALMPHMTVL---DNTAFGMElaGINaeerrekaldalrqvglenyahsypdeLSGGMRQRVGLARALAINPDILLMDEAF 192
Cdd:TIGR00957 738 ALLPDLEILpsgDRTEIGEK--GVN---------------------------LSGGQKQRVSLARAVYSNADIYLFDDPL 788
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16130591 193 SALDPLIRTEMQDELVKLQAK-HQRTIVFISHDLDEAMRIgDRIAIMQNGEVVQVGTPDEIL--NNPANDYVRTF 264
Cdd:TIGR00957 789 SAVDAHVGKHIFEHVIGPEGVlKNKTRILVTHGISYLPQV-DVIIVMSGGKISEMGSYQELLqrDGAFAEFLRTY 862
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
43-244 |
1.32e-11 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 65.91 E-value: 1.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 43 GVK---DASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREvrrKKIAMVFQSFALMP 119
Cdd:PRK10982 10 GVKaldNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEALE---NGISMVHQELNLVL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 120 HMTVLDNTAFG-MELAGINAEE----RREKALdaLRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSA 194
Cdd:PRK10982 87 QRSVMDNMWLGrYPTKGMFVDQdkmyRDTKAI--FDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSS 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 16130591 195 LdplirTEMQ-DELVKLQAKHQRT---IVFISHDLDEAMRIGDRIAIMQNGEVV 244
Cdd:PRK10982 165 L-----TEKEvNHLFTIIRKLKERgcgIVYISHKMEEIFQLCDEITILRDGQWI 213
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
61-224 |
2.90e-11 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 64.91 E-value: 2.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 61 GLSGSGKSTMVRLLNRLIEPTRGQVLID-GVDIAKIS------------------DAELREVRRKKIAMvfqsFALmPHM 121
Cdd:PRK15064 34 GANGCGKSTFMKILGGDLEPSAGNVSLDpNERLGKLRqdqfafeeftvldtvimgHTELWEVKQERDRI----YAL-PEM 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 122 TVLD-------NTAFGmELAGINAEERrekALDALRQVGLENYAHSYP-DELSGGMRQRVGLARALAINPDILLMDEAFS 193
Cdd:PRK15064 109 SEEDgmkvadlEVKFA-EMDGYTAEAR---AGELLLGVGIPEEQHYGLmSEVAPGWKLRVLLAQALFSNPDILLLDEPTN 184
|
170 180 190
....*....|....*....|....*....|...
gi 16130591 194 ALDplIRT--EMQDELVKLQAkhqrTIVFISHD 224
Cdd:PRK15064 185 NLD--INTirWLEDVLNERNS----TMIIISHD 211
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
44-243 |
3.99e-11 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 64.57 E-value: 3.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRlIEPTR--GQVLIDG--VDIAKISDAelrevRRKKIAMVFQS---FA 116
Cdd:PRK13549 278 VDDVSFSLRRGEILGIAGLVGAGRTELVQCLFG-AYPGRweGEIFIDGkpVKIRNPQQA-----IAQGIAMVPEDrkrDG 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 117 LMPHMTV--------LDNTAFGM------ELAGINAEERREKALDALRQVGLENyahsypdeLSGGMRQRVGLARALAIN 182
Cdd:PRK13549 352 IVPVMGVgknitlaaLDRFTGGSriddaaELKTILESIQRLKVKTASPELAIAR--------LSGGNQQKAVLAKCLLLN 423
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16130591 183 PDILLMDEAFSALDPLIRTEMQDELVKLqAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEV 243
Cdd:PRK13549 424 PKILILDEPTRGIDVGAKYEIYKLINQL-VQQGVAIIVISSELPEVLGLSDRVLVMHEGKL 483
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
36-313 |
7.37e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 64.37 E-value: 7.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 36 EKTGLSlgvkDASLAIEEGEIFVIMGLSGSGKSTmvrllnrLIEPTRGQvlidgvdIAKISDAELreVRRKKIAMVFQsF 115
Cdd:PLN03130 629 ERPTLS----NINLDVPVGSLVAIVGSTGEGKTS-------LISAMLGE-------LPPRSDASV--VIRGTVAYVPQ-V 687
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 116 ALMPHMTVLDNTAFGMELAginaEERREKALDAlrqVGLENYAHSYPD-----------ELSGGMRQRVGLARALAINPD 184
Cdd:PLN03130 688 SWIFNATVRDNILFGSPFD----PERYERAIDV---TALQHDLDLLPGgdlteigergvNISGGQKQRVSMARAVYSNSD 760
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 185 ILLMDEAFSALDPLIRTEMQDELVKLQAKHqRTIVFISHDLDEAMRIgDRIAIMQNGEVVQVGTPDEILNN--------- 255
Cdd:PLN03130 761 VYIFDDPLSALDAHVGRQVFDKCIKDELRG-KTRVLVTNQLHFLSQV-DRIILVHEGMIKEEGTYEELSNNgplfqklme 838
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16130591 256 ---PANDYVRTFFRGVDISQvfSAKDIARRTPNGLIRKTPGFGPRSALK--LLQDEDREYGYV 313
Cdd:PLN03130 839 nagKMEEYVEENGEEEDDQT--SSKPVANGNANNLKKDSSSKKKSKEGKsvLIKQEERETGVV 899
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
44-309 |
1.21e-10 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 63.39 E-value: 1.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEpTRGQVLIDGVDIAKISDAELRevrrkkiamvfQSFALMPHMTV 123
Cdd:TIGR01271 1235 LQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVSWNSVTLQTWR-----------KAFGVIPQKVF 1302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 124 LDNTAFGMELAGiNAEERREKALDALRQVGLENYAHSYPDEL-----------SGGMRQRVGLARALAINPDILLMDEAF 192
Cdd:TIGR01271 1303 IFSGTFRKNLDP-YEQWSDEEIWKVAEEVGLKSVIEQFPDKLdfvlvdggyvlSNGHKQLMCLARSILSKAKILLLDEPS 1381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 193 SALDP----LIRTEMQdelvklQAKHQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEILNNpandyvRTFFRgv 268
Cdd:TIGR01271 1382 AHLDPvtlqIIRKTLK------QSFSNCTVILSEHRV-EALLECQQFLVIEGSSVKQYDSIQKLLNE------TSLFK-- 1446
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 16130591 269 disQVFSAKDIARRTPNGLiRKTPGFGPRSALKLLQDEDRE 309
Cdd:TIGR01271 1447 ---QAMSAADRLKLFPLHR-RNSSKRKPQPKITALREEAEE 1483
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
136-252 |
2.08e-10 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 61.67 E-value: 2.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 136 INAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDElVKLQAKHQ 215
Cdd:NF000106 116 LSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDE-VRSMVRDG 194
|
90 100 110
....*....|....*....|....*....|....*..
gi 16130591 216 RTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEI 252
Cdd:NF000106 195 ATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDEL 231
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
54-237 |
2.64e-10 |
|
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: 58.54 E-value: 2.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 54 GEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIdgvdiakisdaelrevrrkkiamvfqsfalmphmtvldntafgmel 133
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIY---------------------------------------------- 35
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 134 agINAEERREKALDALRQVGLENYAHSypdeLSGGMRQRVGLARALAINPDILLMDEAFSALDP-----LIRTEMQDELV 208
Cdd:smart00382 36 --IDGEDILEEVLDQLLLIIVGGKKAS----GSGELRLRLALALARKLKPDVLILDEITSLLDAeqealLLLLEELRLLL 109
|
170 180
....*....|....*....|....*....
gi 16130591 209 KLQAKHQRTIVFISHDLDEAMRIGDRIAI 237
Cdd:smart00382 110 LLKSEKNLTVILTTNDEKDLGPALLRRRF 138
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
24-244 |
3.87e-10 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 59.20 E-value: 3.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 24 YIEQGLSKEQILektglslgvKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPT---RGQVLIDGVDIAKIsdael 100
Cdd:cd03233 12 TTGKGRSKIPIL---------KDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKEF----- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 101 REVRRKKIAMVFQSFALMPHMTVLDNTAFGMELAGinaeerrekaldalrqvglenyaHSYPDELSGGMRQRVGLARALA 180
Cdd:cd03233 78 AEKYPGEIIYVSEEDVHFPTLTVRETLDFALRCKG-----------------------NEFVRGISGGERKRVSIAEALV 134
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16130591 181 INPDILLMDEAFSALDPLIRTEMQDELvKLQAKHQRTIVFIS--HDLDEAMRIGDRIAIMQNGEVV 244
Cdd:cd03233 135 SRASVLCWDNSTRGLDSSTALEILKCI-RTMADVLKTTTFVSlyQASDEIYDLFDKVLVLYEGRQI 199
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
46-244 |
3.94e-10 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 61.50 E-value: 3.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 46 DASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDG-VDIAKISDAELREVRR----------KKIAMVFQS 114
Cdd:PRK11147 21 NAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQdLIVARLQQDPPRNVEGtvydfvaegiEEQAEYLKR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 115 FALMPHMTVLDNTAFGM-ELAGINAE---------ERREKalDALRQVGLEnyAHSYPDELSGGMRQRVGLARALAINPD 184
Cdd:PRK11147 101 YHDISHLVETDPSEKNLnELAKLQEQldhhnlwqlENRIN--EVLAQLGLD--PDAALSSLSGGWLRKAALGRALVSNPD 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 185 ILLMDEAFSALDplirTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVV 244
Cdd:PRK11147 177 VLLLDEPTNHLD----IETIEWLEGFLKTFQGSIIFISHDRSFIRNMATRIVDLDRGKLV 232
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
14-225 |
5.95e-10 |
|
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: 60.95 E-value: 5.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 14 FGEHPQRAFKyieqglSKEQILEKTGLSLGVKDASLAIEEGEIFV-----IMGLSGSGKSTMVRLLNRLIEPTRGQVLID 88
Cdd:COG1245 327 FEVHAPRREK------EEETLVEYPDLTKSYGGFSLEVEGGEIREgevlgIVGPNGIGKTTFAKILAGVLKPDEGEVDED 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 89 gvdiAKIS----------DAELREVRRKKIAmvfqsfalmphmTVLDNTAFGMELAginaeerrekaldalRQVGLENYA 158
Cdd:COG1245 401 ----LKISykpqyispdyDGTVEEFLRSANT------------DDFGSSYYKTEII---------------KPLGLEKLL 449
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16130591 159 HSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDL 225
Cdd:COG1245 450 DKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAENRGKTAMVVDHDI 516
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
35-243 |
9.96e-10 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 60.02 E-value: 9.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 35 LEKTGLS-LGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAE--------LREVRR 105
Cdd:PRK10762 258 LKVDNLSgPGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDglangivyISEDRK 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 106 KKiamvfqsfALMPHMTVLDN---TA---FGMELAGINAEERREKALDALR-----------QVGLenyahsypdeLSGG 168
Cdd:PRK10762 338 RD--------GLVLGMSVKENmslTAlryFSRAGGSLKHADEQQAVSDFIRlfniktpsmeqAIGL----------LSGG 399
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16130591 169 MRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQAKHQrTIVFISHDLDEAMRIGDRIAIMQNGEV 243
Cdd:PRK10762 400 NQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAEGL-SIILVSSEMPEVLGMSDRILVMHEGRI 473
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
25-255 |
1.08e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 60.37 E-value: 1.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 25 IEQG-LSKEQILEKTGLSlgvkDASLAIEEGEIFVIMGLSGSGKSTMVRLLnrlieptrgqvlidgvdIAKISDAELREV 103
Cdd:PLN03232 617 IKNGyFSWDSKTSKPTLS----DINLEIPVGSLVAIVGGTGEGKTSLISAM-----------------LGELSHAETSSV 675
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 104 R-RKKIAMVFQsFALMPHMTVLDNTAFGMELAginaEERREKALDALR-QVGLENYAHSYPDEL-------SGGMRQRVG 174
Cdd:PLN03232 676 ViRGSVAYVPQ-VSWIFNATVRENILFGSDFE----SERYWRAIDVTAlQHDLDLLPGRDLTEIgergvniSGGQKQRVS 750
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 175 LARALAINPDILLMDEAFSALDPLIRTEMQDELVK--LQAKhqrTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEI 252
Cdd:PLN03232 751 MARAVYSNSDIYIFDDPLSALDAHVAHQVFDSCMKdeLKGK---TRVLVTNQL-HFLPLMDRIILVSEGMIKEEGTFAEL 826
|
...
gi 16130591 253 LNN 255
Cdd:PLN03232 827 SKS 829
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
31-243 |
1.49e-09 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 59.36 E-value: 1.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 31 KEQILEKTGLSL----GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAE------- 99
Cdd:PRK10982 247 GEVILEVRNLTSlrqpSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANEainhgfa 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 100 -LREVRRKKIAMVFQSFALMPHMTVLDN--TAFGMeLAGINAEERREKALDALRqVGLENYaHSYPDELSGGMRQRVGLA 176
Cdd:PRK10982 327 lVTEERRSTGIYAYLDIGFNSLISNIRNykNKVGL-LDNSRMKSDTQWVIDSMR-VKTPGH-RTQIGSLSGGNQQKVIIG 403
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16130591 177 RALAINPDILLMDEAFSALDPLIRTEMQDELVKLqAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEV 243
Cdd:PRK10982 404 RWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAEL-AKKDKGIIIISSEMPELLGITDRILVMSNGLV 469
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
14-225 |
1.79e-09 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 59.44 E-value: 1.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 14 FGEHPQRAFKyieqglSKEQILEKTGLSLGVKDASLAIEEGEIFV-----IMGLSGSGKSTMVRLLNRLIEPTRGQVLID 88
Cdd:PRK13409 326 FEERPPRDES------ERETLVEYPDLTKKLGDFSLEVEGGEIYEgevigIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 89 gVDIA----KISDAELREVRrkkiamvfqsFALMPHMTVLDNTAFGMELAginaeerrekaldalRQVGLENYAHSYPDE 164
Cdd:PRK13409 400 -LKISykpqYIKPDYDGTVE----------DLLRSITDDLGSSYYKSEII---------------KPLQLERLLDKNVKD 453
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16130591 165 LSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDL 225
Cdd:PRK13409 454 LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAEEREATALVVDHDI 514
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
48-253 |
5.77e-09 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 57.72 E-value: 5.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELRevrrKKIAMVFQSfaLMPHMTVLDNT 127
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLSFEQLQ----KLVSDEWQR--NNTDMLSPGED 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 128 AFGMELAGINAEERREKALDAL--RQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQD 205
Cdd:PRK10938 97 DTGRTTAEIIQDEVKDPARCEQlaQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAE 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 16130591 206 ELVKLQAKHQrTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEIL 253
Cdd:PRK10938 177 LLASLHQSGI-TLVLVLNRFDEIPDFVQFAGVLADCTLAETGEREEIL 223
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
44-216 |
1.73e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 54.19 E-value: 1.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKIsdaelREVRRKKIAMVFQSFALMPHMTV 123
Cdd:PRK13540 17 LQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKD-----LCTYQKQLCFVGHRSGINPYLTL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 124 LDNTAFGMELAGINAEerrekaLDAL-RQVGLENYAhSYP-DELSGGMRQRVGLARALAINPDILLMDEAFSALDPL--- 198
Cdd:PRK13540 92 RENCLYDIHFSPGAVG------ITELcRLFSLEHLI-DYPcGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELsll 164
|
170 180
....*....|....*....|...
gi 16130591 199 -IRTEMQDELVK----LQAKHQR 216
Cdd:PRK13540 165 tIITKIQEHRAKggavLLTSHQD 187
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
46-223 |
4.76e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 52.95 E-value: 4.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 46 DASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISdaelrevrRKKIAMVFQSFALMPHMTVLD 125
Cdd:PRK13541 18 DLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIA--------KPYCTYIGHNLGLKLEMTVFE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 126 NTAFGMELagINAEERREKALDALRqvgLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRtEMQD 205
Cdd:PRK13541 90 NLKFWSEI--YNSAETLYAAIHYFK---LHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENR-DLLN 163
|
170
....*....|....*...
gi 16130591 206 ELVKLQAKHQRTIVFISH 223
Cdd:PRK13541 164 NLIVMKANSGGIVLLSSH 181
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
45-224 |
7.31e-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: 54.17 E-value: 7.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 45 KDASLAIEEGEIFVIMGLSGSGKSTMVRLLNrlieptrgqvlidGVDiaKISDAELREVRRKKIAMVFQSFALMPHMTVL 124
Cdd:TIGR03719 22 KDISLSFFPGAKIGVLGLNGAGKSTLLRIMA-------------GVD--KDFNGEARPQPGIKVGYLPQEPQLDPTKTVR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 125 DNTAFGM--------ELAGINA-------------------------------EERREKALDALRqvglenyahsYPD-- 163
Cdd:TIGR03719 87 ENVEEGVaeikdaldRFNEISAkyaepdadfdklaaeqaelqeiidaadawdlDSQLEIAMDALR----------CPPwd 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16130591 164 ----ELSGGMRQRVGLARALAINPDILLMDEAFSALDplirTEMQDELVKLQAKHQRTIVFISHD 224
Cdd:TIGR03719 157 advtKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLD----AESVAWLERHLQEYPGTVVAVTHD 217
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
30-248 |
8.09e-08 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 53.11 E-value: 8.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 30 SKEQILEKTGLSLGV------KDASLAIEEGEIFVIMGLSGSGKSTMVRLL--NRLIEPTRGQVLIDGVDIAKIsDAELR 101
Cdd:CHL00131 3 KNKPILEIKNLHASVneneilKGLNLSINKGEIHAIMGPNGSGKSTLSKVIagHPAYKILEGDILFKGESILDL-EPEER 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 102 EvrRKKIAMVFQSFALMPHMTVLD--NTAFG-----MELAGINAEERREKALDALRQVGL-ENYAHSYPDE-LSGGMRQR 172
Cdd:CHL00131 82 A--HLGIFLAFQYPIEIPGVSNADflRLAYNskrkfQGLPELDPLEFLEIINEKLKLVGMdPSFLSRNVNEgFSGGEKKR 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16130591 173 VGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLqAKHQRTIVFISHD---LDEAmrIGDRIAIMQNGEVVQVGT 248
Cdd:CHL00131 160 NEILQMALLDSELAILDETDSGLDIDALKIIAEGINKL-MTSENSIILITHYqrlLDYI--KPDYVHVMQNGKIIKTGD 235
|
|
| CBS_pair_SF |
cd02205 |
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ... |
297-390 |
1.67e-07 |
|
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).
Pssm-ID: 341358 [Multi-domain] Cd Length: 113 Bit Score: 49.17 E-value: 1.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 297 RSALKLLQDEDREYGYVIERGNKFVGAVSIDSLKTALTQQQGLD-----AALIDAPLAVDAQTPLSELLSH-VGQAPCAV 370
Cdd:cd02205 14 REALELMAENGIGALPVVDDDGKLVGIVTERDILRALVEGGLALdtpvaEVMTPDVITVSPDTDLEEALELmLEHGIRRL 93
|
90 100
....*....|....*....|
gi 16130591 371 PVVDEDQQYVGIISKGMLLR 390
Cdd:cd02205 94 PVVDDDGKLVGIVTRRDILR 113
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
18-253 |
1.83e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 53.57 E-value: 1.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 18 PQRAFKYIEQGLSKEQILEKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIE----PTRGQVLIDGvdia 93
Cdd:TIGR00956 51 PNALLKILTRGFRKLKKFRDTKTFDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASNTDgfhiGVEGVITYDG---- 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 94 kISDAELREVRRKKIAMVFQSFALMPHMTVLDNTAFGMELA-------GINAEERREKALD-ALRQVGLenyAHSYP--- 162
Cdd:TIGR00956 127 -ITPEEIKKHYRGDVVYNAETDVHFPHLTVGETLDFAARCKtpqnrpdGVSREEYAKHIADvYMATYGL---SHTRNtkv 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 163 -DEL----SGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELvKLQAKHQRTIVFIS--HDLDEAMRIGDRI 235
Cdd:TIGR00956 203 gNDFvrgvSGGERKRVSIAEASLGGAKIQCWDNATRGLDSATALEFIRAL-KTSANILDTTPLVAiyQCSQDAYELFDKV 281
|
250
....*....|....*...
gi 16130591 236 AIMQNGEVVQVGTPDEIL 253
Cdd:TIGR00956 282 IVLYEGYQIYFGPADKAK 299
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
52-225 |
2.27e-07 |
|
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: 51.60 E-value: 2.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 52 EEGEIFVIMGLSGSGKSTMVRLL-----------------NRLIEPTRGQVLIDGvdIAKISDAELREVRRKkiamvfQS 114
Cdd:cd03236 24 REGQVLGLVGPNGIGKSTALKILagklkpnlgkfddppdwDEILDEFRGSELQNY--FTKLLEGDVKVIVKP------QY 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 115 FALMPhmtvldNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSA 194
Cdd:cd03236 96 VDLIP------KAVKGKVGELLKKKDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSY 169
|
170 180 190
....*....|....*....|....*....|.
gi 16130591 195 LDPLIRTEMQdELVKLQAKHQRTIVFISHDL 225
Cdd:cd03236 170 LDIKQRLNAA-RLIRELAEDDNYVLVVEHDL 199
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
51-239 |
3.85e-07 |
|
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: 49.88 E-value: 3.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 51 IEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAkisdaelreVRRKKIamvfqsfalmphmtvldntafg 130
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITPV---------YKPQYI---------------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 131 melaginaeerrekaldalrqvglenyahsypdELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKL 210
Cdd:cd03222 71 ---------------------------------DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRL 117
|
170 180
....*....|....*....|....*....
gi 16130591 211 QAKHQRTIVFISHDLDEAMRIGDRIAIMQ 239
Cdd:cd03222 118 SEEGKKTALVVEHDLAVLDYLSDRIHVFE 146
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
45-247 |
4.89e-07 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 49.93 E-value: 4.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 45 KDASLAIEEGEIFVIMGLSGSGKSTMVRLL-NRLIEPTR-GQVLIDGvdiakisdAELREVRRKKIAMVFQSFALMPHMT 122
Cdd:cd03232 24 NNISGYVKPGTLTALMGESGAGKTTLLDVLaGRKTAGVItGEILING--------RPLDKNFQRSTGYVEQQDVHSPNLT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 123 VLDNTAFGMELAGINAEERRekaldalrqvglenyahsypdelsggmrqRVGLARALAINPDILLMDEAFSALDPLIRTE 202
Cdd:cd03232 96 VREALRFSALLRGLSVEQRK-----------------------------RLTIGVELAAKPSILFLDEPTSGLDSQAAYN 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 16130591 203 MQDELVKLqAKHQRTIVFISH----DLDEAMrigDRIAIMQ-NGEVVQVG 247
Cdd:cd03232 147 IVRFLKKL-ADSGQAILCTIHqpsaSIFEKF---DRLLLLKrGGKTVYFG 192
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
44-223 |
6.85e-06 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 48.21 E-value: 6.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIePTRGQVLIdgvdiakisdaelrEVRRKKIAMVFQSfalmPHMT- 122
Cdd:TIGR00954 468 IESLSFEVPSGNNLLICGPNGCGKSSLFRILGELW-PVYGGRLT--------------KPAKGKLFYVPQR----PYMTl 528
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 123 -------VLDNTAFGMELAGInAEERREKALDAL-------RQVGLENYAhSYPDELSGGMRQRVGLARALAINPDILLM 188
Cdd:TIGR00954 529 gtlrdqiIYPDSSEDMKRRGL-SDKDLEQILDNVqlthileREGGWSAVQ-DWMDVLSGGEKQRIAMARLFYHKPQFAIL 606
|
170 180 190
....*....|....*....|....*....|....*
gi 16130591 189 DEAFSALDPlirtEMQDELVKLQAKHQRTIVFISH 223
Cdd:TIGR00954 607 DECTSAVSV----DVEGYMYRLCREFGITLFSVSH 637
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
50-225 |
1.22e-05 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 47.50 E-value: 1.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 50 AIEEGEIFVIMGLSGSGKSTMVRLLNRLIEP----TRGQVLIDGVdIAKISDAEL----REVRRKKIAMVF--QSFALMP 119
Cdd:PRK13409 95 IPKEGKVTGILGPNGIGKTTAVKILSGELIPnlgdYEEEPSWDEV-LKRFRGTELqnyfKKLYNGEIKVVHkpQYVDLIP 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 120 HmtVLDNTAfGMELAGINaeeRREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLI 199
Cdd:PRK13409 174 K--VFKGKV-RELLKKVD---ERGKLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRQ 247
|
170 180
....*....|....*....|....*.
gi 16130591 200 RTEMQDELVKLQAKhqRTIVFISHDL 225
Cdd:PRK13409 248 RLNVARLIRELAEG--KYVLVVEHDL 271
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
54-241 |
1.71e-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: 1.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 54 GEIFVIMGLSGSGKSTmvrLLNRLIEPTRGQVLIDGVDIakISDAELREVRRKKIAMVFQSFALMPHMTV---LDNTAFG 130
Cdd:TIGR00956 789 GTLTALMGASGAGKTT---LLNVLAERVTTGVITGGDRL--VNGRPLDSSFQRSIGYVQQQDLHLPTSTVresLRFSAYL 863
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 131 MELAGINAEERREKALDALRQVGLENYAHSY---PDE-LSGGMRQRVGLARALAINPDILL-MDEAFSALDPliRTE--- 202
Cdd:TIGR00956 864 RQPKSVSKSEKMEYVEEVIKLLEMESYADAVvgvPGEgLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLDS--QTAwsi 941
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 16130591 203 MQdeLVKLQAKHQRTIVFISH----DLDEAMrigDRIAIMQNG 241
Cdd:TIGR00956 942 CK--LMRKLADHGQAILCTIHqpsaILFEEF---DRLLLLQKG 979
|
|
| CBS |
COG0517 |
CBS domain [Signal transduction mechanisms]; |
343-398 |
1.97e-05 |
|
CBS domain [Signal transduction mechanisms];
Pssm-ID: 440283 [Multi-domain] Cd Length: 128 Bit Score: 43.70 E-value: 1.97e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 16130591 343 LIDAPLAVDAQTPLSELLSHVGQAPC-AVPVVDEDQQYVGIISKGMLLRALDREGVN 398
Cdd:COG0517 7 MTTDVVTVSPDATVREALELMSEKRIgGLPVVDEDGKLVGIVTDRDLRRALAAEGKD 63
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
35-223 |
3.24e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 46.01 E-value: 3.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 35 LEKTGLSLG----VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLN-RLIE--PTRGQVL-----IDGVDIAKI-----SD 97
Cdd:PLN03073 180 MENFSISVGgrdlIVDASVTLAFGRHYGLVGRNGTGKTTFLRYMAmHAIDgiPKNCQILhveqeVVGDDTTALqcvlnTD 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 98 AELREVRRKKIAMVFQSFAL----------MPHMTVLDNTAFGMELAGI----------NAEERREKALDALRQVglENY 157
Cdd:PLN03073 260 IERTQLLEEEAQLVAQQRELefetetgkgkGANKDGVDKDAVSQRLEEIykrlelidayTAEARAASILAGLSFT--PEM 337
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16130591 158 AHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLqakhQRTIVFISH 223
Cdd:PLN03073 338 QVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKW----PKTFIVVSH 399
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
50-225 |
3.30e-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: 45.93 E-value: 3.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 50 AIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVlIDGVDIAKISDA----EL----REVRRKKI--AMVFQSFALMP 119
Cdd:COG1245 95 VPKKGKVTGILGPNGIGKSTALKILSGELKPNLGDY-DEEPSWDEVLKRfrgtELqdyfKKLANGEIkvAHKPQYVDLIP 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 120 HmtVLDNTAfgMELAGINAEerREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLI 199
Cdd:COG1245 174 K--VFKGTV--RELLEKVDE--RGKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIYQ 247
|
170 180
....*....|....*....|....*.
gi 16130591 200 RTEMQdELVKLQAKHQRTIVFISHDL 225
Cdd:COG1245 248 RLNVA-RLIRELAEEGKYVLVVEHDL 272
|
|
| CBS_pair_chlorobiales |
cd09837 |
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in ... |
299-390 |
4.72e-05 |
|
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in chlorobiales; The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).
Pssm-ID: 341406 [Multi-domain] Cd Length: 111 Bit Score: 42.36 E-value: 4.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 299 ALKLLQDEDREYGYVIERGnKFVGAVSIDSL----KTALTQQQGLDAALIDAPLAVDAQTPLSELLSHVGQAPCA-VPVV 373
Cdd:cd09837 16 VLAFMQAKELSCAPVLHDG-RYVAMVTLADLlparQGTPTAGLKLGELSLEEVGSIGPHEHLFDLFSRLALFPCSiIPVS 94
|
90
....*....|....*..
gi 16130591 374 DEDQQYVGIISKGMLLR 390
Cdd:cd09837 95 DEDGRYIGVVSKKRVLE 111
|
|
| CBS |
COG0517 |
CBS domain [Signal transduction mechanisms]; |
297-395 |
7.39e-05 |
|
CBS domain [Signal transduction mechanisms];
Pssm-ID: 440283 [Multi-domain] Cd Length: 128 Bit Score: 42.16 E-value: 7.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 297 RSALKLLQDEDREYGYVIERGNKFVGAVSI-DSLKTALTQQQGLDAALIDA-----PLAVDAQTPLSELLS-----HVGQ 365
Cdd:COG0517 21 REALELMSEKRIGGLPVVDEDGKLVGIVTDrDLRRALAAEGKDLLDTPVSEvmtrpPVTVSPDTSLEEAAElmeehKIRR 100
|
90 100 110
....*....|....*....|....*....|
gi 16130591 366 apcaVPVVDEDQQYVGIISKGMLLRALDRE 395
Cdd:COG0517 101 ----LPVVDDDGRLVGIITIKDLLKALLEP 126
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
50-241 |
8.95e-05 |
|
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini.
Pssm-ID: 213246 [Multi-domain] Cd Length: 213 Bit Score: 43.41 E-value: 8.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 50 AIEEGEIFVIMGLSGSGKSTmvrllnrlieptrgqvLIDGvdiakISDAELREVRRKKIAMVFQSFALMPHMTVldNTAF 129
Cdd:cd03279 24 GLDNNGLFLICGPTGAGKST----------------ILDA-----ITYALYGKTPRYGRQENLRSVFAPGEDTA--EVSF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 130 GMELAGINAEERREKALDA--------LRQVGLENYAHSYPDELSGGMRQRVGLARALA----------INPDILLMDEA 191
Cdd:cd03279 81 TFQLGGKKYRVERSRGLDYdqftrivlLPQGEFDRFLARPVSTLSGGETFLASLSLALAlsevlqnrggARLEALFIDEG 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 16130591 192 FSALDPLIRtEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNG 241
Cdd:cd03279 161 FGTLDPEAL-EAVATALELIRTENRMVGVISHVEELKERIPQRLEVIKTP 209
|
|
| CBS_pair_peptidase_M50 |
cd04639 |
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in the ... |
312-392 |
1.19e-04 |
|
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in the metalloprotease peptidase M50; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in peptidase M50. Members of the M50 metallopeptidase family include mammalian sterol-regulatory element binding protein (SREBP) site 2 proteases and various hypothetical bacterial homologues. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).
Pssm-ID: 341397 [Multi-domain] Cd Length: 120 Bit Score: 41.40 E-value: 1.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 312 YVIERGNKFVGAVSIDSLKTALTQQqGLDAAL------IDAPLAVDAQTPLSELLSHVGQAPC-AVPVVDEDQQYVGIIS 384
Cdd:cd04639 34 LVTDEAGRLVGLITVDDLRAIPTSQ-WPDTPVrelmkpLEEIPTVAADQSLLEVVKLLEEQQLpALAVVSENGTLVGLIE 112
|
....*...
gi 16130591 385 KGMLLRAL 392
Cdd:cd04639 113 KEDIIELL 120
|
|
| COG2524 |
COG2524 |
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription]; |
297-392 |
1.25e-04 |
|
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];
Pssm-ID: 442013 [Multi-domain] Cd Length: 206 Bit Score: 42.95 E-value: 1.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 297 RSALKLLQDEDREYGYVIERGnKFVGAVSIDSLKTALTQQQGLDAALIDA-----PLAVDAQTPLSELL-----SHVGqa 366
Cdd:COG2524 106 EEALELMLEKGISGLPVVDDG-KLVGIITERDLLKALAEGRDLLDAPVSDimtrdVVTVSEDDSLEEALrlmleHGIG-- 182
|
90 100
....*....|....*....|....*.
gi 16130591 367 pcAVPVVDEDQQYVGIISKGMLLRAL 392
Cdd:COG2524 183 --RLPVVDDDGKLVGIITRTDILRAL 206
|
|
| COG3448 |
COG3448 |
CBS-domain-containing membrane protein [Signal transduction mechanisms]; |
299-395 |
1.27e-04 |
|
CBS-domain-containing membrane protein [Signal transduction mechanisms];
Pssm-ID: 442671 [Multi-domain] Cd Length: 136 Bit Score: 41.77 E-value: 1.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 299 ALKLLqdedREYGY----VIERGNKFVGAVSIDSLKTALTQQQGLDAALIDA-----------PLAVDAQTPLSELL--- 360
Cdd:COG3448 24 ALELM----REHGIrglpVVDEDGRLVGIVTERDLLRALLPDRLDELEERLLdlpvedvmtrpVVTVTPDTPLEEAAelm 99
|
90 100 110
....*....|....*....|....*....|....*..
gi 16130591 361 --SHVGqapcAVPVVDEDQQYVGIISKGMLLRALDRE 395
Cdd:COG3448 100 leHGIH----RLPVVDDDGRLVGIVTRTDLLRALARL 132
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
85-256 |
1.60e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 43.85 E-value: 1.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 85 VLIDGVDIAKISDAELREvrrkkiAMVFqsfalmphmtvLDNTAFGMELAGINAEERRE--KALDALRQVGLENYAHSYP 162
Cdd:TIGR00630 423 VTVGGKSIADVSELSIRE------AHEF-----------FNQLTLTPEEKKIAEEVLKEirERLGFLIDVGLDYLSLSRA 485
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 163 -DELSGGMRQRVGLARAL--AINPDILLMDEAFSALDP-----LIRTemqdeLVKLQAKHQRTIVfISHDlDEAMRIGDR 234
Cdd:TIGR00630 486 aGTLSGGEAQRIRLATQIgsGLTGVLYVLDEPSIGLHQrdnrrLINT-----LKRLRDLGNTLIV-VEHD-EDTIRAADY 558
|
170 180
....*....|....*....|....*...
gi 16130591 235 I------AIMQNGEVVQVGTPDEILNNP 256
Cdd:TIGR00630 559 VidigpgAGEHGGEVVASGTPEEILANP 586
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
165-238 |
1.78e-04 |
|
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: 41.58 E-value: 1.78e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16130591 165 LSGGMRQRVGLARALA---INPDIL-LMDEAFSALDPLiRTEMQDELVKLQAKHQRTIVFISHDLdEAMRIGDRIAIM 238
Cdd:cd03227 78 LSGGEKELSALALILAlasLKPRPLyILDEIDRGLDPR-DGQALAEAILEHLVKGAQVIVITHLP-ELAELADKLIHI 153
|
|
| YtoI |
COG4109 |
Predicted transcriptional regulator containing CBS domains [Transcription]; |
260-392 |
2.04e-04 |
|
Predicted transcriptional regulator containing CBS domains [Transcription];
Pssm-ID: 443285 [Multi-domain] Cd Length: 135 Bit Score: 41.05 E-value: 2.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 260 YVRTFFRGVDISQVFSAKDIARRTPNGLIRKtpgfgprsALKLLqdEDREYGY--VIERGNKFVGAVSIDSLKTALTQQQ 337
Cdd:COG4109 8 SYDTFKEILLVEDIMTLEDVATLSEDDTVED--------ALELL--EKTGHSRfpVVDENGRLVGIVTSKDILGKDDDTP 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 16130591 338 gLDAALIDAPLAVDAQTPL---SELLSHVGQApcAVPVVDEDQQYVGIISKGMLLRAL 392
Cdd:COG4109 78 -IEDVMTKNPITVTPDTSLasaAHKMIWEGIE--LLPVVDDDGRLLGIISRQDVLKAL 132
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
59-226 |
2.96e-04 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 42.80 E-value: 2.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 59 IMGLSGSGKSTMVRLLNRLIEPTRGQ-VLIDGVDIAKIS-----DAE----------LREVRRKK-----IAMVF----- 112
Cdd:PRK11819 38 VLGLNGAGKSTLLRIMAGVDKEFEGEaRPAPGIKVGYLPqepqlDPEktvrenveegVAEVKAALdrfneIYAAYaepda 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 113 QSFALMPHMTVLDNtafgmELAGINA---EERREKALDALR------QVGlenyahsypdELSGGMRQRVGLARALAINP 183
Cdd:PRK11819 118 DFDALAAEQGELQE-----IIDAADAwdlDSQLEIAMDALRcppwdaKVT----------KLSGGERRRVALCRLLLEKP 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 16130591 184 DILLMDEAFSALDplirTEMQDELVKLQAKHQRTIVFISHD---LD 226
Cdd:PRK11819 183 DMLLLDEPTNHLD----AESVAWLEQFLHDYPGTVVAVTHDryfLD 224
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
132-235 |
3.39e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 42.85 E-value: 3.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 132 ELAGINAEERREKALDALRQVGLENYAHSYP-DELSGGMRQRVGLARALAINPDILLMDEAFSA--LDPLIRTEmqdelv 208
Cdd:PRK10636 116 KLDAIDAWTIRSRAASLLHGLGFSNEQLERPvSDFSGGWRMRLNLAQALICRSDLLLLDEPTNHldLDAVIWLE------ 189
|
90 100
....*....|....*....|....*..
gi 16130591 209 KLQAKHQRTIVFISHDLDEAMRIGDRI 235
Cdd:PRK10636 190 KWLKSYQGTLILISHDRDFLDPIVDKI 216
|
|
| CBS |
pfam00571 |
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ... |
347-392 |
3.89e-04 |
|
CBS domain; CBS domains are small intracellular modules that pair together to form a stable globular domain. This family represents a single CBS domain. Pairs of these domains have been termed a Bateman domain. CBS domains have been shown to bind ligands with an adenosyl group such as AMP, ATP and S-AdoMet. CBS domains are found attached to a wide range of other protein domains suggesting that CBS domains may play a regulatory role making proteins sensitive to adenosyl carrying ligands. The region containing the CBS domains in Cystathionine-beta synthase is involved in regulation by S-AdoMet. CBS domain pairs from AMPK bind AMP or ATP. The CBS domains from IMPDH and the chloride channel CLC2 bind ATP.
Pssm-ID: 425756 [Multi-domain] Cd Length: 57 Bit Score: 38.35 E-value: 3.89e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 16130591 347 PLAVDAQTPLSELLSHVGQAPC-AVPVVDEDQQYVGIISKGMLLRAL 392
Cdd:pfam00571 9 VVTVSPDTTLEEALELMREHGIsRLPVVDEDGKLVGIVTLKDLLRAL 55
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
44-247 |
7.31e-04 |
|
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: 40.00 E-value: 7.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 44 VKDASLAIEEGEIFVIMGLSGSGKSTmvrLLNRLIEPTRGQVLIDGvdiakisdaeLREVRRKKIAMVFQsfalmphmtv 123
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKST---LVNEGLYASGKARLISF----------LPKFSRNKLIFIDQ---------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 124 ldntafgmelaginaeerrekaLDALRQVGLENYAHSYP-DELSGGMRQRVGLARALAINPD--ILLMDEAFSALDPLIR 200
Cdd:cd03238 68 ----------------------LQFLIDVGLGYLTLGQKlSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDI 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 16130591 201 TEMQDELVKL-QAKHqrTIVFISHDLDeAMRIGDRIAIM------QNGEVVQVG 247
Cdd:cd03238 126 NQLLEVIKGLiDLGN--TVILIEHNLD-VLSSADWIIDFgpgsgkSGGKVVFSG 176
|
|
| CBS_pair_HPP_assoc |
cd04600 |
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ... |
313-394 |
8.55e-04 |
|
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the HPP motif domain; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the HPP motif domain. These proteins are integral membrane proteins with four transmembrane spanning helices. The function of these proteins is uncertain, but they are thought to be transporters. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).
Pssm-ID: 341375 [Multi-domain] Cd Length: 133 Bit Score: 39.08 E-value: 8.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 313 VIERGNKFVGAVS-IDSLKTA-LTQQQGLDAALIDAPL------------------AVDAQTPLSELLSHVGQAPC-AVP 371
Cdd:cd04600 31 VVDRARRLVGIVTlADLLKHAdLDPPRGLRGRLRRTLGlrrdrpetvgdimtrpvvTVRPDTPIAELVPLFSDGGLhHIP 110
|
90 100
....*....|....*....|...
gi 16130591 372 VVDEDQQYVGIISKGMLLRALDR 394
Cdd:cd04600 111 VVDADGRLVGIVTQSDLIAALYR 133
|
|
| CBS_pair_SF |
cd02205 |
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ... |
347-399 |
2.24e-03 |
|
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).
Pssm-ID: 341358 [Multi-domain] Cd Length: 113 Bit Score: 37.61 E-value: 2.24e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 16130591 347 PLAVDAQTPLSELLSHVGQ-APCAVPVVDEDQQYVGIISKGMLLRALDREGVNN 399
Cdd:cd02205 4 VVTVDPDTTVREALELMAEnGIGALPVVDDDGKLVGIVTERDILRALVEGGLAL 57
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
44-196 |
2.26e-03 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 39.39 E-value: 2.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLL--NRLIEPTRGQVLIDGVDIAKISDAELREvrrKKIAMVFQSFALMPHM 121
Cdd:PRK09580 17 LRGLNLEVRPGEVHAIMGPNGSGKSTLSATLagREDYEVTGGTVEFKGKDLLELSPEDRAG---EGIFMAFQYPVEIPGV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130591 122 TvldnTAFGMELAgINA--EERREKALD------------ALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILL 187
Cdd:PRK09580 94 S----NQFFLQTA-LNAvrSYRGQEPLDrfdfqdlmeekiALLKMPEDLLTRSVNVGFSGGEKKRNDILQMAVLEPELCI 168
|
....*....
gi 16130591 188 MDEAFSALD 196
Cdd:PRK09580 169 LDESDSGLD 177
|
|
| COG2905 |
COG2905 |
Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains ... |
343-398 |
2.59e-03 |
|
Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains [Signal transduction mechanisms];
Pssm-ID: 442149 [Multi-domain] Cd Length: 124 Bit Score: 37.50 E-value: 2.59e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16130591 343 LIDAPLAVDAQTPLSELL-----SHVGqapcAVPVVDEDQQYVGIISKGMLLRALDREGVN 398
Cdd:COG2905 5 MSRDVVTVSPDATVREAArlmteKGVG----SLVVVDDDGRLVGIITDRDLRRRVLAEGLD 61
|
|
| |
