|
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: 721.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 1 MAIKLEIKNLYKIFGEHPHRAFKYIEKGLNKAQILEKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEP 80
Cdd:PRK10070 1 MAIKLEIKNLYKIFGEHPQRAFKYIEQGLSKEQILEKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 81 TRGQVLIDGVDIAKMSDAELREVRRKKIAMVFQSFALMPHMSVLDNTAFGMALAGVPAAEREQKAREALRQVGLENYAHA 160
Cdd:PRK10070 81 TRGQVLIDGVDIAKISDAELREVRRKKIAMVFQSFALMPHMTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 161 WPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELIKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQN 240
Cdd:PRK10070 161 YPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 241 GEVVQVGTPDEILNNPANDYVRTFFRGVDISQVFSAKDIARRSPVGLIRKTPGFGPRSALKLLQDEDREYGYVIERGNRF 320
Cdd:PRK10070 241 GEVVQVGTPDEILNNPANDYVRTFFRGVDISQVFSAKDIARRTPNGLIRKTPGFGPRSALKLLQDEDREYGYVIERGNKF 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 321 VGIVSIDSLKTALSAGQGIEAALIDAPLAVEAQTPLSDLLSHVGHAPCAVPVVDEEQQYIGIISKRMLLQALDREGVNHG 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: 666.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 3 IKLEIKNLYKIFGEHPHRAFKYIEKGLNKAQILEKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTR 82
Cdd:COG4175 2 PKIEVRNLYKIFGKRPERALKLLDQGKSKDEILEKTGQTVGVNDASFDVEEGEIFVIMGLSGSGKSTLVRCLNRLIEPTA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 83 GQVLIDGVDIAKMSDAELREVRRKKIAMVFQSFALMPHMSVLDNTAFGMALAGVPAAEREQKAREALRQVGLENYAHAWP 162
Cdd:COG4175 82 GEVLIDGEDITKLSKKELRELRRKKMSMVFQHFALLPHRTVLENVAFGLEIQGVPKAERRERAREALELVGLAGWEDSYP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 163 DELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELIKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGE 242
Cdd:COG4175 162 DELSGGMQQRVGLARALATDPDILLMDEAFSALDPLIRREMQDELLELQAKLKKTIVFITHDLDEALRLGDRIAIMKDGR 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 243 VVQVGTPDEILNNPANDYVRTFFRGVDISQVFSAKDIARRSPVGLIRKTpgfGPRSALKLLQDEDREYGYVIERGNRFVG 322
Cdd:COG4175 242 IVQIGTPEEILTNPANDYVADFVEDVDRSKVLTAGSVMRPPEAVVSEKD---GPRVALRRMREEGISSLYVVDRDRRLLG 318
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 378980240 323 IVSIDSLKTALSAGQGIEAALIDAPLAVEAQTPLSDLLSHVGHAPCAVPVVDEEQQYIGIISKRMLLQALD 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: 571.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 36 EKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKMSDAELREVRRKKIAMVFQSF 115
Cdd:TIGR01186 1 KKTGGKKGVNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEPTAGQIFIDGENIMKQSPVELREVRRKKIGMVFQQF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 116 ALMPHMSVLDNTAFGMALAGVPAAEREQKAREALRQVGLENYAHAWPDELSGGMRQRVGLARALAINPDILLMDEAFSAL 195
Cdd:TIGR01186 81 ALFPHMTILQNTSLGPELLGWPEQERKEKALELLKLVGLEEYEHRYPDELSGGMQQRVGLARALAAEPDILLMDEAFSAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 196 DPLIRTEMQDELIKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFFRGVDISQVFS 275
Cdd:TIGR01186 161 DPLIRDSMQDELKKLQATLQKTIVFITHDLDEAIRIGDRIVIMKAGEIVQVGTPDEILRNPANEYVEEFIGKVDLSQVFD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 276 AKDIARRSPVGLIRKTPGFGPRSALKLLQDEDREYGYVIERGNRFVGIVSIDSLKTALSAGQGIEAALIDAPLAVEAQTP 355
Cdd:TIGR01186 241 AERIAQRMNTGPITKTADKGPRSALQLMRDERVDSLYVVDRQNKLVGVVDVESIKQARKKAQGLQDVLIDDIYTVDAGTL 320
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 378980240 356 LSDLLSHVGHAPCAVPVVDEEQQYIGIISKRMLLQALD--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: 506.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 5 LEIKNLYKIFGEHPHRAFKYIEKGLNKAQILEKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQ 84
Cdd:cd03294 1 IKIKGLYKIFGKNPQKAFKLLAKGKSKEEILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 85 VLIDGVDIAKMSDAELREVRRKKIAMVFQSFALMPHMSVLDNTAFGMALAGVPAAEREQKAREALRQVGLENYAHAWPDE 164
Cdd:cd03294 81 VLIDGQDIAAMSRKELRELRRKKISMVFQSFALLPHRTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 165 LSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELIKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVV 244
Cdd:cd03294 161 LSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLV 240
|
250 260
....*....|....*....|....*....
gi 378980240 245 QVGTPDEILNNPANDYVRTFFRGVDISQV 273
Cdd:cd03294 241 QVGTPEEILTNPANDYVREFFRGVDRAKV 269
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-265 |
5.59e-99 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 298.55 E-value: 5.59e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 1 MAIKLEIKNLYKIFGEHPhrafkyiekglnkaqilektglslGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEP 80
Cdd:COG3842 2 AMPALELENVSKRYGDVT------------------------ALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETP 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 81 TRGQVLIDGVDIAKMSdAELREvrrkkIAMVFQSFALMPHMSVLDNTAFGMALAGVPAAEREQKAREALRQVGLENYAHA 160
Cdd:COG3842 58 DSGRILLDGRDVTGLP-PEKRN-----VGMVFQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADR 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 161 WPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELIKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQN 240
Cdd:COG3842 132 YPHQLSGGQQQRVALARALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMND 211
|
250 260
....*....|....*....|....*
gi 378980240 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 |
1.01e-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: 293.82 E-value: 1.01e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKMSDAELRevrrKKIAMVFQSFALMPHMSV 123
Cdd:cd03295 17 VNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELR----RKIGYVIQQIGLFPHMTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 124 LDNTAFGMALAGVPAAEREQKAREALRQVGLE--NYAHAWPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRT 201
Cdd:cd03295 93 EENIALVPKLLKWPKEKIRERADELLALVGLDpaEFADRYPHELSGGQQQRVGVARALAADPPLLLMDEPFGALDPITRD 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 378980240 202 EMQDELIKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFF 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 |
7.71e-97 |
|
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: 287.88 E-value: 7.71e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 5 LEIKNLYKIFGEHPHrafkyiekglnkaqilektglslgVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQ 84
Cdd:cd03259 1 LELKGLSKTYGSVRA------------------------LDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGE 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 85 VLIDGVDIAKMSdaelreVRRKKIAMVFQSFALMPHMSVLDNTAFGMALAGVPAAEREQKAREALRQVGLENYAHAWPDE 164
Cdd:cd03259 57 ILIDGRDVTGVP------PERRNIGMVFQDYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHE 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 165 LSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELIKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVV 244
Cdd:cd03259 131 LSGGQQQRVALARALAREPSLLLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIV 210
|
...
gi 378980240 245 QVG 247
Cdd:cd03259 211 QVG 213
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-265 |
2.04e-95 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 289.28 E-value: 2.04e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 1 MAiKLEIKNLYKIFGEHPHrafkyiekglnkaqilektglslgVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEP 80
Cdd:COG3839 1 MA-SLELENVSKSYGGVEA------------------------LKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDP 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 81 TRGQVLIDGVDIAKMsdaelrEVRRKKIAMVFQSFALMPHMSVLDNTAFGMALAGVPAAEREQKAREALRQVGLENYAHA 160
Cdd:COG3839 56 TSGEILIGGRDVTDL------PPKDRNIAMVFQSYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDR 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 161 WPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELIKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQN 240
Cdd:COG3839 130 KPKQLSGGQRQRVALGRALVREPKVFLLDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMND 209
|
250 260
....*....|....*....|....*
gi 378980240 241 GEVVQVGTPDEILNNPANDYVRTFF 265
Cdd:COG3839 210 GRIQQVGTPEELYDRPANLFVAGFI 234
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-249 |
6.31e-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: 274.66 E-value: 6.31e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 1 MAIKLEIKNLYKIFGEhphrafkyiEKGLNKAqilektglslgVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEP 80
Cdd:COG1116 4 AAPALELRGVSKRFPT---------GGGGVTA-----------LDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKP 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 81 TRGQVLIDGVDIAKmsdaelrevRRKKIAMVFQSFALMPHMSVLDNTAFGMALAGVPAAEREQKAREALRQVGLENYAHA 160
Cdd:COG1116 64 TSGEVLVDGKPVTG---------PGPDRGVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDA 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 161 WPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELIKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQN 240
Cdd:COG1116 135 YPHQLSGGMRQRVAIARALANDPEVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFLADRVVVLSA 214
|
250
....*....|....
gi 378980240 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 |
1.88e-88 |
|
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: 267.62 E-value: 1.88e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 1 MAIKLEIKNLYKIFGEHPhrafkyiekglnkaqILektglslgvKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEP 80
Cdd:COG1127 2 SEPMIEVRNLTKSFGDRV---------------VL---------DGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRP 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 81 TRGQVLIDGVDIAKMSDAELREVRRKkIAMVFQSFALMPHMSVLDNTAFGM-ALAGVPAAEREQKAREALRQVGLENYAH 159
Cdd:COG1127 58 DSGEILVDGQDITGLSEKELYELRRR-IGMLFQGGALFDSLTVFENVAFPLrEHTDLSEAEIRELVLEKLELVGLPGAAD 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 160 AWPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPlIRTEMQDELI-KLQAKHQRTIVFISHDLDEAMRIGDRIAIM 238
Cdd:COG1127 137 KMPSELSGGMRKRVALARALALDPEILLYDEPTAGLDP-ITSAVIDELIrELRDELGLTSVVVTHDLDSAFAIADRVAVL 215
|
250 260
....*....|....*....|....*..
gi 378980240 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 ... |
44-238 |
1.60e-87 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 264.33 E-value: 1.60e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGvdiakmsdAELREVRRKkIAMVFQSFALMPHMSV 123
Cdd:cd03293 20 LEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDG--------EPVTGPGPD-RGYVFQQDALLPWLTV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 124 LDNTAFGMALAGVPAAEREQKAREALRQVGLENYAHAWPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEM 203
Cdd:cd03293 91 LDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDEPFSALDALTREQL 170
|
170 180 190
....*....|....*....|....*....|....*
gi 378980240 204 QDELIKLQAKHQRTIVFISHDLDEAMRIGDRIAIM 238
Cdd:cd03293 171 QEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVL 205
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
5-268 |
8.71e-85 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 261.55 E-value: 8.71e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 5 LEIKNLYKIF--GEHPHRAfkyiekglnkaqilektglslgVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTR 82
Cdd:COG1135 2 IELENLSKTFptKGGPVTA----------------------LDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTS 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 83 GQVLIDGVDIAKMSDAELREVRRKkIAMVFQSFALMPHMSVLDNTAFGMALAGVPAAEREQKAREALRQVGLENYAHAWP 162
Cdd:COG1135 60 GSVLVDGVDLTALSERELRAARRK-IGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYP 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 163 DELSGGMRQRVGLARALAINPDILLMDEAFSALDP--------LIRtemqdeliKLQAKHQRTIVFISHDLDEAMRIGDR 234
Cdd:COG1135 139 SQLSGGQKQRVGIARALANNPKVLLCDEATSALDPettrsildLLK--------DINRELGLTIVLITHEMDVVRRICDR 210
|
250 260 270
....*....|....*....|....*....|....
gi 378980240 235 IAIMQNGEVVQVGTPDEILNNPANDYVRTFFRGV 268
Cdd:COG1135 211 VAVLENGRIVEQGPVLDVFANPQSELTRRFLPTV 244
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
5-268 |
1.67e-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: 1.67e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 5 LEIKNLYKIFGEHphrafkyiekglnkaQILektglslgvKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQ 84
Cdd:COG1126 2 IEIENLHKSFGDL---------------EVL---------KGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGT 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 85 VLIDGVDIAkMSDAELREVRRKkIAMVFQSFALMPHMSVLDNTAFG-MALAGVPAAEREQKAREALRQVGLENYAHAWPD 163
Cdd:COG1126 58 ITVDGEDLT-DSKKDINKLRRK-VGMVFQQFNLFPHLTVLENVTLApIKVKKMSKAEAEERAMELLERVGLADKADAYPA 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 164 ELSGGMRQRVGLARALAINPDILLMDEAFSALDPlirtEMQDE---LIKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQN 240
Cdd:COG1126 136 QLSGGQQQRVAIARALAMEPKVMLFDEPTSALDP----ELVGEvldVMRDLAKEGMTMVVVTHEMGFAREVADRVVFMDG 211
|
250 260
....*....|....*....|....*...
gi 378980240 241 GEVVQVGTPDEILNNPANDYVRTFFRGV 268
Cdd:COG1126 212 GRIVEEGPPEEFFENPQHERTRAFLSKV 239
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
5-263 |
4.84e-82 |
|
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: 260.22 E-value: 4.84e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 5 LEIKNLYKIFGEHPHRAFKyiekglnkaqilektglslGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQ 84
Cdd:COG1123 261 LEVRNLSKRYPVRGKGGVR-------------------AVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGS 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 85 VLIDGVDIAKMSDAELREVRRKkIAMVFQ--SFALMPHMSVLDNTAFGMALAGV-PAAEREQKAREALRQVGL-ENYAHA 160
Cdd:COG1123 322 ILFDGKDLTKLSRRSLRELRRR-VQMVFQdpYSSLNPRMTVGDIIAEPLRLHGLlSRAERRERVAELLERVGLpPDLADR 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 161 WPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELIKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQN 240
Cdd:COG1123 401 YPHELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYD 480
|
250 260
....*....|....*....|...
gi 378980240 241 GEVVQVGTPDEILNNPANDYVRT 263
Cdd:COG1123 481 GRIVEDGPTEEVFANPQHPYTRA 503
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
39-264 |
5.59e-81 |
|
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: 248.31 E-value: 5.59e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 39 GLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKMSdaelreVRRKKIAMVFQSFALM 118
Cdd:cd03300 11 GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLP------PHKRPVNTVFQNYALF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 119 PHMSVLDNTAFGMALAGVPAAEREQKAREALRQVGLENYAHAWPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPL 198
Cdd:cd03300 85 PHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALDLK 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 378980240 199 IRTEMQDELIKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTF 264
Cdd:cd03300 165 LRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPANRFVADF 230
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
44-343 |
6.10e-81 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 251.99 E-value: 6.10e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIakMSDaelREVRRKKIAMVFQSFALMPHMSV 123
Cdd:COG1118 18 LDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDL--FTN---LPPRERRVGFVFQHYALFPHMTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 124 LDNTAFGMALAGVPAAEREQKAREALRQVGLENYAHAWPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEM 203
Cdd:COG1118 93 AENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLLLDEPFGALDAKVRKEL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 204 QDELIKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYV------RTFFRGVDISQVFSAK 277
Cdd:COG1118 173 RRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDRPATPFVarflgcVNVLRGRVIGGQLEAD 252
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 378980240 278 DIARRSPVGLIRKTPGFGPR-SALKLLQDEDREYGY--VIERGNRFVGIVSIDsLKTALSAGQGIEAAL 343
Cdd:COG1118 253 GLTLPVAEPLPDGPAVAGVRpHDIEVSREPEGENTFpaTVARVSELGPEVRVE-LKLEDGEGQPLEAEV 320
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
5-264 |
5.26e-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: 245.87 E-value: 5.26e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 5 LEIKNLYKIFGEHphrafkyiekglnkaQILektglslgvKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQ 84
Cdd:cd03261 1 IELRGLTKSFGGR---------------TVL---------KGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGE 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 85 VLIDGVDIAKMSDAELREVRRKkIAMVFQSFALMPHMSVLDNTAFGM----ALagvPAAEREQKAREALRQVGLENYAHA 160
Cdd:cd03261 57 VLIDGEDISGLSEAELYRLRRR-MGMLFQSGALFDSLTVFENVAFPLrehtRL---SEEEIREIVLEKLEAVGLRGAEDL 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 161 WPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPlIRTEMQDELI-KLQAKHQRTIVFISHDLDEAMRIGDRIAIMQ 239
Cdd:cd03261 133 YPAELSGGMKKRVALARALALDPELLLYDEPTAGLDP-IASGVIDDLIrSLKKELGLTSIMVTHDLDTAFAIADRIAVLY 211
|
250 260
....*....|....*....|....*
gi 378980240 240 NGEVVQVGTPDEILNNPaNDYVRTF 264
Cdd:cd03261 212 DGKIVAEGTPEELRASD-DPLVRQF 235
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
5-256 |
4.64e-78 |
|
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: 240.56 E-value: 4.64e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 5 LEIKNLYKIFGEHPHRAfkyiekglnKAqilektglslgVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQ 84
Cdd:cd03258 2 IELKNVSKVFGDTGGKV---------TA-----------LKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGS 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 85 VLIDGVDIAKMSDAELREVRRKkIAMVFQSFALMPHMSVLDNTAFGMALAGVPAAEREQKAREALRQVGLENYAHAWPDE 164
Cdd:cd03258 62 VLVDGTDLTLLSGKELRKARRR-IGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 165 LSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELIKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVV 244
Cdd:cd03258 141 LSGGQKQRVGIARALANNPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVV 220
|
250
....*....|..
gi 378980240 245 QVGTPDEILNNP 256
Cdd:cd03258 221 EEGTVEEVFANP 232
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
5-243 |
4.59e-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: 232.38 E-value: 4.59e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 5 LEIKNLYKIFGEhphrafkyiekGLNKAQILektglslgvKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQ 84
Cdd:cd03255 1 IELKNLSKTYGG-----------GGEKVQAL---------KGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGE 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 85 VLIDGVDIAKMSDAELREVRRKKIAMVFQSFALMPHMSVLDNTAFGMALAGVPAAEREQKAREALRQVGLENYAHAWPDE 164
Cdd:cd03255 61 VRVDGTDISKLSEKELAAFRRRHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSE 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 378980240 165 LSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELIKLQAKHQRTIVFISHDLDEAmRIGDRIAIMQNGEV 243
Cdd:cd03255 141 LSGGQQQRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELA-EYADRIIELRDGKI 218
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-244 |
2.18e-74 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 231.09 E-value: 2.18e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 1 MAIKLEIKNLYKIFGEhphrafkyiekGLNKAQILektglslgvKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEP 80
Cdd:COG1136 1 MSPLLELRNLTKSYGT-----------GEGEVTAL---------RGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRP 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 81 TRGQVLIDGVDIAKMSDAELREVRRKKIAMVFQSFALMPHMSVLDNTAFGMALAGVPAAEREQKAREALRQVGLENYAHA 160
Cdd:COG1136 61 TSGEVLIDGQDISSLSERELARLRRRHIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDH 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 161 WPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELIKLQAKHQRTIVFISHDLdEAMRIGDRIAIMQN 240
Cdd:COG1136 141 RPSQLSGGQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDP-ELAARADRVIRLRD 219
|
....
gi 378980240 241 GEVV 244
Cdd:COG1136 220 GRIV 223
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
5-247 |
3.30e-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: 230.22 E-value: 3.30e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 5 LEIKNLYKIFGEHPhrafkyiekglnkaqilektglslGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQ 84
Cdd:cd03301 1 VELENVTKRFGNVT------------------------ALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGR 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 85 VLIDGVDIAKMSDAElrevrrKKIAMVFQSFALMPHMSVLDNTAFGMALAGVPAAEREQKAREALRQVGLENYAHAWPDE 164
Cdd:cd03301 57 IYIGGRDVTDLPPKD------RDIAMVFQNYALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQ 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 165 LSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELIKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVV 244
Cdd:cd03301 131 LSGGQRQRVALGRAIVREPKVFLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQ 210
|
...
gi 378980240 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 |
3.96e-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: 225.91 E-value: 3.96e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 5 LEIKNLYKIFGEHphrafkyiekglnkaqilektglsLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQ 84
Cdd:cd03229 1 LELKNVSKRYGQK------------------------TVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGS 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 85 VLIDGVDIAKMSDaeLREVRRKKIAMVFQSFALMPHMSVLDNTAFGmalagvpaaereqkarealrqvglenyahawpde 164
Cdd:cd03229 57 ILIDGEDLTDLED--ELPPLRRRIGMVFQDFALFPHLTVLENIALG---------------------------------- 100
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 378980240 165 LSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELIKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGE 242
Cdd:cd03229 101 LSGGQQQRVALARALAMDPDVLLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
5-254 |
8.55e-72 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 224.56 E-value: 8.55e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 5 LEIKNLYKIFGEHPhrafkyiekglnkaqilektglslGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQ 84
Cdd:COG1131 1 IEVRGLTKRYGDKT------------------------ALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGE 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 85 VLIDGVDIAKmsdaELREVRRKkIAMVFQSFALMPHMSVLDNTAFGMALAGVPAAEREQKAREALRQVGLENYAHAWPDE 164
Cdd:COG1131 57 VRVLGEDVAR----DPAEVRRR-IGYVPQEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGT 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 165 LSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELIKLqAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVV 244
Cdd:COG1131 132 LSGGMKQRLGLALALLHDPELLILDEPTSGLDPEARRELWELLREL-AAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIV 210
|
250
....*....|
gi 378980240 245 QVGTPDEILN 254
Cdd:COG1131 211 ADGTPDELKA 220
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
43-289 |
9.16e-72 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 228.15 E-value: 9.16e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKMSDAELREVRRKkIAMVFQSFALMPHMS 122
Cdd:PRK11153 20 ALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKARRQ-IGMIFQHFNLLSSRT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 123 VLDNTAFGMALAGVPAAEREQKAREALRQVGLENYAHAWPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPlirtE 202
Cdd:PRK11153 99 VFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPKVLLCDEATSALDP----A 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 203 MQDELIKLQAKHQR----TIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFFR---GVDISQVFS 275
Cdd:PRK11153 175 TTRSILELLKDINRelglTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHPKHPLTREFIQstlHLDLPEDYL 254
|
250
....*....|....*.
gi 378980240 276 AKDIARRSPVG--LIR 289
Cdd:PRK11153 255 ARLQAEPTTGSgpLLR 270
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
44-256 |
4.89e-71 |
|
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: 222.59 E-value: 4.89e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKmsdAELREVRRKkIAMVFQS-----FAlm 118
Cdd:COG1122 17 LDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITK---KNLRELRRK-VGLVFQNpddqlFA-- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 119 phMSVLDNTAFGMALAGVPAAEREQKAREALRQVGLENYAHAWPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPL 198
Cdd:COG1122 91 --PTVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPR 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 378980240 199 IRTEMQDELIKLQAKHqRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNP 256
Cdd:COG1122 169 GRRELLELLKRLNKEG-KTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDY 225
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
5-257 |
1.40e-70 |
|
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: 224.55 E-value: 1.40e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 5 LEIKNLYKIFgehphrafkYIEKGLNKAqilektglslgVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEP---T 81
Cdd:COG0444 2 LEVRNLKVYF---------PTRRGVVKA-----------VDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiT 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 82 RGQVLIDGVDIAKMSDAELREVRRKKIAMVFQSF--ALMPHMSVLDntAFGMALA---GVPAAEREQKAREALRQVGL-- 154
Cdd:COG0444 62 SGEILFDGEDLLKLSEKELRKIRGREIQMIFQDPmtSLNPVMTVGD--QIAEPLRihgGLSKAEARERAIELLERVGLpd 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 155 -ENYAHAWPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELIKLQAKHQRTIVFISHDLDEAMRIGD 233
Cdd:COG0444 140 pERRLDRYPHELSGGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIAD 219
|
250 260
....*....|....*....|....
gi 378980240 234 RIAIMQNGEVVQVGTPDEILNNPA 257
Cdd:COG0444 220 RVAVMYAGRIVEEGPVEELFENPR 243
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
5-316 |
4.74e-69 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 222.52 E-value: 4.74e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 5 LEIKNLYKIFGEHphrafkyiekglnkaQILektglslgvKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQ 84
Cdd:PRK09452 15 VELRGISKSFDGK---------------EVI---------SNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 85 VLIDGVDIAKMSdAELREVRrkkiaMVFQSFALMPHMSVLDNTAFGMALAGVPAAEREQKAREALRQVGLENYAHAWPDE 164
Cdd:PRK09452 71 IMLDGQDITHVP-AENRHVN-----TVFQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 165 LSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELIKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVV 244
Cdd:PRK09452 145 LSGGQQQRVAIARAVVNKPKVLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIE 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 245 QVGTPDEILNNPANDYVRTFfrgVDISQVFSAKDIARRSP----------VGLIRKTPGFGPRSALKLL----------- 303
Cdd:PRK09452 225 QDGTPREIYEEPKNLFVARF---IGEINIFDATVIERLDEqrvranvegrECNIYVNFAVEPGQKLHVLlrpedlrveei 301
|
330
....*....|....*.
gi 378980240 304 -QDEDREY--GYVIER 316
Cdd:PRK09452 302 nDDEHAEGliGYVRER 317
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1-264 |
1.61e-68 |
|
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: 216.44 E-value: 1.61e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 1 MAIklEIKNLYKIFGEHPhrafkyiekglnkaqilektglslGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEP 80
Cdd:cd03296 1 MSI--EVRNVSKRFGDFV------------------------ALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERP 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 81 TRGQVLIDGVDIAKMSdaelreVRRKKIAMVFQSFALMPHMSVLDNTAFGM----ALAGVPAAEREQKAREALRQVGLEN 156
Cdd:cd03296 55 DSGTILFGGEDATDVP------VQERNVGFVFQHYALFRHMTVFDNVAFGLrvkpRSERPPEAEIRAKVHELLKLVQLDW 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 157 YAHAWPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELIKLQAKHQRTIVFISHDLDEAMRIGDRIA 236
Cdd:cd03296 129 LADRYPAQLSGGQRQRVALARALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVV 208
|
250 260
....*....|....*....|....*...
gi 378980240 237 IMQNGEVVQVGTPDEILNNPANDYVRTF 264
Cdd:cd03296 209 VMNKGRIEQVGTPDEVYDHPASPFVYSF 236
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
5-247 |
3.00e-68 |
|
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: 215.45 E-value: 3.00e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 5 LEIKNLYKIFGEHphrafkyieKGLNKAqilektglslgVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQ 84
Cdd:cd03257 2 LEVKNLSVSFPTG---------GGSVKA-----------LDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGS 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 85 VLIDGVDIAKMSDaELREVRRKKIAMVFQ--SFALMPHMSVLDNTAFGMALAGVP--AAEREQKAREALRQVGL-ENYAH 159
Cdd:cd03257 62 IIFDGKDLLKLSR-RLRKIRRKEIQMVFQdpMSSLNPRMTIGEQIAEPLRIHGKLskKEARKEAVLLLLVGVGLpEEVLN 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 160 AWPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELIKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQ 239
Cdd:cd03257 141 RYPHELSGGQRQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMY 220
|
....*...
gi 378980240 240 NGEVVQVG 247
Cdd:cd03257 221 AGKIVEEG 228
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
59-264 |
6.45e-68 |
|
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: 217.75 E-value: 6.45e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 59 IMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAkmsdaeLREVRRKKIAMVFQSFALMPHMSVLDNTAFGMALAGVPA 138
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVT------NVPPHLRHINMVFQSYALFPHMTVEENVAFGLKMRKVPR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 139 AEREQKAREALRQVGLENYAHAWPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELIKLQAKHQRTI 218
Cdd:TIGR01187 75 AEIKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITF 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 378980240 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 |
1.33e-67 |
|
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: 213.16 E-value: 1.33e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 5 LEIKNLYKIFGEHphrafkyiekglnkaQILektglslgvKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQ 84
Cdd:cd03262 1 IEIKNLHKSFGDF---------------HVL---------KGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGT 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 85 VLIDGVDIAKmSDAELREVRrKKIAMVFQSFALMPHMSVLDNTAFG-MALAGVPAAEREQKAREALRQVGLENYAHAWPD 163
Cdd:cd03262 57 IIIDGLKLTD-DKKNINELR-QKVGMVFQQFNLFPHLTVLENITLApIKVKGMSKAEAEERALELLEKVGLADKADAYPA 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 164 ELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELIKLqAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEV 243
Cdd:cd03262 135 QLSGGQQQRVAIARALAMNPKVMLFDEPTSALDPELVGEVLDVMKDL-AEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
44-252 |
1.56e-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: 1.56e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKMSDAELREVRRKkIAMVFQSFALMPHMSV 123
Cdd:COG3638 19 LDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRRLRRR-IGMIFQQFNLVPRLSV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 124 LDN--------TAFGMALAG-VPAAEReQKAREALRQVGLENYAHAWPDELSGGMRQRVGLARALAINPDILLMDEAFSA 194
Cdd:COG3638 98 LTNvlagrlgrTSTWRSLLGlFPPEDR-ERALEALERVGLADKAYQRADQLSGGQQQRVAIARALVQEPKLILADEPVAS 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 378980240 195 LDPLIRTEMQDELIKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEI 252
Cdd:COG3638 177 LDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRVVFDGPPAEL 234
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
45-238 |
1.27e-66 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 212.41 E-value: 1.27e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 45 KDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKmSDAElREVrrkkiamVFQSFALMPHMSVL 124
Cdd:COG4525 24 QDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTG-PGAD-RGV-------VFQKDALLPWLNVL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 125 DNTAFGMALAGVPAAEREQKAREALRQVGLENYAHAWPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQ 204
Cdd:COG4525 95 DNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLLMDEPFGALDALTREQMQ 174
|
170 180 190
....*....|....*....|....*....|....
gi 378980240 205 DELIKLQAKHQRTIVFISHDLDEAMRIGDRIAIM 238
Cdd:COG4525 175 ELLLDVWQRTGKGVFLITHSVEEALFLATRLVVM 208
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
43-252 |
2.17e-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: 210.89 E-value: 2.17e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKMSDAELREVRRKkIAMVFQSFALMPHMS 122
Cdd:cd03256 16 ALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLRRQ-IGMIFQQFNLIERLS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 123 VLDNTAFGM--------ALAGVPAAEREQKAREALRQVGLENYAHAWPDELSGGMRQRVGLARALAINPDILLMDEAFSA 194
Cdd:cd03256 95 VLENVLSGRlgrrstwrSLFGLFPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIARALMQQPKLILADEPVAS 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 378980240 195 LDPLIRTEMQDELIKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEI 252
Cdd:cd03256 175 LDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAEL 232
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
5-268 |
3.37e-66 |
|
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: 210.81 E-value: 3.37e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 5 LEIKNLYKIFGEHPHRafKYIekglnkaqilektglslgVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQ 84
Cdd:COG1124 2 LEVRNLSVSYGQGGRR--VPV------------------LKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGE 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 85 VLIDGVDIAKMSDAElrevRRKKIAMVFQSF--ALMPHMSVLDNTAFGMALAGVPaaEREQKAREALRQVGL-ENYAHAW 161
Cdd:COG1124 62 VTFDGRPVTRRRRKA----FRRRVQMVFQDPyaSLHPRHTVDRILAEPLRIHGLP--DREERIAELLEQVGLpPSFLDRY 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 162 PDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELIKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNG 241
Cdd:COG1124 136 PHQLSGGQRQRVAIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNG 215
|
250 260
....*....|....*....|....*..
gi 378980240 242 EVVQVGTPDEILNNPANDYVRTFFRGV 268
Cdd:COG1124 216 RIVEELTVADLLAGPKHPYTRELLAAS 242
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
31-264 |
7.79e-65 |
|
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: 206.80 E-value: 7.79e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 31 KAQILEKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKMSDaelrevRRKKIAM 110
Cdd:cd03299 2 KVENLSKDWKEFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPP------EKRDISY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 111 VFQSFALMPHMSVLDNTAFGMALAGVPAAEREQKAREALRQVGLENYAHAWPDELSGGMRQRVGLARALAINPDILLMDE 190
Cdd:cd03299 76 VPQNYALFPHMTVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDE 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 378980240 191 AFSALDPLIRTEMQDELIKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTF 264
Cdd:cd03299 156 PFSALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPKNEFVAEF 229
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
44-252 |
1.74e-64 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 205.49 E-value: 1.74e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIE-----PTRGQVLIDGVDIAKMSDAELrEVRRKkIAMVFQSfALM 118
Cdd:cd03260 16 LKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIYDLDVDVL-ELRRR-VGMVFQK-PNP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 119 PHMSVLDNTAFGMALAGV-PAAEREQKAREALRQVGLENYAH--AWPDELSGGMRQRVGLARALAINPDILLMDEAFSAL 195
Cdd:cd03260 93 FPGSIYDNVAYGLRLHGIkLKEELDERVEEALRKAALWDEVKdrLHALGLSGGQQQRLCLARALANEPEVLLLDEPTSAL 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 378980240 196 DPlIRTEMQDELIKlQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEI 252
Cdd:cd03260 173 DP-ISTAKIEELIA-ELKKEYTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
44-262 |
3.28e-64 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 208.43 E-value: 3.28e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKMSDAELREVRRKkIAMVFQ-SFA-LMPHM 121
Cdd:COG4608 34 VDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELRPLRRR-MQMVFQdPYAsLNPRM 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 122 SVLDNTAFGMALAGV-PAAEREQKAREALRQVGL-ENYAHAWPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLI 199
Cdd:COG4608 113 TVGDIIAEPLRIHGLaSKAERRERVAELLELVGLrPEHADRYPHEFSGGQRQRIGIARALALNPKLIVCDEPVSALDVSI 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 378980240 200 RTEMQDELIKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVR 262
Cdd:COG4608 193 QAQVLNLLEDLQDELGLTYLFISHDLSVVRHISDRVAVMYLGKIVEIAPRDELYARPLHPYTQ 255
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-257 |
1.30e-63 |
|
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: 212.07 E-value: 1.30e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 1 MAIKLEIKNLYKIFGEHPHRAfkyiekglnkaqilektglslgVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEP 80
Cdd:COG1123 1 MTPLLEVRDLSVRYPGGDVPA----------------------VDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPH 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 81 T---RGQVLIDGVDIAKMSDAelreVRRKKIAMVFQSF--ALMPhMSVLDNTAFGMALAGVPAAEREQKAREALRQVGLE 155
Cdd:COG1123 59 GgriSGEVLLDGRDLLELSEA----LRGRRIGMVFQDPmtQLNP-VTVGDQIAEALENLGLSRAEARARVLELLEAVGLE 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 156 NYAHAWPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELIKLQAKHQRTIVFISHDLDEAMRIGDRI 235
Cdd:COG1123 134 RRLDRYPHQLSGGQRQRVAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRV 213
|
250 260
....*....|....*....|..
gi 378980240 236 AIMQNGEVVQVGTPDEILNNPA 257
Cdd:COG1123 214 VVMDDGRIVEDGPPEEILAAPQ 235
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
22-268 |
2.03e-63 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 203.40 E-value: 2.03e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 22 FKYIEKGLNKAQILektglslgvKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIaKMSDAELR 101
Cdd:PRK09493 4 FKNVSKHFGPTQVL---------HNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKV-NDPKVDER 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 102 EVRRKKiAMVFQSFALMPHMSVLDNTAFG-MALAGVPAAEREQKAREALRQVGLENYAHAWPDELSGGMRQRVGLARALA 180
Cdd:PRK09493 74 LIRQEA-GMVFQQFYLFPHLTALENVMFGpLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 181 INPDILLMDEAFSALDPLIRTE----MQDeliklQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNP 256
Cdd:PRK09493 153 VKPKLMLFDEPTSALDPELRHEvlkvMQD-----LAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNP 227
|
250
....*....|..
gi 378980240 257 ANDYVRTFFRGV 268
Cdd:PRK09493 228 PSQRLQEFLQHV 239
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
47-264 |
3.43e-63 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 202.29 E-value: 3.43e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 47 ASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKMSDAElrevrrKKIAMVFQSFALMPHMSVLDN 126
Cdd:COG3840 18 FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAE------RPVSMLFQENNLFPHLTVAQN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 127 TAFGMALAGVPAAEREQKAREALRQVGLENYAHAWPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDE 206
Cdd:COG3840 92 IGLGLRPGLKLTAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDPALRQEMLDL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 378980240 207 LIKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTF 264
Cdd:COG3840 172 VDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPPALAAY 229
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
5-305 |
3.72e-63 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 207.38 E-value: 3.72e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 5 LEIKNLYKIF-GEHphrafkyiekglnkaqilektglslGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRG 83
Cdd:PRK11607 20 LEIRNLTKSFdGQH-------------------------AVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 84 QVLIDGVDIAKMSDaelrevRRKKIAMVFQSFALMPHMSVLDNTAFGMALAGVPAAEREQKAREALRQVGLENYAHAWPD 163
Cdd:PRK11607 75 QIMLDGVDLSHVPP------YQRPINMMFQSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPH 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 164 ELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELIKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEV 243
Cdd:PRK11607 149 QLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKF 228
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 378980240 244 VQVGTPDEILNNPANDYVRTFFRGVDisqVFSAKdIARRSPVGLIRKTPGFgpRSALKLLQD 305
Cdd:PRK11607 229 VQIGEPEEIYEHPTTRYSAEFIGSVN---VFEGV-LKERQEDGLVIDSPGL--VHPLKVDAD 284
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
34-254 |
2.14e-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: 201.04 E-value: 2.14e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 34 ILEKTGLSLG------VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKMSDAElrevRRKK 107
Cdd:COG1120 1 MLEAENLSVGyggrpvLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRE----LARR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 108 IAMVFQSFALMPHMSVLDNTAFG----MALAGVPAAEREQKAREALRQVGLENYAHAWPDELSGGMRQRVGLARALAINP 183
Cdd:COG1120 77 IAYVPQEPPAPFGLTVRELVALGryphLGLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEP 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 378980240 184 DILLMDEAFSALDPLIRTEMQDELIKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILN 254
Cdd:COG1120 157 PLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEVLT 227
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
45-242 |
1.48e-61 |
|
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: 197.69 E-value: 1.48e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 45 KDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKMSDAELRevrrKKIAMVFQSFA---LMPhm 121
Cdd:cd03225 18 DDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELR----RKVGLVFQNPDdqfFGP-- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 122 SVLDNTAFGMALAGVPAAEREQKAREALRQVGLENYAHAWPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRT 201
Cdd:cd03225 92 TVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDPAGRR 171
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 378980240 202 EMQDELIKLQAKHQrTIVFISHDLDEAMRIGDRIAIMQNGE 242
Cdd:cd03225 172 ELLELLKKLKAEGK-TIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
43-252 |
7.75e-61 |
|
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: 196.75 E-value: 7.75e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKMSDAELREVRRKkIAMVFQSFALMPHMS 122
Cdd:TIGR02315 17 ALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKLRKLRRR-IGMIFQHYNLIERLT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 123 VLDNTAFG---------MALAGVPAAEREqKAREALRQVGLENYAHAWPDELSGGMRQRVGLARALAINPDILLMDEAFS 193
Cdd:TIGR02315 96 VLENVLHGrlgykptwrSLLGRFSEEDKE-RALSALERVGLADKAYQRADQLSGGQQQRVAIARALAQQPDLILADEPIA 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 378980240 194 ALDPLIRTEMQDELIKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEI 252
Cdd:TIGR02315 175 SLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSEL 233
|
|
| ABC_arch_GlcV |
NF040933 |
glucose ABC transporter ATP-binding protein GlcV; |
7-265 |
1.26e-60 |
|
glucose ABC transporter ATP-binding protein GlcV;
Pssm-ID: 468866 [Multi-domain] Cd Length: 357 Bit Score: 199.84 E-value: 1.26e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 7 IKNLYKIFGEhphrafkyiEKGLNKAqilektglslgVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVL 86
Cdd:NF040933 5 VENVTKIFKK---------GKKEVVA-----------LDNVNLEIKSGEFFGILGPSGHGKTTFLRIIAGLEVPTDGEIY 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 87 IDGVDIAKmSDAELREVRRKKIAMVFQSFALMPHMSVLDNTAFGMALAGVPAAEREQKAREALRQVGLENYAHAWPDELS 166
Cdd:NF040933 65 FDDKLVAS-PGKIIVPPEDRNIGMVFQNWALYPNMTVFDNIAFPLKIKKVPKDEIEKKVKEVAEILGISEVLDRYPRELS 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 167 GGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELIKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQV 246
Cdd:NF040933 144 GGQQQRVALARALVKNPQVLLLDEPFSNLDARIRDSARALVKKIQRELKITTIIVSHDPADIFSLADRAGVINNGKFQQV 223
|
250
....*....|....*....
gi 378980240 247 GTPDEILNNPANDYVRTFF 265
Cdd:NF040933 224 GKPEEIYDNPANIFVARLI 242
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
25-264 |
3.18e-60 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 198.77 E-value: 3.18e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 25 IEKGLNKAQILektglslgvKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKMSdaelreVR 104
Cdd:PRK10851 8 IKKSFGRTQVL---------NDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLH------AR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 105 RKKIAMVFQSFALMPHMSVLDNTAFGMALagVPAAER------EQKAREALRQVGLENYAHAWPDELSGGMRQRVGLARA 178
Cdd:PRK10851 73 DRKVGFVFQHYALFRHMTVFDNIAFGLTV--LPRRERpnaaaiKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 179 LAINPDILLMDEAFSALDPLIRTEMQDELIKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPAN 258
Cdd:PRK10851 151 LAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREPAT 230
|
....*.
gi 378980240 259 DYVRTF 264
Cdd:PRK10851 231 RFVLEF 236
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
44-247 |
5.48e-60 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 193.73 E-value: 5.48e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKMSDAELREVRRKkIAMVFQSFALMPHMSV 123
Cdd:COG2884 18 LSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYLRRR-IGVVFQDFRLLPDRTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 124 LDNTAFGMALAGVPAAEREQKAREALRQVGLENYAHAWPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPlirtEM 203
Cdd:COG2884 97 YENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLLADEPTGNLDP----ET 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 378980240 204 QDELIKL-QAKHQR--TIVFISHDLDEAMRIGDRIAIMQNGEVVQVG 247
Cdd:COG2884 173 SWEIMELlEEINRRgtTVLIATHDLELVDRMPKRVLELEDGRLVRDE 219
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
44-255 |
1.57e-59 |
|
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: 194.19 E-value: 1.57e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIakMSDAELREVRRKkIAMVFQSfalmPH--- 120
Cdd:TIGR04520 18 LKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDT--LDEENLWEIRKK-VGMVFQN----PDnqf 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 121 --MSVLDNTAFGMALAGVPAAEREQKAREALRQVGLENYAHAWPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPL 198
Cdd:TIGR04520 91 vgATVEDDVAFGLENLGVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLAMRPDIIILDEATSMLDPK 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 378980240 199 IRTEMQDELIKLQAKHQRTIVFISHDLDEAMRiGDRIAIMQNGEVVQVGTPDEILNN 255
Cdd:TIGR04520 171 GRKEVLETIRKLNKEEGITVISITHDMEEAVL-ADRVIVMNKGKIVAEGTPREIFSQ 226
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
44-263 |
1.95e-59 |
|
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: 201.45 E-value: 1.95e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIePTRGQVLIDGVDIAKMSDAELREVRRKkIAMVFQS-FA-LMPHM 121
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLI-PSEGEIRFDGQDLDGLSRRALRPLRRR-MQVVFQDpFGsLSPRM 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 122 SVLDNTAFGMAL--AGVPAAEREQKAREALRQVGL-ENYAHAWPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPL 198
Cdd:COG4172 380 TVGQIIAEGLRVhgPGLSAAERRARVAEALEEVGLdPAARHRYPHEFSGGQRQRIAIARALILEPKLLVLDEPTSALDVS 459
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 378980240 199 IRTEMQDELIKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRT 263
Cdd:COG4172 460 VQAQILDLLRDLQREHGLAYLFISHDLAVVRALAHRVMVMKDGKVVEQGPTEQVFDAPQHPYTRA 524
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
44-264 |
1.37e-58 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 194.55 E-value: 1.37e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKmsdaelREVRRKKIAMVFQSFALMPHMSV 123
Cdd:PRK11432 22 IDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTH------RSIQQRDICMVFQSYALFPHMSL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 124 LDNTAFGMALAGVPAAEREQKAREALRQVGLENYAHAWPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEM 203
Cdd:PRK11432 96 GENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSM 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 378980240 204 QDELIKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTF 264
Cdd:PRK11432 176 REKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPASRFMASF 236
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
44-261 |
2.73e-58 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 190.63 E-value: 2.73e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIE--P---TRGQVLIDGVDI--AKMSDAELRevrrKKIAMVFQS-- 114
Cdd:COG1117 27 LKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDliPgarVEGEILLDGEDIydPDVDVVELR----RRVGMVFQKpn 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 115 -FAlmphMSVLDNTAFGMALAGV-PAAEREQKAREALRQVGLenyahaWpDE-----------LSGGMRQRVGLARALAI 181
Cdd:COG1117 103 pFP----KSIYDNVAYGLRLHGIkSKSELDEIVEESLRKAAL------W-DEvkdrlkksalgLSGGQQQRLCIARALAV 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 182 NPDILLMDEAFSALDPlIRTEMQDELIkLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPAN--- 258
Cdd:COG1117 172 EPEVLLMDEPTSALDP-ISTAKIEELI-LELKKDYTIVIVTHNMQQAARVSDYTAFFYLGELVEFGPTEQIFTNPKDkrt 249
|
....
gi 378980240 259 -DYV 261
Cdd:COG1117 250 eDYI 253
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
45-264 |
4.04e-57 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 191.01 E-value: 4.04e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 45 KDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGvdiAKMSDAELREvrrKKIAMVFQSFALMPHMSVL 124
Cdd:PRK11000 20 KDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGE---KRMNDVPPAE---RGVGMVFQSYALYPHLSVA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 125 DNTAFGMALAGVPAAEREQKAREALRQVGLENYAHAWPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQ 204
Cdd:PRK11000 94 ENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRVQMR 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 205 DELIKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTF 264
Cdd:PRK11000 174 IEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPANRFVAGF 233
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
5-257 |
1.11e-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: 186.40 E-value: 1.11e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 5 LEIKNLYKIFGehphrafkyiekGLnKAqilektglslgVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQ 84
Cdd:COG0411 5 LEVRGLTKRFG------------GL-VA-----------VDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGR 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 85 VLIDGVDIAKMSDaelREVRRKKIAMVFQSFALMPHMSVLDN----------TAFGMALAGVPAAERE-----QKAREAL 149
Cdd:COG0411 61 ILFDGRDITGLPP---HRIARLGIARTFQNPRLFPELTVLENvlvaaharlgRGLLAALLRLPRARREerearERAEELL 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 150 RQVGLENYAHAWPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELIKLQAKHQRTIVFISHDLDEAM 229
Cdd:COG0411 138 ERVGLADRADEPAGNLSYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVM 217
|
250 260
....*....|....*....|....*...
gi 378980240 230 RIGDRIAIMQNGEVVQVGTPDEILNNPA 257
Cdd:COG0411 218 GLADRIVVLDFGRVIAEGTPAEVRADPR 245
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
5-265 |
5.74e-56 |
|
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: 184.29 E-value: 5.74e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 5 LEIKNLYKIFGEHPhrafkyiekglnkaqilektglslGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQ 84
Cdd:COG4555 2 IEVENLSKKYGKVP------------------------ALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGS 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 85 VLIDGVDIAKMSDAelrevRRKKIAMVFQSFALMPHMSVLDNTAFGMALAGVPAAEREQKAREALRQVGLENYAHAWPDE 164
Cdd:COG4555 58 ILIDGEDVRKEPRE-----ARRQIGVLPDERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGE 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 165 LSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELIKLqAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVV 244
Cdd:COG4555 133 LSTGMKKKVALARALVHDPKVLLLDEPTNGLDVMARRLLREILRAL-KKEGKTVLFSSHIMQEVEALCDRVVILHKGKVV 211
|
250 260
....*....|....*....|.
gi 378980240 245 QVGTPDEILNNPANDYVRTFF 265
Cdd:COG4555 212 AQGSLDELREEIGEENLEDAF 232
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
5-262 |
6.62e-56 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 184.66 E-value: 6.62e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 5 LEIKNLYKIFGEHphrafkyieKGLNKAQILEktglslGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQ 84
Cdd:COG4167 5 LEVRNLSKTFKYR---------TGLFRRQQFE------AVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 85 VLIDGVDIAKMSDAelreVRRKKIAMVFQ--SFALMPHMSV---LD-----NTAFgmalagvPAAEREQKAREALRQVGL 154
Cdd:COG4167 70 ILINGHKLEYGDYK----YRCKHIRMIFQdpNTSLNPRLNIgqiLEeplrlNTDL-------TAEEREERIFATLRLVGL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 155 -ENYAHAWPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELIKLQAKHQRTIVFISHDLDEAMRIGD 233
Cdd:COG4167 139 lPEHANFYPHMLSSGQKQRVALARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKHISD 218
|
250 260
....*....|....*....|....*....
gi 378980240 234 RIAIMQNGEVVQVGTPDEILNNPANDYVR 262
Cdd:COG4167 219 KVLVMHQGEVVEYGKTAEVFANPQHEVTK 247
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
44-293 |
1.93e-54 |
|
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: 188.35 E-value: 1.93e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 44 VKDASLAIEEGEIFVIMGLSGSGKS----TMVRLLNRLIEPTRGQVLIDGVDIAKMSDAELREVRRKKIAMVFQ--SFAL 117
Cdd:COG4172 26 VKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERELRRIRGNRIAMIFQepMTSL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 118 MPHMSVLDNTAFGMAL-AGVPAAEREQKAREALRQVGL---ENYAHAWPDELSGGMRQRVGLARALAINPDILLMDEAFS 193
Cdd:COG4172 106 NPLHTIGKQIAEVLRLhRGLSGAAARARALELLERVGIpdpERRLDAYPHQLSGGQRQRVMIAMALANEPDLLIADEPTT 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 194 ALDPLIRTEMQDELIKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFF-------- 265
Cdd:COG4172 186 ALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFADRVAVMRQGEIVEQGPTAELFAAPQHPYTRKLLaaeprgdp 265
|
250 260 270
....*....|....*....|....*....|..
gi 378980240 266 RGVDISQ--VFSAKDIARRSPV--GLIRKTPG 293
Cdd:COG4172 266 RPVPPDAppLLEARDLKVWFPIkrGLFRRTVG 297
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
5-257 |
2.60e-54 |
|
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: 179.56 E-value: 2.60e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 5 LEIKNLYKIFGehphrafkyiekGLnKAqilektglslgVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQ 84
Cdd:cd03219 1 LEVRGLTKRFG------------GL-VA-----------LDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGS 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 85 VLIDGVDIAKMSDaelREVRRKKIAMVFQSFALMPHMSVLDN--------TAFGMALAGVPAAERE--QKAREALRQVGL 154
Cdd:cd03219 57 VLFDGEDITGLPP---HEIARLGIGRTFQIPRLFPELTVLENvmvaaqarTGSGLLLARARREEREarERAEELLERVGL 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 155 ENYAHAWPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMqDELIKLQAKHQRTIVFISHDLDEAMRIGDR 234
Cdd:cd03219 134 ADLADRPAGELSYGQQRRLEIARALATDPKLLLLDEPAAGLNPEETEEL-AELIRELRERGITVLLVEHDMDVVMSLADR 212
|
250 260
....*....|....*....|...
gi 378980240 235 IAIMQNGEVVQVGTPDEILNNPA 257
Cdd:cd03219 213 VTVLDQGRVIAEGTPDEVRNNPR 235
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
44-264 |
1.85e-52 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 178.50 E-value: 1.85e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKMSDAElrevrrKKIAMVFQSFALMPHMSV 123
Cdd:PRK11650 20 IKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPAD------RDIAMVFQNYALYPHMSV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 124 LDNTAFGMALAGVPAAEREQKAREALRQVGLENYAHAWPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEM 203
Cdd:PRK11650 94 RENMAYGLKIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDAKLRVQM 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 378980240 204 QDELIKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTF 264
Cdd:PRK11650 174 RLEIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGGVAEQIGTPVEVYEKPASTFVASF 234
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
44-252 |
3.85e-52 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 175.59 E-value: 3.85e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVdiaKMSDAELREVRRKkIAMVFQSfalmPH--- 120
Cdd:PRK13635 23 LKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGM---VLSEETVWDVRRQ-VGMVFQN----PDnqf 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 121 --MSVLDNTAFGMALAGVPAAEREQKAREALRQVGLENYAHAWPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPL 198
Cdd:PRK13635 95 vgATVQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPR 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 378980240 199 IRTEMQDELIKLQAKHQRTIVFISHDLDEAMRiGDRIAIMQNGEVVQVGTPDEI 252
Cdd:PRK13635 175 GRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEI 227
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
5-243 |
4.16e-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: 171.81 E-value: 4.16e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 5 LEIKNLYKIFGEHPhrafkyiekglnkaqilektglslGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQ 84
Cdd:cd03230 1 IEVRNLSKRYGKKT------------------------ALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGE 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 85 VLIDGVDIAKmsdaELREVRRKkIAMVFQSFALMPHMSVLDNTafgmalagvpaaereqkarealrqvglenyahawpdE 164
Cdd:cd03230 57 IKVLGKDIKK----EPEEVKRR-IGYLPEEPSLYENLTVRENL------------------------------------K 95
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 378980240 165 LSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELIKLqAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEV 243
Cdd:cd03230 96 LSGGMKQRLALAQALLHDPELLILDEPTSGLDPESRREFWELLREL-KKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
45-243 |
1.15e-51 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 171.92 E-value: 1.15e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 45 KDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKMSDAELrevrRKKIAMVFQSFALMPhMSVL 124
Cdd:COG4619 17 SPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEW----RRQVAYVPQEPALWG-GTVR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 125 DNTAFGMALAGVPAaeREQKAREALRQVGLENYAHAWP-DELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEM 203
Cdd:COG4619 92 DNLPFPFQLRERKF--DRERALELLERLGLPPDILDKPvERLSGGERQRLALIRALLLQPDVLLLDEPTSALDPENTRRV 169
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 378980240 204 QDELIKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEV 243
Cdd:COG4619 170 EELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| CBS_pair_ABC_Gly_Pro_assoc |
cd09831 |
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found associated with ... |
278-393 |
2.54e-51 |
|
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: 167.74 E-value: 2.54e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 278 DIARRSPVGLIRKTpGFGPRSALKLLQDEDREYGYVIERGNRFVGIVSIDSLKTALSAG-QGIEAALIDAPLAVEAQTPL 356
Cdd:cd09831 1 DIARKTQVTVIEKT-GDGPRAALQLLREHDREYGYVVDKKRRFLGVVSVDSLRAALKENaQSLEDAFLTDVETVPADTSL 79
|
90 100 110
....*....|....*....|....*....|....*..
gi 378980240 357 SDLLSHVGHAPCAVPVVDEEQQYIGIISKRMLLQALD 393
Cdd:cd09831 80 SDILGLVASAPCPLPVVDEDGRYLGVISKASLLETLD 116
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
46-229 |
5.88e-51 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 171.81 E-value: 5.88e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 46 DASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKMSdAElREVrrkkiamVFQSFALMPHMSVLD 125
Cdd:PRK11248 19 DINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPG-AE-RGV-------VFQNEGLLPWRNVQD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 126 NTAFGMALAGVPAAEREQKAREALRQVGLENYAHAWPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQD 205
Cdd:PRK11248 90 NVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQMQT 169
|
170 180
....*....|....*....|....
gi 378980240 206 ELIKLQAKHQRTIVFISHDLDEAM 229
Cdd:PRK11248 170 LLLKLWQETGKQVLLITHDIEEAV 193
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
45-251 |
1.18e-50 |
|
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: 169.92 E-value: 1.18e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 45 KDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKMSDAELREVRRKKIAMVFQSFALMPHMSVL 124
Cdd:COG4181 29 KGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDARARLRARHVGFVFQSFQLLPTLTAL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 125 DNTAFGMALAGVPAAerEQKAREALRQVGLENYAHAWPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQ 204
Cdd:COG4181 109 ENVMLPLELAGRRDA--RARARALLERVGLGHRLDHYPAQLSGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQII 186
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 378980240 205 DELIKLQAKHQRTIVFISHDLDEAMRIgDRIAIMQNGEVVQVGTPDE 251
Cdd:COG4181 187 DLLFELNRERGTTLVLVTHDPALAARC-DRVLRLRAGRLVEDTAATA 232
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
44-255 |
1.85e-50 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 178.43 E-value: 1.85e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKMSDAELrevrRKKIAMVFQSFALMpHMSV 123
Cdd:COG1132 356 LKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESL----RRQIGVVPQDTFLF-SGTI 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 124 LDNTAFGMalagvPAAEREQkAREALRQVGLENYAHAWPD-----------ELSGGMRQRVGLARALAINPDILLMDEAF 192
Cdd:COG1132 431 RENIRYGR-----PDATDEE-VEEAAKAAQAHEFIEALPDgydtvvgergvNLSGGQRQRIAIARALLKDPPILILDEAT 504
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 378980240 193 SALDPliRTEM--QDELIKLqaKHQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEILNN 255
Cdd:COG1132 505 SALDT--ETEAliQEALERL--MKGRTTIVIAHRL-STIRNADRILVLDDGRIVEQGTHEELLAR 564
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
53-247 |
2.97e-50 |
|
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: 168.24 E-value: 2.97e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 53 EGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKMSDAELREVRRKKIAMVFQSFALMPHMSVLDNTAFGma 132
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRKKINLPPQQRKIGLVFQQYALFPHLNVRENLAFG-- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 133 LAGVPAAEREQKAREALRQVGLENYAHAWPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELIKLQA 212
Cdd:cd03297 100 LKRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELKQIKK 179
|
170 180 190
....*....|....*....|....*....|....*
gi 378980240 213 KHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVG 247
Cdd:cd03297 180 NLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
44-254 |
3.63e-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: 179.64 E-value: 3.63e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKMSDAELrevrRKKIAMVFQSFALMpHMSV 123
Cdd:COG2274 491 LDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASL----RRQIGVVLQDVFLF-SGTI 565
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 124 LDNTAFGMalagvPAAEREQkAREALRQVGLENYAHAWPD-----------ELSGGMRQRVGLARALAINPDILLMDEAF 192
Cdd:COG2274 566 RENITLGD-----PDATDEE-IIEAARLAGLHDFIEALPMgydtvvgeggsNLSGGQRQRLAIARALLRNPRILILDEAT 639
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 378980240 193 SALDPliRTEMQ-DELIKlQAKHQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEILN 254
Cdd:COG2274 640 SALDA--ETEAIiLENLR-RLLKGRTVIIIAHRL-STIRLADRIIVLDKGRIVEDGTHEELLA 698
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
5-252 |
4.51e-50 |
|
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: 168.07 E-value: 4.51e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 5 LEIKNLYKIFGEHPHRAfkyiekglnkaqilektglslgVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQ 84
Cdd:cd03263 1 LQIRNLTKTYKKGTKPA----------------------VDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGT 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 85 VLIDGVDIAKmsdaELREVRRKkIAMVFQSFALMPHMSVLDNTAFGMALAGVPAAEREQKAREALRQVGLENYAHAWPDE 164
Cdd:cd03263 59 AYINGYSIRT----DRKAARQS-LGYCPQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRART 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 165 LSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELIKLqaKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVV 244
Cdd:cd03263 134 LSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPASRRAIWDLILEV--RKGRSIILTTHSMDEAEALCDRIAIMSDGKLR 211
|
....*...
gi 378980240 245 QVGTPDEI 252
Cdd:cd03263 212 CIGSPQEL 219
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
44-256 |
5.25e-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: 5.25e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKMSDAELrevrrkkiaMVFQSFALMPHMSV 123
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRM---------VVFQNYSLLPWLTV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 124 LDNTAFGM--ALAGVPAAEREQKAREALRQVGLENYAHAWPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRT 201
Cdd:TIGR01184 72 RENIALAVdrVLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRG 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 378980240 202 EMQDELIKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGtpdEILNNP 256
Cdd:TIGR01184 152 NLQEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAANIG---QILEVP 203
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
44-254 |
1.09e-49 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 167.96 E-value: 1.09e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKmsdaelrevRRKKIAMVFQSFALMPH--M 121
Cdd:COG1121 22 LEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRR---------ARRRIGYVPQRAEVDWDfpI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 122 SVLDNTAFG----MALAGVPAAEREQKAREALRQVGLENYAHAWPDELSGGMRQRVGLARALAINPDILLMDEAFSALDP 197
Cdd:COG1121 93 TVRDVVLMGrygrRGLFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDA 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 198 lirtEMQDELIKL---QAKHQRTIVFISHDLDEAMRIGDRIAIMqNGEVVQVGTPDEILN 254
Cdd:COG1121 173 ----ATEEALYELlreLRREGKTILVVTHDLGAVREYFDRVLLL-NRGLVAHGPPEEVLT 227
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
34-252 |
1.48e-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: 1.48e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 34 ILEKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKmsdaELREVRRKkIAMVFQ 113
Cdd:cd03265 6 LVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR----EPREVRRR-IGIVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 114 SFALMPHMSVLDNTAFGMALAGVPAAEREQKAREALRQVGLENYAHAWPDELSGGMRQRVGLARALAINPDILLMDEAFS 193
Cdd:cd03265 81 DLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTI 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 378980240 194 ALDPLIRTEMQDELIKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEI 252
Cdd:cd03265 161 GLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
35-247 |
5.36e-49 |
|
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: 164.97 E-value: 5.36e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 35 LEKTGLSLGVK--DASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKMsdaelrEVRRKKIAMVF 112
Cdd:cd03298 3 LDKIRFSYGEQpmHFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAA------PPADRPVSMLF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 113 QSFALMPHMSVLDNTAFGMALAGVPAAEREQKAREALRQVGLENYAHAWPDELSGGMRQRVGLARALAINPDILLMDEAF 192
Cdd:cd03298 77 QENNLFAHLTVEQNVGLGLSPGLKLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPF 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 378980240 193 SALDPLIRTEMQDELIKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVG 247
Cdd:cd03298 157 AALDPALRAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
46-289 |
9.37e-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: 168.74 E-value: 9.37e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 46 DASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDG---VDIAKMSDaelREVRRKKIAMVFQSFALMPHMS 122
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGevlQDSARGIF---LPPHRRRIGYVFQEARLFPHLS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 123 VLDNTAFGMALAgvPAAEREQKAREALRQVGLENYAHAWPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTE 202
Cdd:COG4148 94 VRGNLLYGRKRA--PRAERRISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAE 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 203 MQDELIKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPAndyVRTFFRGVDISQVFSAKDIARR 282
Cdd:COG4148 172 ILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRPD---LLPLAGGEEAGSVLEATVAAHD 248
|
....*..
gi 378980240 283 SPVGLIR 289
Cdd:COG4148 249 PDYGLTR 255
|
|
| ectoine_ehuA |
TIGR03005 |
ectoine/hydroxyectoine ABC transporter, ATP-binding protein; Members of this family are the ... |
47-268 |
4.92e-48 |
|
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: 163.85 E-value: 4.92e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 47 ASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKMSD-------AELREVR--RKKIAMVFQSFAL 117
Cdd:TIGR03005 19 LNFSVAAGEKVALIGPSGSGKSTILRILMTLEPIDEGQIQVEGEQLYHMPGrngplvpADEKHLRqmRNKIGMVFQSFNL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 118 MPHMSVLDN-TAFGMALAGVPAAEREQKAREALRQVGLENYAHAWPDELSGGMRQRVGLARALAINPDILLMDEAFSALD 196
Cdd:TIGR03005 99 FPHKTVLDNvTEAPVLVLGMARAEAEKRAMELLDMVGLADKADHMPAQLSGGQQQRVAIARALAMRPKVMLFDEVTSALD 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 378980240 197 PLIRTEMQDELIKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFFRGV 268
Cdd:TIGR03005 179 PELVGEVLNVIRRLASEHDLTMLLVTHEMGFAREFADRVCFFDKGRIVEQGKPDEIFRQPKEERTREFLSKV 250
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
1-256 |
1.75e-47 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 162.10 E-value: 1.75e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 1 MAIKLeiKNLYKIFGEHphrafkyiekglnkaQILektglslgvKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEP 80
Cdd:COG4161 1 MSIQL--KNINCFYGSH---------------QAL---------FDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETP 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 81 TRGQVLIDGVDI---AKMSDAELREVRRKkIAMVFQSFALMPHMSVLDN-TAFGMALAGVPAAEREQKAREALRQVGLEN 156
Cdd:COG4161 55 DSGQLNIAGHQFdfsQKPSEKAIRLLRQK-VGMVFQQYNLWPHLTVMENlIEAPCKVLGLSKEQAREKAMKLLARLRLTD 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 157 YAHAWPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQdELIKLQAKHQRTIVFISHDLDEAMRIGDRIA 236
Cdd:COG4161 134 KADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQVV-EIIRELSQTGITQVIVTHEVEFARKVASQVV 212
|
250 260
....*....|....*....|
gi 378980240 237 IMQNGEVVQVGTPdEILNNP 256
Cdd:COG4161 213 YMEKGRIIEQGDA-SHFTQP 231
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
44-255 |
1.77e-47 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 162.85 E-value: 1.77e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIakmSDAELREVRrKKIAMVFQSfalmPH--- 120
Cdd:PRK13632 25 LKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITI---SKENLKEIR-KKIGIIFQN----PDnqf 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 121 --MSVLDNTAFGMALAGVPAAEREQKAREALRQVGLENYAHAWPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPL 198
Cdd:PRK13632 97 igATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFDESTSMLDPK 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 378980240 199 IRTEMQDELIKLQAKHQRTIVFISHDLDEAMrIGDRIAIMQNGEVVQVGTPDEILNN 255
Cdd:PRK13632 177 GKREIKKIMVDLRKTRKKTLISITHDMDEAI-LADKVIVFSEGKLIAQGKPKEILNN 232
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
44-247 |
2.19e-46 |
|
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: 157.21 E-value: 2.19e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKMSDAElrevRRKKIAMVFQsfalmphmsv 123
Cdd:cd03214 15 LDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKE----LARKIAYVPQ---------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 124 ldntafgmalagvpaaereqkareALRQVGLENYAHAWPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEM 203
Cdd:cd03214 81 ------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQIEL 136
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 378980240 204 QDELIKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVG 247
Cdd:cd03214 137 LELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
42-257 |
9.52e-46 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 159.03 E-value: 9.52e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 42 LGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLI-DGVDIAKMSDAELREVRrKKIAMVFQsFAlmPH 120
Cdd:PRK13634 21 RALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIgERVITAGKKNKKLKPLR-KKVGIVFQ-FP--EH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 121 M----SVLDNTAFGMALAGVPAAEREQKAREALRQVGL-ENYAHAWPDELSGGMRQRVGLARALAINPDILLMDEAFSAL 195
Cdd:PRK13634 97 QlfeeTVEKDICFGPMNFGVSEEDAKQKAREMIELVGLpEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 378980240 196 DPLIRTEMQDELIKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPA 257
Cdd:PRK13634 177 DPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADPD 238
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
44-247 |
1.44e-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: 1.44e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKMsdaelrevrRKKIAMVFQSFAL---MPh 120
Cdd:cd03235 15 LEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKE---------RKRIGYVPQRRSIdrdFP- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 121 MSVLDNTAFG----MALAGVPAAEREQKAREALRQVGLENYAHAWPDELSGGMRQRVGLARALAINPDILLMDEAFSALD 196
Cdd:cd03235 85 ISVRDVVLMGlyghKGLFRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAGVD 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 378980240 197 PLIRTEMQDELIKLQAKhQRTIVFISHDLDEAMRIGDRIAIMqNGEVVQVG 247
Cdd:cd03235 165 PKTQEDIYELLRELRRE-GMTILVVTHDLGLVLEYFDRVLLL-NRTVVASG 213
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1-255 |
3.66e-45 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 157.52 E-value: 3.66e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 1 MAIKleIKNLYKIFgehphrafkyiekglNKAQILEKTGLslgvKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEP 80
Cdd:PRK13637 1 MSIK--IENLTHIY---------------MEGTPFEKKAL----DNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKP 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 81 TRGQVLIDGVDIAKMSdAELREVRrKKIAMVFQsfalMPHMSVLDNT-----AFGMALAGVPAAEREQKAREALRQVGL- 154
Cdd:PRK13637 60 TSGKIIIDGVDITDKK-VKLSDIR-KKVGLVFQ----YPEYQLFEETiekdiAFGPINLGLSEEEIENRVKRAMNIVGLd 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 155 -ENYAHAWPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELIKLQAKHQRTIVFISHDLDEAMRIGD 233
Cdd:PRK13637 134 yEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLAD 213
|
250 260
....*....|....*....|..
gi 378980240 234 RIAIMQNGEVVQVGTPDEILNN 255
Cdd:PRK13637 214 RIIVMNKGKCELQGTPREVFKE 235
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
44-193 |
4.97e-45 |
|
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: 152.42 E-value: 4.97e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKMSdaelREVRRKKIAMVFQSFALMPHMSV 123
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDE----RKSLRKEIGYVFQDPQLFPRLTV 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 378980240 124 LDNTAFGMALAGVPAAEREQKAREALRQVGLENYAH----AWPDELSGGMRQRVGLARALAINPDILLMDEAFS 193
Cdd:pfam00005 77 RENLRLGLLLKGLSKREKDARAEEALEKLGLGDLADrpvgERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
49-266 |
5.44e-45 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 156.06 E-value: 5.44e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 49 LAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDI--AKMSDAELREVR--RKKIAMVFQSFALMPHMSVL 124
Cdd:PRK11264 24 LEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIdtARSLSQQKGLIRqlRQHVGFVFQNFNLFPHRTVL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 125 DNTAFG-MALAGVPAAEREQKAREALRQVGLENYAHAWPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEM 203
Cdd:PRK11264 104 ENIIEGpVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPEVILFDEPTSALDPELVGEV 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 378980240 204 QDElIKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFFR 266
Cdd:PRK11264 184 LNT-IRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADPQQPRTRQFLE 245
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
44-242 |
5.64e-45 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 153.31 E-value: 5.64e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKMSDAELrevrRKKIAMVFQSFALMpHMSV 123
Cdd:cd03228 18 LKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESL----RKNIAYVPQDPFLF-SGTI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 124 LDNTafgmalagvpaaereqkarealrqvglenyahawpdeLSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEM 203
Cdd:cd03228 93 RENI-------------------------------------LSGGQRQRIAIARALLRDPPILILDEATSALDPETEALI 135
|
170 180 190
....*....|....*....|....*....|....*....
gi 378980240 204 QDELIKLqaKHQRTIVFISHDLdEAMRIGDRIAIMQNGE 242
Cdd:cd03228 136 LEALRAL--AKGKTVIVIAHRL-STIRDADRIIVLDDGR 171
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
44-242 |
5.73e-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: 152.78 E-value: 5.73e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKMSDAELRevrrKKIAMVFQsfalmphmsv 123
Cdd:cd00267 15 LDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELR----RRIGYVPQ---------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 124 ldntafgmalagvpaaereqkarealrqvglenyahawpdeLSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEM 203
Cdd:cd00267 81 -----------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERL 119
|
170 180 190
....*....|....*....|....*....|....*....
gi 378980240 204 QDELIKLqAKHQRTIVFISHDLDEAMRIGDRIAIMQNGE 242
Cdd:cd00267 120 LELLREL-AEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
44-267 |
6.54e-45 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 155.84 E-value: 6.54e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIE-----PTRGQVLIDGVDIAKMSDAELRevrrKKIAMVFQSFALM 118
Cdd:PRK14247 19 LDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElypeaRVSGEVYLDGQDIFKMDVIELR----RRVQMVFQIPNPI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 119 PHMSVLDNTAFGMALAGVPAAERE--QKAREALRQVGL----ENYAHAWPDELSGGMRQRVGLARALAINPDILLMDEAF 192
Cdd:PRK14247 95 PNLSIFENVALGLKLNRLVKSKKElqERVRWALEKAQLwdevKDRLDAPAGKLSGGQQQRLCIARALAFQPEVLLADEPT 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 378980240 193 SALDPlIRTEMQDELIkLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFFRG 267
Cdd:PRK14247 175 ANLDP-ENTAKIESLF-LELKKDMTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTNPRHELTEKYVTG 247
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
46-250 |
7.95e-45 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 155.17 E-value: 7.95e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 46 DASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDG--VDIAKMSDA-ELREVRRKkIAMVFQSFALMPHMS 122
Cdd:PRK11124 20 DITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGnhFDFSKTPSDkAIRELRRN-VGMVFQQYNLWPHLT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 123 VLDN-TAFGMALAGVPAAEREQKAREALRQVGLENYAHAWPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRT 201
Cdd:PRK11124 99 VQQNlIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITA 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 378980240 202 EMQDeLIKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPD 250
Cdd:PRK11124 179 QIVS-IIRELAETGITQVIVTHEVEVARKTASRVVYMENGHIVEQGDAS 226
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
25-262 |
5.83e-44 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 155.51 E-value: 5.83e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 25 IEKGLNKAQILEKtglslGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNrLIE-PTRGQVLIDGVDIAKmSDAELREV 103
Cdd:PRK11308 17 VKRGLFKPERLVK-----ALDGVSFTLERGKTLAVVGESGCGKSTLARLLT-MIEtPTGGELYYQGQDLLK-ADPEAQKL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 104 RRKKIAMVFQS-FA-LMPHMSV--------LDNTAFGmalagvpAAEREQKAREALRQVGL--ENYaHAWPDELSGGMRQ 171
Cdd:PRK11308 90 LRQKIQIVFQNpYGsLNPRKKVgqileeplLINTSLS-------AAERREKALAMMAKVGLrpEHY-DRYPHMFSGGQRQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 172 RVGLARALAINPDILLMDEAFSALDPLIRTEMQDELIKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDE 251
Cdd:PRK11308 162 RIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQ 241
|
250
....*....|.
gi 378980240 252 ILNNPANDYVR 262
Cdd:PRK11308 242 IFNNPRHPYTQ 252
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
46-243 |
7.73e-44 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 151.79 E-value: 7.73e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 46 DASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKMSDAELREVRRKkIAMVFQSFALMPHMSVLD 125
Cdd:cd03292 19 GINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYLRRK-IGVVFQDFRLLPDRNVYE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 126 NTAFGMALAGVPAAEREQKAREALRQVGLENYAHAWPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQD 205
Cdd:cd03292 98 NVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTTWEIMN 177
|
170 180 190
....*....|....*....|....*....|....*...
gi 378980240 206 eLIKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEV 243
Cdd:cd03292 178 -LLKKINKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
44-252 |
3.20e-43 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 152.19 E-value: 3.20e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGvdiAKMSDAELREVRRKkIAMVFQSfalmPH--- 120
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDG---DLLTEENVWDIRHK-IGMVFQN----PDnqf 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 121 --MSVLDNTAFGMALAGVPAAEREQKAREALRQVGLENYAHAWPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPL 198
Cdd:PRK13650 95 vgATVEDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPE 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 378980240 199 IRTEMQDELIKLQAKHQRTIVFISHDLDEaMRIGDRIAIMQNGEVVQVGTPDEI 252
Cdd:PRK13650 175 GRLELIKTIKGIRDDYQMTVISITHDLDE-VALSDRVLVMKNGQVESTSTPREL 227
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
44-270 |
4.57e-43 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 153.32 E-value: 4.57e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKMSDAELREVRrKKIAMVFQS--FALMPHM 121
Cdd:PRK15079 37 VDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRAVR-SDIQMIFQDplASLNPRM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 122 SVLDNTAFGMAL--AGVPAAEREQKAREALRQVGL-ENYAHAWPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPL 198
Cdd:PRK15079 116 TIGEIIAEPLRTyhPKLSRQEVKDRVKAMMLKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVS 195
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 378980240 199 IRTEMQDELIKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFFRGVDI 270
Cdd:PRK15079 196 IQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNPLHPYTKALMSAVPI 267
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
44-257 |
1.10e-42 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 157.24 E-value: 1.10e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKMSDAELREVrrkkIAMVFQSFALMpHMSV 123
Cdd:COG4987 351 LDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRR----IAVVPQRPHLF-DTTL 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 124 LDNTAFgmalaGVPAAEREQkAREALRQVGLENYAHAWPD-----------ELSGGMRQRVGLARALAINPDILLMDEAF 192
Cdd:COG4987 426 RENLRL-----ARPDATDEE-LWAALERVGLGDWLAALPDgldtwlgeggrRLSGGERRRLALARALLRDAPILLLDEPT 499
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 378980240 193 SALDPLIRTEMQDELikLQAKHQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEILNNPA 257
Cdd:COG4987 500 EGLDAATEQALLADL--LEALAGRTVLLITHRL-AGLERMDRILVLEDGRIVEQGTHEELLAQNG 561
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
45-243 |
1.44e-42 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 149.83 E-value: 1.44e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 45 KDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGvdiAKMSDAelrevrRKKIAMVFQSFALMPHMSVL 124
Cdd:PRK11247 29 NQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGT---APLAEA------REDTRLMFQDARLLPWKKVI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 125 DNTafGMALAGvpaaEREQKAREALRQVGLENYAHAWPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQ 204
Cdd:PRK11247 100 DNV--GLGLKG----QWRDAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRIEMQ 173
|
170 180 190
....*....|....*....|....*....|....*....
gi 378980240 205 DELIKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEV 243
Cdd:PRK11247 174 DLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
44-268 |
2.06e-42 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 149.22 E-value: 2.06e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIE-----PTRGQVLIDGVDIAKmSDAELREVRRKkIAMVFQSFALM 118
Cdd:PRK14267 20 IKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElneeaRVEGEVRLFGRNIYS-PDVDPIEVRRE-VGMVFQYPNPF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 119 PHMSVLDNTAFGMALAGV--PAAEREQKAREALRQVGL----ENYAHAWPDELSGGMRQRVGLARALAINPDILLMDEAF 192
Cdd:PRK14267 98 PHLTIYDNVAIGVKLNGLvkSKKELDERVEWALKKAALwdevKDRLNDYPSNLSGGQRQRLVIARALAMKPKILLMDEPT 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 378980240 193 SALDPlIRTEMQDELIkLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFFRGV 268
Cdd:PRK14267 178 ANIDP-VGTAKIEELL-FELKKEYTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENPEHELTEKYVTGA 251
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
48-254 |
2.32e-42 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 148.19 E-value: 2.32e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKMSDAelrevrRKKIAMVFQSFALMPHMSVLDNT 127
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPS------RRPVSMLFQENNLFSHLTVAQNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 128 AFGMALAGVPAAEREQKAREALRQVGLENYAHAWPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDEL 207
Cdd:PRK10771 93 GLGLNPGLKLNAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLV 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 378980240 208 IKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILN 254
Cdd:PRK10771 173 SQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELLS 219
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
22-273 |
4.73e-42 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 149.08 E-value: 4.73e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 22 FKYIEKGLNKAQIlektglslGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKMSDaeLR 101
Cdd:PRK13633 12 YKYESNEESTEKL--------ALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEEN--LW 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 102 EVRRKKiAMVFQSfalmPHMS-----VLDNTAFGMALAGVPAAEREQKAREALRQVGLENYAHAWPDELSGGMRQRVGLA 176
Cdd:PRK13633 82 DIRNKA-GMVFQN----PDNQivatiVEEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 177 RALAINPDILLMDEAFSALDPLIRTEMQDELIKLQAKHQRTIVFISHDLDEAMRiGDRIAIMQNGEVVQVGTPDEILNNp 256
Cdd:PRK13633 157 GILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIFKE- 234
|
250
....*....|....*...
gi 378980240 257 andyVRTFFR-GVDISQV 273
Cdd:PRK13633 235 ----VEMMKKiGLDVPQV 248
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
5-252 |
7.23e-42 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 149.10 E-value: 7.23e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 5 LEIKNLYKIFGEHphRAfkyiekglnkaqilektglslgVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQ 84
Cdd:COG4152 2 LELKGLTKRFGDK--TA----------------------VDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGE 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 85 VLIDGVDIAkmsdaelREVRRKkiamvfqsFALMPH-------MSVLDNTAFGMALAGVPAAEREQKAREALRQVGLENY 157
Cdd:COG4152 58 VLWDGEPLD-------PEDRRR--------IGYLPEerglypkMKVGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDR 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 158 AHAWPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELIKLQAKhQRTIVFISHDLDEAMRIGDRIAI 237
Cdd:COG4152 123 ANKKVEELSKGNQQKVQLIAALLHDPELLILDEPFSGLDPVNVELLKDVIRELAAK-GTTVIFSSHQMELVEELCDRIVI 201
|
250
....*....|....*
gi 378980240 238 MQNGEVVQVGTPDEI 252
Cdd:COG4152 202 INKGRKVLSGSVDEI 216
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
46-278 |
8.94e-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: 150.26 E-value: 8.94e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 46 DASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKMSDAELREVRRKKIAMVFQSFALMPHMSVLD 125
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKGIFLPPEKRRIGYVFQEARLFPHLSVRG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 126 NTAFGMALAGVPaaEREQKAREALRQVGLENYAHAWPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQD 205
Cdd:TIGR02142 95 NLRYGMKRARPS--ERRISFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILP 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 378980240 206 ELIKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFFRGVDISQVFSAKD 278
Cdd:TIGR02142 173 YLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPDLPWLAREDQGSLIEGVVAEHD 245
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
34-251 |
9.49e-42 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 146.09 E-value: 9.49e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 34 ILEKTGLSLG----VKDASLAIEEGEIFVIMGLSGSGKSTmvrLLNRLI---EP---TRGQVLIDGVDIAKMSdaelreV 103
Cdd:COG4136 3 SLENLTITLGgrplLAPLSLTVAPGEILTLMGPSGSGKST---LLAAIAgtlSPafsASGEVLLNGRRLTALP------A 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 104 RRKKIAMVFQSFALMPHMSVLDNTAFGMAlAGVPAAEREQKAREALRQVGLENYAHAWPDELSGGMRQRVGLARALAINP 183
Cdd:COG4136 74 EQRRIGILFQDDLLFPHLSVGENLAFALP-PTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEP 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 378980240 184 DILLMDEAFSALDPLIRTEMQdELIKLQAKHQRTIV-FISHDLDEAmrigdriaiMQNGEVVQVGTPDE 251
Cdd:COG4136 153 RALLLDEPFSKLDAALRAQFR-EFVFEQIRQRGIPAlLVTHDEEDA---------PAAGRVLDLGNWQH 211
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
44-255 |
1.01e-41 |
|
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: 1.01e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKMSDAELRevrrKKIAMVFQSFALmPHMSV 123
Cdd:COG4988 353 LDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWR----RQIAWVPQNPYL-FAGTI 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 124 LDNTAFGMalagvPAAEREQkAREALRQVGLENYAHAWPDE-----------LSGGMRQRVGLARALAINPDILLMDEAF 192
Cdd:COG4988 428 RENLRLGR-----PDASDEE-LEAALEAAGLDEFVAALPDGldtplgeggrgLSGGQAQRLALARALLRDAPLLLLDEPT 501
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 378980240 193 SALDPLIRTEMQDELikLQAKHQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEILNN 255
Cdd:COG4988 502 AHLDAETEAEILQAL--RRLAKGRTVILITHRL-ALLAQADRILVLDDGRIVEQGTHEELLAK 561
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
46-268 |
1.25e-41 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 147.60 E-value: 1.25e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 46 DASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKMSDAELREVRrKKIAMVFQSFALMPHMSVLD 125
Cdd:PRK11831 25 NISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTVR-KRMSMLFQSGALFTDMNVFD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 126 NTAFgmalagvPAAEREQKAREALRQ--------VGLENYAHAWPDELSGGMRQRVGLARALAINPDILLMDEAFSALDP 197
Cdd:PRK11831 104 NVAY-------PLREHTQLPAPLLHStvmmkleaVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDP 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 378980240 198 LIRTEMQDELIKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPaNDYVRTFFRGV 268
Cdd:PRK11831 177 ITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQANP-DPRVRQFLDGI 246
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
44-252 |
2.43e-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: 147.92 E-value: 2.43e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKmsdaELREVRRKkIAMVFQSFALMPHMSV 123
Cdd:TIGR01188 9 VDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVVR----EPRKVRRS-IGIVPQYASVDEDLTG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 124 LDNTAFGMALAGVPAAEREQKAREALRQVGLENYAHAWPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEM 203
Cdd:TIGR01188 84 RENLEMMGRLYGLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPRTRRAI 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 378980240 204 QDELIKLQaKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEI 252
Cdd:TIGR01188 164 WDYIRALK-EEGVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPEEL 211
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
26-267 |
6.75e-41 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 145.50 E-value: 6.75e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 26 EKGLNKAQILEKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIA---------KMS 96
Cdd:PRK10619 3 ENKLNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgqlKVA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 97 DAELREVRRKKIAMVFQSFALMPHMSVLDNTAFG-MALAGVPAAEREQKAREALRQVGLENYAHA-WPDELSGGMRQRVG 174
Cdd:PRK10619 83 DKNQLRLLRTRLTMVFQHFNLWSHMTVLENVMEApIQVLGLSKQEARERAVKYLAKVGIDERAQGkYPVHLSGGQQQRVS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 175 LARALAINPDILLMDEAFSALDPLIRTEMQDELIKLqAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILN 254
Cdd:PRK10619 163 IARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQL-AEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFG 241
|
250
....*....|...
gi 378980240 255 NPANDYVRTFFRG 267
Cdd:PRK10619 242 NPQSPRLQQFLKG 254
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
44-267 |
1.81e-40 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 144.42 E-value: 1.81e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIE------PTRGQVLIDGVDIAKMSDAELrevrRKKIAMVFQSFAL 117
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiydskiKVDGKVLYFGKDIFQIDAIKL----RKEVGMVFQQPNP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 118 MPHMSVLDNTAFGMALAGVPAAEREQK-AREALRQVGLENYAH----AWPDELSGGMRQRVGLARALAINPDILLMDEAF 192
Cdd:PRK14246 102 FPHLSIYDNIAYPLKSHGIKEKREIKKiVEECLRKVGLWKEVYdrlnSPASQLSGGQQQRLTIARALALKPKVLLMDEPT 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 378980240 193 SALDpLIRTEMQDELIKlQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFFRG 267
Cdd:PRK14246 182 SMID-IVNSQAIEKLIT-ELKNEIAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNELTEKYVIG 254
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
44-245 |
3.89e-40 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 143.67 E-value: 3.89e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKMSDAELREVRRKkIAMVFQSF--ALMPHM 121
Cdd:PRK10419 28 LNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQRKAFRRD-IQMVFQDSisAVNPRK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 122 SVLDNTAFGMA-LAGVPAAEREQKAREALRQVGL-ENYAHAWPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLI 199
Cdd:PRK10419 107 TVREIIREPLRhLLSLDKAERLARASEMLRAVDLdDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVL 186
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 378980240 200 RTEMQDELIKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQ 245
Cdd:PRK10419 187 QAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVE 232
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
5-262 |
6.28e-40 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 143.01 E-value: 6.28e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 5 LEIKNLYKifgehphrAFKYiEKGLNKAQILEktglslGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQ 84
Cdd:PRK15112 5 LEVRNLSK--------TFRY-RTGWFRRQTVE------AVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 85 VLIDGVDIAkMSDAELREVRrkkIAMVFQ--SFALMPHMSVLDNTAFGMAL-AGVPAAEREQKAREALRQVGL-ENYAHA 160
Cdd:PRK15112 70 LLIDDHPLH-FGDYSYRSQR---IRMIFQdpSTSLNPRQRISQILDFPLRLnTDLEPEQREKQIIETLRQVGLlPDHASY 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 161 WPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELIKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQN 240
Cdd:PRK15112 146 YPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQ 225
|
250 260
....*....|....*....|..
gi 378980240 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 |
7.79e-40 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 140.88 E-value: 7.79e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 5 LEIKNLYKIFGEHPhrafkyiekglnkaqilektglslGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQ 84
Cdd:cd03269 1 LEVENVTKRFGRVT------------------------ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGE 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 85 VLIDGvdiAKMSDAElrevrRKKIAMVFQSFALMPHMSVLDNTAFGMALAGVPAAEREQKAREALRQVGLENYAHAWPDE 164
Cdd:cd03269 57 VLFDG---KPLDIAA-----RNRIGYLPEERGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEE 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 165 LSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELIKLQAKhQRTIVFISHDLDEAMRIGDRIAIMQNGEVV 244
Cdd:cd03269 129 LSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVNVELLKDVIRELARA-GKTVILSTHQMELVEELCDRVLLLNKGRAV 207
|
...
gi 378980240 245 QVG 247
Cdd:cd03269 208 LYG 210
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
44-256 |
1.18e-39 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 142.63 E-value: 1.18e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEP---TRGQVLIDGVDIAKMSDAELREvrrkKIAMVFQSfalmPH 120
Cdd:PRK13640 23 LNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPddnPNSKITVDGITLTAKTVWDIRE----KVGIVFQN----PD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 121 -----MSVLDNTAFGMALAGVPAAEREQKAREALRQVGLENYAHAWPDELSGGMRQRVGLARALAINPDILLMDEAFSAL 195
Cdd:PRK13640 95 nqfvgATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSML 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 378980240 196 DPLIRTEMQDELIKLQAKHQRTIVFISHDLDEAmRIGDRIAIMQNGEVVQVGTPDEILNNP 256
Cdd:PRK13640 175 DPAGKEQILKLIRKLKKKNNLTVISITHDIDEA-NMADQVLVLDDGKLLAQGSPVEIFSKV 234
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
45-253 |
1.25e-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: 141.52 E-value: 1.25e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 45 KDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIakmSDAELREVRRKkIAMVFQSFALMPhMSVL 124
Cdd:cd03249 20 KGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDI---RDLNLRWLRSQ-IGLVSQEPVLFD-GTIA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 125 DNTAFGMalagvPAAEREQkAREALRQVGLENYAHAWPD-----------ELSGGMRQRVGLARALAINPDILLMDEAFS 193
Cdd:cd03249 95 ENIRYGK-----PDATDEE-VEEAAKKANIHDFIMSLPDgydtlvgergsQLSGGQKQRIAIARALLRNPKILLLDEATS 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 194 ALDPLIRTEMQDELIKlqAKHQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEIL 253
Cdd:cd03249 169 ALDAESEKLVQEALDR--AMKGRTTIVIAHRL-STIRNADLIAVLQNGQVVEQGTHDELM 225
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
44-245 |
1.40e-39 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 141.11 E-value: 1.40e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKMSDAELREVRRKKIAMVFQSFALMPHMSV 123
Cdd:PRK11629 25 LHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAELRNQKLGFIYQFHHLLPDFTA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 124 LDNTAFGMALAGVPAAEREQKAREALRQVGLENYAHAWPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEM 203
Cdd:PRK11629 105 LENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADSI 184
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 378980240 204 QDELIKLQAKHQRTIVFISHDLDEAMRIgDRIAIMQNGEVVQ 245
Cdd:PRK11629 185 FQLLGELNRLQGTAFLVVTHDLQLAKRM-SRQLEMRDGRLTA 225
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
34-261 |
2.57e-39 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 141.07 E-value: 2.57e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 34 ILEKTGLSL------GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRL--IEP---TRGQVLIDGVDI--AKMSDAEL 100
Cdd:PRK14239 5 ILQVSDLSVyynkkkALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndLNPevtITGSIVYNGHNIysPRTDTVDL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 101 RevrrKKIAMVFQSFALMPhMSVLDNTAFGMALAGVPAAEREQKARE-ALRQVGL----ENYAHAWPDELSGGMRQRVGL 175
Cdd:PRK14239 85 R----KEIGMVFQQPNPFP-MSIYENVVYGLRLKGIKDKQVLDEAVEkSLKGASIwdevKDRLHDSALGLSGGQQQRVCI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 176 ARALAINPDILLMDEAFSALDPLIRTEMQDELIKLqaKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNN 255
Cdd:PRK14239 160 ARVLATSPKIILLDEPTSALDPISAGKIEETLLGL--KDDYTMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQMFMN 237
|
250
....*....|
gi 378980240 256 PAN----DYV 261
Cdd:PRK14239 238 PKHketeDYI 247
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
45-256 |
3.63e-39 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 141.37 E-value: 3.63e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 45 KDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIaKMSDAELREVRrKKIAMVFQS-----FAlmP 119
Cdd:PRK13639 19 KGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPI-KYDKKSLLEVR-KTVGIVFQNpddqlFA--P 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 120 hmSVLDNTAFGMALAGVPAAEREQKAREALRQVGLENYAHAWPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLI 199
Cdd:PRK13639 95 --TVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMG 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 378980240 200 RTEMQDELIKLQaKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNP 256
Cdd:PRK13639 173 ASQIMKLLYDLN-KEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDI 228
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
41-254 |
5.67e-39 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 140.66 E-value: 5.67e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 41 SLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIakmSDAELREVRrKKIAMVFQSfalmPH 120
Cdd:PRK13648 22 SFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAI---TDDNFEKLR-KHIGIVFQN----PD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 121 MSVLDNT-----AFGMALAGVPAAEREQKAREALRQVGLENYAHAWPDELSGGMRQRVGLARALAINPDILLMDEAFSAL 195
Cdd:PRK13648 94 NQFVGSIvkydvAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSML 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 378980240 196 DPLIRTEMQDELIKLQAKHQRTIVFISHDLDEAMRiGDRIAIMQNGEVVQVGTPDEILN 254
Cdd:PRK13648 174 DPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIFD 231
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
45-254 |
6.62e-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: 139.29 E-value: 6.62e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 45 KDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKMSDAELrevrRKKIAMVFQSFALMpHMSVL 124
Cdd:cd03253 18 KDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSL----RRAIGVVPQDTVLF-NDTIG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 125 DNTAFGMalagvPAAEREQkAREALRQVGLENYAHAWPD-----------ELSGGMRQRVGLARALAINPDILLMDEAFS 193
Cdd:cd03253 93 YNIRYGR-----PDATDEE-VIEAAKAAQIHDKIMRFPDgydtivgerglKLSGGEKQRVAIARAILKNPPILLLDEATS 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 378980240 194 ALDPLIRTEMQDELIKLQAKhqRTIVFISHDLDEAMRiGDRIAIMQNGEVVQVGTPDEILN 254
Cdd:cd03253 167 ALDTHTEREIQAALRDVSKG--RTTIVIAHRLSTIVN-ADKIIVLKDGRIVERGTHEELLA 224
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-254 |
8.41e-39 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 139.45 E-value: 8.41e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 1 MAIKLEIKNLYKIF--GEHPHRAFKYIEKGLNKAQILEKTGLslgvKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLI 78
Cdd:COG1134 1 MSSMIEVENVSKSYrlYHEPSRSLKELLLRRRRTRREEFWAL----KDVSFEVERGESVGIIGRNGAGKSTLLKLIAGIL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 79 EPTRGQVLIDGvdiakmsdaelrevrrkKIAMVFQ-SFALMPHMSVLDNTAFGMALAGVPAAEREQKAREALRQVGLENY 157
Cdd:COG1134 77 EPTSGRVEVNG-----------------RVSALLElGAGFHPELTGRENIYLNGRLLGLSRKEIDEKFDEIVEFAELGDF 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 158 AhawpDE----LSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELIKLQaKHQRTIVFISHDLDEAMRIGD 233
Cdd:COG1134 140 I----DQpvktYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELR-ESGRTVIFVSHSMGAVRRLCD 214
|
250 260
....*....|....*....|.
gi 378980240 234 RIAIMQNGEVVQVGTPDEILN 254
Cdd:COG1134 215 RAIWLEKGRLVMDGDPEEVIA 235
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
5-228 |
1.50e-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: 137.61 E-value: 1.50e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 5 LEIKNLYKIFGEHPhrafkyiekglnkaqILEktglslgvkDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQ 84
Cdd:COG4133 3 LEAENLSCRRGERL---------------LFS---------GLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGE 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 85 VLIDGVDIAKmsdaeLREVRRKKIAMVFQSFALMPHMSVLDNTAFGMALAGVPAAEREqkAREALRQVGLENYAHAWPDE 164
Cdd:COG4133 59 VLWNGEPIRD-----AREDYRRRLAYLGHADGLKPELTVRENLRFWAALYGLRADREA--IDEALEAVGLAGLADLPVRQ 131
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 378980240 165 LSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQdELIKLQAKHQRTIVFISHDLDEA 228
Cdd:COG4133 132 LSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGVALLA-ELIAAHLARGGAVLLTTHQPLEL 194
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
45-252 |
4.20e-38 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 143.24 E-value: 4.20e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 45 KDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKMSDaelREVRRKKIAMVFQSFALMPHMSVL 124
Cdd:COG1129 21 DGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSP---RDAQAAGIAIIHQELNLVPNLSVA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 125 DNTAFGMALAG---VPAAEREQKAREALRQVGLENYAHAWPDELSGGMRQRVGLARALAINPDILLMDEAFSALDP---- 197
Cdd:COG1129 98 ENIFLGREPRRgglIDWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRDARVLILDEPTASLTEreve 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 378980240 198 ----LIRtemqdeliKLQAKHqRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVG-----TPDEI 252
Cdd:COG1129 178 rlfrIIR--------RLKAQG-VAIIYISHRLDEVFEIADRVTVLRDGRLVGTGpvaelTEDEL 232
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
44-254 |
4.23e-38 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 138.76 E-value: 4.23e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDI-AKMSDAELREVRrKKIAMVFQsfalMPHMS 122
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITItHKTKDKYIRPVR-KRIGMVFQ----FPESQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 123 VLDNTA-----FGMALAGVPAAEREQKAREALRQVGLE-NYAHAWPDELSGGMRQRVGLARALAINPDILLMDEAFSALD 196
Cdd:PRK13646 98 LFEDTVereiiFGPKNFKMNLDEVKNYAHRLLMDLGFSrDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLD 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 378980240 197 PLIRTEMQDELIKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILN 254
Cdd:PRK13646 178 PQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFK 235
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
25-253 |
5.76e-38 |
|
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: 143.40 E-value: 5.76e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 25 IEKGLNKAqilektglslgVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLI----DGVDIAKMSdAEL 100
Cdd:TIGR03269 292 VDRGVVKA-----------VDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdEWVDMTKPG-PDG 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 101 REVRRKKIAMVFQSFALMPHMSVLDN--TAFGMALagvPAAEREQKAREALRQVGL-ENYAHA----WPDELSGGMRQRV 173
Cdd:TIGR03269 360 RGRAKRYIGILHQEYDLYPHRTVLDNltEAIGLEL---PDELARMKAVITLKMVGFdEEKAEEildkYPDELSEGERHRV 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 174 GLARALAINPDILLMDEAFSALDPLIRTEMQDELIKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEIL 253
Cdd:TIGR03269 437 ALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEEIV 516
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
44-247 |
7.25e-38 |
|
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: 135.78 E-value: 7.25e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 44 VKDASLAIEEGeIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKMsdaelREVRRKKIAMVFQSFALMPHMSV 123
Cdd:cd03264 16 LDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQ-----PQKLRRRIGYLPQEFGVYPNFTV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 124 LDNTAFGMALAGVPAAEREQKAREALRQVGLENYAHAWPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEM 203
Cdd:cd03264 90 REFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDPEERIRF 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 378980240 204 QDELIKLQAkhQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVG 247
Cdd:cd03264 170 RNLLSELGE--DRIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
44-276 |
1.17e-37 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 136.78 E-value: 1.17e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKMSDAELREVRrkkiAMVFQ----SFALmp 119
Cdd:COG4559 17 LDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRR----AVLPQhsslAFPF-- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 120 hmSVLDNTAFGMALAGVPAAEREQKAREALRQVGLENYAH-AWPdELSGGMRQRVGLARALA-------INPDILLMDEA 191
Cdd:COG4559 91 --TVEEVVALGRAPHGSSAAQDRQIVREALALVGLAHLAGrSYQ-TLSGGEQQRVQLARVLAqlwepvdGGPRWLFLDEP 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 192 FSALDPL--IRTeMQdeLIKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPAndyvrtffrgvd 269
Cdd:COG4559 168 TSALDLAhqHAV-LR--LARQLARRGGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPEEVLTDEL------------ 232
|
....*..
gi 378980240 270 ISQVFSA 276
Cdd:COG4559 233 LERVYGA 239
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
44-253 |
1.62e-37 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 135.43 E-value: 1.62e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKMSDAELREvrrkKIAMVFQSFALMPHmSV 123
Cdd:cd03254 19 LKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRS----MIGVVLQDTFLFSG-TI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 124 LDNTAFGMALAgvpaaeREQKAREALRQVGLENYAHAWPD-----------ELSGGMRQRVGLARALAINPDILLMDEAF 192
Cdd:cd03254 94 MENIRLGRPNA------TDEEVIEAAKEAGAHDFIMKLPNgydtvlgenggNLSQGERQLLAIARAMLRDPKILILDEAT 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 378980240 193 SALDPLIRTEMQDELIKLQakHQRTIVFISHDLDeAMRIGDRIAIMQNGEVVQVGTPDEIL 253
Cdd:cd03254 168 SNIDTETEKLIQEALEKLM--KGRTSIIIAHRLS-TIKNADKILVLDDGKIIEEGTHDELL 225
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
44-255 |
2.01e-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: 134.87 E-value: 2.01e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKMSdaeLREVRRKKIAMVFQSFALMPHMSV 123
Cdd:cd03224 16 LFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLP---PHERARAGIGYVPEGRRIFPELTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 124 LDNTAFGmALAGVPAAEREQKAR---------EALRQVGlenyahawpDELSGGMRQRVGLARALAINPDILLMDEAFSA 194
Cdd:cd03224 93 EENLLLG-AYARRRAKRKARLERvyelfprlkERRKQLA---------GTLSGGEQQMLAIARALMSRPKLLLLDEPSEG 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 378980240 195 LDPLIRTEMQDELIKLqAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNN 255
Cdd:cd03224 163 LAPKIVEEIFEAIREL-RDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELLAD 222
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
44-257 |
3.09e-37 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 136.27 E-value: 3.09e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKMSdaELREVRrKKIAMVFQSfalmPHM-- 121
Cdd:PRK13644 18 LENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFS--KLQGIR-KLVGIVFQN----PETqf 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 122 ---SVLDNTAFGMALAGVPAAEREQKAREALRQVGLENYAHAWPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPL 198
Cdd:PRK13644 91 vgrTVEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPD 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 378980240 199 IRTEMQDELIKLQAKhQRTIVFISHDLDEaMRIGDRIAIMQNGEVVQVGTPDEILNNPA 257
Cdd:PRK13644 171 SGIAVLERIKKLHEK-GKTIVYITHNLEE-LHDADRIIVMDRGKIVLEGEPENVLSDVS 227
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
5-244 |
3.15e-37 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 135.60 E-value: 3.15e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 5 LEIKNLYKIFgehphrafkyiekglNKAQILEKTGLslgvKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQ 84
Cdd:COG1101 2 LELKNLSKTF---------------NPGTVNEKRAL----DGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGS 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 85 VLIDGVDIAKMSDAElrevRRKKIAMVFQSfALM---PHMSVLDNtafgMALA-----------GVPAAEREQkAREALR 150
Cdd:COG1101 63 ILIDGKDVTKLPEYK----RAKYIGRVFQD-PMMgtaPSMTIEEN----LALAyrrgkrrglrrGLTKKRREL-FRELLA 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 151 QV--GLENYAHAWPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPliRT-----EMQDELIKlqaKHQRTIVFISH 223
Cdd:COG1101 133 TLglGLENRLDTKVGLLSGGQRQALSLLMATLTKPKLLLLDEHTAALDP--KTaalvlELTEKIVE---ENNLTTLMVTH 207
|
250 260
....*....|....*....|.
gi 378980240 224 DLDEAMRIGDRIAIMQNGEVV 244
Cdd:COG1101 208 NMEQALDYGNRLIMMHEGRII 228
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
46-252 |
4.69e-37 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 135.64 E-value: 4.69e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 46 DASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKMS-DAELREVrRKKIAMVFQsFA--LMPHMS 122
Cdd:PRK13649 25 DVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSkNKDIKQI-RKKVGLVFQ-FPesQLFEET 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 123 VLDNTAFGMALAGVPAAEREQKAREALRQVGL-ENYAHAWPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRT 201
Cdd:PRK13649 103 VLKDVAFGPQNFGVSQEEAEALAREKLALVGIsESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGRK 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 378980240 202 EMQDELIKLqakHQR--TIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEI 252
Cdd:PRK13649 183 ELMTLFKKL---HQSgmTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDI 232
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
44-253 |
5.65e-37 |
|
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: 134.28 E-value: 5.65e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKMSDAELrevrRKKIAMVFQSFALMpHMSV 123
Cdd:cd03251 18 LRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASL----RRQIGLVSQDVFLF-NDTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 124 LDNTAFgmalaGVPAAEREQkAREALRQVGLENYAHAWPD-----------ELSGGMRQRVGLARALAINPDILLMDEAF 192
Cdd:cd03251 93 AENIAY-----GRPGATREE-VEEAARAANAHEFIMELPEgydtvigergvKLSGGQRQRIAIARALLKDPPILILDEAT 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 378980240 193 SALDplIRTEM--QDELIKLQAkhQRTIVFISHDLDEAMRIgDRIAIMQNGEVVQVGTPDEIL 253
Cdd:cd03251 167 SALD--TESERlvQAALERLMK--NRTTFVIAHRLSTIENA-DRIVVLEDGKIVERGTHEELL 224
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
44-247 |
9.03e-37 |
|
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: 133.26 E-value: 9.03e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKmsdaELREVRRKkIAMVFQSFALMPHMSV 123
Cdd:cd03266 21 VDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVK----EPAEARRR-LGFVSDSTGLYDRLTA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 124 LDNTAFGMALAGVPAAEREQKAREALRQVGLENYAHAWPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEM 203
Cdd:cd03266 96 RENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRAL 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 378980240 204 QdELIKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVG 247
Cdd:cd03266 176 R-EFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
3-257 |
9.62e-37 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 136.13 E-value: 9.62e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 3 IKLEIKNLYKIFGEHPHRAFKYIEkglnkaqilektglslgvkDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTR 82
Cdd:PRK13631 20 IILRVKNLYCVFDEKQENELVALN-------------------NISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 83 GQVLIDGVDIAKMSDAELREVR------------RKKIAMVFQsfalMPHMSVLDNT-----AFGMALAGVPAAEREQKA 145
Cdd:PRK13631 81 GTIQVGDIYIGDKKNNHELITNpyskkiknfkelRRRVSMVFQ----FPEYQLFKDTiekdiMFGPVALGVKKSEAKKLA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 146 REALRQVGL-ENYAHAWPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDeLIKLQAKHQRTIVFISHD 224
Cdd:PRK13631 157 KFYLNKMGLdDSYLERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQ-LILDAKANNKTVFVITHT 235
|
250 260 270
....*....|....*....|....*....|...
gi 378980240 225 LDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPA 257
Cdd:PRK13631 236 MEHVLEVADEVIVMDKGKILKTGTPYEIFTDQH 268
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
44-253 |
1.14e-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: 133.38 E-value: 1.14e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKMSDAELrevrRKKIAMVFQSFALMpHMSV 123
Cdd:cd03252 18 LDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWL----RRQVGVVLQENVLF-NRSI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 124 LDNTAF---GMALAGVPAAEREQKAREALRQV--GLENYAHAWPDELSGGMRQRVGLARALAINPDILLMDEAFSALDpl 198
Cdd:cd03252 93 RDNIALadpGMSMERVIEAAKLAGAHDFISELpeGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATSALD-- 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 378980240 199 irteMQDELIKLQAKHQ----RTIVFISHDLDEAMRiGDRIAIMQNGEVVQVGTPDEIL 253
Cdd:cd03252 171 ----YESEHAIMRNMHDicagRTVIIIAHRLSTVKN-ADRIIVMEKGRIVEQGSHDELL 224
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
39-267 |
1.50e-36 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 134.14 E-value: 1.50e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 39 GLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNR---LIEPTR--GQVLIDGVDIAKmSDAELREVRRKkIAMVFQ 113
Cdd:PRK14243 21 GSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRlndLIPGFRveGKVTFHGKNLYA-PDVDPVEVRRR-IGMVFQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 114 SFALMPHmSVLDNTAFGMALAGVPAAEREQKAReALRQVGLenyahaWpDE-----------LSGGMRQRVGLARALAIN 182
Cdd:PRK14243 99 KPNPFPK-SIYDNIAYGARINGYKGDMDELVER-SLRQAAL------W-DEvkdklkqsglsLSGGQQQRLCIARAIAVQ 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 183 PDILLMDEAFSALDPlIRTEMQDELIKlQAKHQRTIVFISHDLDEAMRIGDRIAIM---------QNGEVVQVGTPDEIL 253
Cdd:PRK14243 170 PEVILMDEPCSALDP-ISTLRIEELMH-ELKEQYTIIIVTHNMQQAARVSDMTAFFnveltegggRYGYLVEFDRTEKIF 247
|
250
....*....|....
gi 378980240 254 NNPANDYVRTFFRG 267
Cdd:PRK14243 248 NSPQQQATRDYVSG 261
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
44-254 |
1.78e-36 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 133.28 E-value: 1.78e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKMSDAELRevrrKKIAMVFQSFALMPHMSV 123
Cdd:COG4604 17 LDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELA----KRLAILRQENHINSRLTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 124 LDNTAFGma--laGVPAAEREQKAREALRQVGLENYAHAWPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRT 201
Cdd:COG4604 93 RELVAFGrfpyskGRLTAEDREIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQDTDYVLLDEPLNNLDMKHSV 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 378980240 202 EMQDELIKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILN 254
Cdd:COG4604 173 QMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEIIT 225
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
25-262 |
2.39e-36 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 139.07 E-value: 2.39e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 25 IEKGLNKAQILEKTGLslgvKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIePTRGQVLIDGVDIAKMSDAELREVR 104
Cdd:PRK15134 287 IRKGILKRTVDHNVVV----KNISFTLRPGETLGLVGESGSGKSTTGLALLRLI-NSQGEIWFDGQPLHNLNRRQLLPVR 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 105 RKkIAMVFQ--SFALMPHMSVLDNTAFGMAL--AGVPAAEREQKAREALRQVGLE-NYAHAWPDELSGGMRQRVGLARAL 179
Cdd:PRK15134 362 HR-IQVVFQdpNSSLNPRLNVLQIIEEGLRVhqPTLSAAQREQQVIAVMEEVGLDpETRHRYPAEFSGGQRQRIAIARAL 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 180 AINPDILLMDEAFSALDPLIRTEMQDELIKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPAND 259
Cdd:PRK15134 441 ILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERVFAAPQQE 520
|
...
gi 378980240 260 YVR 262
Cdd:PRK15134 521 YTR 523
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
44-264 |
1.39e-35 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 131.31 E-value: 1.39e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEpTRGQVLIDG-VDIAKMSDAELR---EVRRKKIAMVFQSFALMP 119
Cdd:PRK14258 23 LEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNE-LESEVRVEGrVEFFNQNIYERRvnlNRLRRQVSMVHPKPNLFP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 120 hMSVLDNTAFGMALAG-VPAAEREQKAREALRQVGL----ENYAHAWPDELSGGMRQRVGLARALAINPDILLMDEAFSA 194
Cdd:PRK14258 102 -MSVYDNVAYGVKIVGwRPKLEIDDIVESALKDADLwdeiKHKIHKSALDLSGGQQQRLCIARALAVKPKVLLMDEPCFG 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 378980240 195 LDPLIRTEMQDELIKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQN-----GEVVQVGTPDEILNNPANDYVRTF 264
Cdd:PRK14258 181 LDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGnenriGQLVEFGLTKKIFNSPHDSRTREY 255
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-251 |
1.43e-35 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 136.31 E-value: 1.43e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 1 MAIKLEIKNLYKIFGehphrafkyiekglnkaqilektglslGV---KDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRL 77
Cdd:COG3845 2 MPPALELRGITKRFG---------------------------GVvanDDVSLTVRPGEIHALLGENGAGKSTLMKILYGL 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 78 IEPTRGQVLIDG--VDIAKMSDAelrevRRKKIAMVFQSFALMPHMSVLDNTAFGM---ALAGVPAAEREQKAREALRQV 152
Cdd:COG3845 55 YQPDSGEILIDGkpVRIRSPRDA-----IALGIGMVHQHFMLVPNLTVAENIVLGLeptKGGRLDRKAARARIRELSERY 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 153 GLENYAHAWPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPlirtemQ--DELIKL--QAKHQ-RTIVFISHDLDE 227
Cdd:COG3845 130 GLDVDPDAKVEDLSVGEQQRVEILKALYRGARILILDEPTAVLTP------QeaDELFEIlrRLAAEgKSIIFITHKLRE 203
|
250 260
....*....|....*....|....
gi 378980240 228 AMRIGDRIAIMQNGEVVQVGTPDE 251
Cdd:COG3845 204 VMAIADRVTVLRRGKVVGTVDTAE 227
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
35-256 |
2.26e-35 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 131.49 E-value: 2.26e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 35 LEKTGLSlgvkDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDI-AKMSDAELREVRrKKIAMVFQ 113
Cdd:PRK13641 18 MEKKGLD----NISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHItPETGNKNLKKLR-KKVSLVFQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 114 -SFALMPHMSVLDNTAFGMALAGVPAAEREQKAREALRQVGL-ENYAHAWPDELSGGMRQRVGLARALAINPDILLMDEA 191
Cdd:PRK13641 93 fPEAQLFENTVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLsEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEP 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 378980240 192 FSALDPLIRTEMQDELIKLQaKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNP 256
Cdd:PRK13641 173 AAGLDPEGRKEMMQLFKDYQ-KAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDK 236
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
3-281 |
4.34e-35 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 131.36 E-value: 4.34e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 3 IKLEIKNLYKIFgehphrafkyiekglNKAQILEKTGLslgvKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTR 82
Cdd:PRK13651 1 MQIKVKNIVKIF---------------NKKLPTELKAL----DNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDT 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 83 GQVLIDGVDIAKMSDAELREVR--------------------RKKIAMVFQsFA--LMPHMSVLDNTAFGMALAGVPAAE 140
Cdd:PRK13651 62 GTIEWIFKDEKNKKKTKEKEKVleklviqktrfkkikkikeiRRRVGVVFQ-FAeyQLFEQTIEKDIIFGPVSMGVSKEE 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 141 REQKAREALRQVGL-ENYAHAWPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELIKLQaKHQRTIV 219
Cdd:PRK13651 141 AKKRAAKYIELVGLdESYLQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLN-KQGKTII 219
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 378980240 220 FISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNN----------PAN--DYVRTFF-RGVDISQVFSAKDIAR 281
Cdd:PRK13651 220 LVTHDLDNVLEWTKRTIFFKDGKIIKDGDTYDILSDnkfliennmePPKllNFVNKLEkKGIDVPKVTSIEELAS 294
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
5-244 |
7.06e-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: 126.39 E-value: 7.06e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 5 LEIKNLYKIFGehPHRAfkyiekglnkaqilektglslgVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQ 84
Cdd:cd03216 1 LELRGITKRFG--GVKA----------------------LDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGE 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 85 VLIDGVDIAKMSDaelREVRRKKIAMVFQsfalmphmsvldntafgmalagvpaaereqkarealrqvglenyahawpde 164
Cdd:cd03216 57 ILVDGKEVSFASP---RDARRAGIAMVYQ--------------------------------------------------- 82
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 165 LSGGMRQRVGLARALAINPDILLMDEAFSALDPLiRTEMQDELIKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVV 244
Cdd:cd03216 83 LSVGERQMVEIARALARNARLLILDEPTAALTPA-EVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
44-267 |
9.19e-35 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 128.61 E-value: 9.19e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKMSdaeLREVRRKKI------AMVFQsfal 117
Cdd:COG1137 19 VKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLP---MHKRARLGIgylpqeASIFR---- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 118 mpHMSVLDNTafgMA---LAGVPAAEREQKAREALRQVGLENYAHAWPDELSGGMRQRVGLARALAINPDILLMDEAFSA 194
Cdd:COG1137 92 --KLTVEDNI---LAvleLRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKFILLDEPFAG 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 378980240 195 LDPLIRTEMQDELIKLQakhQRTI-VFIS-HDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPAndyVRTFFRG 267
Cdd:COG1137 167 VDPIAVADIQKIIRHLK---ERGIgVLITdHNVRETLGICDRAYIISEGKVLAEGTPEEILNNPL---VRKVYLG 235
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
48-253 |
1.25e-34 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 129.44 E-value: 1.25e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKMSDAELRevrrKKIAMVFQS-FALMPHMSVLDN 126
Cdd:PRK13642 27 SFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLR----RKIGMVFQNpDNQFVGATVEDD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 127 TAFGMALAGVPAAEREQKAREALRQVGLENYAHAWPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDE 206
Cdd:PRK13642 103 VAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMRV 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 378980240 207 LIKLQAKHQRTIVFISHDLDEAMRiGDRIAIMQNGEVVQVGTPDEIL 253
Cdd:PRK13642 183 IHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELF 228
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
44-244 |
5.42e-34 |
|
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: 125.41 E-value: 5.42e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKMSDAelrevrRKKIAMVFQSFALMPHMSV 123
Cdd:cd03268 16 LDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEA------LRRIGALIEAPGFYPNLTA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 124 LDNTAFGMALAGVpaaeREQKAREALRQVGLENYAHAWPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEM 203
Cdd:cd03268 90 RENLRLLARLLGI----RKKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPDGIKEL 165
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 378980240 204 QdELIKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVV 244
Cdd:cd03268 166 R-ELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKLI 205
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
44-257 |
7.77e-34 |
|
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: 125.73 E-value: 7.77e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKMsdaELREVRRKKIAMVFQSFALMPHMSV 123
Cdd:cd03218 16 VNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKL---PMHKRARLGIGYLPQEASIFRKLTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 124 LDNTAFGMALAGVPAAEREQKAREALRQVGLENYAHAWPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEM 203
Cdd:cd03218 93 EENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVDPIAVQDI 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 378980240 204 QdELIKlQAKhQRTI-VFIS-HDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPA 257
Cdd:cd03218 173 Q-KIIK-ILK-DRGIgVLITdHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANEL 225
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-241 |
1.51e-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: 1.51e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 1 MAIKLEIKNLYKIFGEHpHRAFKYIEkglnkaqilektglslGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEP 80
Cdd:COG4778 1 MTTLLEVENLSKTFTLH-LQGGKRLP----------------VLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLP 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 81 TRGQVLID----GVDIAKMSDAELREVRRKKIAMVFQSFALMPHMSVLDNTAFGMALAGVPAAEREQKAREALRQVGL-E 155
Cdd:COG4778 64 DSGSILVRhdggWVDLAQASPREILALRRRTIGYVSQFLRVIPRVSALDVVAEPLLERGVDREEARARARELLARLNLpE 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 156 NYAHAWPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRtEMQDELIkLQAKHQ-RTIVFISHDLDEAMRIGDR 234
Cdd:COG4778 144 RLWDLPPATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANR-AVVVELI-EEAKARgTAIIGIFHDEEVREAVADR 221
|
....*..
gi 378980240 235 IAIMQNG 241
Cdd:COG4778 222 VVDVTPF 228
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
43-255 |
2.21e-33 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 126.28 E-value: 2.21e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKmSDAELREVR--RKKIAMVFQsfalMPH 120
Cdd:PRK13645 26 ALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPA-NLKKIKEVKrlRKEIGLVFQ----FPE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 121 MSVLDNT-----AFGMALAGVPAAEREQKAREALRQVGL-ENYAHAWPDELSGGMRQRVGLARALAINPDILLMDEAFSA 194
Cdd:PRK13645 101 YQLFQETiekdiAFGPVNLGENKQEAYKKVPELLKLVQLpEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGG 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 378980240 195 LDPLIRTEMQDELIKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNN 255
Cdd:PRK13645 181 LDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFSN 241
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
46-292 |
2.96e-33 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 126.00 E-value: 2.96e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 46 DASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDgvDIAKMSDAELREVR--RKKIAMVFQ-SFALMPHMS 122
Cdd:PRK13643 24 DIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVG--DIVVSSTSKQKEIKpvRKKVGVVFQfPESQLFEET 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 123 VLDNTAFGMALAGVPAAEREQKAREALRQVGL-ENYAHAWPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRT 201
Cdd:PRK13643 102 VLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLaDEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKARI 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 202 EMqdelIKL-QAKHQ--RTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPanDYVRTFFRGVDISQVFSakD 278
Cdd:PRK13643 182 EM----MQLfESIHQsgQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQEV--DFLKAHELGVPKATHFA--D 253
|
250
....*....|....
gi 378980240 279 IARRSPVGLIRKTP 292
Cdd:PRK13643 254 QLQKTGAVTFEKLP 267
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
44-285 |
3.63e-33 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 131.13 E-value: 3.63e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDG----------VDIAKMSDAELREVRRKKIAMVFQ 113
Cdd:PRK10261 32 VRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKmllrrrsrqvIELSEQSAAQMRHVRGADMAMIFQ 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 114 S--FALMPHMSVLDNTAFGMAL-AGVPAAEREQKAREALRQVGL---ENYAHAWPDELSGGMRQRVGLARALAINPDILL 187
Cdd:PRK10261 112 EpmTSLNPVFTVGEQIAESIRLhQGASREEAMVEAKRMLDQVRIpeaQTILSRYPHQLSGGMRQRVMIAMALSCRPAVLI 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 188 MDEAFSALDPLIRTEMQdELIK-LQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFFR 266
Cdd:PRK10261 192 ADEPTTALDVTIQAQIL-QLIKvLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQIFHAPQHPYTRALLA 270
|
250
....*....|....*....
gi 378980240 267 GVDISQVFSAKDIARRSPV 285
Cdd:PRK10261 271 AVPQLGAMKGLDYPRRFPL 289
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
44-257 |
3.67e-33 |
|
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: 123.94 E-value: 3.67e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKMSdAElrEVRRKKIAMVFQSFALMPHMSV 123
Cdd:COG0410 19 LHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLP-PH--RIARLGIGYVPEGRRIFPSLTV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 124 LDNTAFGMALAGVPAAEREQKAR---------EALRQVGlenyahawpDELSGGMRQRVGLARALAINPDILLMDEAFSA 194
Cdd:COG0410 96 EENLLLGAYARRDRAEVRADLERvyelfprlkERRRQRA---------GTLSGGEQQMLAIGRALMSRPKLLLLDEPSLG 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 378980240 195 LDPLIRTEMQDELIKLQAKHQrTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPA 257
Cdd:COG0410 167 LAPLIVEEIFEIIRRLNREGV-TILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLADPE 228
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
44-284 |
4.53e-33 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 130.75 E-value: 4.53e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKMSDAELREVRRKkIAMVFQS--FALMPHM 121
Cdd:PRK10261 340 VEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQALRRD-IQFIFQDpyASLDPRQ 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 122 SVLDNTAFGMALAGVPAAEREQK-AREALRQVGLENyAHAW--PDELSGGMRQRVGLARALAINPDILLMDEAFSALDPL 198
Cdd:PRK10261 419 TVGDSIMEPLRVHGLLPGKAAAArVAWLLERVGLLP-EHAWryPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVS 497
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 199 IRTEMQDELIKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFFRGVDISqvfsakD 278
Cdd:PRK10261 498 IRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENPQHPYTRKLMAAVPVA------D 571
|
....*.
gi 378980240 279 IARRSP 284
Cdd:PRK10261 572 PSRQRP 577
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
45-254 |
5.83e-33 |
|
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: 130.85 E-value: 5.83e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 45 KDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKMsdaELREVRRKkIAMVFQSFALMPHmSVL 124
Cdd:TIGR03797 470 DDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAGL---DVQAVRRQ-LGVVLQNGRLMSG-SIF 544
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 125 DNTAfgmalAGVPAAEREqkAREALRQVGLENYAHAWP-------DE----LSGGMRQRVGLARALAINPDILLMDEAFS 193
Cdd:TIGR03797 545 ENIA-----GGAPLTLDE--AWEAARMAGLAEDIRAMPmgmhtviSEgggtLSGGQRQRLLIARALVRKPRILLFDEATS 617
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 378980240 194 ALDPLIRTEMQDELIKLQAkhqrTIVFISHDLDEAMRiGDRIAIMQNGEVVQVGTPDEILN 254
Cdd:TIGR03797 618 ALDNRTQAIVSESLERLKV----TRIVIAHRLSTIRN-ADRIYVLDAGRVVQQGTYDELMA 673
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
32-256 |
1.19e-32 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 123.18 E-value: 1.19e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 32 AQILEKTGLS------LGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKMSDaelREVRR 105
Cdd:PRK11300 3 QPLLSVSGLMmrfgglLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPG---HQIAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 106 KKIAMVFQSFALMPHMSVLDN----------TAFGMALAGVPA---AEREQKAREA--LRQVGLENYAHAWPDELSGGMR 170
Cdd:PRK11300 80 MGVVRTFQHVRLFREMTVIENllvaqhqqlkTGLFSGLLKTPAfrrAESEALDRAAtwLERVGLLEHANRQAGNLAYGQQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 171 QRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELIKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPD 250
Cdd:PRK11300 160 RRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPE 239
|
....*.
gi 378980240 251 EILNNP 256
Cdd:PRK11300 240 EIRNNP 245
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
44-257 |
1.26e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 123.69 E-value: 1.26e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKMSDAELRevrrKKIAMVFQS-----FAlm 118
Cdd:PRK13647 21 LKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVR----SKVGLVFQDpddqvFS-- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 119 phMSVLDNTAFGMALAGVPAAEREQKAREALRQVGLENYAHAWPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPL 198
Cdd:PRK13647 95 --STVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPR 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 378980240 199 IRTEMQDELIKLQaKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPdEILNNPA 257
Cdd:PRK13647 173 GQETLMEILDRLH-NQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDK-SLLTDED 229
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
45-244 |
1.27e-32 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 129.46 E-value: 1.27e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 45 KDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKMSDAELREVRRKKIAMVFQSFALMPHMSVL 124
Cdd:PRK10535 25 KGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQLRREHFGFIFQRYHLLSHLTAA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 125 DNTAFGMALAGVPAAEREQKAREALRQVGLENYAHAWPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQ 204
Cdd:PRK10535 105 QNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDSHSGEEVM 184
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 378980240 205 DELIKLQAKHQrTIVFISHDLDEAMRiGDRIAIMQNGEVV 244
Cdd:PRK10535 185 AILHQLRDRGH-TVIIVTHDPQVAAQ-AERVIEIRDGEIV 222
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
44-244 |
1.74e-32 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 121.21 E-value: 1.74e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAkmsdaelREVRRKKIAMVFQsfalmpHM-- 121
Cdd:cd03226 16 LDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIK-------AKERRKSIGYVMQ------DVdy 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 122 -----SVLDNTAFGMAlagvPAAEREQKAREALRQVGLENYAHAWPDELSGGMRQRVGLARALAINPDILLMDEAFSALD 196
Cdd:cd03226 83 qlftdSVREELLLGLK----ELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLD 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 378980240 197 PlIRTEMQDELIKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVV 244
Cdd:cd03226 159 Y-KNMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
44-253 |
2.04e-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: 2.04e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAkmsDAELREVRRKkIAMVFQSFALMPHmSV 123
Cdd:TIGR02203 348 LDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLA---DYTLASLRRQ-VALVSQDVVLFND-TI 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 124 LDNTAFGmALAGVPAAEreqkAREALRQVGLENYAHAWPD-----------ELSGGMRQRVGLARALAINPDILLMDEAF 192
Cdd:TIGR02203 423 ANNIAYG-RTEQADRAE----IERALAAAYAQDFVDKLPLgldtpigengvLLSGGQRQRLAIARALLKDAPILILDEAT 497
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 378980240 193 SALDPLIRTEMQDELIKLQakHQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEIL 253
Cdd:TIGR02203 498 SALDNESERLVQAALERLM--QGRTTLVIAHRL-STIEKADRIVVMDDGRIVERGTHNELL 555
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
44-254 |
2.16e-32 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 122.57 E-value: 2.16e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKMSDAEL---REVRRKKIAMVFqSFalmph 120
Cdd:PRK13548 18 LDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELarrRAVLPQHSSLSF-PF----- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 121 mSVLDNTAFGMALAGVPAAEREQKAREALRQVGLENYAHAWPDELSGGMRQRVGLARALA------INPDILLMDEAFSA 194
Cdd:PRK13548 92 -TVEEVVAMGRAPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAqlwepdGPPRWLLLDEPTSA 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 378980240 195 LDPLirteMQDELIKL----QAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILN 254
Cdd:PRK13548 171 LDLA----HQHHVLRLarqlAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAEVLT 230
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
34-253 |
3.26e-32 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 122.04 E-value: 3.26e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 34 ILEKTGLSLG------VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKMSDAELrevrRKK 107
Cdd:PRK11231 2 TLRTENLTVGygtkriLNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQL----ARR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 108 IAMVFQSFALMPHMSVLDNTAFG----MALAGVPAAEREQKAREALRQVGLENYAHAWPDELSGGMRQRVGLARALAINP 183
Cdd:PRK11231 78 LALLPQHHLTPEGITVRELVAYGrspwLSLWGRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDT 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 378980240 184 DILLMDEAFSALDplirTEMQDELIKLQAKHQ---RTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEIL 253
Cdd:PRK11231 158 PVVLLDEPTTYLD----INHQVELMRLMRELNtqgKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVM 226
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
44-244 |
6.91e-32 |
|
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: 120.39 E-value: 6.91e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKMSDAELrevrRKKIAMVFQSFALMpHMSV 123
Cdd:cd03245 20 LDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADL----RRNIGYVPQDVTLF-YGTL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 124 LDNTAFGMalagvPAAErEQKAREALRQVGLENYAHAWPD-----------ELSGGMRQRVGLARALAINPDILLMDEAF 192
Cdd:cd03245 95 RDNITLGA-----PLAD-DERILRAAELAGVTDFVNKHPNgldlqigergrGLSGGQRQAVALARALLNDPPILLLDEPT 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 378980240 193 SALDplIRTEMQdeLIK-LQA-KHQRTIVFISHDLdEAMRIGDRIAIMQNGEVV 244
Cdd:cd03245 169 SAMD--MNSEER--LKErLRQlLGDKTLIIITHRP-SLLDLVDRIIVMDSGRIV 217
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
43-253 |
9.55e-32 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 126.61 E-value: 9.55e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKMSDAELrevrRKKIAMVFQSfALMPHMS 122
Cdd:PRK13657 350 GVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASL----RRNIAVVFQD-AGLFNRS 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 123 VLDNTAFGMALAG----VPAAEREQKAREALRQV-GLENYAHAWPDELSGGMRQRVGLARALAINPDILLMDEAFSALDP 197
Cdd:PRK13657 425 IEDNIRVGRPDATdeemRAAAERAQAHDFIERKPdGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDV 504
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 378980240 198 LIRTEMQDELIKLqaKHQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEIL 253
Cdd:PRK13657 505 ETEAKVKAALDEL--MKGRTTFIIAHRL-STVRNADRILVFDNGRVVESGSFDELV 557
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
44-254 |
9.97e-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: 120.57 E-value: 9.97e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLI------DGVDIAkmsdaELRevrrKKIAMVFQSFA- 116
Cdd:COG1119 19 LDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNDVRlfgerrGGEDVW-----ELR----KRIGLVSPALQl 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 117 -LMPHMSVLDntafgMALAGV---------PAAEREQKAREALRQVGLENYAHAWPDELSGGMRQRVGLARALAINPDIL 186
Cdd:COG1119 90 rFPRDETVLD-----VVLSGFfdsiglyrePTDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIARALVKDPELL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 378980240 187 LMDEAFSALDPLIRTEMQDELIKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILN 254
Cdd:COG1119 165 ILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRVVAAGPKEEVLT 232
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
44-252 |
2.39e-31 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 126.39 E-value: 2.39e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIakmsDAELREVRRKKIAMVfQSFALMPHMSV 123
Cdd:NF033858 282 VDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPV----DAGDIATRRRVGYMS-QAFSLYGELTV 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 124 LDNTAFGMALAGVPAAEREQKAREALRQVGLENYAHAWPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEM 203
Cdd:NF033858 357 RQNLELHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVARDMF 436
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 378980240 204 QDELIKLQAKHQRTIvFIS-HDLDEAMRIgDRIAIMQNGEVVQVGTPDEI 252
Cdd:NF033858 437 WRLLIELSREDGVTI-FIStHFMNEAERC-DRISLMHAGRVLASDTPAAL 484
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
19-235 |
3.31e-31 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 118.73 E-value: 3.31e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 19 HRAFKYIEKGLNKAQILekTGLSLGVKDAslaieegEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKMSDA 98
Cdd:PRK10584 10 HHLKKSVGQGEHELSIL--TGVELVVKRG-------ETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 99 ELREVRRKKIAMVFQSFALMPHMSVLDNTAFGMALAGVPAAEREQKAREALRQVGLENYAHAWPDELSGGMRQRVGLARA 178
Cdd:PRK10584 81 ARAKLRAKHVGFVFQSFMLIPTLNALENVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 378980240 179 LAINPDILLMDEAFSALDPLIRTEMQDELIKLQAKHQRTIVFISHDLDEAMRIGDRI 235
Cdd:PRK10584 161 FNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLAARCDRRL 217
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
44-254 |
3.69e-31 |
|
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: 124.53 E-value: 3.69e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRL--IEPTRGQVLI----------------DG--------------VD 91
Cdd:TIGR03269 16 LKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIYhvalcekcgyverpskVGepcpvcggtlepeeVD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 92 IAKMSDAELREVRrKKIAMVFQ-SFALMPHMSVLDNTAFGMALAGVPAAEREQKAREALRQVGLENYAHAWPDELSGGMR 170
Cdd:TIGR03269 96 FWNLSDKLRRRIR-KRIAIMLQrTFALYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEMVQLSHRITHIARDLSGGEK 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 171 QRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELIKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPD 250
Cdd:TIGR03269 175 QRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDLSDKAIWLENGEIKEEGTPD 254
|
....
gi 378980240 251 EILN 254
Cdd:TIGR03269 255 EVVA 258
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
59-256 |
6.31e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 119.14 E-value: 6.31e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 59 IMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKmsdAELREVRrKKIAMVFQSfalmPHMSVLDNT-----AFGMAL 133
Cdd:PRK13652 35 VIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITK---ENIREVR-KFVGLVFQN----PDDQIFSPTveqdiAFGPIN 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 134 AGVPAAEREQKAREALRQVGLENYAHAWPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELIKLQAK 213
Cdd:PRK13652 107 LGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPET 186
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 378980240 214 HQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNP 256
Cdd:PRK13652 187 YGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
45-253 |
1.44e-30 |
|
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: 123.39 E-value: 1.44e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 45 KDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKMSDAELREVrrkkIAMVfqsfalmPHMSVL 124
Cdd:COG5265 375 KGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAA----IGIV-------PQDTVL 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 125 DNTAFGMALA-GVPAAEREQkAREALRQVGLENYAHAWPD-----------ELSGGMRQRVGLARALAINPDILLMDEAF 192
Cdd:COG5265 444 FNDTIAYNIAyGRPDASEEE-VEAAARAAQIHDFIESLPDgydtrvgerglKLSGGEKQRVAIARTLLKNPPILIFDEAT 522
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 378980240 193 SALDPliRTEM--QDELIKLqAKHQRTIVfISHDLDEAMRiGDRIAIMQNGEVVQVGTPDEIL 253
Cdd:COG5265 523 SALDS--RTERaiQAALREV-ARGRTTLV-IAHRLSTIVD-ADEILVLEAGRIVERGTHAELL 580
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
45-256 |
3.37e-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: 3.37e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 45 KDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKMSDAELrevrRKKIAMVFQSFALMPHmSVL 124
Cdd:TIGR00958 498 KGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYL----HRQVALVGQEPVLFSG-SVR 572
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 125 DNTAFGmaLAGVPAAEREQKAREALRQ---VGLENYAHAWPDE----LSGGMRQRVGLARALAINPDILLMDEAFSALDp 197
Cdd:TIGR00958 573 ENIAYG--LTDTPDEEIMAAAKAANAHdfiMEFPNGYDTEVGEkgsqLSGGQKQRIAIARALVRKPRVLILDEATSALD- 649
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 378980240 198 lirTEMQDELIKLQAKHQRTIVFISHDLDEAMRiGDRIAIMQNGEVVQVGTPDEILNNP 256
Cdd:TIGR00958 650 ---AECEQLLQESRSRASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQLMEDQ 704
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
34-243 |
4.82e-30 |
|
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: 114.07 E-value: 4.82e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 34 ILEKTGLSLG--VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKMSdaeLREVRRKKIAMV 111
Cdd:cd03215 4 VLEVRGLSVKgaVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRS---PRDAIRAGIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 112 ---FQSFALMPHMSVLDNTAFgmalagvpaaereqkarealrqvglenyahawPDELSGGMRQRVGLARALAINPDILLM 188
Cdd:cd03215 81 pedRKREGLVLDLSVAENIAL--------------------------------SSLLSGGNQQKVVLARWLARDPRVLIL 128
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 378980240 189 DEAFSALDPLIRTEMQDELIKLqAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEV 243
Cdd:cd03215 129 DEPTRGVDVGAKAEIYRLIREL-ADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
44-266 |
9.79e-30 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 117.15 E-value: 9.79e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIE-PTR---GQVLIDGVDIAKMSDAELREVRRKKIAMVFQS--FAL 117
Cdd:PRK11022 23 VDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDyPGRvmaEKLEFNGQDLQRISEKERRNLVGAEVAMIFQDpmTSL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 118 MPHMSVldntAFGMALA-----GVPAAEREQKAREALRQVGLENYA---HAWPDELSGGMRQRVGLARALAINPDILLMD 189
Cdd:PRK11022 103 NPCYTV----GFQIMEAikvhqGGNKKTRRQRAIDLLNQVGIPDPAsrlDVYPHQLSGGMSQRVMIAMAIACRPKLLIAD 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 378980240 190 EAFSALDPLIRTEMQDELIKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFFR 266
Cdd:PRK11022 179 EPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDIFRAPRHPYTQALLR 255
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
5-247 |
4.35e-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: 112.63 E-value: 4.35e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 5 LEIKNLYKIFgehphRAFKYIEKGLNKAQILEKTGLS---LGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPT 81
Cdd:cd03220 1 IELENVSKSY-----PTYKGGSSSLKKLGILGRKGEVgefWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 82 RGQVlidgvdiakmsdaelrEVRRKKIAMVFQSFALMPHMSVLDNTAFGMALAGVPAAEREQKAREALRQVGLENYAHAW 161
Cdd:cd03220 76 SGTV----------------TVRGRVSSLLGLGGGFNPELTGRENIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLP 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 162 PDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELIKLQaKHQRTIVFISHDLDEAMRIGDRIAIMQNG 241
Cdd:cd03220 140 VKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELL-KQGKTVILVSHDPSSIKRLCDRALVLEKG 218
|
....*.
gi 378980240 242 EVVQVG 247
Cdd:cd03220 219 KIRFDG 224
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
44-262 |
6.73e-29 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 117.88 E-value: 6.73e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 44 VKDASLAIEEGEIFVIMGLSGSGKS-TMVRLLNRLIEP----TRGQVLIDGVDIAKMSDAELREVRRKKIAMVFQSfalm 118
Cdd:PRK15134 25 VNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPpvvyPSGDIRFHGESLLHASEQTLRGVRGNKIAMIFQE---- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 119 PHMSVLDNTAFGMALAGVPAAEREQKaREALR--------QVGLENYA---HAWPDELSGGMRQRVGLARALAINPDILL 187
Cdd:PRK15134 101 PMVSLNPLHTLEKQLYEVLSLHRGMR-REAARgeilncldRVGIRQAAkrlTDYPHQLSGGERQRVMIAMALLTRPELLI 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 378980240 188 MDEAFSALDPLIRTEMQDELIKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVR 262
Cdd:PRK15134 180 ADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAATLFSAPTHPYTQ 254
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
44-253 |
1.02e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 113.40 E-value: 1.02e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDG--VDIAKMSDAELREvrrkKIAMVFQS-----FA 116
Cdd:PRK13636 22 LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGkpIDYSRKGLMKLRE----SVGMVFQDpdnqlFS 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 117 lmphMSVLDNTAFGMALAGVPAAEREQKAREALRQVGLENYAHAWPDELSGGMRQRVGLARALAINPDILLMDEAFSALD 196
Cdd:PRK13636 98 ----ASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLD 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 378980240 197 PLIRTEMQDELIKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEIL 253
Cdd:PRK13636 174 PMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVF 230
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
59-268 |
1.42e-28 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 112.88 E-value: 1.42e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 59 IMGLSGSGKSTMVRLLNRLIEPTRG-----QVLIDGVDIAKMSDaeLREVRRKkIAMVFQSFALMPhMSVLDNTAFGM-A 132
Cdd:PRK14271 52 LMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIFNYRD--VLEFRRR-VGMLFQRPNPFP-MSIMDNVLAGVrA 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 133 LAGVPAAEREQKAREALRQVGL----ENYAHAWPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPlIRTEMQDELI 208
Cdd:PRK14271 128 HKLVPRKEFRGVAQARLTEVGLwdavKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDP-TTTEKIEEFI 206
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 209 KLQAKhQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFFRGV 268
Cdd:PRK14271 207 RSLAD-RLTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKHAETARYVAGL 265
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
44-256 |
2.42e-28 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 114.94 E-value: 2.42e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKMSDAELrevrRKKIAMVFQSFAL------ 117
Cdd:PRK09536 19 LDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAA----SRRVASVPQDTSLsfefdv 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 118 --------MPHMSVLDntafGMALAGVPAAEReqkareALRQVGLENYAHAWPDELSGGMRQRVGLARALAINPDILLMD 189
Cdd:PRK09536 95 rqvvemgrTPHRSRFD----TWTETDRAAVER------AMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLD 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 378980240 190 EAFSALD--PLIRTEmqdELIKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNP 256
Cdd:PRK09536 165 EPTASLDinHQVRTL---ELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVLTAD 230
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
44-243 |
3.48e-28 |
|
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: 108.84 E-value: 3.48e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKMSDAELRevrrKKIAMVFQSFALMPHmSV 123
Cdd:cd03246 18 LRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELG----DHVGYLPQDDELFSG-SI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 124 LDNTafgmalagvpaaereqkarealrqvglenyahawpdeLSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEM 203
Cdd:cd03246 93 AENI-------------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERAL 135
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 378980240 204 QDELIKLQAKhQRTIVFISHDLdEAMRIGDRIAIMQNGEV 243
Cdd:cd03246 136 NQAIAALKAA-GATRIVIAHRP-ETLASADRILVLEDGRV 173
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
48-266 |
7.84e-28 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 111.92 E-value: 7.84e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEP----TRGQVLIDGVDIAKMSDAELREVRRKKIAMVFQSfalmPhMSV 123
Cdd:COG4170 27 SLTLNEGEIRGLVGESGSGKSLIAKAICGITKDnwhvTADRFRWNGIDLLKLSPRERRKIIGREIAMIFQE----P-SSC 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 124 LD--NTAFGMALAGVPAAE-----------REQKAREALRQVGLENYAH---AWPDELSGGMRQRVGLARALAINPDILL 187
Cdd:COG4170 102 LDpsAKIGDQLIEAIPSWTfkgkwwqrfkwRKKRAIELLHRVGIKDHKDimnSYPHELTEGECQKVMIAMAIANQPRLLI 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 378980240 188 MDEAFSALDPLIRTEMQDELIKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFFR 266
Cdd:COG4170 182 ADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYCGQTVESGPTEQILKSPHHPYTKALLR 260
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
45-255 |
1.85e-27 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 114.15 E-value: 1.85e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 45 KDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKMSDAELREvrrkKIAMVFQSFALMPHmSVL 124
Cdd:PRK11160 357 KGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQ----AISVVSQRVHLFSA-TLR 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 125 DNTAFGMALAGvpaaerEQKAREALRQVGLENYAH------AWPDE----LSGGMRQRVGLARALAINPDILLMDEAFSA 194
Cdd:PRK11160 432 DNLLLAAPNAS------DEALIEVLQQVGLEKLLEddkglnAWLGEggrqLSGGEQRRLGIARALLHDAPLLLLDEPTEG 505
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 378980240 195 LDPliRTEMQD-ELIKLQAKHqRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEILNN 255
Cdd:PRK11160 506 LDA--ETERQIlELLAEHAQN-KTVLMITHRL-TGLEQFDRICVMDNGQIIEQGTHQELLAQ 563
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
43-238 |
3.09e-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: 113.15 E-value: 3.09e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKMSDAELrevrRKKIAMVFQSFALMPHmS 122
Cdd:TIGR02857 337 ALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSW----RDQIAWVPQHPFLFAG-T 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 123 VLDNTAFgmALAGVPAAEreqkAREALRQVGLENYAHAWPD-----------ELSGGMRQRVGLARALAINPDILLMDEA 191
Cdd:TIGR02857 412 IAENIRL--ARPDASDAE----IREALERAGLDEFVAALPQgldtpigeggaGLSGGQAQRLALARAFLRDAPLLLLDEP 485
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 378980240 192 FSALDPLIRTEMQDELikLQAKHQRTIVFISHDLdEAMRIGDRIAIM 238
Cdd:TIGR02857 486 TAHLDAETEAEVLEAL--RALAQGRTVLLVTHRL-ALAALADRIVVL 529
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
44-254 |
6.76e-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: 6.76e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKMSdaelREVRRKKIAMVFQSFALMpHMSV 123
Cdd:TIGR03796 495 IENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIPREEIP----REVLANSVAMVDQDIFLF-EGTV 569
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 124 LDNTAfgMALAGVPAAEREQKAREA------LRQVGleNYAHAWPD---ELSGGMRQRVGLARALAINPDILLMDEAFSA 194
Cdd:TIGR03796 570 RDNLT--LWDPTIPDADLVRACKDAaihdviTSRPG--GYDAELAEggaNLSGGQRQRLEIARALVRNPSILILDEATSA 645
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 378980240 195 LDPlirtemQDELIKLQAKHQR--TIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEILN 254
Cdd:TIGR03796 646 LDP------ETEKIIDDNLRRRgcTCIIVAHRL-STIRDCDEIIVLERGKVVQRGTHEELWA 700
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
44-243 |
7.17e-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: 106.79 E-value: 7.17e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKMSDAELREvrrkKIAMVFQSFALMPHmSV 123
Cdd:cd03248 30 LQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHS----KVSLVGQEPVLFAR-SL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 124 LDNTAFGmaLAGVPAAEREQKAREALRQVGLENYAHAWPDE-------LSGGMRQRVGLARALAINPDILLMDEAFSALD 196
Cdd:cd03248 105 QDNIAYG--LQSCSFECVKEAAQKAHAHSFISELASGYDTEvgekgsqLSGGQKQRVAIARALIRNPQVLILDEATSALD 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 378980240 197 plIRTEMQDELIKLQAKHQRTIVFISHDLDEAMRiGDRIAIMQNGEV 243
Cdd:cd03248 183 --AESEQQVQQALYDWPERRTVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
59-257 |
8.09e-27 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 109.58 E-value: 8.09e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 59 IMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGvdiAKMSDAELR-----EVRRkkIAMVFQSFALMPHMSVLDNTAFGMAl 133
Cdd:PRK11144 29 IFGRSGAGKTSLINAISGLTRPQKGRIVLNG---RVLFDAEKGiclppEKRR--IGYVFQDARLFPHYKVRGNLRYGMA- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 134 agvpAAEREQKAReALRQVGLENYAHAWPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELIKLQAK 213
Cdd:PRK11144 103 ----KSMVAQFDK-IVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLERLARE 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 378980240 214 HQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPA 257
Cdd:PRK11144 178 INIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVWASSA 221
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
44-225 |
8.42e-27 |
|
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: 112.07 E-value: 8.42e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKMSDAELRevrrkKIAMVFQSFALMPHMSV 123
Cdd:TIGR02868 351 LDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVR-----RRVSVCAQDAHLFDTTV 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 124 LDNTAFGMALAGvpaaerEQKAREALRQVGLENYAHAWPD-----------ELSGGMRQRVGLARALAINPDILLMDEAF 192
Cdd:TIGR02868 426 RENLRLARPDAT------DEELWAALERVGLADWLRALPDgldtvlgeggaRLSGGERQRLALARALLADAPILLLDEPT 499
|
170 180 190
....*....|....*....|....*....|...
gi 378980240 193 SALDPLIRTEMQDELikLQAKHQRTIVFISHDL 225
Cdd:TIGR02868 500 EHLDAETADELLEDL--LAALSGRTVVLITHHL 530
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
44-254 |
1.62e-26 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 111.38 E-value: 1.62e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKMSDAELREVrrkkIAMVFQSFALMPHmSV 123
Cdd:COG4618 348 LRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRH----IGYLPQDVELFDG-TI 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 124 LDNTA-FGMAlagvpaaeREQKAREALRQVGlenyAHAW----PD-----------ELSGGMRQRVGLARALAINPDILL 187
Cdd:COG4618 423 AENIArFGDA--------DPEKVVAAAKLAG----VHEMilrlPDgydtrigeggaRLSGGQRQRIGLARALYGDPRLVV 490
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 378980240 188 MDEAFSALDP-----LIRTemqdelIKLQAKHQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEILN 254
Cdd:COG4618 491 LDEPNSNLDDegeaaLAAA------IRALKARGATVVVITHRP-SLLAAVDKLLVLRDGRVQAFGPRDEVLA 555
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
39-249 |
1.70e-26 |
|
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: 105.65 E-value: 1.70e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 39 GLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKMSDAELRevrrKKIAMVFQSFALM 118
Cdd:cd03244 15 NLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLR----SRISIIPQDPVLF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 119 PHmSVLDNTA-FGMAlagvpaaeREQKAREALRQVGLENYAHAWPDEL-----------SGGMRQRVGLARALAINPDIL 186
Cdd:cd03244 91 SG-TIRSNLDpFGEY--------SDEELWQALERVGLKEFVESLPGGLdtvveeggenlSVGQRQLLCLARALLRKSKIL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 378980240 187 LMDEAFSALDPLIRTEMQdELIKLQAKHqRTIVFISHDLDEAMRIgDRIAIMQNGEVVQVGTP 249
Cdd:cd03244 162 VLDEATASVDPETDALIQ-KTIREAFKD-CTVLTIAHRLDTIIDS-DRILVLDKGRVVEFDSP 221
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
49-266 |
1.75e-26 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 106.64 E-value: 1.75e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 49 LAIEEGEIFVIMGLSGSGKSTMVRLLNRLIE-----PTRGQVLIDGVDIAKMSDAELREvRRKKIAMVFQSFALMPHMSV 123
Cdd:PRK09984 25 LNIHHGEMVALLGPSGSGKSTLLRHLSGLITgdksaGSHIELLGRTVQREGRLARDIRK-SRANTGYIFQQFNLVNRLSV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 124 LDNTAFGmALAGVP---------AAEREQKAREALRQVGLENYAHAWPDELSGGMRQRVGLARALAINPDILLMDEAFSA 194
Cdd:PRK09984 104 LENVLIG-ALGSTPfwrtcfswfTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVILADEPIAS 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 378980240 195 LDPLIRTEMQDELIKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFFR 266
Cdd:PRK09984 183 LDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQQFDNERFDHLYRSINR 254
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
39-260 |
2.19e-26 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 107.89 E-value: 2.19e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 39 GLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEP---TRGQVLIDGVDIAKMSDAELREVRRKKIAMVFQS- 114
Cdd:PRK09473 27 GDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAAngrIGGSATFNGREILNLPEKELNKLRAEQISMIFQDp 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 115 -FALMPHMSVLDN-TAFGMALAGVPAAER-EQKAR--------EALRQVGLenyahaWPDELSGGMRQRVGLARALAINP 183
Cdd:PRK09473 107 mTSLNPYMRVGEQlMEVLMLHKGMSKAEAfEESVRmldavkmpEARKRMKM------YPHEFSGGMRQRVMIAMALLCRP 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 378980240 184 DILLMDEAFSALDPLIRTEMQDELIKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDY 260
Cdd:PRK09473 181 KLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARDVFYQPSHPY 257
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
30-249 |
2.48e-26 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 111.64 E-value: 2.48e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 30 NKAQILEKTGLSlGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKMSDAElrevrRKKIA 109
Cdd:TIGR01257 933 NLVKIFEPSGRP-AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDAV-----RQSLG 1006
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 110 MVFQSFALMPHMSVLDNTAFGMALAGVPAAEREQKAREALRQVGLENYAHAWPDELSGGMRQRVGLARALAINPDILLMD 189
Cdd:TIGR01257 1007 MCPQHNILFHHLTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLD 1086
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 190 EAFSALDPLIRTEMQDELIKLQAKhqRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTP 249
Cdd:TIGR01257 1087 EPTSGVDPYSRRSIWDLLLKYRSG--RTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTP 1144
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
39-253 |
4.76e-26 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 106.43 E-value: 4.76e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 39 GLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKMSdaelrEVRRKKIAMVFQSFALM 118
Cdd:PRK13537 18 GDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRA-----RHARQRVGVVPQFDNLD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 119 PHMSVLDNTAFGMALAGVPAAEREQKAREALRQVGLENYAHAWPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPL 198
Cdd:PRK13537 93 PDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQ 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 378980240 199 IRTEMQDELIKLQAKhQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEIL 253
Cdd:PRK13537 173 ARHLMWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALI 226
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
54-244 |
8.14e-26 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 103.80 E-value: 8.14e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 54 GEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKMSDAELREVRRKkIAMVFQSFALMPHMSVLDNTAFGMAL 133
Cdd:PRK10908 28 GEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPFLRRQ-IGMIFQDHHLLMDRTVYDNVAIPLII 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 134 AGVPAAEREQKAREALRQVGLENYAHAWPDELSGGMRQRVGLARALAINPDILLMDEAFSALDplirTEMQDELIKLQAK 213
Cdd:PRK10908 107 AGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLD----DALSEGILRLFEE 182
|
170 180 190
....*....|....*....|....*....|....
gi 378980240 214 HQR---TIVFISHDLDEAMRIGDRIAIMQNGEVV 244
Cdd:PRK10908 183 FNRvgvTVLMATHDIGLISRRSYRMLTLSDGHLH 216
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
48-256 |
1.02e-25 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 104.87 E-value: 1.02e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKM-SDAELREVrrkkiAMVFQSFALMPHMSVLDN 126
Cdd:PRK10575 31 SLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWsSKAFARKV-----AYLPQQLPAAEGMTVREL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 127 TAFGM-----ALAGVPAAEREqKAREALRQVGLENYAHAWPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRT 201
Cdd:PRK10575 106 VAIGRypwhgALGRFGAADRE-KVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQV 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 378980240 202 EMQDELIKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNP 256
Cdd:PRK10575 185 DVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRGE 239
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
33-263 |
1.05e-25 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 104.40 E-value: 1.05e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 33 QILEKTGLSLG-----VKDASLAIEEGEIFVIMGLSGSGKS-TMVRLLNRL---IEPTRGQVLIDGVDIAkmsdaeLREV 103
Cdd:PRK10418 3 QQIELRNIALQaaqplVHGVSLTLQRGRVLALVGGSGSGKSlTCAAALGILpagVRQTAGRVLLDGKPVA------PCAL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 104 RRKKIAMVFQS--FALMPHMSVLDNTAFGMALAGVPAaeREQKAREALRQVGLENYA---HAWPDELSGGMRQRVGLARA 178
Cdd:PRK10418 77 RGRKIATIMQNprSAFNPLHTMHTHARETCLALGKPA--DDATLTAALEAVGLENAArvlKLYPFEMSGGMLQRMMIALA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 179 LAINPDILLMDEAFSALDPLIRTEMQDELIKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPAN 258
Cdd:PRK10418 155 LLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPKH 234
|
....*
gi 378980240 259 DYVRT 263
Cdd:PRK10418 235 AVTRS 239
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
35-227 |
1.92e-25 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 102.87 E-value: 1.92e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 35 LEKTGLSLG----VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKMSDaelrEVRRKKIAM 110
Cdd:PRK10247 10 LQNVGYLAGdakiLNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKP----EIYRQQVSY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 111 VFQSFALMPHmSVLDNTAFGMALAGvpAAEREQKAREALRQVGL-ENYAHAWPDELSGGMRQRVGLARALAINPDILLMD 189
Cdd:PRK10247 86 CAQTPTLFGD-TVYDNLIFPWQIRN--QQPDPAIFLDDLERFALpDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLD 162
|
170 180 190
....*....|....*....|....*....|....*...
gi 378980240 190 EAFSALDPLIRTEMQDELIKLQAKHQRTIVFISHDLDE 227
Cdd:PRK10247 163 EITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDE 200
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
43-260 |
3.99e-25 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 103.08 E-value: 3.99e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDG-----VDIAKMSDAELREVRRKKIAMVFQSFAL 117
Cdd:PRK11701 21 GCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMrdgqlRDLYALSEAERRRLLRTEWGFVHQHPRD 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 118 MPHMSVldntafgmaLAGVPAAEReqkareaLRQVGLENY------AHAW--------------PDELSGGMRQRVGLAR 177
Cdd:PRK11701 101 GLRMQV---------SAGGNIGER-------LMAVGARHYgdiratAGDWlerveidaariddlPTTFSGGMQQRLQIAR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 178 ALAINPDILLMDEAFSALDPLIRTEMQDELIKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPA 257
Cdd:PRK11701 165 NLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVVESGLTDQVLDDPQ 244
|
...
gi 378980240 258 NDY 260
Cdd:PRK11701 245 HPY 247
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
34-252 |
5.31e-25 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 106.26 E-value: 5.31e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 34 ILEKTGLSLG--VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDG--VDIAKMSDAelrevRRKKIA 109
Cdd:COG1129 256 VLEVEGLSVGgvVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGkpVRIRSPRDA-----IRAGIA 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 110 MV---FQSFALMPHMSVLDNTAFG----MALAGV--PAAERE--QKAREALR--------QVGlenyahawpdELSGGMR 170
Cdd:COG1129 331 YVpedRKGEGLVLDLSIRENITLAsldrLSRGGLldRRRERAlaEEYIKRLRiktpspeqPVG----------NLSGGNQ 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 171 QRVGLARALAINPDILLMDE--------AfsaldpliRTEMQdELIKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGE 242
Cdd:COG1129 401 QKVVLAKWLATDPKVLILDEptrgidvgA--------KAEIY-RLIRELAAEGKAVIVISSELPELLGLSDRILVMREGR 471
|
250
....*....|
gi 378980240 243 VVQVGTPDEI 252
Cdd:COG1129 472 IVGELDREEA 481
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
44-254 |
7.82e-25 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 103.76 E-value: 7.82e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKMSDAElrevrRKKIAMVFQSFALMPHMSV 123
Cdd:PRK13536 57 VNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLA-----RARIGVVPQFDNLDLEFTV 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 124 LDNTAFGMALAGVPAAEREQKAREALRQVGLENYAHAWPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEM 203
Cdd:PRK13536 132 RENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLI 211
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 378980240 204 QDELIKLQAKhQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILN 254
Cdd:PRK13536 212 WERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHALID 261
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
34-260 |
4.17e-24 |
|
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: 99.90 E-value: 4.17e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 34 ILEKTGLS------LGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDG-----VDIAKMSDAELRE 102
Cdd:TIGR02323 3 LLQVSGLSksygggKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMrsgaeLELYQLSEAERRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 103 VRRKKIAMVFQSFALMPHMSVLDNTAFG---MALAGVPAAEREQKAREALRQVGLE-NYAHAWPDELSGGMRQRVGLARA 178
Cdd:TIGR02323 83 LMRTEWGFVHQNPRDGLRMRVSAGANIGerlMAIGARHYGNIRATAQDWLEEVEIDpTRIDDLPRAFSGGMQQRLQIARN 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 179 LAINPDILLMDEAFSALDPLIRTEMQDELIKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPAN 258
Cdd:TIGR02323 163 LVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRVVESGLTDQVLDDPQH 242
|
..
gi 378980240 259 DY 260
Cdd:TIGR02323 243 PY 244
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
44-255 |
5.61e-24 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 99.20 E-value: 5.61e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKMSdaeLREVRRKKIAMVFQSFALMPHMSV 123
Cdd:PRK10895 19 VEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLP---LHARARRGIGYLPQEASIFRRLSV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 124 LDNTafgMALAGV----PAAEREQKAREALRQVGLENYAHAWPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLI 199
Cdd:PRK10895 96 YDNL---MAVLQIrddlSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPIS 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 200 RTEmqdelIKLQAKHQRT----IVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNN 255
Cdd:PRK10895 173 VID-----IKRIIEHLRDsglgVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQD 227
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
45-254 |
8.71e-24 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 103.17 E-value: 8.71e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 45 KDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKMSDAELREvrrkKIAMVFQSFALMpHMSVL 124
Cdd:PRK11176 360 RNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRN----QVALVSQNVHLF-NDTIA 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 125 DNTAFgmalagvpaAEREQKAREALRQVGLENYAHAWPDE---------------LSGGMRQRVGLARALAINPDILLMD 189
Cdd:PRK11176 435 NNIAY---------ARTEQYSREQIEEAARMAYAMDFINKmdngldtvigengvlLSGGQRQRIAIARALLRDSPILILD 505
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 378980240 190 EAFSALDPLIRTEMQDELIKLQakHQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEILN 254
Cdd:PRK11176 506 EATSALDTESERAIQAALDELQ--KNRTSLVIAHRL-STIEKADEILVVEDGEIVERGTHAELLA 567
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
59-253 |
1.56e-23 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 98.93 E-value: 1.56e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 59 IMGLSGSGKSTMVRLLNRLIEPTRGQVLIDG--VDIAKMSDAELREvrrkKIAMVFQSFALMPHMSVLD-NTAFGMALAG 135
Cdd:PRK13638 32 LVGANGCGKSTLFMNLSGLLRPQKGAVLWQGkpLDYSKRGLLALRQ----QVATVFQDPEQQIFYTDIDsDIAFSLRNLG 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 136 VPAAEREQKAREALRQVGLENYAHAWPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQdELIKLQAKHQ 215
Cdd:PRK13638 108 VPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQMI-AIIRRIVAQG 186
|
170 180 190
....*....|....*....|....*....|....*...
gi 378980240 216 RTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEIL 253
Cdd:PRK13638 187 NHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVF 224
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
25-276 |
2.04e-23 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 101.78 E-value: 2.04e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 25 IEKGLNKAQILEKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKMSDAELREVr 104
Cdd:PRK09700 2 ATPYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQL- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 105 rkKIAMVFQSFALMPHMSVLDNTAFGMALA----GVPA---AEREQKAREALRQVGLENYAHAWPDELSGGMRQRVGLAR 177
Cdd:PRK09700 81 --GIGIIYQELSVIDELTVLENLYIGRHLTkkvcGVNIidwREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 178 ALAINPDILLMDEAFSALdplirteMQDELIKLQA------KHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDE 251
Cdd:PRK09700 159 TLMLDAKVIIMDEPTSSL-------TNKEVDYLFLimnqlrKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSD 231
|
250 260
....*....|....*....|....*
gi 378980240 252 IlnnpANDYVRTFFRGVDISQVFSA 276
Cdd:PRK09700 232 V----SNDDIVRLMVGRELQNRFNA 252
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
42-247 |
2.30e-23 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 97.34 E-value: 2.30e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 42 LGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEP---TRGQVLIDG--VDIAKMsdaelrevrRKKIAMVFQSFA 116
Cdd:cd03234 21 RILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGggtTSGQILFNGqpRKPDQF---------QKCVAYVRQDDI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 117 LMPHMSVLDNTAFGMALA-GVPAAEREQKAREA---LRQVGLENYAHAWPDELSGGMRQRVGLARALAINPDILLMDEAF 192
Cdd:cd03234 92 LLPGLTVRETLTYTAILRlPRKSSDAIRKKRVEdvlLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPT 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 378980240 193 SALDPLIRTEMQDELIKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVG 247
Cdd:cd03234 172 SGLDSFTALNLVSTLSQLARRNRIVILTIHQPRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
44-238 |
2.82e-23 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 96.15 E-value: 2.82e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVlidgvdiakmsdaelREVRRKKIAMVFQSFAL---MPh 120
Cdd:NF040873 8 LHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTV---------------RRAGGARVAYVPQRSEVpdsLP- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 121 MSVLDNTAFG----MALAGVPAAEREQKAREALRQVGLENYAHAWPDELSGGMRQRVGLARALAINPDILLMDEAFSALD 196
Cdd:NF040873 72 LTVRDLVAMGrwarRGLWRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLD 151
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 378980240 197 PLIRTEMqDELIKLQAKHQRTIVFISHDLDEAMRIgDRIAIM 238
Cdd:NF040873 152 AESRERI-IALLAEEHARGATVVVVTHDLELVRRA-DPCVLL 191
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
44-247 |
2.90e-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: 2.90e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKMSDAelrevRRKKIAMVFQSfalmPHM-- 121
Cdd:cd03247 18 LKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKA-----LSSLISVLNQR----PYLfd 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 122 -SVLDNtafgmalagvpaaereqkarealrqVGLEnyahawpdeLSGGMRQRVGLARALAINPDILLMDEAFSALDPliR 200
Cdd:cd03247 89 tTLRNN-------------------------LGRR---------FSGGERQRLALARILLQDAPIVLLDEPTVGLDP--I 132
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 378980240 201 TEMQdeLIKLQAKH--QRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVG 247
Cdd:cd03247 133 TERQ--LLSLIFEVlkDKTLIWITHHL-TGIEHMDKILFLENGKIIMQG 178
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
44-247 |
3.66e-23 |
|
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: 95.70 E-value: 3.66e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLL-NRLIEP-TRGQVLIDGVDIAKmsdaelrEVRRKKIAMVFQSFALMPHM 121
Cdd:cd03213 25 LKNVSGKAKPGELTAIMGPSGAGKSTLLNALaGRRTGLgVSGEVLINGRPLDK-------RSFRKIIGYVPQDDILHPTL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 122 SVLDNTAFgmalagvpAAEreqkareaLRQvglenyahawpdeLSGGMRQRVGLARALAINPDILLMDEAFSALDP---- 197
Cdd:cd03213 98 TVRETLMF--------AAK--------LRG-------------LSGGERKRVSIALELVSNPSLLFLDEPTSGLDSssal 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 378980240 198 -LIRTemqdeLIKLqAKHQRTIVFISHDL-DEAMRIGDRIAIMQNGEVVQVG 247
Cdd:cd03213 149 qVMSL-----LRRL-ADTGRTIICSIHQPsSEIFELFDKLLLLSQGRVIYFG 194
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
45-253 |
4.52e-23 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 97.36 E-value: 4.52e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 45 KDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKMSDaelREVRRKkIAMVFQSFALMPHMSVL 124
Cdd:PRK10253 24 ENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYAS---KEVARR-IGLLAQNATTPGDITVQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 125 DNTAFG----MALAGVPAAEREQKAREALRQVGLENYAHAWPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIR 200
Cdd:PRK10253 100 ELVARGryphQPLFTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQ 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 378980240 201 TEMQDELIKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEIL 253
Cdd:PRK10253 180 IDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIV 232
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
44-268 |
6.91e-23 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 98.34 E-value: 6.91e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLL----NRLIEPTRGQVLIDGVDIAKMSDAELREVRRKKIAMVFQSfalmP 119
Cdd:PRK15093 23 VDRVSMTLTEGEIRGLVGESGSGKSLIAKAIcgvtKDNWRVTADRMRFDDIDLLRLSPRERRKLVGHNVSMIFQE----P 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 120 HmSVLD-NTAFGMALA-GVPAAE-----------REQKAREALRQVGLENYA---HAWPDELSGGMRQRVGLARALAINP 183
Cdd:PRK15093 99 Q-SCLDpSERVGRQLMqNIPGWTykgrwwqrfgwRKRRAIELLHRVGIKDHKdamRSFPYELTEGECQKVMIAIALANQP 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 184 DILLMDEAFSALDPLIRTEMQDELIKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRT 263
Cdd:PRK15093 178 RLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTVETAPSKELVTTPHHPYTQA 257
|
....*
gi 378980240 264 FFRGV 268
Cdd:PRK15093 258 LIRAI 262
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
42-252 |
1.03e-21 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 96.63 E-value: 1.03e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 42 LGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKMSdaeLREVRRKKIAMV---FQSFALM 118
Cdd:COG3845 272 PALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLS---PRERRRLGVAYIpedRLGRGLV 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 119 PHMSVLDNTAFG------MALAGV--PAAEREQkAREALRQ-----VGLENYAHAwpdeLSGGMRQRVGLARALAINPDI 185
Cdd:COG3845 349 PDMSVAENLILGryrrppFSRGGFldRKAIRAF-AEELIEEfdvrtPGPDTPARS----LSGGNQQKVILARELSRDPKL 423
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 378980240 186 LLMDEAFSALDP----LIRtemqDELIKLQAKhQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEI 252
Cdd:COG3845 424 LIAAQPTRGLDVgaieFIH----QRLLELRDA-GAAVLLISEDLDEILALSDRIAVMYEGRIVGEVPAAEA 489
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
48-253 |
5.35e-21 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 91.06 E-value: 5.35e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 48 SLAIEEGEIFVIMGLSGSGKSTmvrLLNRL--IEPTRGQVLIDGVDIAKMSDAELREVRrkkiAMVFQSFALMPHMSVLD 125
Cdd:COG4138 16 SAQVNAGELIHLIGPNGAGKST---LLARMagLLPGQGEILLNGRPLSDWSAAELARHR----AYLSQQQSPPFAMPVFQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 126 NTAFGMAlAGVPAAEREQKAREALRQVGLENYAHAWPDELSGGMRQRVGLARAL-----AINPD--ILLMDEAFSALDpl 198
Cdd:COG4138 89 YLALHQP-AGASSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLlqvwpTINPEgqLLLLDEPMNSLD-- 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 378980240 199 IRTE-MQDELIKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEIL 253
Cdd:COG4138 166 VAQQaALDRLLRELCQQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEVM 221
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
5-244 |
7.66e-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: 90.47 E-value: 7.66e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 5 LEIKNLYKIFGEHPHRA-FKYIEKGLNKAQILEKTGLslgvKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRG 83
Cdd:cd03267 1 IEVSNLSKSYRVYSKEPgLIGSLKSLFKRKYREVEAL----KGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 84 QVLIDGVDIAKMSDAELRevrrkKIAMVF-QSFALMPHMSVLDNTAFGMALAGVPAAEREQKAREALRQVGLENYAHAWP 162
Cdd:cd03267 77 EVRVAGLVPWKRRKKFLR-----RIGVVFgQKTQLWWDLPVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 163 DELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELIKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGE 242
Cdd:cd03267 152 RQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGR 231
|
..
gi 378980240 243 VV 244
Cdd:cd03267 232 LL 233
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
44-223 |
1.57e-20 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 93.33 E-value: 1.57e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLI-DGVDIA------KMSDAELREVrrkkiamvfqsfa 116
Cdd:COG4178 379 LEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARpAGARVLflpqrpYLPLGTLREA------------- 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 117 lmphmsvldntafgMALAGVPAAEREQKAREALRQVGLENYAH------AWPDELSGGMRQRVGLARALAINPDILLMDE 190
Cdd:COG4178 446 --------------LLYPATAEAFSDAELREALEAVGLGHLAErldeeaDWDQVLSLGEQQRLAFARLLLHKPDWLFLDE 511
|
170 180 190
....*....|....*....|....*....|....*
gi 378980240 191 AFSALDPlirtEMQDELIKL--QAKHQRTIVFISH 223
Cdd:COG4178 512 ATSALDE----ENEAALYQLlrEELPGTTVISVGH 542
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
44-249 |
1.64e-20 |
|
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: 89.01 E-value: 1.64e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKMsdaELREVRRKkIAMVFQSFALMphMSV 123
Cdd:cd03369 24 LKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTI---PLEDLRSS-LTIIPQDPTLF--SGT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 124 LDNT--AFGMalagvpaaEREQKAREALR-QVGLENyahawpdeLSGGMRQRVGLARALAINPDILLMDEAFSALD---- 196
Cdd:cd03369 98 IRSNldPFDE--------YSDEEIYGALRvSEGGLN--------LSQGQRQLLCLARALLKRPRVLVLDEATASIDyatd 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 378980240 197 ----PLIRTEMQDEliklqakhqrTIVFISHDLDEAMRIgDRIAIMQNGEVVQVGTP 249
Cdd:cd03369 162 aliqKTIREEFTNS----------TILTIAHRLRTIIDY-DKILVMDAGEVKEYDHP 207
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
45-243 |
5.46e-20 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 91.66 E-value: 5.46e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 45 KDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDgvdiakmsdaelrevRRKKIAMVFQSFALMPHMSVL 124
Cdd:COG0488 15 DDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIP---------------KGLRIGYLPQEPPLDDDLTVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 125 DNTAfgMALAGVPAAER----------------------------------EQKAREALRQVGLENYAHAWP-DELSGGM 169
Cdd:COG0488 80 DTVL--DGDAELRALEAeleeleaklaepdedlerlaelqeefealggweaEARAEEILSGLGFPEEDLDRPvSELSGGW 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 378980240 170 RQRVGLARALAINPDILLMDEAFSALDplirTEMQDELIKLQAKHQRTIVFISHD---LDeamRIGDRIAIMQNGEV 243
Cdd:COG0488 158 RRRVALARALLSEPDLLLLDEPTNHLD----LESIEWLEEFLKNYPGTVLVVSHDryfLD---RVATRILELDRGKL 227
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
37-253 |
7.54e-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: 91.93 E-value: 7.54e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 37 KTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKMSDAELRevrrkkiamvFQsFA 116
Cdd:TIGR00957 1295 REDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLR----------FK-IT 1363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 117 LMPHMSVLDNTAFGMALAgvPAAE-REQKAREALRQVGLENYAHAWPDE-----------LSGGMRQRVGLARALAINPD 184
Cdd:TIGR00957 1364 IIPQDPVLFSGSLRMNLD--PFSQySDEEVWWALELAHLKTFVSALPDKldhecaeggenLSVGQRQLVCLARALLRKTK 1441
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 378980240 185 ILLMDEAFSALDplIRTemqDELIKLQAKHQR---TIVFISHDLDEAMRIgDRIAIMQNGEVVQVGTPDEIL 253
Cdd:TIGR00957 1442 ILVLDEATAAVD--LET---DNLIQSTIRTQFedcTVLTIAHRLNTIMDY-TRVIVLDKGEVAEFGAPSNLL 1507
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
48-256 |
1.03e-19 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 91.06 E-value: 1.03e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 48 SLAIEEGEIFVIMGLSGSGKSTmvrLLNRLIE--PTRGQVLIDGVdiakmsdaELREVR----RKKIAMVFQSfALMPHM 121
Cdd:PRK11174 370 NFTLPAGQRIALVGPSGAGKTS---LLNALLGflPYQGSLKINGI--------ELRELDpeswRKHLSWVGQN-PQLPHG 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 122 SVLDNTAFGMALAGvpaaerEQKAREALRQVGLENYAHAWPD-----------ELSGGMRQRVGLARALAINPDILLMDE 190
Cdd:PRK11174 438 TLRDNVLLGNPDAS------DEQLQQALENAWVSEFLPLLPQgldtpigdqaaGLSVGQAQRLALARALLQPCQLLLLDE 511
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 378980240 191 AFSALDplIRTEMQDELIKLQAKHQRTIVFISHDLDEAMRIgDRIAIMQNGEVVQVGTPDEILNNP 256
Cdd:PRK11174 512 PTASLD--AHSEQLVMQALNAASRRQTTLMVTHQLEDLAQW-DQIWVMQDGQIVQQGDYAELSQAG 574
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
48-267 |
2.94e-19 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 86.09 E-value: 2.94e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKMSDAelrEVRRKKIAMVFQSFALMPHMSVLDNT 127
Cdd:PRK11614 25 SLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTA---KIMREAVAIVPEGRRVFSRMTVEENL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 128 AFGMALagvpaAEREQKAREALRQVG----LENYAHAWPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEM 203
Cdd:PRK11614 102 AMGGFF-----AERDQFQERIKWVYElfprLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPIIIQQI 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 378980240 204 QDELIKLQAKHQrTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILnnpANDYVRTFFRG 267
Cdd:PRK11614 177 FDTIEQLREQGM-TIFLVEQNANQALKLADRGYVLENGHVVLEDTGDALL---ANEAVRSAYLG 236
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
48-256 |
3.15e-19 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 86.14 E-value: 3.15e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 48 SLAIEEGEIFVIMGLSGSGKSTmvrLLNRL--IEPTRGQVLIDGVDIAKMSDAELREVR-------RKKIAM-VFQSFAL 117
Cdd:PRK03695 16 SAEVRAGEILHLVGPNGAGKST---LLARMagLLPGSGSIQFAGQPLEAWSAAELARHRaylsqqqTPPFAMpVFQYLTL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 118 mpHMSvldntafgmalAGVPAAEREQKAREALRQVGLENYAHAWPDELSGGMRQRVGLARAL-----AINPD--ILLMDE 190
Cdd:PRK03695 93 --HQP-----------DKTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVlqvwpDINPAgqLLLLDE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 378980240 191 AFSALDPLIRTEMqDELIKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNP 256
Cdd:PRK03695 160 PMNSLDVAQQAAL-DRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVLTPE 224
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
48-255 |
4.57e-19 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 89.80 E-value: 4.57e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKMSDAELREVrrkkiamvfqsFALMPHMSVLDNT 127
Cdd:PLN03130 1259 SFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKV-----------LGIIPQAPVLFSG 1327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 128 AFGMALAgvPAAER------EQKAREALRQV------GLENYAHAWPDELSGGMRQRVGLARALAINPDILLMDEAFSAL 195
Cdd:PLN03130 1328 TVRFNLD--PFNEHndadlwESLERAHLKDVirrnslGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAV 1405
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 378980240 196 DplIRTemqDELIklqakhQRTI---------VFISHDLDEAMRIgDRIAIMQNGEVVQVGTPDEILNN 255
Cdd:PLN03130 1406 D--VRT---DALI------QKTIreefksctmLIIAHRLNTIIDC-DRILVLDAGRVVEFDTPENLLSN 1462
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
44-255 |
7.56e-19 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 86.68 E-value: 7.56e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKmsdaelREVR-RKKIAMVF-QSFALMPHM 121
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPFK------RRKEfARRIGVVFgQRSQLWWDL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 122 SVLDNTAFGMALAGVPAAEREQKAREALRQVGLENYAHAWPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRT 201
Cdd:COG4586 112 PAIDSFRLLKAIYRIPDAEYKKRLDELVELLDLGELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKE 191
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 378980240 202 EMQDELIKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNN 255
Cdd:COG4586 192 AIREFLKEYNRERGTTILLTSHDMDDIEALCDRVIVIDHGRIIYDGSLEELKER 245
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
36-242 |
8.37e-19 |
|
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: 84.06 E-value: 8.37e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 36 EKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTmvrLLNRLI---EPTRGQVLIDGvdiakmsdaelrevrrkKIAMVF 112
Cdd:cd03250 13 GEQETSFTLKDINLEVPKGELVAIVGPVGSGKSS---LLSALLgelEKLSGSVSVPG-----------------SIAYVS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 113 QSFALMPhMSVLDNTAFGMALagvpaaeREQKAREALRQVGLENYAHAWPD-------E----LSGGMRQRVGLARALAI 181
Cdd:cd03250 73 QEPWIQN-GTIRENILFGKPF-------DEERYEKVIKACALEPDLEILPDgdlteigEkginLSGGQKQRISLARAVYS 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 378980240 182 NPDILLMDEAFSALDPLIRTEMQDELIKLQAKHQRTIVFISHDLdEAMRIGDRIAIMQNGE 242
Cdd:cd03250 145 DADIYLLDDPLSAVDAHVGRHIFENCILGLLLNNKTRILVTHQL-QLLPHADQIVVLDNGR 204
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
45-256 |
9.80e-19 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 87.85 E-value: 9.80e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 45 KDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKMSDAELRevrrKKIAMVFQSFALMPHmSVL 124
Cdd:PRK10789 332 ENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWR----SRLAVVSQTPFLFSD-TVA 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 125 DNTAFGMALAgvPAAEREQKAREA------LR-------QVGLENYAhawpdeLSGGMRQRVGLARALAINPDILLMDEA 191
Cdd:PRK10789 407 NNIALGRPDA--TQQEIEHVARLAsvhddiLRlpqgydtEVGERGVM------LSGGQKQRISIARALLLNAEILILDDA 478
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 378980240 192 FSALDPliRTEMQDELIKLQAKHQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEILNNP 256
Cdd:PRK10789 479 LSAVDG--RTEHQILHNLRQWGEGRTVIISAHRL-SALTEASEILVMQHGHIAQRGNHDQLAQQS 540
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
43-248 |
1.47e-18 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 87.29 E-value: 1.47e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 43 GVK---DASLAIEEGEIFVIMGLSGSGKSTMVRLLNRlIEPT---RGQVLIDGvdiAKMSDAELREVRRKKIAMVFQSFA 116
Cdd:PRK13549 17 GVKaldNVSLKVRAGEIVSLCGENGAGKSTLMKVLSG-VYPHgtyEGEIIFEG---EELQASNIRDTERAGIAIIHQELA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 117 LMPHMSVLDN-------TAFGMalagVPAAEREQKAREALRQVGLENYAHAWPDELSGGMRQRVGLARALAINPDILLMD 189
Cdd:PRK13549 93 LVKELSVLENiflgneiTPGGI----MDYDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQARLLILD 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 378980240 190 EAFSALdplirTEMQDE----LIKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEvvQVGT 248
Cdd:PRK13549 169 EPTASL-----TESETAvlldIIRDLKAHGIACIYISHKLNEVKAISDTICVIRDGR--HIGT 224
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
44-242 |
2.03e-18 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 86.95 E-value: 2.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGvdiaKMSDAELREVRRKKIAMVFQSFALMPHMsv 123
Cdd:PRK10522 339 VGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDG----KPVTAEQPEDYRKLFSAVFTDFHLFDQL-- 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 124 LDNTAFGMALAGVPAAEREQKAREALRQVG--LENYahawpdELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRT 201
Cdd:PRK10522 413 LGPEGKPANPALVEKWLERLKMAHKLELEDgrISNL------KLSKGQKKRLALLLALAEERDILLLDEWAADQDPHFRR 486
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 378980240 202 EMQDELIKLQAKHQRTIVFISHDlDEAMRIGDRIAIMQNGE 242
Cdd:PRK10522 487 EFYQVLLPLLQEMGKTIFAISHD-DHYFIHADRLLEMRNGQ 526
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
48-196 |
2.93e-18 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 82.54 E-value: 2.93e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKmsdaeLREVRRKKIAMVFQSFALMPHMSVLDNT 127
Cdd:PRK13538 21 SFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRR-----QRDEYHQDLLYLGHQPGIKTELTALENL 95
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 378980240 128 AFGMALAGVPaaeREQKAREALRQVGLENYAHAWPDELSGGMRQRVGLARALAINPDILLMDEAFSALD 196
Cdd:PRK13538 96 RFYQRLHGPG---DDEALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAID 161
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
48-262 |
3.17e-18 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 86.95 E-value: 3.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKMSDAELREVrrkkIAMVFQSFALMPHMSVLDNT 127
Cdd:PLN03232 1256 SFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRV----LSIIPQSPVLFSGTVRFNID 1331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 128 AFG-MALAGVPAAEREQKAREALRQ--VGLENYAHAWPDELSGGMRQRVGLARALAINPDILLMDEAFSALDplIRTemq 204
Cdd:PLN03232 1332 PFSeHNDADLWEALERAHIKDVIDRnpFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVD--VRT--- 1406
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 378980240 205 DELIKLQAKHQR---TIVFISHDLDEAMRIgDRIAIMQNGEVVQVGTPDEILNNPANDYVR 262
Cdd:PLN03232 1407 DSLIQRTIREEFkscTMLVIAHRLNTIIDC-DKILVLSSGQVLEYDSPQELLSRDTSAFFR 1466
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
45-252 |
3.64e-18 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 86.26 E-value: 3.64e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 45 KDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKMSDAELREVrrkKIAMVFQSFALMPHMSVL 124
Cdd:PRK15439 28 KGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQL---GIYLVPQEPLLFPNLSVK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 125 DNTAFGMAlagvPAAEREQKAREALRQVGLENYAHAWPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQ 204
Cdd:PRK15439 105 ENILFGLP----KRQASMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILILDEPTASLTPAETERLF 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 378980240 205 DELIKLQAKHQrTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEI 252
Cdd:PRK15439 181 SRIRELLAQGV-GIVFISHKLPEIRQLADRISVMRDGTIALSGKTADL 227
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
25-263 |
5.27e-18 |
|
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: 86.61 E-value: 5.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 25 IEKGLNKAQILEKTGL--------SLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKms 96
Cdd:TIGR01257 1928 IISGGNKTDILRLNELtkvysgtsSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT-- 2005
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 97 daelrevrrkKIAMVFQSFALMPHMSVLDNTAFGMA-------LAGVPAAEREQKAREALRQVGLENYAHAWPDELSGGM 169
Cdd:TIGR01257 2006 ----------NISDVHQNMGYCPQFDAIDDLLTGREhlylyarLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGN 2075
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 170 RQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELIKLqAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTP 249
Cdd:TIGR01257 2076 KRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSI-IREGRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGTI 2154
|
250
....*....|....
gi 378980240 250 DEILNNPANDYVRT 263
Cdd:TIGR01257 2155 QHLKSKFGDGYIVT 2168
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
48-196 |
6.14e-18 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 81.46 E-value: 6.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAkmsDAELREVrrkkIAMVFQSFALMPHMSVLDNT 127
Cdd:PRK13539 22 SFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDID---DPDVAEA----CHYLGHRNAMKPALTVAENL 94
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 378980240 128 AFGMALAGvpaaEREQKAREALRQVGLENYAHAWPDELSGGMRQRVGLARALAINPDILLMDEAFSALD 196
Cdd:PRK13539 95 EFWAAFLG----GEELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALD 159
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
48-197 |
6.29e-18 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 81.25 E-value: 6.29e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAkmsdaELREVRRKKIAMVFQSFALMPHMSVLDNT 127
Cdd:TIGR01189 20 SFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLA-----EQRDEPHENILYLGHLPGLKPELSALENL 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 128 AFGMALAGvpAAEREqkAREALRQVGLENYAHAWPDELSGGMRQRVGLARALAINPDILLMDEAFSALDP 197
Cdd:TIGR01189 95 HFWAAIHG--GAQRT--IEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDK 160
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
45-250 |
7.40e-18 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 82.04 E-value: 7.40e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 45 KDASLAIEEGEIFVIMGLSGSGKSTMVRLL--NRLIEPTRGQVLIDGVDIAKMSDAElrevR-RKKIAMVFQSFALMPHM 121
Cdd:COG0396 17 KGVNLTIKPGEVHAIMGPNGSGKSTLAKVLmgHPKYEVTSGSILLDGEDILELSPDE----RaRAGIFLAFQYPVEIPGV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 122 SVLD--NTAFG-MALAGVPAAEREQKAREALRQVGL-ENYAHAWPDE-LSGGMRQRVGLARALAINPDILLMDEAFSALD 196
Cdd:COG0396 93 SVSNflRTALNaRRGEELSAREFLKLLKEKMKELGLdEDFLDRYVNEgFSGGEKKRNEILQMLLLEPKLAILDETDSGLD 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 378980240 197 -----PLIRT--EMQDEliklqakhQRTIVFISH-----DLDEAmrigDRIAIMQNGEVVQVGTPD 250
Cdd:COG0396 173 idalrIVAEGvnKLRSP--------DRGILIITHyqrilDYIKP----DFVHVLVDGRIVKSGGKE 226
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
45-259 |
1.01e-17 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 85.47 E-value: 1.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 45 KDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDgvDIAKMSDAELREvRRKKIAMVFQSFALMPHmSVL 124
Cdd:PTZ00265 402 KDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIIN--DSHNLKDINLKW-WRSKIGVVSQDPLLFSN-SIK 477
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 125 DNTAFGM-ALAGVPAAERE-----------QKAREALR---------------------------------------QVG 153
Cdd:PTZ00265 478 NNIKYSLySLKDLEALSNYynedgndsqenKNKRNSCRakcagdlndmsnttdsneliemrknyqtikdsevvdvskKVL 557
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 154 LENYAHAWPDE-----------LSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELIKLQAKHQRTIVFIS 222
Cdd:PTZ00265 558 IHDFVSALPDKyetlvgsnaskLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIA 637
|
250 260 270
....*....|....*....|....*....|....*..
gi 378980240 223 HDLdEAMRIGDRIAIMQNGEVVQVGTPDEILNNPAND 259
Cdd:PTZ00265 638 HRL-STIRYANTIFVLSNRERGSTVDVDIIGEDPTKD 673
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
1-253 |
1.45e-17 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 81.79 E-value: 1.45e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 1 MAIKLEIKNLYKifgehPHRAFKYIEKGLNKAQILEKTGLSL-GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIE 79
Cdd:PRK13546 1 MNVSVNIKNVTK-----EYRIYRTNKERMKDALIPKHKNKTFfALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 80 PTRGQVLIDGvdiakmsdaelrevrrkKIAMVFQSFALMPHMSVLDNTAFGMALAGVPAAEREQKAREALRQVGLENYAH 159
Cdd:PRK13546 76 PTVGKVDRNG-----------------EVSVIAISAGLSGQLTGIENIEFKMLCMGFKRKEIKAMTPKIIEFSELGEFIY 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 160 AWPDELSGGMRQRVGLARALAINPDILLMDEAFSALDpliRTEMQDELIKLQ--AKHQRTIVFISHDLDEAMRIGDRIAI 237
Cdd:PRK13546 139 QPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGD---QTFAQKCLDKIYefKEQNKTIFFVSHNLGQVRQFCTKIAW 215
|
250
....*....|....*.
gi 378980240 238 MQNGEVVQVGTPDEIL 253
Cdd:PRK13546 216 IEGGKLKDYGELDDVL 231
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
44-253 |
1.95e-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: 1.95e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 44 VKDASLAIEEGEIFVIMGLSGSGKSTmvrLLNRLI-----EPTRGQVLIDGVDIAKMsdaELREVRRKKIAMVFQSFALM 118
Cdd:cd03217 16 LKGVNLTIKKGEVHALMGPNGSGKST---LAKTIMghpkyEVTEGEILFKGEDITDL---PPEERARLGIFLAFQYPPEI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 119 PhmsvldntafgmalaGVpaaereqKAREALRQVGlenyahawpDELSGGMRQRVGLARALAINPDILLMDEAFSALDpL 198
Cdd:cd03217 90 P---------------GV-------KNADFLRYVN---------EGFSGGEKKRNEILQLLLLEPDLAILDEPDSGLD-I 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 199 IRTEMQDELIKLQAKHQRTIVFISH-----DLDEAmrigDRIAIMQNGEVVQVGTPDEIL 253
Cdd:cd03217 138 DALRLVAEVINKLREEGKSVLIITHyqrllDYIKP----DRVHVLYDGRIVKSGDKELAL 193
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
48-250 |
3.34e-17 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 83.34 E-value: 3.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRlIEPT---RGQVLIDGVDIAKMSdaeLREVRRKKIAMVFQSFALMPHMSVL 124
Cdd:TIGR02633 21 DLEVRPGECVGLCGENGAGKSTLMKILSG-VYPHgtwDGEIYWSGSPLKASN---IRDTERAGIVIIHQELTLVPELSVA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 125 DNTAFG--MALAGVPAAERE--QKAREALRQVGLENYAHAWP-DELSGGMRQRVGLARALAINPDILLMDEAFSALDPLi 199
Cdd:TIGR02633 97 ENIFLGneITLPGGRMAYNAmyLRAKNLLRELQLDADNVTRPvGDYGGGQQQLVEIAKALNKQARLLILDEPSSSLTEK- 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 378980240 200 RTEMQDELIKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEvvQVGTPD 250
Cdd:TIGR02633 176 ETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQ--HVATKD 224
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
83-254 |
4.24e-17 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 83.54 E-value: 4.24e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 83 GQVLIDGVDIAkmsDAELREVRrKKIAMVFQSFALMpHMSVLDNTAFGmalagvpaaeREQKAREALRQV----GLENYA 158
Cdd:PTZ00265 1277 GKILLDGVDIC---DYNLKDLR-NLFSIVSQEPMLF-NMSIYENIKFG----------KEDATREDVKRAckfaAIDEFI 1341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 159 HAWPDE-----------LSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELIKLQAKHQRTIVFISHDLDE 227
Cdd:PTZ00265 1342 ESLPNKydtnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIAS 1421
|
170 180 190
....*....|....*....|....*....|..
gi 378980240 228 AMRiGDRIAIMQN----GEVVQV-GTPDEILN 254
Cdd:PTZ00265 1422 IKR-SDKIVVFNNpdrtGSFVQAhGTHEELLS 1452
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
45-253 |
4.43e-17 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 82.84 E-value: 4.43e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 45 KDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKMSDAELrevrRKKIAMVFQSFALMPHmSVL 124
Cdd:PRK10790 358 QNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVL----RQGVAMVQQDPVVLAD-TFL 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 125 DNTAFGMALAgvpaaerEQKAREALRQVGLENYAHAWPD-----------ELSGGMRQRVGLARALAINPDILLMDEAFS 193
Cdd:PRK10790 433 ANVTLGRDIS-------EEQVWQALETVQLAELARSLPDglytplgeqgnNLSVGQKQLLALARVLVQTPQILILDEATA 505
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 378980240 194 ALDPLIRTEMQDELIKLqaKHQRTIVFISHDLD---EAmrigDRIAIMQNGEVVQVGTPDEIL 253
Cdd:PRK10790 506 NIDSGTEQAIQQALAAV--REHTTLVVIAHRLStivEA----DTILVLHRGQAVEQGTHQQLL 562
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
43-245 |
7.65e-17 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 81.88 E-value: 7.65e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 43 GVK---DASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKMSDAELREVrrkKIAMVFQSFALMP 119
Cdd:PRK11288 16 GVKaldDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAALAA---GVAIIYQELHLVP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 120 HMSVLDN-------TAFGMalagVPAAEREQKAREALRQVGLENYAHAWPDELSGGMRQRVGLARALAINPDILLMDEAF 192
Cdd:PRK11288 93 EMTVAENlylgqlpHKGGI----VNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAFDEPT 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 378980240 193 SAL-----DPLIRtemqdeLIKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQ 245
Cdd:PRK11288 169 SSLsareiEQLFR------VIRELRAEGRVILYVSHRMEEIFALCDAITVFKDGRYVA 220
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
45-263 |
8.74e-17 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 82.02 E-value: 8.74e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 45 KDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEP---TRGQVLIDGVDIakmsdaELREVRRKKiAMVFQSFALMPHM 121
Cdd:TIGR00955 42 KNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKgvkGSGSVLLNGMPI------DAKEMRAIS-AYVQQDDLFIPTL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 122 SVLDNTAFgMAL----AGVPAAEREQKAREALRQVGLENYAH---AWPDE---LSGGMRQRVGLARALAINPDILLMDEA 191
Cdd:TIGR00955 115 TVREHLMF-QAHlrmpRRVTKKEKRERVDEVLQALGLRKCANtriGVPGRvkgLSGGERKRLAFASELLTDPPLLFCDEP 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 192 FSALDPLIRTEMQDELIKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILN-------------NPAN 258
Cdd:TIGR00955 194 TSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQPSSELFELFDKIILMAEGRVAYLGSPDQAVPffsdlghpcpenyNPAD 273
|
....*
gi 378980240 259 DYVRT 263
Cdd:TIGR00955 274 FYVQV 278
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
47-244 |
1.85e-16 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 80.73 E-value: 1.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 47 ASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDG--VDIAKMSDAelreVR---------RKKIAMVfqsf 115
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGkpIDIRSPRDA----IRagimlcpedRKAEGII---- 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 116 almPHMSVLDNTA---------FGMALagvpaaEREQKAREALRQVGLENYAHAWPDE----LSGGMRQRVGLARALAIN 182
Cdd:PRK11288 344 ---PVHSVADNINisarrhhlrAGCLI------NNRWEAENADRFIRSLNIKTPSREQlimnLSGGNQQKAILGRWLSED 414
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 378980240 183 PDILLMDEAFSALDPLIRTEMQDELIKLqAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVV 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 |
2.04e-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: 2.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGvdiakMSDAELREVRRKKIAMVFQSFALMPHMSVLDNT 127
Cdd:cd03231 20 SFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNG-----GPLDFQRDSIARGLLYLGHAPGIKTTLSVLENL 94
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 378980240 128 AFGMALAGVPAAEreqkarEALRQVGLENYAHAWPDELSGGMRQRVGLARALAINPDILLMDEAFSALD 196
Cdd:cd03231 95 RFWHADHSDEQVE------EALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALD 157
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
32-246 |
8.27e-16 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 75.77 E-value: 8.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 32 AQILEKTGLSLGV------KDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKMSDAelrevrr 105
Cdd:COG2401 28 AIVLEAFGVELRVveryvlRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVDVPDNQFGREA------- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 106 kkiamvfqsfalmphmSVLDNtafgMALAGVPAAereqkAREALRQVGLeNYAHAW---PDELSGGMRQRVGLARALAIN 182
Cdd:COG2401 101 ----------------SLIDA----IGRKGDFKD-----AVELLNAVGL-SDAVLWlrrFKELSTGQKFRFRLALLLAER 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 378980240 183 PDILLMDEAFSALDPLIRTEMQDELIKLQAKHQRTIVFISH--DLDEAMrIGDRIAIMQNGEVVQV 246
Cdd:COG2401 155 PKLLVIDEFCSHLDRQTAKRVARNLQKLARRAGITLVVATHhyDVIDDL-QPDLLIFVGYGGVPEE 219
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
44-258 |
1.07e-15 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 76.46 E-value: 1.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKmsdaelrEVRRKKIAMVFQS------FAL 117
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQ-------ALQKNLVAYVPQSeevdwsFPV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 118 MPHMSVLDNTAFGMALAGVPAAEREQKAREALRQVGLENYAHAWPDELSGGMRQRVGLARALAINPDILLMDEAFSALDP 197
Cdd:PRK15056 96 LVEDVVMMGRYGHMGWLRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDV 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 378980240 198 LIRTEMQDELIKLQAKhQRTIVFISHDLDEAMRIGDrIAIMQNGEVVQVGtPDEILNNPAN 258
Cdd:PRK15056 176 KTEARIISLLRELRDE-GKTMLVSTHNLGSVTEFCD-YTVMVKGTVLASG-PTETTFTAEN 233
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
44-223 |
1.35e-15 |
|
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: 73.73 E-value: 1.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVlidgvdiakmsdaelrevrrkkiamvfqsfalmpHMSV 123
Cdd:cd03223 17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI----------------------------------GMPE 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 124 LDNTAFgmalagVPaaereQKA-------REALrqvglenyAHAWPDELSGGMRQRVGLARALAINPDILLMDEAFSALD 196
Cdd:cd03223 63 GEDLLF------LP-----QRPylplgtlREQL--------IYPWDDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALD 123
|
170 180
....*....|....*....|....*..
gi 378980240 197 PlirtEMQDELIKLQAKHQRTIVFISH 223
Cdd:cd03223 124 E----ESEDRLYQLLKELGITVISVGH 146
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
48-250 |
2.92e-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: 77.15 E-value: 2.92e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIakmsDAELREVRRKKIAMVFQSFALMPHmsvldnt 127
Cdd:COG4615 352 DLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPV----TADNREAYRQLFSAVFSDFHLFDR------- 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 128 afgmaLAGVPAAEREQKAREALRQVGLEN----YAHAWPD-ELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTE 202
Cdd:COG4615 421 -----LLGLDGEADPARARELLERLELDHkvsvEDGRFSTtDLSQGQRKRLALLVALLEDRPILVFDEWAADQDPEFRRV 495
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 378980240 203 MQDELI-KLQAKhQRTIVFISHDlDEAMRIGDRIAIMQNGEVVQVGTPD 250
Cdd:COG4615 496 FYTELLpELKAR-GKTVIAISHD-DRYFDLADRVLKMDYGKLVELTGPA 542
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
43-243 |
7.44e-15 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 75.86 E-value: 7.44e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKMSDAElrevrRKKIAMVF-----QSFAL 117
Cdd:PRK15439 278 GFRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQ-----RLARGLVYlpedrQSSGL 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 118 MPHMSVLDNTAfgmALAGVPAAEREQKAREALRqvgLENYAHAW------PDE----LSGGMRQRVGLARALAINPDILL 187
Cdd:PRK15439 353 YLDAPLAWNVC---ALTHNRRGFWIKPARENAV---LERYRRALnikfnhAEQaartLSGGNQQKVLIAKCLEASPQLLI 426
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 378980240 188 MDEAFSALDPLIRTEMQDeLIKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEV 243
Cdd:PRK15439 427 VDEPTRGVDVSARNDIYQ-LIRSIAAQNVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
44-252 |
2.50e-14 |
|
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: 72.58 E-value: 2.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGvdiakmsdaelrevrrkKIAMVFQSFALMPHmSV 123
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG-----------------RISFSSQFSWIMPG-TI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 124 LDNTAFGMALagvpaaeREQKAREALRQVGLENYAHAWPDE-----------LSGGMRQRVGLARALAINPDILLMDEAF 192
Cdd:cd03291 115 KENIIFGVSY-------DEYRYKSVVKACQLEEDITKFPEKdntvlgeggitLSGGQRARISLARAVYKDADLYLLDSPF 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 378980240 193 SALDPLIRTEMQDE-LIKLQAKHQRTIVfisHDLDEAMRIGDRIAIMQNGEVVQVGTPDEI 252
Cdd:cd03291 188 GYLDVFTEKEIFEScVCKLMANKTRILV---TSKMEHLKKADKILILHEGSSYFYGTFSEL 245
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
11-255 |
3.07e-14 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 74.16 E-value: 3.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 11 YKIFGEHPHRAFKYIEKGLNKAQIL----EKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVL 86
Cdd:PRK13545 3 YKVKFEHVTKKYKMYNKPFDKLKDLffrsKDGEYHYALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 87 IDGvdiakmsdaelrevrrkKIAMVFQSFALMPHMSVLDNtafgMALAGVPAAEREQKAREALRQV----GLENYAHAWP 162
Cdd:PRK13545 83 IKG-----------------SAALIAISSGLNGQLTGIEN----IELKGLMMGLTKEKIKEIIPEIiefaDIGKFIYQPV 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 163 DELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELIKLQAKhQRTIVFISHDLDEAMRIGDRIAIMQNGE 242
Cdd:PRK13545 142 KTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKCLDKMNEFKEQ-GKTIFFISHSLSQVKSFCTKALWLHYGQ 220
|
250
....*....|...
gi 378980240 243 VVQVGTPDEILNN 255
Cdd:PRK13545 221 VKEYGDIKEVVDH 233
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
44-243 |
3.92e-14 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 73.71 E-value: 3.92e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPT-RGQVLIDG--VDIAKMSDAelrevRRKKIAMVFQS---FAL 117
Cdd:TIGR02633 276 VDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGkpVDIRNPAQA-----IRAGIAMVPEDrkrHGI 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 118 MPHMSVLDNTAFGM-----ALAGVPAAEREQKAREALRQVGLENYAHAWP-DELSGGMRQRVGLARALAINPDILLMDEA 191
Cdd:TIGR02633 351 VPILGVGKNITLSVlksfcFKMRIDAAAELQIIGSAIQRLKVKTASPFLPiGRLSGGNQQKAVLAKMLLTNPRVLILDEP 430
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 378980240 192 FSALDPLIRTEMQdELIKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEV 243
Cdd:TIGR02633 431 TRGVDVGAKYEIY-KLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGKL 481
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
46-253 |
4.76e-14 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 74.01 E-value: 4.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 46 DASLAIEEGEIFVIMGLSGSGKSTMVRLLN--RLIEptRGQVLIDGVDiakMSDAELREVRRKKIAMVFQSFA--LMPHM 121
Cdd:NF033858 19 DVSLDIPAGCMVGLIGPDGVGKSSLLSLIAgaRKIQ--QGRVEVLGGD---MADARHRRAVCPRIAYMPQGLGknLYPTL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 122 SVLDNTAFGMALAGVPAAEREQKAREALRQVGLenyaHAWPD----ELSGGMRQRVGLARALAINPDILLMDEAFSALDP 197
Cdd:NF033858 94 SVFENLDFFGRLFGQDAAERRRRIDELLRATGL----APFADrpagKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDP 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 378980240 198 LIRTEMQdELI-KLQAKHQRTIVFIS-HDLDEAMRIgDRIAIMQNGEVVQVGTPDEIL 253
Cdd:NF033858 170 LSRRQFW-ELIdRIRAERPGMSVLVAtAYMEEAERF-DWLVAMDAGRVLATGTPAELL 225
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
33-253 |
4.83e-14 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 73.56 E-value: 4.83e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 33 QILEKTGLSLG------VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIdGVDIakmsdaelrevrrk 106
Cdd:COG0488 314 KVLELEGLSKSygdktlLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETV-------------- 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 107 KIAMVFQSFA-LMPHMSVLDNtafgmaLAGVPAAEREQKAR-----------EALRQVGlenyahawpdELSGGMRQRVG 174
Cdd:COG0488 379 KIGYFDQHQEeLDPDKTVLDE------LRDGAPGGTEQEVRgylgrflfsgdDAFKPVG----------VLSGGEKARLA 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 175 LARALAINPDILLMDEAFSALDPlirtEMQDELIKLQAKHQRTIVFISHD---LDeamRIGDRIAIMQNGEVVQ-VGTPD 250
Cdd:COG0488 443 LAKLLLSPPNVLLLDEPTNHLDI----ETLEALEEALDDFPGTVLLVSHDryfLD---RVATRILEFEDGGVREyPGGYD 515
|
...
gi 378980240 251 EIL 253
Cdd:COG0488 516 DYL 518
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
39-235 |
5.30e-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: 5.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 39 GLSLGVKDASlaIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAkmsdaelreVRRKKIAMVFQSFALM 118
Cdd:cd03237 12 EFTLEVEGGS--ISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVS---------YKPQYIKADYEGTVRD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 119 PHMSVLDNtafgmalagvpAAEREQKAREALRQVGLENYAHAWPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPL 198
Cdd:cd03237 81 LLSSITKD-----------FYTHPYFKTEIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVE 149
|
170 180 190
....*....|....*....|....*....|....*...
gi 378980240 199 IRTeMQDELIKLQAKH-QRTIVFISHDLDEAMRIGDRI 235
Cdd:cd03237 150 QRL-MASKVIRRFAENnEKTAFVVEHDIIMIDYLADRL 186
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
5-242 |
7.57e-14 |
|
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: 68.24 E-value: 7.57e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 5 LEIKNLYKIFGEHPhrafkyiekglnkaqILektglslgvKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQ 84
Cdd:cd03221 1 IELENLSKTYGGKL---------------LL---------KDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGI 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 85 VLIDgvdiakmsdaelrevRRKKIAMVFQsfalmphmsvldntafgmalagvpaaereqkarealrqvglenyahawpde 164
Cdd:cd03221 57 VTWG---------------STVKIGYFEQ--------------------------------------------------- 70
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 165 LSGGMRQRVGLARALAINPDILLMDEAFSALDplirTEMQDELIKLQAKHQRTIVFISHD---LDeamRIGDRIAIMQNG 241
Cdd:cd03221 71 LSGGEKMRLALAKLLLENPNLLLLDEPTNHLD----LESIEALEEALKEYPGTVILVSHDryfLD---QVATKIIELEDG 143
|
.
gi 378980240 242 E 242
Cdd:cd03221 144 K 144
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
43-245 |
8.15e-14 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 72.90 E-value: 8.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 43 GVK---DASLAIEEGEIFVIMGLSGSGKSTMVRLLNRlIEPT---RGQVLIDGvDIAKMSDaeLREVRRKKIAMVFQSFA 116
Cdd:NF040905 13 GVKaldDVNLSVREGEIHALCGENGAGKSTLMKVLSG-VYPHgsyEGEILFDG-EVCRFKD--IRDSEALGIVIIHQELA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 117 LMPHMSVLDNTAFG--MALAGV-PAAEREQKAREALRQVGLENYAHAWPDELSGGMRQRVGLARALAINPDILLMDEAFS 193
Cdd:NF040905 89 LIPYLSIAENIFLGneRAKRGViDWNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLILDEPTA 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 378980240 194 AL-----DPLIrtemqdELIkLQAKHQR-TIVFISHDLDEAMRIGDRIAIMQNGEVVQ 245
Cdd:NF040905 169 ALneedsAALL------DLL-LELKAQGiTSIIISHKLNEIRRVADSITVLRDGRTIE 219
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
44-285 |
8.46e-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: 73.41 E-value: 8.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGvdiakmsdaelrevrrkKIAMVFQSFALMPHmSV 123
Cdd:TIGR01271 442 LKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG-----------------RISFSPQTSWIMPG-TI 503
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 124 LDNTAFGMALagvpaaeREQKAREALRQVGLENYAHAWPDE-----------LSGGMRQRVGLARALAINPDILLMDEAF 192
Cdd:TIGR01271 504 KDNIIFGLSY-------DEYRYTSVIKACQLEEDIALFPEKdktvlgeggitLSGGQRARISLARAVYKDADLYLLDSPF 576
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 193 SALDPLIRTEMQDE-LIKLQAKHQRTIVfiSHDLdEAMRIGDRIAIMQNGEVVQVGTPDEiLNNPANDYvRTFFRGVDIS 271
Cdd:TIGR01271 577 THLDVVTEKEIFEScLCKLMSNKTRILV--TSKL-EHLKKADKILLLHEGVCYFYGTFSE-LQAKRPDF-SSLLLGLEAF 651
|
250
....*....|....
gi 378980240 272 QVFSAKdiaRRSPV 285
Cdd:TIGR01271 652 DNFSAE---RRNSI 662
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
51-197 |
8.78e-14 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 69.88 E-value: 8.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 51 IEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGvdiAKMSDAElrevRRKKIAMVFQSFALMPHMSVLDNTAFG 130
Cdd:PRK13543 34 VDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDG---KTATRGD----RSRFMAYLGHLPGLKADLSTLENLHFL 106
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 378980240 131 MALAGVPAaerEQKAREALRQVGLENYAHAWPDELSGGMRQRVGLARaLAINPDIL-LMDEAFSALDP 197
Cdd:PRK13543 107 CGLHGRRA---KQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALAR-LWLSPAPLwLLDEPYANLDL 170
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
39-256 |
1.45e-13 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 72.89 E-value: 1.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 39 GLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKMSdaeLREVRRKkiamvfqsFALM 118
Cdd:PTZ00243 1321 GLPLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYG---LRELRRQ--------FSMI 1389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 119 PHMSVL-DNTA------FGMAL-AGVPAA-----EREQKARE-----ALRQVGLENYahawpdelSGGMRQRVGLARA-L 179
Cdd:PTZ00243 1390 PQDPVLfDGTVrqnvdpFLEASsAEVWAAlelvgLRERVASEsegidSRVLEGGSNY--------SVGQRQLMCMARAlL 1461
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 378980240 180 AINPDILLMDEAFSALDPLIRTEMQDELIKLQAKHqrTIVFISHDLDEAMRIgDRIAIMQNGEVVQVGTPDEILNNP 256
Cdd:PTZ00243 1462 KKGSGFILMDEATANIDPALDRQIQATVMSAFSAY--TVITIAHRLHTVAQY-DKIIVMDHGAVAEMGSPRELVMNR 1535
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
44-246 |
2.18e-13 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 71.35 E-value: 2.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 44 VKDASLAIEEGEIFVIMGLSGSGKStmvRLLNRL--IEPTR-GQVLIDGVDIAKMSD--------AELREVRRKKiaMVF 112
Cdd:PRK09700 279 VRDISFSVCRGEILGFAGLVGSGRT---ELMNCLfgVDKRAgGEIRLNGKDISPRSPldavkkgmAYITESRRDN--GFF 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 113 QSFALMPHMSV---LDNTAFGMALaGVPAAEREQKAREALRQVgLENYAHAWPD---ELSGGMRQRVGLARALAINPDIL 186
Cdd:PRK09700 354 PNFSIAQNMAIsrsLKDGGYKGAM-GLFHEVDEQRTAENQREL-LALKCHSVNQnitELSGGNQQKVLISKWLCCCPEVI 431
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 187 LMDEAFSALDPLIRTEMQDELIKLqAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQV 246
Cdd:PRK09700 432 IFDEPTRGIDVGAKAEIYKVMRQL-ADDGKVILMVSSELPEIITVCDRIAVFCEGRLTQI 490
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
51-263 |
2.80e-13 |
|
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: 69.17 E-value: 2.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 51 IEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKMSDAELREvrrkKIAMVFQS---------FALMPHM 121
Cdd:cd03288 44 IKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRS----RLSIILQDpilfsgsirFNLDPEC 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 122 SVLDNTAFgmalagvpaaereqkarEALRQVGLENYAHAWP-----------DELSGGMRQRVGLARALAINPDILLMDE 190
Cdd:cd03288 120 KCTDDRLW-----------------EALEIAQLKNMVKSLPggldavvteggENFSVGQRQLFCLARAFVRKSSILIMDE 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 378980240 191 AFSALDplIRTEMQDELIKLQAKHQRTIVFISHDLDEAMRiGDRIAIMQNGEVVQVGTPDEIL---NNPANDYVRT 263
Cdd:cd03288 183 ATASID--MATENILQKVVMTAFADRTVVTIAHRVSTILD-ADLVLVLSRGILVECDTPENLLaqeDGVFASLVRT 255
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
35-256 |
3.61e-13 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 68.99 E-value: 3.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 35 LEKTGLSLG----VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLidgvdiakmSDAELRevrrkkIAM 110
Cdd:PRK09544 7 LENVSVSFGqrrvLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK---------RNGKLR------IGY 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 111 VFQSFALMPHMSvLDNTAFGMALAGVpaaeREQKAREALRQVGLENYAHAWPDELSGGMRQRVGLARALAINPDILLMDE 190
Cdd:PRK09544 72 VPQKLYLDTTLP-LTVNRFLRLRPGT----KKEDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDE 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 378980240 191 AFSALDPLIRTEMQDELIKLQAKHQRTIVFISHDLDEAMRIGDRIAIMqNGEVVQVGTPDEILNNP 256
Cdd:PRK09544 147 PTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCL-NHHICCSGTPEVVSLHP 211
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
44-243 |
9.39e-13 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 69.57 E-value: 9.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRlIEPTR--GQVLIDG--VDIAKMSDAelrevRRKKIAMVFQS---FA 116
Cdd:PRK13549 278 VDDVSFSLRRGEILGIAGLVGAGRTELVQCLFG-AYPGRweGEIFIDGkpVKIRNPQQA-----IAQGIAMVPEDrkrDG 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 117 LMPHMSVLDNTAFG----MALAGVPAAEREQK-AREALRQVGLENyahAWPD----ELSGGMRQRVGLARALAINPDILL 187
Cdd:PRK13549 352 IVPVMGVGKNITLAaldrFTGGSRIDDAAELKtILESIQRLKVKT---ASPElaiaRLSGGNQQKAVLAKCLLLNPKILI 428
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 378980240 188 MDEAFSALDPLIRTEMQdELIKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEV 243
Cdd:PRK13549 429 LDEPTRGIDVGAKYEIY-KLINQLVQQGVAIIVISSELPEVLGLSDRVLVMHEGKL 483
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
44-241 |
9.76e-13 |
|
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: 66.97 E-value: 9.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKMSDAELREVRRKKIAMVFQSFALMpHMSV 123
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRNRYSVAYAAQKPWLL-NATV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 124 LDNTAFGMALagvpaaeREQKAREALRQVGLENYAHAWP--DE---------LSGGMRQRVGLARALAINPDILLMDEAF 192
Cdd:cd03290 96 EENITFGSPF-------NKQRYKAVTDACSLQPDIDLLPfgDQteigerginLSGGQRQRICVARALYQNTNIVFLDDPF 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 378980240 193 SALDPLIRTE-MQDELIKLQAKHQRTIVFISHDLdEAMRIGDRIAIMQNG 241
Cdd:cd03290 169 SALDIHLSDHlMQEGILKFLQDDKRTLVLVTHKL-QYLPHADWIIAMKDG 217
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
44-253 |
4.36e-12 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 66.00 E-value: 4.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLL-NRLIEPT-------RGQVLIDGVDIAKMsDAELREVRRKKIAMVFQ-S 114
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALaGDLTGGGaprgarvTGDVTLNGEPLAAI-DAPRLARLRAVLPQAAQpA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 115 FALMPHMSVLDNTAFGMALAGVPAAEREQKAREALRQVGLENYAHAWPDELSGGMRQRVGLARALA---------INPDI 185
Cdd:PRK13547 96 FAFSAREIVLLGRYPHARRAGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLAqlwpphdaaQPPRY 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 378980240 186 LLMDEAFSALDPLIRTEMQDELIKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEIL 253
Cdd:PRK13547 176 LLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPADVL 243
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
33-223 |
5.40e-12 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 67.60 E-value: 5.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 33 QILEKTGLSlGVKDAslaIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPT--RGQVLIDGVDIAKMSdaelrevrRKKIAM 110
Cdd:PLN03211 77 QIQERTILN-GVTGM---ASPGEILAVLGPSGSGKSTLLNALAGRIQGNnfTGTILANNRKPTKQI--------LKRTGF 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 111 VFQSFALMPHMSVLDNTAFGMALAGVPAAEREQKAREA---LRQVGL---EN--YAHAWPDELSGGMRQRVGLARALAIN 182
Cdd:PLN03211 145 VTQDDILYPHLTVRETLVFCSLLRLPKSLTKQEKILVAesvISELGLtkcENtiIGNSFIRGISGGERKRVSIAHEMLIN 224
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 378980240 183 PDILLMDEAFSALDPLIRTEMQDELIKLqAKHQRTIVFISH 223
Cdd:PLN03211 225 PSLLILDEPTSGLDATAAYRLVLTLGSL-AQKGKTIVTSMH 264
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
45-250 |
8.95e-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: 64.59 E-value: 8.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 45 KDASLAIEEGEIFVIMGLSGSGKSTMVRLL--NRLIEPTRGQVLIDGVDIAKMsdaELREVRRKKIAMVFQSFALMPHMS 122
Cdd:TIGR01978 17 KGVNLTVKKGEIHAIMGPNGSGKSTLSKTIagHPSYEVTSGTILFKGQDLLEL---EPDERARAGLFLAFQYPEEIPGVS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 123 VLD---------NTAFGMALAGVPAAERE-QKAREALRQVglENYAHAWPDE-LSGGMRQRVGLARALAINPDILLMDEA 191
Cdd:TIGR01978 94 NLEflrsalnarRSARGEEPLDLLDFEKLlKEKLALLDMD--EEFLNRSVNEgFSGGEKKRNEILQMALLEPKLAILDEI 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 378980240 192 FSALDPLIRTEMQDELIKLQAKHqRTIVFISHDLdeamRIGDRIA-----IMQNGEVVQVGTPD 250
Cdd:TIGR01978 172 DSGLDIDALKIVAEGINRLREPD-RSFLIITHYQ----RLLNYIKpdyvhVLLDGRIVKSGDVE 230
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
61-224 |
1.07e-11 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 66.45 E-value: 1.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 61 GLSGSGKSTMVRLLNRLIEPTRGQVLID-GVDIAK------------------MSDAELREVRRKKIAMvfqsFALmPHM 121
Cdd:PRK15064 34 GANGCGKSTFMKILGGDLEPSAGNVSLDpNERLGKlrqdqfafeeftvldtviMGHTELWEVKQERDRI----YAL-PEM 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 122 SVLDntafGMALAGVPA--AE-----REQKAREALRQVGLENYAHAWP-DELSGGMRQRVGLARALAINPDILLMDEAFS 193
Cdd:PRK15064 109 SEED----GMKVADLEVkfAEmdgytAEARAGELLLGVGIPEEQHYGLmSEVAPGWKLRVLLAQALFSNPDILLLDEPTN 184
|
170 180 190
....*....|....*....|....*....|...
gi 378980240 194 ALDplIRT--EMQDELIKLQAkhqrTIVFISHD 224
Cdd:PRK15064 185 NLD--INTirWLEDVLNERNS----TMIIISHD 211
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
43-244 |
1.36e-11 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 65.91 E-value: 1.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 43 GVK---DASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKMSDAELREvrrKKIAMVFQSFALMP 119
Cdd:PRK10982 10 GVKaldNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEALE---NGISMVHQELNLVL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 120 HMSVLDNTAFG-MALAGVPAAE----REQKAreALRQVGLENYAHAWPDELSGGMRQRVGLARALAINPDILLMDEAFSA 194
Cdd:PRK10982 87 QRSVMDNMWLGrYPTKGMFVDQdkmyRDTKA--IFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSS 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 378980240 195 LdplirTEMQ-DELIKLQAKHQRT---IVFISHDLDEAMRIGDRIAIMQNGEVV 244
Cdd:PRK10982 165 L-----TEKEvNHLFTIIRKLKERgcgIVYISHKMEEIFQLCDEITILRDGQWI 213
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
48-264 |
2.64e-11 |
|
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: 65.74 E-value: 2.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGV-----DIAKMSDAELRE-------VRRKKIAMVFQSF 115
Cdd:TIGR00957 658 TFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSvayvpQQAWIQNDSLREnilfgkaLNEKYYQQVLEAC 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 116 ALMPHMSVLdntafgmalagvPAAEREQKAREALrqvglenyahawpdELSGGMRQRVGLARALAINPDILLMDEAFSAL 195
Cdd:TIGR00957 738 ALLPDLEIL------------PSGDRTEIGEKGV--------------NLSGGQKQRVSLARAVYSNADIYLFDDPLSAV 791
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 378980240 196 DPLIRTEMQDELIKLQAK-HQRTIVFISHDLDEAMRIgDRIAIMQNGEVVQVGTPDEIL--NNPANDYVRTF 264
Cdd:TIGR00957 792 DAHVGKHIFEHVIGPEGVlKNKTRILVTHGISYLPQV-DVIIVMSGGKISEMGSYQELLqrDGAFAEFLRTY 862
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
44-309 |
5.63e-11 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 62.56 E-value: 5.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEpTRGQVLIDGVDIAKMSDAELRevrrkkiamvfQSFALMPHMSV 123
Cdd:cd03289 20 LENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQKWR-----------KAFGVIPQKVF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 124 LDNTAFGMALAGVPAAEREQKAREAlRQVGLENYAHAWPDEL-----------SGGMRQRVGLARALAINPDILLMDEAF 192
Cdd:cd03289 88 IFSGTFRKNLDPYGKWSDEEIWKVA-EEVGLKSVIEQFPGQLdfvlvdggcvlSHGHKQLMCLARSVLSKAKILLLDEPS 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 193 SALDPLIRTEMQDELikLQAKHQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEILNNpandyvRTFFRGVdISQ 272
Cdd:cd03289 167 AHLDPITYQVIRKTL--KQAFADCTVILSEHRI-EAMLECQRFLVIEENKVRQYDSIQKLLNE------KSHFKQA-ISP 236
|
250 260 270
....*....|....*....|....*....|....*..
gi 378980240 273 VFSAKDIARRSPVGLIRKtpgfgPRSALKLLQDEDRE 309
Cdd:cd03289 237 SDRLKLFPRRNSSKSKRK-----PRPQIQALQEETEE 268
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
43-242 |
1.91e-10 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 62.33 E-value: 1.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 43 GVK---DASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKMSDaelREVRRKKIAMVFQSFALMP 119
Cdd:PRK10762 16 GVKalsGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGP---KSSQEAGIGIIHQELNLIP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 120 HMSVLDNTAFGM----ALAGVPAAEREQKAREALRQVGLENYAHAWPDELSGGMRQRVGLARALAINPDILLMDEAFSAL 195
Cdd:PRK10762 93 QLTIAENIFLGRefvnRFGRIDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDAL 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 378980240 196 DPlIRTEMQDELIK-LQAKHqRTIVFISHDLDEAMRIGDRIAIMQNGE 242
Cdd:PRK10762 173 TD-TETESLFRVIReLKSQG-RGIVYISHRLKEIFEICDDVTVFRDGQ 218
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
44-247 |
2.35e-10 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 62.49 E-value: 2.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLidgvdiakmsdAElrevrrKKIAMVFQSFALMpHMSV 123
Cdd:PTZ00243 676 LRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVW-----------AE------RSIAYVPQQAWIM-NATV 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 124 LDNTAFgmalAGVPAAEREQKA-----REA-LRQV--GLENYAHAWPDELSGGMRQRVGLARALAINPDILLMDEAFSAL 195
Cdd:PTZ00243 738 RGNILF----FDEEDAARLADAvrvsqLEAdLAQLggGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSAL 813
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 378980240 196 DPLIRTEMQDELIkLQAKHQRTIVFISHDLDEAMRiGDRIAIMQNGEVVQVG 247
Cdd:PTZ00243 814 DAHVGERVVEECF-LGALAGKTRVLATHQVHVVPR-ADYVVALGDGRVEFSG 863
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
46-244 |
2.47e-10 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 62.28 E-value: 2.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 46 DASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDG-VDIAKMSDAELREVRR----------KKIAMVFQS 114
Cdd:PRK11147 21 NAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQdLIVARLQQDPPRNVEGtvydfvaegiEEQAEYLKR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 115 FALMPHMSVLDNTAFGMA-LAGVPAA-------EREQKAREALRQVGLEnyAHAWPDELSGGMRQRVGLARALAINPDIL 186
Cdd:PRK11147 101 YHDISHLVETDPSEKNLNeLAKLQEQldhhnlwQLENRINEVLAQLGLD--PDAALSSLSGGWLRKAALGRALVSNPDVL 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 378980240 187 LMDEAFSALDplIRT-EMQDELIKlqaKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVV 244
Cdd:PRK11147 179 LLDEPTNHLD--IETiEWLEGFLK---TFQGSIIFISHDRSFIRNMATRIVDLDRGKLV 232
|
|
| CBS_pair_SF |
cd02205 |
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ... |
297-390 |
4.19e-10 |
|
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: 56.87 E-value: 4.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 297 RSALKLLQDEDREYGYVIERGNRFVGIVSIDSLKTALSAGQG-----IEAALIDAPLAVEAQTPLSDLLSH-VGHAPCAV 370
Cdd:cd02205 14 REALELMAENGIGALPVVDDDGKLVGIVTERDILRALVEGGLaldtpVAEVMTPDVITVSPDTDLEEALELmLEHGIRRL 93
|
90 100
....*....|....*....|
gi 378980240 371 PVVDEEQQYIGIISKRMLLQ 390
Cdd:cd02205 94 PVVDDDGKLVGIVTRRDILR 113
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
24-244 |
5.04e-10 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 58.81 E-value: 5.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 24 YIEKGLNKAQILektglslgvKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPT---RGQVLIDGVDIAKMsdael 100
Cdd:cd03233 12 TTGKGRSKIPIL---------KDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKEF----- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 101 REVRRKKIAMVFQSFALMPHMSVLDNTAFGMALagvpaaereqKAREALRQVglenyahawpdelSGGMRQRVGLARALA 180
Cdd:cd03233 78 AEKYPGEIIYVSEEDVHFPTLTVRETLDFALRC----------KGNEFVRGI-------------SGGERKRVSIAEALV 134
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 378980240 181 INPDILLMDEAFSALDPLIRTEMQdELIKLQAKHQRTIVFIS--HDLDEAMRIGDRIAIMQNGEVV 244
Cdd:cd03233 135 SRASVLCWDNSTRGLDSSTALEIL-KCIRTMADVLKTTTFVSlyQASDEIYDLFDKVLVLYEGRQI 199
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
44-309 |
5.13e-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: 61.46 E-value: 5.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEpTRGQVLIDGVDIAKMSDAELRevrrkkiamvfQSFALMPHMSV 123
Cdd:TIGR01271 1235 LQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVSWNSVTLQTWR-----------KAFGVIPQKVF 1302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 124 LDNTAFGMALAgvPAAE-REQKAREALRQVGLENYAHAWPDEL-----------SGGMRQRVGLARALAINPDILLMDEA 191
Cdd:TIGR01271 1303 IFSGTFRKNLD--PYEQwSDEEIWKVAEEVGLKSVIEQFPDKLdfvlvdggyvlSNGHKQLMCLARSILSKAKILLLDEP 1380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 192 FSALDP----LIRTEMQdeliklQAKHQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEILNNpandyvRTFFRg 267
Cdd:TIGR01271 1381 SAHLDPvtlqIIRKTLK------QSFSNCTVILSEHRV-EALLECQQFLVIEGSSVKQYDSIQKLLNE------TSLFK- 1446
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 378980240 268 vdisQVFSAKDIARRSPVGLiRKTPGFGPRSALKLLQDEDRE 309
Cdd:TIGR01271 1447 ----QAMSAADRLKLFPLHR-RNSSKRKPQPKITALREEAEE 1483
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
35-243 |
5.60e-10 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 60.79 E-value: 5.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 35 LEKTGLS-LGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKMSDAE--------LREVRR 105
Cdd:PRK10762 258 LKVDNLSgPGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDglangivyISEDRK 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 106 KKiamvfqsfALMPHMSVLDNtafgMAL---------AGVPAAEREQKAREALrqVGLENYAHAWPDE----LSGGMRQR 172
Cdd:PRK10762 338 RD--------GLVLGMSVKEN----MSLtalryfsraGGSLKHADEQQAVSDF--IRLFNIKTPSMEQaiglLSGGNQQK 403
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 378980240 173 VGLARALAINPDILLMDEAFSALDPLIRTEMQDeLIKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEV 243
Cdd:PRK10762 404 VAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQ-LINQFKAEGLSIILVSSEMPEVLGMSDRILVMHEGRI 473
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
144-252 |
6.13e-10 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 60.13 E-value: 6.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 144 KAREALRQVGLENYAHAWPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDElIKLQAKHQRTIVFISH 223
Cdd:NF000106 124 RADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDE-VRSMVRDGATVLLTTQ 202
|
90 100
....*....|....*....|....*....
gi 378980240 224 DLDEAMRIGDRIAIMQNGEVVQVGTPDEI 252
Cdd:NF000106 203 YMEEAEQLAHELTVIDRGRVIADGKVDEL 231
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
36-255 |
2.32e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 59.37 E-value: 2.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 36 EKTGLSlgvkDASLAIEEGEIFVIMGLSGSGKSTmvrllnrLIEPTRGQvlidgvdIAKMSDAELreVRRKKIAMVFQsF 115
Cdd:PLN03130 629 ERPTLS----NINLDVPVGSLVAIVGSTGEGKTS-------LISAMLGE-------LPPRSDASV--VIRGTVAYVPQ-V 687
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 116 ALMPHMSVLDNTAFGMALAgvpaAEREQKAreaLRQVGLENYAHAWPD-----------ELSGGMRQRVGLARALAINPD 184
Cdd:PLN03130 688 SWIFNATVRDNILFGSPFD----PERYERA---IDVTALQHDLDLLPGgdlteigergvNISGGQKQRVSMARAVYSNSD 760
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 378980240 185 ILLMDEAFSALDPLIRTEMQDELIKLQAKHqRTIVFISHDLDEAMRIgDRIAIMQNGEVVQVGTPDEILNN 255
Cdd:PLN03130 761 VYIFDDPLSALDAHVGRQVFDKCIKDELRG-KTRVLVTNQLHFLSQV-DRIILVHEGMIKEEGTYEELSNN 829
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
54-237 |
2.80e-09 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 55.46 E-value: 2.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 54 GEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDiakmsdaelrevrrkkiamvfqsfalmphmsvldntafgmal 133
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGE------------------------------------------ 39
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 134 agvpaaereqKAREALRQVGLENYAHAWPDELSGGMRQRVGLARALAINPDILLMDEAFSALDP-----LIRTEMQDELI 208
Cdd:smart00382 40 ----------DILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAeqealLLLLEELRLLL 109
|
170 180
....*....|....*....|....*....
gi 378980240 209 KLQAKHQRTIVFISHDLDEAMRIGDRIAI 237
Cdd:smart00382 110 LLKSEKNLTVILTTNDEKDLGPALLRRRF 138
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
48-253 |
1.07e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 56.95 E-value: 1.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKMSDAELRevrrKKIAMVFQ---SFALMPHMSVL 124
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLSFEQLQ----KLVSDEWQrnnTDMLSPGEDDT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 125 DNTAFGMALAGVPAAER-EQKARealrQVGLENYAHAWPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEM 203
Cdd:PRK10938 99 GRTTAEIIQDEVKDPARcEQLAQ----QFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQL 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 378980240 204 QDELIKLQAKHQrTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEIL 253
Cdd:PRK10938 175 AELLASLHQSGI-TLVLVLNRFDEIPDFVQFAGVLADCTLAETGEREEIL 223
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
35-255 |
1.79e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 56.52 E-value: 1.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 35 LEKTGLSlgvkDASLAIEEGEIFVIMGLSGSGKSTMVR-LLNRLIEPTRGQVLIDGV-----DIAKMSDAELREvrrkki 108
Cdd:PLN03232 628 TSKPTLS----DINLEIPVGSLVAIVGGTGEGKTSLISaMLGELSHAETSSVVIRGSvayvpQVSWIFNATVRE------ 697
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 109 AMVFQS-FALMPHMSVLDNTAFGMALAGVPAAEREQKAREALrqvglenyahawpdELSGGMRQRVGLARALAINPDILL 187
Cdd:PLN03232 698 NILFGSdFESERYWRAIDVTALQHDLDLLPGRDLTEIGERGV--------------NISGGQKQRVSMARAVYSNSDIYI 763
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 188 MDEAFSALDPLIRTEMQDELIK--LQAKhqrTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEILNN 255
Cdd:PLN03232 764 FDDPLSALDAHVAHQVFDSCMKdeLKGK---TRVLVTNQL-HFLPLMDRIILVSEGMIKEEGTFAELSKS 829
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
14-225 |
1.86e-08 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 56.33 E-value: 1.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 14 FGEHPHRAFKyiekglNKAQILEKTGLSLGVKDASLAIEEGEIFV-----IMGLSGSGKSTMVRLLNRLIEPTRGQVLID 88
Cdd:COG1245 327 FEVHAPRREK------EEETLVEYPDLTKSYGGFSLEVEGGEIREgevlgIVGPNGIGKTTFAKILAGVLKPDEGEVDED 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 89 gVDIA-K------MSDAELREVRRKKIAMVFQSfalmphmSVLDNtafgmalagvpaaereqkarEALRQVGLENYAHAW 161
Cdd:COG1245 401 -LKISyKpqyispDYDGTVEEFLRSANTDDFGS-------SYYKT--------------------EIIKPLGLEKLLDKN 452
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 378980240 162 PDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELIKLQAKHQRTIVFISHDL 225
Cdd:COG1245 453 VKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAENRGKTAMVVDHDI 516
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
31-243 |
1.89e-08 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 55.89 E-value: 1.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 31 KAQILEKTGLSL----GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKMSDAE------- 99
Cdd:PRK10982 247 GEVILEVRNLTSlrqpSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANEainhgfa 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 100 -LREVRRKKIAMVFQSFALMPHMSVLDN--TAFGMaLAGVPAAEREQKAREALRQVGLENYAHAwpDELSGGMRQRVGLA 176
Cdd:PRK10982 327 lVTEERRSTGIYAYLDIGFNSLISNIRNykNKVGL-LDNSRMKSDTQWVIDSMRVKTPGHRTQI--GSLSGGNQQKVIIG 403
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 378980240 177 RALAINPDILLMDEAFSALDPLIRTEMQdELIKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEV 243
Cdd:PRK10982 404 RWLLTQPEILMLDEPTRGIDVGAKFEIY-QLIAELAKKDKGIIIISSEMPELLGITDRILVMSNGLV 469
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
5-248 |
4.36e-08 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 53.88 E-value: 4.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 5 LEIKNLYKIFGEHPhrafkyIEKGLNkaqilektglslgvkdasLAIEEGEIFVIMGLSGSGKSTMVRLL--NRLIEPTR 82
Cdd:CHL00131 8 LEIKNLHASVNENE------ILKGLN------------------LSINKGEIHAIMGPNGSGKSTLSKVIagHPAYKILE 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 83 GQVLIDGVDIAKMsDAELREvrRKKIAMVFQSFALMPHMSVLD--NTAFG-----MALAGVPAAEREQKAREALRQVGL- 154
Cdd:CHL00131 64 GDILFKGESILDL-EPEERA--HLGIFLAFQYPIEIPGVSNADflRLAYNskrkfQGLPELDPLEFLEIINEKLKLVGMd 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 155 ENYAHAWPDE-LSGGMRQRVGLARALAINPDILLMDEAFSALDplIrtemqDEL------IKLQAKHQRTIVFISHD--- 224
Cdd:CHL00131 141 PSFLSRNVNEgFSGGEKKRNEILQMALLDSELAILDETDSGLD--I-----DALkiiaegINKLMTSENSIILITHYqrl 213
|
250 260
....*....|....*....|....
gi 378980240 225 LDEAmrIGDRIAIMQNGEVVQVGT 248
Cdd:CHL00131 214 LDYI--KPDYVHVMQNGKIIKTGD 235
|
|
| CBS_pair_chlorobiales |
cd09837 |
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in ... |
299-389 |
8.24e-08 |
|
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: 50.06 E-value: 8.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 299 ALKLLQDEDREYGYVIERGnRFVGIVSIDSL----KTALSAGQGIEAALIDAPLAVEAQTPLSDLLSHVGHAPCA-VPVV 373
Cdd:cd09837 16 VLAFMQAKELSCAPVLHDG-RYVAMVTLADLlparQGTPTAGLKLGELSLEEVGSIGPHEHLFDLFSRLALFPCSiIPVS 94
|
90
....*....|....*.
gi 378980240 374 DEEQQYIGIISKRMLL 389
Cdd:cd09837 95 DEDGRYIGVVSKKRVL 110
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
45-247 |
3.20e-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: 50.32 E-value: 3.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 45 KDASLAIEEGEIFVIMGLSGSGKSTMVRLL-NRLIEPTR-GQVLIDGvdiakmsdaelrevrrKKIAMVFQ-SFALMPHM 121
Cdd:cd03232 24 NNISGYVKPGTLTALMGESGAGKTTLLDVLaGRKTAGVItGEILING----------------RPLDKNFQrSTGYVEQQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 122 SVLdntafgmalagvpaaEREQKAREALRqvglenyAHAWPDELSGGMRQRVGLARALAINPDILLMDEAFSALDP---- 197
Cdd:cd03232 88 DVH---------------SPNLTVREALR-------FSALLRGLSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSqaay 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 378980240 198 -LIRtemqdeLIKLQAKHQRTIVFISH----DLDEAMrigDRIAIMQ-NGEVVQVG 247
Cdd:cd03232 146 nIVR------FLKKLADSGQAILCTIHqpsaSIFEKF---DRLLLLKrGGKTVYFG 192
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
51-239 |
3.78e-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: 3.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 51 IEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAkmsdaelreVRRKKIamvfqsfalmphmsvldntafg 130
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITPV---------YKPQYI---------------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 131 malagvpaaereqkarealrqvglenyahawpdELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELIKL 210
Cdd:cd03222 71 ---------------------------------DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRL 117
|
170 180
....*....|....*....|....*....
gi 378980240 211 QAKHQRTIVFISHDLDEAMRIGDRIAIMQ 239
Cdd:cd03222 118 SEEGKKTALVVEHDLAVLDYLSDRIHVFE 146
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
45-224 |
4.88e-07 |
|
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: 51.86 E-value: 4.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 45 KDASLAIEEGEIFVIMGLSGSGKSTMVRLLNrlieptrgqvlidGVDiaKMSDAELREVRRKKIAMVFQSFALMPHMSVL 124
Cdd:TIGR03719 22 KDISLSFFPGAKIGVLGLNGAGKSTLLRIMA-------------GVD--KDFNGEARPQPGIKVGYLPQEPQLDPTKTVR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 125 DNTAFGM--------------ALAGVPAAEREQKAREalrQVGLEN---YAHAW---------------PD------ELS 166
Cdd:TIGR03719 87 ENVEEGVaeikdaldrfneisAKYAEPDADFDKLAAE---QAELQEiidAADAWdldsqleiamdalrcPPwdadvtKLS 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 378980240 167 GGMRQRVGLARALAINPDILLMDEAFSALDplirTEMQDELIKLQAKHQRTIVFISHD 224
Cdd:TIGR03719 164 GGERRRVALCRLLLSKPDMLLLDEPTNHLD----AESVAWLERHLQEYPGTVVAVTHD 217
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
14-225 |
5.27e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 51.73 E-value: 5.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 14 FGEHPHRAFKyiekglNKAQILEKTGLSLGVKDASLAIEEGEIFV-----IMGLSGSGKSTMVRLLNRLIEPTRGQVLID 88
Cdd:PRK13409 326 FEERPPRDES------ERETLVEYPDLTKKLGDFSLEVEGGEIYEgevigIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 89 gVDIA-------KMSDAELREVRRkKIAMVFQSfalmphmSVLDNtafgmalagvpaaereqkarEALRQVGLENYAHAW 161
Cdd:PRK13409 400 -LKISykpqyikPDYDGTVEDLLR-SITDDLGS-------SYYKS--------------------EIIKPLQLERLLDKN 450
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 378980240 162 PDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELIKLQAKHQRTIVFISHDL 225
Cdd:PRK13409 451 VKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAEEREATALVVDHDI 514
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
52-225 |
5.47e-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: 50.44 E-value: 5.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 52 EEGEIFVIMGLSGSGKSTMVRLL-----------------NRLIEPTRGQVLIDGvdIAKMSDAELREVRRKkiamvfQS 114
Cdd:cd03236 24 REGQVLGLVGPNGIGKSTALKILagklkpnlgkfddppdwDEILDEFRGSELQNY--FTKLLEGDVKVIVKP------QY 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 115 FALMPhmsvldNTAFGMALAGVPAAEREQKAREALRQVGLENYAHAWPDELSGGMRQRVGLARALAINPDILLMDEAFSA 194
Cdd:cd03236 96 VDLIP------KAVKGKVGELLKKKDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSY 169
|
170 180 190
....*....|....*....|....*....|.
gi 378980240 195 LDPLIRTEMQdELIKLQAKHQRTIVFISHDL 225
Cdd:cd03236 170 LDIKQRLNAA-RLIRELAEDDNYVLVVEHDL 199
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
44-198 |
9.11e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 49.18 E-value: 9.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKMsdaelREVRRKKIAMVFQSFALMPHMSV 123
Cdd:PRK13540 17 LQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKD-----LCTYQKQLCFVGHRSGINPYLTL 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 378980240 124 LDNTAFGMALAGVpaaerEQKAREALRQVGLENYAHAWPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPL 198
Cdd:PRK13540 92 RENCLYDIHFSPG-----AVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDEL 161
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
54-241 |
9.62e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 51.26 E-value: 9.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 54 GEIFVIMGLSGSGKSTmvrLLNRLIEPTRGQVLIDGVDIakMSDAELREVRRKKIAMVFQSFALMPHMSVLDNTAFGMAL 133
Cdd:TIGR00956 789 GTLTALMGASGAGKTT---LLNVLAERVTTGVITGGDRL--VNGRPLDSSFQRSIGYVQQQDLHLPTSTVRESLRFSAYL 863
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 134 ---AGVPAAEREQKAREALRQVGLENYAHAW---PDE-LSGGMRQRVGLARALAINPDILL-MDEAFSALDPliRTE--- 202
Cdd:TIGR00956 864 rqpKSVSKSEKMEYVEEVIKLLEMESYADAVvgvPGEgLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLDS--QTAwsi 941
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 378980240 203 MQdeLIKLQAKHQRTIVFISH----DLDEAMrigDRIAIMQNG 241
Cdd:TIGR00956 942 CK--LMRKLADHGQAILCTIHqpsaILFEEF---DRLLLLQKG 979
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
44-223 |
1.09e-06 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 50.52 E-value: 1.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIePTRGQVLIdgvdiakmsdaelrEVRRKKIAMVFQSfalmPHMS- 122
Cdd:TIGR00954 468 IESLSFEVPSGNNLLICGPNGCGKSSLFRILGELW-PVYGGRLT--------------KPAKGKLFYVPQR----PYMTl 528
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 123 -------VLDNTAFGMALAGVPAAEREQKAREA------LRQVGLENYAHaWPDELSGGMRQRVGLARALAINPDILLMD 189
Cdd:TIGR00954 529 gtlrdqiIYPDSSEDMKRRGLSDKDLEQILDNVqlthilEREGGWSAVQD-WMDVLSGGEKQRIAMARLFYHKPQFAILD 607
|
170 180 190
....*....|....*....|....*....|....
gi 378980240 190 EAFSALDPlirtEMQDELIKLQAKHQRTIVFISH 223
Cdd:TIGR00954 608 ECTSAVSV----DVEGYMYRLCREFGITLFSVSH 637
|
|
| COG3448 |
COG3448 |
CBS-domain-containing membrane protein [Signal transduction mechanisms]; |
276-399 |
1.23e-06 |
|
CBS-domain-containing membrane protein [Signal transduction mechanisms];
Pssm-ID: 442671 [Multi-domain] Cd Length: 136 Bit Score: 47.55 E-value: 1.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 276 AKDIARRSPVGLIRKTPgfgPRSALKLLqdedREYGY----VIERGNRFVGIVSIDSLKTALSAGQGIEAALIDAPLAVE 351
Cdd:COG3448 4 VRDIMTRDVVTVSPDTT---LREALELM----REHGIrglpVVDEDGRLVGIVTERDLLRALLPDRLDELEERLLDLPVE 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 378980240 352 -----------AQTPLSDLL-----SHVGHapcaVPVVDEEQQYIGIISKRMLLQALDREGVNH 399
Cdd:COG3448 77 dvmtrpvvtvtPDTPLEEAAelmleHGIHR----LPVVDDDGRLVGIVTRTDLLRALARLLEEE 136
|
|
| YtoI |
COG4109 |
Predicted transcriptional regulator containing CBS domains [Transcription]; |
313-392 |
1.83e-06 |
|
Predicted transcriptional regulator containing CBS domains [Transcription];
Pssm-ID: 443285 [Multi-domain] Cd Length: 135 Bit Score: 46.83 E-value: 1.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 313 VIERGNRFVGIVSIDSLKTALSAGQgIEAALIDAPLAVEAQTPL---SDLLSHVGHApcAVPVVDEEQQYIGIISKRMLL 389
Cdd:COG4109 53 VVDENGRLVGIVTSKDILGKDDDTP-IEDVMTKNPITVTPDTSLasaAHKMIWEGIE--LLPVVDDDGRLLGIISRQDVL 129
|
...
gi 378980240 390 QAL 392
Cdd:COG4109 130 KAL 132
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
46-223 |
2.29e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 47.94 E-value: 2.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 46 DASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKmsdaelreVRRKKIAMVFQSFALMPHMSVLD 125
Cdd:PRK13541 18 DLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINN--------IAKPYCTYIGHNLGLKLEMTVFE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 126 NTAFGM----ALAGVPAAEREQKAREALRQvglENYAhawpdeLSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRt 201
Cdd:PRK13541 90 NLKFWSeiynSAETLYAAIHYFKLHDLLDE---KCYS------LSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENR- 159
|
170 180
....*....|....*....|..
gi 378980240 202 EMQDELIKLQAKHQRTIVFISH 223
Cdd:PRK13541 160 DLLNNLIVMKANSGGIVLLSSH 181
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
50-225 |
5.41e-06 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 48.27 E-value: 5.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 50 AIEEGEIFVIMGLSGSGKSTMVRLLNRLIEP----TRGQVLIDGVdIAKMSDAEL----REVRRKKIAMVF--QSFALMP 119
Cdd:PRK13409 95 IPKEGKVTGILGPNGIGKTTAVKILSGELIPnlgdYEEEPSWDEV-LKRFRGTELqnyfKKLYNGEIKVVHkpQYVDLIP 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 120 hmSVLDNTAfGMALAGVPaaEREqKAREALRQVGLENYAHAWPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLI 199
Cdd:PRK13409 174 --KVFKGKV-RELLKKVD--ERG-KLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRQ 247
|
170 180
....*....|....*....|....*.
gi 378980240 200 RTEMQDeLIKLQAKhQRTIVFISHDL 225
Cdd:PRK13409 248 RLNVAR-LIRELAE-GKYVLVVEHDL 271
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
18-253 |
7.20e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 48.18 E-value: 7.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 18 PHRAFKYIEKGLNKAQILEKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIE----PTRGQVLIDGVDIA 93
Cdd:TIGR00956 51 PNALLKILTRGFRKLKKFRDTKTFDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASNTDgfhiGVEGVITYDGITPE 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 94 KMsdaelreVRRKKIAMVFQSFA--LMPHMSVLDNTAFGMALAGV---PAAEREQKAREALRQVGLENY--AHAWP---- 162
Cdd:TIGR00956 131 EI-------KKHYRGDVVYNAETdvHFPHLTVGETLDFAARCKTPqnrPDGVSREEYAKHIADVYMATYglSHTRNtkvg 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 163 DEL----SGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELiKLQAKHQRTIVFIS--HDLDEAMRIGDRIA 236
Cdd:TIGR00956 204 NDFvrgvSGGERKRVSIAEASLGGAKIQCWDNATRGLDSATALEFIRAL-KTSANILDTTPLVAiyQCSQDAYELFDKVI 282
|
250
....*....|....*..
gi 378980240 237 IMQNGEVVQVGTPDEIL 253
Cdd:TIGR00956 283 VLYEGYQIYFGPADKAK 299
|
|
| CBS |
COG0517 |
CBS domain [Signal transduction mechanisms]; |
297-395 |
1.27e-05 |
|
CBS domain [Signal transduction mechanisms];
Pssm-ID: 440283 [Multi-domain] Cd Length: 128 Bit Score: 44.47 E-value: 1.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 297 RSALKLLQDEDREYGYVIERGNRFVGIVSI-DSLKTALSAGQGIEAALIDA-----PLAVEAQTPLSDLLS-----HVGH 365
Cdd:COG0517 21 REALELMSEKRIGGLPVVDEDGKLVGIVTDrDLRRALAAEGKDLLDTPVSEvmtrpPVTVSPDTSLEEAAElmeehKIRR 100
|
90 100 110
....*....|....*....|....*....|
gi 378980240 366 apcaVPVVDEEQQYIGIISKRMLLQALDRE 395
Cdd:COG0517 101 ----LPVVDDDGRLVGIITIKDLLKALLEP 126
|
|
| COG2524 |
COG2524 |
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription]; |
297-392 |
1.53e-05 |
|
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];
Pssm-ID: 442013 [Multi-domain] Cd Length: 206 Bit Score: 45.64 E-value: 1.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 297 RSALKLLQDEDREYGYVIErGNRFVGIVSIDSLKTALSAGQGIEAALIDA-----PLAVEAQTPLSDLLSH-VGHAPCAV 370
Cdd:COG2524 106 EEALELMLEKGISGLPVVD-DGKLVGIITERDLLKALAEGRDLLDAPVSDimtrdVVTVSEDDSLEEALRLmLEHGIGRL 184
|
90 100
....*....|....*....|..
gi 378980240 371 PVVDEEQQYIGIISKRMLLQAL 392
Cdd:COG2524 185 PVVDDDGKLVGIITRTDILRAL 206
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
59-224 |
1.67e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 47.16 E-value: 1.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 59 IMGLSGSGKSTMVRLLNRLIEPTRGQVLidgvdiakmsdaelrevRRKKIAM-VFQSFalmpHMSVLD---NTAFGMA-- 132
Cdd:PLN03073 540 MVGPNGIGKSTILKLISGELQPSSGTVF-----------------RSAKVRMaVFSQH----HVDGLDlssNPLLYMMrc 598
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 133 LAGVPaaerEQKAREALRQVGLE-NYAHAWPDELSGGMRQRVGLARALAINPDILLMDEAFSALDplirTEMQDELIKLQ 211
Cdd:PLN03073 599 FPGVP----EQKLRAHLGSFGVTgNLALQPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLD----LDAVEALIQGL 670
|
170
....*....|...
gi 378980240 212 AKHQRTIVFISHD 224
Cdd:PLN03073 671 VLFQGGVLMVSHD 683
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
50-225 |
2.06e-05 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 46.70 E-value: 2.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 50 AIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVL----IDGVdIAKMSDAEL----REVRRKKI--AMVFQSFALMP 119
Cdd:COG1245 95 VPKKGKVTGILGPNGIGKSTALKILSGELKPNLGDYDeepsWDEV-LKRFRGTELqdyfKKLANGEIkvAHKPQYVDLIP 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 120 hmSVLDNTAfGMALAGVpaAEREqKAREALRQVGLENYAHAWPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLI 199
Cdd:COG1245 174 --KVFKGTV-RELLEKV--DERG-KLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIYQ 247
|
170 180
....*....|....*....|....*.
gi 378980240 200 RTEMQdELIKLQAKHQRTIVFISHDL 225
Cdd:COG1245 248 RLNVA-RLIRELAEEGKYVLVVEHDL 272
|
|
| CBS_pair_HPP_assoc |
cd04600 |
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ... |
313-394 |
6.98e-05 |
|
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: 42.16 E-value: 6.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 313 VIERGNRFVGIVS-IDSLKTA-LSAGQGIEAALIDAPL------------------AVEAQTPLSDL---LSHVGHApcA 369
Cdd:cd04600 31 VVDRARRLVGIVTlADLLKHAdLDPPRGLRGRLRRTLGlrrdrpetvgdimtrpvvTVRPDTPIAELvplFSDGGLH--H 108
|
90 100
....*....|....*....|....*
gi 378980240 370 VPVVDEEQQYIGIISKRMLLQALDR 394
Cdd:cd04600 109 IPVVDADGRLVGIVTQSDLIAALYR 133
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
44-196 |
7.91e-05 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 44.01 E-value: 7.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLL--NRLIEPTRGQVLIDGVDIAKMSDAELREvrrKKIAMVFQSFALMPHM 121
Cdd:PRK09580 17 LRGLNLEVRPGEVHAIMGPNGSGKSTLSATLagREDYEVTGGTVEFKGKDLLELSPEDRAG---EGIFMAFQYPVEIPGV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 122 SvldNTAFgmaLAGVPAAEREQKAREALRQVGLENYAHA------WPDEL---------SGGMRQRVGLARALAINPDIL 186
Cdd:PRK09580 94 S---NQFF---LQTALNAVRSYRGQEPLDRFDFQDLMEEkiallkMPEDLltrsvnvgfSGGEKKRNDILQMAVLEPELC 167
|
170
....*....|
gi 378980240 187 LMDEAFSALD 196
Cdd:PRK09580 168 ILDESDSGLD 177
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
165-238 |
1.01e-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: 42.35 E-value: 1.01e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 378980240 165 LSGGMRQRVGLARALA---INPDIL-LMDEAFSALDPLiRTEMQDELIKLQAKHQRTIVFISHDLdEAMRIGDRIAIM 238
Cdd:cd03227 78 LSGGEKELSALALILAlasLKPRPLyILDEIDRGLDPR-DGQALAEAILEHLVKGAQVIVITHLP-ELAELADKLIHI 153
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
114-256 |
1.02e-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: 44.62 E-value: 1.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 114 SFALMPHMSVLDNTAFGMALAGVPaaEREQKAREALRQ----------VGLE--NYAHAwPDELSGGMRQRVGLARAL-- 179
Cdd:TIGR00630 429 SIADVSELSIREAHEFFNQLTLTP--EEKKIAEEVLKEirerlgflidVGLDylSLSRA-AGTLSGGEAQRIRLATQIgs 505
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 180 AINPDILLMDEAFSALDP-----LIRTemqdeLIKLQAKHQRTIVfISHDlDEAMRIGDRI------AIMQNGEVVQVGT 248
Cdd:TIGR00630 506 GLTGVLYVLDEPSIGLHQrdnrrLINT-----LKRLRDLGNTLIV-VEHD-EDTIRAADYVidigpgAGEHGGEVVASGT 578
|
....*...
gi 378980240 249 PDEILNNP 256
Cdd:TIGR00630 579 PEEILANP 586
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
59-224 |
1.14e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 44.39 E-value: 1.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 59 IMGLSGSGKSTMVRLLNRLIEPTRGQV-LIDGVDIAKMSDAELREVRRKKIAMvfqsfalmPHMSVLdntafgmalagvP 137
Cdd:PRK10636 343 LLGRNGAGKSTLIKLLAGELAPVSGEIgLAKGIKLGYFAQHQLEFLRADESPL--------QHLARL------------A 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 138 AAEREQKAREALRQVGLENYAHAWPDE-LSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELIKLQAkhqr 216
Cdd:PRK10636 403 PQELEQKLRDYLGGFGFQGDKVTEETRrFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIDFEG---- 478
|
....*...
gi 378980240 217 TIVFISHD 224
Cdd:PRK10636 479 ALVVVSHD 486
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
35-223 |
1.65e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 43.70 E-value: 1.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 35 LEKTGLSLG----VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLN-RLIE--PTRGQVL-----IDGVDIAKM-----SD 97
Cdd:PLN03073 180 MENFSISVGgrdlIVDASVTLAFGRHYGLVGRNGTGKTTFLRYMAmHAIDgiPKNCQILhveqeVVGDDTTALqcvlnTD 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 98 AELREVRRKKIAMVFQSFAL-MPHMSVLDNTAFGMALAGVPAAER-EQ-------------KAREALRQVGLE---NYAH 159
Cdd:PLN03073 260 IERTQLLEEEAQLVAQQRELeFETETGKGKGANKDGVDKDAVSQRlEEiykrlelidaytaEARAASILAGLSftpEMQV 339
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 378980240 160 AWPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELIKLqakhQRTIVFISH 223
Cdd:PLN03073 340 KATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKW----PKTFIVVSH 399
|
|
| CBS |
COG0517 |
CBS domain [Signal transduction mechanisms]; |
339-398 |
2.03e-04 |
|
CBS domain [Signal transduction mechanisms];
Pssm-ID: 440283 [Multi-domain] Cd Length: 128 Bit Score: 41.00 E-value: 2.03e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 378980240 339 IEAALIDAPLAVEAQTPLSDLLS-----HVGHapcaVPVVDEEQQYIGIISKRMLLQALDREGVN 398
Cdd:COG0517 3 VKDIMTTDVVTVSPDATVREALElmsekRIGG----LPVVDEDGKLVGIVTDRDLRRALAAEGKD 63
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
44-247 |
2.71e-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: 41.54 E-value: 2.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 44 VKDASLAIEEGEIFVIMGLSGSGKSTmvrLLNRLIEPTRGQVLIDGvdiakmsdaeLREVRRKKIAMVFQsfalmphMSV 123
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKST---LVNEGLYASGKARLISF----------LPKFSRNKLIFIDQ-------LQF 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 124 LDNTAFGMALAGVPAAEreqkarealrqvglenyahawpdeLSGGMRQRVGLARALAINPD--ILLMDEAFSALDPLIRT 201
Cdd:cd03238 71 LIDVGLGYLTLGQKLST------------------------LSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDIN 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 378980240 202 EMQDELIKL-QAKHqrTIVFISHDLDeAMRIGDRIAIM------QNGEVVQVG 247
Cdd:cd03238 127 QLLEVIKGLiDLGN--TVILIEHNLD-VLSSADWIIDFgpgsgkSGGKVVFSG 176
|
|
| CBS_pair_CBS |
cd04608 |
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ... |
308-389 |
4.13e-04 |
|
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the pyridoxal-phosphate (PALP) dependent enzyme domain; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the pyridoxal-phosphate (PALP) dependent enzyme domain upstream. Cystathionine beta-synthase (CBS ) contains, besides the C-terminal regulatory CBS-pair, an N-terminal heme-binding module, followed by a pyridoxal phosphate (PLP) domain, which houses the active site. It is the first enzyme in the transsulfuration pathway, catalyzing the conversion of serine and homocysteine to cystathionine and water. In general, 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: 341382 [Multi-domain] Cd Length: 120 Bit Score: 39.82 E-value: 4.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 308 REYGY----VIERGNRFVGIVSIDSLKTALSAGQG-----IEAALIDAPLAVEAQTPLSDLLSHVGHAPCAVpVVDEEQQ 378
Cdd:cd04608 29 REYGVdqlpVVDEDGRVVGMVTEGNLLSSLLAGRAqpsdpVSKAMYKQFKQVDLDTPLGALSRILERDHFAL-VVDGQGK 107
|
90
....*....|.
gi 378980240 379 YIGIISKRMLL 389
Cdd:cd04608 108 VLGIVTRIDLL 118
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
166-235 |
4.25e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 42.46 E-value: 4.25e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 378980240 166 SGGMRQRVGLARALAINPDILLMDEAFSALDplirtemQDELIKLQ---AKHQRTIVFISHDLDEAMRIGDRI 235
Cdd:PRK10636 151 SGGWRMRLNLAQALICRSDLLLLDEPTNHLD-------LDAVIWLEkwlKSYQGTLILISHDRDFLDPIVDKI 216
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
165-241 |
5.20e-04 |
|
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini.
Pssm-ID: 213246 [Multi-domain] Cd Length: 213 Bit Score: 41.10 E-value: 5.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 165 LSGGMRQRVGLARALA----------INPDILLMDEAFSALDPLIRtEMQDELIKLQAKHQRTIVFISHDLDEAMRIGDR 234
Cdd:cd03279 124 LSGGETFLASLSLALAlsevlqnrggARLEALFIDEGFGTLDPEAL-EAVATALELIRTENRMVGVISHVEELKERIPQR 202
|
....*..
gi 378980240 235 IAIMQNG 241
Cdd:cd03279 203 LEVIKTP 209
|
|
| GntK |
COG3265 |
Gluconate kinase [Carbohydrate transport and metabolism]; Gluconate kinase is part of the ... |
56-96 |
9.78e-04 |
|
Gluconate kinase [Carbohydrate transport and metabolism]; Gluconate kinase is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway
Pssm-ID: 442496 [Multi-domain] Cd Length: 164 Bit Score: 39.73 E-value: 9.78e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 378980240 56 IFVIMGLSGSGKSTMVRLL-NRLieptrGQVLIDGVD------IAKMS 96
Cdd:COG3265 3 VIVVMGVSGSGKSTVGQALaERL-----GWPFIDGDDfhppanIAKMA 45
|
|
| MgtE |
COG2239 |
Mg/Co/Ni transporter MgtE (contains CBS domain) [Inorganic ion transport and metabolism]; |
299-383 |
1.45e-03 |
|
Mg/Co/Ni transporter MgtE (contains CBS domain) [Inorganic ion transport and metabolism];
Pssm-ID: 441840 [Multi-domain] Cd Length: 443 Bit Score: 40.44 E-value: 1.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 299 ALKLL--QDEDRE---YGYVIERGNRFVGIVSIDSLKTAlSAGQGIEAALIDAPLAVEAQTPLS---------DLLshvg 364
Cdd:COG2239 151 ALRYLrrQAEDPEtiyYIYVVDDDGRLVGVVSLRDLLLA-DPDTKVSDIMDTDVISVPADDDQEevarlferyDLL---- 225
|
90
....*....|....*....
gi 378980240 365 hapcAVPVVDEEQQYIGII 383
Cdd:COG2239 226 ----ALPVVDEEGRLVGII 240
|
|
| CBS |
pfam00571 |
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ... |
347-392 |
1.94e-03 |
|
CBS domain; CBS domains are small intracellular modules that pair together to form a stable globular domain. This family represents a single CBS domain. Pairs of these domains have been termed a Bateman domain. CBS domains have been shown to bind ligands with an adenosyl group such as AMP, ATP and S-AdoMet. CBS domains are found attached to a wide range of other protein domains suggesting that CBS domains may play a regulatory role making proteins sensitive to adenosyl carrying ligands. The region containing the CBS domains in Cystathionine-beta synthase is involved in regulation by S-AdoMet. CBS domain pairs from AMPK bind AMP or ATP. The CBS domains from IMPDH and the chloride channel CLC2 bind ATP.
Pssm-ID: 425756 [Multi-domain] Cd Length: 57 Bit Score: 36.04 E-value: 1.94e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 378980240 347 PLAVEAQTPLSDLLSHVGHAPC-AVPVVDEEQQYIGIISKRMLLQAL 392
Cdd:pfam00571 9 VVTVSPDTTLEEALELMREHGIsRLPVVDEDGKLVGIVTLKDLLRAL 55
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
165-196 |
2.66e-03 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 39.72 E-value: 2.66e-03
10 20 30
....*....|....*....|....*....|..
gi 378980240 165 LSGGMRQRVGLARALAINPDILLMDEAFSALD 196
Cdd:PRK11819 164 LSGGERRRVALCRLLLEKPDMLLLDEPTNHLD 195
|
|
| CBS_pair_Mg_transporter |
cd04606 |
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the magnesium ... |
299-383 |
2.85e-03 |
|
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the magnesium transporter, MgtE; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domain in the magnesium transporter, MgtE. MgtE and its homologs are found in eubacteria, archaebacteria, and eukaryota. Members of this family transport Mg2+ or other divalent cations into the cell via two highly conserved aspartates. 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: 341380 [Multi-domain] Cd Length: 121 Bit Score: 37.31 E-value: 2.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 299 ALKLLQDEDRE-----YGYVIERGNRFVGIVSIDSLKTAlSAGQGIEAALIDAPLAVEAQTPLS---------DLLshvg 364
Cdd:cd04606 23 ALEYLRRLAPDpetiyYIYVVDEDRRLLGVVSLRDLLLA-DPDTKVSDIMDTDVISVSADDDQEevarlfakyDLL---- 97
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90
....*....|....*....
gi 378980240 365 hapcAVPVVDEEQQYIGII 383
Cdd:cd04606 98 ----ALPVVDEEGRLVGII 112
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| CBS_pair_bac |
cd04643 |
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria; ... |
359-391 |
4.26e-03 |
|
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria; 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: 341400 [Multi-domain] Cd Length: 130 Bit Score: 37.09 E-value: 4.26e-03
10 20 30
....*....|....*....|....*....|...
gi 378980240 359 LLSHVGHApcAVPVVDEEQQYIGIISKRMLLQA 391
Cdd:cd04643 24 VLTKSGYS--RIPVLDKDYKLVGLISLSMILDA 54
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| CBS_pair_ABC_OpuCA_assoc |
cd04583 |
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found associated with ... |
313-392 |
4.29e-03 |
|
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found associated with the ABC transporter OpuCA; 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: 341360 [Multi-domain] Cd Length: 110 Bit Score: 36.73 E-value: 4.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 313 VIERGNRFVGIVSIDSLKTALSAGQGIEAALIDAPLAVEAQTPLSDLLS-----HVGHapcaVPVVDEEQQYIGIISKRM 387
Cdd:cd04583 30 VVDKDNVLLGIVDIEDINRNYRKAKKVGEIMERDVFTVKEDSLLRDTVDrilkrGLKY----VPVVDEQGRLVGLVTRAS 105
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....*
gi 378980240 388 LLQAL 392
Cdd:cd04583 106 LVDIV 110
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| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
136-242 |
5.70e-03 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 38.84 E-value: 5.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378980240 136 VPAAEReQKAREALRQVGLENY-AHAWPDELSGGmRQRVGL-ARALAINPDILLMDEAFSALDPLIRTEMQ---DELIkl 210
Cdd:PRK10938 373 VSDRQQ-KLAQQWLDILGIDKRtADAPFHSLSWG-QQRLALiVRALVKHPTLLILDEPLQGLDPLNRQLVRrfvDVLI-- 448
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90 100 110
....*....|....*....|....*....|...
gi 378980240 211 qAKHQRTIVFISHDLDEAMR-IGDRIAIMQNGE 242
Cdd:PRK10938 449 -SEGETQLLFVSHHAEDAPAcITHRLEFVPDGD 480
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| CBS_pair_SF |
cd02205 |
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ... |
347-398 |
5.83e-03 |
|
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).
Pssm-ID: 341358 [Multi-domain] Cd Length: 113 Bit Score: 36.45 E-value: 5.83e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 378980240 347 PLAVEAQTPLSDLLSH-VGHAPCAVPVVDEEQQYIGIISKRMLLQALDREGVN 398
Cdd:cd02205 4 VVTVDPDTTVREALELmAENGIGALPVVDDDGKLVGIVTERDILRALVEGGLA 56
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