|
Name |
Accession |
Description |
Interval |
E-value |
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
32-600 |
2.74e-167 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 508.94 E-value: 2.74e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 32 WILMALGLIGAVGDGFITPVVVFIFNTLLNNLGTSSSnnktfMQTISKNVVALLYVACGSWVICFLEGYCWTRTGERQAA 111
Cdd:COG1132 20 RGLLILALLLLLLSALLELLLPLLLGRIIDALLAGGD-----LSALLLLLLLLLGLALLRALLSYLQRYLLARLAQRVVA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 112 RMREKYLRAVLRQDVGYFDLHvtSTSDVITSISSDSLVIQDFLSEKLPNFLMNASAFVASYIVSFILMWRLTIVGFPFII 191
Cdd:COG1132 95 DLRRDLFEHLLRLPLSFFDRR--RTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVIDWRLALIVLLVLP 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 192 LLLVPGLMYGRALVSISRKIHEQYNEAGSIAEQAISSVRTVYAFGSENKMIGKFSTALRGSVKLGLRQGLAKGI-TIGSN 270
Cdd:COG1132 173 LLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRAARLSALfFPLME 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 271 GVTHAIWAFLTWYGSRLVMNHGSKGGTVFVVISCITYGGVSLGQSLSNLKYFSEAFVAWERILEVIKRVPDIDsNKKEGQ 350
Cdd:COG1132 253 LLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLDEPPEIP-DPPGAV 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 351 ILERMKGEVEFNHVKFTYlsRPETTIFDDLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYDPIAGEILIDGVSIDKLQV 430
Cdd:COG1132 332 PLPPVRGEIEFENVSFSY--PGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTL 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 431 NWLRSQMGLVSQEPVLFATSITENILFGKEDASLDEVVEAAKASNAHTFISQFPLGYKTQVGERGVQMSGGQKQRIAIAR 510
Cdd:COG1132 410 ESLRRQIGVVPQDTFLFSGTIRENIRYGRPDATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLSGGQRQRIAIAR 489
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 511 AIIKSPKILLLDEATSALDSESERVVQESLDNASIGRTTIVIAHRLSTIRNADVICVIHNGQIVETGSHEELLKRiDGQY 590
Cdd:COG1132 490 ALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQGTHEELLAR-GGLY 568
|
570
....*....|
gi 15232977 591 TSLVSLQQME 600
Cdd:COG1132 569 ARLYRLQFGE 578
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
657-1236 |
6.76e-165 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 502.77 E-value: 6.76e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 657 SFTRLMVMNRPEWKHALYGCLSAALVGVLQPVSAYSAGSVISVFFlTSHDQikEKTRIYVLLFVGLAIFSFLVNISQHYG 736
Cdd:COG1132 8 LLRRLLRYLRPYRGLLILALLLLLLSALLELLLPLLLGRIIDALL-AGGDL--SALLLLLLLLLGLALLRALLSYLQRYL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 737 FAYMGEYLTKRIREQMLSKILTFEVNWFDidDNSSGAICSRLAKDANVVRSMVGDRMSLLVQTISAVIIACIIGLVIAWR 816
Cdd:COG1132 85 LARLAQRVVADLRRDLFEHLLRLPLSFFD--RRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVIDWR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 817 LAIVMISVQPLIVVCFYTQRVLLKSLSEKASKAQDESSKLAAEAVSNIRTITAFSSQERIIKLLKKVQEGPRRESVHRSW 896
Cdd:COG1132 163 LALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRAAR 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 897 LAGIVLGTSRSLITCTSALNFWYGGRLIADGKIVSKAFFEIFLIFVTTGRVIADAGTMTTDLARGLDAVGSVFAVLDRCT 976
Cdd:COG1132 243 LSALFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLDEPP 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 977 TIEPKnPDGYVAEKIKGQITFLNVDFAYPTRPDVVifENFSIEIDEGKSTAIVGTSGSGKSTIIGLIERFYDPLKGTVKI 1056
Cdd:COG1132 323 EIPDP-PGAVPLPPVRGEIEFENVSFSYPGDRPVL--KDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILI 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1057 DGRDIRSYHLRSLRKYISLVSQEPMLFAGTIRENIMYGgtSDKIDESEIIEAAKAANAHDFITSLSNGYDTNCGDKGVQL 1136
Cdd:COG1132 400 DGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYG--RPDATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNL 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1137 SGGQKQRIAIARAVLKNPSVLLLDEATSALDSKSERVVQDALERVMVGRTSIMIAHRLSTIQNCDMIVVLGKGKIVESGT 1216
Cdd:COG1132 478 SGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQGT 557
|
570 580
....*....|....*....|
gi 15232977 1217 HSSLLEKGptGTYFSLAGIQ 1236
Cdd:COG1132 558 HEELLARG--GLYARLYRLQ 575
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
34-1233 |
5.16e-160 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 516.50 E-value: 5.16e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 34 LMALGLIGAVGDGFITPVVVFIFNTLLNNLGTSSSNNKTfmqtisknVVALLYVACGSWVICFLEGYCWTRTGERQAARM 113
Cdd:PTZ00265 61 LLGVSFVCATISGGTLPFFVSVFGVIMKNMNLGENVNDI--------IFSLVLIGIFQFILSFISSFCMDVVTTKILKTL 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 114 REKYLRAVLRQDVGYFDLHVTS--TSDVITSISSdslvIQDFLSEKLPNFLMNASAFVASYIVSFILMWRLTIVGFPFII 191
Cdd:PTZ00265 133 KLEFLKSVFYQDGQFHDNNPGSklTSDLDFYLEQ----VNAGIGTKFITIFTYASAFLGLYIWSLFKNARLTLCITCVFP 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 192 LLLVPGLMYGRAlVSISRKIHEQYNE-AGSIAEQAISSVRTVYAFGSENKMIGKFSTALRGSVKLGLRQGLAKGITIGS- 269
Cdd:PTZ00265 209 LIYICGVICNKK-VKINKKTSLLYNNnTMSIIEEALVGIRTVVSYCGEKTILKKFNLSEKLYSKYILKANFMESLHIGMi 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 270 NGVTHAIWAFLTWYGSRLVMNHGSK--------GGTVFVVISCITYGGVSLGQSLSNLKYFSEAFVAWERILEVIKRVPD 341
Cdd:PTZ00265 288 NGFILASYAFGFWYGTRIIISDLSNqqpnndfhGGSVISILLGVLISMFMLTIILPNITEYMKSLEATNSLYEIINRKPL 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 342 IDSNKkEGQILERMKgEVEFNHVKFTYLSRPETTIFDDLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYDPIAGEILI- 420
Cdd:PTZ00265 368 VENND-DGKKLKDIK-KIQFKNVRFHYDTRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIIn 445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 421 DGVSIDKLQVNWLRSQMGLVSQEPVLFATSITENILFG--------------KEDASL---------------------- 464
Cdd:PTZ00265 446 DSHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIKYSlyslkdlealsnyyNEDGNDsqenknkrnscrakcagdlndm 525
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 465 ---------------------DEVVEAAKASNAHTFISQFPLGYKTQVGERGVQMSGGQKQRIAIARAIIKSPKILLLDE 523
Cdd:PTZ00265 526 snttdsneliemrknyqtikdSEVVDVSKKVLIHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDE 605
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 524 ATSALDSESERVVQESLDN--ASIGRTTIVIAHRLSTIRNADVICVIHNGQ----------------------------- 572
Cdd:PTZ00265 606 ATSSLDNKSEYLVQKTINNlkGNENRITIIIAHRLSTIRYANTIFVLSNRErgstvdvdiigedptkdnkennnknnkdd 685
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 573 ------------------IVETGSHEELLKRIDGQYTSLVSLQQMENEESNVNIN-------VSVTKD------------ 615
Cdd:PTZ00265 686 nnnnnnnnnnkinnagsyIIEQGTHDALMKNKNGIYYTMINNQKVSSKKSSNNDNdkdsdmkSSAYKDsergydpdemng 765
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 616 ------QVMSLSKDFKYSQHNSIGSTSSSIVTNVSDLIpnDNQPLVPSFTRLMVMNRPEWKHAL-YGCLSAALVGVLQPV 688
Cdd:PTZ00265 766 nskhenESASNKKSCKMSDENASENNAGGKLPFLRNLF--KRKPKAPNNLRIVYREIFSYKKDVtIIALSILVAGGLYPV 843
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 689 SAYSAGSVISVFF-LTSHDQIKEKTRIYVLLfvgLAIFSFLVNISQHYGFAYMGEYLTKRIREQMLSKILTFEVNWFDID 767
Cdd:PTZ00265 844 FALLYAKYVSTLFdFANLEANSNKYSLYILV---IAIAMFISETLKNYYNNVIGEKVEKTMKRRLFENILYQEISFFDQD 920
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 768 DNSSGAICSRLAKDANVVRSMVGDRMSLLVQTISAVIIACIIGLVIAWRLAIVMISVQPLIVVCFYTQRVLLKSLS-EKA 846
Cdd:PTZ00265 921 KHAPGLLSAHINRDVHLLKTGLVNNIVIFTHFIVLFLVSMVMSFYFCPIVAAVLTGTYFIFMRVFAIRARLTANKDvEKK 1000
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 847 SKAQ----------DESSK----LAAEAVSNIRTITAFSSQERIIKLLKKVQEGPRRESVHRSWLAGIVLGTSRSLITCT 912
Cdd:PTZ00265 1001 EINQpgtvfaynsdDEIFKdpsfLIQEAFYNMNTVIIYGLEDYFCNLIEKAIDYSNKGQKRKTLVNSMLWGFSQSAQLFI 1080
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 913 SALNFWYGGRLIADGKIVSKAFFEIFLIFVTTGRVIADAGTMTTDLARGLDAVGSVFAVLDRCTTIEPKNPDGYVAEK-- 990
Cdd:PTZ00265 1081 NSFAYWFGSFLIRRGTILVDDFMKSLFTFLFTGSYAGKLMSLKGDSENAKLSFEKYYPLIIRKSNIDVRDNGGIRIKNkn 1160
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 991 -IKGQITFLNVDFAYPTRPDVVIFENFSIEIDEGKSTAIVGTSGSGKSTIIGLIERFYDpLK------------------ 1051
Cdd:PTZ00265 1161 dIKGKIEIMDVNFRYISRPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYD-LKndhhivfknehtndmtne 1239
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1052 -------------------------------------GTVKIDGRDIRSYHLRSLRKYISLVSQEPMLFAGTIRENIMYG 1094
Cdd:PTZ00265 1240 qdyqgdeeqnvgmknvnefsltkeggsgedstvfknsGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFG 1319
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1095 gtSDKIDESEIIEAAKAANAHDFITSLSNGYDTNCGDKGVQLSGGQKQRIAIARAVLKNPSVLLLDEATSALDSKSERVV 1174
Cdd:PTZ00265 1320 --KEDATREDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLI 1397
|
1370 1380 1390 1400 1410 1420
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15232977 1175 QDALERV--MVGRTSIMIAHRLSTIQNCDMIVVLGK----GKIVES-GTHSSLL--EKGPTGTYFSLA 1233
Cdd:PTZ00265 1398 EKTIVDIkdKADKTIITIAHRIASIKRSDKIVVFNNpdrtGSFVQAhGTHEELLsvQDGVYKKYVKLA 1465
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
359-597 |
8.46e-138 |
|
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: 418.48 E-value: 8.46e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 359 VEFNHVKFTYLSRPETTIFDDLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYDPIAGEILIDGVSIDKLQVNWLRSQMG 438
Cdd:cd03249 1 IEFKNVSFRYPSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 439 LVSQEPVLFATSITENILFGKEDASLDEVVEAAKASNAHTFISQFPLGYKTQVGERGVQMSGGQKQRIAIARAIIKSPKI 518
Cdd:cd03249 81 LVSQEPVLFDGTIAENIRYGKPDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKI 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15232977 519 LLLDEATSALDSESERVVQESLDNASIGRTTIVIAHRLSTIRNADVICVIHNGQIVETGSHEELLKRiDGQYTSLVSLQ 597
Cdd:cd03249 161 LLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQ-KGVYAKLVKAQ 238
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
33-598 |
4.06e-134 |
|
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: 426.56 E-value: 4.06e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 33 ILMALGLIGAVGdgFITPVVV-FIFNTLLNNlgtsssNNKTFMQTIsknVVALLYVACGSWVICFLEGYCWTRTGERQAA 111
Cdd:COG2274 161 VLLASLLINLLA--LATPLFTqVVIDRVLPN------QDLSTLWVL---AIGLLLALLFEGLLRLLRSYLLLRLGQRIDL 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 112 RMREKYLRAVLRQDVGYFDLHvtSTSDVITSISsDSLVIQDFLSEKLPNFLMNASAFVASYIVSFILMWRLTIVGFPFII 191
Cdd:COG2274 230 RLSSRFFRHLLRLPLSFFESR--SVGDLASRFR-DVESIREFLTGSLLTALLDLLFVLIFLIVLFFYSPPLALVVLLLIP 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 192 LLLVPGLMYGRALVSISRKIHEQYNEAGSIAEQAISSVRTVYAFGSENKMIGKFSTALRGSVKLGLRQG-LAKGITIGSN 270
Cdd:COG2274 307 LYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETIKALGAESRFRRRWENLLAKYLNARFKLRrLSNLLSTLSG 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 271 GVTHAIWAFLTWYGSRLVMNHGSKGGTVfvvISCITYGG---VSLGQSLSNLKYFSEAFVAWERILEVIKRVPDIDSNKK 347
Cdd:COG2274 387 LLQQLATVALLWLGAYLVIDGQLTLGQL---IAFNILSGrflAPVAQLIGLLQRFQDAKIALERLDDILDLPPEREEGRS 463
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 348 EgQILERMKGEVEFNHVKFTYlSRPETTIFDDLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYDPIAGEILIDGVSIDK 427
Cdd:COG2274 464 K-LSLPRLKGDIELENVSFRY-PGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQ 541
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 428 LQVNWLRSQMGLVSQEPVLFATSITENILFGKEDASLDEVVEAAKASNAHTFISQFPLGYKTQVGERGVQMSGGQKQRIA 507
Cdd:COG2274 542 IDPASLRRQIGVVLQDVFLFSGTIRENITLGDPDATDEEIIEAARLAGLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLA 621
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 508 IARAIIKSPKILLLDEATSALDSESERVVQESLDNASIGRTTIVIAHRLSTIRNADVICVIHNGQIVETGSHEELLKRiD 587
Cdd:COG2274 622 IARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEELLAR-K 700
|
570
....*....|.
gi 15232977 588 GQYTSLVSLQQ 598
Cdd:COG2274 701 GLYAELVQQQL 711
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
995-1236 |
3.08e-131 |
|
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: 401.15 E-value: 3.08e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 995 ITFLNVDFAYPTRPDVVIFENFSIEIDEGKSTAIVGTSGSGKSTIIGLIERFYDPLKGTVKIDGRDIRSYHLRSLRKYIS 1074
Cdd:cd03249 1 IEFKNVSFRYPSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1075 LVSQEPMLFAGTIRENIMYGgtSDKIDESEIIEAAKAANAHDFITSLSNGYDTNCGDKGVQLSGGQKQRIAIARAVLKNP 1154
Cdd:cd03249 81 LVSQEPVLFDGTIAENIRYG--KPDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1155 SVLLLDEATSALDSKSERVVQDALERVMVGRTSIMIAHRLSTIQNCDMIVVLGKGKIVESGTHSSLLEKGptGTYFSLAG 1234
Cdd:cd03249 159 KILLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQK--GVYAKLVK 236
|
..
gi 15232977 1235 IQ 1236
Cdd:cd03249 237 AQ 238
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
75-594 |
3.18e-129 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 413.35 E-value: 3.18e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 75 QTISKNVVALLYVACGSWVICFLEGYCWTRTGERQAARMREKYLRAVLRQDVGYFDLHvtSTSDVITSISSDSLVIQDFL 154
Cdd:TIGR00958 198 PALASAIFFMCLLSIASSVSAGLRGGSFNYTMARINLRIREDLFRSLLRQDLGFFDEN--KTGELTSRLSSDTQTMSRSL 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 155 SEKLPNFLMNASAFVASYIVSFILMWRLTIVGFPFIILLLVPGLMYGRALVSISRKIHEQYNEAGSIAEQAISSVRTVYA 234
Cdd:TIGR00958 276 SLNVNVLLRNLVMLLGLLGFMLWLSPRLTMVTLINLPLVFLAEKVFGKRYQLLSEELQEAVAKANQVAEEALSGMRTVRS 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 235 FGSENKMIGKFSTALRGSVKLGLRQGLAKGITIGSNGVTH-AIWAFLTWYGSRLVMNHGSKGGTVfvvISCITYGgVSLG 313
Cdd:TIGR00958 356 FAAEEGEASRFKEALEETLQLNKRKALAYAGYLWTTSVLGmLIQVLVLYYGGQLVLTGKVSSGNL---VSFLLYQ-EQLG 431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 314 QSLSNLKYF----SEAFVAWERILEVIKRVPDIDSNKkeGQILERMKGEVEFNHVKFTYLSRPETTIFDDLCLKIPAGKT 389
Cdd:TIGR00958 432 EAVRVLSYVysgmMQAVGASEKVFEYLDRKPNIPLTG--TLAPLNLEGLIEFQDVSFSYPNRPDVPVLKGLTFTLHPGEV 509
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 390 VALVGGSGSGKSTVISLLQRFYDPIAGEILIDGVSIDKLQVNWLRSQMGLVSQEPVLFATSITENILFGKEDASLDEVVE 469
Cdd:TIGR00958 510 VALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGLTDTPDEEIMA 589
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 470 AAKASNAHTFISQFPLGYKTQVGERGVQMSGGQKQRIAIARAIIKSPKILLLDEATSALDSESERVVQESldNASIGRTT 549
Cdd:TIGR00958 590 AAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQES--RSRASRTV 667
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 15232977 550 IVIAHRLSTIRNADVICVIHNGQIVETGSHEELLKRiDGQYTSLV 594
Cdd:TIGR00958 668 LLIAHRLSTVERADQILVLKKGSVVEMGTHKQLMED-QGCYKHLV 711
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
75-597 |
5.45e-126 |
|
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ATP transporter that exports lipid A and to eukaryotic P-glycoproteins.
Pssm-ID: 131259 [Multi-domain] Cd Length: 576 Bit Score: 400.23 E-value: 5.45e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 75 QTISKNVVALLYVACGSWVICFLEGYCWTRTGERQAARMREKYLRAVLRQDVGYFDlhVTSTSDVITSISSDSLVIQDFL 154
Cdd:TIGR02204 55 GLLNRYFAFLLVVALVLALGTAARFYLVTWLGERVVADIRRAVFAHLISLSPSFFD--KNRSGEVVSRLTTDTTLLQSVI 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 155 SEKLPNFLMNASAFVASYIVSFILMWRLTIVGFPFIILLLVPGLMYGRALVSISRKIHEQYNEAGSIAEQAISSVRTVYA 234
Cdd:TIGR02204 133 GSSLSMALRNALMCIGGLIMMFITSPKLTSLVLLAVPLVLLPILLFGRRVRKLSRESQDRIADAGSYAGETLGAIRTVQA 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 235 FGSENKMIGKFSTALRGSVKLGlRQGLAKGITIGSNGVTHAIWAF--LTWYGSRLVMNHGSKGGTV--FVVISCITYGGV 310
Cdd:TIGR02204 213 FGHEDAERSRFGGAVEKAYEAA-RQRIRTRALLTAIVIVLVFGAIvgVLWVGAHDVIAGKMSAGTLgqFVFYAVMVAGSI 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 311 -SLGQSLSNLkyfSEAFVAWERILEVIKRVPDIDSNKKEGQILERMKGEVEFNHVKFTYLSRPETTIFDDLCLKIPAGKT 389
Cdd:TIGR02204 292 gTLSEVWGEL---QRAAGAAERLIELLQAEPDIKAPAHPKTLPVPLRGEIEFEQVNFAYPARPDQPALDGLNLTVRPGET 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 390 VALVGGSGSGKSTVISLLQRFYDPIAGEILIDGVSIDKLQVNWLRSQMGLVSQEPVLFATSITENILFGKEDASLDEVVE 469
Cdd:TIGR02204 369 VALVGPSGAGKSTLFQLLLRFYDPQSGRILLDGVDLRQLDPAELRARMALVPQDPVLFAASVMENIRYGRPDATDEEVEA 448
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 470 AAKASNAHTFISQFPLGYKTQVGERGVQMSGGQKQRIAIARAIIKSPKILLLDEATSALDSESERVVQESLDNASIGRTT 549
Cdd:TIGR02204 449 AARAAHAHEFISALPEGYDTYLGERGVTLSGGQRQRIAIARAILKDAPILLLDEATSALDAESEQLVQQALETLMKGRTT 528
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 15232977 550 IVIAHRLSTIRNADVICVIHNGQIVETGSHEELLKRiDGQYTSLVSLQ 597
Cdd:TIGR02204 529 LIIAHRLATVLKADRIVVMDQGRIVAQGTHAELIAK-GGLYARLARLQ 575
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
666-1236 |
2.99e-121 |
|
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: 391.89 E-value: 2.99e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 666 RPEWKHALYGCLSAALVGVLQPVSAYSAGSVISvFFLTSHDQikekTRIYVLL--FVGLAIFSFLVNISQHYGFAYMGEY 743
Cdd:COG2274 152 RRYRRLLLQVLLASLLINLLALATPLFTQVVID-RVLPNQDL----STLWVLAigLLLALLFEGLLRLLRSYLLLRLGQR 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 744 LTKRIREQMLSKILTFEVNWFDidDNSSGAICSRLaKDANVVRSMVgdrMSLLVQTISAVIIACIIGLVIA---WRLAIV 820
Cdd:COG2274 227 IDLRLSSRFFRHLLRLPLSFFE--SRSVGDLASRF-RDVESIREFL---TGSLLTALLDLLFVLIFLIVLFfysPPLALV 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 821 MISVQPLIV-VCFYTQRvLLKSLSEKASKAQDESSKLAAEAVSNIRTITAFSSQERIIKLLKKVQEGPRRESVHRSWLAG 899
Cdd:COG2274 301 VLLLIPLYVlLGLLFQP-RLRRLSREESEASAKRQSLLVETLRGIETIKALGAESRFRRRWENLLAKYLNARFKLRRLSN 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 900 IVLGTSRSLITCTSALNFWYGGRLIADGKI-----VSkafFEIFLifvttGRVIADAGTMTTDLARGLDAVGSV---FAV 971
Cdd:COG2274 380 LLSTLSGLLQQLATVALLWLGAYLVIDGQLtlgqlIA---FNILS-----GRFLAPVAQLIGLLQRFQDAKIALerlDDI 451
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 972 LDrcTTIEPKNPDGYV-AEKIKGQITFLNVDFAYPTRPDVVIfENFSIEIDEGKSTAIVGTSGSGKSTIIGLIERFYDPL 1050
Cdd:COG2274 452 LD--LPPEREEGRSKLsLPRLKGDIELENVSFRYPGDSPPVL-DNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPT 528
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1051 KGTVKIDGRDIRSYHLRSLRKYISLVSQEPMLFAGTIRENIMYGGTSdkIDESEIIEAAKAANAHDFITSLSNGYDTNCG 1130
Cdd:COG2274 529 SGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLGDPD--ATDEEIIEAARLAGLHDFIEALPMGYDTVVG 606
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1131 DKGVQLSGGQKQRIAIARAVLKNPSVLLLDEATSALDSKSERVVQDALERVMVGRTSIMIAHRLSTIQNCDMIVVLGKGK 1210
Cdd:COG2274 607 EGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIRLADRIIVLDKGR 686
|
570 580
....*....|....*....|....*.
gi 15232977 1211 IVESGTHSSLLEKGptGTYFSLAGIQ 1236
Cdd:COG2274 687 IVEDGTHEELLARK--GLYAELVQQQ 710
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
660-1232 |
1.15e-116 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 379.84 E-value: 1.15e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 660 RLMVMNRPEWKH---ALYGCLSAALVGVLQPvsaYSAGSVISVFFLT-SHDQIKEKTRIYVLLFVGLAIFSFLVNISqhy 735
Cdd:TIGR00958 151 RLLGLSGRDWPWlisAFVFLTLSSLGEMFIP---FYTGRVIDTLGGDkGPPALASAIFFMCLLSIASSVSAGLRGGS--- 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 736 gFAYMGEYLTKRIREQMLSKILTFEVNWFDidDNSSGAICSRLAKDANVVRSMVGDRMSLLVQTISAVIIACIIGLVIAW 815
Cdd:TIGR00958 225 -FNYTMARINLRIREDLFRSLLRQDLGFFD--ENKTGELTSRLSSDTQTMSRSLSLNVNVLLRNLVMLLGLLGFMLWLSP 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 816 RLAIVMISVQPLIvvcFYTQRVLLK---SLSEKASKAQDESSKLAAEAVSNIRTITAFSSQE----RIIKLLKKVQEGPR 888
Cdd:TIGR00958 302 RLTMVTLINLPLV---FLAEKVFGKryqLLSEELQEAVAKANQVAEEALSGMRTVRSFAAEEgeasRFKEALEETLQLNK 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 889 RESvhrswLAGIVLGTSRSLITCTSALN-FWYGGRLIADGKiVSKAFFEIFLIF-VTTGRVIADAGTMTTDLARGLDAVG 966
Cdd:TIGR00958 379 RKA-----LAYAGYLWTTSVLGMLIQVLvLYYGGQLVLTGK-VSSGNLVSFLLYqEQLGEAVRVLSYVYSGMMQAVGASE 452
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 967 SVFAVLDRCTTIEPknPDGYVAEKIKGQITFLNVDFAYPTRPDVVIFENFSIEIDEGKSTAIVGTSGSGKSTIIGLIERF 1046
Cdd:TIGR00958 453 KVFEYLDRKPNIPL--TGTLAPLNLEGLIEFQDVSFSYPNRPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNL 530
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1047 YDPLKGTVKIDGRDIRSYHLRSLRKYISLVSQEPMLFAGTIRENIMYGgtSDKIDESEIIEAAKAANAHDFITSLSNGYD 1126
Cdd:TIGR00958 531 YQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYG--LTDTPDEEIMAAAKAANAHDFIMEFPNGYD 608
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1127 TNCGDKGVQLSGGQKQRIAIARAVLKNPSVLLLDEATSALDSKSERVVQDALERvmVGRTSIMIAHRLSTIQNCDMIVVL 1206
Cdd:TIGR00958 609 TEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQESRSR--ASRTVLLIAHRLSTVERADQILVL 686
|
570 580
....*....|....*....|....*.
gi 15232977 1207 GKGKIVESGTHSSLLEKGptGTYFSL 1232
Cdd:TIGR00958 687 KKGSVVEMGTHKQLMEDQ--GCYKHL 710
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
704-1236 |
1.01e-115 |
|
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ATP transporter that exports lipid A and to eukaryotic P-glycoproteins.
Pssm-ID: 131259 [Multi-domain] Cd Length: 576 Bit Score: 372.88 E-value: 1.01e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 704 SHDQIKEKTRIYVLLFV---GLAIFSFLvnisQHYGFAYMGEYLTKRIREQMLSKILTFEVNWFDidDNSSGAICSRLAK 780
Cdd:TIGR02204 50 SKDSSGLLNRYFAFLLVvalVLALGTAA----RFYLVTWLGERVVADIRRAVFAHLISLSPSFFD--KNRSGEVVSRLTT 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 781 DANVVRSMVGDRMSLLVQTISAVIIACIIGLVIAWRLAIVMISVQPLIV--VCFYTQRVllKSLSEKASKAQDESSKLAA 858
Cdd:TIGR02204 124 DTTLLQSVIGSSLSMALRNALMCIGGLIMMFITSPKLTSLVLLAVPLVLlpILLFGRRV--RKLSRESQDRIADAGSYAG 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 859 EAVSNIRTITAFSSQE----RIIKLLKKVQEGPRRESVHRSWLAGIVLgtsrSLITCTSALNFWYGGRLIADGKIVSKAF 934
Cdd:TIGR02204 202 ETLGAIRTVQAFGHEDaersRFGGAVEKAYEAARQRIRTRALLTAIVI----VLVFGAIVGVLWVGAHDVIAGKMSAGTL 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 935 FEIFLIFVTTGRVIADAGTMTTDLARGLDAVGSVFAVLDRCTTIE-PKNPDGyVAEKIKGQITFLNVDFAYPTRPDVVIF 1013
Cdd:TIGR02204 278 GQFVFYAVMVAGSIGTLSEVWGELQRAAGAAERLIELLQAEPDIKaPAHPKT-LPVPLRGEIEFEQVNFAYPARPDQPAL 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1014 ENFSIEIDEGKSTAIVGTSGSGKSTIIGLIERFYDPLKGTVKIDGRDIRSYHLRSLRKYISLVSQEPMLFAGTIRENIMY 1093
Cdd:TIGR02204 357 DGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDGVDLRQLDPAELRARMALVPQDPVLFAASVMENIRY 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1094 GgTSDKIDEsEIIEAAKAANAHDFITSLSNGYDTNCGDKGVQLSGGQKQRIAIARAVLKNPSVLLLDEATSALDSKSERV 1173
Cdd:TIGR02204 437 G-RPDATDE-EVEAAARAAHAHEFISALPEGYDTYLGERGVTLSGGQRQRIAIARAILKDAPILLLDEATSALDAESEQL 514
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15232977 1174 VQDALERVMVGRTSIMIAHRLSTIQNCDMIVVLGKGKIVESGTHSSLLEKGptGTYFSLAGIQ 1236
Cdd:TIGR02204 515 VQQALETLMKGRTTLIIAHRLATVLKADRIVVMDQGRIVAQGTHAELIAKG--GLYARLARLQ 575
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
657-1236 |
4.42e-113 |
|
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: 365.58 E-value: 4.42e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 657 SFTRLMVMNRPEWKHALYGCLSAALVGVLQPVSAysagSVISvfFLTSHDQIKEKTRIYV---LLFVGLAIFSFLVNISQ 733
Cdd:TIGR02203 1 TFRRLWSYVRPYKAGLVLAGVAMILVAATESTLA----ALLK--PLLDDGFGGRDRSVLWwvpLVVIGLAVLRGICSFVS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 734 HYGFAYMGEYLTKRIREQMLSKILTFEVNWFDidDNSSGAICSRLAKDANVVRSMVGDRMSLLVQTISAVIIACIIGLVI 813
Cdd:TIGR02203 75 TYLLSWVSNKVVRDIRVRMFEKLLGLPVSFFD--RQPTGTLLSRITFDSEQVASAATDAFIVLVRETLTVIGLFIVLLYY 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 814 AWRLAIVMISVQPLIVVCFYTQRVLLKSLSEKASKAQDESSKLAAEAVSNIRTITAFSSQERIIKLLKKVQEGPRRESVH 893
Cdd:TIGR02203 153 SWQLTLIVVVMLPVLSILMRRVSKRLRRISKEIQNSMGQVTTVAEETLQGYRVVKLFGGQAYETRRFDAVSNRNRRLAMK 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 894 RSWLAGIVLGTSRSLITCTSALNFWYGGRLIADGKIVSKAFFEIFLIFVTTGRVIADAGTMTTDLARGLDAVGSVFAVLD 973
Cdd:TIGR02203 233 MTSAGSISSPITQLIASLALAVVLFIALFQAQAGSLTAGDFTAFITAMIALIRPLKSLTNVNAPMQRGLAAAESLFTLLD 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 974 rcTTIEPKnpDGYVA-EKIKGQITFLNVDFAYPTRpDVVIFENFSIEIDEGKSTAIVGTSGSGKSTIIGLIERFYDPLKG 1052
Cdd:TIGR02203 313 --SPPEKD--TGTRAiERARGDVEFRNVTFRYPGR-DRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSG 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1053 TVKIDGRDIRSYHLRSLRKYISLVSQEPMLFAGTIRENIMYGGTSDkIDESEIIEAAKAANAHDFITSLSNGYDTNCGDK 1132
Cdd:TIGR02203 388 QILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIAYGRTEQ-ADRAEIERALAAAYAQDFVDKLPLGLDTPIGEN 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1133 GVQLSGGQKQRIAIARAVLKNPSVLLLDEATSALDSKSERVVQDALERVMVGRTSIMIAHRLSTIQNCDMIVVLGKGKIV 1212
Cdd:TIGR02203 467 GVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKADRIVVMDDGRIV 546
|
570 580
....*....|....*....|....
gi 15232977 1213 ESGTHSSLLEKgpTGTYFSLAGIQ 1236
Cdd:TIGR02203 547 ERGTHNELLAR--NGLYAQLHNMQ 568
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
359-593 |
6.87e-112 |
|
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: 349.61 E-value: 6.87e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 359 VEFNHVKFTYLSRpETTIFDDLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYDPIAGEILIDGVSIDKLQVNWLRSQMG 438
Cdd:cd03251 1 VEFKNVTFRYPGD-GPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 439 LVSQEPVLFATSITENILFGKEDASLDEVVEAAKASNAHTFISQFPLGYKTQVGERGVQMSGGQKQRIAIARAIIKSPKI 518
Cdd:cd03251 80 LVSQDVFLFNDTVAENIAYGRPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15232977 519 LLLDEATSALDSESERVVQESLDNASIGRTTIVIAHRLSTIRNADVICVIHNGQIVETGSHEELLKRiDGQYTSL 593
Cdd:cd03251 160 LILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQ-GGVYAKL 233
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
314-603 |
2.05e-108 |
|
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: 354.13 E-value: 2.05e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 314 QSLSNLkyfseafvawERILEVIKRVPDIdSNKKEGQILERMKGEVEFNHVKFTYlsRPETTIFDDLCLKIPAGKTVALV 393
Cdd:COG5265 324 QALADM----------ERMFDLLDQPPEV-ADAPDAPPLVVGGGEVRFENVSFGY--DPERPILKGVSFEVPAGKTVAIV 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 394 GGSGSGKSTVISLLQRFYDPIAGEILIDGVSIDKLQVNWLRSQMGLVSQEPVLFATSITENILFGKEDASLDEVVEAAKA 473
Cdd:COG5265 391 GPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNIAYGRPDASEEEVEAAARA 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 474 SNAHTFISQFPLGYKTQVGERGVQMSGGQKQRIAIARAIIKSPKILLLDEATSALDSESERVVQESLDNASIGRTTIVIA 553
Cdd:COG5265 471 AQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGRTTLVIA 550
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 15232977 554 HRLSTIRNADVICVIHNGQIVETGSHEELLKRiDGQYTSLVSLQQMENEE 603
Cdd:COG5265 551 HRLSTIVDADEILVLEAGRIVERGTHAELLAQ-GGLYAQMWARQQEEEEA 599
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
995-1232 |
1.17e-107 |
|
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: 338.05 E-value: 1.17e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 995 ITFLNVDFAYPTRPDVVIfENFSIEIDEGKSTAIVGTSGSGKSTIIGLIERFYDPLKGTVKIDGRDIRSYHLRSLRKYIS 1074
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVL-RDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1075 LVSQEPMLFAGTIRENIMYGgtSDKIDESEIIEAAKAANAHDFITSLSNGYDTNCGDKGVQLSGGQKQRIAIARAVLKNP 1154
Cdd:cd03251 80 LVSQDVFLFNDTVAENIAYG--RPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDP 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15232977 1155 SVLLLDEATSALDSKSERVVQDALERVMVGRTSIMIAHRLSTIQNCDMIVVLGKGKIVESGTHSSLLEKGptGTYFSL 1232
Cdd:cd03251 158 PILILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQG--GVYAKL 233
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
662-978 |
3.52e-105 |
|
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1 (ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350022 [Multi-domain] Cd Length: 317 Bit Score: 334.81 E-value: 3.52e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 662 MVMNRPEWKHALYGCLSAALVGVLQPVSAYSAGSVISVFFLTSHDQIKEKTRIYVLLFVGLAIFSFLVNISQHYGFAYMG 741
Cdd:cd18578 1 LKLNKPEWPLLLLGLIGAIIAGAVFPVFAILFSKLISVFSLPDDDELRSEANFWALMFLVLAIVAGIAYFLQGYLFGIAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 742 EYLTKRIREQMLSKILTFEVNWFDIDDNSSGAICSRLAKDANVVRSMVGDRMSLLVQTISAVIIACIIGLVIAWRLAIVM 821
Cdd:cd18578 81 ERLTRRLRKLAFRAILRQDIAWFDDPENSTGALTSRLSTDASDVRGLVGDRLGLILQAIVTLVAGLIIAFVYGWKLALVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 822 ISVQPLIVVCFYTQRVLLKSLSEKASKAQDESSKLAAEAVSNIRTITAFSSQERIIKLLKKVQEGPRRESVHRSWLAGIV 901
Cdd:cd18578 161 LATVPLLLLAGYLRMRLLSGFEEKNKKAYEESSKIASEAVSNIRTVASLTLEDYFLEKYEEALEEPLKKGLRRALISGLG 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15232977 902 LGTSRSLITCTSALNFWYGGRLIADGKIVSKAFFEIFLIFVTTGRVIADAGTMTTDLARGLDAVGSVFAVLDRCTTI 978
Cdd:cd18578 241 FGLSQSLTFFAYALAFWYGGRLVANGEYTFEQFFIVFMALIFGAQSAGQAFSFAPDIAKAKAAAARIFRLLDRKPEI 317
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
32-597 |
4.26e-105 |
|
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: 344.01 E-value: 4.26e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 32 WILMALGLIGAVGDGFITPVVVFIFNTLLNnlGTSSSNNKTFMQTISKNVVaLLYVACGswvIC-FLEGYCWTRTGERQA 110
Cdd:TIGR02203 13 KAGLVLAGVAMILVAATESTLAALLKPLLD--DGFGGRDRSVLWWVPLVVI-GLAVLRG---ICsFVSTYLLSWVSNKVV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 111 ARMREKYLRAVLRQDVGYFDLHVTSTsdVITSISSDSLVIQDFLSEKLPNFLMNASAFVASYIVSFILMWRLTIvgfpfI 190
Cdd:TIGR02203 87 RDIRVRMFEKLLGLPVSFFDRQPTGT--LLSRITFDSEQVASAATDAFIVLVRETLTVIGLFIVLLYYSWQLTL-----I 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 191 ILLLVP---GLM--YGRALVSISRKIHEQYNEAGSIAEQAISSVRTVYAFGSENKMIGKFSTALRGSVKLGLRQGLAKGI 265
Cdd:TIGR02203 160 VVVMLPvlsILMrrVSKRLRRISKEIQNSMGQVTTVAEETLQGYRVVKLFGGQAYETRRFDAVSNRNRRLAMKMTSAGSI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 266 T------IGSNGVTHAIWAFLtwygSRLVMNHGSKGGTVFVVISCITYggVSLGQSLSNLKY-FSEAFVAWERILEVIKR 338
Cdd:TIGR02203 240 SspitqlIASLALAVVLFIAL----FQAQAGSLTAGDFTAFITAMIAL--IRPLKSLTNVNApMQRGLAAAESLFTLLDS 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 339 VPDIDSNKKEgqiLERMKGEVEFNHVKFTYLSRpETTIFDDLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYDPIAGEI 418
Cdd:TIGR02203 314 PPEKDTGTRA---IERARGDVEFRNVTFRYPGR-DRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQI 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 419 LIDGVSIDKLQVNWLRSQMGLVSQEPVLFATSITENILFGK-EDASLDEVVEAAKASNAHTFISQFPLGYKTQVGERGVQ 497
Cdd:TIGR02203 390 LLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIAYGRtEQADRAEIERALAAAYAQDFVDKLPLGLDTPIGENGVL 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 498 MSGGQKQRIAIARAIIKSPKILLLDEATSALDSESERVVQESLDNASIGRTTIVIAHRLSTIRNADVICVIHNGQIVETG 577
Cdd:TIGR02203 470 LSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKADRIVVMDDGRIVERG 549
|
570 580
....*....|....*....|
gi 15232977 578 SHEELLKRiDGQYTSLVSLQ 597
Cdd:TIGR02203 550 THNELLAR-NGLYAQLHNMQ 568
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
359-597 |
1.37e-103 |
|
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: 327.26 E-value: 1.37e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 359 VEFNHVKFTYlsRPETTIFDDLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYDPIAGEILIDGVSIDKLQVNWLRSQMG 438
Cdd:cd03253 1 IEFENVTFAY--DPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 439 LVSQEPVLFATSITENILFGKEDASLDEVVEAAKASNAHTFISQFPLGYKTQVGERGVQMSGGQKQRIAIARAIIKSPKI 518
Cdd:cd03253 79 VVPQDTVLFNDTIGYNIRYGRPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPI 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15232977 519 LLLDEATSALDSESERVVQESLDNASIGRTTIVIAHRLSTIRNADVICVIHNGQIVETGSHEELLKRiDGQYTSLVSLQ 597
Cdd:cd03253 159 LLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAK-GGLYAEMWKAQ 236
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
968-1237 |
1.28e-100 |
|
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: 332.55 E-value: 1.28e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 968 VFAVLDRctTIEPKNPDGYVAEKIK-GQITFLNVDFAY-PTRPdvvIFENFSIEIDEGKSTAIVGTSGSGKSTIIGLIER 1045
Cdd:COG5265 332 MFDLLDQ--PPEVADAPDAPPLVVGgGEVRFENVSFGYdPERP---ILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFR 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1046 FYDPLKGTVKIDGRDIRSYHLRSLRKYISLVSQEPMLFAGTIRENIMYGgtSDKIDESEIIEAAKAANAHDFITSLSNGY 1125
Cdd:COG5265 407 FYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNIAYG--RPDASEEEVEAAARAAQIHDFIESLPDGY 484
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1126 DTNCGDKGVQLSGGQKQRIAIARAVLKNPSVLLLDEATSALDSKSERVVQDALERVMVGRTSIMIAHRLSTIQNCDMIVV 1205
Cdd:COG5265 485 DTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGRTTLVIAHRLSTIVDADEILV 564
|
250 260 270
....*....|....*....|....*....|..
gi 15232977 1206 LGKGKIVESGTHSSLLEKGptGTYFSLAGIQR 1237
Cdd:COG5265 565 LEAGRIVERGTHAELLAQG--GLYAQMWARQQ 594
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
995-1236 |
2.04e-99 |
|
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: 315.71 E-value: 2.04e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 995 ITFLNVDFAY-PTRPdvvIFENFSIEIDEGKSTAIVGTSGSGKSTIIGLIERFYDPLKGTVKIDGRDIRSYHLRSLRKYI 1073
Cdd:cd03253 1 IEFENVTFAYdPGRP---VLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1074 SLVSQEPMLFAGTIRENIMYGgTSDKIDEsEIIEAAKAANAHDFITSLSNGYDTNCGDKGVQLSGGQKQRIAIARAVLKN 1153
Cdd:cd03253 78 GVVPQDTVLFNDTIGYNIRYG-RPDATDE-EVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKN 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1154 PSVLLLDEATSALDSKSERVVQDALERVMVGRTSIMIAHRLSTIQNCDMIVVLGKGKIVESGTHSSLLEKGptGTYFSLA 1233
Cdd:cd03253 156 PPILLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKG--GLYAEMW 233
|
...
gi 15232977 1234 GIQ 1236
Cdd:cd03253 234 KAQ 236
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
660-1225 |
1.43e-95 |
|
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: 317.47 E-value: 1.43e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 660 RLMVMNRPEWKHALYGCLSAALVGVLQPVSAYSAGSVISVFFLtsHDQIKEKTRIYVLLFVGLAIFSFLVN-ISQHYGFA 738
Cdd:COG4988 7 RLKRLARGARRWLALAVLLGLLSGLLIIAQAWLLASLLAGLII--GGAPLSALLPLLGLLLAVLLLRALLAwLRERAAFR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 739 YmGEYLTKRIREQMLSKILTFEVNWfdIDDNSSGAICSRLAKDanvVRSMVGDRMSLLVQTISAVIIACIIGLVIA---W 815
Cdd:COG4988 85 A-AARVKRRLRRRLLEKLLALGPAW--LRGKSTGELATLLTEG---VEALDGYFARYLPQLFLAALVPLLILVAVFpldW 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 816 RLAIVMISVQPLIVVcFYtqrVLLKSLSEKASKAQ-DESSKLAA---EAVSNIRTITAFSSQERIIKLLKKVQEGPRRE- 890
Cdd:COG4988 159 LSGLILLVTAPLIPL-FM---ILVGKGAAKASRRQwRALARLSGhflDRLRGLTTLKLFGRAKAEAERIAEASEDFRKRt 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 891 -SVHR-SWLAGIVLGTSRSLITCTSALNFwyGGRLIaDGKIvskAFFEIFLIFVttgrvIA--------DAGTMTTDLAR 960
Cdd:COG4988 235 mKVLRvAFLSSAVLEFFASLSIALVAVYI--GFRLL-GGSL---TLFAALFVLL-----LApefflplrDLGSFYHARAN 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 961 GLDAVGSVFAVLDrctTIEPKNPDGYVAEKIKG--QITFLNVDFAYPTRPDVVifENFSIEIDEGKSTAIVGTSGSGKST 1038
Cdd:COG4988 304 GIAAAEKIFALLD---APEPAAPAGTAPLPAAGppSIELEDVSFSYPGGRPAL--DGLSLTIPPGERVALVGPSGAGKST 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1039 IIGLIERFYDPLKGTVKIDGRDIRSYHLRSLRKYISLVSQEPMLFAGTIRENIMYGGTSdkIDESEIIEAAKAANAHDFI 1118
Cdd:COG4988 379 LLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGRPD--ASDEELEAALEAAGLDEFV 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1119 TSLSNGYDTNCGDKGVQLSGGQKQRIAIARAVLKNPSVLLLDEATSALDSKSERVVQDALERVMVGRTSIMIAHRLSTIQ 1198
Cdd:COG4988 457 AALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLA 536
|
570 580
....*....|....*....|....*..
gi 15232977 1199 NCDMIVVLGKGKIVESGTHSSLLEKGP 1225
Cdd:COG4988 537 QADRILVLDDGRIVEQGTHEELLAKNG 563
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
993-1224 |
2.51e-94 |
|
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: 301.84 E-value: 2.51e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 993 GQITFLNVDFAYptRPDVVIFENFSIEIDEGKSTAIVGTSGSGKSTIIGLIERFYDPLKGTVKIDGRDIRSYHLRSLRKY 1072
Cdd:cd03254 1 GEIEFENVNFSY--DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1073 ISLVSQEPMLFAGTIRENIMYGgtSDKIDESEIIEAAKAANAHDFITSLSNGYDTNCGDKGVQLSGGQKQRIAIARAVLK 1152
Cdd:cd03254 79 IGVVLQDTFLFSGTIMENIRLG--RPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLR 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15232977 1153 NPSVLLLDEATSALDSKSERVVQDALERVMVGRTSIMIAHRLSTIQNCDMIVVLGKGKIVESGTHSSLLEKG 1224
Cdd:cd03254 157 DPKILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKK 228
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
357-585 |
1.31e-93 |
|
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: 299.91 E-value: 1.31e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 357 GEVEFNHVKFTYlsRPETTIFDDLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYDPIAGEILIDGVSIDKLQVNWLRSQ 436
Cdd:cd03254 1 GEIEFENVNFSY--DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 437 MGLVSQEPVLFATSITENILFGKEDASLDEVVEAAKASNAHTFISQFPLGYKTQVGERGVQMSGGQKQRIAIARAIIKSP 516
Cdd:cd03254 79 IGVVLQDTFLFSGTIMENIRLGRPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15232977 517 KILLLDEATSALDSESERVVQESLDNASIGRTTIVIAHRLSTIRNADVICVIHNGQIVETGSHEELLKR 585
Cdd:cd03254 159 KILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAK 227
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
35-332 |
2.19e-92 |
|
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1 (ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350021 [Multi-domain] Cd Length: 300 Bit Score: 299.39 E-value: 2.19e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 35 MALGLIGAVGDGFITPVVVFIFNTLLNNL---GTSSSNNKTFMQTISKNVVALLYVACGSWVICFLEGYCWTRTGERQAA 111
Cdd:cd18577 1 LIIGLLAAIAAGAALPLMTIVFGDLFDAFtdfGSGESSPDEFLDDVNKYALYFVYLGIGSFVLSYIQTACWTITGERQAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 112 RMREKYLRAVLRQDVGYFDLHvtSTSDVITSISSDSLVIQDFLSEKLPNFLMNASAFVASYIVSFILMWRLTIVGFPFII 191
Cdd:cd18577 81 RIRKRYLKALLRQDIAWFDKN--GAGELTSRLTSDTNLIQDGIGEKLGLLIQSLSTFIAGFIIAFIYSWKLTLVLLATLP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 192 LLLVPGLMYGRALVSISRKIHEQYNEAGSIAEQAISSVRTVYAFGSENKMIGKFSTALRGSVKLGLRQGLAKGITIG-SN 270
Cdd:cd18577 159 LIAIVGGIMGKLLSKYTKKEQEAYAKAGSIAEEALSSIRTVKAFGGEEKEIKRYSKALEKARKAGIKKGLVSGLGLGlLF 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15232977 271 GVTHAIWAFLTWYGSRLVMNHGSKGGTVFVVISCITYGGVSLGQSLSNLKYFSEAFVAWERI 332
Cdd:cd18577 239 FIIFAMYALAFWYGSRLVRDGEISPGDVLTVFFAVLIGAFSLGQIAPNLQAFAKARAAAAKI 300
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
717-1236 |
3.26e-92 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 308.87 E-value: 3.26e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 717 LLFVGLAIFSFLVNISQHYGFAYMGEYLTKRIREQMLSKILTFEVNWFDidDNSSGAICSRLAKDANVVRSmvgdrmsll 796
Cdd:PRK11176 69 LVVIGLMILRGITSFISSYCISWVSGKVVMTMRRRLFGHMMGMPVSFFD--KQSTGTLLSRITYDSEQVAS--------- 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 797 vQTISAVII-----ACIIGLVI-----AWRLAIVMISVQPLIVVCFYTQRVLLKSLSEKASKAQDESSKLAAEAVSNIRT 866
Cdd:PRK11176 138 -SSSGALITvvregASIIGLFImmfyySWQLSLILIVIAPIVSIAIRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKE 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 867 ITAFSSQERIIKLLKKVQEGPRRESVhrswlagivlgtsrSLITCTSalnfwyggrlIADGKIVSKAFFEI-FLIFVTTG 945
Cdd:PRK11176 217 VLIFGGQEVETKRFDKVSNRMRQQGM--------------KMVSASS----------ISDPIIQLIASLALaFVLYAASF 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 946 RVIAD---AGTMT--------------------TDLARGLDAVGSVFAVLDrcttIEPKNPDG-YVAEKIKGQITFLNVD 1001
Cdd:PRK11176 273 PSVMDtltAGTITvvfssmialmrplksltnvnAQFQRGMAACQTLFAILD----LEQEKDEGkRVIERAKGDIEFRNVT 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1002 FAYPTRpDVVIFENFSIEIDEGKSTAIVGTSGSGKSTIIGLIERFYDPLKGTVKIDGRDIRSYHLRSLRKYISLVSQEPM 1081
Cdd:PRK11176 349 FTYPGK-EVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVALVSQNVH 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1082 LFAGTIRENIMYGGTsDKIDESEIIEAAKAANAHDFITSLSNGYDTNCGDKGVQLSGGQKQRIAIARAVLKNPSVLLLDE 1161
Cdd:PRK11176 428 LFNDTIANNIAYART-EQYSREQIEEAARMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDE 506
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15232977 1162 ATSALDSKSERVVQDALERVMVGRTSIMIAHRLSTIQNCDMIVVLGKGKIVESGTHSSLLEKGptGTYFSLAGIQ 1236
Cdd:PRK11176 507 ATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAELLAQN--GVYAQLHKMQ 579
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
352-604 |
5.75e-91 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 305.73 E-value: 5.75e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 352 LERMKGEVEFNHVKFTYLSRPETtiFDDLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYDPIAGEILIDGVSIDKLQVN 431
Cdd:PRK13657 328 LGRVKGAVEFDDVSFSYDNSRQG--VEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRA 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 432 WLRSQMGLVSQEPVLFATSITENILFGKEDASLDEVVEAAKASNAHTFISQFPLGYKTQVGERGVQMSGGQKQRIAIARA 511
Cdd:PRK13657 406 SLRRNIAVVFQDAGLFNRSIEDNIRVGRPDATDEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIARA 485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 512 IIKSPKILLLDEATSALDSESERVVQESLDNASIGRTTIVIAHRLSTIRNADVICVIHNGQIVETGSHEELLKRiDGQYT 591
Cdd:PRK13657 486 LLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVESGSFDELVAR-GGRFA 564
|
250
....*....|...
gi 15232977 592 SLVSLQQMENEES 604
Cdd:PRK13657 565 ALLRAQGMLQEDE 577
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
328-585 |
7.04e-90 |
|
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: 301.68 E-value: 7.04e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 328 AWERILEVIKRvPDIDSNKKEGQILERMKGEVEFNHVKFTYLSRpeTTIFDDLCLKIPAGKTVALVGGSGSGKSTVISLL 407
Cdd:COG4988 307 AAEKIFALLDA-PEPAAPAGTAPLPAAGPPSIELEDVSFSYPGG--RPALDGLSLTIPPGERVALVGPSGAGKSTLLNLL 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 408 QRFYDPIAGEILIDGVSIDKLQVNWLRSQMGLVSQEPVLFATSITENILFGKEDASLDEVVEAAKASNAHTFISQFPLGY 487
Cdd:COG4988 384 LGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGRPDASDEELEAALEAAGLDEFVAALPDGL 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 488 KTQVGERGVQMSGGQKQRIAIARAIIKSPKILLLDEATSALDSESERVVQESLDNASIGRTTIVIAHRLSTIRNADVICV 567
Cdd:COG4988 464 DTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLAQADRILV 543
|
250
....*....|....*...
gi 15232977 568 IHNGQIVETGSHEELLKR 585
Cdd:COG4988 544 LDDGRIVEQGTHEELLAK 561
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
46-597 |
2.46e-89 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 300.78 E-value: 2.46e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 46 GFITPVVVFIFNTLLNNLGTS----------SSNNKTFMQTISKNVVALLYVACGSwviCFLEGYCWTRTGERQAARMRE 115
Cdd:PRK11176 26 GLIVAGVALILNAASDTFMLSllkpllddgfGKADRSVLKWMPLVVIGLMILRGIT---SFISSYCISWVSGKVVMTMRR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 116 KYLRAVLRQDVGYFDLHvtSTSDVITSISSDSLVIQDFLSEKLPNFLMNASAFVASYIVSFILMWRLTIvgfpfIILLLV 195
Cdd:PRK11176 103 RLFGHMMGMPVSFFDKQ--STGTLLSRITYDSEQVASSSSGALITVVREGASIIGLFIMMFYYSWQLSL-----ILIVIA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 196 PGLMYGRALVS-----ISRKIHEQYNEAGSIAEQAISSVRTVYAFGS---ENKMIGKFSTALRgsvklglRQGL----AK 263
Cdd:PRK11176 176 PIVSIAIRVVSkrfrnISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGqevETKRFDKVSNRMR-------QQGMkmvsAS 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 264 GItigSNGVTHAI----WAFLTWYGS-RLVMNHGSkGGTVFVVISCItYGGVSLGQSLSNLK-YFSEAFVAWERILEVIk 337
Cdd:PRK11176 249 SI---SDPIIQLIaslaLAFVLYAASfPSVMDTLT-AGTITVVFSSM-IALMRPLKSLTNVNaQFQRGMAACQTLFAIL- 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 338 rvpDIDSNKKEGQI-LERMKGEVEFNHVKFTYLSRpETTIFDDLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYDPIAG 416
Cdd:PRK11176 323 ---DLEQEKDEGKRvIERAKGDIEFRNVTFTYPGK-EVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEG 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 417 EILIDGVSIDKLQVNWLRSQMGLVSQEPVLFATSITENILFGKEDA-SLDEVVEAAKASNAHTFISQFPLGYKTQVGERG 495
Cdd:PRK11176 399 EILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIAYARTEQySREQIEEAARMAYAMDFINKMDNGLDTVIGENG 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 496 VQMSGGQKQRIAIARAIIKSPKILLLDEATSALDSESERVVQESLDNASIGRTTIVIAHRLSTIRNADVICVIHNGQIVE 575
Cdd:PRK11176 479 VLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVEDGEIVE 558
|
570 580
....*....|....*....|..
gi 15232977 576 TGSHEELLKRiDGQYTSLVSLQ 597
Cdd:PRK11176 559 RGTHAELLAQ-NGVYAQLHKMQ 579
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
108-596 |
1.23e-87 |
|
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: 295.91 E-value: 1.23e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 108 RQAARMREKYLRAVLRQDVGYfdLHVTSTSDVITSISSDSLVIQDFLseklPNFLMNASAFVASYIVSFILMWR------ 181
Cdd:COG4987 85 RLLADLRVRLYRRLEPLAPAG--LARLRSGDLLNRLVADVDALDNLY----LRVLLPLLVALLVILAAVAFLAFfspala 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 182 LTIVGFPFIILLLVPGLMYgRALVSISRKIHEQYNEAGSIAEQAISSVRTVYAFGSENKMIGKFSTA----LRGSVKLGL 257
Cdd:COG4987 159 LVLALGLLLAGLLLPLLAA-RLGRRAGRRLAAARAALRARLTDLLQGAAELAAYGALDRALARLDAAearlAAAQRRLAR 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 258 RQGLAKGITIGSNGVthAIWAFLtWYGSRLVmNHGSKGGTVFVVISCITyggVSLGQSLSNL----KYFSEAFVAWERIL 333
Cdd:COG4987 238 LSALAQALLQLAAGL--AVVAVL-WLAAPLV-AAGALSGPLLALLVLAA---LALFEALAPLpaaaQHLGRVRAAARRLN 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 334 EVIKRVPDIDSNKKEGQILERmkGEVEFNHVKFTYLSRPETtIFDDLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYDP 413
Cdd:COG4987 311 ELLDAPPAVTEPAEPAPAPGG--PSLELEDVSFRYPGAGRP-VLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDP 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 414 IAGEILIDGVSIDKLQVNWLRSQMGLVSQEPVLFATSITENILFGKEDASLDEVVEAAKASNAHTFISQFPLGYKTQVGE 493
Cdd:COG4987 388 QSGSITLGGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLARPDATDEELWAALERVGLGDWLAALPDGLDTWLGE 467
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 494 RGVQMSGGQKQRIAIARAIIKSPKILLLDEATSALDSESERVVQESLDNASIGRTTIVIAHRLSTIRNADVICVIHNGQI 573
Cdd:COG4987 468 GGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERMDRILVLEDGRI 547
|
490 500
....*....|....*....|...
gi 15232977 574 VETGSHEELLKRiDGQYTSLVSL 596
Cdd:COG4987 548 VEQGTHEELLAQ-NGRYRQLYQR 569
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
799-1233 |
2.23e-86 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 293.02 E-value: 2.23e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 799 TISAVIIACIIGLVIAWRLAIVMISVqpLIVVCFYTQRVLLKSlseKASKAQDES--SKLAA---EAVSNIRTITAFSSQ 873
Cdd:PRK13657 140 TLVALVVLLPLALFMNWRLSLVLVVL--GIVYTLITTLVMRKT---KDGQAAVEEhyHDLFAhvsDAIGNVSVVQSYNRI 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 874 ERIIKLLKKVQEgpRRESVHR---SWLAgIVLGTSRSLITCTSALNFWYGGRLIAD-----GKIVSKAFFEIFLI----- 940
Cdd:PRK13657 215 EAETQALRDIAD--NLLAAQMpvlSWWA-LASVLNRAASTITMLAILVLGAALVQKgqlrvGEVVAFVGFATLLIgrldq 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 941 ---FVTtgRVIADAGTMTtDLARGLDavgSVFAVLDRCTTIEPKNpdgyvaekIKGQITFLNVDFAYPTRPDVVifENFS 1017
Cdd:PRK13657 292 vvaFIN--QVFMAAPKLE-EFFEVED---AVPDVRDPPGAIDLGR--------VKGAVEFDDVSFSYDNSRQGV--EDVS 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1018 IEIDEGKSTAIVGTSGSGKSTIIGLIERFYDPLKGTVKIDGRDIRSYHLRSLRKYISLVSQEPMLFAGTIRENIMYGGTs 1097
Cdd:PRK13657 356 FEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIRVGRP- 434
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1098 DKIDEsEIIEAAKAANAHDFITSLSNGYDTNCGDKGVQLSGGQKQRIAIARAVLKNPSVLLLDEATSALDSKSERVVQDA 1177
Cdd:PRK13657 435 DATDE-EMRAAAERAQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAA 513
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 15232977 1178 LERVMVGRTSIMIAHRLSTIQNCDMIVVLGKGKIVESGTHSSLLEKGptGTYFSLA 1233
Cdd:PRK13657 514 LDELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVESGSFDELVARG--GRFAALL 567
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
359-597 |
3.38e-86 |
|
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: 279.76 E-value: 3.38e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 359 VEFNHVKFTYlsRP-ETTIFDDLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYDPIAGEILIDGVSIDKLQVNWLRSQM 437
Cdd:cd03252 1 ITFEHVRFRY--KPdGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 438 GLVSQEPVLFATSITENILFGKEDASLDEVVEAAKASNAHTFISQFPLGYKTQVGERGVQMSGGQKQRIAIARAIIKSPK 517
Cdd:cd03252 79 GVVLQENVLFNRSIRDNIALADPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 518 ILLLDEATSALDSESERVVQESLDNASIGRTTIVIAHRLSTIRNADVICVIHNGQIVETGSHEELLKRiDGQYTSLVSLQ 597
Cdd:cd03252 159 ILIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAE-NGLYAYLYQLQ 237
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
991-1211 |
5.09e-83 |
|
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: 270.50 E-value: 5.09e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 991 IKGQITFLNVDFAYPTRPDVVIFENFSIEIDEGKSTAIVGTSGSGKSTIIGLIERFYDPLKGTVKIDGRDIRSYHLRSLR 1070
Cdd:cd03248 8 LKGIVKFQNVTFAYPTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLH 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1071 KYISLVSQEPMLFAGTIRENIMYGGTSDKIDEseIIEAAKAANAHDFITSLSNGYDTNCGDKGVQLSGGQKQRIAIARAV 1150
Cdd:cd03248 88 SKVSLVGQEPVLFARSLQDNIAYGLQSCSFEC--VKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARAL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15232977 1151 LKNPSVLLLDEATSALDSKSERVVQDALERVMVGRTSIMIAHRLSTIQNCDMIVVLGKGKI 1211
Cdd:cd03248 166 IRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
355-573 |
8.81e-83 |
|
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: 269.73 E-value: 8.81e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 355 MKGEVEFNHVKFTYLSRPETTIFDDLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYDPIAGEILIDGVSIDKLQVNWLR 434
Cdd:cd03248 8 LKGIVKFQNVTFAYPTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLH 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 435 SQMGLVSQEPVLFATSITENILFGKEDASLDEVVEAAKASNAHTFISQFPLGYKTQVGERGVQMSGGQKQRIAIARAIIK 514
Cdd:cd03248 88 SKVSLVGQEPVLFARSLQDNIAYGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIR 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15232977 515 SPKILLLDEATSALDSESERVVQESLDNASIGRTTIVIAHRLSTIRNADVICVIHNGQI 573
Cdd:cd03248 168 NPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
770-1232 |
2.22e-82 |
|
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: 280.88 E-value: 2.22e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 770 SSGAICSRLAKDANVVRSmvgdrmsLLVQTISAVIIACIIGLV-------IAWRLAIVMISVqpLIVVCF---YTQRVLL 839
Cdd:COG4987 110 RSGDLLNRLVADVDALDN-------LYLRVLLPLLVALLVILAavaflafFSPALALVLALG--LLLAGLllpLLAARLG 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 840 KSLSEKASKAQDESSKLAAEAVSNIRTITAFSSQERIIKLLKKVQEGPRRESVHRSWLAGIvlgtSRSLITC----TSAL 915
Cdd:COG4987 181 RRAGRRLAAARAALRARLTDLLQGAAELAAYGALDRALARLDAAEARLAAAQRRLARLSAL----AQALLQLaaglAVVA 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 916 NFWYGGRLIADGKI----------VSKAFFEIFLifvttgrVIADAGTMttdLARGLDAVGSVFAVLDRC-TTIEPKNPd 984
Cdd:COG4987 257 VLWLAAPLVAAGALsgpllallvlAALALFEALA-------PLPAAAQH---LGRVRAAARRLNELLDAPpAVTEPAEP- 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 985 gyVAEKIKGQITFLNVDFAYPTRPDVViFENFSIEIDEGKSTAIVGTSGSGKSTIIGLIERFYDPLKGTVKIDGRDIRSY 1064
Cdd:COG4987 326 --APAPGGPSLELEDVSFRYPGAGRPV-LDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDL 402
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1065 HLRSLRKYISLVSQEPMLFAGTIRENIMYGgtSDKIDESEIIEAAKAANAHDFITSLSNGYDTNCGDKGVQLSGGQKQRI 1144
Cdd:COG4987 403 DEDDLRRRIAVVPQRPHLFDTTLRENLRLA--RPDATDEELWAALERVGLGDWLAALPDGLDTWLGEGGRRLSGGERRRL 480
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1145 AIARAVLKNPSVLLLDEATSALDSKSERVVQDALERVMVGRTSIMIAHRLSTIQNCDMIVVLGKGKIVESGTHSSLLEKG 1224
Cdd:COG4987 481 ALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERMDRILVLEDGRIVEQGTHEELLAQN 560
|
....*...
gi 15232977 1225 ptGTYFSL 1232
Cdd:COG4987 561 --GRYRQL 566
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
74-597 |
2.71e-82 |
|
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 273831 [Multi-domain] Cd Length: 694 Bit Score: 284.33 E-value: 2.71e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 74 MQTISKNVVALLYVACGSWVICFLEGYCWTRTGERQAARMREKYLRAVLRQDVGYFDLHvtSTSDVITSISSdslviqdf 153
Cdd:TIGR01846 175 LSTLSVLALAMLAVAIFEPALGGLRTYLFAHLTSRIDVELGARLYRHLLGLPLGYFESR--RVGDTVARVRE-------- 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 154 lSEKLPNFLMNASAFVA---SYIVSFI-LMWRLTIVGFPFIILLLVPGLMYGRALVSISRK-IHEQYN---EAGSIAEQA 225
Cdd:TIGR01846 245 -LEQIRNFLTGSALTVVldlLFVVVFLaVMFFYSPTLTGVVIGSLVCYALLSVFVGPILRKrVEDKFErsaAATSFLVES 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 226 ISSVRTVYAFGSENKMIGKFSTALRGSVKLGlrQGLAKGITIGSNG---VTHAIWAFLTWYGSRLVMNhgskggtvfvvi 302
Cdd:TIGR01846 324 VTGIETIKATATEPQFQNRWDRQLAAYVAAS--FRVTNLGNIAGQAielIQKLTFAILLWFGAHLVIG------------ 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 303 scityGGVSLGQsLSNLKYFSEAFVA--------WERILEV---IKRVPDI-----DSNKKEGQILERMKGEVEFNHVKF 366
Cdd:TIGR01846 390 -----GALSPGQ-LVAFNMLAGRVTQpvlrlaqlWQDFQQTgiaLERLGDIlnsptEPRSAGLAALPELRGAITFENIRF 463
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 367 TYlsRPET-TIFDDLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYDPIAGEILIDGVSIDKLQVNWLRSQMGLVSQEPV 445
Cdd:TIGR01846 464 RY--APDSpEVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPAWLRRQMGVVLQENV 541
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 446 LFATSITENILFGKEDASLDEVVEAAKASNAHTFISQFPLGYKTQVGERGVQMSGGQKQRIAIARAIIKSPKILLLDEAT 525
Cdd:TIGR01846 542 LFSRSIRDNIALCNPGAPFEHVIHAAKLAGAHDFISELPQGYNTEVGEKGANLSGGQRQRIAIARALVGNPRILIFDEAT 621
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15232977 526 SALDSESERVVQESLDNASIGRTTIVIAHRLSTIRNADVICVIHNGQIVETGSHEELLkRIDGQYTSLVSLQ 597
Cdd:TIGR01846 622 SALDYESEALIMRNMREICRGRTVIIIAHRLSTVRACDRIIVLEKGQIAESGRHEELL-ALQGLYARLWQQQ 692
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
995-1236 |
2.15e-76 |
|
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: 252.41 E-value: 2.15e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 995 ITFLNVDFAYptRPD-VVIFENFSIEIDEGKSTAIVGTSGSGKSTIIGLIERFYDPLKGTVKIDGRDIRSYHLRSLRKYI 1073
Cdd:cd03252 1 ITFEHVRFRY--KPDgPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1074 SLVSQEPMLFAGTIRENIMYGGTSdkIDESEIIEAAKAANAHDFITSLSNGYDTNCGDKGVQLSGGQKQRIAIARAVLKN 1153
Cdd:cd03252 79 GVVLQENVLFNRSIRDNIALADPG--MSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHN 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1154 PSVLLLDEATSALDSKSERVVQDALERVMVGRTSIMIAHRLSTIQNCDMIVVLGKGKIVESGTHSSLLEKGptGTYFSLA 1233
Cdd:cd03252 157 PRILIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAEN--GLYAYLY 234
|
...
gi 15232977 1234 GIQ 1236
Cdd:cd03252 235 QLQ 237
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
819-1224 |
3.04e-76 |
|
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 273831 [Multi-domain] Cd Length: 694 Bit Score: 267.38 E-value: 3.04e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 819 IVMISVQPLIVVCFYTQRVLLKSLSEKASKAQDESSKLAaEAVSNIRTITAFSSQERIIKLLKKVQEGPRRESvHRSWLA 898
Cdd:TIGR01846 283 VVIGSLVCYALLSVFVGPILRKRVEDKFERSAAATSFLV-ESVTGIETIKATATEPQFQNRWDRQLAAYVAAS-FRVTNL 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 899 GIVLGTSRSLIT-CTSALNFWYGGRLIADGKIVSKAF--FEIFLIFVTtGRVIADAgTMTTDLARGLDAVGSVFAVLDrc 975
Cdd:TIGR01846 361 GNIAGQAIELIQkLTFAILLWFGAHLVIGGALSPGQLvaFNMLAGRVT-QPVLRLA-QLWQDFQQTGIALERLGDILN-- 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 976 TTIEPKnPDGYVA-EKIKGQITFLNVDFAYptRPDV-VIFENFSIEIDEGKSTAIVGTSGSGKSTIIGLIERFYDPLKGT 1053
Cdd:TIGR01846 437 SPTEPR-SAGLAAlPELRGAITFENIRFRY--APDSpEVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQ 513
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1054 VKIDGRDIRSYHLRSLRKYISLVSQEPMLFAGTIRENIMYGgtSDKIDESEIIEAAKAANAHDFITSLSNGYDTNCGDKG 1133
Cdd:TIGR01846 514 VLVDGVDLAIADPAWLRRQMGVVLQENVLFSRSIRDNIALC--NPGAPFEHVIHAAKLAGAHDFISELPQGYNTEVGEKG 591
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1134 VQLSGGQKQRIAIARAVLKNPSVLLLDEATSALDSKSERVVQDALERVMVGRTSIMIAHRLSTIQNCDMIVVLGKGKIVE 1213
Cdd:TIGR01846 592 ANLSGGQRQRIAIARALVGNPRILIFDEATSALDYESEALIMRNMREICRGRTVIIIAHRLSTVRACDRIIVLEKGQIAE 671
|
410
....*....|.
gi 15232977 1214 SGTHSSLLEKG 1224
Cdd:TIGR01846 672 SGRHEELLALQ 682
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
995-1210 |
3.43e-76 |
|
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: 249.22 E-value: 3.43e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 995 ITFLNVDFAYPTRPDVViFENFSIEIDEGKSTAIVGTSGSGKSTIIGLIERFYDPLKGTVKIDGRDIRSYHLRSLRKYIS 1074
Cdd:cd03228 1 IEFKNVSFSYPGRPKPV-LKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1075 LVSQEPMLFAGTIRENImyggtsdkideseiieaakaanahdfitslsngydtncgdkgvqLSGGQKQRIAIARAVLKNP 1154
Cdd:cd03228 80 YVPQDPFLFSGTIRENI--------------------------------------------LSGGQRQRIAIARALLRDP 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 15232977 1155 SVLLLDEATSALDSKSERVVQDALERVMVGRTSIMIAHRLSTIQNCDMIVVLGKGK 1210
Cdd:cd03228 116 PILILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
359-572 |
1.20e-75 |
|
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: 247.68 E-value: 1.20e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 359 VEFNHVKFTYLSRPETtIFDDLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYDPIAGEILIDGVSIDKLQVNWLRSQMG 438
Cdd:cd03228 1 IEFKNVSFSYPGRPKP-VLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 439 LVSQEPVLFATSITENILfgkedasldevveaakasnahtfisqfplgyktqvgergvqmSGGQKQRIAIARAIIKSPKI 518
Cdd:cd03228 80 YVPQDPFLFSGTIRENIL------------------------------------------SGGQRQRIAIARALLRDPPI 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15232977 519 LLLDEATSALDSESERVVQESLDNASIGRTTIVIAHRLSTIRNADVICVIHNGQ 572
Cdd:cd03228 118 LILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
366-1233 |
3.27e-73 |
|
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: 268.35 E-value: 3.27e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 366 FTYlSRPETTIFDDLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYDPIAGEILIDGvsidklqvnwlrsQMGLVSQEPV 445
Cdd:TIGR00957 644 FTW-ARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKG-------------SVAYVPQQAW 709
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 446 LFATSITENILFGK--EDASLDEVVEAAKASNAhtfISQFPLGYKTQVGERGVQMSGGQKQRIAIARAIIKSPKILLLDE 523
Cdd:TIGR00957 710 IQNDSLRENILFGKalNEKYYQQVLEACALLPD---LEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDD 786
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 524 ATSALDSESERVVQESL---DNASIGRTTIVIAHRLSTIRNADVICVIHNGQIVETGSHEELLKRiDGQYTSLV-----S 595
Cdd:TIGR00957 787 PLSAVDAHVGKHIFEHVigpEGVLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQR-DGAFAEFLrtyapD 865
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 596 LQQMENEESNVN-----------------INVSVTKDQVMSLSKDFKYS-----QHNSIGSTSSSIVTNVSDLIPNDNQP 653
Cdd:TIGR00957 866 EQQGHLEDSWTAlvsgegkeakliengmlVTDVVGKQLQRQLSASSSDSgdqsrHHGSSAELQKAEAKEETWKLMEADKA 945
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 654 LVPSfTRLMVMnrpeWKHA----LYGCLSAALVGVLQPVSAYSAGSVISVFfltSHDQI----KEKTRIYVLLFVGLAIF 725
Cdd:TIGR00957 946 QTGQ-VELSVY----WDYMkaigLFITFLSIFLFVCNHVSALASNYWLSLW---TDDPMvngtQNNTSLRLSVYGALGIL 1017
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 726 SFLVNISQHYGFAYMGEYLTKRIREQMLSKILTFEVNWFDidDNSSGAICSRLAKDANVVRSMVGDRMSLLVQTISAVII 805
Cdd:TIGR00957 1018 QGFAVFGYSMAVSIGGIQASRVLHQDLLHNKLRSPMSFFE--RTPSGNLVNRFSKELDTVDSMIPPVIKMFMGSLFNVIG 1095
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 806 ACIIgLVIAWRLAIVMISvqPLIVVCFYTQRVLLKS---LSEKASKAQDESSKLAAEAVSNIRTITAFSSQER-IIKLLK 881
Cdd:TIGR00957 1096 ALIV-ILLATPIAAVIIP--PLGLLYFFVQRFYVASsrqLKRLESVSRSPVYSHFNETLLGVSVIRAFEEQERfIHQSDL 1172
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 882 KVQEGPRR---ESVHRSWLAgIVLGTSRSLITCTSALNFWYGGRLIADGKIVSKAFFEIFLIFVTTGRViadagTMTTDL 958
Cdd:TIGR00957 1173 KVDENQKAyypSIVANRWLA-VRLECVGNCIVLFAALFAVISRHSLSAGLVGLSVSYSLQVTFYLNWLV-----RMSSEM 1246
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 959 ARGLDAVGSVFAVLDRCTTI-----EPKNPDGYVAekiKGQITFLNVDFAYptRPDV-VIFENFSIEIDEGKSTAIVGTS 1032
Cdd:TIGR00957 1247 ETNIVAVERLKEYSETEKEApwqiqETAPPSGWPP---RGRVEFRNYCLRY--REDLdLVLRHINVTIHGGEKVGIVGRT 1321
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1033 GSGKSTIIGLIERFYDPLKGTVKIDGRDIRSYHLRSLRKYISLVSQEPMLFAGTIRENI-MYGGTSDKidesEIIEAAKA 1111
Cdd:TIGR00957 1322 GAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNLdPFSQYSDE----EVWWALEL 1397
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1112 ANAHDFITSLSNGYDTNCGDKGVQLSGGQKQRIAIARAVLKNPSVLLLDEATSALDSKSERVVQDALERVMVGRTSIMIA 1191
Cdd:TIGR00957 1398 AHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIA 1477
|
890 900 910 920
....*....|....*....|....*....|....*....|..
gi 15232977 1192 HRLSTIQNCDMIVVLGKGKIVESGTHSSLLEKgpTGTYFSLA 1233
Cdd:TIGR00957 1478 HRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQ--RGIFYSMA 1517
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
91-595 |
2.04e-72 |
|
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: 256.41 E-value: 2.04e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 91 SWVICFLEGYCWTRTGERQAARMREKYLRAVLRQDVGYFDLHvtSTSDVITSISSDSLViQDFLSEKLPNFLMNASAFVA 170
Cdd:TIGR03796 207 QGVLTWLQLYYLRRLEIKLAVGMSARFLWHILRLPVRFFAQR--HAGDIASRVQLNDQV-AEFLSGQLATTALDAVMLVF 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 171 SYIVSFILMWRLTIVGFPFIILLLVPGLMYGRALVSISRKIHEQYNEAGSIAEQAISSVRTVYAFGSENKMIGKFS---- 246
Cdd:TIGR03796 284 YALLMLLYDPVLTLIGIAFAAINVLALQLVSRRRVDANRRLQQDAGKLTGVAISGLQSIETLKASGLESDFFSRWAgyqa 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 247 TALRGSVKLGLRQGLAKGITIGSNGVTHAIwafLTWYGSRLVMNhGSkggtvfvviscITYGGVSLGQSLsnLKYFSE-- 324
Cdd:TIGR03796 364 KLLNAQQELGVLTQILGVLPTLLTSLNSAL---ILVVGGLRVME-GQ-----------LTIGMLVAFQSL--MSSFLEpv 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 325 ----AFVAWERILEV-IKRVPDIDSNKKEGQILE------------RMKGEVEFNHVKFTYlSRPETTIFDDLCLKIPAG 387
Cdd:TIGR03796 427 nnlvGFGGTLQELEGdLNRLDDVLRNPVDPLLEEpegsaatsepprRLSGYVELRNITFGY-SPLEPPLIENFSLTLQPG 505
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 388 KTVALVGGSGSGKSTVISLLQRFYDPIAGEILIDGVSIDKLQVNWLRSQMGLVSQEPVLFATSITENI-LFgkeDASL-- 464
Cdd:TIGR03796 506 QRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIPREEIPREVLANSVAMVDQDIFLFEGTVRDNLtLW---DPTIpd 582
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 465 DEVVEAAKASNAHTFISQFPLGYKTQVGERGVQMSGGQKQRIAIARAIIKSPKILLLDEATSALDSESERVVQESLdnAS 544
Cdd:TIGR03796 583 ADLVRACKDAAIHDVITSRPGGYDAELAEGGANLSGGQRQRLEIARALVRNPSILILDEATSALDPETEKIIDDNL--RR 660
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 15232977 545 IGRTTIVIAHRLSTIRNADVICVIHNGQIVETGSHEELLKRiDGQYTSLVS 595
Cdd:TIGR03796 661 RGCTCIIVAHRLSTIRDCDEIIVLERGKVVQRGTHEELWAV-GGAYARLIR 710
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
744-1229 |
3.22e-71 |
|
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: 252.94 E-value: 3.22e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 744 LTKRIREQMLSKILTFEVNWFDidDNSSGAICSRLAKDANVVRSMVGDRMSLLVQTISAVIIAcIIGLVIAWRLAIVMIS 823
Cdd:TIGR03796 225 LAVGMSARFLWHILRLPVRFFA--QRHAGDIASRVQLNDQVAEFLSGQLATTALDAVMLVFYA-LLMLLYDPVLTLIGIA 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 824 VQPLIVVCFytqRVLLKSLSEKASKAQDESSKLAAEAVS---NIRTITAFSSQERII--------KLLKKVQEgprresv 892
Cdd:TIGR03796 302 FAAINVLAL---QLVSRRRVDANRRLQQDAGKLTGVAISglqSIETLKASGLESDFFsrwagyqaKLLNAQQE------- 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 893 hrSWLAGIVLGTSRSLITC-TSALNFWYGGRLIADGK------IVSKAFFEIFLIFVTTgrVIADAGT---MTTDLARgL 962
Cdd:TIGR03796 372 --LGVLTQILGVLPTLLTSlNSALILVVGGLRVMEGQltigmlVAFQSLMSSFLEPVNN--LVGFGGTlqeLEGDLNR-L 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 963 DAVGSvfAVLDRcTTIEPKNPDGYVAE--KIKGQITFLNVDFAY-PTRPDVVifENFSIEIDEGKSTAIVGTSGSGKSTI 1039
Cdd:TIGR03796 447 DDVLR--NPVDP-LLEEPEGSAATSEPprRLSGYVELRNITFGYsPLEPPLI--ENFSLTLQPGQRVALVGGSGSGKSTI 521
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1040 IGLIERFYDPLKGTVKIDGRDIRSYHLRSLRKYISLVSQEPMLFAGTIRENI-MYGGTsdkIDESEIIEAAKAANAHDFI 1118
Cdd:TIGR03796 522 AKLVAGLYQPWSGEILFDGIPREEIPREVLANSVAMVDQDIFLFEGTVRDNLtLWDPT---IPDADLVRACKDAAIHDVI 598
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1119 TSLSNGYDTNCGDKGVQLSGGQKQRIAIARAVLKNPSVLLLDEATSALDSKSERVVQDALERVmvGRTSIMIAHRLSTIQ 1198
Cdd:TIGR03796 599 TSRPGGYDAELAEGGANLSGGQRQRLEIARALVRNPSILILDEATSALDPETEKIIDDNLRRR--GCTCIIVAHRLSTIR 676
|
490 500 510
....*....|....*....|....*....|.
gi 15232977 1199 NCDMIVVLGKGKIVESGTHSSLLEKGptGTY 1229
Cdd:TIGR03796 677 DCDEIIVLERGKVVQRGTHEELWAVG--GAY 705
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
122-597 |
3.52e-71 |
|
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: 252.57 E-value: 3.52e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 122 LRQDVGYFDLHvtSTSDVITSISSDSlVIQDFLSEKLPNFLMNASAFVASYIVSFILMWRLTIVGFPFIILLLVPGLMYG 201
Cdd:TIGR03797 220 LRLPVSFFRQY--STGDLASRAMGIS-QIRRILSGSTLTTLLSGIFALLNLGLMFYYSWKLALVAVALALVAIAVTLVLG 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 202 RALVSISRKIHEQYNEAGSIAEQAISSVRTVYAFGSENKMIGKFSTALRGSVKLGLR-QGLAKGITIGSNG----VTHAI 276
Cdd:TIGR03797 297 LLQVRKERRLLELSGKISGLTVQLINGISKLRVAGAENRAFARWAKLFSRQRKLELSaQRIENLLTVFNAVlpvlTSAAL 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 277 WAFLTWYGSRLVMNHGSKGGtvFVVISCITYGGVSlgqSLSNLkyFSEAFVA---WERILEVIKRVPDIDSNKKEGQILe 353
Cdd:TIGR03797 377 FAAAISLLGGAGLSLGSFLA--FNTAFGSFSGAVT---QLSNT--LISILAViplWERAKPILEALPEVDEAKTDPGKL- 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 354 rmKGEVEFNHVKFTYlsRPETT-IFDDLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYDPIAGEILIDGVSIDKLQVNW 432
Cdd:TIGR03797 449 --SGAIEVDRVTFRY--RPDGPlILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAGLDVQA 524
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 433 LRSQMGLVSQEPVLFATSITENILfGKEDASLDEVVEAAKASNAHTFISQFPLGYKTQVGERGVQMSGGQKQRIAIARAI 512
Cdd:TIGR03797 525 VRRQLGVVLQNGRLMSGSIFENIA-GGAPLTLDEAWEAARMAGLAEDIRAMPMGMHTVISEGGGTLSGGQRQRLLIARAL 603
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 513 IKSPKILLLDEATSALDSESERVVQESLDNASIGRttIVIAHRLSTIRNADVICVIHNGQIVETGSHEELLKRiDGQYTS 592
Cdd:TIGR03797 604 VRKPRILLFDEATSALDNRTQAIVSESLERLKVTR--IVIAHRLSTIRNADRIYVLDAGRVVQQGTYDELMAR-EGLFAQ 680
|
....*
gi 15232977 593 LVSLQ 597
Cdd:TIGR03797 681 LARRQ 685
|
|
| chvA |
TIGR01192 |
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ... |
166-594 |
4.84e-70 |
|
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein in bacteria. It belongs to the larger ABC transporter superfamily with the characteristic ATP binding motif. The In general, this protein is in some ways implicated in osmoregulation and suggested to participate in the export of glucan from the cytoplasm to periplasm. The cyclic beta-1,2-glucan in the bactrerial periplasmic space is suggested to confer the property of high osmolority. It has also been demonstrated that mutants in this loci have lost functions of virulence and motility. It is unclear as to how virulence and osmoadaptaion are related. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 130260 [Multi-domain] Cd Length: 585 Bit Score: 246.34 E-value: 4.84e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 166 SAFVASYI---VSFILMWRLTIVgfpfIILLLVPGLMYGRALVSISRK----IHEQYNEAGSIAEQAISSVRTVYAFG-- 236
Cdd:TIGR01192 139 ATFVALFLlipTAFAMDWRLSIV----LMVLGILYILIAKLVMQRTKNgqaaVEHHYHNVFKHVSDSISNVSVVHSYNri 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 237 -SENKMIGKFSTALRGSVKLGLRQ-GLAKGITIGSNGVTHAIWAFLtwyGSRLVMNHGSKGGTVfvvISCITYGGVSLGQ 314
Cdd:TIGR01192 215 eAETSALKQFTNNLLSAQYPVLDWwALASGLNRMASTISMMCILVI---GTVLVIKGELSVGEV---IAFIGFANLLIGR 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 315 sLSNLKYFSEAFVAWERILEVIKRVPDIDSNKKE---GQILERMKGEVEFNHVKFTYLSRPETTIfdDLCLKIPAGKTVA 391
Cdd:TIGR01192 289 -LDQMSGFITQIFEARAKLEDFFDLEDSVFQREEpadAPELPNVKGAVEFRHITFEFANSSQGVF--DVSFEAKAGQTVA 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 392 LVGGSGSGKSTVISLLQRFYDPIAGEILIDGVSIDKLQVNWLRSQMGLVSQEPVLFATSITENILFGKEDASLDEVVEAA 471
Cdd:TIGR01192 366 IVGPTGAGKTTLINLLQRVYDPTVGQILIDGIDINTVTRESLRKSIATVFQDAGLFNRSIRENIRLGREGATDEEVYEAA 445
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 472 KASNAHTFISQFPLGYKTQVGERGVQMSGGQKQRIAIARAIIKSPKILLLDEATSALDSESERVVQESLDNASIGRTTIV 551
Cdd:TIGR01192 446 KAAAAHDFILKRSNGYDTLVGERGNRLSGGERQRLAIARAILKNAPILVLDEATSALDVETEARVKNAIDALRKNRTTFI 525
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 15232977 552 IAHRLSTIRNADVICVIHNGQIVETGSHEELLKRiDGQYTSLV 594
Cdd:TIGR01192 526 IAHRLSTVRNADLVLFLDQGRLIEKGSFQELIQK-DGRFYKLL 567
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
718-1206 |
9.13e-69 |
|
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: 241.04 E-value: 9.13e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 718 LFVGLAIFSFLVNIsqhygFAYMGEYLTKR--------IREQMLSKILTFEVNWfdIDDNSSGAICSRLAKDanvVRSMV 789
Cdd:TIGR02857 46 ALGALALVLLLRAL-----LGWLQERAAARaaaavksqLRERLLEAVAALGPRW--LQGRPSGELATLALEG---VEALD 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 790 GDRMSLLVQTISAVIIACIIGLVIA---WRLAIVMISVQPLIVVcFYtqrVLLKSLSEKASKAQ-DESSKLAA---EAVS 862
Cdd:TIGR02857 116 GYFARYLPQLVLAVIVPLAILAAVFpqdWISGLILLLTAPLIPI-FM---ILIGWAAQAAARKQwAALSRLSGhflDRLR 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 863 NIRTITAFSSQERIIKLLKKVQEGPRRE--SVHR-SWLAGIVLGTSRSLITCTSALNFwyGGRLIADGKIVSKAFF---- 935
Cdd:TIGR02857 192 GLPTLKLFGRAKAQAAAIRRSSEEYRERtmRVLRiAFLSSAVLELFATLSVALVAVYI--GFRLLAGDLDLATGLFvlll 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 936 --EIFLifvttgrVIADAGTMTTDLARGLDAVGSVFAVLDRCTTIEPknPDGYVAEKIKGQITFLNVDFAYPTRPDVVif 1013
Cdd:TIGR02857 270 apEFYL-------PLRQLGAQYHARADGVAAAEALFAVLDAAPRPLA--GKAPVTAAPASSLEFSGVSVAYPGRRPAL-- 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1014 ENFSIEIDEGKSTAIVGTSGSGKSTIIGLIERFYDPLKGTVKIDGRDIRSYHLRSLRKYISLVSQEPMLFAGTIRENIMY 1093
Cdd:TIGR02857 339 RPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIRL 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1094 GgTSDKiDESEIIEAAKAANAHDFITSLSNGYDTNCGDKGVQLSGGQKQRIAIARAVLKNPSVLLLDEATSALDSKSERV 1173
Cdd:TIGR02857 419 A-RPDA-SDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAE 496
|
490 500 510
....*....|....*....|....*....|...
gi 15232977 1174 VQDALERVMVGRTSIMIAHRLSTIQNCDMIVVL 1206
Cdd:TIGR02857 497 VLEALRALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
31-342 |
8.88e-68 |
|
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1 (ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350022 [Multi-domain] Cd Length: 317 Bit Score: 231.19 E-value: 8.88e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 31 DWILMALGLIGAVGDGFITPVVVFIFNTLLNNLgtSSSNNKTFMQTISKNVVALLYVACGSWVICFLEGYCWTRTGERQA 110
Cdd:cd18578 7 EWPLLLLGLIGAIIAGAVFPVFAILFSKLISVF--SLPDDDELRSEANFWALMFLVLAIVAGIAYFLQGYLFGIAGERLT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 111 ARMREKYLRAVLRQDVGYFDLHVTSTSDVITSISSDSLVIQDFLSEKLPNFLMNASAFVASYIVSFILMWRLTIVGFPFI 190
Cdd:cd18578 85 RRLRKLAFRAILRQDIAWFDDPENSTGALTSRLSTDASDVRGLVGDRLGLILQAIVTLVAGLIIAFVYGWKLALVGLATV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 191 ILLLVPGLMYGRALVSISRKIHEQYNEAGSIAEQAISSVRTVYAFGSENKMIGKFSTALRGSVKLGLRQGLAKGITIG-S 269
Cdd:cd18578 165 PLLLLAGYLRMRLLSGFEEKNKKAYEESSKIASEAVSNIRTVASLTLEDYFLEKYEEALEEPLKKGLRRALISGLGFGlS 244
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15232977 270 NGVTHAIWAFLTWYGSRLVMNHGSKGGTVFVVISCITYGGVSLGQSLSNLKYFSEAFVAWERILEVIKRVPDI 342
Cdd:cd18578 245 QSLTFFAYALAFWYGGRLVANGEYTFEQFFIVFMALIFGAQSAGQAFSFAPDIAKAKAAAARIFRLLDRKPEI 317
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
21-598 |
1.08e-67 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 251.10 E-value: 1.08e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 21 RSIFMHADgvDWILMALGLIGAvgdGFITPVVVFIF----NTLLNNLGTSSSNNKTfmqtisknVVALLYVACGSWVICF 96
Cdd:PTZ00265 818 REIFSYKK--DVTIIALSILVA---GGLYPVFALLYakyvSTLFDFANLEANSNKY--------SLYILVIAIAMFISET 884
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 97 LEGYCWTRTGERQAARMREKYLRAVLRQDVGYFDLHVTSTSDVITSISSDSLVIQDFLSEKLPNFLMNASAFVASYIVSF 176
Cdd:PTZ00265 885 LKNYYNNVIGEKVEKTMKRRLFENILYQEISFFDQDKHAPGLLSAHINRDVHLLKTGLVNNIVIFTHFIVLFLVSMVMSF 964
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 177 ----ILMWRLTIVGFPFIILLLVpglmygRALVSISRKIHEQ-YNEAGSI----------------AEQAISSVRTVYAF 235
Cdd:PTZ00265 965 yfcpIVAAVLTGTYFIFMRVFAI------RARLTANKDVEKKeINQPGTVfaynsddeifkdpsflIQEAFYNMNTVIIY 1038
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 236 GSENKMIGKFSTALRGSVKLGLRQGLAKGITIG-SNGVTHAIWAFLTWYGSRLVmnhgsKGGTV---------FVVISCI 305
Cdd:PTZ00265 1039 GLEDYFCNLIEKAIDYSNKGQKRKTLVNSMLWGfSQSAQLFINSFAYWFGSFLI-----RRGTIlvddfmkslFTFLFTG 1113
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 306 TYGGvslgqSLSNLKYFSE-AFVAWERILEVIKRVPDIDSNKKEGQILER---MKGEVEFNHVKFTYLSRPETTIFDDLC 381
Cdd:PTZ00265 1114 SYAG-----KLMSLKGDSEnAKLSFEKYYPLIIRKSNIDVRDNGGIRIKNkndIKGKIEIMDVNFRYISRPNVPIYKDLT 1188
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 382 LKIPAGKTVALVGGSGSGKSTVISLLQRFYD------------------------------------------------- 412
Cdd:PTZ00265 1189 FSCDSKKTTAIVGETGSGKSTVMSLLMRFYDlkndhhivfknehtndmtneqdyqgdeeqnvgmknvnefsltkeggsge 1268
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 413 -----PIAGEILIDGVSIDKLQVNWLRSQMGLVSQEPVLFATSITENILFGKEDASLDEVVEAAKASNAHTFISQFPLGY 487
Cdd:PTZ00265 1269 dstvfKNSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKEDATREDVKRACKFAAIDEFIESLPNKY 1348
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 488 KTQVGERGVQMSGGQKQRIAIARAIIKSPKILLLDEATSALDSESERVVQESL----DNASigRTTIVIAHRLSTIRNAD 563
Cdd:PTZ00265 1349 DTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIvdikDKAD--KTIITIAHRIASIKRSD 1426
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 15232977 564 VICVIHN----GQIVET-GSHEELLKRIDGQYTSLVSLQQ 598
Cdd:PTZ00265 1427 KIVVFNNpdrtGSFVQAhGTHEELLSVQDGVYKKYVKLAK 1466
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
366-1223 |
8.41e-67 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 248.35 E-value: 8.41e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 366 FTYLSRPETTIFDDLCLKIPAGKTVALVGGSGSGKSTVISLLqrfydpiAGEIL-IDGVSIDklqvnwLRSQMGLVSQEP 444
Cdd:PLN03232 622 FSWDSKTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAM-------LGELShAETSSVV------IRGSVAYVPQVS 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 445 VLFATSITENILFGKEDASlDEVVEAAKASNAHTFISQFPLGYKTQVGERGVQMSGGQKQRIAIARAIIKSPKILLLDEA 524
Cdd:PLN03232 689 WIFNATVRENILFGSDFES-ERYWRAIDVTALQHDLDLLPGRDLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDP 767
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 525 TSALDSESERVVQES-LDNASIGRTTIVIAHRLSTIRNADVICVIHNGQIVETGSHEELLKridgqyTSLVSLQQMENE- 602
Cdd:PLN03232 768 LSALDAHVAHQVFDScMKDELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAELSK------SGSLFKKLMENAg 841
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 603 ESNVNINVSVTKDQVMSLSKDFKYSQHN-SIGSTSSSIVTNVSDLIPNDNQPLVPSFTRLMvmnrpEWKHALYGCLsaaL 681
Cdd:PLN03232 842 KMDATQEVNTNDENILKLGPTVTIDVSErNLGSTKQGKRGRSVLVKQEERETGIISWNVLM-----RYNKAVGGLW---V 913
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 682 VGVLqpVSAYSAGSVISVF------FLTSHDQIKEKTRIYVLLFVGLAIF-SFLVNISQHYGFAYMGEYLTKRIREQMLS 754
Cdd:PLN03232 914 VMIL--LVCYLTTEVLRVSsstwlsIWTDQSTPKSYSPGFYIVVYALLGFgQVAVTFTNSFWLISSSLHAAKRLHDAMLN 991
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 755 KILTFEVNWFDIddNSSGAICSRLAKDA-----NVVRSMvGDRMSLLVQTISAVIIACIIGLVIAWrlaivmiSVQPLIV 829
Cdd:PLN03232 992 SILRAPMLFFHT--NPTGRVINRFSKDIgdidrNVANLM-NMFMNQLWQLLSTFALIGTVSTISLW-------AIMPLLI 1061
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 830 VcFYTQRVLLKSLSEKA----SKAQDESSKLAAEAVSNIRTITAFSSQERIIKLLKKVQEGPRRESV----HRSWLAGIV 901
Cdd:PLN03232 1062 L-FYAAYLYYQSTSREVrrldSVTRSPIYAQFGEALNGLSSIRAYKAYDRMAKINGKSMDNNIRFTLantsSNRWLTIRL 1140
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 902 LGTSRSLITCTSALNFWYGGRliADGKIVSKAFFEIFLIF---VTT--GRVIADAGTMTTDLaRGLDAVGSVFAVLDRCT 976
Cdd:PLN03232 1141 ETLGGVMIWLTATFAVLRNGN--AENQAGFASTMGLLLSYtlnITTllSGVLRQASKAENSL-NSVERVGNYIDLPSEAT 1217
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 977 TIEPKN--PDGYvaeKIKGQITFLNVDFAY-PTRPDVVifENFSIEIDEGKSTAIVGTSGSGKSTIIGLIERFYDPLKGT 1053
Cdd:PLN03232 1218 AIIENNrpVSGW---PSRGSIKFEDVHLRYrPGLPPVL--HGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGR 1292
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1054 VKIDGRDIRSYHLRSLRKYISLVSQEPMLFAGTIRENImyggtsDKIDE---SEIIEAAKAANAHDFITSLSNGYDTNCG 1130
Cdd:PLN03232 1293 IMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNI------DPFSEhndADLWEALERAHIKDVIDRNPFGLDAEVS 1366
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1131 DKGVQLSGGQKQRIAIARAVLKNPSVLLLDEATSALDSKSERVVQDALERVMVGRTSIMIAHRLSTIQNCDMIVVLGKGK 1210
Cdd:PLN03232 1367 EGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQ 1446
|
890
....*....|...
gi 15232977 1211 IVESGTHSSLLEK 1223
Cdd:PLN03232 1447 VLEYDSPQELLSR 1459
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
993-1215 |
2.96e-66 |
|
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: 222.85 E-value: 2.96e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 993 GQITFLNVDFAYPTRPDVVIfENFSIEIDEGKSTAIVGTSGSGKSTIIGLIERFYDPLKGTVKIDGRDIRSYHLRSLRKY 1072
Cdd:cd03245 1 GRIEFRNVSFSYPNQEIPAL-DNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1073 ISLVSQEPMLFAGTIRENIMYGGTSdkIDESEIIEAAKAANAHDFITSLSNGYDTNCGDKGVQLSGGQKQRIAIARAVLK 1152
Cdd:cd03245 80 IGYVPQDVTLFYGTLRDNITLGAPL--ADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLN 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15232977 1153 NPSVLLLDEATSALDSKSERVVQDALERVMVGRTSIMIAHRLSTIQNCDMIVVLGKGKIVESG 1215
Cdd:cd03245 158 DPPILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
357-577 |
1.06e-64 |
|
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: 218.61 E-value: 1.06e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 357 GEVEFNHVKFTYLSRPETTIfDDLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYDPIAGEILIDGVSIDKLQVNWLRSQ 436
Cdd:cd03245 1 GRIEFRNVSFSYPNQEIPAL-DNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 437 MGLVSQEPVLFATSITENILFGKEDASLDEVVEAAKASNAHTFISQFPLGYKTQVGERGVQMSGGQKQRIAIARAIIKSP 516
Cdd:cd03245 80 IGYVPQDVTLFYGTLRDNITLGAPLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15232977 517 KILLLDEATSALDSESERVVQESLDNASIGRTTIVIAHRLSTIRNADVICVIHNGQIVETG 577
Cdd:cd03245 160 PILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
674-1206 |
5.71e-64 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 239.16 E-value: 5.71e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 674 YGCLSAA---LVGVLQPVSAYSAGSV---ISVF-FLTSHDQIKEKTRIYVLLFVGLAIFSFLVNISQHYGFAYMGEYLTK 746
Cdd:PTZ00265 51 FKCLPAShrkLLGVSFVCATISGGTLpffVSVFgVIMKNMNLGENVNDIIFSLVLIGIFQFILSFISSFCMDVVTTKILK 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 747 RIREQMLSKILtFEVNWFDidDNSSGaicSRLAKDANV----VRSMVGDRMSLLVQTISAVIIACIIGLVIAWRLAIVMI 822
Cdd:PTZ00265 131 TLKLEFLKSVF-YQDGQFH--DNNPG---SKLTSDLDFyleqVNAGIGTKFITIFTYASAFLGLYIWSLFKNARLTLCIT 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 823 SVQPLIVVCFYTQRVLLKsLSEKASKAQDESS-KLAAEAVSNIRTITAFSSQERIIKLLKKVQEGPRRESVHRSWLAGIV 901
Cdd:PTZ00265 205 CVFPLIYICGVICNKKVK-INKKTSLLYNNNTmSIIEEALVGIRTVVSYCGEKTILKKFNLSEKLYSKYILKANFMESLH 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 902 LGTSRSLITCTSALNFWYGGRLIAD-------------GKIVSKAFFEIFLIFVTTgrVIADAgtmTTDLARGLDAVGSV 968
Cdd:PTZ00265 284 IGMINGFILASYAFGFWYGTRIIISdlsnqqpnndfhgGSVISILLGVLISMFMLT--IILPN---ITEYMKSLEATNSL 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 969 FAVLDRCTTIEpKNPDGYVAEKIKgQITFLNVDFAYPTRPDVVIFENFSIEIDEGKSTAIVGTSGSGKSTIIGLIERFYD 1048
Cdd:PTZ00265 359 YEIINRKPLVE-NNDDGKKLKDIK-KIQFKNVRFHYDTRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYD 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1049 PLKGTVKI-DGRDIRSYHLRSLRKYISLVSQEPMLFAGTIRENIMYGGTSDK---------------------------- 1099
Cdd:PTZ00265 437 PTEGDIIInDSHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIKYSLYSLKdlealsnyynedgndsqenknkrnscra 516
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1100 ---------------------------IDESEIIEAAKAANAHDFITSLSNGYDTNCGDKGVQLSGGQKQRIAIARAVLK 1152
Cdd:PTZ00265 517 kcagdlndmsnttdsneliemrknyqtIKDSEVVDVSKKVLIHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIR 596
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*.
gi 15232977 1153 NPSVLLLDEATSALDSKSERVVQDALERVM--VGRTSIMIAHRLSTIQNCDMIVVL 1206
Cdd:PTZ00265 597 NPKILILDEATSSLDNKSEYLVQKTINNLKgnENRITIIIAHRLSTIRYANTIFVL 652
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
366-1231 |
6.55e-63 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 236.17 E-value: 6.55e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 366 FTYLSRPETTIFDDLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYDPIAGEILIdgvsidklqvnwLRSQMGLVSQEPV 445
Cdd:PLN03130 622 FSWDSKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDASVV------------IRGTVAYVPQVSW 689
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 446 LFATSITENILFGKE-DASLDEvvEAAKASNAHTFISQFPLGYKTQVGERGVQMSGGQKQRIAIARAIIKSPKILLLDEA 524
Cdd:PLN03130 690 IFNATVRDNILFGSPfDPERYE--RAIDVTALQHDLDLLPGGDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDP 767
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 525 TSALDSESERVVQES-LDNASIGRTTIVIAHRLSTIRNADVICVIHNGQIVETGSHEEL------LKRIDGQYTSLVSLQ 597
Cdd:PLN03130 768 LSALDAHVGRQVFDKcIKDELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEELsnngplFQKLMENAGKMEEYV 847
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 598 QMENEESNVNINVSVTKDQVMS-LSKDFKYSQHNSIGStsssivtnvSDLIPNDNQPL-VPSFTRLMvmnrpEWKHALYG 675
Cdd:PLN03130 848 EENGEEEDDQTSSKPVANGNANnLKKDSSSKKKSKEGK---------SVLIKQEERETgVVSWKVLE-----RYKNALGG 913
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 676 clsAALVGVLqpVSAYSAGSVISVffLTS------HDQIKEKTR---IYVLLFVGLAIFSFLVNISQHYGFAYMGEYLTK 746
Cdd:PLN03130 914 ---AWVVMIL--FLCYVLTEVFRV--SSStwlsewTDQGTPKTHgplFYNLIYALLSFGQVLVTLLNSYWLIMSSLYAAK 986
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 747 RIREQMLSKILTFEVNWFDIddNSSGAICSRLAKDANVVRSMVGDRMSLLVQTISAVIIACI-IGLVIAWRLAIVMisvq 825
Cdd:PLN03130 987 RLHDAMLGSILRAPMSFFHT--NPLGRIINRFAKDLGDIDRNVAVFVNMFLGQIFQLLSTFVlIGIVSTISLWAIM---- 1060
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 826 PLIVVcFYTQRVLLKSLSEKAsKAQDESSKLA-----AEAVSNIRTITAFSSQERIIKLLKKVQEGPRResvhrswlagi 900
Cdd:PLN03130 1061 PLLVL-FYGAYLYYQSTAREV-KRLDSITRSPvyaqfGEALNGLSTIRAYKAYDRMAEINGRSMDNNIR----------- 1127
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 901 vlgtsRSLITCTSalNFWYGGRLIADGKIVskaffeIFLI--FVTTGRVIAD-----AGTMTTDLARGLDAVGSVFAVL- 972
Cdd:PLN03130 1128 -----FTLVNMSS--NRWLAIRLETLGGLM------IWLTasFAVMQNGRAEnqaafASTMGLLLSYALNITSLLTAVLr 1194
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 973 ------------DRCTT-----------IEP-KNPDGYVAEkikGQITFLNVDFAYptRPDVV-IFENFSIEIDEGKSTA 1027
Cdd:PLN03130 1195 laslaenslnavERVGTyidlpseaplvIENnRPPPGWPSS---GSIKFEDVVLRY--RPELPpVLHGLSFEISPSEKVG 1269
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1028 IVGTSGSGKSTIIGLIERFYDPLKGTVKIDGRDIRSYHLRSLRKYISLVSQEPMLFAGTIRENImyggtsDKIDE---SE 1104
Cdd:PLN03130 1270 IVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSGTVRFNL------DPFNEhndAD 1343
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1105 IIEAAKAANAHDFITSLSNGYDTNCGDKGVQLSGGQKQRIAIARAVLKNPSVLLLDEATSALDSKSERVVQDALERVMVG 1184
Cdd:PLN03130 1344 LWESLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDALIQKTIREEFKS 1423
|
890 900 910 920
....*....|....*....|....*....|....*....|....*..
gi 15232977 1185 RTSIMIAHRLSTIQNCDMIVVLGKGKIVESGTHSSLLEKGptGTYFS 1231
Cdd:PLN03130 1424 CTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLSNE--GSAFS 1468
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
112-598 |
1.31e-61 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 222.29 E-value: 1.31e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 112 RMREKYLRAVLRQDVGYFDLHvtSTSDVITSISSDSLVIQDFLSEKLPNFLMNASAFVASYIVSFILMWRLTIVG---FP 188
Cdd:PRK10790 99 QLRTDVMDAALRQPLSAFDTQ--PVGQLISRVTNDTEVIRDLYVTVVATVLRSAALIGAMLVAMFSLDWRMALVAimiFP 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 189 FIILLLVpglMYGRALVSISRK-------IHEQYNEAgsiaeqaISSVRTVYAFGSENKMIGKFSTALRGSVklglrqgL 261
Cdd:PRK10790 177 AVLVVMV---IYQRYSTPIVRRvrayladINDGFNEV-------INGMSVIQQFRQQARFGERMGEASRSHY-------M 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 262 AKGITIGSNGV----THAIWAFLTWYGsrLVMNHG-SKGGT--VFVVISCITYGGvSLGQSLSNL----KYFSEAFVAWE 330
Cdd:PRK10790 240 ARMQTLRLDGFllrpLLSLFSALILCG--LLMLFGfSASGTieVGVLYAFISYLG-RLNEPLIELttqqSMLQQAVVAGE 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 331 RILEVIkrvpdiDSNKKEGQILER--MKGEVEFNHVKFTYlsRPETTIFDDLCLKIPAGKTVALVGGSGSGKSTVISLLQ 408
Cdd:PRK10790 317 RVFELM------DGPRQQYGNDDRplQSGRIDIDNVSFAY--RDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLM 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 409 RFYDPIAGEILIDGVSIDKLQVNWLRSQMGLVSQEPVLFATSITENILFGKeDASLDEVVEAAKASNAHTFISQFPLGYK 488
Cdd:PRK10790 389 GYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLANVTLGR-DISEEQVWQALETVQLAELARSLPDGLY 467
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 489 TQVGERGVQMSGGQKQRIAIARAIIKSPKILLLDEATSALDSESERVVQESLDNASIGRTTIVIAHRLSTIRNADVICVI 568
Cdd:PRK10790 468 TPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLSTIVEADTILVL 547
|
490 500 510
....*....|....*....|....*....|
gi 15232977 569 HNGQIVETGSHEELLKRiDGQYTSLVSLQQ 598
Cdd:PRK10790 548 HRGQAVEQGTHQQLLAA-QGRYWQMYQLQL 576
|
|
| chvA |
TIGR01192 |
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ... |
991-1232 |
2.16e-61 |
|
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein in bacteria. It belongs to the larger ABC transporter superfamily with the characteristic ATP binding motif. The In general, this protein is in some ways implicated in osmoregulation and suggested to participate in the export of glucan from the cytoplasm to periplasm. The cyclic beta-1,2-glucan in the bactrerial periplasmic space is suggested to confer the property of high osmolority. It has also been demonstrated that mutants in this loci have lost functions of virulence and motility. It is unclear as to how virulence and osmoadaptaion are related. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 130260 [Multi-domain] Cd Length: 585 Bit Score: 221.30 E-value: 2.16e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 991 IKGQITFLNVDFAYPTRPDVVifENFSIEIDEGKSTAIVGTSGSGKSTIIGLIERFYDPLKGTVKIDGRDIRSYHLRSLR 1070
Cdd:TIGR01192 331 VKGAVEFRHITFEFANSSQGV--FDVSFEAKAGQTVAIVGPTGAGKTTLINLLQRVYDPTVGQILIDGIDINTVTRESLR 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1071 KYISLVSQEPMLFAGTIRENIMYGGTSDKIDEseIIEAAKAANAHDFITSLSNGYDTNCGDKGVQLSGGQKQRIAIARAV 1150
Cdd:TIGR01192 409 KSIATVFQDAGLFNRSIRENIRLGREGATDEE--VYEAAKAAAAHDFILKRSNGYDTLVGERGNRLSGGERQRLAIARAI 486
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1151 LKNPSVLLLDEATSALDSKSERVVQDALERVMVGRTSIMIAHRLSTIQNCDMIVVLGKGKIVESGTHSSLLEKGptGTYF 1230
Cdd:TIGR01192 487 LKNAPILVLDEATSALDVETEARVKNAIDALRKNRTTFIIAHRLSTVRNADLVLFLDQGRLIEKGSFQELIQKD--GRFY 564
|
..
gi 15232977 1231 SL 1232
Cdd:TIGR01192 565 KL 566
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
993-1216 |
5.71e-61 |
|
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: 207.73 E-value: 5.71e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 993 GQITFLNVDFAY-PTRPDVVifENFSIEIDEGKSTAIVGTSGSGKSTIIGLIERFYDPLKGTVKIDGRDIRSYHLRSLRK 1071
Cdd:cd03244 1 GDIEFKNVSLRYrPNLPPVL--KNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1072 YISLVSQEPMLFAGTIRENI-MYGGTSDkideSEIIEAAKAANAHDFITSLSNGYDTNCGDKGVQLSGGQKQRIAIARAV 1150
Cdd:cd03244 79 RISIIPQDPVLFSGTIRSNLdPFGEYSD----EELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARAL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15232977 1151 LKNPSVLLLDEATSALDSKSERVVQDALERVMVGRTSIMIAHRLSTIQNCDMIVVLGKGKIVESGT 1216
Cdd:cd03244 155 LRKSKILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
357-578 |
6.74e-61 |
|
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: 207.73 E-value: 6.74e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 357 GEVEFNHVKFTYlsRPET-TIFDDLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYDPIAGEILIDGVSIDKLQVNWLRS 435
Cdd:cd03244 1 GDIEFKNVSLRY--RPNLpPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 436 QMGLVSQEPVLFATSITENI-LFGKedASLDEVVEAAKASNAHTFISQFPLGYKTQVGERGVQMSGGQKQRIAIARAIIK 514
Cdd:cd03244 79 RISIIPQDPVLFSGTIRSNLdPFGE--YSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLR 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15232977 515 SPKILLLDEATSALDSESERVVQESLDNASIGRTTIVIAHRLSTIRNADVICVIHNGQIVETGS 578
Cdd:cd03244 157 KSKILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
74-594 |
1.22e-60 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 221.92 E-value: 1.22e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 74 MQTISKNVVALLYVACGSWVICFLEGYCWTRTGERQAARMREKYLRAVLRQDVGYFDlhvTSTSDVITSISSDSLVIQDF 153
Cdd:TIGR01193 192 MGTLGIISIGLIIAYIIQQILSYIQIFLLNVLGQRLSIDIILSYIKHLFELPMSFFS---TRRTGEIVSRFTDASSIIDA 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 154 LseklpnflmnasafvASYIVS-FILMWRLTIVGFPF---------IILLLVPglMYGRALVSISR---KIHEQYNEAGS 220
Cdd:TIGR01193 269 L---------------ASTILSlFLDMWILVIVGLFLvrqnmllflLSLLSIP--VYAVIIILFKRtfnKLNHDAMQANA 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 221 IAEQAI----SSVRTVYAFGSE----NKMIGKFSTALRGSVKLGLRQGLAKGITIGSNGVthaIWAFLTWYGSRLVMNHG 292
Cdd:TIGR01193 332 VLNSSIiedlNGIETIKSLTSEaerySKIDSEFGDYLNKSFKYQKADQGQQAIKAVTKLI---LNVVILWTGAYLVMRGK 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 293 SKGGTVFVVISCITYGGVSLgQSLSNLK-YFSEAFVAWERILEVIkRVPDIDSNKKEGQILERMKGEVEFNHVKFTY-LS 370
Cdd:TIGR01193 409 LTLGQLITFNALLSYFLTPL-ENIINLQpKLQAARVANNRLNEVY-LVDSEFINKKKRTELNNLNGDIVINDVSYSYgYG 486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 371 RPettIFDDLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYDPIAGEILIDGVSIDKLQVNWLRSQMGLVSQEPVLFATS 450
Cdd:TIGR01193 487 SN---ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYLPQEPYIFSGS 563
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 451 ITENILFG-KEDASLDEVVEAAKASNAHTFISQFPLGYKTQVGERGVQMSGGQKQRIAIARAIIKSPKILLLDEATSALD 529
Cdd:TIGR01193 564 ILENLLLGaKENVSQDEIWAACEIAEIKDDIENMPLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLD 643
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15232977 530 SESERVVQESLDNASiGRTTIVIAHRLSTIRNADVICVIHNGQIVETGSHEELLKRiDGQYTSLV 594
Cdd:TIGR01193 644 TITEKKIVNNLLNLQ-DKTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDELLDR-NGFYASLI 706
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
110-616 |
6.50e-60 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 216.50 E-value: 6.50e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 110 AARMREKYLRAVLRQDVGYF------DLHVTSTSDV-----------ITSIssDSLViqdflseklpnflMNASAFVasy 172
Cdd:PRK10789 68 AVELREDFYRQLSRQHPEFYlrhrtgDLMARATNDVdrvvfaagegvLTLV--DSLV-------------MGCAVLI--- 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 173 IVSFILMWRLTIvgfpfIILLLVPgLMygrALVsISR---KIHEQYNEAGSI-------AEQAISSVRTVYAFGSENKMI 242
Cdd:PRK10789 130 VMSTQISWQLTL-----LALLPMP-VM---AIM-IKRygdQLHERFKLAQAAfsslndrTQESLTSIRMIKAFGLEDRQS 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 243 GKFSTALRGSVKLGLRQ---------------GLAKGITIGSngvthaiwafltwyGSRLVMnHGSKggTVFVVISCITY 307
Cdd:PRK10789 200 ALFAADAEDTGKKNMRVaridarfdptiyiaiGMANLLAIGG--------------GSWMVV-NGSL--TLGQLTSFVMY 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 308 GGVSLGQSLSNLKYFS---EAFVAWERILEVIKRVPDIDSNKKEgqiLERMKGEVEFNHVKFTYlsrPETT--IFDDLCL 382
Cdd:PRK10789 263 LGLMIWPMLALAWMFNiveRGSAAYSRIRAMLAEAPVVKDGSEP---VPEGRGELDVNIRQFTY---PQTDhpALENVNF 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 383 KIPAGKTVALVGGSGSGKSTVISLLQRFYDPIAGEILIDGVSIDKLQVNWLRSQMGLVSQEPVLFATSITENILFGKEDA 462
Cdd:PRK10789 337 TLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFLFSDTVANNIALGRPDA 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 463 SLDEVVEAAKASNAHTFISQFPLGYKTQVGERGVQMSGGQKQRIAIARAIIKSPKILLLDEATSALDSESERVVQESLDN 542
Cdd:PRK10789 417 TQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQ 496
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15232977 543 ASIGRTTIVIAHRLSTIRNADVICVIHNGQIVETGSHEELLKRiDGQYTSLVSLQQMENEESNVNINVSVTKDQ 616
Cdd:PRK10789 497 WGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQ-SGWYRDMYRYQQLEAALDDAPEIREEAVDA 569
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
165-593 |
1.40e-59 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 215.84 E-value: 1.40e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 165 ASAFVASYIVSFILMW-----RLTIVGFPFIILLLVPGLMY------GRALVSISRKIHEQYNEAgsIAEQAISSVrtvy 233
Cdd:PRK11160 142 VAALVVILVLTIGLSFfdltlALTLGGILLLLLLLLPLLFYrlgkkpGQDLTHLRAQYRVQLTEW--LQGQAELTL---- 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 234 aFGSEnkmiGKFSTALRGSVKLGLRQ--------GLAKGITIGSNGVTHAIwafLTWYGSRLVMNHGSKGG----TVFVV 301
Cdd:PRK11160 216 -FGAE----DRYRQQLEQTEQQWLAAqrrqanltGLSQALMILANGLTVVL---MLWLAAGGVGGNAQPGAlialFVFAA 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 302 ISCI-TYGGVS-----LGQSLSnlkyfseafvAWERILEVIKRVPDIDSNKKEGQILERmkGEVEFNHVKFTYLSRPETT 375
Cdd:PRK11160 288 LAAFeALMPVAgafqhLGQVIA----------SARRINEITEQKPEVTFPTTSTAAADQ--VSLTLNNVSFTYPDQPQPV 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 376 IfDDLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYDPIAGEILIDGVSIDKLQVNWLRSQMGLVSQEPVLFATSITENI 455
Cdd:PRK11160 356 L-KGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNL 434
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 456 LFGKEDASLDEVVEAAKASNAHTFISQfPLGYKTQVGERGVQMSGGQKQRIAIARAIIKSPKILLLDEATSALDSESERV 535
Cdd:PRK11160 435 LLAAPNASDEALIEVLQQVGLEKLLED-DKGLNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQ 513
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 15232977 536 VQESLDNASIGRTTIVIAHRLSTIRNADVICVIHNGQIVETGSHEELLKRiDGQYTSL 593
Cdd:PRK11160 514 ILELLAEHAQNKTVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQELLAQ-QGRYYQL 570
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
324-568 |
2.22e-59 |
|
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: 213.69 E-value: 2.22e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 324 EAFVAWERILEVIKRVPDIDSNKKEgqILERMKGEVEFNHVKFTYLSRPEttIFDDLCLKIPAGKTVALVGGSGSGKSTV 403
Cdd:TIGR02857 289 DGVAAAEALFAVLDAAPRPLAGKAP--VTAAPASSLEFSGVSVAYPGRRP--ALRPVSFTVPPGERVALVGPSGAGKSTL 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 404 ISLLQRFYDPIAGEILIDGVSIDKLQVNWLRSQMGLVSQEPVLFATSITENILFGKEDASLDEVVEAAKASNAHTFISQF 483
Cdd:TIGR02857 365 LNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIRLARPDASDAEIREALERAGLDEFVAAL 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 484 PLGYKTQVGERGVQMSGGQKQRIAIARAIIKSPKILLLDEATSALDSESERVVQESLDNASIGRTTIVIAHRLSTIRNAD 563
Cdd:TIGR02857 445 PQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALAD 524
|
....*
gi 15232977 564 VICVI 568
Cdd:TIGR02857 525 RIVVL 529
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1015-1220 |
4.34e-59 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 214.71 E-value: 4.34e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1015 NFSIEidEGKSTAIVGTSGSGKSTIIGLIERFYdPLKGTVKIDGRDIRSYHLRSLRKYISLVSQEPMLFAGTIRENIMYG 1094
Cdd:PRK11174 370 NFTLP--AGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVLLG 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1095 GTSdkIDESEIIEAAKAANAHDFITSLSNGYDTNCGDKGVQLSGGQKQRIAIARAVLKNPSVLLLDEATSALDSKSERVV 1174
Cdd:PRK11174 447 NPD--ASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLV 524
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 15232977 1175 QDALERVMVGRTSIMIAHRLSTIQNCDMIVVLGKGKIVESGTHSSL 1220
Cdd:PRK11174 525 MQALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAEL 570
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
992-1223 |
2.01e-57 |
|
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: 208.83 E-value: 2.01e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 992 KGQITFLNVDFAYPTRpDVVIFENFSIEIDEGKSTAIVGTSGSGKST----IIGLIErfydPLKGTVKIDGRDIRSYHLR 1067
Cdd:COG4618 328 KGRLSVENLTVVPPGS-KRPILRGVSFSLEPGEVLGVIGPSGSGKSTlarlLVGVWP----PTAGSVRLDGADLSQWDRE 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1068 SLRKYISLVSQEPMLFAGTIRENI--MyggtsDKIDESEIIEAAKAANAHDFITSLSNGYDTNCGDKGVQLSGGQKQRIA 1145
Cdd:COG4618 403 ELGRHIGYLPQDVELFDGTIAENIarF-----GDADPEKVVAAAKLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQRIG 477
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15232977 1146 IARAVLKNPSVLLLDEATSALDSKSERVVQDALERV-MVGRTSIMIAHRLSTIQNCDMIVVLGKGKIVESGTHSSLLEK 1223
Cdd:COG4618 478 LARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALkARGATVVVITHRPSLLAAVDKLLVLRDGRVQAFGPRDEVLAR 556
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
988-1237 |
2.46e-57 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 208.91 E-value: 2.46e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 988 AEKIKGQITFLNVDFAYPTRPDVVIfENFSIEIDEGKSTAIVGTSGSGKSTIIGLIERFYDPLKGTVKIDGRDIRSYHLR 1067
Cdd:PRK11160 332 AAADQVSLTLNNVSFTYPDQPQPVL-KGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEA 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1068 SLRKYISLVSQEPMLFAGTIRENIMYGgtSDKIDESEIIEAAKAANAHDFITSlSNGYDTNCGDKGVQLSGGQKQRIAIA 1147
Cdd:PRK11160 411 ALRQAISVVSQRVHLFSATLRDNLLLA--APNASDEALIEVLQQVGLEKLLED-DKGLNAWLGEGGRQLSGGEQRRLGIA 487
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1148 RAVLKNPSVLLLDEATSALDSKSERVVQDALERVMVGRTSIMIAHRLSTIQNCDMIVVLGKGKIVESGTHSSLLEKGptG 1227
Cdd:PRK11160 488 RALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQELLAQQ--G 565
|
250
....*....|
gi 15232977 1228 TYFSLagIQR 1237
Cdd:PRK11160 566 RYYQL--KQR 573
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
912-1239 |
8.69e-57 |
|
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: 209.81 E-value: 8.69e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 912 TSALNFWYGGRLIADGKIVSK---AFFEIFLIFVTTgrviadagtmTTDLARGLDAVGSVFAVLDRCTTI---EPKNPDG 985
Cdd:TIGR03797 372 TSAALFAAAISLLGGAGLSLGsflAFNTAFGSFSGA----------VTQLSNTLISILAVIPLWERAKPIleaLPEVDEA 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 986 YVAE-KIKGQITFLNVDFAYptRPD-VVIFENFSIEIDEGKSTAIVGTSGSGKSTIIGLIERFYDPLKGTVKIDGRDIRS 1063
Cdd:TIGR03797 442 KTDPgKLSGAIEVDRVTFRY--RPDgPLILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAG 519
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1064 YHLRSLRKYISLVSQEPMLFAGTIRENIMyGGTSDKIDESeiIEAAKAANAHDFITSLSNGYDTNCGDKGVQLSGGQKQR 1143
Cdd:TIGR03797 520 LDVQAVRRQLGVVLQNGRLMSGSIFENIA-GGAPLTLDEA--WEAARMAGLAEDIRAMPMGMHTVISEGGGTLSGGQRQR 596
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1144 IAIARAVLKNPSVLLLDEATSALDSKSERVVQDALERVMVGRtsIMIAHRLSTIQNCDMIVVLGKGKIVESGTHSSLLEK 1223
Cdd:TIGR03797 597 LLIARALVRKPRILLFDEATSALDNRTQAIVSESLERLKVTR--IVIAHRLSTIRNADRIYVLDAGRVVQQGTYDELMAR 674
|
330
....*....|....*.
gi 15232977 1224 GptGTYFSLAgiQRTL 1239
Cdd:TIGR03797 675 E--GLFAQLA--RRQL 686
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
379-1222 |
1.12e-55 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 213.10 E-value: 1.12e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 379 DLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYDPIAGEIlidgvsidklqvnWLRSQMGLVSQEPVLFATSITENILF- 457
Cdd:PTZ00243 678 DVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV-------------WAERSIAYVPQQAWIMNATVRGNILFf 744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 458 GKEDASldEVVEAAKASNAHTFISQFPLGYKTQVGERGVQMSGGQKQRIAIARAIIKSPKILLLDEATSALDSE-SERVV 536
Cdd:PTZ00243 745 DEEDAA--RLADAVRVSQLEADLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHvGERVV 822
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 537 QESLDNASIGRTTIVIAHRLSTIRNADVICVIHNGQIVETGSHEELLKridgqyTSLVSLQQMENEESNVNINVSVTKDQ 616
Cdd:PTZ00243 823 EECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSGSSADFMR------TSLYATLAAELKENKDSKEGDADAEV 896
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 617 VMSLSKDFKYSQHNSigstssSIVTNVSDLIPNDNQPLVPSFTRLMVMNRPE-----WK--HALYGCLSAALVgvlqpvs 689
Cdd:PTZ00243 897 AEVDAAPGGAVDHEP------PVAKQEGNAEGGDGAALDAAAGRLMTREEKAsgsvpWStyVAYLRFCGGLHA------- 963
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 690 aysAGSVISVFFLT--------------SHDQIKEKTRIYVLLFVG---LAIFSFLVNISQHYGFAYMGeylTKRIREQM 752
Cdd:PTZ00243 964 ---AGFVLATFAVTelvtvssgvwlsmwSTRSFKLSAATYLYVYLGivlLGTFSVPLRFFLSYEAMRRG---SRNMHRDL 1037
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 753 LSKILTFEVNWFDIddNSSGAICSRLAKDANVVRSMVGDRMSLLVQtisaviiaCIIGLVIAwrlAIVMISVQPLIVV-- 830
Cdd:PTZ00243 1038 LRSVSRGTMSFFDT--TPLGRILNRFSRDIDILDNTLPMSYLYLLQ--------CLFSICSS---ILVTSASQPFVLVal 1104
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 831 ---CFYTQRVLL------KSLSEKASKAQDESSKLAAEAVSNIRTITAFSSQERIIkllkkvQEGPRR----------ES 891
Cdd:PTZ00243 1105 vpcGYLYYRLMQfynsanREIRRIKSVAKSPVFTLLEEALQGSATITAYGKAHLVM------QEALRRldvvyscsylEN 1178
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 892 VHRSWLA--------------------GIVLGTSR--------SL---ITCTSALNfW---YGGRLIADGKIVSKAFFEI 937
Cdd:PTZ00243 1179 VANRWLGvrveflsnivvtvialigviGTMLRATSqeiglvslSLtmaMQTTATLN-WlvrQVATVEADMNSVERLLYYT 1257
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 938 FLI---FVTTGRVIADAGTMTTDLARglDAVGSVfavldrctTIEPKNPDGYVAEKIK-GQITFLNVDFAYPTRPDVVIf 1013
Cdd:PTZ00243 1258 DEVpheDMPELDEEVDALERRTGMAA--DVTGTV--------VIEPASPTSAAPHPVQaGSLVFEGVQMRYREGLPLVL- 1326
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1014 ENFSIEIDEGKSTAIVGTSGSGKSTIIGLIERFYDPLKGTVKIDGRDIRSYHLRSLRKYISLVSQEPMLFAGTIRENImy 1093
Cdd:PTZ00243 1327 RGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFSMIPQDPVLFDGTVRQNV-- 1404
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1094 ggtsDKIDES---EIIEAAKAANAHDFITSLSNGYDTNCGDKGVQLSGGQKQRIAIARAVLKNPS-VLLLDEATSALDSK 1169
Cdd:PTZ00243 1405 ----DPFLEAssaEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLKKGSgFILMDEATANIDPA 1480
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|...
gi 15232977 1170 SERVVQDALERVMVGRTSIMIAHRLSTIQNCDMIVVLGKGKIVESGTHSSLLE 1222
Cdd:PTZ00243 1481 LDRQIQATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELVM 1533
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
314-586 |
2.72e-55 |
|
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: 202.67 E-value: 2.72e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 314 QSLSNLKYFSEAFVAWERILEVIKRVPDidsnKKEGQILERMKGEVEFNHVKFTYlsrPETT--IFDDLCLKIPAGKTVA 391
Cdd:COG4618 290 QAIGGWKQFVSARQAYRRLNELLAAVPA----EPERMPLPRPKGRLSVENLTVVP---PGSKrpILRGVSFSLEPGEVLG 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 392 LVGGSGSGKSTVISLLQRFYDPIAGEILIDGVSIDklqvNWLRSQ----MGLVSQEPVLFATSITENI-LFGKEDAslDE 466
Cdd:COG4618 363 VIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLS----QWDREElgrhIGYLPQDVELFDGTIAENIaRFGDADP--EK 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 467 VVEAAKASNAHTFISQFPLGYKTQVGERGVQMSGGQKQRIAIARAIIKSPKILLLDEATSALDSESERVVQESLDNA-SI 545
Cdd:COG4618 437 VVAAAKLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALkAR 516
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 15232977 546 GRTTIVIAHRLSTIRNADVICVIHNGQIVETGSHEELLKRI 586
Cdd:COG4618 517 GATVVVITHRPSLLAAVDKLLVLRDGRVQAFGPRDEVLARL 557
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
380-582 |
4.50e-55 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 202.77 E-value: 4.50e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 380 LCLKIPAGKTVALVGGSGSGKSTVISLLQRFYdPIAGEILIDGVSIDKLQVNWLRSQMGLVSQEPVLFATSITENILFGK 459
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVLLGN 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 460 EDASLDEVVEAAKASNAHTFISQFPLGYKTQVGERGVQMSGGQKQRIAIARAIIKSPKILLLDEATSALDSESERVVQES 539
Cdd:PRK11174 448 PDASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQA 527
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 15232977 540 LDNASIGRTTIVIAHRLSTIRNADVICVIHNGQIVETGSHEEL 582
Cdd:PRK11174 528 LNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAEL 570
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
675-968 |
5.62e-55 |
|
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1 (ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350021 [Multi-domain] Cd Length: 300 Bit Score: 193.84 E-value: 5.62e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 675 GCLSAALVGVLQPVSAYSAGSVISVF-----FLTSHDQIKEKTRIYVLLFVGLAIFSFLVNISQHYGFAYMGEYLTKRIR 749
Cdd:cd18577 4 GLLAAIAAGAALPLMTIVFGDLFDAFtdfgsGESSPDEFLDDVNKYALYFVYLGIGSFVLSYIQTACWTITGERQARRIR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 750 EQMLSKILTFEVNWFDidDNSSGAICSRLAKDANVVRSMVGDRMSLLVQTISAVIIACIIGLVIAWRLAIVMISVQPLIV 829
Cdd:cd18577 84 KRYLKALLRQDIAWFD--KNGAGELTSRLTSDTNLIQDGIGEKLGLLIQSLSTFIAGFIIAFIYSWKLTLVLLATLPLIA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 830 VCFYTQRVLLKSLSEKASKAQDESSKLAAEAVSNIRTITAFSSQERIIKLLKKVQEGPRRESVHRSWLAGIVLGTSRSLI 909
Cdd:cd18577 162 IVGGIMGKLLSKYTKKEQEAYAKAGSIAEEALSSIRTVKAFGGEEKEIKRYSKALEKARKAGIKKGLVSGLGLGLLFFII 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 15232977 910 TCTSALNFWYGGRLIADGKIVSKAFFEIFLIFVTTGRVIADAGTMTTDLARGLDAVGSV 968
Cdd:cd18577 242 FAMYALAFWYGSRLVRDGEISPGDVLTVFFAVLIGAFSLGQIAPNLQAFAKARAAAAKI 300
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
649-1237 |
1.21e-53 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 198.79 E-value: 1.21e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 649 NDNQPLVPSFTRLMVMNRPEWKHALYGCLS---AALVGVLQPVsaysagsVISVFFltshDQIKEKTRIYVLLFVGLAIF 725
Cdd:PRK10790 2 RSFSQLWPTLKRLLAYGSPWRKPLGLAVLMlwvAAAAEVSGPL-------LISYFI----DNMVAKGNLPLGLVAGLAAA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 726 SFLVNI---SQHYGFAYMGEY----LTKRIREQMLSKILTFEVNWFDIddNSSGAICSRLAKDANVVRSmvgdrmsLLVQ 798
Cdd:PRK10790 71 YVGLQLlaaGLHYAQSLLFNRaavgVVQQLRTDVMDAALRQPLSAFDT--QPVGQLISRVTNDTEVIRD-------LYVT 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 799 TISAVI--IACIIGLVIA-----WRLAIVMISVQP--LIVVCFYtQRV---LLKSLSEKASKAQDESSklaaEAVSNIRT 866
Cdd:PRK10790 142 VVATVLrsAALIGAMLVAmfsldWRMALVAIMIFPavLVVMVIY-QRYstpIVRRVRAYLADINDGFN----EVINGMSV 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 867 ITAFSSQERiikLLKKVQEGPRRESVHRSW---LAGIVLGTSRSL----ITCTSALNFWYGGRliadGKI---VSKAFFE 936
Cdd:PRK10790 217 IQQFRQQAR---FGERMGEASRSHYMARMQtlrLDGFLLRPLLSLfsalILCGLLMLFGFSAS----GTIevgVLYAFIS 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 937 IF------LIFVTTGRVIadagtmttdLARGLDAVGSVFAVLDRcttiePKNPDGYVAEKIK-GQITFLNVDFAYptRPD 1009
Cdd:PRK10790 290 YLgrlnepLIELTTQQSM---------LQQAVVAGERVFELMDG-----PRQQYGNDDRPLQsGRIDIDNVSFAY--RDD 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1010 VVIFENFSIEIDEGKSTAIVGTSGSGKSTIIGLIERFYDPLKGTVKIDGRDIRSYHLRSLRKYISLVSQEPMLFAGTIRE 1089
Cdd:PRK10790 354 NLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLA 433
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1090 NIMYGgtsDKIDESEIIEAAKAANAHDFITSLSNGYDTNCGDKGVQLSGGQKQRIAIARAVLKNPSVLLLDEATSALDSK 1169
Cdd:PRK10790 434 NVTLG---RDISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSG 510
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15232977 1170 SERVVQDALERVMVGRTSIMIAHRLSTIQNCDMIVVLGKGKIVESGTHSSLLEKgpTGTYFSLAGIQR 1237
Cdd:PRK10790 511 TEQAIQQALAAVREHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAA--QGRYWQMYQLQL 576
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
819-1223 |
3.47e-50 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 187.17 E-value: 3.47e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 819 IVMISVQPLIVVCFYTQRVLLKSLSEkASKAQDESSKLAAEAVSNIRTITAFSSQERIIKLLKKVQEGPRRESVHRSWLA 898
Cdd:TIGR01842 146 LALGGAVVLVGLALLNNRATKKPLKE-ATEASIRANNLADSALRNAEVIEAMGMMGNLTKRWGRFHSKYLSAQSAASDRA 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 899 GIVLGTSRSLITCTSALNFWYGGRLIADGKIvskaffeiflifvTTGRVIADAGTMTTDLARGLDAVG------SVFAVL 972
Cdd:TIGR01842 225 GMLSNLSKYFRIVLQSLVLGLGAYLAIDGEI-------------TPGMMIAGSILVGRALAPIDGAIGgwkqfsGARQAY 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 973 DRCTTI---EPKNPDGYVAEKIKGQITFLNVDFAyPTRPDVVIFENFSIEIDEGKSTAIVGTSGSGKSTIIGLIERFYDP 1049
Cdd:TIGR01842 292 KRLNELlanYPSRDPAMPLPEPEGHLSVENVTIV-PPGGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPP 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1050 LKGTVKIDGRDIRSYHLRSLRKYISLVSQEPMLFAGTIRENIMYGGtsDKIDESEIIEAAKAANAHDFITSLSNGYDTNC 1129
Cdd:TIGR01842 371 TSGSVRLDGADLKQWDRETFGKHIGYLPQDVELFPGTVAENIARFG--ENADPEKIIEAAKLAGVHELILRLPDGYDTVI 448
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1130 GDKGVQLSGGQKQRIAIARAVLKNPSVLLLDEATSALDSKSERVVQDALERVMV-GRTSIMIAHRLSTIQNCDMIVVLGK 1208
Cdd:TIGR01842 449 GPGGATLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQALANAIKALKArGITVVVITHRPSLLGCVDKILVLQD 528
|
410
....*....|....*
gi 15232977 1209 GKIVESGTHSSLLEK 1223
Cdd:TIGR01842 529 GRIARFGERDEVLAK 543
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
314-586 |
2.38e-49 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 184.86 E-value: 2.38e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 314 QSLSNLKYFSEAFVAWERILEVIKRVPDidsnKKEGQILERMKGEVEFNHVKFTYlSRPETTIFDDLCLKIPAGKTVALV 393
Cdd:TIGR01842 276 GAIGGWKQFSGARQAYKRLNELLANYPS----RDPAMPLPEPEGHLSVENVTIVP-PGGKKPTLRGISFSLQAGEALAII 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 394 GGSGSGKSTVISLLQRFYDPIAGEILIDGVSIDKLQVNWLRSQMGLVSQEPVLFATSITENILFGKEDASLDEVVEAAKA 473
Cdd:TIGR01842 351 GPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGKHIGYLPQDVELFPGTVAENIARFGENADPEKIIEAAKL 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 474 SNAHTFISQFPLGYKTQVGERGVQMSGGQKQRIAIARAIIKSPKILLLDEATSALDSESERVVQESLDNASI-GRTTIVI 552
Cdd:TIGR01842 431 AGVHELILRLPDGYDTVIGPGGATLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQALANAIKALKArGITVVVI 510
|
250 260 270
....*....|....*....|....*....|....
gi 15232977 553 AHRLSTIRNADVICVIHNGQIVETGSHEELLKRI 586
Cdd:TIGR01842 511 THRPSLLGCVDKILVLQDGRIARFGERDEVLAKL 544
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
108-556 |
7.46e-49 |
|
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: 182.95 E-value: 7.46e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 108 RQAARMREKYLRAVLRQdvGYFDLHVTSTSDVITSISSDSLVIQDFLSEKLpnFLMNASAFVASYIVSFI--LMWR--LT 183
Cdd:TIGR02868 83 RSLGALRVRVYERLARQ--ALAGRRRLRRGDLLGRLGADVDALQDLYVRVI--VPAGVALVVGAAAVAAIavLSVPaaLI 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 184 IVGFPFIILLLVPGLMY--GRALVSISRKIHEQYNEAGSIAEQAISSVRtvyAFGSENKMIGKFSTALRGSVKLGLRQ-- 259
Cdd:TIGR02868 159 LAAGLLLAGFVAPLVSLraARAAEQALARLRGELAAQLTDALDGAAELV---ASGALPAALAQVEEADRELTRAERRAaa 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 260 --GLAKGITIGSNGVthAIWAFLtWYGSRLVMNHGSKGGTVFVVISCItyggVSLGQSLSNLkyfSEAFVAWERILEVIK 337
Cdd:TIGR02868 236 atALGAALTLLAAGL--AVLGAL-WAGGPAVADGRLAPVTLAVLVLLP----LAAFEAFAAL---PAAAQQLTRVRAAAE 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 338 RVPDIDSNKKEGQI--------LERMKGEVEFNHVKFTYLSRPEttIFDDLCLKIPAGKTVALVGGSGSGKSTVISLLQR 409
Cdd:TIGR02868 306 RIVEVLDAAGPVAEgsapaagaVGLGKPTLELRDLSAGYPGAPP--VLDGVSLDLPPGERVAILGPSGSGKSTLLATLAG 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 410 FYDPIAGEILIDGVSIDKLQVNWLRSQMGLVSQEPVLFATSITENILFGKEDASLDEVVEAAKASNAHTFISQFPLGYKT 489
Cdd:TIGR02868 384 LLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLARPDATDEELWAALERVGLADWLRALPDGLDT 463
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15232977 490 QVGERGVQMSGGQKQRIAIARAIIKSPKILLLDEATSALDSESERVVQESLDNASIGRTTIVIAHRL 556
Cdd:TIGR02868 464 VLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHHL 530
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
999-1211 |
1.69e-48 |
|
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: 170.47 E-value: 1.69e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 999 NVDFAYP--TRPdvvIFENFSIEIDEGKSTAIVGTSGSGKST----IIGLIErfydPLKGTVKIDGRDIRSYHLRSLRKY 1072
Cdd:cd03246 5 NVSFRYPgaEPP---VLRNVSFSIEPGESLAIIGPSGSGKSTlarlILGLLR----PTSGRVRLDGADISQWDPNELGDH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1073 ISLVSQEPMLFAGTIRENImyggtsdkideseiieaakaanahdfitslsngydtncgdkgvqLSGGQKQRIAIARAVLK 1152
Cdd:cd03246 78 VGYLPQDDELFSGSIAENI--------------------------------------------LSGGQRQRLGLARALYG 113
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1153 NPSVLLLDEATSALDSKSERVVQDALERV-MVGRTSIMIAHRLSTIQNCDMIVVLGKGKI 1211
Cdd:cd03246 114 NPRILVLDEPNSHLDVEGERALNQAIAALkAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
998-1229 |
1.85e-47 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 179.52 E-value: 1.85e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 998 LNVD---FAYPTRpDVVIFENFSIEIDEGKSTAIVGTSGSGKSTIIGLIERFYDPLKGTVKIDGRDIRSYHLRSLRKYIS 1074
Cdd:PRK10789 314 LDVNirqFTYPQT-DHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLA 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1075 LVSQEPMLFAGTIRENIMYGGTSDKidESEIIEAAKAANAHDFITSLSNGYDTNCGDKGVQLSGGQKQRIAIARAVLKNP 1154
Cdd:PRK10789 393 VVSQTPFLFSDTVANNIALGRPDAT--QQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNA 470
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15232977 1155 SVLLLDEATSALDSKSERVVQDALERVMVGRTSIMIAHRLSTIQNCDMIVVLGKGKIVESGTHSSLLEKgpTGTY 1229
Cdd:PRK10789 471 EILILDDALSAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQ--SGWY 543
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
376-582 |
3.34e-47 |
|
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: 168.51 E-value: 3.34e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 376 IFDDLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYD-----PIAGEILIDGVSIDKLQVN--WLRSQMGLVSQEPVLFA 448
Cdd:cd03260 15 ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIYDLDVDvlELRRRVGMVFQKPNPFP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 449 TSITENILFG------KEDASLDEVVEAA--KAsnahtfisqfplGYKTQVGER--GVQMSGGQKQRIAIARAIIKSPKI 518
Cdd:cd03260 95 GSIYDNVAYGlrlhgiKLKEELDERVEEAlrKA------------ALWDEVKDRlhALGLSGGQQQRLCLARALANEPEV 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15232977 519 LLLDEATSALDSESERVVQESLDNASiGRTTIVIA-HRLS-TIRNADVICVIHNGQIVETGSHEEL 582
Cdd:cd03260 163 LLLDEPTSALDPISTAKIEELIAELK-KEYTIVIVtHNMQqAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
677-1232 |
8.13e-47 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 180.32 E-value: 8.13e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 677 LSAALVGVLQPVSAYSAGSVISVFFltsHDQIKEKTRIYVLLFVGLAIFSFLVNISQHYGFAYMGEYLTKRIREQMLSKI 756
Cdd:TIGR01193 163 IAAIIVTLISIAGSYYLQKIIDTYI---PHKMMGTLGIISIGLIIAYIIQQILSYIQIFLLNVLGQRLSIDIILSYIKHL 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 757 LTFEVNWFDIddNSSGAICSRLAKDANVVRSMVGDRMSLLVQTISAVIIACIIGLVIAWRLAIVMISVqPLIVVCFYTQR 836
Cdd:TIGR01193 240 FELPMSFFST--RRTGEIVSRFTDASSIIDALASTILSLFLDMWILVIVGLFLVRQNMLLFLLSLLSI-PVYAVIIILFK 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 837 VLLKSLSEKASKAQDESSKLAAEAVSNIRTITAFSSQE--------RIIKLLKKVQEGPRRESVHRSWLAGIVLGTSRSL 908
Cdd:TIGR01193 317 RTFNKLNHDAMQANAVLNSSIIEDLNGIETIKSLTSEAeryskidsEFGDYLNKSFKYQKADQGQQAIKAVTKLILNVVI 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 909 ItctsalnfWYGGRLIADGKIvskaffeiflifvTTGRVIAdagtmttdlargLDAVGSVFAV-LDRCTTIEPKNPDGYV 987
Cdd:TIGR01193 397 L--------WTGAYLVMRGKL-------------TLGQLIT------------FNALLSYFLTpLENIINLQPKLQAARV 443
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 988 A-------------EKIKGQITFLN----------VDFAYPTRPDVVifENFSIEIDEGKSTAIVGTSGSGKSTIIGLIE 1044
Cdd:TIGR01193 444 AnnrlnevylvdseFINKKKRTELNnlngdivindVSYSYGYGSNIL--SDISLTIKMNSKTTIVGMSGSGKSTLAKLLV 521
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1045 RFYDPLKGTVKIDGRDIRSYHLRSLRKYISLVSQEPMLFAGTIRENIMYGgTSDKIDESEIIEAAKAANAHDFITSLSNG 1124
Cdd:TIGR01193 522 GFFQARSGEILLNGFSLKDIDRHTLRQFINYLPQEPYIFSGSILENLLLG-AKENVSQDEIWAACEIAEIKDDIENMPLG 600
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1125 YDTNCGDKGVQLSGGQKQRIAIARAVLKNPSVLLLDEATSALDSKSERVVQDALERvMVGRTSIMIAHRLSTIQNCDMIV 1204
Cdd:TIGR01193 601 YQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLN-LQDKTIIFVAHRLSVAKQSDKII 679
|
570 580
....*....|....*....|....*...
gi 15232977 1205 VLGKGKIVESGTHSSLLEKGptGTYFSL 1232
Cdd:TIGR01193 680 VLDHGKIIEQGSHDELLDRN--GFYASL 705
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
770-1194 |
1.55e-46 |
|
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: 176.01 E-value: 1.55e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 770 SSGAICSRLAKDANVVRSMvgdrmslLVQTISAVIIACIIGLVIAWRLAIVMISVQPLIVVCFYTQRVLLKSLSEKASKA 849
Cdd:TIGR02868 108 RRGDLLGRLGADVDALQDL-------YVRVIVPAGVALVVGAAAVAAIAVLSVPAALILAAGLLLAGFVAPLVSLRAARA 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 850 QDES-----SKLAAEAVSNIR---TITAFSSQERIIKLLKKVQEGPRRESVHRSWLAGivLGTSRSLITCTSA--LNFWY 919
Cdd:TIGR02868 181 AEQAlarlrGELAAQLTDALDgaaELVASGALPAALAQVEEADRELTRAERRAAAATA--LGAALTLLAAGLAvlGALWA 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 920 GGRLIADGKI----------VSKAFFEIF----LIFVTTGRVIADAGTMTtDLARglDAVGSVFAVLDRCTTIEPKNPdg 985
Cdd:TIGR02868 259 GGPAVADGRLapvtlavlvlLPLAAFEAFaalpAAAQQLTRVRAAAERIV-EVLD--AAGPVAEGSAPAAGAVGLGKP-- 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 986 yvaekikgQITFLNVDFAYPTRPDVviFENFSIEIDEGKSTAIVGTSGSGKSTIIGLIERFYDPLKGTVKIDGRDIRSYH 1065
Cdd:TIGR02868 334 --------TLELRDLSAGYPGAPPV--LDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLD 403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1066 LRSLRKYISLVSQEPMLFAGTIRENIMYGgTSDKIDEsEIIEAAKAANAHDFITSLSNGYDTNCGDKGVQLSGGQKQRIA 1145
Cdd:TIGR02868 404 QDEVRRRVSVCAQDAHLFDTTVRENLRLA-RPDATDE-ELWAALERVGLADWLRALPDGLDTVLGEGGARLSGGERQRLA 481
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 15232977 1146 IARAVLKNPSVLLLDEATSALDSKSERVVQDALERVMVGRTSIMIAHRL 1194
Cdd:TIGR02868 482 LARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHHL 530
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
995-1215 |
6.19e-46 |
|
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: 163.25 E-value: 6.19e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 995 ITFLNVDFAYPTRpDVVIFENFSIEIDEGKSTAIVGTSGSGKSTIIGLIERFYDPLKGTVKIDGRDIRSYHlRSLRKYIS 1074
Cdd:cd03247 1 LSINNVSFSYPEQ-EQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLIS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1075 LVSQEPMLFAGTIRENImyggtsdkideseiieaakaanahdfitslsngydtncgdkGVQLSGGQKQRIAIARAVLKNP 1154
Cdd:cd03247 79 VLNQRPYLFDTTLRNNL-----------------------------------------GRRFSGGERQRLALARILLQDA 117
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15232977 1155 SVLLLDEATSALDSKSERVVQDALERVMVGRTSIMIAHRLSTIQNCDMIVVLGKGKIVESG 1215
Cdd:cd03247 118 PIVLLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
993-1216 |
2.13e-45 |
|
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: 162.58 E-value: 2.13e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 993 GQITFLNVDFAY-PTRPDVVifENFSIEIDEGKSTAIVGTSGSGKSTIIGLIERFYDPLKGTVKIDGRDIRSYHLRSLRK 1071
Cdd:cd03369 5 GEIEVENLSVRYaPDLPPVL--KNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1072 YISLVSQEPMLFAGTIRENImygGTSDKIDESEIIEAAKaanahdfitsLSNGydtncgdkGVQLSGGQKQRIAIARAVL 1151
Cdd:cd03369 83 SLTIIPQDPTLFSGTIRSNL---DPFDEYSDEEIYGALR----------VSEG--------GLNLSQGQRQLLCLARALL 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15232977 1152 KNPSVLLLDEATSALDSKSERVVQDALERVMVGRTSIMIAHRLSTIQNCDMIVVLGKGKIVESGT 1216
Cdd:cd03369 142 KRPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
995-1216 |
3.52e-45 |
|
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: 162.89 E-value: 3.52e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 995 ITFLNVDFAYPtrPDVVIFENFSIEIDEGKSTAIVGTSGSGKSTIIGLIERFYDPLKGTVKIDGRDIRSYHLRSLRKYIS 1074
Cdd:COG1122 1 IELENLSFSYP--GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1075 LVSQEP--MLFAGTIRENIMYGGTSDKIDESEIIE-AAKAANAHDfITSLsngydtncGDKGV-QLSGGQKQRIAIARAV 1150
Cdd:COG1122 79 LVFQNPddQLFAPTVEEDVAFGPENLGLPREEIRErVEEALELVG-LEHL--------ADRPPhELSGGQKQRVAIAGVL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15232977 1151 LKNPSVLLLDEATSALDSKSERVVQDALERV-MVGRTSIMIAHRLSTI-QNCDMIVVLGKGKIVESGT 1216
Cdd:COG1122 150 AMEPEVLVLDEPTAGLDPRGRRELLELLKRLnKEGKTVIIVTHDLDLVaELADRVIVLDDGRIVADGT 217
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
359-587 |
2.06e-44 |
|
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: 160.58 E-value: 2.06e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 359 VEFNHVKFTYlsRPETTIFDDLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYDPIAGEILIDGVSIDKLQVNWLRSQMG 438
Cdd:COG1122 1 IELENLSFSY--PGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 439 LVSQEPV--LFATSITENILFGKEDASLDE------VVEAAKASNAHTFISQFPLgyktqvgergvQMSGGQKQRIAIAR 510
Cdd:COG1122 79 LVFQNPDdqLFAPTVEEDVAFGPENLGLPReeirerVEEALELVGLEHLADRPPH-----------ELSGGQKQRVAIAG 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15232977 511 AIIKSPKILLLDEATSALDSESERVVQESLDN-ASIGRTTIVIAHRLSTI-RNADVICVIHNGQIVETGSHEELLKRID 587
Cdd:COG1122 148 VLAMEPEVLVLDEPTAGLDPRGRRELLELLKRlNKEGKTVIIVTHDLDLVaELADRVIVLDDGRIVADGTPREVFSDYE 226
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
995-1211 |
4.82e-44 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 158.83 E-value: 4.82e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 995 ITFLNVDFAYPTRPdvvIFENFSIEIDEGKSTAIVGTSGSGKSTIIGLIERFYDPLKGTVKIDGRDIRSYHLRSLRKYIS 1074
Cdd:COG4619 1 LELEGLSFRVGGKP---ILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1075 LVSQEPMLFAGTIRENIM--YGGTSDKIDESEIIEAAKAANahdfitsLSNGY-DTNCGDkgvqLSGGQKQRIAIARAVL 1151
Cdd:COG4619 78 YVPQEPALWGGTVRDNLPfpFQLRERKFDRERALELLERLG-------LPPDIlDKPVER----LSGGERQRLALIRALL 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15232977 1152 KNPSVLLLDEATSALDSKSERVVQDALERVM--VGRTSIMIAHRLSTIQN-CDMIVVLGKGKI 1211
Cdd:COG4619 147 LQPDVLLLDEPTSALDPENTRRVEELLREYLaeEGRAVLWVSHDPEQIERvADRVLTLEAGRL 209
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
360-573 |
1.14e-43 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 157.67 E-value: 1.14e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 360 EFNHVKFTYLSRPettIFDDLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYDPIAGEILIDGVSIDKLQVNWLRSQMGL 439
Cdd:COG4619 2 ELEGLSFRVGGKP---ILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 440 VSQEPVLFATSITENILFG----KEDASLDEVVEAAKAsnahtfisqfpLGYKTQVGERGV-QMSGGQKQRIAIARAIIK 514
Cdd:COG4619 79 VPQEPALWGGTVRDNLPFPfqlrERKFDRERALELLER-----------LGLPPDILDKPVeRLSGGERQRLALIRALLL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15232977 515 SPKILLLDEATSALDSESERVVQESLDN--ASIGRTTIVIAHRLSTI-RNADVICVIHNGQI 573
Cdd:COG4619 148 QPDVLLLDEPTSALDPENTRRVEELLREylAEEGRAVLWVSHDPEQIeRVADRVLTLEAGRL 209
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
359-572 |
1.69e-43 |
|
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: 157.25 E-value: 1.69e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 359 VEFNHVKFTYLSRPETT--IFDDLCLKIPAGKTVALVGGSGSGKSTVISLlqrfydpIAGEI-LIDGvsidKLQVNwlrS 435
Cdd:cd03250 1 ISVEDASFTWDSGEQETsfTLKDINLEVPKGELVAIVGPVGSGKSSLLSA-------LLGELeKLSG----SVSVP---G 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 436 QMGLVSQEPVLFATSITENILFGKE--DASLDEVVEAAKASNAhtfISQFPLGYKTQVGERGVQMSGGQKQRIAIARAII 513
Cdd:cd03250 67 SIAYVSQEPWIQNGTIRENILFGKPfdEERYEKVIKACALEPD---LEILPDGDLTEIGEKGINLSGGQKQRISLARAVY 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15232977 514 KSPKILLLDEATSALDSESERVVQES--LDNASIGRTTIVIAHRLSTIRNADVICVIHNGQ 572
Cdd:cd03250 144 SDADIYLLDDPLSAVDAHVGRHIFENciLGLLLNNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
359-577 |
4.58e-43 |
|
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: 154.78 E-value: 4.58e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 359 VEFNHVKFTYLSRpETTIFDDLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYDPIAGEILIDGVSIDKLQVNwLRSQMG 438
Cdd:cd03247 1 LSINNVSFSYPEQ-EQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKA-LSSLIS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 439 LVSQEPVLFATSITENIlfgkedasldevveaakasnahtfisqfplgyktqvgerGVQMSGGQKQRIAIARAIIKSPKI 518
Cdd:cd03247 79 VLNQRPYLFDTTLRNNL---------------------------------------GRRFSGGERQRLALARILLQDAPI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15232977 519 LLLDEATSALDSESERVVQESLDNASIGRTTIVIAHRLSTIRNADVICVIHNGQIVETG 577
Cdd:cd03247 120 VLLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
673-939 |
1.23e-42 |
|
ABC transporter transmembrane region; This family represents a unit of six transmembrane helices. Many members of the ABC transporter family (pfam00005) have two such regions.
Pssm-ID: 459896 [Multi-domain] Cd Length: 274 Bit Score: 157.42 E-value: 1.23e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 673 LYGCLSAALVGVLQPVSAYSAGSVISVFFLTShDQIKEKTRIYVLLFVGLAIFSFLVNISQHYGFAYMGEYLTKRIREQM 752
Cdd:pfam00664 2 ILAILLAILSGAISPAFPLVLGRILDVLLPDG-DPETQALNVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 753 LSKILTFEVNWFDidDNSSGAICSRLAKDANVVRSMVGDRMSLLVQTISAVIIACIIGLVIAWRLAIVMISVQPLIVVCF 832
Cdd:pfam00664 81 FKKILRQPMSFFD--TNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILVS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 833 YTQRVLLKSLSEKASKAQDESSKLAAEAVSNIRTITAFSSQERIIKLLKKVQEGPRRESVHRSWLAGIVLGTSRSLITCT 912
Cdd:pfam00664 159 AVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLS 238
|
250 260 270
....*....|....*....|....*....|...
gi 15232977 913 SALNFWYGGRLIADGK------IVSKAFFEIFL 939
Cdd:pfam00664 239 YALALWFGAYLVISGElsvgdlVAFLSLFAQLF 271
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
995-1215 |
1.62e-42 |
|
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: 155.03 E-value: 1.62e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 995 ITFLNVDFAYPtrpDVVIFENFSIEIDEGKSTAIVGTSGSGKSTIIGLIERFYD-----PLKGTVKIDGRDIRS--YHLR 1067
Cdd:cd03260 1 IELRDLNVYYG---DKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIYDldVDVL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1068 SLRKYISLVSQEPMLFAGTIRENIMYG----GTSDKIDESEIIEAA--KAA---NAHDFITSLSngydtncgdkgvqLSG 1138
Cdd:cd03260 78 ELRRRVGMVFQKPNPFPGSIYDNVAYGlrlhGIKLKEELDERVEEAlrKAAlwdEVKDRLHALG-------------LSG 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15232977 1139 GQKQRIAIARAVLKNPSVLLLDEATSALDSKSERVVQDALERVMVGRTSIMIAHRLSTIQNC-DMIVVLGKGKIVESG 1215
Cdd:cd03260 145 GQQQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARVaDRTAFLLNGRLVEFG 222
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
995-1213 |
3.36e-42 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 154.43 E-value: 3.36e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 995 ITFLNVDFAYPT-RPDVVIFENFSIEIDEGKSTAIVGTSGSGKST---IIGLIERfydPLKGTVKIDGRDIRSY------ 1064
Cdd:COG1136 5 LELRNLTKSYGTgEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTllnILGGLDR---PTSGEVLIDGQDISSLserela 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1065 HLRslRKYISLVSQEPMLFAG-TIRENIM----YGGTSDKIDESEIIEAAKAANAHDFITSLSNgydtncgdkgvQLSGG 1139
Cdd:COG1136 82 RLR--RRHIGFVFQFFNLLPElTALENVAlpllLAGVSRKERRERARELLERVGLGDRLDHRPS-----------QLSGG 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15232977 1140 QKQRIAIARAVLKNPSVLLLDEATSALDSKSERVVQDALERV--MVGRTSIMIAHRLSTIQNCDMIVVLGKGKIVE 1213
Cdd:COG1136 149 QQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELnrELGTTIVMVTHDPELAARADRVIRLRDGRIVS 224
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
373-573 |
2.15e-41 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 150.06 E-value: 2.15e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 373 ETTIFDDLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYDPIAGEILIDGVSIDKLQVNWLRSQMGLVSQEPVLFATSIT 452
Cdd:cd03246 14 EPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGYLPQDDELFSGSIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 453 ENILfgkedasldevveaakasnahtfisqfplgyktqvgergvqmSGGQKQRIAIARAIIKSPKILLLDEATSALDSES 532
Cdd:cd03246 94 ENIL------------------------------------------SGGQRQRLGLARALYGNPRILVLDEPNSHLDVEG 131
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 15232977 533 ERVVQESLDNASI-GRTTIVIAHRLSTIRNADVICVIHNGQI 573
Cdd:cd03246 132 ERALNQAIAALKAaGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
360-572 |
3.91e-41 |
|
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: 150.70 E-value: 3.91e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 360 EFNHVKFTYlSRPETTIFDDLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYDPIAGEILIDGVSIDKLQVNWLRSQMGL 439
Cdd:cd03225 1 ELKNLSFSY-PDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 440 VSQEP--VLFATSITENILFGKEDASLDE------VVEAAKASNAHTFISQFPLgyktqvgergvQMSGGQKQRIAIARA 511
Cdd:cd03225 80 VFQNPddQFFGPTVEEEVAFGLENLGLPEeeieerVEEALELVGLEGLRDRSPF-----------TLSGGQKQRVAIAGV 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15232977 512 IIKSPKILLLDEATSALDSESERVVQESLDN-ASIGRTTIVIAHRLSTIRN-ADVICVIHNGQ 572
Cdd:cd03225 149 LAMDPDILLLDEPTAGLDPAGRRELLELLKKlKAEGKTIIIVTHDLDLLLElADRVIVLEDGK 211
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
999-1210 |
8.39e-41 |
|
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: 149.54 E-value: 8.39e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 999 NVDFAYPTRpDVVIFENFSIEIDEGKSTAIVGTSGSGKSTIIGLIERFYDPLKGTVKIDGRDIRSYHLRSLRKYISLVSQ 1078
Cdd:cd03225 4 NLSFSYPDG-ARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1079 EP--MLFAGTIRENIMYGGTSDKIDESEIIEAAKAANAHDFITSLSNgYDTNcgdkgvQLSGGQKQRIAIARAVLKNPSV 1156
Cdd:cd03225 83 NPddQFFGPTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRD-RSPF------TLSGGQKQRVAIAGVLAMDPDI 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 15232977 1157 LLLDEATSALDSKSERVVQDALERVM-VGRTSIMIAHRLSTIQN-CDMIVVLGKGK 1210
Cdd:cd03225 156 LLLDEPTAGLDPAGRRELLELLKKLKaEGKTIIIVTHDLDLLLElADRVIVLEDGK 211
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
359-591 |
8.49e-41 |
|
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: 158.53 E-value: 8.49e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 359 VEFNHVKFTYLSRP--ETTIFDDLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYDPIAGEILIDGVSIDKL---QVNWL 433
Cdd:COG1123 261 LEVRNLSKRYPVRGkgGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLsrrSLREL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 434 RSQMGLVSQEPV--LF-----ATSITE--NILFGKEDASLDEVVEAA------KASNAHTFISQFplgyktqvgergvqm 498
Cdd:COG1123 341 RRRVQMVFQDPYssLNprmtvGDIIAEplRLHGLLSRAERRERVAELlervglPPDLADRYPHEL--------------- 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 499 SGGQKQRIAIARAIIKSPKILLLDEATSALDSESERVVQESLD--NASIGRTTIVIAHRLSTIRN-ADVICVIHNGQIVE 575
Cdd:COG1123 406 SGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRdlQRELGLTYLFISHDLAVVRYiADRVAVMYDGRIVE 485
|
250
....*....|....*.
gi 15232977 576 TGSHEELLKRIDGQYT 591
Cdd:COG1123 486 DGPTEEVFANPQHPYT 501
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
377-526 |
1.02e-40 |
|
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: 147.02 E-value: 1.02e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 377 FDDLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYDPIAGEILIDGVSIDKLQVNWLRSQMGLVSQEPVLF-ATSITENI 455
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFpRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15232977 456 LFGkedASLDEVVEAAKASNAHTFISQFPLGY--KTQVGERGVQMSGGQKQRIAIARAIIKSPKILLLDEATS 526
Cdd:pfam00005 81 RLG---LLLKGLSKREKDARAEEALEKLGLGDlaDRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
357-578 |
1.28e-40 |
|
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: 149.10 E-value: 1.28e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 357 GEVEFNHVKFTYlsRPE-TTIFDDLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYDPIAGEILIDGVSIDKLQVNWLRS 435
Cdd:cd03369 5 GEIEVENLSVRY--APDlPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 436 QMGLVSQEPVLFATSITENI-LFGKEDAslDEVVEAAKasnahtfisqfplgyktqVGERGVQMSGGQKQRIAIARAIIK 514
Cdd:cd03369 83 SLTIIPQDPTLFSGTIRSNLdPFDEYSD--EEIYGALR------------------VSEGGLNLSQGQRQLLCLARALLK 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15232977 515 SPKILLLDEATSALDSESERVVQESLDNASIGRTTIVIAHRLSTIRNADVICVIHNGQIVETGS 578
Cdd:cd03369 143 RPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
999-1216 |
4.39e-40 |
|
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: 149.04 E-value: 4.39e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 999 NVDFAYPTRPdvvIFENFSIEIDEGKSTAIVGTSGSGKSTIIGLIERFYDPLKGTVKIDGRDIRSYHLRSLRKYISLVSQ 1078
Cdd:COG1120 6 NLSVGYGGRP---VLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAYVPQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1079 EPML-FAGTIRENIMYG--------GTSDKIDESEIIEAAKAANAHDFItslsngydtncgDKGV-QLSGGQKQRIAIAR 1148
Cdd:COG1120 83 EPPApFGLTVRELVALGryphlglfGRPSAEDREAVEEALERTGLEHLA------------DRPVdELSGGERQRVLIAR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15232977 1149 AVLKNPSVLLLDEATSALDSKS-----ERVVQDALERvmvGRTSIMIAHRLS-TIQNCDMIVVLGKGKIVESGT 1216
Cdd:COG1120 151 ALAQEPPLLLLDEPTSHLDLAHqlevlELLRRLARER---GRTVVMVLHDLNlAARYADRLVLLKDGRIVAQGP 221
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
3-594 |
6.52e-40 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 162.07 E-value: 6.52e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 3 KEDEKESGrdkMKSFGSIRSiFMHADGVDWILMALGLIgavgdgFITPVVVFIFNTLLNNLGTSSSNNKTFMQTISKNVV 82
Cdd:PLN03232 887 KQEERETG---IISWNVLMR-YNKAVGGLWVVMILLVC------YLTTEVLRVSSSTWLSIWTDQSTPKSYSPGFYIVVY 956
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 83 ALLyvACGSWVICFLEGYcWTRTGERQAA-RMREKYLRAVLRQDVGYFdlHVTSTSDVITSISSDSLVIQDFLSEKLPNF 161
Cdd:PLN03232 957 ALL--GFGQVAVTFTNSF-WLISSSLHAAkRLHDAMLNSILRAPMLFF--HTNPTGRVINRFSKDIGDIDRNVANLMNMF 1031
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 162 LMNA----SAFVASYIVSFILMWRLtivgFPFIILLLVPGLMYG------RALVSISRK-IHEQYNEAgsiaEQAISSVR 230
Cdd:PLN03232 1032 MNQLwqllSTFALIGTVSTISLWAI----MPLLILFYAAYLYYQstsrevRRLDSVTRSpIYAQFGEA----LNGLSSIR 1103
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 231 TVYAFGSENKMIGKFstaLRGSVKLGLRQGLAKG-ITIGS---NGVThaIWAFLTW--YGSRLVMNHGSKGGTVFVVISc 304
Cdd:PLN03232 1104 AYKAYDRMAKINGKS---MDNNIRFTLANTSSNRwLTIRLetlGGVM--IWLTATFavLRNGNAENQAGFASTMGLLLS- 1177
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 305 ITYGGVSLgqsLSN-LKYFSEAfvawERILEVIKRV----------PDIDSNKKEGQILErMKGEVEFNHVKFTYlsRPE 373
Cdd:PLN03232 1178 YTLNITTL---LSGvLRQASKA----ENSLNSVERVgnyidlpseaTAIIENNRPVSGWP-SRGSIKFEDVHLRY--RPG 1247
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 374 -TTIFDDLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYDPIAGEILIDGVSIDKLQVNWLRSQMGLVSQEPVLFATSIT 452
Cdd:PLN03232 1248 lPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVR 1327
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 453 ENILFGKE--DASLDEVVEAAKASNAhtfISQFPLGYKTQVGERGVQMSGGQKQRIAIARAIIKSPKILLLDEATSALDS 530
Cdd:PLN03232 1328 FNIDPFSEhnDADLWEALERAHIKDV---IDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDV 1404
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15232977 531 ESERVVQESLDNASIGRTTIVIAHRLSTIRNADVICVIHNGQIVETGSHEELLKRIDGQYTSLV 594
Cdd:PLN03232 1405 RTDSLIQRTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRDTSAFFRMV 1468
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
35-303 |
7.72e-40 |
|
ABC transporter transmembrane region; This family represents a unit of six transmembrane helices. Many members of the ABC transporter family (pfam00005) have two such regions.
Pssm-ID: 459896 [Multi-domain] Cd Length: 274 Bit Score: 149.33 E-value: 7.72e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 35 MALGLIGAVGDGFITPVVVFIFNTLLNNLGTSSSNNKtfmQTISKNVVALLYVACGSWVICFLEGYCWTRTGERQAARMR 114
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILDVLLPDGDPET---QALNVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 115 EKYLRAVLRQDVGYFDlhVTSTSDVITSISSDSLVIQDFLSEKLPNFLMNASAFVASYIVSFILMWRLTIVGFPFIILLL 194
Cdd:pfam00664 78 RKLFKKILRQPMSFFD--TNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 195 VPGLMYGRALVSISRKIHEQYNEAGSIAEQAISSVRTVYAFGSENKMIGKFSTALRGSVKLGLRQGLAKGITIG-SNGVT 273
Cdd:pfam00664 156 LVSAVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGiTQFIG 235
|
250 260 270
....*....|....*....|....*....|
gi 15232977 274 HAIWAFLTWYGSRLVMNHGSKGGTVFVVIS 303
Cdd:pfam00664 236 YLSYALALWFGAYLVISGELSVGDLVAFLS 265
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
998-1222 |
9.22e-40 |
|
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: 155.45 E-value: 9.22e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 998 LNVDFAYPTRPDVVIFENFSIEIDEGKSTAIVGTSGSGKSTIIGLIERFYDPLKGTVKIDGRDIRSYH---LRSLRKYIS 1074
Cdd:COG1123 266 LSKRYPVRGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSrrsLRELRRRVQ 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1075 LVSQEP--MLFAG-TIRENIMYG----GTSDKIDESEIIEA--------AKAANAHDFitslsngydtncgdkgvQLSGG 1139
Cdd:COG1123 346 MVFQDPysSLNPRmTVGDIIAEPlrlhGLLSRAERRERVAEllervglpPDLADRYPH-----------------ELSGG 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1140 QKQRIAIARAVLKNPSVLLLDEATSALDSKSERVVQDALERV--MVGRTSIMIAHRLSTIQN-CDMIVVLGKGKIVESGT 1216
Cdd:COG1123 409 QRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLqrELGLTYLFISHDLAVVRYiADRVAVMYDGRIVEDGP 488
|
....*.
gi 15232977 1217 HSSLLE 1222
Cdd:COG1123 489 TEEVFA 494
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
359-585 |
1.64e-39 |
|
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: 146.96 E-value: 1.64e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 359 VEFNHVKFTYLSRP-ETTIFDDLCLKIPAGKTVALVGGSGSGKSTV---ISLLQRfydPIAGEILIDGVSIDKL---QVN 431
Cdd:cd03258 2 IELKNVSKVFGDTGgKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLircINGLER---PTSGSVLVDGTDLTLLsgkELR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 432 WLRSQMGLVSQEPVLFAT-SITENILFGKEDASLDEVVEAAKASNAHTFIsqfplGYKTQVGERGVQMSGGQKQRIAIAR 510
Cdd:cd03258 79 KARRRIGMIFQHFNLLSSrTVFENVALPLEIAGVPKAEIEERVLELLELV-----GLEDKADAYPAQLSGGQKQRVGIAR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15232977 511 AIIKSPKILLLDEATSALDSESERVVQESLD--NASIGRTTIVIAHRLSTIRN-ADVICVIHNGQIVETGSHEELLKR 585
Cdd:cd03258 154 ALANNPKVLLCDEATSALDPETTQSILALLRdiNRELGLTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTVEEVFAN 231
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
995-1210 |
2.07e-39 |
|
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: 145.30 E-value: 2.07e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 995 ITFLNVDFAYPTRPDV--VIFENFSIEIDEGKSTAIVGTSGSGKST----IIGLIERfydpLKGTVKIDGRdirsyhlrs 1068
Cdd:cd03250 1 ISVEDASFTWDSGEQEtsFTLKDINLEVPKGELVAIVGPVGSGKSSllsaLLGELEK----LSGSVSVPGS--------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1069 lrkyISLVSQEPMLFAGTIRENIMYGgtsDKIDESEIIEAAKAANAHDFITSLSNGYDTNCGDKGVQLSGGQKQRIAIAR 1148
Cdd:cd03250 68 ----IAYVSQEPWIQNGTIRENILFG---KPFDEERYEKVIKACALEPDLEILPDGDLTEIGEKGINLSGGQKQRISLAR 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15232977 1149 AVLKNPSVLLLDEATSALDSK-SERVVQDAL-ERVMVGRTSIMIAHRLSTIQNCDMIVVLGKGK 1210
Cdd:cd03250 141 AVYSDADIYLLDDPLSAVDAHvGRHIFENCIlGLLLNNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
359-584 |
3.43e-39 |
|
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: 146.28 E-value: 3.43e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 359 VEFNHVKFTYLSRpetTIFDDLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYDPIAGEILIDGVSIDKL---QVNWLRS 435
Cdd:COG1127 6 IEVRNLTKSFGDR---VVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLsekELYELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 436 QMGLVSQEPVLFaTSIT--ENILF------GKEDASLDEVVEAAkasnahtfisqfpLGyktQVGERGV------QMSGG 501
Cdd:COG1127 83 RIGMLFQGGALF-DSLTvfENVAFplrehtDLSEAEIRELVLEK-------------LE---LVGLPGAadkmpsELSGG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 502 QKQRIAIARAIIKSPKILLLDEATSALDSESERVVQE---SLdNASIGRTTIVIAHRLSTIRN-ADVICVIHNGQIVETG 577
Cdd:COG1127 146 MRKRVALARALALDPEILLYDEPTAGLDPITSAVIDElirEL-RDELGLTSVVVTHDLDSAFAiADRVAVLADGKIIAEG 224
|
....*..
gi 15232977 578 SHEELLK 584
Cdd:COG1127 225 TPEELLA 231
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
359-584 |
4.11e-39 |
|
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: 145.72 E-value: 4.11e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 359 VEFNHVKFTYLSRpetTIFDDLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYDPIAGEILIDGVSIDKLQVNWL---RS 435
Cdd:cd03261 1 IELRGLTKSFGGR---TVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELyrlRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 436 QMGLVSQEPVLFaTSIT--ENILFG-KEDASLDEvveaakasnahTFISQFPLGYKTQVGERGV------QMSGGQKQRI 506
Cdd:cd03261 78 RMGMLFQSGALF-DSLTvfENVAFPlREHTRLSE-----------EEIREIVLEKLEAVGLRGAedlypaELSGGMKKRV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 507 AIARAIIKSPKILLLDEATSALDSESERVVQE---SLdNASIGRTTIVIAHRLSTIRN-ADVICVIHNGQIVETGSHEEL 582
Cdd:cd03261 146 ALARALALDPELLLYDEPTAGLDPIASGVIDDlirSL-KKELGLTSIMVTHDLDTAFAiADRIAVLYDGKIVAEGTPEEL 224
|
..
gi 15232977 583 LK 584
Cdd:cd03261 225 RA 226
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
995-1223 |
5.54e-39 |
|
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: 145.77 E-value: 5.54e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 995 ITFLNVDFAYPtrpDVVIFENFSIEIDEGKSTAIVGTSGSGKSTIIGLIERFYDPLKGTVKIDGRDIRSYhLRSLRKYIS 1074
Cdd:COG4555 2 IEVENLSKKYG---KVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKE-PREARRQIG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1075 LVSQEPMLFAG-TIRENIMYGGTSDKIDESEIIEAAKAAnAHDFItsLSNGYDTNCGDkgvqLSGGQKQRIAIARAVLKN 1153
Cdd:COG4555 78 VLPDERGLYDRlTVRENIRYFAELYGLFDEELKKRIEEL-IELLG--LEEFLDRRVGE----LSTGMKKKVALARALVHD 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15232977 1154 PSVLLLDEATSALDSKSERVVQDALERVM-VGRTSIMIAHRLSTIQN-CDMIVVLGKGKIVESGTHSSLLEK 1223
Cdd:COG4555 151 PKVLLLDEPTNGLDVMARRLLREILRALKkEGKTVLFSSHIMQEVEAlCDRVVILHKGKVVAQGSLDELREE 222
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
355-575 |
6.11e-39 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 144.80 E-value: 6.11e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 355 MKGEVEFNHVKFTY-LSRPETTIFDDLCLKIPAGKTVALVGGSGSGKST---VISLLQRfydPIAGEILIDGVSIDKL-- 428
Cdd:COG1136 1 MSPLLELRNLTKSYgTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTllnILGGLDR---PTSGEVLIDGQDISSLse 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 429 -QVNWLRSQ-MGLVSQEPVLFAT-SITENILFGkedASLDEVVEAAKASNAHTFISQFPLGYKtqVGERGVQMSGGQKQR 505
Cdd:COG1136 78 rELARLRRRhIGFVFQFFNLLPElTALENVALP---LLLAGVSRKERRERARELLERVGLGDR--LDHRPSQLSGGQQQR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15232977 506 IAIARAIIKSPKILLLDEATSALDSESERVVQESLD--NASIGRTTIVIAHRLSTIRNADVICVIHNGQIVE 575
Cdd:COG1136 153 VAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRelNRELGTTIVMVTHDPELAARADRVIRLRDGRIVS 224
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
999-1215 |
1.07e-38 |
|
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: 144.19 E-value: 1.07e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 999 NVDFAYPTRPDVV-IFENFSIEIDEGKSTAIVGTSGSGKSTIIGLIERFYDPLKGTVKIDGRDIRSY---HLRSLRKYIS 1074
Cdd:cd03257 6 NLSVSFPTGGGSVkALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLsrrLRKIRRKEIQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1075 LVSQEPM-----LFagTIRENIM-----YGGTSDKIDESEIIEAAKAA--NAHDFITSLSNgydtncgdkgvQLSGGQKQ 1142
Cdd:cd03257 86 MVFQDPMsslnpRM--TIGEQIAeplriHGKLSKKEARKEAVLLLLVGvgLPEEVLNRYPH-----------ELSGGQRQ 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15232977 1143 RIAIARAVLKNPSVLLLDEATSALDSKSERVVQDALE--RVMVGRTSIMIAHRLSTIQN-CDMIVVLGKGKIVESG 1215
Cdd:cd03257 153 RVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKklQEELGLTLLFITHDLGVVAKiADRVAVMYAGKIVEEG 228
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
1013-1164 |
1.14e-38 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 141.25 E-value: 1.14e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1013 FENFSIEIDEGKSTAIVGTSGSGKSTIIGLIERFYDPLKGTVKIDGRDIRSYHLRSLRKYISLVSQEPMLFAG-TIRENI 1091
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15232977 1092 MYG----GTSDKIDESEIIEAAKAANAHDFItslsngyDTNCGDKGVQLSGGQKQRIAIARAVLKNPSVLLLDEATS 1164
Cdd:pfam00005 81 RLGlllkGLSKREKDARAEEALEKLGLGDLA-------DRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
54-339 |
1.31e-38 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This group includes ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection, as well as ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins.
Pssm-ID: 350001 [Multi-domain] Cd Length: 289 Bit Score: 146.17 E-value: 1.31e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 54 FIFNTLLNNLGTSSSnnktfMQTISKNVVALLYVACGSWVICFLEGYCWTRTGERQAARMREKYLRAVLRQDVGYFDLHv 133
Cdd:cd18557 17 YLIGRLIDTIIKGGD-----LDVLNELALILLAIYLLQSVFTFVRYYLFNIAGERIVARLRRDLFSSLLRQEIAFFDKH- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 134 tSTSDVITSISSDSLVIQDFLSEKLPNFLMNASAFVASYIVSFILMWRLTIVGFPFIILLLVPGLMYGRALVSISRKIHE 213
Cdd:cd18557 91 -KTGELTSRLSSDTSVLQSAVTDNLSQLLRNILQVIGGLIILFILSWKLTLVLLLVIPLLLIASKIYGRYIRKLSKEVQD 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 214 QYNEAGSIAEQAISSVRTVYAFGSENKMIGKFSTALRGSVKLGLRQGLAKGITIGSNGVTHAIWAFLT-WYGSRLVMnhg 292
Cdd:cd18557 170 ALAKAGQVAEESLSNIRTVRSFSAEEKEIRRYSEALDRSYRLARKKALANALFQGITSLLIYLSLLLVlWYGGYLVL--- 246
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 15232977 293 SKGGTVFVVISCITYGGvSLGQSLSNLkyfSEAFVAWERILEVIKRV 339
Cdd:cd18557 247 SGQLTVGELTSFILYTI-MVASSVGGL---SSLLADIMKALGASERV 289
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
995-1221 |
5.50e-38 |
|
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: 142.33 E-value: 5.50e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 995 ITFLNVDFAYPTRP-DVVIFENFSIEIDEGKSTAIVGTSGSGKSTIIGLIERFYDPLKGTVKIDGRDI---RSYHLRSLR 1070
Cdd:cd03258 2 IELKNVSKVFGDTGgKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLtllSGKELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1071 KYISLVSQEPMLFAG-TIRENIMYGGTSDKIDESEIIEAAKA-------ANAHDFITSlsngydtncgdkgvQLSGGQKQ 1142
Cdd:cd03258 82 RRIGMIFQHFNLLSSrTVFENVALPLEIAGVPKAEIEERVLEllelvglEDKADAYPA--------------QLSGGQKQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1143 RIAIARAVLKNPSVLLLDEATSALDSKSERVVQDALERV--MVGRTSIMIAHRLSTIQN-CDMIVVLGKGKIVESGTHSS 1219
Cdd:cd03258 148 RVGIARALANNPKVLLCDEATSALDPETTQSILALLRDInrELGLTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTVEE 227
|
..
gi 15232977 1220 LL 1221
Cdd:cd03258 228 VF 229
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
359-577 |
9.08e-38 |
|
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: 141.12 E-value: 9.08e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 359 VEFNHVKFTYlsrPETTIFDDLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYDPIAGEILIDGVSIDKLQVNwlRSQMG 438
Cdd:cd03259 1 LELKGLSKTY---GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE--RRNIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 439 LVSQEPVLFAT-SITENILFGKEDASLDE------VVEAAKASNAHTFISQFPLgyktqvgergvQMSGGQKQRIAIARA 511
Cdd:cd03259 76 MVFQDYALFPHlTVAENIAFGLKLRGVPKaeirarVRELLELVGLEGLLNRYPH-----------ELSGGQQQRVALARA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15232977 512 IIKSPKILLLDEATSALDSESERVVQESLDN--ASIGRTTIVIAHRLS-TIRNADVICVIHNGQIVETG 577
Cdd:cd03259 145 LAREPSLLLLDEPLSALDAKLREELREELKElqRELGITTIYVTHDQEeALALADRIAVMNEGRIVQVG 213
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
1006-1215 |
1.65e-37 |
|
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: 140.35 E-value: 1.65e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1006 TRPDVVIFENFSIEIDEGKSTAIVGTSGSGKSTIIGLIERFYDPLKGTVKIDGRDIrsYHLRSLRKYISLVSQEPMLFAG 1085
Cdd:cd03259 9 TYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDV--TGVPPERRNIGMVFQDYALFPH 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1086 -TIRENIMYGGTSDKIDESEIIEAAKAANAHDFITSLSNGYDTncgdkgvQLSGGQKQRIAIARAVLKNPSVLLLDEATS 1164
Cdd:cd03259 87 lTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPH-------ELSGGQQQRVALARALAREPSLLLLDEPLS 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15232977 1165 ALDSKSERVVQDALERVM--VGRTSIMIAHRLS-TIQNCDMIVVLGKGKIVESG 1215
Cdd:cd03259 160 ALDAKLREELREELKELQreLGITTIYVTHDQEeALALADRIAVMNEGRIVQVG 213
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
355-585 |
1.67e-37 |
|
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: 148.90 E-value: 1.67e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 355 MKGEVEFNHVKFTYLSRPETTIfDDLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYDP---IAGEILIDGVSIDKLQVN 431
Cdd:COG1123 1 MTPLLEVRDLSVRYPGGDVPAV-DGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHggrISGEVLLDGRDLLELSEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 432 WLRSQMGLVSQEP--VLFATSITENILFGKE------DASLDEVVEAAKASNAHTFISQFPLgyktqvgergvQMSGGQK 503
Cdd:COG1123 80 LRGRRIGMVFQDPmtQLNPVTVGDQIAEALEnlglsrAEARARVLELLEAVGLERRLDRYPH-----------QLSGGQR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 504 QRIAIARAIIKSPKILLLDEATSALDSESERVVQESLD--NASIGRTTIVIAHRLSTI-RNADVICVIHNGQIVETGSHE 580
Cdd:COG1123 149 QRVAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRelQRERGTTVLLITHDLGVVaEIADRVVVMDDGRIVEDGPPE 228
|
....*
gi 15232977 581 ELLKR 585
Cdd:COG1123 229 EILAA 233
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
359-577 |
2.21e-37 |
|
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: 140.33 E-value: 2.21e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 359 VEFNHVKFTYLSRP-ETTIFDDLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYDPIAGEILIDGVSIDKL---QVNWLR 434
Cdd:cd03257 2 LEVKNLSVSFPTGGgSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLsrrLRKIRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 435 SQMGLVSQEPVL-------FATSITE--NILFGKEDASLDEVVEAAKAS---NAHTFISQFPlgyktqvgergVQMSGGQ 502
Cdd:cd03257 82 KEIQMVFQDPMSslnprmtIGEQIAEplRIHGKLSKKEARKEAVLLLLVgvgLPEEVLNRYP-----------HELSGGQ 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15232977 503 KQRIAIARAIIKSPKILLLDEATSALDSESERVVQESLDN--ASIGRTTIVIAHRLSTIRN-ADVICVIHNGQIVETG 577
Cdd:cd03257 151 RQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKlqEELGLTLLFITHDLGVVAKiADRVAVMYAGKIVEEG 228
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
359-586 |
3.10e-37 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 140.20 E-value: 3.10e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 359 VEFNHVKFTYlsrPETTIFDDLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYDPIAGEILIDGVSIDKLQVNWlRSQMG 438
Cdd:COG1131 1 IEVRGLTKRY---GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEV-RRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 439 LVSQEPVLFAT-SITENI-----LFGKEDASLDEVVEAAkasnahtfISQFPLG--YKTQVGergvQMSGGQKQRIAIAR 510
Cdd:COG1131 77 YVPQEPALYPDlTVRENLrffarLYGLPRKEARERIDEL--------LELFGLTdaADRKVG----TLSGGMKQRLGLAL 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15232977 511 AIIKSPKILLLDEATSALDSESERVVQESLDNASIGRTTIVIA-HRLSTI-RNADVICVIHNGQIVETGSHEELLKRI 586
Cdd:COG1131 145 ALLHDPELLILDEPTSGLDPEARRELWELLRELAAEGKTVLLStHYLEEAeRLCDRVAIIDKGRIVADGTPDELKARL 222
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
995-1222 |
4.89e-37 |
|
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: 147.36 E-value: 4.89e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 995 ITFLNVDFAYPTRPDVVIfENFSIEIDEGKSTAIVGTSGSGKST----IIGLIERFYDpLKGTVKIDGRDIRSYHLRSLR 1070
Cdd:COG1123 5 LEVRDLSVRYPGGDVPAV-DGVSLTIAPGETVALVGESGSGKSTlalaLMGLLPHGGR-ISGEVLLDGRDLLELSEALRG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1071 KYISLVSQEPM--LFAGTIRENIMYGGTSDKIDESEIIEAAKAANAHDFITSLSNGYDTncgdkgvQLSGGQKQRIAIAR 1148
Cdd:COG1123 83 RRIGMVFQDPMtqLNPVTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPH-------QLSGGQRQRVAIAM 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15232977 1149 AVLKNPSVLLLDEATSALDSKSERVVQDALERVMV--GRTSIMIAHRLSTI-QNCDMIVVLGKGKIVESGTHSSLLE 1222
Cdd:COG1123 156 ALALDPDLLIADEPTTALDVTTQAEILDLLRELQRerGTTVLLITHDLGVVaEIADRVVVMDDGRIVEDGPPEEILA 232
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
1009-1223 |
6.90e-37 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 139.43 E-value: 6.90e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1009 DVVIFENFSIEIDEGKSTAIVGTSGSGKSTIIGLIERFYDPLKGTVKIDGRDIRSyHLRSLRKYISLVSQEPMLFAG-TI 1087
Cdd:COG1131 12 DKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVAR-DPAEVRRRIGYVPQEPALYPDlTV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1088 RENI-MYG---GTSDKIDESEIIEAAKAANAHDFItslsngyDTNCGdkgvQLSGGQKQRIAIARAVLKNPSVLLLDEAT 1163
Cdd:COG1131 91 RENLrFFArlyGLPRKEARERIDELLELFGLTDAA-------DRKVG----TLSGGMKQRLGLALALLHDPELLILDEPT 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15232977 1164 SALDSKSERVVQDALERVMVGRTSIMIA-HRLSTIQN-CDMIVVLGKGKIVESGTHSSLLEK 1223
Cdd:COG1131 160 SGLDPEARRELWELLRELAAEGKTVLLStHYLEEAERlCDRVAIIDKGRIVADGTPDELKAR 221
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
379-582 |
7.20e-37 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 140.17 E-value: 7.20e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 379 DLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYD--PIA---GEILIDGVSI--DKLQVNWLRSQMGLVSQEPVLFATSI 451
Cdd:COG1117 29 DINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDliPGArveGEILLDGEDIydPDVDVVELRRRVGMVFQKPNPFPKSI 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 452 TENILFG------KEDASLDEVVEAAkasnahtfisqfpLgykTQVG----------ERGVQMSGGQKQRIAIARAIIKS 515
Cdd:COG1117 109 YDNVAYGlrlhgiKSKSELDEIVEES-------------L---RKAAlwdevkdrlkKSALGLSGGQQQRLCIARALAVE 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15232977 516 PKILLLDEATSALDSESERVVQESLDNASiGRTTIVI-------AHRLStirnaDVICVIHNGQIVETGSHEEL 582
Cdd:COG1117 173 PEVLLMDEPTSALDPISTAKIEELILELK-KDYTIVIvthnmqqAARVS-----DYTAFFYLGELVEFGPTEQI 240
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
359-583 |
1.68e-36 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 138.20 E-value: 1.68e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 359 VEFNHVKFTYlsrPETTIFDDLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYDPIAGEILIDGVSID--KLQVNWLRSQ 436
Cdd:COG1126 2 IEIENLHKSF---GDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTdsKKDINKLRRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 437 MGLVSQEPVLFA-TSITENILFG--------KEDAS------LDEVVEAAKASnahtfisQFPlgyktqvgergVQMSGG 501
Cdd:COG1126 79 VGMVFQQFNLFPhLTVLENVTLApikvkkmsKAEAEeramelLERVGLADKAD-------AYP-----------AQLSGG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 502 QKQRIAIARAIIKSPKILLLDEATSALDSEserVVQESLDN----ASIGRTTIVIAHRLSTIRN-ADVICVIHNGQIVET 576
Cdd:COG1126 141 QQQRVAIARALAMEPKVMLFDEPTSALDPE---LVGEVLDVmrdlAKEGMTMVVVTHEMGFAREvADRVVFMDGGRIVEE 217
|
....*..
gi 15232977 577 GSHEELL 583
Cdd:COG1126 218 GPPEEFF 224
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
999-1210 |
2.62e-36 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 134.68 E-value: 2.62e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 999 NVDFAYPTRPdvvIFENFSIEIDEGKSTAIVGTSGSGKSTIIGLIERFYDPLKGTVKIDGRDIRSYHLRSLRKYISLVSQ 1078
Cdd:cd00267 4 NLSFRYGGRT---ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1079 epmlfagtirenimyggtsdkideseiieaakaanahdfitslsngydtncgdkgvqLSGGQKQRIAIARAVLKNPSVLL 1158
Cdd:cd00267 81 ---------------------------------------------------------LSGGQRQRVALARALLLNPDLLL 103
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15232977 1159 LDEATSALDSKSERVVQDALERVMV-GRTSIMIAHRLSTIQN-CDMIVVLGKGK 1210
Cdd:cd00267 104 LDEPTSGLDPASRERLLELLRELAEeGRTVIIVTHDPELAELaADRVIVLKDGK 157
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
995-1216 |
3.81e-36 |
|
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: 137.25 E-value: 3.81e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 995 ITFLNVDFAYPTRpdvVIFENFSIEIDEGKSTAIVGTSGSGKSTIIGLIERFYDPLKGTVKIDGRDIRS---YHLRSLRK 1071
Cdd:cd03261 1 IELRGLTKSFGGR---TVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGlseAELYRLRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1072 YISLVSQEPMLFAG-TIRENIMY------GGTSDKIDE--SEIIEAAKAANAHDFITSlsngydtncgdkgvQLSGGQKQ 1142
Cdd:cd03261 78 RMGMLFQSGALFDSlTVFENVAFplrehtRLSEEEIREivLEKLEAVGLRGAEDLYPA--------------ELSGGMKK 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15232977 1143 RIAIARAVLKNPSVLLLDEATSALDSKSERVVQDALERV--MVGRTSIMIAHRLSTI-QNCDMIVVLGKGKIVESGT 1216
Cdd:cd03261 144 RVALARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLkkELGLTSIMVTHDLDTAfAIADRIAVLYDGKIVAEGT 220
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
359-576 |
4.09e-36 |
|
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: 136.45 E-value: 4.09e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 359 VEFNHVKFTY-LSRPETTIFDDLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYDPIAGEILIDGVSIDKLqvnwlRSQM 437
Cdd:cd03293 1 LEVRNVSKTYgGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGP-----GPDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 438 GLVSQEPVLFA-TSITENILFGKEdasLDEVVEAAKASNAHTFISQFPLgyKTQVGERGVQMSGGQKQRIAIARAIIKSP 516
Cdd:cd03293 76 GYVFQQDALLPwLTVLDNVALGLE---LQGVPKAEARERAEELLELVGL--SGFENAYPHQLSGGMRQRVALARALAVDP 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15232977 517 KILLLDEATSALDSESERVVQESLDN--ASIGRTTIVIAHRLS-TIRNADVICVIHN--GQIVET 576
Cdd:cd03293 151 DVLLLDEPFSALDALTREQLQEELLDiwRETGKTVLLVTHDIDeAVFLADRVVVLSArpGRIVAE 215
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
995-1213 |
4.82e-36 |
|
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: 136.45 E-value: 4.82e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 995 ITFLNVDFAYPT-RPDVVIFENFSIEIDEGKSTAIVGTSGSGKSTIIGLIERFYDPLKGTVKIDGRDIRSYHLRslrkyI 1073
Cdd:cd03293 1 LEVRNVSKTYGGgGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPD-----R 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1074 SLVSQEPMLFA-GTIRENIMYGGTSDKIDESEIIEAAKAA--------NAHDFITslsngydtncgdkgvQLSGGQKQRI 1144
Cdd:cd03293 76 GYVFQQDALLPwLTVLDNVALGLELQGVPKAEARERAEELlelvglsgFENAYPH---------------QLSGGMRQRV 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15232977 1145 AIARAVLKNPSVLLLDEATSALDSKSERVVQDALERVMV--GRTSIMIAHRLS-TIQNCDMIVVLGK--GKIVE 1213
Cdd:cd03293 141 ALARALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRetGKTVLLVTHDIDeAVFLADRVVVLSArpGRIVA 214
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
999-1229 |
5.46e-36 |
|
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: 137.24 E-value: 5.46e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 999 NVDFAYPTRP-DVVIFENFSIEIDEGKSTAIVGTSGSGKSTIIGLIERFYDPLKGTVKIDGRDIRSYHLRSLRKYISLVS 1077
Cdd:COG1124 6 NLSVSYGQGGrRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRVQMVF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1078 QEPML-------FAGTIRENIMYGGTSDkiDESEIIEAAKAAN-AHDFITSLSNgydtncgdkgvQLSGGQKQRIAIARA 1149
Cdd:COG1124 86 QDPYAslhprhtVDRILAEPLRIHGLPD--REERIAELLEQVGlPPSFLDRYPH-----------QLSGGQRQRVAIARA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1150 VLKNPSVLLLDEATSALDSkserVVQ----DALERVMV--GRTSIMIAHRLSTIQN-CDMIVVLGKGKIVESGThSSLLE 1222
Cdd:COG1124 153 LILEPELLLLDEPTSALDV----SVQaeilNLLKDLREerGLTYLFVSHDLAVVAHlCDRVAVMQNGRIVEELT-VADLL 227
|
....*..
gi 15232977 1223 KGPTGTY 1229
Cdd:COG1124 228 AGPKHPY 234
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
355-585 |
6.43e-36 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 140.23 E-value: 6.43e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 355 MKGEVEFNHVKFTYlsrPETTIFDDLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYDPIAGEILIDGVSIDKLQVNwlR 434
Cdd:COG3842 2 AMPALELENVSKRY---GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPE--K 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 435 SQMGLVSQEPVLFA-TSITENILFG-------KEDAslDEVVEAAkasnahtfISQFPLGyktQVGERGV-QMSGGQKQR 505
Cdd:COG3842 77 RNVGMVFQDYALFPhLTVAENVAFGlrmrgvpKAEI--RARVAEL--------LELVGLE---GLADRYPhQLSGGQQQR 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 506 IAIARAIIKSPKILLLDEATSALDSESERVVQESLDN--ASIGRTTIVIAHRLS---TIrnADVICVIHNGQIVETGSHE 580
Cdd:COG3842 144 VALARALAPEPRVLLLDEPLSALDAKLREEMREELRRlqRELGITFIYVTHDQEealAL--ADRIAVMNDGRIEQVGTPE 221
|
....*
gi 15232977 581 ELLKR 585
Cdd:COG3842 222 EIYER 226
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
995-1216 |
6.83e-36 |
|
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: 136.65 E-value: 6.83e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 995 ITFLNVDFAYPTRpdvVIFENFSIEIDEGKSTAIVGTSGSGKST----IIGLIErfydPLKGTVKIDGRDI---RSYHLR 1067
Cdd:COG1127 6 IEVRNLTKSFGDR---VVLDGVSLDVPRGEILAIIGGSGSGKSVllklIIGLLR----PDSGEILVDGQDItglSEKELY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1068 SLRKYISLVSQEPMLFAG-TIRENIMYG---GTsdKIDESEIIEAAKA-------ANAHDFITSlsngydtncgdkgvQL 1136
Cdd:COG1127 79 ELRRRIGMLFQGGALFDSlTVFENVAFPlreHT--DLSEAEIRELVLEklelvglPGAADKMPS--------------EL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1137 SGGQKQRIAIARAVLKNPSVLLLDEATSALDSKSERVV-------QDALervmvGRTSIMIAHRLSTIQN-CDMIVVLGK 1208
Cdd:COG1127 143 SGGMRKRVALARALALDPEILLYDEPTAGLDPITSAVIdelirelRDEL-----GLTSVVVTHDLDSAFAiADRVAVLAD 217
|
....*...
gi 15232977 1209 GKIVESGT 1216
Cdd:COG1127 218 GKIIAEGT 225
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
359-573 |
7.08e-36 |
|
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: 135.70 E-value: 7.08e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 359 VEFNHVKFTYLSRPETT-IFDDLCLKIPAGKTVALVGGSGSGKST---VISLLQRfydPIAGEILIDGVSIDKLQVNWL- 433
Cdd:cd03255 1 IELKNLSKTYGGGGEKVqALKGVSLSIEKGEFVAIVGPSGSGKSTllnILGGLDR---PTSGEVRVDGTDISKLSEKELa 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 434 ---RSQMGLVSQEPVLFAT-SITENILFGkedASLDEVVEAAKASNAHTFISQfpLGYKTQVGERGVQMSGGQKQRIAIA 509
Cdd:cd03255 78 afrRRHIGFVFQSFNLLPDlTALENVELP---LLLAGVPKKERRERAEELLER--VGLGDRLNHYPSELSGGQQQRVAIA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15232977 510 RAIIKSPKILLLDEATSALDSESERVVQESLD--NASIGRTTIVIAHRLSTIRNADVICVIHNGQI 573
Cdd:cd03255 153 RALANDPKIILADEPTGNLDSETGKEVMELLRelNKEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
106-584 |
7.26e-36 |
|
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: 148.94 E-value: 7.26e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 106 GERQAAR-MREKYLRAVLRQDVGYFDlhVTSTSDVITSISSDSLVIQDFLSEKLPNFLMNASAFVASYIVSFILMWRLTI 184
Cdd:TIGR00957 1032 GGIQASRvLHQDLLHNKLRSPMSFFE--RTPSGNLVNRFSKELDTVDSMIPPVIKMFMGSLFNVIGALIVILLATPIAAV 1109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 185 VGFPFIILLLVPGLMYG------RALVSISRK-IHEQYNEAgsiaeqaISSVRTVYAFGSENKMIGKFSTALRGSVKLGL 257
Cdd:TIGR00957 1110 IIPPLGLLYFFVQRFYVassrqlKRLESVSRSpVYSHFNET-------LLGVSVIRAFEEQERFIHQSDLKVDENQKAYY 1182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 258 RQGLA-KGITIGSNGVTHAIWAFLTWYG--SRLVMNHGSKGGTVFVVISCITYggvslgqslsnLKYFSEAFVAWERILE 334
Cdd:TIGR00957 1183 PSIVAnRWLAVRLECVGNCIVLFAALFAviSRHSLSAGLVGLSVSYSLQVTFY-----------LNWLVRMSSEMETNIV 1251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 335 VIKRVPDIDSNKKEG--QILERM-------KGEVEFNHVKFTYlsRPETT-IFDDLCLKIPAGKTVALVGGSGSGKSTVI 404
Cdd:TIGR00957 1252 AVERLKEYSETEKEApwQIQETAppsgwppRGRVEFRNYCLRY--REDLDlVLRHINVTIHGGEKVGIVGRTGAGKSSLT 1329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 405 SLLQRFYDPIAGEILIDGVSIDKLQVNWLRSQMGLVSQEPVLFATSITENI-LFGKedASLDEVVEAAKASNAHTFISQF 483
Cdd:TIGR00957 1330 LGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNLdPFSQ--YSDEEVWWALELAHLKTFVSAL 1407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 484 PLGYKTQVGERGVQMSGGQKQRIAIARAIIKSPKILLLDEATSALDSESERVVQESLDNASIGRTTIVIAHRLSTIRNAD 563
Cdd:TIGR00957 1408 PDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYT 1487
|
490 500
....*....|....*....|.
gi 15232977 564 VICVIHNGQIVETGSHEELLK 584
Cdd:TIGR00957 1488 RVIVLDKGEVAEFGAPSNLLQ 1508
|
|
| ABC_6TM_Pgp_ABCB1 |
cd18558 |
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; ... |
35-328 |
7.48e-36 |
|
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1(ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350002 [Multi-domain] Cd Length: 312 Bit Score: 138.95 E-value: 7.48e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 35 MALGLIGAVGDGFITPVVVFIFNTLLNNLGTSSSNNKTFM-------------QTISKNVVALLY--VACGSWVICFLEG 99
Cdd:cd18558 1 MVVGILCAIIHGGLLPAFMVIFGDMTDSFTNGGMTNITGNssglnssagpfekLEEEMTLYAYYYliIGAIVLITAYIQG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 100 YCWTRTGERQAARMREKYLRAVLRQDVGYFDLHvtSTSDVITSISSDSLVIQDFLSEKLPNFLMNASAFVASYIVSFILM 179
Cdd:cd18558 81 SFWGLAAGRQTKKIRYKFFHAIMRQEIGWFDVN--DTGELNTRLADDVSKINEGIGDKIGVIFQNIATFGTGFIIGFIRG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 180 WRLTIVGFPFIILLLVPGLMYGRALVSISRKIHEQYNEAGSIAEQAISSVRTVYAFGSENKMIGKFSTALRGSVKLGLRQ 259
Cdd:cd18558 159 WKLTLVILAISPVLGLSAVVWAKILSGFTDKEKKAYAKAGAVAEEVLEAFRTVIAFGGQQKEETRYAQNLEIAKRNGIKK 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 260 GLAKGITIG-SNGVTHAIWAFLTWYGSRLVMNHGSKGGTVFVVISCITYGGVSLGQSLSNLKYFSEAFVA 328
Cdd:cd18558 239 AITFNISMGaAFLLIYASYALAFWYGTYLVTQQEYSIGEVLTVFFSVLIGAFSAGQQVPSIEAFANARGA 308
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
359-591 |
8.42e-36 |
|
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: 136.47 E-value: 8.42e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 359 VEFNHVKFTYLSRPE-TTIFDDLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYDPIAGEILIDGVSIDKLQVNWLRSQM 437
Cdd:COG1124 2 LEVRNLSVSYGQGGRrVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 438 GLVSQEP---------VlfATSITENILFGKEDASLDEVVEAAKASN-AHTFISQFPlgyktqvgergVQMSGGQKQRIA 507
Cdd:COG1124 82 QMVFQDPyaslhprhtV--DRILAEPLRIHGLPDREERIAELLEQVGlPPSFLDRYP-----------HQLSGGQRQRVA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 508 IARAIIKSPKILLLDEATSALDSeserVVQ-ESLD-----NASIGRTTIVIAHRLSTI-RNADVICVIHNGQIVETGSHE 580
Cdd:COG1124 149 IARALILEPELLLLDEPTSALDV----SVQaEILNllkdlREERGLTYLFVSHDLAVVaHLCDRVAVMQNGRIVEELTVA 224
|
250
....*....|.
gi 15232977 581 ELLKRIDGQYT 591
Cdd:COG1124 225 DLLAGPKHPYT 235
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
995-1221 |
9.03e-36 |
|
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: 136.28 E-value: 9.03e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 995 ITFLNVDFAYPTRPDVVifENFSIEIDEGKSTAIVGTSGSGKSTIIGLIERFYDPLKGTVKIDGRDIRSYHLRSLRKYIS 1074
Cdd:cd03295 1 IEFENVTKRYGGGKKAV--NNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1075 LVSQEPMLFAG-TIRENIMYGGTSDKIDESEIIEAAKAANA--HDFITSLSNGYDTncgdkgvQLSGGQKQRIAIARAVL 1151
Cdd:cd03295 79 YVIQQIGLFPHmTVEENIALVPKLLKWPKEKIRERADELLAlvGLDPAEFADRYPH-------ELSGGQQQRVGVARALA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15232977 1152 KNPSVLLLDEATSALDSKSERVVQDALERV--MVGRTSIMIAHRL-STIQNCDMIVVLGKGKIVESGTHSSLL 1221
Cdd:cd03295 152 ADPPLLLMDEPFGALDPITRDQLQEEFKRLqqELGKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEIL 224
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
995-1222 |
1.42e-35 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 136.66 E-value: 1.42e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 995 ITFLNVDFAYPTRPDVVIfENFSIEIDEGKSTAIVGTSGSGKSTIIGLIERFYDPLKGTVKIDGRDIRSYHLRSLRKYIS 1074
Cdd:PRK13632 8 IKVENVSFSYPNSENNAL-KNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1075 LVSQEP-MLFAG-TIRENIMYGGTSDKIDESE----IIEAAKAANAHDFItslsngydtncgDKGVQ-LSGGQKQRIAIA 1147
Cdd:PRK13632 87 IIFQNPdNQFIGaTVEDDIAFGLENKKVPPKKmkdiIDDLAKKVGMEDYL------------DKEPQnLSGGQKQRVAIA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15232977 1148 RAVLKNPSVLLLDEATSALDSKSERVVQDALE--RVMVGRTSIMIAHRLSTIQNCDMIVVLGKGKIVESGTHSSLLE 1222
Cdd:PRK13632 155 SVLALNPEIIIFDESTSMLDPKGKREIKKIMVdlRKTRKKTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEILN 231
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
995-1211 |
1.57e-35 |
|
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: 134.92 E-value: 1.57e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 995 ITFLNVDFAYPTRPD-VVIFENFSIEIDEGKSTAIVGTSGSGKST---IIGLIERfydPLKGTVKIDGRDIRSYHLRSL- 1069
Cdd:cd03255 1 IELKNLSKTYGGGGEkVQALKGVSLSIEKGEFVAIVGPSGSGKSTllnILGGLDR---PTSGEVRVDGTDISKLSEKELa 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1070 ---RKYISLVSQE----PMLfagTIRENIMYGGTSDKIDESEIIEAAKAA--------NAHDFITslsngydtncgdkgv 1134
Cdd:cd03255 78 afrRRHIGFVFQSfnllPDL---TALENVELPLLLAGVPKKERRERAEELlervglgdRLNHYPS--------------- 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15232977 1135 QLSGGQKQRIAIARAVLKNPSVLLLDEATSALDSKSERVVQDALERV--MVGRTSIMIAHRLSTIQNCDMIVVLGKGKI 1211
Cdd:cd03255 140 ELSGGQQQRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRELnkEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
359-572 |
2.33e-35 |
|
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: 132.70 E-value: 2.33e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 359 VEFNHVKFTYlsrPETTIFDDLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYDPIAGEILIDGVSIDKLQVNW--LRSQ 436
Cdd:cd03229 1 LELKNVSKRY---GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELppLRRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 437 MGLVSQEPVLFAT-SITENILFGkedasldevveaakasnahtfisqfplgyktqvgergvqMSGGQKQRIAIARAIIKS 515
Cdd:cd03229 78 IGMVFQDFALFPHlTVLENIALG---------------------------------------LSGGQQQRVALARALAMD 118
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 516 PKILLLDEATSALDSESERVVQESLD--NASIGRTTIVIAHRLS-TIRNADVICVIHNGQ 572
Cdd:cd03229 119 PDVLLLDEPTSALDPITRREVRALLKslQAQLGITVVLVTHDLDeAARLADRVVVLRDGK 178
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
384-594 |
2.84e-35 |
|
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: 135.42 E-value: 2.84e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 384 IPAGKTVALVGGSGSGKSTVISLLQRFYDPIAGEILIDGVSIDKLQVNWLRSQMGLVSQEPVLFATSITENILFGKE--D 461
Cdd:cd03288 44 IKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPILFSGSIRFNLDPECKctD 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 462 ASLDEVVEAAKASNahtFISQFPLGYKTQVGERGVQMSGGQKQRIAIARAIIKSPKILLLDEATSALDSESERVVQESLD 541
Cdd:cd03288 124 DRLWEALEIAQLKN---MVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENILQKVVM 200
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15232977 542 NASIGRTTIVIAHRLSTIRNADVICVIHNGQIVETGSHEELLKRIDGQYTSLV 594
Cdd:cd03288 201 TAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQEDGVFASLV 253
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
359-585 |
3.47e-35 |
|
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: 134.74 E-value: 3.47e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 359 VEFNHVKFTYLSRPetTIFDDLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYDPIAGEILIDGVSIDKLQVNWLRSQMG 438
Cdd:cd03295 1 IEFENVTKRYGGGK--KAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 439 LVSQEPVLFA-TSITENI-LFGKedasLDEVVEAAKASNAHTFISQFPLGYKTQVGERGVQMSGGQKQRIAIARAIIKSP 516
Cdd:cd03295 79 YVIQQIGLFPhMTVEENIaLVPK----LLKWPKEKIRERADELLALVGLDPAEFADRYPHELSGGQQQRVGVARALAADP 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15232977 517 KILLLDEATSALDSESERVVQESLD--NASIGRTTIVIAHRL-STIRNADVICVIHNGQIVETGSHEELLKR 585
Cdd:cd03295 155 PLLLMDEPFGALDPITRDQLQEEFKrlQQELGKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEILRS 226
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
359-587 |
3.90e-35 |
|
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: 135.25 E-value: 3.90e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 359 VEFNHVKFTYlsrPETTIF--DDLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYDPIAGEILIDGVS-IDKLQVNWLRS 435
Cdd:TIGR04520 1 IEVENVSFSY---PESEKPalKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDtLDEENLWEIRK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 436 QMGLVSQEP--VLFATSITENILFGKEDASLD------EVVEAAKASNAHTFISQFPLgyktqvgergvQMSGGQKQRIA 507
Cdd:TIGR04520 78 KVGMVFQNPdnQFVGATVEDDVAFGLENLGVPreemrkRVDEALKLVGMEDFRDREPH-----------LLSGGQKQRVA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 508 IARAIIKSPKILLLDEATSALDSESERVVQESLD--NASIGRTTIVIAHRLSTIRNADVICVIHNGQIVETGSHEELLKR 585
Cdd:TIGR04520 147 IAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRklNKEEGITVISITHDMEEAVLADRVIVMNKGKIVAEGTPREIFSQ 226
|
..
gi 15232977 586 ID 587
Cdd:TIGR04520 227 VE 228
|
|
| ABC_6TM_Pgp_ABCB1 |
cd18558 |
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; ... |
673-971 |
5.85e-35 |
|
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1(ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350002 [Multi-domain] Cd Length: 312 Bit Score: 136.25 E-value: 5.85e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 673 LYGCLSAALVGVLQPVSAYSAGSVISVFFLTSHDQI-----------------KEKTRIYVLLFVGLAIFSFLVNISQHY 735
Cdd:cd18558 2 VVGILCAIIHGGLLPAFMVIFGDMTDSFTNGGMTNItgnssglnssagpfeklEEEMTLYAYYYLIIGAIVLITAYIQGS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 736 GFAYMGEYLTKRIREQMLSKILTFEVNWFDIddNSSGAICSRLAKDANVVRSMVGDRMSLLVQTISAVIIACIIGLVIAW 815
Cdd:cd18558 82 FWGLAAGRQTKKIRYKFFHAIMRQEIGWFDV--NDTGELNTRLADDVSKINEGIGDKIGVIFQNIATFGTGFIIGFIRGW 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 816 RLAIVMISVQPLIVVCFYTQRVLLKSLSEKASKAQDESSKLAAEAVSNIRTITAFSSQERIIKLLKKVQEGPRRESVHRS 895
Cdd:cd18558 160 KLTLVILAISPVLGLSAVVWAKILSGFTDKEKKAYAKAGAVAEEVLEAFRTVIAFGGQQKEETRYAQNLEIAKRNGIKKA 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15232977 896 WLAGIVLGTSRSLITCTSALNFWYGGRLIADGKIvskAFFEIFLIFVTTGRVIADAGTMTTDLARGLDAVGSVFAV 971
Cdd:cd18558 240 ITFNISMGAAFLLIYASYALAFWYGTYLVTQQEY---SIGEVLTVFFSVLIGAFSAGQQVPSIEAFANARGAAYHI 312
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
1006-1210 |
6.06e-35 |
|
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: 131.54 E-value: 6.06e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1006 TRPDVVIFENFSIEIDEGKSTAIVGTSGSGKSTIIGLIERFYDPLKGTVKIDGRDIRSY--HLRSLRKYISLVSQEPMLF 1083
Cdd:cd03229 9 RYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLedELPPLRRRIGMVFQDFALF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1084 AG-TIRENIMYGgtsdkideseiieaakaanahdfitslsngydtncgdkgvqLSGGQKQRIAIARAVLKNPSVLLLDEA 1162
Cdd:cd03229 89 PHlTVLENIALG-----------------------------------------LSGGQQQRVALARALAMDPDVLLLDEP 127
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 15232977 1163 TSALDSKSERVVQDALERV--MVGRTSIMIAHRLSTIQN-CDMIVVLGKGK 1210
Cdd:cd03229 128 TSALDPITRREVRALLKSLqaQLGITVVLVTHDLDEAARlADRVVVLRDGK 178
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
360-572 |
7.92e-35 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 130.44 E-value: 7.92e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 360 EFNHVKFTYlsrPETTIFDDLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYDPIAGEILIDGVSIDKLQVNWLRSQMGL 439
Cdd:cd00267 1 EIENLSFRY---GGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 440 VSQepvlfatsitenilfgkedasldevveaakasnahtfisqfplgyktqvgergvqMSGGQKQRIAIARAIIKSPKIL 519
Cdd:cd00267 78 VPQ-------------------------------------------------------LSGGQRQRVALARALLLNPDLL 102
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15232977 520 LLDEATSALDSESERVVQESL-DNASIGRTTIVIAHRLSTIRNA-DVICVIHNGQ 572
Cdd:cd00267 103 LLDEPTSGLDPASRERLLELLrELAEEGRTVIIVTHDPELAELAaDRVIVLKDGK 157
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
359-583 |
9.93e-35 |
|
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: 133.63 E-value: 9.93e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 359 VEFNHVKFTYlsrPETTIFDDLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYDPIAGEILIDGVSIDKLQVNWLRSQMG 438
Cdd:COG1120 2 LEAENLSVGY---GGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 439 LVSQEPVL-FATSITENIL---------FGKEDASLDEVVEAA-KASNAHTFIsqfplgyktqvgERGV-QMSGGQKQRI 506
Cdd:COG1120 79 YVPQEPPApFGLTVRELVAlgryphlglFGRPSAEDREAVEEAlERTGLEHLA------------DRPVdELSGGERQRV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 507 AIARAIIKSPKILLLDEATSALD----SESERVVQESldNASIGRTTIVIAHRLS-TIRNADVICVIHNGQIVETGSHEE 581
Cdd:COG1120 147 LIARALAQEPPLLLLDEPTSHLDlahqLEVLELLRRL--ARERGRTVVMVLHDLNlAARYADRLVLLKDGRIVAQGPPEE 224
|
..
gi 15232977 582 LL 583
Cdd:COG1120 225 VL 226
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
360-589 |
1.05e-34 |
|
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: 133.44 E-value: 1.05e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 360 EFNHVKFTYLSRPettIFDDLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYDPIAGEILIDGVSIDKlQVNWLRSQMGL 439
Cdd:COG4555 3 EVENLSKKYGKVP---ALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRK-EPREARRQIGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 440 VSQEPVLFAT-SITENI-----LFGKEDASLDEVVEAakasnahtFISQFPLG--YKTQVGErgvqMSGGQKQRIAIARA 511
Cdd:COG4555 79 LPDERGLYDRlTVRENIryfaeLYGLFDEELKKRIEE--------LIELLGLEefLDRRVGE----LSTGMKKKVALARA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 512 IIKSPKILLLDEATSALDSESERVVQESLDN-ASIGRTTIVIAHRLSTIRN-ADVICVIHNGQIVETGSHEELLKRIDGQ 589
Cdd:COG4555 147 LVHDPKVLLLDEPTNGLDVMARRLLREILRAlKKEGKTVLFSSHIMQEVEAlCDRVVILHKGKVVAQGSLDELREEIGEE 226
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
1015-1223 |
1.47e-34 |
|
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: 133.54 E-value: 1.47e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1015 NFSIEIDEGKSTAIVGTSGSGKSTIIGLIERFYDPLKGTVKIDGRDIRSYH---LRSLR-KYISLVSQEPMLFAG-TIRE 1089
Cdd:cd03294 42 DVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSrkeLRELRrKKISMVFQSFALLPHrTVLE 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1090 NIMYG----GTSDKIDESEIIEAAKAANAHDFITSLSNgydtncgdkgvQLSGGQKQRIAIARAVLKNPSVLLLDEATSA 1165
Cdd:cd03294 122 NVAFGlevqGVPRAEREERAAEALELVGLEGWEHKYPD-----------ELSGGMQQRVGLARALAVDPDILLMDEAFSA 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15232977 1166 LDSKSERVVQDALERV--MVGRTSIMIAHRLS-TIQNCDMIVVLGKGKIVESGTHSSLLEK 1223
Cdd:cd03294 191 LDPLIRREMQDELLRLqaELQKTIVFITHDLDeALRLGDRIAIMKDGRLVQVGTPEEILTN 251
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
995-1216 |
1.66e-34 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 135.59 E-value: 1.66e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 995 ITFLNVDFAYPTRP-DVVIFENFSIEIDEGKSTAIVGTSGSGKSTIIGLI---ERfydPLKGTVKIDGRDIRSYH---LR 1067
Cdd:COG1135 2 IELENLSKTFPTKGgPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCInllER---PTSGSVLVDGVDLTALSereLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1068 SLRKYISLVSQEPMLFAG-TIRENIMYGGTSDKIDESEIieAAKAANAHDFItSLSngydtncgDKG----VQLSGGQKQ 1142
Cdd:COG1135 79 AARRKIGMIFQHFNLLSSrTVAENVALPLEIAGVPKAEI--RKRVAELLELV-GLS--------DKAdaypSQLSGGQKQ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15232977 1143 RIAIARAVLKNPSVLLLDEATSALDSKSERVVQDALERV---MvGRTSIMIAHRLSTIQN-CDMIVVLGKGKIVESGT 1216
Cdd:COG1135 148 RVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDInreL-GLTIVLITHEMDVVRRiCDRVAVLENGRIVEQGP 224
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
995-1223 |
3.78e-34 |
|
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: 132.55 E-value: 3.78e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 995 ITFLNVDFAYPTRPDVVIfENFSIEIDEGKSTAIVGTSGSGKSTIIGLIERFYDPLKGTVKIDGRDIRS-YHLRSLRKYI 1073
Cdd:TIGR04520 1 IEVENVSFSYPESEKPAL-KNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLDeENLWEIRKKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1074 SLVSQEP--MLFAGTIRENIMYGGTSDKIDESEII----EAAKAANAHDFITSLSNgydtncgdkgvQLSGGQKQRIAIA 1147
Cdd:TIGR04520 80 GMVFQNPdnQFVGATVEDDVAFGLENLGVPREEMRkrvdEALKLVGMEDFRDREPH-----------LLSGGQKQRVAIA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1148 RAVLKNPSVLLLDEATSALDSKSERVVQDALERVM--VGRTSIMIAHRLSTIQNCDMIVVLGKGKIVESGT------HSS 1219
Cdd:TIGR04520 149 GVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNkeEGITVISITHDMEEAVLADRVIVMNKGKIVAEGTpreifsQVE 228
|
....
gi 15232977 1220 LLEK 1223
Cdd:TIGR04520 229 LLKE 232
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
359-609 |
6.68e-34 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 132.04 E-value: 6.68e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 359 VEFNHVKFTYlSRPETTIFDDLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYDPIAGEILIDGVSIDKLQVNWLRSQMG 438
Cdd:PRK13632 8 IKVENVSFSY-PNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 439 LVSQEP--VLFATSITENILFGKEDASLDE------VVEAAKASNAHTFISQFPLgyktqvgergvQMSGGQKQRIAIAR 510
Cdd:PRK13632 87 IIFQNPdnQFIGATVEDDIAFGLENKKVPPkkmkdiIDDLAKKVGMEDYLDKEPQ-----------NLSGGQKQRVAIAS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 511 AIIKSPKILLLDEATSALDSESERVVQESLDN--ASIGRTTIVIAHRLSTIRNADVICVIHNGQIVETGSHEELLK---- 584
Cdd:PRK13632 156 VLALNPEIIIFDESTSMLDPKGKREIKKIMVDlrKTRKKTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEILNnkei 235
|
250 260
....*....|....*....|....*....
gi 15232977 585 ----RIDGQYTSLVSlQQMENEESNVNIN 609
Cdd:PRK13632 236 lekaKIDSPFIYKLS-KKLKGIDPTYNEE 263
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
995-1216 |
6.83e-34 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 134.07 E-value: 6.83e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 995 ITFLNVDFAYPtrpDVVIFENFSIEIDEGKSTAIVGTSGSGKSTIIGLIERFYDPLKGTVKIDGRDIRsyHLRSLRKYIS 1074
Cdd:COG3842 6 LELENVSKRYG---DVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVT--GLPPEKRNVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1075 LVSQEPMLFAG-TIRENIMYGGTSDKIDESEIieAAKAANAHDfITSLSnGYdtncGDKGV-QLSGGQKQRIAIARAVLK 1152
Cdd:COG3842 81 MVFQDYALFPHlTVAENVAFGLRMRGVPKAEI--RARVAELLE-LVGLE-GL----ADRYPhQLSGGQQQRVALARALAP 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15232977 1153 NPSVLLLDEATSALDSKSERVVQDALERVM--VGRTSIMIAH------RLStiqncDMIVVLGKGKIVESGT 1216
Cdd:COG3842 153 EPRVLLLDEPLSALDAKLREEMREELRRLQreLGITFIYVTHdqeealALA-----DRIAVMNDGRIEQVGT 219
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
995-1213 |
8.93e-34 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 130.98 E-value: 8.93e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 995 ITFLNVDFAYPTRP-DVVIFENFSIEIDEGKSTAIVGTSGSGKSTIIGLIERFYDPLKGTVKIDGRDIRSYHLRslrkyI 1073
Cdd:COG1116 8 LELRGVSKRFPTGGgGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPD-----R 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1074 SLVSQEPMLFA-GTIRENIMYGGTSDKIDESEIIEAAKAANAH----DFITSLSNgydtncgdkgvQLSGGQKQRIAIAR 1148
Cdd:COG1116 83 GVVFQEPALLPwLTVLDNVALGLELRGVPKAERRERARELLELvglaGFEDAYPH-----------QLSGGMRQRVAIAR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15232977 1149 AVLKNPSVLLLDEATSALDSKSERVVQDALERVM--VGRTSIMIAH------RLStiqncDMIVVLGK--GKIVE 1213
Cdd:COG1116 152 ALANDPEVLLMDEPFGALDALTRERLQDELLRLWqeTGKTVLFVTHdvdeavFLA-----DRVVVLSArpGRIVE 221
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
378-585 |
1.14e-33 |
|
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: 132.48 E-value: 1.14e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 378 DDLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYDP---IAGEILIDGVSIDKL---QVNWLR-SQMGLVSQEPvlfATS 450
Cdd:COG0444 22 DGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLsekELRKIRgREIQMIFQDP---MTS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 451 ----------ITENIL----FGKEDAsLDEVVEAAKA---SNAHTFISQFPlgyktqvgergVQMSGGQKQRIAIARAII 513
Cdd:COG0444 99 lnpvmtvgdqIAEPLRihggLSKAEA-RERAIELLERvglPDPERRLDRYP-----------HELSGGMRQRVMIARALA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 514 KSPKILLLDEATSALDseserV-VQesldnASI-----------GRTTIVIAHRLSTIRN-ADVICVIHNGQIVETGSHE 580
Cdd:COG0444 167 LEPKLLIADEPTTALD-----VtIQ-----AQIlnllkdlqrelGLAILFITHDLGVVAEiADRVAVMYAGRIVEEGPVE 236
|
....*
gi 15232977 581 ELLKR 585
Cdd:COG0444 237 ELFEN 241
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
359-574 |
1.33e-33 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 130.18 E-value: 1.33e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 359 VEFNHVKFTYLSRpeTTIFDDLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYDPIAGEILIDGVSIDKL---QVNWLRS 435
Cdd:COG3638 3 LELRNLSKRYPGG--TPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALrgrALRRLRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 436 QMGLVSQEPVLFA-TSITENILFGKedasldevveAAKASNAHTFISQFP-------LGYKTQVG------ERGVQMSGG 501
Cdd:COG3638 81 RIGMIFQQFNLVPrLSVLTNVLAGR----------LGRTSTWRSLLGLFPpedreraLEALERVGladkayQRADQLSGG 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15232977 502 QKQRIAIARAIIKSPKILLLDEATSALDSESERVVQESL--DNASIGRTTIVIAHRLSTIRN-ADVICVIHNGQIV 574
Cdd:COG3638 151 QQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLrrIAREDGITVVVNLHQVDLARRyADRIIGLRDGRVV 226
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
359-575 |
1.33e-33 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 129.40 E-value: 1.33e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 359 VEFNHVKFTYlsRPETTIFDDLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYDPIAGEILIDGVSIDKL---QVNWLRS 435
Cdd:COG2884 2 IRFENVSKRY--PGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLkrrEIPYLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 436 QMGLVSQE-PVLFATSITENILF-----GKEDASLDEVVEAAkasnahtfISQFPLGYKTQVgeRGVQMSGGQKQRIAIA 509
Cdd:COG2884 80 RIGVVFQDfRLLPDRTVYENVALplrvtGKSRKEIRRRVREV--------LDLVGLSDKAKA--LPHELSGGEQQRVAIA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15232977 510 RAIIKSPKILLLDEATSALDSE-SERVVQ--ESLdNASiGrTTIVIA-HRLSTIRNAD--VIcVIHNGQIVE 575
Cdd:COG2884 150 RALVNRPELLLADEPTGNLDPEtSWEIMEllEEI-NRR-G-TTVLIAtHDLELVDRMPkrVL-ELEDGRLVR 217
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
366-1206 |
1.86e-33 |
|
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: 140.82 E-value: 1.86e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 366 FTYLSRPETTIFDDLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYDPIAGEILIDGvsidklqvnwlrsQMGLVSQEPV 445
Cdd:TIGR01271 431 FSNFSLYVTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG-------------RISFSPQTSW 497
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 446 LFATSITENILFGkedASLDEV--VEAAKASNAHTFISQFPLGYKTQVGERGVQMSGGQKQRIAIARAIIKSPKILLLDE 523
Cdd:TIGR01271 498 IMPGTIKDNIIFG---LSYDEYryTSVIKACQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDS 574
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 524 ATSALDSESERVVQES-LDNASIGRTTIVIAHRLSTIRNADVICVIHNGQIVETGSHEELL-KRID--GQYTSLVSLQQM 599
Cdd:TIGR01271 575 PFTHLDVVTEKEIFEScLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSELQaKRPDfsSLLLGLEAFDNF 654
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 600 ENEESNVNINVSVTKDQVMSLSKDFKYSQ--HNSIGST--------SSSIVTN--------------------------V 643
Cdd:TIGR01271 655 SAERRNSILTETLRRVSIDGDSTVFSGPEtiKQSFKQPppefaekrKQSIILNpiasarkfsfvqmgpqkaqattiedaV 734
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 644 SD-------LIPNDNQ--PLVP-------------------------------------SFTRLMVMNRPE--------- 668
Cdd:TIGR01271 735 REpserkfsLVPEDEQgeESLPrgnqyhhglqhqaqrrqsvlqlmthsnrgenrreqlqTSFRKKSSITQQnelaseldi 814
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 669 --------------------------------------WKHAL-YGCLSAALVGVLQPV----SAYSAGSVISVFFLT-- 703
Cdd:TIGR01271 815 ysrrlskdsvyeiseeineedlkecfaderenvfetttWNTYLrYITTNRNLVFVLIFClvifLAEVAASLLGLWLITdn 894
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 704 ---------------SHDQIKEK----TRIYVLLFVGLAIFSFLVNISQHYGFAYMGEYLT--KRIREQMLSKILTFEVN 762
Cdd:TIGR01271 895 psapnyvdqqhanasSPDVQKPViitpTSAYYIFYIYVGTADSVLALGFFRGLPLVHTLLTvsKRLHEQMLHSVLQAPMA 974
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 763 WFdiDDNSSGAICSRLAKDANVVRSMVGDRMSLLVQTISAVIIA-CIIGLVIAWrlaiVMISVQPLIVVcFYTQRVLLKS 841
Cdd:TIGR01271 975 VL--NTMKAGRILNRFTKDMAIIDDMLPLTLFDFIQLTLIVLGAiFVVSVLQPY----IFIAAIPVAVI-FIMLRAYFLR 1047
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 842 LSEKASKAQDES-SKLAAEAVSNIR---TITAFSSQERIIKLLKKVQegprreSVHRS-WLagIVLGTSRslitctsaln 916
Cdd:TIGR01271 1048 TSQQLKQLESEArSPIFSHLITSLKglwTIRAFGRQSYFETLFHKAL------NLHTAnWF--LYLSTLR---------- 1109
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 917 fWYGGRLiadgKIVSKAFFE--IFLIFVTTGRVIADAGTMTT-----------------DLARGLDAVGSVFAVLDRCTT 977
Cdd:TIGR01271 1110 -WFQMRI----DIIFVFFFIavTFIAIGTNQDGEGEVGIILTlamnilstlqwavnssiDVDGLMRSVSRVFKFIDLPQE 1184
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 978 I-EPKNPDGYV------------AEKI---KGQITFLNVDFAYpTRPDVVIFENFSIEIDEGKSTAIVGTSGSGKSTIIG 1041
Cdd:TIGR01271 1185 EpRPSGGGGKYqlstvlvienphAQKCwpsGGQMDVQGLTAKY-TEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLS 1263
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1042 LIERFYDPlKGTVKIDGRDIRSYHLRSLRKYISLVSQEPMLFAGTIRENI-MYGGTSDKidesEIIEAAKAANAHDFITS 1120
Cdd:TIGR01271 1264 ALLRLLST-EGEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKNLdPYEQWSDE----EIWKVAEEVGLKSVIEQ 1338
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1121 LSNGYDTNCGDKGVQLSGGQKQRIAIARAVLKNPSVLLLDEATSALDSKSERVVQDALERVMVGRTSIMIAHRLSTIQNC 1200
Cdd:TIGR01271 1339 FPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRVEALLEC 1418
|
....*.
gi 15232977 1201 DMIVVL 1206
Cdd:TIGR01271 1419 QQFLVI 1424
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
976-1229 |
1.96e-33 |
|
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: 130.03 E-value: 1.96e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 976 TTIEPKNPDGYVAEKIKGQITFLNVDFAYPTRPdvvIFENFSIEIDEGKSTAIVGTSGSGKSTIIGLIERFYDPLKGTVK 1055
Cdd:cd03288 3 ASISGSSNSGLVGLGGEIKIHDLCVRYENNLKP---VLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1056 IDGRDIRSYHLRSLRKYISLVSQEPMLFAGTIRENImygGTSDKIDESEIIEAAKAANAHDFITSLSNGYDTNCGDKGVQ 1135
Cdd:cd03288 80 IDGIDISKLPLHTLRSRLSIILQDPILFSGSIRFNL---DPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGEN 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1136 LSGGQKQRIAIARAVLKNPSVLLLDEATSALDSKSERVVQDALERVMVGRTSIMIAHRLSTIQNCDMIVVLGKGKIVESG 1215
Cdd:cd03288 157 FSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECD 236
|
250
....*....|....*.
gi 15232977 1216 THSSLL--EKGPTGTY 1229
Cdd:cd03288 237 TPENLLaqEDGVFASL 252
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
999-1215 |
2.08e-33 |
|
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: 127.17 E-value: 2.08e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 999 NVDFAYPTRpdvVIFENFSIEIDEGKSTAIVGTSGSGKSTIIGLIERFYDPLKGTVKIDGRDIRSYHLRSLRKYISLVSQ 1078
Cdd:cd03214 4 NLSVGYGGR---TVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1079 epmlfagtirenimyggtsdkideseiieAAKAANAHDFItslsngydtncgDKGV-QLSGGQKQRIAIARAVLKNPSVL 1157
Cdd:cd03214 81 -----------------------------ALELLGLAHLA------------DRPFnELSGGERQRVLLARALAQEPPIL 119
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15232977 1158 LLDEATSALDSKS-----ERVVQDALERvmvGRTSIMIAHRLS-TIQNCDMIVVLGKGKIVESG 1215
Cdd:cd03214 120 LLDEPTSHLDIAHqiellELLRRLARER---GKTVVMVLHDLNlAARYADRVILLKDGRIVAQG 180
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
357-594 |
2.64e-33 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 140.64 E-value: 2.64e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 357 GEVEFNHVKFTYlsRPE-TTIFDDLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYDPIAGEILIDGVSIDKLQVNWLRS 435
Cdd:PLN03130 1236 GSIKFEDVVLRY--RPElPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRK 1313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 436 QMGLVSQEPVLFATSITENI-LFGK-EDASLDEVVEAAKASNAhtfISQFPLGYKTQVGERGVQMSGGQKQRIAIARAII 513
Cdd:PLN03130 1314 VLGIIPQAPVLFSGTVRFNLdPFNEhNDADLWESLERAHLKDV---IRRNSLGLDAEVSEAGENFSVGQRQLLSLARALL 1390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 514 KSPKILLLDEATSALDSESERVVQESLDNASIGRTTIVIAHRLSTIRNADVICVIHNGQIVETGSHEELLKRIDGQYTSL 593
Cdd:PLN03130 1391 RRSKILVLDEATAAVDVRTDALIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLSNEGSAFSKM 1470
|
.
gi 15232977 594 V 594
Cdd:PLN03130 1471 V 1471
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
376-573 |
4.74e-33 |
|
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: 127.65 E-value: 4.74e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 376 IFDDLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYDPIAGEILIDGVSI--DKLQVNWLRSQMGLVSQEPVLFA-TSIT 452
Cdd:cd03262 15 VLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLtdDKKNINELRQKVGMVFQQFNLFPhLTVL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 453 ENILFG--------KEDAS------LDEVVEAAKASnahtfisQFPlgyktqvgergVQMSGGQKQRIAIARAIIKSPKI 518
Cdd:cd03262 95 ENITLApikvkgmsKAEAEeralelLEKVGLADKAD-------AYP-----------AQLSGGQQQRVAIARALAMNPKV 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 519 LLLDEATSALDSEserVVQESLDN----ASIGRTTIVIAHRLSTIRN-ADVICVIHNGQI 573
Cdd:cd03262 157 MLFDEPTSALDPE---LVGEVLDVmkdlAEEGMTMVVVTHEMGFAREvADRVIFMDDGRI 213
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
359-582 |
5.56e-33 |
|
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: 128.12 E-value: 5.56e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 359 VEFNHVKFTYLSrpeTTIFDDLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYDPIAGEILIDGVSIDKLQVNwlRSQMG 438
Cdd:cd03300 1 IELENVSKFYGG---FVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPH--KRPVN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 439 LVSQEPVLFA-TSITENILFGKEDASLDEVVEAAKASNAHTFISQFPLGYKtqvgeRGVQMSGGQKQRIAIARAIIKSPK 517
Cdd:cd03300 76 TVFQNYALFPhLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANR-----KPSQLSGGQQQRVAIARALVNEPK 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15232977 518 ILLLDEATSALDSESERVVQESLDN--ASIGRTTIVIAHRLS-TIRNADVICVIHNGQIVETGSHEEL 582
Cdd:cd03300 151 VLLLDEPLGALDLKLRKDMQLELKRlqKELGITFVFVTHDQEeALTMSDRIAVMNKGKIQQIGTPEEI 218
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
359-585 |
8.06e-33 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 130.58 E-value: 8.06e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 359 VEFNHVKFTYLSRP-ETTIFDDLCLKIPAGKTVALVGGSGSGKST---VISLLQRfydPIAGEILIDGVSIDKL---QVN 431
Cdd:COG1135 2 IELENLSKTFPTKGgPVTALDDVSLTIEKGEIFGIIGYSGAGKSTlirCINLLER---PTSGSVLVDGVDLTALserELR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 432 WLRSQMGLVSQEPVLFAtSIT--ENILF-------GKED-----ASLDEVVE-AAKASnahtfisQFPlgyktqvgergV 496
Cdd:COG1135 79 AARRKIGMIFQHFNLLS-SRTvaENVALpleiagvPKAEirkrvAELLELVGlSDKAD-------AYP-----------S 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 497 QMSGGQKQRIAIARAIIKSPKILLLDEATSALDSESERVVQESLD--NASIGRTTIVIAHRLSTIRN-ADVICVIHNGQI 573
Cdd:COG1135 140 QLSGGQKQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKdiNRELGLTIVLITHEMDVVRRiCDRVAVLENGRI 219
|
250
....*....|..
gi 15232977 574 VETGSHEELLKR 585
Cdd:COG1135 220 VEQGPVLDVFAN 231
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
360-582 |
9.89e-33 |
|
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: 127.68 E-value: 9.89e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 360 EFNHVKFTYLSrpETTIFDDLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYDPIAGEILIDGVSIDKLQVNWL---RSQ 436
Cdd:cd03256 2 EVENLSKTYPN--GKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALrqlRRQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 437 MGLVSQEPVLFA-TSITENILFGKedasldevveAAKASNAHTFISQFP-------LGYKTQVG------ERGVQMSGGQ 502
Cdd:cd03256 80 IGMIFQQFNLIErLSVLENVLSGR----------LGRRSTWRSLFGLFPkeekqraLAALERVGlldkayQRADQLSGGQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 503 KQRIAIARAIIKSPKILLLDEATSALDSESERVVQESL--DNASIGRTTIVIAHRLSTIR-NADVICVIHNGQIVETGSH 579
Cdd:cd03256 150 QQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLkrINREEGITVIVSLHQVDLAReYADRIVGLKDGRIVFDGPP 229
|
...
gi 15232977 580 EEL 582
Cdd:cd03256 230 AEL 232
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
359-576 |
1.72e-32 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 127.51 E-value: 1.72e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 359 VEFNHVKFTYLSRP-ETTIFDDLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYDPIAGEILIDGVSIDKLqvnwlRSQM 437
Cdd:COG1116 8 LELRGVSKRFPTGGgGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGP-----GPDR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 438 GLVSQEPVLFA-TSITENILFGKEDASLDEvveAAKASNAHTFISQfplgyktqVGERGV------QMSGGQKQRIAIAR 510
Cdd:COG1116 83 GVVFQEPALLPwLTVLDNVALGLELRGVPK---AERRERARELLEL--------VGLAGFedayphQLSGGMRQRVAIAR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15232977 511 AIIKSPKILLLDEATSALDSESERVVQESLDN--ASIGRTTIVIAH------RLstirnADVICVIHN--GQIVET 576
Cdd:COG1116 152 ALANDPEVLLMDEPFGALDALTRERLQDELLRlwQETGKTVLFVTHdvdeavFL-----ADRVVVLSArpGRIVEE 222
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
1009-1216 |
2.17e-32 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 126.26 E-value: 2.17e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1009 DVVIFENFSIEIDEGKSTAIVGTSGSGKSTIIGLIERFYDPLKGTVKIDGRDI--RSYHLRSLRKYISLVSQEPMLFAG- 1085
Cdd:COG1126 13 DLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLtdSKKDINKLRRKVGMVFQQFNLFPHl 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1086 TIRENIMYGG-TSDKIDESEIIEAAKA----------ANAHDFitslsngydtncgdkgvQLSGGQKQRIAIARAVLKNP 1154
Cdd:COG1126 93 TVLENVTLAPiKVKKMSKAEAEERAMEllervgladkADAYPA-----------------QLSGGQQQRVAIARALAMEP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15232977 1155 SVLLLDEATSALDSkseRVVQDALErVMV-----GRTSIMIAHRLSTIQN-CDMIVVLGKGKIVESGT 1216
Cdd:COG1126 156 KVMLFDEPTSALDP---ELVGEVLD-VMRdlakeGMTMVVVTHEMGFAREvADRVVFMDGGRIVEEGP 219
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1015-1216 |
3.99e-32 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 129.11 E-value: 3.99e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1015 NFSIEIDEGKSTAIVGTSGSGKST---IIGLIERfydPLKGTVKIDGRDIRSyHLRSLRKYISLVSQEPMLFAG-TIREN 1090
Cdd:COG1118 20 DVSLEIASGELVALLGPSGSGKTTllrIIAGLET---PDSGRIVLNGRDLFT-NLPPRERRVGFVFQHYALFPHmTVAEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1091 IMYGGTSDKIDESEIieaakAANAHDFI-----TSLSNGYDTncgdkgvQLSGGQKQRIAIARAVLKNPSVLLLDEATSA 1165
Cdd:COG1118 96 IAFGLRVRPPSKAEI-----RARVEELLelvqlEGLADRYPS-------QLSGGQRQRVALARALAVEPEVLLLDEPFGA 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15232977 1166 LDSKservVQDALERVM------VGRTSIMIAH------RLstiqnCDMIVVLGKGKIVESGT 1216
Cdd:COG1118 164 LDAK----VRKELRRWLrrlhdeLGGTTVFVTHdqeealEL-----ADRVVVMNQGRIEQVGT 217
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
673-929 |
4.01e-32 |
|
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family represents a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in this family. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting chemical diversity of the translocated substrates, whereas NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional unit. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349983 [Multi-domain] Cd Length: 292 Bit Score: 127.28 E-value: 4.01e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 673 LYGCLSAALVGVLQPVSAYSAGSVISVFFLtshDQIKEKTRIYVLLFVGLAIFSFLVNISQHYGFAYMGEYLTKRIREQM 752
Cdd:cd07346 2 LLALLLLLLATALGLALPLLTKLLIDDVIP---AGDLSLLLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 753 LSKILTFEVNWFDidDNSSGAICSRLAKDANVVRSMVGDRMSLLVQTISAVIIACIIGLVIAWRLAIVMISVQPLIVVCF 832
Cdd:cd07346 79 FRHLQRLSLSFFD--RNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVLIL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 833 YTQRVLLKSLSEKASKAQDESSKLAAEAVSNIRTITAFSSQERIIKLLKKVQEGPRRESVHRSWLAGIVLGTSRSLITCT 912
Cdd:cd07346 157 RYFRRRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGLLTALG 236
|
250
....*....|....*..
gi 15232977 913 SALNFWYGGRLIADGKI 929
Cdd:cd07346 237 TALVLLYGGYLVLQGSL 253
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
379-583 |
5.75e-32 |
|
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: 126.22 E-value: 5.75e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 379 DLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYDPIAGEILIDGVSIDKL---QVNWLRSQ-MGLVSQEPVLFA-TSITE 453
Cdd:cd03294 42 DVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMsrkELRELRRKkISMVFQSFALLPhRTVLE 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 454 NILFGKEDASLDEVVEAAKASNAhtfISQFPL-GYKTQVGErgvQMSGGQKQRIAIARAIIKSPKILLLDEATSALDSES 532
Cdd:cd03294 122 NVAFGLEVQGVPRAEREERAAEA---LELVGLeGWEHKYPD---ELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLI 195
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15232977 533 ERVVQESLDN--ASIGRTTIVIAHRLS-TIRNADVICVIHNGQIVETGSHEELL 583
Cdd:cd03294 196 RREMQDELLRlqAELQKTIVFITHDLDeALRLGDRIAIMKDGRLVQVGTPEEIL 249
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
74-319 |
6.84e-32 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen processing; This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350016 [Multi-domain] Cd Length: 289 Bit Score: 126.50 E-value: 6.84e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 74 MQTISKNVVALLYVACGSWVICFLEGYCWTRTGERQAARMREKYLRAVLRQDVGYFDlhVTSTSDVITSISSDSLVIQDF 153
Cdd:cd18572 32 REAFYRAVLLLLLLSVLSGLFSGLRGGCFSYAGTRLVRRLRRDLFRSLLRQDIAFFD--ATKTGELTSRLTSDCQKVSDP 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 154 LSEKLPNFLMNASAFVASYIVSFILMWRLTIVGF-PFIILLLVPGLmYGRALVSISRKIHEQYNEAGSIAEQAISSVRTV 232
Cdd:cd18572 110 LSTNLNVFLRNLVQLVGGLAFMFSLSWRLTLLAFiTVPVIALITKV-YGRYYRKLSKEIQDALAEANQVAEEALSNIRTV 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 233 YAFGSENKMIGKFSTALRGSVKLGLRQGLAKGITIGSNGVT-HAIWAFLTWYGSRLVMNHGSKGGTvfvVISCITYGGvS 311
Cdd:cd18572 189 RSFATEEREARRYERALDKALKLSVRQALAYAGYVAVNTLLqNGTQVLVLFYGGHLVLSGRMSAGQ---LVTFMLYQQ-Q 264
|
....*...
gi 15232977 312 LGQSLSNL 319
Cdd:cd18572 265 LGEAFQSL 272
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
359-573 |
8.72e-32 |
|
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: 122.51 E-value: 8.72e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 359 VEFNHVKFTYlsrPETTIFDDLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYDPIAGEILIDGVSIDKLQVNwLRSQMG 438
Cdd:cd03230 1 IEVRNLSKRY---GKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEE-VKRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 439 LVSQEPVLFAT-SITENILFgkedasldevveaakasnahtfisqfplgyktqvgergvqmSGGQKQRIAIARAIIKSPK 517
Cdd:cd03230 77 YLPEEPSLYENlTVRENLKL-----------------------------------------SGGMKQRLALAQALLHDPE 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15232977 518 ILLLDEATSALDSESERVVQESLDN-ASIGRTTIVIAHRLSTIRN-ADVICVIHNGQI 573
Cdd:cd03230 116 LLILDEPTSGLDPESRREFWELLRElKKEGKTILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
999-1211 |
1.23e-31 |
|
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: 123.41 E-value: 1.23e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 999 NVDFAYPTRPdvvIFENFSIEIDEGKSTAIVGTSGSGKST----IIGLIErfydPLKGTVKIDGRdirsyHLRSLRKYIS 1074
Cdd:cd03235 4 DLTVSYGGHP---VLEDVSFEVKPGEFLAIVGPNGAGKSTllkaILGLLK----PTSGSIRVFGK-----PLEKERKRIG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1075 LVSQEPML---FAGTIRENIMYGGTS--------DKIDESEIIEAAKAANAHDFItslsngyDTNCGdkgvQLSGGQKQR 1143
Cdd:cd03235 72 YVPQRRSIdrdFPISVRDVVLMGLYGhkglfrrlSKADKAKVDEALERVGLSELA-------DRQIG----ELSGGQQQR 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1144 IAIARAVLKNPSVLLLDEATSALDSKSERVVQDALERV-MVGRTSIMIAHRLSTIQN-CDMIVVLGKGKI 1211
Cdd:cd03235 141 VLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELrREGMTILVVTHDLGLVLEyFDRVLLLNRTVV 210
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
999-1211 |
1.26e-31 |
|
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: 122.12 E-value: 1.26e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 999 NVDFAYPTRPdvvIFENFSIEIDEGKSTAIVGTSGSGKSTIIGLIERFYDPLKGTVKIDGRDIRSyHLRSLRKYISLVSQ 1078
Cdd:cd03230 5 NLSKRYGKKT---ALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK-EPEEVKRRIGYLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1079 EPMLFAG-TIRENIMYggtsdkideseiieaakaanahdfitslsngydtncgdkgvqlSGGQKQRIAIARAVLKNPSVL 1157
Cdd:cd03230 81 EPSLYENlTVRENLKL-------------------------------------------SGGMKQRLALAQALLHDPELL 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 15232977 1158 LLDEATSALDSKSERVVQDAL-ERVMVGRTSIMIAHRLSTIQN-CDMIVVLGKGKI 1211
Cdd:cd03230 118 ILDEPTSGLDPESRREFWELLrELKKEGKTILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
995-1238 |
2.64e-31 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 123.66 E-value: 2.64e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 995 ITFLNVDFAYPTRPdvvIFENFSIEIDEGKSTAIVGTSGSGKST----IIGLIErfydPLKGTVKIDGRDIRSyhlrsLR 1070
Cdd:COG1121 7 IELENLTVSYGGRP---VLEDVSLTIPPGEFVAIVGPNGAGKSTllkaILGLLP----PTSGTVRLFGKPPRR-----AR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1071 KYISLVSQEPML---FAGTIRENIMYG--------GTSDKIDESEIIEAAKAANAHDFItslsngydtncgDKGV-QLSG 1138
Cdd:COG1121 75 RRIGYVPQRAEVdwdFPITVRDVVLMGrygrrglfRRPSRADREAVDEALERVGLEDLA------------DRPIgELSG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1139 GQKQRIAIARAVLKNPSVLLLDEATSALDSKSERVVQDALER-VMVGRTSIMIAHRLSTI-QNCDMIVVLGKGKIVEsgt 1216
Cdd:COG1121 143 GQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRElRREGKTILVVTHDLGAVrEYFDRVLLLNRGLVAH--- 219
|
250 260
....*....|....*....|..
gi 15232977 1217 hssllekGPTGTYFSLAGIQRT 1238
Cdd:COG1121 220 -------GPPEEVLTPENLSRA 234
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
999-1215 |
3.09e-31 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 123.61 E-value: 3.09e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 999 NVDFAYPTRPdvvIFENFSIEIDEGKSTAIVGTSGSGKSTIIGLIERFYD--P---LKGTVKIDGRDI--RSYHLRSLRK 1071
Cdd:COG1117 16 NLNVYYGDKQ---ALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDliPgarVEGEILLDGEDIydPDVDVVELRR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1072 YISLVSQEPMLFAGTIRENIMYG----GTSDKIDESEIIEAA--KAA---NAHDfitslsngydtNCGDKGVQLSGGQKQ 1142
Cdd:COG1117 93 RVGMVFQKPNPFPKSIYDNVAYGlrlhGIKSKSELDEIVEESlrKAAlwdEVKD-----------RLKKSALGLSGGQQQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1143 RIAIARAVLKNPSVLLLDEATSALDSKSERVVQDALERvMVGRTSIMI-------AHRLStiqncDMIVVLGKGKIVESG 1215
Cdd:COG1117 162 RLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILE-LKKDYTIVIvthnmqqAARVS-----DYTAFFYLGELVEFG 235
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
48-290 |
3.64e-31 |
|
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, member 10) and similar proteins; This group includes the 6-TM subunit of the ABC10 (also known as ABC mitochondrial erythroid, ABC-me, mABC2, or ABCBA), which is one of the three ATP-binding cassette (ABC) transporters found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. In mammals, ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane.
Pssm-ID: 350017 [Multi-domain] Cd Length: 294 Bit Score: 124.55 E-value: 3.64e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 48 ITPVVVFIFNTLLNNLGTSSSNNKTFMQTISKNVVALLYVACGSWVICFLEGYCWTRTGERQAARMREKYLRAVLRQDVG 127
Cdd:cd18573 11 VTMSVPFAIGKLIDVASKESGDIEIFGLSLKTFALALLGVFVVGAAANFGRVYLLRIAGERIVARLRKRLFKSILRQDAA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 128 YFDlhVTSTSDVITSISSDSLVIQDFLSEKLPNFLMNASAFVASYIVSFILMWRLTIVGFPFIILLLVPGLMYGRALVSI 207
Cdd:cd18573 91 FFD--KNKTGELVSRLSSDTSVVGKSLTQNLSDGLRSLVSGVGGIGMMLYISPKLTLVMLLVVPPIAVGAVFYGRYVRKL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 208 SRKIHEQYNEAGSIAEQAISSVRTVYAFGSENKMIGKFSTALRGSVKLGLRQGLAKGITIGSNGVT--HAIWAFLtWYGS 285
Cdd:cd18573 169 SKQVQDALADATKVAEERLSNIRTVRAFAAERKEVERYAKKVDEVFDLAKKEALASGLFFGSTGFSgnLSLLSVL-YYGG 247
|
....*
gi 15232977 286 RLVMN 290
Cdd:cd18573 248 SLVAS 252
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
355-585 |
4.91e-31 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 125.64 E-value: 4.91e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 355 MKGEVEfnHVKFTYlsrPETTIFDDLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYDPIAGEILIDG--VSIDkLQVnw 432
Cdd:COG1118 1 MSIEVR--NISKRF---GSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGrdLFTN-LPP-- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 433 LRSQMGLVSQEPVLFA-TSITENILFGKEDASLDEvveAAKASNAHTFISQFPLgykTQVGERGV-QMSGGQKQRIAIAR 510
Cdd:COG1118 73 RERRVGFVFQHYALFPhMTVAENIAFGLRVRPPSK---AEIRARVEELLELVQL---EGLADRYPsQLSGGQRQRVALAR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 511 AIIKSPKILLLDEATSALDS----ESERVVQESLDNasIGRTTIVIAH-RLSTIRNADVICVIHNGQIVETGSHEELLKR 585
Cdd:COG1118 147 ALAVEPEVLLLDEPFGALDAkvrkELRRWLRRLHDE--LGGTTVFVTHdQEEALELADRVVVMNQGRIEQVGTPDEVYDR 224
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
1004-1216 |
7.84e-31 |
|
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: 121.46 E-value: 7.84e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1004 YPTRPDVVIfENFSIEIDEGKSTAIVGTSGSGKSTIIGLIERFYDPLKGTVKIDGRDIRsYHLRSLRKYISLVSQEPMLF 1083
Cdd:cd03263 10 YKKGTKPAV-DDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIR-TDRKAARQSLGYCPQFDALF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1084 AG-TIRENIMY----GGTSDKIDESEIIEAAKAANAHDFITSLSNgydtncgdkgvQLSGGQKQRIAIARAVLKNPSVLL 1158
Cdd:cd03263 88 DElTVREHLRFyarlKGLPKSEIKEEVELLLRVLGLTDKANKRAR-----------TLSGGMKRKLSLAIALIGGPSVLL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15232977 1159 LDEATSALDSKSERVVQDALERVMVGRTSIMIAHRLSTIQN-CDMIVVLGKGKIVESGT 1216
Cdd:cd03263 157 LDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAEAlCDRIAIMSDGKLRCIGS 215
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
81-290 |
9.13e-31 |
|
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 and similar proteins; This group includes Arabidopsis ABC transporter B family member 27 (also known as AtABCB27, aluminum tolerance-related ATP-binding cassette transporter, transporter associated with antigen processing-like protein 2, AtTAP2, and ALS1) which may play a role in aluminum resistance. The ABC_6TM_TAP_ABCB8_10_like subgroup of the ABC_6TM exporter family includes ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection, as well as ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. The ABC_6TM exporter family represents the six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in the ABC_6TM exporter family.
Pssm-ID: 350053 [Multi-domain] Cd Length: 295 Bit Score: 123.51 E-value: 9.13e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 81 VVALLYVACGSWVICFLEGYCWTRTGERQAARMREKYLRAVLRQDVGYFDlhVTSTSDVITSISSDSLVIQDFLSEKLPN 160
Cdd:cd18780 45 VLILLGVVLIGSIATFLRSWLFTLAGERVVARLRKRLFSAIIAQEIAFFD--VTRTGELLNRLSSDTQVLQNAVTVNLSM 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 161 FLMNASAFVASYIVSFILMWRLTIVGFPFIILLLVPGLMYGRALVSISRKIHEQYNEAGSIAEQAISSVRTVYAFGSENK 240
Cdd:cd18780 123 LLRYLVQIIGGLVFMFTTSWKLTLVMLSVVPPLSIGAVIYGKYVRKLSKKFQDALAAASTVAEESISNIRTVRSFAKETK 202
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15232977 241 MIGKFSTALRGSVKLGLRQGLAKGITIGSNGV--THAIwAFLTWYGSRLVMN 290
Cdd:cd18780 203 EVSRYSEKINESYLLGKKLARASGGFNGFMGAaaQLAI-VLVLWYGGRLVID 253
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
1009-1223 |
9.96e-31 |
|
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: 121.58 E-value: 9.96e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1009 DVVIFENFSIEIDEGKSTAIVGTSGSGKSTIIGLIERFYDPLKGTVKIDGRDIrsYHLRSLRKYISLVSQEPMLFAG-TI 1087
Cdd:cd03300 12 GFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDI--TNLPPHKRPVNTVFQNYALFPHlTV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1088 RENIMYGGTSDKIDESEIieAAKAANAHDFITSLSNGYDtncgdKGVQLSGGQKQRIAIARAVLKNPSVLLLDEATSALD 1167
Cdd:cd03300 90 FENIAFGLRLKKLPKAEI--KERVAEALDLVQLEGYANR-----KPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALD 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15232977 1168 SKSERVVQDALERV--MVGRTSIMIAHRLS-TIQNCDMIVVLGKGKIVESGTHSSLLEK 1223
Cdd:cd03300 163 LKLRKDMQLELKRLqkELGITFVFVTHDQEeALTMSDRIAVMNKGKIQQIGTPEEIYEE 221
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
995-1223 |
1.60e-30 |
|
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: 121.14 E-value: 1.60e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 995 ITFLNVDFAYPTrpDVVIFENFSIEIDEGKSTAIVGTSGSGKSTIIGLIERFYDPLKGTVKIDGRDIRSY---HLRSLRK 1071
Cdd:cd03256 1 IEVENLSKTYPN--GKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLkgkALRQLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1072 YISLVSQEPMLFAG-TIRENIMYG---------GTSDKIDESEIIEAAKAANAHDFITSLSNGYDtncgdkgvQLSGGQK 1141
Cdd:cd03256 79 QIGMIFQQFNLIERlSVLENVLSGrlgrrstwrSLFGLFPKEEKQRALAALERVGLLDKAYQRAD--------QLSGGQQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1142 QRIAIARAVLKNPSVLLLDEATSALDSKSERVVQDALERV--MVGRTSIMIAHRLSTI-QNCDMIVVLGKGKIVESGTHS 1218
Cdd:cd03256 151 QRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRInrEEGITVIVSLHQVDLArEYADRIVGLKDGRIVFDGPPA 230
|
....*
gi 15232977 1219 SLLEK 1223
Cdd:cd03256 231 ELTDE 235
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
677-945 |
1.99e-30 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This group includes ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection, as well as ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins.
Pssm-ID: 350001 [Multi-domain] Cd Length: 289 Bit Score: 122.28 E-value: 1.99e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 677 LSAALVGVLQPvsaYSAGSVISVFFLTSH-DQIKEKTRIYVLLFVGLAIFSFLvnisQHYGFAYMGEYLTKRIREQMLSK 755
Cdd:cd18557 6 LISSAAQLLLP---YLIGRLIDTIIKGGDlDVLNELALILLAIYLLQSVFTFV----RYYLFNIAGERIVARLRRDLFSS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 756 ILTFEVNWFDidDNSSGAICSRLAKDANVVRSMVGDRMSLLVQTISAVIIACIIGLVIAWRLAIVMISVQPLIVVCFYTQ 835
Cdd:cd18557 79 LLRQEIAFFD--KHKTGELTSRLSSDTSVLQSAVTDNLSQLLRNILQVIGGLIILFILSWKLTLVLLLVIPLLLIASKIY 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 836 RVLLKSLSEKASKAQDESSKLAAEAVSNIRTITAFSSQERIIKLLKKVQEGPRRESVHRSWLAGIVLGTSRSLITCTSAL 915
Cdd:cd18557 157 GRYIRKLSKEVQDALAKAGQVAEESLSNIRTVRSFSAEEKEIRRYSEALDRSYRLARKKALANALFQGITSLLIYLSLLL 236
|
250 260 270
....*....|....*....|....*....|..
gi 15232977 916 NFWYGGRLIADGKIVSKAF--FEIFLIFVTTG 945
Cdd:cd18557 237 VLWYGGYLVLSGQLTVGELtsFILYTIMVASS 268
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
378-585 |
3.03e-30 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 122.92 E-value: 3.03e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 378 DDLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYDPIAGEILIDGVSIDKL---QVNWLRSQMGLVSQEPVlfatsiten 454
Cdd:COG4608 35 DGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLsgrELRPLRRRMQMVFQDPY--------- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 455 ilfgkedASLD------EVVEAAKAsnAHTfisqfpLGYKTQVGERGVQM------------------SGGQKQRIAIAR 510
Cdd:COG4608 106 -------ASLNprmtvgDIIAEPLR--IHG------LASKAERRERVAELlelvglrpehadryphefSGGQRQRIGIAR 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 511 AIIKSPKILLLDEATSALD-SESERVV------QESLdnasiGRTTIVIAHRLSTIRN-ADVICVIHNGQIVETGSHEEL 582
Cdd:COG4608 171 ALALNPKLIVCDEPVSALDvSIQAQVLnlledlQDEL-----GLTYLFISHDLSVVRHiSDRVAVMYLGKIVEIAPRDEL 245
|
...
gi 15232977 583 LKR 585
Cdd:COG4608 246 YAR 248
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
359-583 |
3.43e-30 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 120.20 E-value: 3.43e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 359 VEFNHVKFTYlsrPETTIFDDLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYDPIAGEILIDGVSI--DKLQVNWLRSQ 436
Cdd:PRK09493 2 IEFKNVSKHF---GPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVndPKVDERLIRQE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 437 MGLVSQEPVLFA--TSItENILFG--------KEDA---SLDEVVEAAKASNAHTFISQfplgyktqvgergvqMSGGQK 503
Cdd:PRK09493 79 AGMVFQQFYLFPhlTAL-ENVMFGplrvrgasKEEAekqARELLAKVGLAERAHHYPSE---------------LSGGQQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 504 QRIAIARAIIKSPKILLLDEATSALDSE-SERVVQESLDNASIGRTTIVIAHRLSTIRN-ADVICVIHNGQIVETGSHEE 581
Cdd:PRK09493 143 QRVAIARALAVKPKLMLFDEPTSALDPElRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKvASRLIFIDKGRIAEDGDPQV 222
|
..
gi 15232977 582 LL 583
Cdd:PRK09493 223 LI 224
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
998-1216 |
5.12e-30 |
|
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: 122.08 E-value: 5.12e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 998 LNVDFayPTRPDVV-IFENFSIEIDEGKSTAIVGTSGSGKST----IIGLIERFYDpLKGTVKIDGRDIRSYHLRSLRKY 1072
Cdd:COG0444 7 LKVYF--PTRRGVVkAVDGVSFDVRRGETLGLVGESGSGKSTlaraILGLLPPPGI-TSGEILFDGEDLLKLSEKELRKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1073 ----ISLVSQEPM-----LFagTIRENIM-----YGGTSDKIDESEIIE---------AAKAANA--Hdfitslsngydt 1127
Cdd:COG0444 84 rgreIQMIFQDPMtslnpVM--TVGDQIAeplriHGGLSKAEARERAIEllervglpdPERRLDRypH------------ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1128 ncgdkgvQLSGGQKQRIAIARAVLKNPSVLLLDEATSALDskserV-VQDALERVMV------GRTSIMIAHRLSTI-QN 1199
Cdd:COG0444 150 -------ELSGGMRQRVMIARALALEPKLLIADEPTTALD-----VtIQAQILNLLKdlqrelGLAILFITHDLGVVaEI 217
|
250
....*....|....*..
gi 15232977 1200 CDMIVVLGKGKIVESGT 1216
Cdd:COG0444 218 ADRVAVMYAGRIVEEGP 234
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
355-585 |
5.14e-30 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 120.89 E-value: 5.14e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 355 MKGEVEFNHVKFTYlsrPETT--IFDDLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYDPIAGEILIDGVSIDKLQVNW 432
Cdd:PRK13635 2 KEEIIRVEHISFRY---PDAAtyALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 433 LRSQMGLVSQEP--VLFATSITENILFGKEDASL--DEVVE----AAKASNAHTFISQFPlgyktqvgergVQMSGGQKQ 504
Cdd:PRK13635 79 VRRQVGMVFQNPdnQFVGATVQDDVAFGLENIGVprEEMVErvdqALRQVGMEDFLNREP-----------HRLSGGQKQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 505 RIAIARAIIKSPKILLLDEATSALDSESERVVQESLD--NASIGRTTIVIAHRLSTIRNADVICVIHNGQIVETGSHEEL 582
Cdd:PRK13635 148 RVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRqlKEQKGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEI 227
|
...
gi 15232977 583 LKR 585
Cdd:PRK13635 228 FKS 230
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
995-1221 |
8.68e-30 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 118.70 E-value: 8.68e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 995 ITFLNVDFAYPTRPdvvifENFSIEIDEGKSTAIVGTSGSGKSTIIGLIERFYDPLKGTVKIDGRDIRSYHLrSLRKyIS 1074
Cdd:COG3840 2 LRLDDLTYRYGDFP-----LRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPP-AERP-VS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1075 LVSQEPMLFAG-TIRENIMYGGTSD-KIDESE---IIEAAKAANAHDFITSLsngydtnCGdkgvQLSGGQKQRIAIARA 1149
Cdd:COG3840 75 MLFQENNLFPHlTVAQNIGLGLRPGlKLTAEQraqVEQALERVGLAGLLDRL-------PG----QLSGGQRQRVALARC 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15232977 1150 VLKNPSVLLLDEATSALDS--KSE--RVVQD-ALERvmvGRTSIMIAHRLSTIQN-CDMIVVLGKGKIVESGTHSSLL 1221
Cdd:COG3840 144 LVRKRPILLLDEPFSALDPalRQEmlDLVDElCRER---GLTVLMVTHDPEDAARiADRVLLVADGRIAADGPTAALL 218
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1008-1216 |
1.65e-29 |
|
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: 118.21 E-value: 1.65e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1008 PDVVIFENFSIEIDEGKSTAIVGTSGSGKSTIIGLIERFYDPLKGTVKIDGRDIRSYHLRslRKYISLVSQEPMLFAG-T 1086
Cdd:cd03296 13 GDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQ--ERNVGFVFQHYALFRHmT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1087 IRENIMYG----GTSDKIDESEIieAAKAANAHDFI--TSLSNGYDTncgdkgvQLSGGQKQRIAIARAVLKNPSVLLLD 1160
Cdd:cd03296 91 VFDNVAFGlrvkPRSERPPEAEI--RAKVHELLKLVqlDWLADRYPA-------QLSGGQRQRVALARALAVEPKVLLLD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15232977 1161 EATSALDSKSERVVQDALERVM--VGRTSIMIAHRLS-TIQNCDMIVVLGKGKIVESGT 1216
Cdd:cd03296 162 EPFGALDAKVRKELRRWLRRLHdeLHVTTVFVTHDQEeALEVADRVVVMNKGRIEQVGT 220
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
360-577 |
1.66e-29 |
|
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: 116.00 E-value: 1.66e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 360 EFNHVKFTYlsrPETTIFDDLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYDPIAGEILIDGVSIDKLQVNWLRSQMGL 439
Cdd:cd03214 1 EVENLSVGY---GGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 440 VSQepVLFATSITEnilfgKEDASLDEvveaakasnahtfisqfplgyktqvgergvqMSGGQKQRIAIARAIIKSPKIL 519
Cdd:cd03214 78 VPQ--ALELLGLAH-----LADRPFNE-------------------------------LSGGERQRVLLARALAQEPPIL 119
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15232977 520 LLDEATSALDSESERVVQESLD--NASIGRTTIVIAHRLS-TIRNADVICVIHNGQIVETG 577
Cdd:cd03214 120 LLDEPTSHLDIAHQIELLELLRrlARERGKTVVMVLHDLNlAARYADRVILLKDGRIVAQG 180
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
377-585 |
1.67e-29 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 117.93 E-value: 1.67e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 377 FDdlcLKIPAGKTVALVGGSGSGKSTVISLLQRFYDPIAGEILIDGVSIDKLQVnwlrSQ--MGLVSQEPVLFA-TSITE 453
Cdd:COG3840 18 FD---LTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPP----AErpVSMLFQENNLFPhLTVAQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 454 NILFG-KEDASLDE-----VVEAAKASNAHTFISQFPlgyktqvgergVQMSGGQKQRIAIARAIIKSPKILLLDEATSA 527
Cdd:COG3840 91 NIGLGlRPGLKLTAeqraqVEQALERVGLAGLLDRLP-----------GQLSGGQRQRVALARCLVRKRPILLLDEPFSA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15232977 528 LDSeSERvvQESLD-----NASIGRTTIVIAHRLS-TIRNADVICVIHNGQIVETGSHEELLKR 585
Cdd:COG3840 160 LDP-ALR--QEMLDlvdelCRERGLTVLMVTHDPEdAARIADRVLLVADGRIAADGPTAALLDG 220
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
359-578 |
2.47e-29 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 120.68 E-value: 2.47e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 359 VEFNHVKFTY-LSRPETTIFDDLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYDPIAGEILIDGVSIDKLQVNWLRS-- 435
Cdd:PRK11153 2 IELKNISKVFpQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 436 -QMGLVSQEPVLFAtSIT--ENILF-----GKEDASLDEVVE--------AAKAsnahtfiSQFPlgyktqvgergVQMS 499
Cdd:PRK11153 82 rQIGMIFQHFNLLS-SRTvfDNVALplelaGTPKAEIKARVTellelvglSDKA-------DRYP-----------AQLS 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 500 GGQKQRIAIARAIIKSPKILLLDEATSALDSESERVVQESLdnASIGRT---TIV-IAHRLSTIRN-ADVICVIHNGQIV 574
Cdd:PRK11153 143 GGQKQRVAIARALASNPKVLLCDEATSALDPATTRSILELL--KDINRElglTIVlITHEMDVVKRiCDRVAVIDAGRLV 220
|
....
gi 15232977 575 ETGS 578
Cdd:PRK11153 221 EQGT 224
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
999-1224 |
2.48e-29 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 118.96 E-value: 2.48e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 999 NVDFAYP--TRPDVvifENFSIEIDEGKSTAIVGTSGSGKSTIIGLIERFYDPLKGTVKIDGRDIRSYHLRSLRKYISLV 1076
Cdd:PRK13635 10 HISFRYPdaATYAL---KDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVGMV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1077 SQEP-MLFAG-TIRENIMYGGTSDKIDESEIIEAAKAA----NAHDFITslsngydtncgDKGVQLSGGQKQRIAIARAV 1150
Cdd:PRK13635 87 FQNPdNQFVGaTVQDDVAFGLENIGVPREEMVERVDQAlrqvGMEDFLN-----------REPHRLSGGQKQRVAIAGVL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15232977 1151 LKNPSVLLLDEATSALDSKSERVVQDALeRVMV---GRTSIMIAHRLSTIQNCDMIVVLGKGKIVESGTHSSLLEKG 1224
Cdd:PRK13635 156 ALQPDIIILDEATSMLDPRGRREVLETV-RQLKeqkGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEIFKSG 231
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
1012-1211 |
2.77e-29 |
|
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: 116.48 E-value: 2.77e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1012 IFENFSIEIDEGKSTAIVGTSGSGKSTIIGLIERFYDPLKGTVKIDGRDI--RSYHLRSLRKYISLVSQEPMLFAG-TIR 1088
Cdd:cd03262 15 VLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLtdDKKNINELRQKVGMVFQQFNLFPHlTVL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1089 ENIMYGGTS-DKIDESEIIEAAKAANAHDFITSLSNGYDtncgdkgVQLSGGQKQRIAIARAVLKNPSVLLLDEATSALD 1167
Cdd:cd03262 95 ENITLAPIKvKGMSKAEAEERALELLEKVGLADKADAYP-------AQLSGGQQQRVAIARALAMNPKVMLFDEPTSALD 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15232977 1168 SKserVVQDALErVMV-----GRTSIMIAHRLSTIQN-CDMIVVLGKGKI 1211
Cdd:cd03262 168 PE---LVGEVLD-VMKdlaeeGMTMVVVTHEMGFAREvADRVIFMDDGRI 213
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
359-579 |
2.85e-29 |
|
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: 116.74 E-value: 2.85e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 359 VEFNHVKFTYlsRPETTIFDDLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYDPIAGEILIDGVSIDKL---QVNWLRS 435
Cdd:cd03292 1 IEFINVTKTY--PNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLrgrAIPYLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 436 QMGLVSQEPVLFAT-SITENILFGKE--DASLDEVVEAAKASNAHtfisqfpLGYKTQVGERGVQMSGGQKQRIAIARAI 512
Cdd:cd03292 79 KIGVVFQDFRLLPDrNVYENVAFALEvtGVPPREIRKRVPAALEL-------VGLSHKHRALPAELSGGEQQRVAIARAI 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15232977 513 IKSPKILLLDEATSALDSESERVVQESLDNASIGRTTIVIAhrlstirnadvicvIHNGQIVETGSH 579
Cdd:cd03292 152 VNSPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVA--------------THAKELVDTTRH 204
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
355-583 |
3.06e-29 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 117.50 E-value: 3.06e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 355 MKGE--VEFNHVKFTYLSRPettIFDDLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYDPIAGEILIDGVSIDKLqvnw 432
Cdd:COG1121 1 MMMMpaIELENLTVSYGGRP---VLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRA---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 433 lRSQMGLVSQEPVL---FATSITENIL------------FGKEDAslDEVVEAAKASNAHTFISQfplgyktQVGErgvq 497
Cdd:COG1121 74 -RRRIGYVPQRAEVdwdFPITVRDVVLmgrygrrglfrrPSRADR--EAVDEALERVGLEDLADR-------PIGE---- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 498 MSGGQKQRIAIARAIIKSPKILLLDEATSALDSESERVVQESLDN-ASIGRTTIVIAHRLSTIR-NAD-VICVihNGQIV 574
Cdd:COG1121 140 LSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRElRREGKTILVVTHDLGAVReYFDrVLLL--NRGLV 217
|
....*....
gi 15232977 575 ETGSHEELL 583
Cdd:COG1121 218 AHGPPEEVL 226
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
998-1215 |
4.19e-29 |
|
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: 116.24 E-value: 4.19e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 998 LNVDFAYPtrpdvviFENFSIEID---EGKSTAIVGTSGSGKSTIIGLIERFYDPLKGTVKIDGR---DIR-SYHLRSLR 1070
Cdd:cd03297 2 LCVDIEKR-------LPDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTvlfDSRkKINLPPQQ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1071 KYISLVSQEPMLFAG-TIRENIMYG-----GTSDKIDESEIIEAAKaanahdfITSLSNGYDTncgdkgvQLSGGQKQRI 1144
Cdd:cd03297 75 RKIGLVFQQYALFPHlNVRENLAFGlkrkrNREDRISVDELLDLLG-------LDHLLNRYPA-------QLSGGEKQRV 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15232977 1145 AIARAVLKNPSVLLLDEATSALDSKSERVVQDALERVM--VGRTSIMIAHRLSTIQN-CDMIVVLGKGKIVESG 1215
Cdd:cd03297 141 ALARALAAQPELLLLDEPFSALDRALRLQLLPELKQIKknLNIPVIFVTHDLSEAEYlADRIVVMEDGRLQYIG 214
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
995-1216 |
5.01e-29 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 119.52 E-value: 5.01e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 995 ITFLNVDFAYPT-RPDVVIFENFSIEIDEGKSTAIVGTSGSGKSTIIGLIERFYDPLKGTVKIDGRDIRSY---HLRSLR 1070
Cdd:PRK11153 2 IELKNISKVFPQgGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALsekELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1071 KYISLVSQEPMLFAG-TIRENI-----MYGGTSDKIDE--SEIIEAAKAANAHDFITSlsngydtncgdkgvQLSGGQKQ 1142
Cdd:PRK11153 82 RQIGMIFQHFNLLSSrTVFDNValpleLAGTPKAEIKArvTELLELVGLSDKADRYPA--------------QLSGGQKQ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15232977 1143 RIAIARAVLKNPSVLLLDEATSALDSKSERVVQDALERV--MVGRTSIMIAHRLSTI-QNCDMIVVLGKGKIVESGT 1216
Cdd:PRK11153 148 RVAIARALASNPKVLLCDEATSALDPATTRSILELLKDInrELGLTIVLITHEMDVVkRICDRVAVIDAGRLVEQGT 224
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
378-585 |
6.36e-29 |
|
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: 122.87 E-value: 6.36e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 378 DDLCLKIPAGKTVALVGGSGSGKSTV-ISLLQrfYDPIAGEILIDGVSIDKL---QVNWLRSQMGLVSQEPvlFAT---- 449
Cdd:COG4172 303 DGVSLTLRRGETLGLVGESGSGKSTLgLALLR--LIPSEGEIRFDGQDLDGLsrrALRPLRRRMQVVFQDP--FGSlspr 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 450 -----SITENILF---GKEDASLDEVVEAA------KASNAHTFISQFplgyktqvgergvqmSGGQKQRIAIARAIIKS 515
Cdd:COG4172 379 mtvgqIIAEGLRVhgpGLSAAERRARVAEAleevglDPAARHRYPHEF---------------SGGQRQRIAIARALILE 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 516 PKILLLDEATSALDseseRVVQesldnASI-----------GRTTIVIAHRLSTIRN-ADVICVIHNGQIVETGSHEELL 583
Cdd:COG4172 444 PKLLVLDEPTSALD----VSVQ-----AQIldllrdlqrehGLAYLFISHDLAVVRAlAHRVMVMKDGKVVEQGPTEQVF 514
|
..
gi 15232977 584 KR 585
Cdd:COG4172 515 DA 516
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
35-332 |
8.44e-29 |
|
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family represents a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in this family. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting chemical diversity of the translocated substrates, whereas NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional unit. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349983 [Multi-domain] Cd Length: 292 Bit Score: 117.65 E-value: 8.44e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 35 MALGLIGAVGDGFITPVVVFIFNTLLNNLGTSSSnnktfMQTISKNVVALLYVACGSWVICFLEGYCWTRTGERQAARMR 114
Cdd:cd07346 1 LLLALLLLLLATALGLALPLLTKLLIDDVIPAGD-----LSLLLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 115 EKYLRAVLRQDVGYFDlhVTSTSDVITSISSDSLVIQDFLSEKLPNFLMNASAFVASYIVSFILMWRLTIVGFPFIILLL 194
Cdd:cd07346 76 RDLFRHLQRLSLSFFD--RNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 195 VPGLMYGRALVSISRKIHEQYNEAGSIAEQAISSVRTVYAFGSENKMIGKFSTALRGSVKLGLRQGLAKGITIGSNG-VT 273
Cdd:cd07346 154 LILRYFRRRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGlLT 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15232977 274 HAIWAFLTWYGSRLVMNHGSKGGTVFVVISCIT--YGGVslgQSLSNLkY--FSEAFVAWERI 332
Cdd:cd07346 234 ALGTALVLLYGGYLVLQGSLTIGELVAFLAYLGmlFGPI---QRLANL-YnqLQQALASLERI 292
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1012-1216 |
9.67e-29 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 119.67 E-value: 9.67e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1012 IFENFSIEIDEGKSTAIVGTSGSGKSTIIGLIERFYDPLKGTVKIDGRDIRsyHLRSLRKYISLVSQEPMLFAG-TIREN 1090
Cdd:PRK09452 29 VISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDIT--HVPAENRHVNTVFQSYALFPHmTVFEN 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1091 IMYGGTSDKIDESEI----IEAAKAANAHDFITSlsngydtncgdKGVQLSGGQKQRIAIARAVLKNPSVLLLDEATSAL 1166
Cdd:PRK09452 107 VAFGLRMQKTPAAEItprvMEALRMVQLEEFAQR-----------KPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSAL 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15232977 1167 DSKSERVVQDALERVM--VGRTSIMIAH-RLSTIQNCDMIVVLGKGKIVESGT 1216
Cdd:PRK09452 176 DYKLRKQMQNELKALQrkLGITFVFVTHdQEEALTMSDRIVVMRDGRIEQDGT 228
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
1014-1223 |
1.09e-28 |
|
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: 115.51 E-value: 1.09e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1014 ENFSIEIDEGKSTAIVGTSGSGKSTIIGLIERFYDPLKGTVKIDGRDIRSyhLRSLRKYISLVSQEPMLFAG-TIRENIM 1092
Cdd:cd03299 16 KNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITN--LPPEKRDISYVPQNYALFPHmTVYKNIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1093 YGGTSDKIDESEI----IEAAKAANahdfITSLSNgydtncgDKGVQLSGGQKQRIAIARAVLKNPSVLLLDEATSALDS 1168
Cdd:cd03299 94 YGLKKRKVDKKEIerkvLEIAEMLG----IDHLLN-------RKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDV 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15232977 1169 KSERVVQDALERVM--VGRTSIMIAHRLSTIQN-CDMIVVLGKGKIVESGTHSSLLEK 1223
Cdd:cd03299 163 RTKEKLREELKKIRkeFGVTVLHVTHDFEEAWAlADKVAIMLNGKLIQVGKPEEVFKK 220
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
995-1215 |
1.14e-28 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 115.15 E-value: 1.14e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 995 ITFLNVDFAYPtrPDVVIFENFSIEIDEGKSTAIVGTSGSGKSTIIGLIERFYDPLKGTVKIDGRD---IRSYHLRSLRK 1071
Cdd:COG2884 2 IRFENVSKRYP--GGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDlsrLKRREIPYLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1072 YISLVSQEPMLFAG-TIRENIMYG----GTSDKIDESEIIEAAK----AANAHDFItslsngydtncgdkgVQLSGGQKQ 1142
Cdd:COG2884 80 RIGVVFQDFRLLPDrTVYENVALPlrvtGKSRKEIRRRVREVLDlvglSDKAKALP---------------HELSGGEQQ 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15232977 1143 RIAIARAVLKNPSVLLLDEATSALDSK-SERVVqDALERV-MVGRTSIMIAHRLSTIQNCDM-IVVLGKGKIVESG 1215
Cdd:COG2884 145 RVAIARALVNRPELLLADEPTGNLDPEtSWEIM-ELLEEInRRGTTVLIATHDLELVDRMPKrVLELEDGRLVRDE 219
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
355-587 |
1.57e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 116.37 E-value: 1.57e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 355 MKGEVEFNHVKFTYLSRPETTIFDDLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYDPIAGEILIDGVSIDKLQVNWLR 434
Cdd:PRK13650 1 MSNIIEVKNLTFKYKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 435 SQMGLVSQEP--VLFATSITENILFGKEDA--SLDEVVEAAKASNAHTFISQFplgyKTQVGERgvqMSGGQKQRIAIAR 510
Cdd:PRK13650 81 HKIGMVFQNPdnQFVGATVEDDVAFGLENKgiPHEEMKERVNEALELVGMQDF----KEREPAR---LSGGQKQRVAIAG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 511 AIIKSPKILLLDEATSALDSESE----RVVQESLDnaSIGRTTIVIAHRLSTIRNADVICVIHNGQIVETGSHEELLKRI 586
Cdd:PRK13650 154 AVAMRPKIIILDEATSMLDPEGRleliKTIKGIRD--DYQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPRELFSRG 231
|
.
gi 15232977 587 D 587
Cdd:PRK13650 232 N 232
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
995-1224 |
2.76e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 116.03 E-value: 2.76e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 995 ITFLNVDFAYP--TRPDVVIFENFSIEIDEGKSTAIVGTSGSGKSTIIGLIERFYDPLKGTVKIDGRDI----RSYHLRS 1068
Cdd:PRK13646 3 IRFDNVSYTYQkgTPYEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIthktKDKYIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1069 LRKYISLVSQ--EPMLFAGTIRENIMYGGTSDKIDeseiIEAAKAaNAHDFITSLsnGYDTNCGDKG-VQLSGGQKQRIA 1145
Cdd:PRK13646 83 VRKRIGMVFQfpESQLFEDTVEREIIFGPKNFKMN----LDEVKN-YAHRLLMDL--GFSRDVMSQSpFQMSGGQMRKIA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1146 IARAVLKNPSVLLLDEATSALDSKSERVVQDALERVMV--GRTSIMIAHRLSTI-QNCDMIVVLGKGKIVESGTHSSLLE 1222
Cdd:PRK13646 156 IVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTdeNKTIILVSHDMNEVaRYADEVIVMKEGSIVSQTSPKELFK 235
|
..
gi 15232977 1223 KG 1224
Cdd:PRK13646 236 DK 237
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
1011-1234 |
4.01e-28 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 123.74 E-value: 4.01e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1011 VIFENFSIEIDEGKSTAIVGTSGSGKSTIIGLIERFYDPLKGTVkidgrdirsYHLRSlrkyISLVSQEPMLFAGTIREN 1090
Cdd:PTZ00243 674 VLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV---------WAERS----IAYVPQQAWIMNATVRGN 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1091 IMYggtSDKIDESEIIEAAKAANAHDFITSLSNGYDTNCGDKGVQLSGGQKQRIAIARAVLKNPSVLLLDEATSALDSK- 1169
Cdd:PTZ00243 741 ILF---FDEEDAARLADAVRVSQLEADLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHv 817
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15232977 1170 SERVVQDALERVMVGRTSIMIAHRLSTIQNCDMIVVLGKGKIVESGTHSSLLEkgpTGTYFSLAG 1234
Cdd:PTZ00243 818 GERVVEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSGSSADFMR---TSLYATLAA 879
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
901-1206 |
1.19e-27 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 119.53 E-value: 1.19e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 901 VLGTSRSLITCTSALNFW---YGgrliadgkivskAFFEIFLIFVTTGRVIAdaGTMTT-DLARGLDAVGSVF------- 969
Cdd:COG4178 254 VIANWRRLIRRQRNLTFFttgYG------------QLAVIFPILVAAPRYFA--GEITLgGLMQAASAFGQVQgalswfv 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 970 ----------AVLDRCTT----IEPKNPDGYVAEKIK----GQITFLNVDFAyptRPDV-VIFENFSIEIDEGKSTAIVG 1030
Cdd:COG4178 320 dnyqslaewrATVDRLAGfeeaLEAADALPEAASRIEtsedGALALEDLTLR---TPDGrPLLEDLSLSLKPGERLLITG 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1031 TSGSGKSTII-----------GLIERfydPlkgtvkiDGRDIrsyhlrslrkyiSLVSQEPMLFAGTIRENIMYGGTSDK 1099
Cdd:COG4178 397 PSGSGKSTLLraiaglwpygsGRIAR---P-------AGARV------------LFLPQRPYLPLGTLREALLYPATAEA 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1100 IDESEIIEAAKAANAHDFITSLsngyDTNcGDKGVQLSGGQKQRIAIARAVLKNPSVLLLDEATSALDSKSERVVQDALE 1179
Cdd:COG4178 455 FSDAELREALEAVGLGHLAERL----DEE-ADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLR 529
|
330 340
....*....|....*....|....*..
gi 15232977 1180 RVMVGRTSIMIAHRLSTIQNCDMIVVL 1206
Cdd:COG4178 530 EELPGTTVISVGHRSTLAAFHDRVLEL 556
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
373-587 |
1.67e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 113.60 E-value: 1.67e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 373 ETTIFDDLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYDPIAGEILIDGVSIDKLQVNW--LRSQMGLVSQEP--VLFA 448
Cdd:PRK13637 19 EKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKLsdIRKKVGLVFQYPeyQLFE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 449 TSITENILFGKEDASL--DEVVEAAKASnahtfISQFPLGYKTQVGERGVQMSGGQKQRIAIARAIIKSPKILLLDEATS 526
Cdd:PRK13637 99 ETIEKDIAFGPINLGLseEEIENRVKRA-----MNIVGLDYEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTA 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15232977 527 ALDSESERVVQESLDN--ASIGRTTIVIAHRLSTI-RNADVICVIHNGQIVETGSHEELLKRID 587
Cdd:PRK13637 174 GLDPKGRDEILNKIKElhKEYNMTIILVSHSMEDVaKLADRIIVMNKGKCELQGTPREVFKEVE 237
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1014-1216 |
1.99e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 113.60 E-value: 1.99e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1014 ENFSIEIDEGKSTAIVGTSGSGKSTIIGLIERFYDPLKGTVKIDGRDI--RSYHLRSLRKYISLVSQEP--MLFAGTIRE 1089
Cdd:PRK13637 24 DNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDItdKKVKLSDIRKKVGLVFQYPeyQLFEETIEK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1090 NIMYGGTSDKIDESEIIEAAKAANAhdfITSLSngYDTNCGDKGVQLSGGQKQRIAIARAVLKNPSVLLLDEATSALDSK 1169
Cdd:PRK13637 104 DIAFGPINLGLSEEEIENRVKRAMN---IVGLD--YEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPK 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15232977 1170 SErvvQDALERVM-----VGRTSIMIAHRLSTIQN-CDMIVVLGKGKIVESGT 1216
Cdd:PRK13637 179 GR---DEILNKIKelhkeYNMTIILVSHSMEDVAKlADRIIVMNKGKCELQGT 228
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
995-1224 |
2.14e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 112.92 E-value: 2.14e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 995 ITFLNVDFAYPTRPDVVIfENFSIEIDEGKSTAIVGTSGSGKSTIIGLIERFYDPLKGTVKIDGRDIRSYHLRSLRKYIS 1074
Cdd:PRK13648 8 IVFKNVSFQYQSDASFTL-KDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1075 LVSQEP-MLFAGTI-RENIMYGGTSDKIDESEIIEAAKAAnahdfitsLSNGYDTNCGDKGVQ-LSGGQKQRIAIARAVL 1151
Cdd:PRK13648 87 IVFQNPdNQFVGSIvKYDVAFGLENHAVPYDEMHRRVSEA--------LKQVDMLERADYEPNaLSGGQKQRVAIAGVLA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15232977 1152 KNPSVLLLDEATSALDSKSERVVQDALERVMVGR--TSIMIAHRLSTIQNCDMIVVLGKGKIVESGTHSSLLEKG 1224
Cdd:PRK13648 159 LNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHniTIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEIFDHA 233
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
370-567 |
2.41e-27 |
|
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: 110.65 E-value: 2.41e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 370 SRPETTIFDDLCLKIPAGKTVALVGGSGSGKST---VISLLQRfydPIAGEILIDGVSIDKLQVNWlRSQMGLVSQEPVL 446
Cdd:COG4133 11 RRGERLLFSGLSFTLAAGEALALTGPNGSGKTTllrILAGLLP---PSAGEVLWNGEPIRDAREDY-RRRLAYLGHADGL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 447 FAT-SITENILF-------GKEDASLDEVVEAAK-ASNAHTFISQFplgyktqvgergvqmSGGQKQRIAIARAIIKSPK 517
Cdd:COG4133 87 KPElTVRENLRFwaalyglRADREAIDEALEAVGlAGLADLPVRQL---------------SAGQKRRVALARLLLSPAP 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 15232977 518 ILLLDEATSALDSESERVVQESLDNASIGRTTIVIA-HRLSTIRNADVICV 567
Cdd:COG4133 152 LWLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTtHQPLELAAARVLDL 202
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
358-574 |
3.19e-27 |
|
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: 109.95 E-value: 3.19e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 358 EVEFNHVKFT---YLSRPETTIFDDLCLKIPAGKTVALVGGSGSGKSTVISLL--QRFYDPIAGEILIDGVSIDKlqvNW 432
Cdd:cd03213 3 TLSFRNLTVTvksSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALagRRTGLGVSGEVLINGRPLDK---RS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 433 LRSQMGLVSQEPVLFAT-SITENILFgkedasldevveAAKAsnahtfisqfplgyktqvgeRGVqmSGGQKQRIAIARA 511
Cdd:cd03213 80 FRKIIGYVPQDDILHPTlTVRETLMF------------AAKL--------------------RGL--SGGERKRVSIALE 125
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15232977 512 IIKSPKILLLDEATSALDSESERVVQESLDN-ASIGRTTIVIAHRLST--IRNADVICVIHNGQIV 574
Cdd:cd03213 126 LVSNPSLLFLDEPTSGLDSSSALQVMSLLRRlADTGRTIICSIHQPSSeiFELFDKLLLLSQGRVI 191
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
999-1215 |
3.96e-27 |
|
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: 110.36 E-value: 3.96e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 999 NVDFAYPTRpdvVIFENFSIEIDEGkSTAIVGTSGSGKSTIIGLIERFYDPLKGTVKIDGRDIRSyHLRSLRKYISLVSQ 1078
Cdd:cd03264 5 NLTKRYGKK---RALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLK-QPQKLRRRIGYLPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1079 EPMLFAG-TIRENIMY----GGTSDKIDESEIIEAAKAANAHDFITslsngydtncgDKGVQLSGGQKQRIAIARAVLKN 1153
Cdd:cd03264 80 EFGVYPNfTVREFLDYiawlKGIPSKEVKARVDEVLELVNLGDRAK-----------KKIGSLSGGMRRRVGIAQALVGD 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15232977 1154 PSVLLLDEATSALDSKSERVVQDALERVMVGRTSIMIAHRLSTIQN-CDMIVVLGKGKIVESG 1215
Cdd:cd03264 149 PSILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESlCNQVAVLNKGKLVFEG 211
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
357-582 |
5.52e-27 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 114.01 E-value: 5.52e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 357 GEVEFNHVKFTYlsrPETTIFDDLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYDPIAGEILIDGVSidklqVNWLRSQ 436
Cdd:COG3839 2 ASLELENVSKSY---GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRD-----VTDLPPK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 437 ---MGLVSQEPVLF-ATSITENILFG----KED-ASLDE-VVEAAKAsnahtfisqfpLGYkTQVGERGV-QMSGGQKQR 505
Cdd:COG3839 74 drnIAMVFQSYALYpHMTVYENIAFPlklrKVPkAEIDRrVREAAEL-----------LGL-EDLLDRKPkQLSGGQRQR 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 506 IAIARAIIKSPKILLLDEATSALDSESeRV--------VQESLdnasiGRTTIVIAHRLS---TIrnADVICVIHNGQIV 574
Cdd:COG3839 142 VALGRALVREPKVFLLDEPLSNLDAKL-RVemraeikrLHRRL-----GTTTIYVTHDQVeamTL--ADRIAVMNDGRIQ 213
|
....*...
gi 15232977 575 ETGSHEEL 582
Cdd:COG3839 214 QVGTPEEL 221
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
373-583 |
6.66e-27 |
|
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: 110.22 E-value: 6.66e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 373 ETTIFDDLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYDPIAGEILIDGVSIDKLQVnWLRSQMGL--VSQEPVLFAT- 449
Cdd:cd03224 12 KSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPP-HERARAGIgyVPEGRRIFPEl 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 450 SITENILFG-------KEDASLDEVVEAakasnahtfisqFP-LgyKTQVGERGVQMSGGQKQRIAIARAIIKSPKILLL 521
Cdd:cd03224 91 TVEENLLLGayarrraKRKARLERVYEL------------FPrL--KERRKQLAGTLSGGEQQMLAIARALMSRPKLLLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15232977 522 DEATSALdseSERVVQESLD-----NASiGRTTIVIAHRLSTIRN-ADVICVIHNGQIVETGSHEELL 583
Cdd:cd03224 157 DEPSEGL---APKIVEEIFEairelRDE-GVTILLVEQNARFALEiADRAYVLERGRVVLEGTAAELL 220
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
995-1211 |
9.46e-27 |
|
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: 109.42 E-value: 9.46e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 995 ITFLNVDFAYPtrPDVVIFENFSIEIDEGKSTAIVGTSGSGKSTIIGLIERFYDPLKGTVKIDGRDIRSYHLRS---LRK 1071
Cdd:cd03292 1 IEFINVTKTYP--NGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAipyLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1072 YISLVSQE-PMLFAGTIRENIMYGGTSDKIDESEIIEAAKAANAHDFITSLSNGYDTncgdkgvQLSGGQKQRIAIARAV 1150
Cdd:cd03292 79 KIGVVFQDfRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPA-------ELSGGEQQRVAIARAI 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15232977 1151 LKNPSVLLLDEATSALDSKSERVVQDALERVMVGRTSIMIAHRLSTIQNcDM---IVVLGKGKI 1211
Cdd:cd03292 152 VNSPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVD-TTrhrVIALERGKL 214
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
359-588 |
1.19e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 110.61 E-value: 1.19e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 359 VEFNHVKFTYLSRPETTIfDDLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYDPIAGEILIDGVSIDKLQVNWLRSQMG 438
Cdd:PRK13648 8 IVFKNVSFQYQSDASFTL-KDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 439 LVSQEPV-LFATSITE-NILFGKEDASL--DEVVEAAKASnahtfISQfpLGYKTQVGERGVQMSGGQKQRIAIARAIIK 514
Cdd:PRK13648 87 IVFQNPDnQFVGSIVKyDVAFGLENHAVpyDEMHRRVSEA-----LKQ--VDMLERADYEPNALSGGQKQRVAIAGVLAL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15232977 515 SPKILLLDEATSALDSESE----RVVQESLDNASIgrTTIVIAHRLSTIRNADVICVIHNGQIVETGSHEELLKRIDG 588
Cdd:PRK13648 160 NPSVIILDEATSMLDPDARqnllDLVRKVKSEHNI--TIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEIFDHAEE 235
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
1012-1215 |
1.37e-26 |
|
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: 108.41 E-value: 1.37e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1012 IFENFSIEIDEGKSTAIVGTSGSGKSTIIGLI--ERFYDPLKGTVKIDGRDIrsyHLRSLRKYISLVSQEPMLFAG-TIR 1088
Cdd:cd03213 24 LLKNVSGKAKPGELTAIMGPSGAGKSTLLNALagRRTGLGVSGEVLINGRPL---DKRSFRKIIGYVPQDDILHPTlTVR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1089 ENIMYggtsdkideseiieAAKaanahdfitsLSngydtncgdkgvQLSGGQKQRIAIARAVLKNPSVLLLDEATSALDS 1168
Cdd:cd03213 101 ETLMF--------------AAK----------LR------------GLSGGERKRVSIALELVSNPSLLFLDEPTSGLDS 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15232977 1169 KSERVVQDALER-VMVGRTSIMIAHRLST--IQNCDMIVVLGKGKIVESG 1215
Cdd:cd03213 145 SSALQVMSLLRRlADTGRTIICSIHQPSSeiFELFDKLLLLSQGRVIYFG 194
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
999-1221 |
1.74e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 110.57 E-value: 1.74e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 999 NVDFAYPTRPDVVIFENFSIEIDEGKSTAIVGTSGSGKSTIIGLIERFYDPLKGTVKIDGRDIRSYHLRSLRKYISLVSQ 1078
Cdd:PRK13642 9 NLVFKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIGMVFQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1079 EP--MLFAGTIRENIMYGGTSDKIDESEII----EAAKAANAHDFITSlsngydtncgdKGVQLSGGQKQRIAIARAVLK 1152
Cdd:PRK13642 89 NPdnQFVGATVEDDVAFGMENQGIPREEMIkrvdEALLAVNMLDFKTR-----------EPARLSGGQKQRVAVAGIIAL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15232977 1153 NPSVLLLDEATSALD--SKSE--RVVQDALERVMVgrTSIMIAHRLSTIQNCDMIVVLGKGKIVESGTHSSLL 1221
Cdd:PRK13642 158 RPEIIILDESTSMLDptGRQEimRVIHEIKEKYQL--TVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELF 228
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
378-585 |
2.17e-26 |
|
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: 108.96 E-value: 2.17e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 378 DDLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYDPIAGEILIDGVSIDKLqvNWLRSQMGLVSQEPVLFA-TSITENIL 456
Cdd:cd03299 16 KNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNL--PPEKRDISYVPQNYALFPhMTVYKNIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 457 FG--------KEDASldEVVEAAKASNAHTFISQFPLgyktqvgergvQMSGGQKQRIAIARAIIKSPKILLLDEATSAL 528
Cdd:cd03299 94 YGlkkrkvdkKEIER--KVLEIAEMLGIDHLLNRKPE-----------TLSGGEQQRVAIARALVVNPKILLLDEPFSAL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 529 DSESERVVQESLDNA--SIGRTTIVIAHRLSTIRN-ADVICVIHNGQIVETGSHEELLKR 585
Cdd:cd03299 161 DVRTKEKLREELKKIrkEFGVTVLHVTHDFEEAWAlADKVAIMLNGKLIQVGKPEEVFKK 220
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
978-1216 |
2.18e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 111.48 E-value: 2.18e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 978 IEPKNPdgyVAEKIKGQITFLNVDFAYPTRPDVVIFENFSIEIDEGKSTAIVGTSGSGKSTIIGLIERFYDPLKGTV--- 1054
Cdd:PRK13631 10 LKVPNP---LSDDIILRVKNLYCVFDEKQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIqvg 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1055 ------KIDGRDIRSYHL-------RSLRKYISLVSQEP--MLFAGTIRENIMYGGTSDKIDEseiIEAAKAANAHDFIT 1119
Cdd:PRK13631 87 diyigdKKNNHELITNPYskkiknfKELRRRVSMVFQFPeyQLFKDTIEKDIMFGPVALGVKK---SEAKKLAKFYLNKM 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1120 SLSNGY-DTNcgdkGVQLSGGQKQRIAIARAVLKNPSVLLLDEATSALDSKSER-VVQDALERVMVGRTSIMIAHRLSTI 1197
Cdd:PRK13631 164 GLDDSYlERS----PFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHeMMQLILDAKANNKTVFVITHTMEHV 239
|
250 260
....*....|....*....|
gi 15232977 1198 -QNCDMIVVLGKGKIVESGT 1216
Cdd:PRK13631 240 lEVADEVIVMDKGKILKTGT 259
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
391-582 |
2.27e-26 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 109.48 E-value: 2.27e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 391 ALVGGSGSGKSTVISLLQRFYD-----PIAGEILIDGVSI-----DKLQvnwLRSQMGLVSQEPVLFATSITENILFG-- 458
Cdd:PRK14239 35 ALIGPSGSGKSTLLRSINRMNDlnpevTITGSIVYNGHNIysprtDTVD---LRKEIGMVFQQPNPFPMSIYENVVYGlr 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 459 ----KEDASLDEVVEAA-KASNAHTFIsqfplgyKTQVGERGVQMSGGQKQRIAIARAIIKSPKILLLDEATSALDSESE 533
Cdd:PRK14239 112 lkgiKDKQVLDEAVEKSlKGASIWDEV-------KDRLHDSALGLSGGQQQRVCIARVLATSPKIILLDEPTSALDPISA 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15232977 534 RVVQESLDNASIGRTTIVIAHRLSTI-RNADVICVIHNGQIVETGSHEEL 582
Cdd:PRK14239 185 GKIEETLLGLKDDYTMLLVTRSMQQAsRISDRTGFFLDGDLIEYNDTKQM 234
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
995-1212 |
2.62e-26 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 108.99 E-value: 2.62e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 995 ITFLNVDFAYPTrpDVVIFENFSIEIDEGKSTAIVGTSGSGKSTIIGLIERFYDPLKGTVKIDGRDI---RSYHLRSLRK 1071
Cdd:COG3638 3 LELRNLSKRYPG--GTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVtalRGRALRRLRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1072 YISLVSQEPMLFAG-TIRENIMYGgtsdkideseiieaakAANAHDFITSLSNGYDTNCGDKGV---------------- 1134
Cdd:COG3638 81 RIGMIFQQFNLVPRlSVLTNVLAG----------------RLGRTSTWRSLLGLFPPEDRERALealervgladkayqra 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1135 -QLSGGQKQRIAIARAVLKNPSVLLLDEATSALDSKSERVVQDALERVMV--GRTSIMIAHRLSTIQN-CDMIVVLGKGK 1210
Cdd:COG3638 145 dQLSGGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIARedGITVVVNLHQVDLARRyADRIIGLRDGR 224
|
..
gi 15232977 1211 IV 1212
Cdd:COG3638 225 VV 226
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
999-1216 |
2.94e-26 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 109.36 E-value: 2.94e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 999 NVDFAYPTRPdvvIFENFSIEIDEGKSTAIVGTSGSGKSTIIGLIERFYDpLKGTVKIDGR------DI--RSYHLRSLR 1070
Cdd:PRK14258 12 NLSFYYDTQK---ILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNE-LESEVRVEGRveffnqNIyeRRVNLNRLR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1071 KYISLVSQEPMLFAGTIRENIMYG----GTSDKIDESEIIEAA-KAANAHDFITSlsngydtNCGDKGVQLSGGQKQRIA 1145
Cdd:PRK14258 88 RQVSMVHPKPNLFPMSVYDNVAYGvkivGWRPKLEIDDIVESAlKDADLWDEIKH-------KIHKSALDLSGGQQQRLC 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1146 IARAVLKNPSVLLLDEATSALDS----KSERVVQDALERVMVgrTSIMIAHRLSTIQNCDMIVVLGKG------KIVESG 1215
Cdd:PRK14258 161 IARALAVKPKVLLMDEPCFGLDPiasmKVESLIQSLRLRSEL--TMVIVSHNLHQVSRLSDFTAFFKGnenrigQLVEFG 238
|
.
gi 15232977 1216 T 1216
Cdd:PRK14258 239 L 239
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
359-628 |
5.02e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 109.48 E-value: 5.02e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 359 VEFNHVKFTYLS-RP-ETTIFDDLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYDPIAGEILIDGVSI-----DKlQVN 431
Cdd:PRK13646 3 IRFDNVSYTYQKgTPyEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIthktkDK-YIR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 432 WLRSQMGLVSQ--EPVLFATSITENILFGKEDASLDevVEAAKaSNAHTFISQfpLGYKTQVGERG-VQMSGGQKQRIAI 508
Cdd:PRK13646 82 PVRKRIGMVFQfpESQLFEDTVEREIIFGPKNFKMN--LDEVK-NYAHRLLMD--LGFSRDVMSQSpFQMSGGQMRKIAI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 509 ARAIIKSPKILLLDEATSALDSESERVVQESLDNASI--GRTTIVIAHRLSTI-RNADVICVIHNGQIVETGSHEELLKr 585
Cdd:PRK13646 157 VSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTdeNKTIILVSHDMNEVaRYADEVIVMKEGSIVSQTSPKELFK- 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 15232977 586 iDGQYTS--------LVSLQQMENEESNVNIN-VSVTKDQVMSLSKDFKYSQ 628
Cdd:PRK13646 236 -DKKKLAdwhiglpeIVQLQYDFEQKYQTKLKdIALTEEEFVSLYKEWQHEK 286
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
1008-1215 |
5.35e-26 |
|
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: 107.34 E-value: 5.35e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1008 PDVVIFENFSIEIDEGKSTAIVGTSGSGKSTIIGLIERFYDPLKGTVKIDGRDIRSyhLRSLRKYISLVSQEPMLFAG-T 1086
Cdd:cd03301 11 GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTD--LPPKDRDIAMVFQNYALYPHmT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1087 IRENIMYGGTSDKIDESEIIEAAKAANAHDFITSLSNGYDTncgdkgvQLSGGQKQRIAIARAVLKNPSVLLLDEATSAL 1166
Cdd:cd03301 89 VYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPK-------QLSGGQRQRVALGRAIVREPKVFLMDEPLSNL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15232977 1167 DSKSERVVQDALERVM--VGRTSIMIAH-RLSTIQNCDMIVVLGKGKIVESG 1215
Cdd:cd03301 162 DAKLRVQMRAELKRLQqrLGTTTIYVTHdQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
378-582 |
5.66e-26 |
|
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: 107.81 E-value: 5.66e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 378 DDLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYDPIAGEILIDGVSIDKLQVNwlRSQMGLVSQEPVLFA-TSITENIL 456
Cdd:cd03296 19 DDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQ--ERNVGFVFQHYALFRhMTVFDNVA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 457 FG-KEDASLDEVVEAAKASNAHTFISQFPLgykTQVGER-GVQMSGGQKQRIAIARAIIKSPKILLLDEATSALDS---- 530
Cdd:cd03296 97 FGlRVKPRSERPPEAEIRAKVHELLKLVQL---DWLADRyPAQLSGGQRQRVALARALAVEPKVLLLDEPFGALDAkvrk 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15232977 531 ESERVVQESLDNasIGRTTIVIAHRLS-TIRNADVICVIHNGQIVETGSHEEL 582
Cdd:cd03296 174 ELRRWLRRLHDE--LHVTTVFVTHDQEeALEVADRVVVMNKGRIEQVGTPDEV 224
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1006-1205 |
6.84e-26 |
|
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: 106.79 E-value: 6.84e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1006 TRPDVVIFENFSIEIDEGKSTAIVGTSGSGKST----IIGLIErfydPLKGTVKIDGRDIRSyHLRSLRKYISLVSQEPM 1081
Cdd:COG4133 11 RRGERLLFSGLSFTLAAGEALALTGPNGSGKTTllriLAGLLP----PSAGEVLWNGEPIRD-AREDYRRRLAYLGHADG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1082 LFAG-TIRENI-----MYGgtsDKIDESEIIEAAKAANAHDFItslsngyDTNCGdkgvQLSGGQKQRIAIARAVLKNPS 1155
Cdd:COG4133 86 LKPElTVRENLrfwaaLYG---LRADREAIDEALEAVGLAGLA-------DLPVR----QLSAGQKRRVALARLLLSPAP 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15232977 1156 VLLLDEATSALDSKS----ERVVQDALERvmvGRTSIMIAHRLSTIQNCDMIVV 1205
Cdd:COG4133 152 LWLLDEPFTALDAAGvallAELIAAHLAR---GGAVLLTTHQPLELAAARVLDL 202
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
1012-1225 |
1.10e-25 |
|
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: 115.39 E-value: 1.10e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1012 IFENFSIEIDEGKSTAIVGTSGSGKSTIIGLIERFYDPLKGTVKIDGRdirsyhlrslrkyISLVSQEPMLFAGTIRENI 1091
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR-------------ISFSPQTSWIMPGTIKDNI 507
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1092 MYGGTSDKIDESEIIeaaKAANAHDFITSLSNGYDTNCGDKGVQLSGGQKQRIAIARAVLKNPSVLLLDEATSALDSKSE 1171
Cdd:TIGR01271 508 IFGLSYDEYRYTSVI---KACQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTE 584
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15232977 1172 R-VVQDALERVMVGRTSIMIAHRLSTIQNCDMIVVLGKGKIVESGTHSSLLEKGP 1225
Cdd:TIGR01271 585 KeIFESCLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSELQAKRP 639
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
363-574 |
1.17e-25 |
|
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: 105.80 E-value: 1.17e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 363 HVKFTYlsRPETTIFDDLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYDPIAGEILIDGVSIDKLQvnwLRSQMGLVSQ 442
Cdd:cd03226 4 NISFSY--KKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKE---RRKSIGYVMQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 443 EP--VLFATSITENILFGKEDASLD-EVVEAA-KASNAHTFISQFPLgyktqvgergvQMSGGQKQRIAIARAIIKSPKI 518
Cdd:cd03226 79 DVdyQLFTDSVREELLLGLKELDAGnEQAETVlKDLDLYALKERHPL-----------SLSGGQKQRLAIAAALLSGKDL 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15232977 519 LLLDEATSALDSESERVVQES-LDNASIGRTTIVIAHRLSTI-RNADVICVIHNGQIV 574
Cdd:cd03226 148 LIFDEPTSGLDYKNMERVGELiRELAAQGKAVIVITHDYEFLaKVCDRVLLLANGAIV 205
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
1017-1222 |
1.29e-25 |
|
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: 106.36 E-value: 1.29e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1017 SIEIDEGKSTAIVGTSGSGKST----IIGLIerfyDPLKGTVKIDGRDIRSY--HLRsLRKYISLVSQEPMLFAG-TIRE 1089
Cdd:cd03224 20 SLTVPEGEIVALLGRNGAGKTTllktIMGLL----PPRSGSIRFDGRDITGLppHER-ARAGIGYVPEGRRIFPElTVEE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1090 NI-MYGGTSDKIDESEIIEAAkaanahdfitslsngYD------TNCGDKGVQLSGGQKQRIAIARAVLKNPSVLLLDEA 1162
Cdd:cd03224 95 NLlLGAYARRRAKRKARLERV---------------YElfprlkERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15232977 1163 TSALDSKSERVVQDALERVMVGRTSIMI----AHRLSTIqnCDMIVVLGKGKIVESGTHSSLLE 1222
Cdd:cd03224 160 SEGLAPKIVEEIFEAIRELRDEGVTILLveqnARFALEI--ADRAYVLERGRVVLEGTAAELLA 221
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
355-585 |
1.32e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 107.90 E-value: 1.32e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 355 MKGEVEFNHVKFTYlsRPETTIFDDLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYDPIAGEILIDGVSIDKLQVNWLR 434
Cdd:PRK13647 1 MDNIIEVEDLHFRY--KDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 435 SQMGLVSQEP--VLFATSITENILFGKEDASLDE------VVEAAKASNAHTFISQFPLgyktqvgergvQMSGGQKQRI 506
Cdd:PRK13647 79 SKVGLVFQDPddQVFSSTVWDDVAFGPVNMGLDKdeverrVEEALKAVRMWDFRDKPPY-----------HLSYGQKKRV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 507 AIARAIIKSPKILLLDEATSALDSESERVVQESLDNASIGRTTIVIA-HRLS-TIRNADVICVIHNGQIVETGSHEELLK 584
Cdd:PRK13647 148 AIAGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVAtHDVDlAAEWADQVIVLKEGRVLAEGDKSLLTD 227
|
.
gi 15232977 585 R 585
Cdd:PRK13647 228 E 228
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
378-584 |
1.77e-25 |
|
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: 106.37 E-value: 1.77e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 378 DDLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYDPIAGEILIDGVSIDKLQVNwLRSQMGLVS--QEPVLFAT-SITEN 454
Cdd:cd03219 17 DDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPH-EIARLGIGRtfQIPRLFPElTVLEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 455 ILFG-----KEDASLDEVVEAAKASN--AHTFISQFPLGYK--TQVGErgvqMSGGQKQRIAIARAIIKSPKILLLDEAT 525
Cdd:cd03219 96 VMVAaqartGSGLLLARARREEREARerAEELLERVGLADLadRPAGE----LSYGQQRRLEIARALATDPKLLLLDEPA 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15232977 526 SAL-DSESERVVQESLDNASIGRTTIVIAHRLSTIRN-ADVICVIHNGQIVETGSHEELLK 584
Cdd:cd03219 172 AGLnPEETEELAELIRELRERGITVLLVEHDMDVVMSlADRVTVLDQGRVIAEGTPDEVRN 232
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
995-1223 |
1.77e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 107.52 E-value: 1.77e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 995 ITFLNVDFAYPT-RPdvviFE-----NFSIEIDEGKSTAIVGTSGSGKSTIIGLIERFYDPLKGTVKIDGRDIRSY---- 1064
Cdd:PRK13649 3 INLQNVSYTYQAgTP----FEgralfDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTsknk 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1065 HLRSLRKYISLVSQ--EPMLFAGTIRENIMYG----GTSDKidESEIIEAAKAANAhdfitslsnGYDTNCGDKG-VQLS 1137
Cdd:PRK13649 79 DIKQIRKKVGLVFQfpESQLFEETVLKDVAFGpqnfGVSQE--EAEALAREKLALV---------GISESLFEKNpFELS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1138 GGQKQRIAIARAVLKNPSVLLLDEATSALDSKSERVVQDALERV-MVGRTSIMIAHRLSTIQN-CDMIVVLGKGKIVESG 1215
Cdd:PRK13649 148 GGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLhQSGMTIVLVTHLMDDVANyADFVYVLEKGKLVLSG 227
|
....*...
gi 15232977 1216 THSSLLEK 1223
Cdd:PRK13649 228 KPKDIFQD 235
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
360-577 |
2.46e-25 |
|
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: 105.31 E-value: 2.46e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 360 EFNHVKFTYLSRPettIFDDLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYDPIAGEILIDGVSIDKLqvnwlRSQMGL 439
Cdd:cd03235 1 EVEDLTVSYGGHP---VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKE-----RKRIGY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 440 VSQEPVL---FATSITENILFG------------KEDAslDEVVEAAKASNAHTFISQfPLGyktqvgergvQMSGGQKQ 504
Cdd:cd03235 73 VPQRRSIdrdFPISVRDVVLMGlyghkglfrrlsKADK--AKVDEALERVGLSELADR-QIG----------ELSGGQQQ 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15232977 505 RIAIARAIIKSPKILLLDEATSALDSESERVVQESLDN-ASIGRTTIVIAHRLSTIRNA--DVICVihNGQIVETG 577
Cdd:cd03235 140 RVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRElRREGMTILVVTHDLGLVLEYfdRVLLL--NRTVVASG 213
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
1017-1215 |
2.53e-25 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 108.28 E-value: 2.53e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1017 SIEIDEGKSTAIVGTSGSGKSTIIGLIERFYDPLKGTVKIDGRDIRSYH---LRSLRKYISLVSQEP-------MLFAGT 1086
Cdd:COG4608 38 SFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSgreLRPLRRRMQMVFQDPyaslnprMTVGDI 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1087 IRENIMYGGTSDKIDESEIIEA--------AKAAN--AHDFitslsngydtncgdkgvqlSGGQKQRIAIARAVLKNPSV 1156
Cdd:COG4608 118 IAEPLRIHGLASKAERRERVAEllelvglrPEHADryPHEF-------------------SGGQRQRIGIARALALNPKL 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15232977 1157 LLLDEATSALD-SKSERVV------QDALervmvGRTSIMIAHRLSTIQN-CDMIVVLGKGKIVESG 1215
Cdd:COG4608 179 IVCDEPVSALDvSIQAQVLnlledlQDEL-----GLTYLFISHDLSVVRHiSDRVAVMYLGKIVEIA 240
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
993-1216 |
2.95e-25 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 108.62 E-value: 2.95e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 993 GQITFLNVDFAYPtrpDVVIFENFSIEIDEGKSTAIVGTSGSGKSTIIGLIERFYDPLKGTVKIDGRDIrsYHLRSLRKY 1072
Cdd:COG3839 2 ASLELENVSKSYG---GVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDV--TDLPPKDRN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1073 ISLVSQEPMLF-AGTIRENIMYGGTSDKIDESEI----IEAAKAANahdfITSLSNgydtncgDKGVQLSGGQKQRIAIA 1147
Cdd:COG3839 77 IAMVFQSYALYpHMTVYENIAFPLKLRKVPKAEIdrrvREAAELLG----LEDLLD-------RKPKQLSGGQRQRVALG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1148 RAVLKNPSVLLLDEATSALDSKSeRV--------VQDALervmvGRTSIMIAH------RLStiqncDMIVVLGKGKIVE 1213
Cdd:COG3839 146 RALVREPKVFLLDEPLSNLDAKL-RVemraeikrLHRRL-----GTTTIYVTHdqveamTLA-----DRIAVMNDGRIQQ 214
|
...
gi 15232977 1214 SGT 1216
Cdd:COG3839 215 VGT 217
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
995-1213 |
4.39e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 106.84 E-value: 4.39e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 995 ITFLNVDFAY-PTRP-DVVIFENFSIEIDEGKSTAIVGTSGSGKSTIIGLIERFYDPLKGTVKIDGRDIR----SYHLRS 1068
Cdd:PRK13641 3 IKFENVDYIYsPGTPmEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpetgNKNLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1069 LRKYISLVSQ--EPMLFAGTIRENIMYG----GTSDKIDESEIIEAAKAAnahdfitslsnGYDTNCGDKG-VQLSGGQK 1141
Cdd:PRK13641 83 LRKKVSLVFQfpEAQLFENTVLKDVEFGpknfGFSEDEAKEKALKWLKKV-----------GLSEDLISKSpFELSGGQM 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15232977 1142 QRIAIARAVLKNPSVLLLDEATSALDSKS-ERVVQDALERVMVGRTSIMIAHRLSTI-QNCDMIVVLGKGKIVE 1213
Cdd:PRK13641 152 RRVAIAGVMAYEPEILCLDEPAAGLDPEGrKEMMQLFKDYQKAGHTVILVTHNMDDVaEYADDVLVLEHGKLIK 225
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1014-1229 |
4.86e-25 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 108.77 E-value: 4.86e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1014 ENFSIEIDEGKSTAIVGTSGSGKSTIIGLIERFYDPLKGTVKIDGRDIRsyHLRSLRKYISLVSQEPMLFAG-TIRENIM 1092
Cdd:PRK11607 36 DDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLS--HVPPYQRPINMMFQSYALFPHmTVEQNIA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1093 YGGTSDKIDESEIieaakAANAHDFITSLSngYDTNCGDKGVQLSGGQKQRIAIARAVLKNPSVLLLDEATSALDSK-SE 1171
Cdd:PRK11607 114 FGLKQDKLPKAEI-----ASRVNEMLGLVH--MQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKlRD 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15232977 1172 RV---VQDALERvmVGRTSIMIAH-RLSTIQNCDMIVVLGKGKIVESGTHSSLLEKgPTGTY 1229
Cdd:PRK11607 187 RMqleVVDILER--VGVTCVMVTHdQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEH-PTTRY 245
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
369-585 |
5.19e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 105.38 E-value: 5.19e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 369 LSRPETTIFDDLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYD-----PIAGEILIDGVSIDKLQVNWLRSQMGLVSQE 443
Cdd:PRK14247 11 VSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElypeaRVSGEVYLDGQDIFKMDVIELRRRVQMVFQI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 444 PVLFAT-SITENILFG-------KEDASLDEVVEAAKASnahtfiSQFPLGYKTQVGERGVQMSGGQKQRIAIARAIIKS 515
Cdd:PRK14247 91 PNPIPNlSIFENVALGlklnrlvKSKKELQERVRWALEK------AQLWDEVKDRLDAPAGKLSGGQQQRLCIARALAFQ 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15232977 516 PKILLLDEATSALDSESERVVQESLDNASIGRTTIVIAH-RLSTIRNADVICVIHNGQIVETGSHEELLKR 585
Cdd:PRK14247 165 PEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHfPQQAARISDYVAFLYKGQIVEWGPTREVFTN 235
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
1015-1216 |
5.69e-25 |
|
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: 104.83 E-value: 5.69e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1015 NFSIEIDEGKSTAIVGTSGSGKSTIIGLIERFYDPLKGTVKIDGRDI--RSYHLRSlRKYISLVSQEPMLFAG-TIRENI 1091
Cdd:cd03219 18 DVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDItgLPPHEIA-RLGIGRTFQIPRLFPElTVLENV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1092 MYG-------GTSDKIDESEIIEA-AKAANAHDFITsLSNGYDTNCGDkgvqLSGGQKQRIAIARAVLKNPSVLLLDEAT 1163
Cdd:cd03219 97 MVAaqartgsGLLLARARREEREArERAEELLERVG-LADLADRPAGE----LSYGQQRRLEIARALATDPKLLLLDEPA 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15232977 1164 SALDSKSERVVQDALERVMV-GRTSIMIAHRLSTIQN-CDMIVVLGKGKIVESGT 1216
Cdd:cd03219 172 AGLNPEETEELAELIRELRErGITVLLVEHDMDVVMSlADRVTVLDQGRVIAEGT 226
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
995-1223 |
6.37e-25 |
|
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: 113.12 E-value: 6.37e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 995 ITFLNVDFAYpTRPDVVIFENFSIEIDEGKSTAIVGTSGSGKSTIIGLIERFYDPLKGTVKIDGRdirsyhlrslrkyIS 1074
Cdd:TIGR00957 637 ITVHNATFTW-ARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS-------------VA 702
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1075 LVSQEPMLFAGTIRENIMYGGTSDKIDESEIIEAAkaANAHDfITSLSNGYDTNCGDKGVQLSGGQKQRIAIARAVLKNP 1154
Cdd:TIGR00957 703 YVPQQAWIQNDSLRENILFGKALNEKYYQQVLEAC--ALLPD-LEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNA 779
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15232977 1155 SVLLLDEATSALDSKSERVVQDAL---ERVMVGRTSIMIAHRLSTIQNCDMIVVLGKGKIVESGTHSSLLEK 1223
Cdd:TIGR00957 780 DIYLFDDPLSAVDAHVGKHIFEHVigpEGVLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQR 851
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
359-577 |
6.94e-25 |
|
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: 103.87 E-value: 6.94e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 359 VEFNHVKFTYlsrPETTIFDDLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYDPIAGEILIDGVSIDKLQVNwlRSQMG 438
Cdd:cd03301 1 VELENVTKRF---GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPK--DRDIA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 439 LVSQEPVLFA-TSITENILFG------KEDASLDEVVEAAKAsnahtfisqfpLGYKTQVGERGVQMSGGQKQRIAIARA 511
Cdd:cd03301 76 MVFQNYALYPhMTVYDNIAFGlklrkvPKDEIDERVREVAEL-----------LQIEHLLDRKPKQLSGGQRQRVALGRA 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15232977 512 IIKSPKILLLDEATSALD--------SESERVVQEsldnasIGRTTIVIAH-RLSTIRNADVICVIHNGQIVETG 577
Cdd:cd03301 145 IVREPKVFLMDEPLSNLDaklrvqmrAELKRLQQR------LGTTTIYVTHdQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
999-1212 |
7.32e-25 |
|
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: 103.49 E-value: 7.32e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 999 NVDFAYPTRPDVVifENFSIEIDEGKSTAIVGTSGSGKSTIIGLIERFYDPLKGTVKIDGRDIrsyHLRSLRKYISLVSQ 1078
Cdd:cd03226 4 NISFSYKKGTEIL--DDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPI---KAKERRKSIGYVMQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1079 EP--MLFAGTIRENIMYG--GTSDKIDESEII----EAAKAANAHDFItslsngydtncgdkgvqLSGGQKQRIAIARAV 1150
Cdd:cd03226 79 DVdyQLFTDSVREELLLGlkELDAGNEQAETVlkdlDLYALKERHPLS-----------------LSGGQKQRLAIAAAL 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15232977 1151 LKNPSVLLLDEATSALDSKSERVVQDALERVM-VGRTSIMIAHRLSTIQN-CDMIVVLGKGKIV 1212
Cdd:cd03226 142 LSGKDLLIFDEPTSGLDYKNMERVGELIRELAaQGKAVIVITHDYEFLAKvCDRVLLLANGAIV 205
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1015-1194 |
9.82e-25 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 104.86 E-value: 9.82e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1015 NFSIEIDEGKSTAIVGTSGSGKSTIIGLIERFYD-----PLKGTVKIDGRDIrsYHLRS----LRKYISLVSQEPMLFAG 1085
Cdd:PRK14239 23 SVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDlnpevTITGSIVYNGHNI--YSPRTdtvdLRKEIGMVFQQPNPFPM 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1086 TIRENIMYG----GTSDKIDESEIIEAA-KAANAHDFITSLSNgydtncgDKGVQLSGGQKQRIAIARAVLKNPSVLLLD 1160
Cdd:PRK14239 101 SIYENVVYGlrlkGIKDKQVLDEAVEKSlKGASIWDEVKDRLH-------DSALGLSGGQQQRVCIARVLATSPKIILLD 173
|
170 180 190
....*....|....*....|....*....|....
gi 15232977 1161 EATSALDSKSERVVQDALERVMVGRTSIMIAHRL 1194
Cdd:PRK14239 174 EPTSALDPISAGKIEETLLGLKDDYTMLLVTRSM 207
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
375-576 |
1.18e-24 |
|
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: 104.05 E-value: 1.18e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 375 TIFDDLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYDPIAGEILIDGVSIDKL---QVNWLRSQ-MGLVSQEPVLFAT- 449
Cdd:COG4181 26 TILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALdedARARLRARhVGFVFQSFQLLPTl 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 450 SITENI-----LFGKEDAsldevveAAKASNAhtfisqfpLGyktQVG--ERG----VQMSGGQKQRIAIARAIIKSPKI 518
Cdd:COG4181 106 TALENVmlpleLAGRRDA-------RARARAL--------LE---RVGlgHRLdhypAQLSGGEQQRVALARAFATEPAI 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 519 LLLDEATSALDSESERVVQESLD--NASIGRTTIVIAHRLSTIRNADVICVIHNGQIVET 576
Cdd:COG4181 168 LFADEPTGNLDAATGEQIIDLLFelNRERGTTLVLVTHDPALAARCDRVLRLRAGRLVED 227
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
995-1216 |
1.35e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 105.49 E-value: 1.35e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 995 ITFLNVDFAY-PTRPdvviFE-----NFSIEIDEGKSTAIVGTSGSGKSTIIGLIERFYDPLKGTVKIDGRDI----RSY 1064
Cdd:PRK13634 3 ITFQKVEHRYqYKTP----FErralyDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVItagkKNK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1065 HLRSLRKYISLVSQ--EPMLFAGTIRENIMYGGTSDKIDESEIIEAAKAANAhdfITSLSNGYDTNcgdKGVQLSGGQKQ 1142
Cdd:PRK13634 79 KLKPLRKKVGIVFQfpEHQLFEETVEKDICFGPMNFGVSEEDAKQKAREMIE---LVGLPEELLAR---SPFELSGGQMR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15232977 1143 RIAIARAVLKNPSVLLLDEATSALDSKSERVVQDALERVM--VGRTSIMIAHRLSTIQN-CDMIVVLGKGKIVESGT 1216
Cdd:PRK13634 153 RVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHkeKGLTTVLVTHSMEDAARyADQIVVMHKGTVFLQGT 229
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
375-585 |
1.64e-24 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 106.73 E-value: 1.64e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 375 TIFDDLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYDPIAGEILIDGVSIDKLQVNwlRSQMGLVSQEPVLFA-TSITE 453
Cdd:PRK11432 20 TVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQ--QRDICMVFQSYALFPhMSLGE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 454 NILFG--KEDASLDEVVEAAKASNAHTFISQFplgyktqvGERGV-QMSGGQKQRIAIARAIIKSPKILLLDEATSALDS 530
Cdd:PRK11432 98 NVGYGlkMLGVPKEERKQRVKEALELVDLAGF--------EDRYVdQISGGQQQRVALARALILKPKVLLFDEPLSNLDA 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15232977 531 ESERVVQESLD--NASIGRTTIVIAHRLS-TIRNADVICVIHNGQIVETGSHEELLKR 585
Cdd:PRK11432 170 NLRRSMREKIRelQQQFNITSLYVTHDQSeAFAVSDTVIVMNKGKIMQIGSPQELYRQ 227
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
379-590 |
1.65e-24 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 107.43 E-value: 1.65e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 379 DLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYDPIAGEILIDGVSIDKLQVNWLRS----QMGLVSQEPVLFA-TSITE 453
Cdd:PRK10070 46 DASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREvrrkKIAMVFQSFALMPhMTVLD 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 454 NILFGKEDASLDEVVEAAKASNA--HTFISQFPLGYKTqvgergvQMSGGQKQRIAIARAIIKSPKILLLDEATSALDSE 531
Cdd:PRK10070 126 NTAFGMELAGINAEERREKALDAlrQVGLENYAHSYPD-------ELSGGMRQRVGLARALAINPDILLMDEAFSALDPL 198
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15232977 532 SERVVQESLD--NASIGRTTIVIAHRL-STIRNADVICVIHNGQIVETGSHEELLKRIDGQY 590
Cdd:PRK10070 199 IRTEMQDELVklQAKHQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDY 260
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
714-929 |
1.94e-24 |
|
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 and similar proteins; This group includes Arabidopsis ABC transporter B family member 27 (also known as AtABCB27, aluminum tolerance-related ATP-binding cassette transporter, transporter associated with antigen processing-like protein 2, AtTAP2, and ALS1) which may play a role in aluminum resistance. The ABC_6TM_TAP_ABCB8_10_like subgroup of the ABC_6TM exporter family includes ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection, as well as ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. The ABC_6TM exporter family represents the six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in the ABC_6TM exporter family.
Pssm-ID: 350053 [Multi-domain] Cd Length: 295 Bit Score: 105.02 E-value: 1.94e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 714 IYVLLFVGLAIFSFLvnisQHYGFAYMGEYLTKRIREQMLSKILTFEVNWFDIddNSSGAICSRLAKDANVVRSMVGDRM 793
Cdd:cd18780 47 ILLGVVLIGSIATFL----RSWLFTLAGERVVARLRKRLFSAIIAQEIAFFDV--TRTGELLNRLSSDTQVLQNAVTVNL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 794 SLLVQTISAVIIACIIGLVIAWRLAIVMISVQPLIVVCFYTQRVLLKSLSEKASKAQDESSKLAAEAVSNIRTITAFSSQ 873
Cdd:cd18780 121 SMLLRYLVQIIGGLVFMFTTSWKLTLVMLSVVPPLSIGAVIYGKYVRKLSKKFQDALAAASTVAEESISNIRTVRSFAKE 200
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 15232977 874 ERIIKLLKKVQEGPRRESVHRSWLAGIVLGTSRSLITCTSALNFWYGGRLIADGKI 929
Cdd:cd18780 201 TKEVSRYSEKINESYLLGKKLARASGGFNGFMGAAAQLAIVLVLWYGGRLVIDGEL 256
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
379-587 |
1.97e-24 |
|
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: 106.35 E-value: 1.97e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 379 DLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYDPIAGEILIDGV----SIDKLQVNWLRSQMGLVSQEPVLFA-TSITE 453
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRtlfdSRKGIFLPPEKRRIGYVFQEARLFPhLSVRG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 454 NILFGKEDA-------SLDEVVEAakasnahtfisqfpLGYKTQVGERGVQMSGGQKQRIAIARAIIKSPKILLLDEATS 526
Cdd:TIGR02142 95 NLRYGMKRArpserriSFERVIEL--------------LGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15232977 527 ALDSESERVVQESLDN--ASIGRTTIVIAHRLSTI-RNADVICVIHNGQIVETGSHEELLKRID 587
Cdd:TIGR02142 161 ALDDPRKYEILPYLERlhAEFGIPILYVSHSLQEVlRLADRVVVLEDGRVAAAGPIAEVWASPD 224
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
1012-1225 |
2.51e-24 |
|
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: 104.55 E-value: 2.51e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1012 IFENFSIEIDEGKSTAIVGTSGSGKSTIIGLIERFYDPLKGTVKIDGRdirsyhlrslrkyISLVSQEPMLFAGTIRENI 1091
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR-------------ISFSSQFSWIMPGTIKENI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1092 MYGGTSDKIDESEIIeaaKAANAHDFITSLSNGYDTNCGDKGVQLSGGQKQRIAIARAVLKNPSVLLLDEATSALDSKSE 1171
Cdd:cd03291 119 IFGVSYDEYRYKSVV---KACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTE 195
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15232977 1172 R-VVQDALERVMVGRTSIMIAHRLSTIQNCDMIVVLGKGKIVESGTHSSLLEKGP 1225
Cdd:cd03291 196 KeIFESCVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQSLRP 250
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
1017-1223 |
2.70e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 104.05 E-value: 2.70e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1017 SIEIDEGKSTAIVGTSGSGKSTIIGLIERFYDPLKGTVKIDGRDIRSYHLRSLRKYISLVSQEP--MLFAGTIRENIMYG 1094
Cdd:PRK13647 25 SLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGLVFQDPddQVFSSTVWDDVAFG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1095 GTSDKIDESEII----EAAKAANAHDFitslsngydtncGDKG-VQLSGGQKQRIAIARAVLKNPSVLLLDEATSALDSK 1169
Cdd:PRK13647 105 PVNMGLDKDEVErrveEALKAVRMWDF------------RDKPpYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPR 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 15232977 1170 SERVVQDALERVMVGRTSIMIA-HRLS-TIQNCDMIVVLGKGKIVESGTHSSLLEK 1223
Cdd:PRK13647 173 GQETLMEILDRLHNQGKTVIVAtHDVDlAAEWADQVIVLKEGRVLAEGDKSLLTDE 228
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
387-577 |
3.07e-24 |
|
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: 101.99 E-value: 3.07e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 387 GKTVALVGGSGSGKSTVISLLQRFYDPIAGEILIDGV----SIDKLQVNWLRSQMGLVSQEPVLFA-TSITENILFG--- 458
Cdd:cd03297 23 EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTvlfdSRKKINLPPQQRKIGLVFQQYALFPhLNVRENLAFGlkr 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 459 KEDASLDEVVEAAKASnahtfisqFPLgykTQVGERGV-QMSGGQKQRIAIARAIIKSPKILLLDEATSALDSESERVVQ 537
Cdd:cd03297 103 KRNREDRISVDELLDL--------LGL---DHLLNRYPaQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLL 171
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 15232977 538 ESLDN--ASIGRTTIVIAHRLSTI-RNADVICVIHNGQIVETG 577
Cdd:cd03297 172 PELKQikKNLNIPVIFVTHDLSEAeYLADRIVVMEDGRLQYIG 214
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
382-583 |
3.63e-24 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 102.91 E-value: 3.63e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 382 LKIPAGKTVALVGGSGSGKSTVISLLQRFYDPIAGEILIDGVSID--------KLQVNWLRSQMGLVSQEPVLFA-TSIT 452
Cdd:PRK11264 24 LEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDtarslsqqKGLIRQLRQHVGFVFQNFNLFPhRTVL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 453 ENILFG-----KEDAslDEVVEAAKASNAHTFISqfplGYKTQVGERgvqMSGGQKQRIAIARAIIKSPKILLLDEATSA 527
Cdd:PRK11264 104 ENIIEGpvivkGEPK--EEATARARELLAKVGLA----GKETSYPRR---LSGGQQQRVAIARALAMRPEVILFDEPTSA 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15232977 528 LDSEserVVQESLDN----ASIGRTTIVIAHRLSTIRN-ADVICVIHNGQIVETGSHEELL 583
Cdd:PRK11264 175 LDPE---LVGEVLNTirqlAQEKRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAKALF 232
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
378-582 |
3.90e-24 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 107.80 E-value: 3.90e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 378 DDLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYDPIAGEILIDGVSIDklqvnwLRS-----QMG--LVSQEPVLFAT- 449
Cdd:COG1129 21 DGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVR------FRSprdaqAAGiaIIHQELNLVPNl 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 450 SITENILFGKEDAS---LD--EVVEAAKAsnahtFISQFPLGY--KTQVGErgvqMSGGQKQRIAIARAIIKSPKILLLD 522
Cdd:COG1129 95 SVAENIFLGREPRRgglIDwrAMRRRARE-----LLARLGLDIdpDTPVGD----LSVAQQQLVEIARALSRDARVLILD 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15232977 523 EATSAL-DSESER---VVQEsLdnASIGRTTIVIAHRLSTIRN-ADVICVIHNGQIVETGSHEEL 582
Cdd:COG1129 166 EPTASLtEREVERlfrIIRR-L--KAQGVAIIYISHRLDEVFEiADRVTVLRDGRLVGTGPVAEL 227
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
372-576 |
4.11e-24 |
|
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: 100.20 E-value: 4.11e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 372 PETTIFDDLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYDPIAGEILIDGvsidklqvnwlrsqmglvsqEPVLFATsi 451
Cdd:cd03216 11 GGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDG--------------------KEVSFAS-- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 452 tenilfgkedasldeVVEAAKAsnahtfisqfplgyktqvgerGV----QMSGGQKQRIAIARAIIKSPKILLLDEATSA 527
Cdd:cd03216 69 ---------------PRDARRA---------------------GIamvyQLSVGERQMVEIARALARNARLLILDEPTAA 112
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 15232977 528 L-DSESERVVQESLDNASIGRTTIVIAHRLSTIRN-ADVICVIHNGQIVET 576
Cdd:cd03216 113 LtPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEiADRVTVLRDGRVVGT 163
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
1013-1216 |
4.45e-24 |
|
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: 105.57 E-value: 4.45e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1013 FENFSIEID----EGKSTAIVGTSGSGKSTIIGLI---ERfydPLKGTVKIDGR---DIRSY-----HLRSlrkyISLVS 1077
Cdd:COG4148 11 RGGFTLDVDftlpGRGVTALFGPSGSGKTTLLRAIaglER---PDSGRIRLGGEvlqDSARGiflppHRRR----IGYVF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1078 QEPMLFAG-TIRENIMYG-----GTSDKIDESEIIEAAKaanahdfITSLSngydtncgDKGV-QLSGGQKQRIAIARAV 1150
Cdd:COG4148 84 QEARLFPHlSVRGNLLYGrkrapRAERRISFDEVVELLG-------IGHLL--------DRRPaTLSGGERQRVAIGRAL 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1151 LKNPSVLLLDEATSALDSKSERVVQDALERVmVGRTSI---MIAHRLSTIQN-CDMIVVLGKGKIVESGT 1216
Cdd:COG4148 149 LSSPRLLLMDEPLAALDLARKAEILPYLERL-RDELDIpilYVSHSLDEVARlADHVVLLEQGRVVASGP 217
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
368-583 |
4.78e-24 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 102.82 E-value: 4.78e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 368 YLSRPETTIFDDLCLKIPAGKTVALVGGSGSGKSTVISLLQRF---YDP---IAGEILIDGVSIDKLQVNWLRSQMGLVS 441
Cdd:PRK14246 17 YLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLieiYDSkikVDGKVLYFGKDIFQIDAIKLRKEVGMVF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 442 QEPVLFA-TSITENILFGKEDASLDEVVEAAKASNAhtfiSQFPLGYKTQVGER----GVQMSGGQKQRIAIARAIIKSP 516
Cdd:PRK14246 97 QQPNPFPhLSIYDNIAYPLKSHGIKEKREIKKIVEE----CLRKVGLWKEVYDRlnspASQLSGGQQQRLTIARALALKP 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15232977 517 KILLLDEATSALDSESERVVQESLDNASIGRTTIVIAHRLSTI-RNADVICVIHNGQIVETGSHEELL 583
Cdd:PRK14246 173 KVLLMDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVaRVADYVAFLYNGELVEWGSSNEIF 240
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
359-586 |
4.92e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 103.34 E-value: 4.92e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 359 VEFNHVKFTYLSRPETtIFDDLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYDPIAGE---ILIDGVSIDKLQVNWLRS 435
Cdd:PRK13640 6 VEFKHVSFTYPDSKKP-ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPnskITVDGITLTAKTVWDIRE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 436 QMGLVSQEP--VLFATSITENILFGKEDASldeVVEAAKASNAHTFISQfpLGYKTQVGERGVQMSGGQKQRIAIARAII 513
Cdd:PRK13640 85 KVGIVFQNPdnQFVGATVGDDVAFGLENRA---VPRPEMIKIVRDVLAD--VGMLDYIDSEPANLSGGQKQRVAIAGILA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 514 KSPKILLLDEATSALDSESER-----VVQESLDNasiGRTTIVIAHRLSTIRNADVICVIHNGQIVETGS------HEEL 582
Cdd:PRK13640 160 VEPKIIILDESTSMLDPAGKEqilklIRKLKKKN---NLTVISITHDIDEANMADQVLVLDDGKLLAQGSpveifsKVEM 236
|
....
gi 15232977 583 LKRI 586
Cdd:PRK13640 237 LKEI 240
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
379-578 |
6.40e-24 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 102.55 E-value: 6.40e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 379 DLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYDPIA-----GEILIDGVSIDKLQVN--WLRSQMGLVSQEPVLFATSI 451
Cdd:PRK14243 28 NVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLIPgfrveGKVTFHGKNLYAPDVDpvEVRRRIGMVFQKPNPFPKSI 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 452 TENILFGKE----DASLDEVVEAAkasnahtfISQFPL--GYKTQVGERGVQMSGGQKQRIAIARAIIKSPKILLLDEAT 525
Cdd:PRK14243 108 YDNIAYGARingyKGDMDELVERS--------LRQAALwdEVKDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDEPC 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15232977 526 SALDSESERVVQESLDNASIGRTTIVIAHRLSTIRNADVICVIHNGQIVETGS 578
Cdd:PRK14243 180 SALDPISTLRIEELMHELKEQYTIIIVTHNMQQAARVSDMTAFFNVELTEGGG 232
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
373-585 |
6.44e-24 |
|
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: 107.46 E-value: 6.44e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 373 ETTIFDDLCLKIPAGKTVALVGGSGSGKS-TVISLLQRFYDPIA---GEILIDGVSIDKL---QVNWLR-SQMGLVSQEP 444
Cdd:COG4172 22 TVEAVKGVSFDIAAGETLALVGESGSGKSvTALSILRLLPDPAAhpsGSILFDGQDLLGLserELRRIRgNRIAMIFQEP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 445 VlfaTS----------ITENIL----FGKEDAS------LDEVveaaKASNAHTFISQFPLgyktqvgergvQMSGGQKQ 504
Cdd:COG4172 102 M---TSlnplhtigkqIAEVLRlhrgLSGAAARaralelLERV----GIPDPERRLDAYPH-----------QLSGGQRQ 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 505 RIAIARAIIKSPKILLLDEATSALDseserV-VQ-ESLD-----NASIGRTTIVIAHRLSTIRN-ADVICVIHNGQIVET 576
Cdd:COG4172 164 RVMIAMALANEPDLLIADEPTTALD-----VtVQaQILDllkdlQRELGMALLLITHDLGVVRRfADRVAVMRQGEIVEQ 238
|
....*....
gi 15232977 577 GSHEELLKR 585
Cdd:COG4172 239 GPTAELFAA 247
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
995-1224 |
7.14e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 102.89 E-value: 7.14e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 995 ITFLNVDFAYPTRPDVVIFENFSIEIDEGKSTAIVGTSGSGKSTIIGLIERFYDPLKGTVKIDGRDIRSYHLRSLRKYIS 1074
Cdd:PRK13650 5 IEVKNLTFKYKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1075 LVSQEP-MLFAG-TIRENIMYGGTSDKIDESEIIEAAKAA----NAHDFITSlsngydtncgdKGVQLSGGQKQRIAIAR 1148
Cdd:PRK13650 85 MVFQNPdNQFVGaTVEDDVAFGLENKGIPHEEMKERVNEAlelvGMQDFKER-----------EPARLSGGQKQRVAIAG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1149 AVLKNPSVLLLDEATSALDSKSE----RVVQDALERvmVGRTSIMIAHRLSTIQNCDMIVVLGKGKIVESGTHSSLLEKG 1224
Cdd:PRK13650 154 AVAMRPKIIILDEATSMLDPEGRleliKTIKGIRDD--YQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPRELFSRG 231
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
359-577 |
1.01e-23 |
|
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: 100.43 E-value: 1.01e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 359 VEFNHVKFTYlsrPETTIFDDLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYDPIAGEILIDGVSIDKLQvnwlRSQMG 438
Cdd:cd03269 1 LEVENVTKRF---GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAA----RNRIG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 439 LVSQEPVLF-ATSITENILFGkedASLDEVVEAAKASNAHTFISQFPLG-YKTQVGErgvQMSGGQKQRIAIARAIIKSP 516
Cdd:cd03269 74 YLPEERGLYpKMKVIDQLVYL---AQLKGLKKEEARRRIDEWLERLELSeYANKRVE---ELSKGNQQKVQFIAAVIHDP 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15232977 517 KILLLDEATSALDSESERVVQESLDN-ASIGRTTIVIAHRLSTI-RNADVICVIHNGQIVETG 577
Cdd:cd03269 148 ELLILDEPFSGLDPVNVELLKDVIRElARAGKTVILSTHQMELVeELCDRVLLLNKGRAVLYG 210
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
694-929 |
1.02e-23 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen processing; This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350016 [Multi-domain] Cd Length: 289 Bit Score: 102.62 E-value: 1.02e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 694 GSVI-SVFFLTSHDQIKEKTRIYVLLFVGLAIFSFLvnisQHYGFAYMGEYLTKRIREQMLSKILTFEVNWFDidDNSSG 772
Cdd:cd18572 20 GAVIdAVVADGSREAFYRAVLLLLLLSVLSGLFSGL----RGGCFSYAGTRLVRRLRRDLFRSLLRQDIAFFD--ATKTG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 773 AICSRLAKD----ANVVRSMVGDRMSLLVQTISAVIIAciigLVIAWRLAIV-MISVQPLIVVC-FYTQRVllKSLSEKA 846
Cdd:cd18572 94 ELTSRLTSDcqkvSDPLSTNLNVFLRNLVQLVGGLAFM----FSLSWRLTLLaFITVPVIALITkVYGRYY--RKLSKEI 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 847 SKAQDESSKLAAEAVSNIRTITAFSSQERIIKLLKKVQEGPRRESVHRSWLAGIVLGTSRSLITCTSALNFWYGGRLIAD 926
Cdd:cd18572 168 QDALAEANQVAEEALSNIRTVRSFATEEREARRYERALDKALKLSVRQALAYAGYVAVNTLLQNGTQVLVLFYGGHLVLS 247
|
...
gi 15232977 927 GKI 929
Cdd:cd18572 248 GRM 250
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
993-1211 |
1.06e-23 |
|
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: 102.24 E-value: 1.06e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 993 GQITFLNVDFAYpTRPDVVIFENFSIEIDEGKSTAIVGTSGSGKSTIIGLIERFYDpLKGTVKIDGRDIRSYHLRSLRKY 1072
Cdd:cd03289 1 GQMTVKDLTAKY-TEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQKWRKA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1073 ISLVSQEPMLFAGTIRENI-MYGGTSDKidesEIIEAAKAANAHDFITSLSNGYDTNCGDKGVQLSGGQKQRIAIARAVL 1151
Cdd:cd03289 79 FGVIPQKVFIFSGTFRKNLdPYGKWSDE----EIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1152 KNPSVLLLDEATSALDSKSERVVQDALERVMVGRTSIMIAHRLSTIQNCDMIVVLGKGKI 1211
Cdd:cd03289 155 SKAKILLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKV 214
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
374-583 |
1.13e-23 |
|
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: 102.24 E-value: 1.13e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 374 TTIFDDLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYDpIAGEILIDGVSIDKLQVNWLRSQMGLVSQEPVLFATSITE 453
Cdd:cd03289 17 NAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQKWRKAFGVIPQKVFIFSGTFRK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 454 NI-LFGKEdaSLDEVVEAAKASNAHTFISQFPLGYKTQVGERGVQMSGGQKQRIAIARAIIKSPKILLLDEATSALDSES 532
Cdd:cd03289 96 NLdPYGKW--SDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPIT 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 15232977 533 ERVVQESLDNASIGRTTIVIAHRLSTIRNADVICVIHNGQIVETGSHEELL 583
Cdd:cd03289 174 YQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLL 224
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
359-582 |
1.13e-23 |
|
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: 100.66 E-value: 1.13e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 359 VEFNHVKFTYlSRPETTIFDDLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYDPIAGEILIDGVSIDKlQVNWLRSQMG 438
Cdd:cd03263 1 LQIRNLTKTY-KKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT-DRKAARQSLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 439 LVSQEPVLFAT-SITENILF-----GKEDASLDEVVEAakasnahtFISQFPLGYK--TQVGergvQMSGGQKQRIAIAR 510
Cdd:cd03263 79 YCPQFDALFDElTVREHLRFyarlkGLPKSEIKEEVEL--------LLRVLGLTDKanKRAR----TLSGGMKRKLSLAI 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15232977 511 AIIKSPKILLLDEATSALDSESERVVQESLDNASIGRTTIVIAHRLSTIRN-ADVICVIHNGQIVETGSHEEL 582
Cdd:cd03263 147 ALIGGPSVLLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAEAlCDRIAIMSDGKLRCIGSPQEL 219
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
1016-1215 |
1.15e-23 |
|
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: 100.26 E-value: 1.15e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1016 FSIEIDEGKSTAIVGTSGSGKSTIIGLIERFYDPLKGTVKIDGRDIRsyHLRSLRKYISLVSQEPMLFAG-TIRENIMYG 1094
Cdd:cd03298 17 FDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVT--AAPPADRPVSMLFQENNLFAHlTVEQNVGLG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1095 GTSDKIDESEIIEAAKAANAHDFItslsNGYDTNCGDkgvQLSGGQKQRIAIARAVLKNPSVLLLDEATSALDSKSERVV 1174
Cdd:cd03298 95 LSPGLKLTAEDRQAIEVALARVGL----AGLEKRLPG---ELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEM 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 15232977 1175 QDALERV--MVGRTSIMIAHRLSTIQNC-DMIVVLGKGKIVESG 1215
Cdd:cd03298 168 LDLVLDLhaETKMTVLMVTHQPEDAKRLaQRVVFLDNGRIAAQG 211
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
1008-1209 |
1.21e-23 |
|
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: 100.48 E-value: 1.21e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1008 PDVVIFENFSIEIDEGKSTAIVGTSGSGKSTIIGLIERFYDPLKGTV----KIDGRDIRSYHLRSLRKYISLVSQEPMLF 1083
Cdd:cd03290 12 SGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhwsnKNESEPSFEATRSRNRYSVAYAAQKPWLL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1084 AGTIRENIMYGGTSDKIDESEIIEAAKAANAHDFitsLSNGYDTNCGDKGVQLSGGQKQRIAIARAVLKNPSVLLLDEAT 1163
Cdd:cd03290 92 NATVEENITFGSPFNKQRYKAVTDACSLQPDIDL---LPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPF 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 15232977 1164 SALDSK-SERVVQDALERVMVG--RTSIMIAHRLSTIQNCDMIVVLGKG 1209
Cdd:cd03290 169 SALDIHlSDHLMQEGILKFLQDdkRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
995-1225 |
1.32e-23 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 108.67 E-value: 1.32e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 995 ITFLNVDFAYPTRPDVVIFENFSIEIDEGKSTAIVGTSGSGKSTIIGLIERFYDPLKGTVKIdgrdirsyhlrsLRKYIS 1074
Cdd:PLN03130 615 ISIKNGYFSWDSKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDASVV------------IRGTVA 682
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1075 LVSQEPMLFAGTIRENIMYGGTSDKIDESEIIEAAkaANAHDfITSLSNGYDTNCGDKGVQLSGGQKQRIAIARAVLKNP 1154
Cdd:PLN03130 683 YVPQVSWIFNATVRDNILFGSPFDPERYERAIDVT--ALQHD-LDLLPGGDLTEIGERGVNISGGQKQRVSMARAVYSNS 759
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15232977 1155 SVLLLDEATSALDSKSERVVQDA-LERVMVGRTSIMIAHRLSTIQNCDMIVVLGKGKIVESGTHSSLLEKGP 1225
Cdd:PLN03130 760 DVYIFDDPLSALDAHVGRQVFDKcIKDELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEELSNNGP 831
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
994-1232 |
1.36e-23 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 101.63 E-value: 1.36e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 994 QITFLNVDFAYPTRPdvvIFENFSIEIDEGKSTAIVGTSGSGKSTIIGLIERFYDPLKGTVKIDGRDIRSYHLRSLRKYI 1073
Cdd:PRK11231 2 TLRTENLTVGYGTKR---ILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1074 SLVSQEPMLFAG-TIRENIMYG-----------GTSDKidesEIIEAAKAANAhdfITSLSngydtncgDKGV-QLSGGQ 1140
Cdd:PRK11231 79 ALLPQHHLTPEGiTVRELVAYGrspwlslwgrlSAEDN----ARVNQAMEQTR---INHLA--------DRRLtDLSGGQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1141 KQRIAIARAVLKNPSVLLLDEATSALDSkSERVVQDALERVM--VGRTSIMIAHRLS-TIQNCDMIVVLGKGKIVESGTH 1217
Cdd:PRK11231 144 RQRAFLAMVLAQDTPVVLLDEPTTYLDI-NHQVELMRLMRELntQGKTVVTVLHDLNqASRYCDHLVVLANGHVMAQGTP 222
|
250
....*....|....*
gi 15232977 1218 SSLLEKGPTGTYFSL 1232
Cdd:PRK11231 223 EEVMTPGLLRTVFDV 237
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
358-580 |
1.57e-23 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 100.86 E-value: 1.57e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 358 EVEFNHVKFTYLSRPettIFDDLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYDPIAGEILIDGVSID---KL---QVN 431
Cdd:COG4161 2 SIQLKNINCFYGSHQ---ALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFDfsqKPsekAIR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 432 WLRSQMGLVSQE----PVLfatSITENIL--------FGKEDAsLDEVVEAAKASNAHTFISQFPLgyktqvgergvQMS 499
Cdd:COG4161 79 LLRQKVGMVFQQynlwPHL---TVMENLIeapckvlgLSKEQA-REKAMKLLARLRLTDKADRFPL-----------HLS 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 500 GGQKQRIAIARAIIKSPKILLLDEATSALDSE-SERVVQESLDNASIGRTTIVIAHRLSTIRN-ADVICVIHNGQIVETG 577
Cdd:COG4161 144 GGQQQRVAIARALMMEPQVLLFDEPTAALDPEiTAQVVEIIRELSQTGITQVIVTHEVEFARKvASQVVYMEKGRIIEQG 223
|
...
gi 15232977 578 SHE 580
Cdd:COG4161 224 DAS 226
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
359-584 |
1.78e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 102.21 E-value: 1.78e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 359 VEFNHVKFTYlsRPETTI----FDDLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYDPIAGEILIDGVSIDKLQVNW-- 432
Cdd:PRK13641 3 IKFENVDYIY--SPGTPMekkgLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNKnl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 433 --LRSQMGLVSQ--EPVLFATSITENILFGKED--ASLDEVVEAAKasnahTFISQfpLGYKTQVGERG-VQMSGGQKQR 505
Cdd:PRK13641 81 kkLRKKVSLVFQfpEAQLFENTVLKDVEFGPKNfgFSEDEAKEKAL-----KWLKK--VGLSEDLISKSpFELSGGQMRR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 506 IAIARAIIKSPKILLLDEATSALDSES-ERVVQESLDNASIGRTTIVIAHRLSTIRN-ADVICVIHNGQIVETGSHEELL 583
Cdd:PRK13641 154 VAIAGVMAYEPEILCLDEPAAGLDPEGrKEMMQLFKDYQKAGHTVILVTHNMDDVAEyADDVLVLEHGKLIKHASPKEIF 233
|
.
gi 15232977 584 K 584
Cdd:PRK13641 234 S 234
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
93-290 |
2.03e-23 |
|
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 350020 [Multi-domain] Cd Length: 289 Bit Score: 101.79 E-value: 2.03e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 93 VICFLEGYCWTRTGERQAARMREKYLRAVLRQDVGYFdlHVTSTSDVITSISSDSLVIQDFLSEKLPNFLMNASAFVASY 172
Cdd:cd18576 51 VFSFFRIYLFARVGERVVADLRKDLYRHLQRLPLSFF--HERRVGELTSRLSNDVTQIQDTLTTTLAEFLRQILTLIGGV 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 173 IVSFILMWRLTIV---GFPFIILLLVpglMYGRALVSISRKIHEQYNEAGSIAEQAISSVRTVYAFGSENKMIGKFSTAL 249
Cdd:cd18576 129 VLLFFISWKLTLLmlaTVPVVVLVAV---LFGRRIRKLSKKVQDELAEANTIVEETLQGIRVVKAFTREDYEIERYRKAL 205
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 15232977 250 RGSVKLGLRQGLAKG------ITIGSNGVthaiwAFLTWYGSRLVMN 290
Cdd:cd18576 206 ERVVKLALKRARIRAlfssfiIFLLFGAI-----VAVLWYGGRLVLA 247
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
998-1216 |
2.78e-23 |
|
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: 105.54 E-value: 2.78e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 998 LNVDFAYP------TRPDVVIFENFSIEIDEGKSTAIVGTSGSGKST----IIGLIerfydPLKGTVKIDGRDIRSYH-- 1065
Cdd:COG4172 281 LKVWFPIKrglfrrTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTlglaLLRLI-----PSEGEIRFDGQDLDGLSrr 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1066 -LRSLRKYISLVSQEPmlFAG-----TIRENIMYG------GTSDKIDESEIIEA-------AKAAN--AHDFitslsng 1124
Cdd:COG4172 356 aLRPLRRRMQVVFQDP--FGSlsprmTVGQIIAEGlrvhgpGLSAAERRARVAEAleevgldPAARHryPHEF------- 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1125 ydtncgdkgvqlSGGQKQRIAIARAVLKNPSVLLLDEATSALDskseRVVQ----DAL-----ERvmvGRTSIMIAHRLS 1195
Cdd:COG4172 427 ------------SGGQRQRIAIARALILEPKLLVLDEPTSALD----VSVQaqilDLLrdlqrEH---GLAYLFISHDLA 487
|
250 260
....*....|....*....|..
gi 15232977 1196 TIQN-CDMIVVLGKGKIVESGT 1216
Cdd:COG4172 488 VVRAlAHRVMVMKDGKVVEQGP 509
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
378-592 |
3.12e-23 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 103.38 E-value: 3.12e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 378 DDLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYDPIAGEILIDGVsiDKLQVNWLRSQMGLVSQEPVLFA-TSITENIL 456
Cdd:PRK11607 36 DDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGV--DLSHVPPYQRPINMMFQSYALFPhMTVEQNIA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 457 FGKEDaslDEVVEAAKASNAHTFISqfpLGYKTQVGERGV-QMSGGQKQRIAIARAIIKSPKILLLDEATSALDSE-SER 534
Cdd:PRK11607 114 FGLKQ---DKLPKAEIASRVNEMLG---LVHMQEFAKRKPhQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKlRDR 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 535 VVQESLDNAS-IGRTTIVIAH-RLSTIRNADVICVIHNGQIVETGSHEELLKRIDGQYTS 592
Cdd:PRK11607 188 MQLEVVDILErVGVTCVMVTHdQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSA 247
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
383-594 |
3.51e-23 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 107.56 E-value: 3.51e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 383 KIPAGKTVALVGGSGSGKSTVISLLQRFYDPIAGEILIDGVSIDKLQVNWLRSQMGLVSQEPVLFATSITENILFGKEdA 462
Cdd:PTZ00243 1332 RIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFSMIPQDPVLFDGTVRQNVDPFLE-A 1410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 463 SLDEVVEAAKASNAHTFISQFPLGYKTQVGERGVQMSGGQKQRIAIARAIIK-SPKILLLDEATSALDSESERVVQESLD 541
Cdd:PTZ00243 1411 SSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLKkGSGFILMDEATANIDPALDRQIQATVM 1490
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15232977 542 NASIGRTTIVIAHRLSTIRNADVICVIHNGQIVETGSHEELLKRIDGQYTSLV 594
Cdd:PTZ00243 1491 SAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELVMNRQSIFHSMV 1543
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
994-1212 |
3.68e-23 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 100.55 E-value: 3.68e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 994 QITFLNVDFAYPTRPDVVIFENFSIEIDEGKSTAIVGTSGSGKSTIIGLIERFYDPLKGTVKIDGRDI--RSYHLRSlrK 1071
Cdd:COG1101 3 ELKNLSKTFNPGTVNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVtkLPEYKRA--K 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1072 YISLVSQEPMlfAGT-----IRENIM------------YGGTSDKIDEseiieaakaanAHDFITSLSNGYDTNCGDKGV 1134
Cdd:COG1101 81 YIGRVFQDPM--MGTapsmtIEENLAlayrrgkrrglrRGLTKKRREL-----------FRELLATLGLGLENRLDTKVG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1135 QLSGGQKQRIAIARAVLKNPSVLLLDEATSALDSKSERVVQDALERVmVGR---TSIMIAHRLS-TIQNCDMIVVLGKGK 1210
Cdd:COG1101 148 LLSGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKI-VEEnnlTTLMVTHNMEqALDYGNRLIMMHEGR 226
|
..
gi 15232977 1211 IV 1212
Cdd:COG1101 227 II 228
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1009-1206 |
4.45e-23 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 99.02 E-value: 4.45e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1009 DVVIFENFSIEIDEGKSTAIVGTSGSGKSTIIGLIERFYDPLKGTVKIDGRDIRSYHLRSLRKYISLVSQEPMLFAGTIR 1088
Cdd:PRK10247 19 DAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQTPTLFGDTVY 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1089 ENIMYggtSDKIDESEIIEAAKAANAHDFitslsnGYDTNCGDKGV-QLSGGQKQRIAIARAVLKNPSVLLLDEATSALD 1167
Cdd:PRK10247 99 DNLIF---PWQIRNQQPDPAIFLDDLERF------ALPDTILTKNIaELSGGEKQRISLIRNLQFMPKVLLLDEITSALD 169
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 15232977 1168 SKSERVVQDALERVMV--GRTSIMIAHRLSTIQNCDMIVVL 1206
Cdd:PRK10247 170 ESNKHNVNEIIHRYVReqNIAVLWVTHDKDEINHADKVITL 210
|
|
| ABC_6TM_ABCB9_like |
cd18784 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ... |
74-319 |
4.51e-23 |
|
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and similar proteins; ATP-binding cassette sub-family B member 9 is also known as transporter associated with antigen processing, TAP-like protein, TAPL, and ABCB9. It is a half transporter comprises a homodimeric lysosomal peptide transport complex. It belongs to the ABC_6TM_TAP_ABCB8_10_like subgroup of the ABC_6TM exporter family. The ABC_6TM exporter family represents the six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in the ABC_6TM exporter family. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs. The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting chemical diversity of the translocated substrates, whereas NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional unit.
Pssm-ID: 350057 [Multi-domain] Cd Length: 289 Bit Score: 100.85 E-value: 4.51e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 74 MQTISKNVVALLYVACGSWVICFLEGYCWTRTGERQAARMREKYLRAVLRQDVGYFDlhVTSTSDVITSISSDSLVIQDF 153
Cdd:cd18784 32 QDKFSRAIIIMGLLAIASSVAAGIRGGLFTLAMARLNIRIRNLLFRSIVSQEIGFFD--TVKTGDITSRLTSDTTTMSDT 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 154 LSEKLPNFLMNASAFVASYIVSFILMWRLTIV---GFPFIILLlvpGLMYGRALVSISRKIHEQYNEAGSIAEQAISSVR 230
Cdd:cd18784 110 VSLNLNIFLRSLVKAIGVIVFMFKLSWQLSLVtliGLPLIAIV---SKVYGDYYKKLSKAVQDSLAKANEVAEETISSIR 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 231 TVYAFGSENKMIGKFSTALRGSVKLGLRQGLAKGITIGSNGVTHAIWAFLT-WYGSRLVMNHGSKGGTvfvVISCITYgG 309
Cdd:cd18784 187 TVRSFANEDGEANRYSEKLKDTYKLKIKEALAYGGYVWSNELTELALTVSTlYYGGHLVITGQISGGN---LISFILY-Q 262
|
250
....*....|
gi 15232977 310 VSLGQSLSNL 319
Cdd:cd18784 263 LELGSCLESV 272
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
386-595 |
4.75e-23 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 101.58 E-value: 4.75e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 386 AGKTVALVGGSGSGKSTVISLLQRFYDPIAGEILIDGVSI---DKLQVNWLRSQMGLVSQEPvlFAT--------SITEN 454
Cdd:PRK11308 40 RGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLlkaDPEAQKLLRQKIQIVFQNP--YGSlnprkkvgQILEE 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 455 ILFGKEDASLDEVVEAAKASNAHtfisqfpLGYKTQVGERGVQM-SGGQKQRIAIARAIIKSPKILLLDEATSALD-SES 532
Cdd:PRK11308 118 PLLINTSLSAAERREKALAMMAK-------VGLRPEHYDRYPHMfSGGQRQRIAIARALMLDPDVVVADEPVSALDvSVQ 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15232977 533 ERVVQESLD-NASIGRTTIVIAHRLSTIRN-ADVICVIHNGQIVETGSHEELLKRIDGQYT-SLVS 595
Cdd:PRK11308 191 AQVLNLMMDlQQELGLSYVFISHDLSVVEHiADEVMVMYLGRCVEKGTKEQIFNNPRHPYTqALLS 256
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
359-577 |
4.76e-23 |
|
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: 98.72 E-value: 4.76e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 359 VEFNHVKFTYLSRPETtiFDdlcLKIPAGKTVALVGGSGSGKSTVISLLQRFYDPIAGEILIDGVSIDKLQVNwlRSQMG 438
Cdd:cd03298 1 VRLDKIRFSYGEQPMH--FD---LTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPA--DRPVS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 439 LVSQEPVLFA-TSITENILFGKEDA-SLDEV-VEAAKASNAHTFISQFPLgyktqvgERGVQMSGGQKQRIAIARAIIKS 515
Cdd:cd03298 74 MLFQENNLFAhLTVEQNVGLGLSPGlKLTAEdRQAIEVALARVGLAGLEK-------RLPGELSGGERQRVALARVLVRD 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15232977 516 PKILLLDEATSALD----SESERVVQESldNASIGRTTIVIAHRLSTIRN-ADVICVIHNGQIVETG 577
Cdd:cd03298 147 KPVLLLDEPFAALDpalrAEMLDLVLDL--HAETKMTVLMVTHQPEDAKRlAQRVVFLDNGRIAAQG 211
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
359-583 |
4.92e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 100.11 E-value: 4.92e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 359 VEFNHVKFTYLSRpetTIFDDLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYDpIAGEILIDG--------VSIDKLQV 430
Cdd:PRK14258 8 IKVNNLSFYYDTQ---KILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNE-LESEVRVEGrveffnqnIYERRVNL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 431 NWLRSQMGLVSQEPVLFATSITENILFG------KEDASLDEVVEAA-KASNAHTFIsqfplgyKTQVGERGVQMSGGQK 503
Cdd:PRK14258 84 NRLRRQVSMVHPKPNLFPMSVYDNVAYGvkivgwRPKLEIDDIVESAlKDADLWDEI-------KHKIHKSALDLSGGQQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 504 QRIAIARAIIKSPKILLLDEATSALDSESERVVQESLDNASIGR--TTIVIAHRLSTI-RNADVICVIHN-----GQIVE 575
Cdd:PRK14258 157 QRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSelTMVIVSHNLHQVsRLSDFTAFFKGnenriGQLVE 236
|
....*...
gi 15232977 576 TGSHEELL 583
Cdd:PRK14258 237 FGLTKKIF 244
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
374-581 |
4.97e-23 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 102.72 E-value: 4.97e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 374 TTIFDDLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYDPIAGEILIDGVSIDKL-----QVNwlrsqmgLVSQEPVLFA 448
Cdd:PRK09452 27 KEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVpaenrHVN-------TVFQSYALFP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 449 -TSITENILFG--------KEDASldEVVEAAKASNAHTFISQFPLgyktqvgergvQMSGGQKQRIAIARAIIKSPKIL 519
Cdd:PRK09452 100 hMTVFENVAFGlrmqktpaAEITP--RVMEALRMVQLEEFAQRKPH-----------QLSGGQQQRVAIARAVVNKPKVL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15232977 520 LLDEATSALDSESERVVQESLD--NASIGRTTIVIAH-RLSTIRNADVICVIHNGQIVETGSHEE 581
Cdd:PRK09452 167 LLDESLSALDYKLRKQMQNELKalQRKLGITFVFVTHdQEEALTMSDRIVVMRDGRIEQDGTPRE 231
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
355-583 |
7.01e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 100.17 E-value: 7.01e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 355 MKGEVEFNHVKFTYLSRPETTIFDDLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYDPIAGEILIDGVSIDKLQVNWLR 434
Cdd:PRK13642 1 MNKILEVENLVFKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 435 SQMGLVSQEP--VLFATSITENILFGKEDAS------LDEVVEAAKASNAHTFISQFPlgyktqvgergVQMSGGQKQRI 506
Cdd:PRK13642 81 RKIGMVFQNPdnQFVGATVEDDVAFGMENQGipreemIKRVDEALLAVNMLDFKTREP-----------ARLSGGQKQRV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 507 AIARAIIKSPKILLLDEATSALD----SESERVVQESLDNASIgrTTIVIAHRLSTIRNADVICVIHNGQIVETGSHEEL 582
Cdd:PRK13642 150 AVAGIIALRPEIIILDESTSMLDptgrQEIMRVIHEIKEKYQL--TVLSITHDLDEAASSDRILVMKAGEIIKEAAPSEL 227
|
.
gi 15232977 583 L 583
Cdd:PRK13642 228 F 228
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
355-586 |
7.57e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 100.16 E-value: 7.57e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 355 MKGEVEFNHVKFTYLSRPETT---IFDDLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYDPIAGEILIDGVSIDKLQVN 431
Cdd:PRK13633 1 MNEMIKCKNVSYKYESNEESTeklALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 432 W-LRSQMGLVSQEP--VLFATSITENILFGKEDASLD------EVVEAAKASNAHTFISQFPLgyktqvgergvQMSGGQ 502
Cdd:PRK13633 81 WdIRNKAGMVFQNPdnQIVATIVEEDVAFGPENLGIPpeeireRVDESLKKVGMYEYRRHAPH-----------LLSGGQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 503 KQRIAIARAIIKSPKILLLDEATSALDSESERVVQESLD--NASIGRTTIVIAHRLSTIRNADVICVIHNGQIVETGSHE 580
Cdd:PRK13633 150 KQRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKelNKKYGITIILITHYMEEAVEADRIIVMDSGKVVMEGTPK 229
|
....*.
gi 15232977 581 ELLKRI 586
Cdd:PRK13633 230 EIFKEV 235
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
382-587 |
7.88e-23 |
|
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: 101.72 E-value: 7.88e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 382 LKIPAGKTVALVGGSGSGKSTVISL---LQRfydPIAGEILIDG-VSIDKLQVNWL---RSQMGLVSQEPVLFAT-SITE 453
Cdd:COG4148 20 FTLPGRGVTALFGPSGSGKTTLLRAiagLER---PDSGRIRLGGeVLQDSARGIFLpphRRRIGYVFQEARLFPHlSVRG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 454 NILFG-------KEDASLDEVVEAakasnahtfisqfpLGyktqVG---ERGV-QMSGGQKQRIAIARAIIKSPKILLLD 522
Cdd:COG4148 97 NLLYGrkrapraERRISFDEVVEL--------------LG----IGhllDRRPaTLSGGERQRVAIGRALLSSPRLLLMD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 523 EATSALDSES--------ERVVQE----------SLDNASigrttiviahRLstirnADVICVIHNGQIVETGSHEELLK 584
Cdd:COG4148 159 EPLAALDLARkaeilpylERLRDEldipilyvshSLDEVA----------RL-----ADHVVLLEQGRVVASGPLAEVLS 223
|
...
gi 15232977 585 RID 587
Cdd:COG4148 224 RPD 226
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1017-1215 |
9.29e-23 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 103.56 E-value: 9.29e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1017 SIEIDEGKSTAIVGTSGSGKSTIIGLIERFYDPLKGTVKIDGR--DIRSYHlRSLRKYISLVSQEPMLFAG-TIRENIMY 1093
Cdd:COG1129 24 SLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEpvRFRSPR-DAQAAGIAIIHQELNLVPNlSVAENIFL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1094 G---GTSDKIDESEIIEAAKAAnahdfITSLsnGYDTNCGDKGVQLSGGQKQRIAIARAVLKNPSVLLLDEATSALDSK- 1169
Cdd:COG1129 103 GrepRRGGLIDWRAMRRRAREL-----LARL--GLDIDPDTPVGDLSVAQQQLVEIARALSRDARVLILDEPTASLTERe 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15232977 1170 SER---VVQDALERvmvGRTSIMIAHRLSTIQN-CDMIVVLGKGKIVESG 1215
Cdd:COG1129 176 VERlfrIIRRLKAQ---GVAIIYISHRLDEVFEiADRVTVLRDGRLVGTG 222
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
1017-1229 |
9.56e-23 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 102.42 E-value: 9.56e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1017 SIEIDEGKSTAIVGTSGSGKSTIIGLIERFYDPLKGTVKIDGRD---IRSYHLRSL-RKYISLVSQEPMLFAG-TIRENI 1091
Cdd:PRK10070 48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDiakISDAELREVrRKKIAMVFQSFALMPHmTVLDNT 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1092 MYGGTSDKIDESEIIEAAKAANAHDFITSLSNGYDTncgdkgvQLSGGQKQRIAIARAVLKNPSVLLLDEATSALDSKSE 1171
Cdd:PRK10070 128 AFGMELAGINAEERREKALDALRQVGLENYAHSYPD-------ELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIR 200
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15232977 1172 RVVQDALERVMVG--RTSIMIAHRL-STIQNCDMIVVLGKGKIVESGTHSSLLEKgPTGTY 1229
Cdd:PRK10070 201 TEMQDELVKLQAKhqRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEILNN-PANDY 260
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
369-529 |
1.04e-22 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 97.55 E-value: 1.04e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 369 LSRPETTIFDDLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYDP---IAGEILIDGVSIDKLQVnwLRSQMGLVSQEPV 445
Cdd:COG4136 9 ITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLTALPA--EQRRIGILFQDDL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 446 LFA-TSITENILFG-----KEDASLDEVVEAAKASNAHTFISQFPlgyktqvgergVQMSGGQKQRIAIARAIIKSPKIL 519
Cdd:COG4136 87 LFPhLSVGENLAFAlpptiGRAQRRARVEQALEEAGLAGFADRDP-----------ATLSGGQRARVALLRALLAEPRAL 155
|
170
....*....|
gi 15232977 520 LLDEATSALD 529
Cdd:COG4136 156 LLDEPFSKLD 165
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
995-1224 |
1.15e-22 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 105.83 E-value: 1.15e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 995 ITFLNVDFAYPTRPDVVIFENFSIEIDEGKSTAIVGTSGSGKSTIIGLIERFYDPLKGTVKIdgrdirsyhlrsLRKYIS 1074
Cdd:PLN03232 615 ISIKNGYFSWDSKTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAETSSVV------------IRGSVA 682
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1075 LVSQEPMLFAGTIRENIMYGGTSDKIDESEIIEAAkaANAHDFitSLSNGYD-TNCGDKGVQLSGGQKQRIAIARAVLKN 1153
Cdd:PLN03232 683 YVPQVSWIFNATVRENILFGSDFESERYWRAIDVT--ALQHDL--DLLPGRDlTEIGERGVNISGGQKQRVSMARAVYSN 758
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15232977 1154 PSVLLLDEATSALDSKSERVVQDA-LERVMVGRTSIMIAHRLSTIQNCDMIVVLGKGKIVESGTHSSLLEKG 1224
Cdd:PLN03232 759 SDIYIFDDPLSALDAHVAHQVFDScMKDELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAELSKSG 830
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
375-583 |
1.15e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 99.40 E-value: 1.15e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 375 TIFDDLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYDPIAG-----EILIDGVSI-DKLQVNWLRSQMGLVSQEPVLFA 448
Cdd:PRK14271 35 TVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIfNYRDVLEFRRRVGMLFQRPNPFP 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 449 TSITENILFGKEDASLDEVVEAAKASNAHTFISQFPLGYKTQVGERGVQMSGGQKQRIAIARAIIKSPKILLLDEATSAL 528
Cdd:PRK14271 115 MSIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSAL 194
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 15232977 529 DSESERVVQESLDNASIGRTTIVIAHRLS-TIRNADVICVIHNGQIVETGSHEELL 583
Cdd:PRK14271 195 DPTTTEKIEEFIRSLADRLTVIIVTHNLAqAARISDRAALFFDGRLVEEGPTEQLF 250
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
359-580 |
1.20e-22 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 98.55 E-value: 1.20e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 359 VEFNHVKFTYLSrpeTTIFDDLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYDPIAGEILIDG------VSIDKLQVNW 432
Cdd:PRK11124 3 IQLNGINCFYGA---HQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGnhfdfsKTPSDKAIRE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 433 LRSQMGLVSQEPVLFA-TSITENIL--------FGKEDA--SLDEVVEAAKASNahtFISQFPLgyktqvgergvQMSGG 501
Cdd:PRK11124 80 LRRNVGMVFQQYNLWPhLTVQQNLIeapcrvlgLSKDQAlaRAEKLLERLRLKP---YADRFPL-----------HLSGG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 502 QKQRIAIARAIIKSPKILLLDEATSALDSE-SERVVQESLDNASIGRTTIVIAHRLSTIRN-ADVICVIHNGQIVETGSH 579
Cdd:PRK11124 146 QQQRVAIARALMMEPQVLLFDEPTAALDPEiTAQIVSIIRELAETGITQVIVTHEVEVARKtASRVVYMENGHIVEQGDA 225
|
.
gi 15232977 580 E 580
Cdd:PRK11124 226 S 226
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1008-1212 |
1.32e-22 |
|
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: 95.57 E-value: 1.32e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1008 PDVVIFENFSIEIDEGKSTAIVGTSGSGKSTIIGLIERFYDPLKGTVKIDGRDIRSYHLR-SLRKYISLVSQepmlfagt 1086
Cdd:cd03216 11 GGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRdARRAGIAMVYQ-------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1087 irenimyggtsdkideseiieaakaanahdfitslsngydtncgdkgvqLSGGQKQRIAIARAVLKNPSVLLLDEATSAL 1166
Cdd:cd03216 83 -------------------------------------------------LSVGERQMVEIARALARNARLLILDEPTAAL 113
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 15232977 1167 DSKSERVVQDALERVMV-GRTSIMIAHRLSTIQN-CDMIVVLGKGKIV 1212
Cdd:cd03216 114 TPAEVERLFKVIRRLRAqGVAVIFISHRLDEVFEiADRVTVLRDGRVV 161
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
677-935 |
1.78e-22 |
|
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; The bacterial lipid flippase MsbA is found in Gram-negative bacteria and transports lipid A and lipopolysaccharide (LPS) from the cytoplasmic leaflet to the periplasmic leaflet of the inner membrane. MsbA is also a polyspecific transporter capable of transporting a broad spectrum of drug molecules. Additionally, MsbA exhibits significant sequence similarity to mammalian multidrug resistance (MDR) proteins such as human MDR protein 1 (MDR1) and LmrA from Lactococcus lactis. This subgroup also contains a putative transporter Brevibacillus brevis TycD; the location of the tycD gene within the Tyc (tyrocidine) biosynthesis operon suggests that TycD may play a role in the secretion of the cyclic decapeptide antibiotic tyrocidine. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349996 [Multi-domain] Cd Length: 292 Bit Score: 99.03 E-value: 1.78e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 677 LSAALVGVLQPVSAYSAGSVIsvffltshDQIKEKTRIYVLLFVGLAIF-SFLV-NIS---QHYGFAYMGEYLTKRIREQ 751
Cdd:cd18552 6 LGMILVAATTAALAWLLKPLL--------DDIFVEKDLEALLLVPLAIIgLFLLrGLAsylQTYLMAYVGQRVVRDLRND 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 752 MLSKILTFEVNWFDidDNSSGAICSRLAKDANVVRSMVGDRMSLLVQTISAVIIACIIGLVIAWRLAIVMISVQPLIVVC 831
Cdd:cd18552 78 LFDKLLRLPLSFFD--RNSSGDLISRITNDVNQVQNALTSALTVLVRDPLTVIGLLGVLFYLDWKLTLIALVVLPLAALP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 832 FytqRVLLKSLSEKASKAQDESSKLAA---EAVSNIRTITAFSSQERIIKLLKKVQEGPRRESVHRSWLAGIVLGTSRSL 908
Cdd:cd18552 156 I---RRIGKRLRKISRRSQESMGDLTSvlqETLSGIRVVKAFGAEDYEIKRFRKANERLRRLSMKIARARALSSPLMELL 232
|
250 260
....*....|....*....|....*..
gi 15232977 909 ITCTSALNFWYGGRLIADGKIVSKAFF 935
Cdd:cd18552 233 GAIAIALVLWYGGYQVISGELTPGEFI 259
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
378-581 |
1.99e-22 |
|
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: 98.19 E-value: 1.99e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 378 DDLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYDPIAGEILIDGVSIDKLQVnWLRSQMGLVS--QEPVLFAT-SITEN 454
Cdd:COG0411 21 DDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPP-HRIARLGIARtfQNPRLFPElTVLEN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 455 ILFG---------------------KEDASLDEVVEAAKAsnahtfisqfpLGYKTQVGERGVQMSGGQKQRIAIARAII 513
Cdd:COG0411 100 VLVAaharlgrgllaallrlprarrEEREARERAEELLER-----------VGLADRADEPAGNLSYGQQRRLEIARALA 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15232977 514 KSPKILLLDEATSAL-DSESERVVQ--ESLdNASIGRTTIVIAHRLSTIRN-ADVICVIHNGQIVETGSHEE 581
Cdd:COG0411 169 TEPKLLLLDEPAAGLnPEETEELAEliRRL-RDERGITILLIEHDMDLVMGlADRIVVLDFGRVIAEGTPAE 239
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
359-577 |
2.17e-22 |
|
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: 96.52 E-value: 2.17e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 359 VEFNHVKFTYLSRpetTIFDDLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYDPIAGEILIDGVSIDKLQVNWlrSQMG 438
Cdd:cd03268 1 LKTNDLTKTYGKK---RVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEAL--RRIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 439 LVSQEPVLFAT-SITENI-----LFGKEDASLDEVVEAAKASN-AHTFISQFPLGyktqvgergvqMsggqKQRIAIARA 511
Cdd:cd03268 76 ALIEAPGFYPNlTARENLrllarLLGIRKKRIDEVLDVVGLKDsAKKKVKGFSLG-----------M----KQRLGIALA 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15232977 512 IIKSPKILLLDEATSALDSESERVVQESL-DNASIGRTTIVIAHRLSTIRN-ADVICVIHNGQIVETG 577
Cdd:cd03268 141 LLGNPDLLILDEPTNGLDPDGIKELRELIlSLRDQGITVLISSHLLSEIQKvADRIGIINKGKLIEEG 208
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
379-583 |
2.22e-22 |
|
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: 97.36 E-value: 2.22e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 379 DLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYDPIAGEILIDGVSIDKLQVnWLRSQMGL--VSQEPVLFAT-SITENI 455
Cdd:COG0410 21 GVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPP-HRIARLGIgyVPEGRRIFPSlTVEENL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 456 LFG--------KEDASLDEVVEAakasnahtfisqFPlgyktQVGER----GVQMSGGQKQRIAIARAIIKSPKILLLDE 523
Cdd:COG0410 100 LLGayarrdraEVRADLERVYEL------------FP-----RLKERrrqrAGTLSGGEQQMLAIGRALMSRPKLLLLDE 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15232977 524 ATSALdseSERVVQEsldnasIGR---------TTIVI----AHRLSTIrnADVICVIHNGQIVETGSHEELL 583
Cdd:COG0410 163 PSLGL---APLIVEE------IFEiirrlnregVTILLveqnARFALEI--ADRAYVLERGRIVLEGTAAELL 224
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
995-1221 |
2.25e-22 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 101.07 E-value: 2.25e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 995 ITFLNVDFAyptrpDVVIFENFSIEIDEGKSTAIVGTSGSGKSTIIGLIERFYDPLKGTVKIDGRDIRSYHLRSLRKYIS 1074
Cdd:PRK09536 6 VSDLSVEFG-----DTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1075 LVSQEPML-FAGTIRENIMYG--------GTSDKIDESEIIEAAKAANAHDFItslsngydtncgDKGV-QLSGGQKQRI 1144
Cdd:PRK09536 81 SVPQDTSLsFEFDVRQVVEMGrtphrsrfDTWTETDRAAVERAMERTGVAQFA------------DRPVtSLSGGERQRV 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15232977 1145 AIARAVLKNPSVLLLDEATSALD-SKSERVVQDALERVMVGRTSIMIAHRLS-TIQNCDMIVVLGKGKIVESGTHSSLL 1221
Cdd:PRK09536 149 LLARALAQATPVLLLDEPTASLDiNHQVRTLELVRRLVDDGKTAVAAIHDLDlAARYCDELVLLADGRVRAAGPPADVL 227
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
1015-1216 |
2.27e-22 |
|
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: 100.19 E-value: 2.27e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1015 NFSIEIDEGKS----TAIVGTSGSGKSTIIGLIERFYDPLKGTVKIDGRDIRS----YHLRSLRKYISLVSQEPMLFAG- 1085
Cdd:TIGR02142 11 DFSLDADFTLPgqgvTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDsrkgIFLPPEKRRIGYVFQEARLFPHl 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1086 TIRENIMYGGTSDKIDESEIIEAAkaanahdfITSLSnGYDTNCGDKGVQLSGGQKQRIAIARAVLKNPSVLLLDEATSA 1165
Cdd:TIGR02142 91 SVRGNLRYGMKRARPSERRISFER--------VIELL-GIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15232977 1166 LDSKSERVVQDALERVM--VGRTSIMIAHRLSTIQN-CDMIVVLGKGKIVESGT 1216
Cdd:TIGR02142 162 LDDPRKYEILPYLERLHaeFGIPILYVSHSLQEVLRlADRVVVLEDGRVAAAGP 215
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
995-1226 |
2.46e-22 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 97.47 E-value: 2.46e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 995 ITFLNVDFAYPtrpDVVIFENFSIEIDEGKSTAIVGTSGSGKSTIIGLIERFYDPLKGTVKIDGRDIRSYHL--RSLRKY 1072
Cdd:PRK09493 2 IEFKNVSKHFG---PTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVdeRLIRQE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1073 ISLVSQEPMLFAG-TIRENIMYGGTSdkideseiIEAAKAANAHDFITSL---------SNGYDTncgdkgvQLSGGQKQ 1142
Cdd:PRK09493 79 AGMVFQQFYLFPHlTALENVMFGPLR--------VRGASKEEAEKQARELlakvglaerAHHYPS-------ELSGGQQQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1143 RIAIARAVLKNPSVLLLDEATSALDS--KSE--RVVQDALERVMvgrTSIMIAHRLSTIQNC-DMIVVLGKGKIVESGTH 1217
Cdd:PRK09493 144 RVAIARALAVKPKLMLFDEPTSALDPelRHEvlKVMQDLAEEGM---TMVIVTHEIGFAEKVaSRLIFIDKGRIAEDGDP 220
|
....*....
gi 15232977 1218 SSLLEKGPT 1226
Cdd:PRK09493 221 QVLIKNPPS 229
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
349-582 |
2.56e-22 |
|
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: 98.39 E-value: 2.56e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 349 GQILERMKGEV-------EFNHVKFTYLSRPETTIFDDLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYDPIAGEILID 421
Cdd:cd03291 18 GELLEKAKQENndrkhssDDNNLFFSNLCLVGAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHS 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 422 GVSIDKLQVNWLrsqmglvsqepvlFATSITENILFGkedASLDEV--VEAAKASNAHTFISQFPLGYKTQVGERGVQMS 499
Cdd:cd03291 98 GRISFSSQFSWI-------------MPGTIKENIIFG---VSYDEYryKSVVKACQLEEDITKFPEKDNTVLGEGGITLS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 500 GGQKQRIAIARAIIKSPKILLLDEATSALDSESERVVQES-LDNASIGRTTIVIAHRLSTIRNADVICVIHNGQIVETGS 578
Cdd:cd03291 162 GGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEIFEScVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGT 241
|
....
gi 15232977 579 HEEL 582
Cdd:cd03291 242 FSEL 245
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
372-571 |
3.08e-22 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 96.63 E-value: 3.08e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 372 PETTIFDDLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYDPIAGEILIDGVSIDKLQVNWLRSQ----MGLVSQEPVLF 447
Cdd:cd03290 12 SGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRnrysVAYAAQKPWLL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 448 ATSITENILFGK--EDASLDEVVEAAkasNAHTFISQFPLGYKTQVGERGVQMSGGQKQRIAIARAIIKSPKILLLDEAT 525
Cdd:cd03290 92 NATVEENITFGSpfNKQRYKAVTDAC---SLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPF 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15232977 526 SALDSE-SERVVQESL-----DNAsigRTTIVIAHRLSTIRNADVICVIHNG 571
Cdd:cd03290 169 SALDIHlSDHLMQEGIlkflqDDK---RTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
1012-1213 |
3.22e-22 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 97.95 E-value: 3.22e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1012 IFENFSIEIDEGKSTAIVGTSGSGKSTIIGLIERFYDPLKGTVKIDGRDIrsYHL-----RSLRKYISLVSQE------P 1080
Cdd:TIGR02769 26 VLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDL--YQLdrkqrRAFRRDVQLVFQDspsavnP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1081 MLFAGTIRENIMYGGTSdkIDESEiiEAAKAANAHDFItslsnGYDTNCGDK-GVQLSGGQKQRIAIARAVLKNPSVLLL 1159
Cdd:TIGR02769 104 RMTVRQIIGEPLRHLTS--LDESE--QKARIAELLDMV-----GLRSEDADKlPRQLSGGQLQRINIARALAVKPKLIVL 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15232977 1160 DEATSALDSKSERVVQDALE--RVMVGRTSIMIAHRLSTIQN-CDMIVVLGKGKIVE 1213
Cdd:TIGR02769 175 DEAVSNLDMVLQAVILELLRklQQAFGTAYLFITHDLRLVQSfCQRVAVMDKGQIVE 231
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
360-570 |
4.05e-22 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 96.32 E-value: 4.05e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 360 EFNHVKFtylSRPETTIFDDLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYDPIAGEILIDGVSIDKLQVNWLRSQMGL 439
Cdd:PRK10247 9 QLQNVGY---LAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 440 VSQEPVLFATSITENILFG--------KEDASLDevveaakasnahtFISQFPLGyKTQVGERGVQMSGGQKQRIAIARA 511
Cdd:PRK10247 86 CAQTPTLFGDTVYDNLIFPwqirnqqpDPAIFLD-------------DLERFALP-DTILTKNIAELSGGEKQRISLIRN 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15232977 512 IIKSPKILLLDEATSALDSESERVVQEsldnasigrttivIAHRLSTIRNADVICVIHN 570
Cdd:PRK10247 152 LQFMPKVLLLDEITSALDESNKHNVNE-------------IIHRYVREQNIAVLWVTHD 197
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
375-583 |
4.75e-22 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 97.18 E-value: 4.75e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 375 TIFDDLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYDPIAGEILIDGVSIDKL---QVNWLRSQMGLVSQE-PVLFATS 450
Cdd:TIGR02769 25 PVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLdrkQRRAFRRDVQLVFQDsPSAVNPR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 451 ITENILFGKEDASLDEVVEAAKASNAHTFISQfpLGYKTQVGER-GVQMSGGQKQRIAIARAIIKSPKILLLDEATSALD 529
Cdd:TIGR02769 105 MTVRQIIGEPLRHLTSLDESEQKARIAELLDM--VGLRSEDADKlPRQLSGGQLQRINIARALAVKPKLIVLDEAVSNLD 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15232977 530 SESERVVQESLD--NASIGRTTIVIAHRLSTI-RNADVICVIHNGQIVETGSHEELL 583
Cdd:TIGR02769 183 MVLQAVILELLRklQQAFGTAYLFITHDLRLVqSFCQRVAVMDKGQIVEECDVAQLL 239
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
1010-1220 |
6.10e-22 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 99.02 E-value: 6.10e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1010 VVIfENFSIEIDEGKSTAIVGTSGSGKSTIIGLIERFYDPLKGTVKIDGRDI--RSYHLRSlrkyISLVSQEPMLFAG-T 1086
Cdd:PRK11432 20 TVI-DNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVthRSIQQRD----ICMVFQSYALFPHmS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1087 IRENIMYGGTSDKIDESEIIEAAKAANAhdfITSLSnGYdtncGDKGV-QLSGGQKQRIAIARAVLKNPSVLLLDEATSA 1165
Cdd:PRK11432 95 LGENVGYGLKMLGVPKEERKQRVKEALE---LVDLA-GF----EDRYVdQISGGQQQRVALARALILKPKVLLFDEPLSN 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15232977 1166 LDSKSERVVQDALERVM--VGRTSIMIAHRLS-TIQNCDMIVVLGKGKIVESGTHSSL 1220
Cdd:PRK11432 167 LDANLRRSMREKIRELQqqFNITSLYVTHDQSeAFAVSDTVIVMNKGKIMQIGSPQEL 224
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
359-587 |
8.83e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 96.74 E-value: 8.83e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 359 VEFNHVKFTYlsrPETTIFD-----DLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYDPIAGEILIDGVSIDKLQVN-- 431
Cdd:PRK13649 3 INLQNVSYTY---QAGTPFEgralfDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNkd 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 432 --WLRSQMGLVSQ--EPVLFATSITENILFGKED--ASLDEVVEAAKASNAHTFISQfplgyktQVGERG-VQMSGGQKQ 504
Cdd:PRK13649 80 ikQIRKKVGLVFQfpESQLFEETVLKDVAFGPQNfgVSQEEAEALAREKLALVGISE-------SLFEKNpFELSGGQMR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 505 RIAIARAIIKSPKILLLDEATSALDSESERVVQESLDNASIGRTTIV-IAHRLSTIRN-ADVICVIHNGQIVETGSHEEL 582
Cdd:PRK13649 153 RVAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVlVTHLMDDVANyADFVYVLEKGKLVLSGKPKDI 232
|
....*
gi 15232977 583 LKRID 587
Cdd:PRK13649 233 FQDVD 237
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
363-577 |
9.01e-22 |
|
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: 94.95 E-value: 9.01e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 363 HVKFTYlsrPETTIFDDLCLKIPAGKTvALVGGSGSGKSTVISLLQRFYDPIAGEILIDGVSIDKlQVNWLRSQMGLVSQ 442
Cdd:cd03264 5 NLTKRY---GKKRALDGVSLTLGPGMY-GLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLK-QPQKLRRRIGYLPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 443 EPVLFAtSIT-----------ENILFGKEDASLDEVVEAAKASN-AHTFISQFplgyktqvgergvqmSGGQKQRIAIAR 510
Cdd:cd03264 80 EFGVYP-NFTvrefldyiawlKGIPSKEVKARVDEVLELVNLGDrAKKKIGSL---------------SGGMRRRVGIAQ 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15232977 511 AIIKSPKILLLDEATSALDSESERVVQESLDNASIGRTTIVIAHRLSTIRN-ADVICVIHNGQIVETG 577
Cdd:cd03264 144 ALVGDPSILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESlCNQVAVLNKGKLVFEG 211
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1010-1213 |
9.61e-22 |
|
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: 95.58 E-value: 9.61e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1010 VVIFENFSIEIDEGKSTAIVGTSGSGKSTIIGLI---ERfydPLKGTVKIDGRDIRSY------HLRslRKYISLVSQEP 1080
Cdd:COG4181 25 LTILKGISLEVEAGESVAIVGASGSGKSTLLGLLaglDR---PTSGTVRLAGQDLFALdedaraRLR--ARHVGFVFQSF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1081 MLFAG-TIRENIM----YGGTSDkideseiieAAKAANA------------HdfitslsngYDTncgdkgvQLSGGQKQR 1143
Cdd:COG4181 100 QLLPTlTALENVMlpleLAGRRD---------ARARARAllervglghrldH---------YPA-------QLSGGEQQR 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15232977 1144 IAIARAVLKNPSVLLLDEATSALDSKSERVVQDALERVM--VGRTSIMIAHRLSTIQNCDMIVVLGKGKIVE 1213
Cdd:COG4181 155 VALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNreRGTTLVLVTHDPALAARCDRVLRLRAGRLVE 226
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
373-582 |
1.01e-21 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 95.28 E-value: 1.01e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 373 ETTIFDDLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYDPIAGEILIDGVSIDKLQVNWL-RSQMGLVSQEPVLFAT-S 450
Cdd:TIGR03410 12 QSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERaRAGIAYVPQGREIFPRlT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 451 ITENILFGkedasldevveAAKASNAHTFISQ-----FPLgYKTQVGERGVQMSGGQKQRIAIARAIIKSPKILLLDEAT 525
Cdd:TIGR03410 92 VEENLLTG-----------LAALPRRSRKIPDeiyelFPV-LKEMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDEPT 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15232977 526 SALD----SESERVVQESldNASIGRTTIVIAHRLSTIRN-ADVICVIHNGQIVETGSHEEL 582
Cdd:TIGR03410 160 EGIQpsiiKDIGRVIRRL--RAEGGMAILLVEQYLDFARElADRYYVMERGRVVASGAGDEL 219
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
677-927 |
1.04e-21 |
|
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar proteins; This group represents the six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA from Lactococcus lactis and similar proteins. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349995 [Multi-domain] Cd Length: 289 Bit Score: 96.73 E-value: 1.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 677 LSAALVGVLQPvsaYSAGSVISVFFLtshdqiKEKTRIYVLLFVGLAIFSFLVNISQHYGFAYMGEYLTKRIREQMLSKI 756
Cdd:cd18551 9 LLGTAASLAQP---LLVKNLIDALSA------GGSSGGLLALLVALFLLQAVLSALSSYLLGRTGERVVLDLRRRLWRRL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 757 LTFEVNWFdiDDNSSGAICSRLAKDANVVRSMVgdrMSLLVQTISAVII---ACIIGLVIAWRLAIVMISVQPLIVVCFY 833
Cdd:cd18551 80 LRLPVSFF--DRRRSGDLVSRVTNDTTLLRELI---TSGLPQLVTGVLTvvgAVVLMFLLDWVLTLVTLAVVPLAFLIIL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 834 tqrVLLKSLSEKASKAQDESSKLAA---EAVSNIRTITAFSSQERIIKLLKKVQEGPRRESVHRSWLAGIVLGTSRSLIT 910
Cdd:cd18551 155 ---PLGRRIRKASKRAQDALGELSAaleRALSAIRTVKASNAEERETKRGGEAAERLYRAGLKAAKIEALIGPLMGLAVQ 231
|
250
....*....|....*..
gi 15232977 911 CTSALNFWYGGRLIADG 927
Cdd:cd18551 232 LALLVVLGVGGARVASG 248
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
995-1223 |
1.10e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 96.73 E-value: 1.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 995 ITFLNVDFAY-PTRP--DVVIFEnFSIEIDEGKSTAIVGTSGSGKSTIIGLIERFYDPLKGTVKIDgrDI------RSYH 1065
Cdd:PRK13643 2 IKFEKVNYTYqPNSPfaSRALFD-IDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVG--DIvvsstsKQKE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1066 LRSLRKYISLVSQEP--MLFAGTIRENIMYGGTSDKIDESEiieAAKAANAHDFITSLSNGYdtnCGDKGVQLSGGQKQR 1143
Cdd:PRK13643 79 IKPVRKKVGVVFQFPesQLFEETVLKDVAFGPQNFGIPKEK---AEKIAAEKLEMVGLADEF---WEKSPFELSGGQMRR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1144 IAIARAVLKNPSVLLLDEATSALDSKSERVVQDALERV-MVGRTSIMIAHRLSTIQN-CDMIVVLGKGKIVESGTHSSLL 1221
Cdd:PRK13643 153 VAIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIhQSGQTVVLVTHLMDDVADyADYVYLLEKGHIISCGTPSDVF 232
|
..
gi 15232977 1222 EK 1223
Cdd:PRK13643 233 QE 234
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
373-583 |
1.50e-21 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 95.81 E-value: 1.50e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 373 ETTIFDDLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYDPIAGEILIDGVSI-------------DKLQVNWLRSQMGL 439
Cdd:PRK10619 17 EHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTInlvrdkdgqlkvaDKNQLRLLRTRLTM 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 440 VSQEPVLFA-TSITENILfgkeDASLdEVVEAAKA---SNAHTFISQFPLGYKTQvGERGVQMSGGQKQRIAIARAIIKS 515
Cdd:PRK10619 97 VFQHFNLWShMTVLENVM----EAPI-QVLGLSKQearERAVKYLAKVGIDERAQ-GKYPVHLSGGQQQRVSIARALAME 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15232977 516 PKILLLDEATSALD----SESERVVQESldnASIGRTTIVIAHRLSTIRN-ADVICVIHNGQIVETGSHEELL 583
Cdd:PRK10619 171 PEVLLFDEPTSALDpelvGEVLRIMQQL---AEEGKTMVVVTHEMGFARHvSSHVIFLHQGKIEEEGAPEQLF 240
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
378-577 |
1.57e-21 |
|
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: 94.36 E-value: 1.57e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 378 DDLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYDPIAGEILIDG--VSIDKLQVnwlRSQMGLVSQEPVLFA-TSITEN 454
Cdd:cd03266 22 DGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGfdVVKEPAEA---RRRLGFVSDSTGLYDrLTAREN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 455 IL-FG-----KEDASLDEVVEAAKAsnahtfisqfpLGYKTQVGERGVQMSGGQKQRIAIARAIIKSPKILLLDEATSAL 528
Cdd:cd03266 99 LEyFAglyglKGDELTARLEELADR-----------LGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 15232977 529 DSESERVVQESLDN-ASIGRTTIVIAHRLSTI-RNADVICVIHNGQIVETG 577
Cdd:cd03266 168 DVMATRALREFIRQlRALGKCILFSTHIMQEVeRLCDRVVVLHRGRVVYEG 218
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
373-574 |
2.16e-21 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 95.15 E-value: 2.16e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 373 ETTIFDDLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYDPIAGEILIDGVSIDKLQVnWLRSQM-GLVSQEPVL---FA 448
Cdd:COG1101 18 EKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPE-YKRAKYiGRVFQDPMMgtaPS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 449 TSITENIL------------FGKEDASLDEVVEAakasnahtfISQFPLGY----KTQVGergvQMSGGQKQRIAIARAI 512
Cdd:COG1101 97 MTIEENLAlayrrgkrrglrRGLTKKRRELFREL---------LATLGLGLenrlDTKVG----LLSGGQRQALSLLMAT 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15232977 513 IKSPKILLLDEATSALD---SE-----SERVVQESldnasiGRTTIVIAHRLS-TIRNADVICVIHNGQIV 574
Cdd:COG1101 164 LTKPKLLLLDEHTAALDpktAAlvlelTEKIVEEN------NLTTLMVTHNMEqALDYGNRLIMMHEGRII 228
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
995-1221 |
2.26e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 95.44 E-value: 2.26e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 995 ITFLNVDFAYPTRPDVVifENFSIEIDEGKSTAIVGTSGSGKSTIIGLIERFYDPLKGTVKIDGRDIRSY-HLRSLRKYI 1073
Cdd:PRK13644 2 IRLENVSYSYPDGTPAL--ENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFsKLQGIRKLV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1074 SLVSQEP-MLFAG-TIRENIMYGGTSDKIDESEIIEAAKAANAHdfitslsNGYDTNCGDKGVQLSGGQKQRIAIARAVL 1151
Cdd:PRK13644 80 GIVFQNPeTQFVGrTVEEDLAFGPENLCLPPIEIRKRVDRALAE-------IGLEKYRHRSPKTLSGGQGQCVALAGILT 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15232977 1152 KNPSVLLLDEATSALDSKSERVVQDALERVM-VGRTSIMIAHRLSTIQNCDMIVVLGKGKIVESGTHSSLL 1221
Cdd:PRK13644 153 MEPECLIFDEVTSMLDPDSGIAVLERIKKLHeKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVL 223
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
364-583 |
2.41e-21 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 101.53 E-value: 2.41e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 364 VKFTYLSRpetTIFDDLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYDpIAGEILIDGVSIDKLQVNWLRSQMGLVSQE 443
Cdd:TIGR01271 1225 AKYTEAGR---AVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVSWNSVTLQTWRKAFGVIPQK 1300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 444 PVLFATSITENiLFGKEDASLDEVVEAAKASNAHTFISQFPLGYKTQVGERGVQMSGGQKQRIAIARAIIKSPKILLLDE 523
Cdd:TIGR01271 1301 VFIFSGTFRKN-LDPYEQWSDEEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDE 1379
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 524 ATSALDSESERVVQESLDNASIGRTTIVIAHRLSTIRNADVICVIHNGQIVETGSHEELL 583
Cdd:TIGR01271 1380 PSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRVEALLECQQFLVIEGSSVKQYDSIQKLL 1439
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
995-1223 |
2.50e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 95.64 E-value: 2.50e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 995 ITFLNVDFAYPTRPDVVIfENFSIEIDEGKSTAIVGTSGSGKSTIIGLIERFYDP---LKGTVKIDGRDIRSYHLRSLRK 1071
Cdd:PRK13640 6 VEFKHVSFTYPDSKKPAL-NDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPddnPNSKITVDGITLTAKTVWDIRE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1072 YISLVSQEP-MLFAG-TIRENIMYGGTSDKIDESEIIEAAKAANAH----DFITSlsngydtncgdKGVQLSGGQKQRIA 1145
Cdd:PRK13640 85 KVGIVFQNPdNQFVGaTVGDDVAFGLENRAVPRPEMIKIVRDVLADvgmlDYIDS-----------EPANLSGGQKQRVA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1146 IARAVLKNPSVLLLDEATSALDSKSERVVQDALERVMV--GRTSIMIAHRLSTIQNCDMIVVLGKGKIVESGTHSSLLEK 1223
Cdd:PRK13640 154 IAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKknNLTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEIFSK 233
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
995-1221 |
3.12e-21 |
|
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: 94.38 E-value: 3.12e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 995 ITFLNVDFAYPTRPdvvIFENFSIEIDEGKSTAIVGTSGSGKSTIIGLIERFYDPLKG-TVKIDGRDIRSYHLRSLRKYI 1073
Cdd:COG1119 4 LELRNVTVRRGGKT---ILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRGGEDVWELRKRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1074 SLVS---QEPMLFAGTIRENIMYGGTS-----DKIDESEIIEAAKAANAHDfITSLSN-GYDTncgdkgvqLSGGQKQRI 1144
Cdd:COG1119 81 GLVSpalQLRFPRDETVLDVVLSGFFDsiglyREPTDEQRERARELLELLG-LAHLADrPFGT--------LSQGEQRRV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1145 AIARAVLKNPSVLLLDEATSALDSKSERVVQDALERVMV--GRTSIMIAHRLSTIQNC-DMIVVLGKGKIVESGTHSSLL 1221
Cdd:COG1119 152 LIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAegAPTLVLVTHHVEEIPPGiTHVLLLKDGRVVAAGPKEEVL 231
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1009-1215 |
3.68e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 94.21 E-value: 3.68e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1009 DVVIFENFSIEIDEGKSTAIVGTSGSGKSTIIG----LIERFYDP-LKGTVKIDGRDIRSYHLRSLRKYISLVSQEPMLF 1083
Cdd:PRK14247 15 QVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRvfnrLIELYPEArVSGEVYLDGQDIFKMDVIELRRRVQMVFQIPNPI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1084 AG-TIRENIMYGGTSDKIDES--EIIEAAK-AANAHDFITSLSNGYDTNCGdkgvQLSGGQKQRIAIARAVLKNPSVLLL 1159
Cdd:PRK14247 95 PNlSIFENVALGLKLNRLVKSkkELQERVRwALEKAQLWDEVKDRLDAPAG----KLSGGQQQRLCIARALAFQPEVLLA 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15232977 1160 DEATSALDSKSERVVQDALERVMVGRTSIMIAH------RLStiqncDMIVVLGKGKIVESG 1215
Cdd:PRK14247 171 DEPTANLDPENTAKIESLFLELKKDMTIVLVTHfpqqaaRIS-----DYVAFLYKGQIVEWG 227
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1018-1221 |
4.53e-21 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 94.05 E-value: 4.53e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1018 IEIDEGKSTAIVGTSGSGKSTIIGLIERFYDPLKGTVK-----IDG-RDIRSYH--LRSLRKYISLVSQEPMLFAG-TIR 1088
Cdd:PRK11264 24 LEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRvgditIDTaRSLSQQKglIRQLRQHVGFVFQNFNLFPHrTVL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1089 ENIMYGGT-SDKIDESEIIEAAKAANAHDFITSLSNGYDTncgdkgvQLSGGQKQRIAIARAVLKNPSVLLLDEATSALD 1167
Cdd:PRK11264 104 ENIIEGPViVKGEPKEEATARARELLAKVGLAGKETSYPR-------RLSGGQQQRVAIARALAMRPEVILFDEPTSALD 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1168 SKSERVV-----QDALERvmvgRTSIMIAHRLSTIQN-CDMIVVLGKGKIVESGTHSSLL 1221
Cdd:PRK11264 177 PELVGEVlntirQLAQEK----RTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAKALF 232
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
35-339 |
4.59e-21 |
|
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; The bacterial lipid flippase MsbA is found in Gram-negative bacteria and transports lipid A and lipopolysaccharide (LPS) from the cytoplasmic leaflet to the periplasmic leaflet of the inner membrane. MsbA is also a polyspecific transporter capable of transporting a broad spectrum of drug molecules. Additionally, MsbA exhibits significant sequence similarity to mammalian multidrug resistance (MDR) proteins such as human MDR protein 1 (MDR1) and LmrA from Lactococcus lactis. This subgroup also contains a putative transporter Brevibacillus brevis TycD; the location of the tycD gene within the Tyc (tyrocidine) biosynthesis operon suggests that TycD may play a role in the secretion of the cyclic decapeptide antibiotic tyrocidine. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349996 [Multi-domain] Cd Length: 292 Bit Score: 95.18 E-value: 4.59e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 35 MALGLIGAVGDGFITPVVVFIFNTLLNNLGtsssnnktfmqtISKNVVALLYVACGswVIC---------FLEGYCWTRT 105
Cdd:cd18552 1 LALAILGMILVAATTAALAWLLKPLLDDIF------------VEKDLEALLLVPLA--IIGlfllrglasYLQTYLMAYV 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 106 GERQAARMREKYLRAVLRQDVGYFDLHvtSTSDVITSISSDSLVIQDFLSEKLPNFLMNASAFVASYIVSFILMWRLTIV 185
Cdd:cd18552 67 GQRVVRDLRNDLFDKLLRLPLSFFDRN--SSGDLISRITNDVNQVQNALTSALTVLVRDPLTVIGLLGVLFYLDWKLTLI 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 186 GFPFIILLLVPGLMYGRALVSISRKIHEQYNEAGSIAEQAISSVRTVYAFGSENKMIGKFSTALRGSVKLGLRQGLAKGI 265
Cdd:cd18552 145 ALVVLPLAALPIRRIGKRLRKISRRSQESMGDLTSVLQETLSGIRVVKAFGAEDYEIKRFRKANERLRRLSMKIARARAL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 266 ------TIGSNGVthaiwAFLTWYGSRLVMNHGSKGGTVFVVIscityggVSLGQSLSNLKYFSEAFVAWERILEVIKRV 339
Cdd:cd18552 225 ssplmeLLGAIAI-----ALVLWYGGYQVISGELTPGEFISFI-------TALLLLYQPIKRLSNVNANLQRGLAAAERI 292
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
357-587 |
5.35e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 94.69 E-value: 5.35e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 357 GEVEFNHVKFTYLSRP--ETTIFDDLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYDPIAGEILIDGVSI----DKL-Q 429
Cdd:PRK13645 5 KDIILDNVSYTYAKKTpfEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIpanlKKIkE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 430 VNWLRSQMGLVSQEP--VLFATSITENILFGKEDASLDEVvEAAKASNAHTFISQFPLGYktqVGERGVQMSGGQKQRIA 507
Cdd:PRK13645 85 VKRLRKEIGLVFQFPeyQLFQETIEKDIAFGPVNLGENKQ-EAYKKVPELLKLVQLPEDY---VKRSPFELSGGQKRRVA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 508 IARAIIKSPKILLLDEATSALDSESERVVQESLD--NASIGRTTIVIAHRLSTI-RNADVICVIHNGQIVETG------S 578
Cdd:PRK13645 161 LAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFErlNKEYKKRIIMVTHNMDQVlRIADEVIVMHEGKVISIGspfeifS 240
|
....*....
gi 15232977 579 HEELLKRID 587
Cdd:PRK13645 241 NQELLTKIE 249
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
359-583 |
5.44e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 94.53 E-value: 5.44e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 359 VEFNHVKFTYLSrpETTIFDDLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYDPIAGEILIDGVSID--KLQVNWLRSQ 436
Cdd:PRK13636 6 LKVEELNYNYSD--GTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDysRKGLMKLRES 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 437 MGLVSQEP--VLFATSITENILFGKEDASL--DEVVEAAKASNAHTFISqfPLGYKTQVGergvqMSGGQKQRIAIARAI 512
Cdd:PRK13636 84 VGMVFQDPdnQLFSASVYQDVSFGAVNLKLpeDEVRKRVDNALKRTGIE--HLKDKPTHC-----LSFGQKKRVAIAGVL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15232977 513 IKSPKILLLDEATSALD----SESERVVQESLDNASIgrtTIVIA-HRLSTIR-NADVICVIHNGQIVETGSHEELL 583
Cdd:PRK13636 157 VMEPKVLVLDEPTAGLDpmgvSEIMKLLVEMQKELGL---TIIIAtHDIDIVPlYCDNVFVMKEGRVILQGNPKEVF 230
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
999-1216 |
5.84e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 94.38 E-value: 5.84e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 999 NVDFAY-----PTRPDVVifENFSIEIDEGKSTAIVGTSGSGKSTIIGLIERFYDPLKGTVKIDGRDIRSY-HLRSLRKY 1072
Cdd:PRK13633 9 NVSYKYesneeSTEKLAL--DDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEeNLWDIRNK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1073 ISLVSQEP--MLFAGTIRENIMYGGTSDKIDESEII----EAAKAANAHDFITSLSNgydtncgdkgvQLSGGQKQRIAI 1146
Cdd:PRK13633 87 AGMVFQNPdnQIVATIVEEDVAFGPENLGIPPEEIRervdESLKKVGMYEYRRHAPH-----------LLSGGQKQRVAI 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15232977 1147 ARAVLKNPSVLLLDEATSALDSKSERVVQDALERV--MVGRTSIMIAHRLSTIQNCDMIVVLGKGKIVESGT 1216
Cdd:PRK13633 156 AGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELnkKYGITIILITHYMEEAVEADRIIVMDSGKVVMEGT 227
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
373-586 |
8.64e-21 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 93.15 E-value: 8.64e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 373 ETTIFDDLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYDPIAGEILIDGVSIDKLQVNWLRSQMGLVSQEPVlfatsIT 452
Cdd:PRK11231 14 TKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQHHL-----TP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 453 ENI---------------LFGKEDASLDEVVEAAKASnahTFISQFplgyktqvGERGV-QMSGGQKQRIAIARAIIKSP 516
Cdd:PRK11231 89 EGItvrelvaygrspwlsLWGRLSAEDNARVNQAMEQ---TRINHL--------ADRRLtDLSGGQRQRAFLAMVLAQDT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 517 KILLLDEATSALD----SESERVVQESLDNasiGRTTIVIAHRLS-TIRNADVICVIHNGQIVETGSHEE-----LLKRI 586
Cdd:PRK11231 158 PVVLLDEPTTYLDinhqVELMRLMRELNTQ---GKTVVTVLHDLNqASRYCDHLVVLANGHVMAQGTPEEvmtpgLLRTV 234
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
359-583 |
8.96e-21 |
|
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: 93.23 E-value: 8.96e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 359 VEFNHVKFtylSRPETTIFDDLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYDPIAG---EIL---IDGVSIdklqvnW 432
Cdd:COG1119 4 LELRNVTV---RRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGndvRLFgerRGGEDV------W 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 433 -LRSQMGLVS---QEPVLFATSITENILFGKEDAS-LDEVVEAAKASNAHTFISQFPLGYKTQvgERGVQMSGGQKQRIA 507
Cdd:COG1119 75 eLRKRIGLVSpalQLRFPRDETVLDVVLSGFFDSIgLYREPTDEQRERARELLELLGLAHLAD--RPFGTLSQGEQRRVL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 508 IARAIIKSPKILLLDEATSALDSESERVVQESLDN-ASIGRTTIV-IAHRLSTIrnadVICVIH-----NGQIVETGSHE 580
Cdd:COG1119 153 IARALVKDPELLILDEPTAGLDLGARELLLALLDKlAAEGAPTLVlVTHHVEEI----PPGITHvlllkDGRVVAAGPKE 228
|
...
gi 15232977 581 ELL 583
Cdd:COG1119 229 EVL 231
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
359-624 |
9.77e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 93.60 E-value: 9.77e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 359 VEFNHVKFTYlsrPE-TTIFDDLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYDPIAGEILIDGVSI--DKLQVNWLRS 435
Cdd:PRK13639 2 LETRDLKYSY---PDgTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIkyDKKSLLEVRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 436 QMGLVSQEP--VLFATSITENILFGKEDASLDE------VVEAAKASNAHTFISQFPLgyktqvgergvQMSGGQKQRIA 507
Cdd:PRK13639 79 TVGIVFQNPddQLFAPTVEEDVAFGPLNLGLSKeevekrVKEALKAVGMEGFENKPPH-----------HLSGGQKKRVA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 508 IARAIIKSPKILLLDEATSALDSESERVVQESLDNASIGRTTIVIA-HRLSTI-RNADVICVIHNGQIVETG------SH 579
Cdd:PRK13639 148 IAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIIStHDVDLVpVYADKVYVMSDGKIIKEGtpkevfSD 227
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 15232977 580 EELLKRIDGQYTSLVSLQQMENEESNVNINVSVTKDQVMSLSKDF 624
Cdd:PRK13639 228 IETIRKANLRLPRVAHLIEILNKEDNLPIKMGYTIGEARRNIKEL 272
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
999-1216 |
9.77e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 93.60 E-value: 9.77e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 999 NVDFAYPTrpDVVIFENFSIEIDEGKSTAIVGTSGSGKSTIIGLIERFYDPLKGTVKIDGRDIrSYHLRSL---RKYISL 1075
Cdd:PRK13639 6 DLKYSYPD--GTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPI-KYDKKSLlevRKTVGI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1076 VSQEP--MLFAGTIRENIMYGGTSDKIDESEI----IEAAKAANAHDFITSLSNgydtncgdkgvQLSGGQKQRIAIARA 1149
Cdd:PRK13639 83 VFQNPddQLFAPTVEEDVAFGPLNLGLSKEEVekrvKEALKAVGMEGFENKPPH-----------HLSGGQKKRVAIAGI 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15232977 1150 VLKNPSVLLLDEATSALD----SKSERVVQDALERvmvGRTSIMIAHRLSTIQ-NCDMIVVLGKGKIVESGT 1216
Cdd:PRK13639 152 LAMKPEIIVLDEPTSGLDpmgaSQIMKLLYDLNKE---GITIIISTHDVDLVPvYADKVYVMSDGKIIKEGT 220
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
371-576 |
1.01e-20 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 93.60 E-value: 1.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 371 RPETTIFDDLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYDPIAGEILIDGVSIDKL---QVNWLRSQMGLVSQ----- 442
Cdd:PRK10419 22 HQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLnraQRKAFRRDIQMVFQdsisa 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 443 ------------EPVLFATSITEnilfGKEDASLDEVVEAAKASNAHtfISQFPlgyktqvgergVQMSGGQKQRIAIAR 510
Cdd:PRK10419 102 vnprktvreiirEPLRHLLSLDK----AERLARASEMLRAVDLDDSV--LDKRP-----------PQLSGGQLQRVCLAR 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15232977 511 AIIKSPKILLLDEATSALDseseRVVQ-ESLD-----NASIGRTTIVIAHRLSTI-RNADVICVIHNGQIVET 576
Cdd:PRK10419 165 ALAVEPKLLILDEAVSNLD----LVLQaGVIRllkklQQQFGTACLFITHDLRLVeRFCQRVMVMDNGQIVET 233
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
373-573 |
1.05e-20 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 93.20 E-value: 1.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 373 ETTIFDDLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYDPIAGEILIDGVSIDKLqvnwlRSQMGLVSQEPVLFA-TSI 451
Cdd:PRK11247 24 ERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEA-----REDTRLMFQDARLLPwKKV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 452 TENILFGKEDASLDEVVEAAKAsnahtfisqfpLGYKTQVGERGVQMSGGQKQRIAIARAIIKSPKILLLDEATSALDSE 531
Cdd:PRK11247 99 IDNVGLGLKGQWRDAALQALAA-----------VGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDAL 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 15232977 532 SERVVQESLDN--ASIGRTTIVIAHRLS-TIRNADVICVIHNGQI 573
Cdd:PRK11247 168 TRIEMQDLIESlwQQHGFTVLLVTHDVSeAVAMADRVLLIEEGKI 212
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
1012-1221 |
1.16e-20 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 93.11 E-value: 1.16e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1012 IFENFSIEIDEGKSTAIVGTSGSGKSTIIGLIERFYDPLKGTVKIDGRDIR-------------SYHLRSLRKYISLVSQ 1078
Cdd:PRK10619 20 VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgqlkvadKNQLRLLRTRLTMVFQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1079 EPMLFAG-TIRENIMYGGTsdkidesEIIEAAKAANAHDFITSLSN-GYDTNCGDK-GVQLSGGQKQRIAIARAVLKNPS 1155
Cdd:PRK10619 100 HFNLWSHmTVLENVMEAPI-------QVLGLSKQEARERAVKYLAKvGIDERAQGKyPVHLSGGQQQRVSIARALAMEPE 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15232977 1156 VLLLDEATSALD----SKSERVVQDALERvmvGRTSIMIAHRLSTIQNC-DMIVVLGKGKIVESGTHSSLL 1221
Cdd:PRK10619 173 VLLFDEPTSALDpelvGEVLRIMQQLAEE---GKTMVVVTHEMGFARHVsSHVIFLHQGKIEEEGAPEQLF 240
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
382-591 |
1.18e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 92.98 E-value: 1.18e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 382 LKIPAGKTVALVGGSGSGKSTVISLLQRFYD-----PIAGEILIDGVSIDKLQVNWL--RSQMGLVSQEPVLFA-TSITE 453
Cdd:PRK14267 25 LKIPQNGVFALMGPSGCGKSTLLRTFNRLLElneeaRVEGEVRLFGRNIYSPDVDPIevRREVGMVFQYPNPFPhLTIYD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 454 NILFG-------KEDASLDEVVEAAKASNAhtfisqFPLGYKTQVGERGVQMSGGQKQRIAIARAIIKSPKILLLDEATS 526
Cdd:PRK14267 105 NVAIGvklnglvKSKKELDERVEWALKKAA------LWDEVKDRLNDYPSNLSGGQRQRLVIARALAMKPKILLMDEPTA 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15232977 527 ALDSESERVVQESLDNASIGRTTIVIAHR-LSTIRNADVICVIHNGQIVETGSHEELLKRIDGQYT 591
Cdd:PRK14267 179 NIDPVGTAKIEELLFELKKEYTIVLVTHSpAQAARVSDYVAFLYLGKLIEVGPTRKVFENPEHELT 244
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
385-587 |
1.33e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 93.33 E-value: 1.33e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 385 PAGKTVALVGGSGSGKSTVISLLQRFYDPIAGEILIDGVSIDKLQVNWLRSQMGLVSQEP--VLFATSITENILFGKEDA 462
Cdd:PRK13652 28 PRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLVFQNPddQIFSPTVEQDIAFGPINL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 463 SLDEVVEAAKASNA-HTF-ISQfplgYKTQVGErgvQMSGGQKQRIAIARAIIKSPKILLLDEATSALDSESERVVQESL 540
Cdd:PRK13652 108 GLDEETVAHRVSSAlHMLgLEE----LRDRVPH---HLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFL 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15232977 541 DNASI--GRTTIVIAHRLSTIRN-ADVICVIHNGQIVETGSHEELLKRID 587
Cdd:PRK13652 181 NDLPEtyGMTVIFSTHQLDLVPEmADYIYVMDKGRIVAYGTVEEIFLQPD 230
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1017-1223 |
1.51e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 93.37 E-value: 1.51e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1017 SIEIDEGKSTAIVGTSGSGKSTIIGLIERFYDPLKGTVKIDGR--DIRSYHLRSLRKYISLVSQEP--MLFAGTIRENIM 1092
Cdd:PRK13636 26 NINIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKpiDYSRKGLMKLRESVGMVFQDPdnQLFSASVYQDVS 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1093 YGGTSDKIDESEIIEAAKAANAHDFITSLSNGyDTNCgdkgvqLSGGQKQRIAIARAVLKNPSVLLLDEATSALDSKSER 1172
Cdd:PRK13636 106 FGAVNLKLPEDEVRKRVDNALKRTGIEHLKDK-PTHC------LSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVS 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15232977 1173 VVQDALERVM--VGRTSIMIAHRLSTIQ-NCDMIVVLGKGKIVESGTHSSLLEK 1223
Cdd:PRK13636 179 EIMKLLVEMQkeLGLTIIIATHDIDIVPlYCDNVFVMKEGRVILQGNPKEVFAE 232
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
1002-1215 |
1.57e-20 |
|
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: 91.83 E-value: 1.57e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1002 FAYPTRPDVVIFENFSIEIDEGKSTAIVGTSGSGKSTIIGLIERFYDPLKGTVKIDGRdirsyhlrslrkyislVSqePM 1081
Cdd:cd03220 27 GRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGR----------------VS--SL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1082 LFAG-------TIRENI-----MYGGTSDKIDESEiieaakaanahDFITSLSN-GydtNCGDKGV-QLSGGQKQRIAIA 1147
Cdd:cd03220 89 LGLGggfnpelTGRENIylngrLLGLSRKEIDEKI-----------DEIIEFSElG---DFIDLPVkTYSSGMKARLAFA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15232977 1148 RAVLKNPSVLLLDEATSALDS----KSERVVQdalERVMVGRTSIMIAHRLSTI-QNCDMIVVLGKGKIVESG 1215
Cdd:cd03220 155 IATALEPDILLIDEVLAVGDAafqeKCQRRLR---ELLKQGKTVILVSHDPSSIkRLCDRALVLEKGKIRFDG 224
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
993-1216 |
1.59e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 93.53 E-value: 1.59e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 993 GQITFLNVDFAYPTRP--DVVIFENFSIEIDEGKSTAIVGTSGSGKSTIIGL-----IERFYDPLKGTVKIDGRDIRSYH 1065
Cdd:PRK13645 5 KDIILDNVSYTYAKKTpfEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLtngliISETGQTIVGDYAIPANLKKIKE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1066 LRSLRKYISLVSQEP--MLFAGTIRENIMYGGTSDKIDESEIIEaaKAANAHDFItSLSNGYDTNcgdKGVQLSGGQKQR 1143
Cdd:PRK13645 85 VKRLRKEIGLVFQFPeyQLFQETIEKDIAFGPVNLGENKQEAYK--KVPELLKLV-QLPEDYVKR---SPFELSGGQKRR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15232977 1144 IAIARAVLKNPSVLLLDEATSALDSKSERVVQDALERV--MVGRTSIMIAHRLSTI-QNCDMIVVLGKGKIVESGT 1216
Cdd:PRK13645 159 VALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLnkEYKKRIIMVTHNMDQVlRIADEVIVMHEGKVISIGS 234
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
77-332 |
1.60e-20 |
|
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 350019 [Multi-domain] Cd Length: 289 Bit Score: 93.32 E-value: 1.60e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 77 ISKNVVALLYVACGSWVICFLEGYCWTRTGERQAARMREKYLRAVLRQDVGYFDlhVTSTSDVITSISSDSLVIQDFLSE 156
Cdd:cd18575 35 LNRAFLLLLAVALVLALASALRFYLVSWLGERVVADLRKAVFAHLLRLSPSFFE--TTRTGEVLSRLTTDTTLIQTVVGS 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 157 KLPNFLMNASAFVASYIVSFILMWRLTIVGFPFIILLLVPGLMYGRALVSISRKIHEQYNEAGSIAEQAISSVRTVYAFG 236
Cdd:cd18575 113 SLSIALRNLLLLIGGLVMLFITSPKLTLLVLLVIPLVVLPIILFGRRVRRLSRASQDRLADLSAFAEETLSAIKTVQAFT 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 237 SENKMIGKFSTALRGSVKLGLRQGLAKG------ITIGSNGVThaiwaFLTWYGSRLVMNHGSKGG--TVFVVISCITYG 308
Cdd:cd18575 193 REDAERQRFATAVEAAFAAALRRIRARAlltalvIFLVFGAIV-----FVLWLGAHDVLAGRMSAGelSQFVFYAVLAAG 267
|
250 260
....*....|....*....|....*
gi 15232977 309 GV-SLGQSLSNLkyfSEAFVAWERI 332
Cdd:cd18575 268 SVgALSEVWGDL---QRAAGAAERL 289
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1017-1222 |
1.66e-20 |
|
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: 91.97 E-value: 1.66e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1017 SIEIDEGKSTAIVGTSGSGKST----IIGLIerfyDPLKGTVKIDGRDI--RSYHLRSlRKYISLVSQEPMLFAG-TIRE 1089
Cdd:COG0410 23 SLEVEEGEIVALLGRNGAGKTTllkaISGLL----PPRSGSIRFDGEDItgLPPHRIA-RLGIGYVPEGRRIFPSlTVEE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1090 NIMYGG--TSDKIDESEIIEAAkaanahdfitslsngYDT------NCGDKGVQLSGGQKQRIAIARAVLKNPSVLLLDE 1161
Cdd:COG0410 98 NLLLGAyaRRDRAEVRADLERV---------------YELfprlkeRRRQRAGTLSGGEQQMLAIGRALMSRPKLLLLDE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15232977 1162 ATSALdskSERVVQ---DALERVMVGRTSIMI----AHRLSTIqnCDMIVVLGKGKIVESGTHSSLLE 1222
Cdd:COG0410 163 PSLGL---APLIVEeifEIIRRLNREGVTILLveqnARFALEI--ADRAYVLERGRIVLEGTAAELLA 225
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
32-260 |
1.79e-20 |
|
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar proteins; This group represents the six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA from Lactococcus lactis and similar proteins. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349995 [Multi-domain] Cd Length: 289 Bit Score: 93.27 E-value: 1.79e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 32 WILMALGLIGAVGdGFITPVVVfifNTLLNNLGTSSSNNKTfmqtisknVVALLYVACGSWVICFLEGYCWTRTGERQAA 111
Cdd:cd18551 2 ILALLLSLLGTAA-SLAQPLLV---KNLIDALSAGGSSGGL--------LALLVALFLLQAVLSALSSYLLGRTGERVVL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 112 RMREKYLRAVLRQDVGYFDLHvtSTSDVITSISSDSLVIQDFLSEKLPNFLMNASAFVASYIVSFILMWRLTIV---GFP 188
Cdd:cd18551 70 DLRRRLWRRLLRLPVSFFDRR--RSGDLVSRVTNDTTLLRELITSGLPQLVTGVLTVVGAVVLMFLLDWVLTLVtlaVVP 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15232977 189 FIILLLVPglmYGRALVSISRKIHEQYNEAGSIAEQAISSVRTVYAFGSENKMIGKFSTALRGSVKLGLRQG 260
Cdd:cd18551 148 LAFLIILP---LGRRIRKASKRAQDALGELSAALERALSAIRTVKASNAEERETKRGGEAAERLYRAGLKAA 216
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
358-587 |
2.25e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 92.78 E-value: 2.25e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 358 EVEFNHVKFTYLSRpetTIFDDLCLK-----IPAGKTVALVGGSGSGKSTVISLLQRFYDPIAGEILI------DGVSID 426
Cdd:PRK13634 2 DITFQKVEHRYQYK---TPFERRALYdvnvsIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIgervitAGKKNK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 427 KLQVnwLRSQMGLVSQ--EPVLFATSITENILFGKEDASLDEVVEAAKASNAHTFIsqfplGYKTQVGERG-VQMSGGQK 503
Cdd:PRK13634 79 KLKP--LRKKVGIVFQfpEHQLFEETVEKDICFGPMNFGVSEEDAKQKAREMIELV-----GLPEELLARSpFELSGGQM 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 504 QRIAIARAIIKSPKILLLDEATSALDSESERVVQESLDN--ASIGRTTIVIAHRLSTIRN-ADVICVIHNGQIVETGSHE 580
Cdd:PRK13634 152 RRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKlhKEKGLTTVLVTHSMEDAARyADQIVVMHKGTVFLQGTPR 231
|
....*..
gi 15232977 581 ELLKRID 587
Cdd:PRK13634 232 EIFADPD 238
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
373-587 |
2.34e-20 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 91.67 E-value: 2.34e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 373 ETTIFDDLCLKIPAGKTVALVGGSGSGKST---VISLLQRfYDPIAGEILIDGVSIDKLQVNwLRSQMGL-VS-QEPV-- 445
Cdd:COG0396 12 GKEILKGVNLTIKPGEVHAIMGPNGSGKSTlakVLMGHPK-YEVTSGSILLDGEDILELSPD-ERARAGIfLAfQYPVei 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 446 ------LFATSITENILFGKEDA--SLDEVVEAAKAsnahtfisqfpLGYKTQVGERGVQ--MSGGQKQRIAIARAIIKS 515
Cdd:COG0396 90 pgvsvsNFLRTALNARRGEELSAreFLKLLKEKMKE-----------LGLDEDFLDRYVNegFSGGEKKRNEILQMLLLE 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15232977 516 PKILLLDEATSALDSESERVVQESLDN-ASIGRTTIVIAH--RLSTIRNADVICVIHNGQIVETGShEELLKRID 587
Cdd:COG0396 159 PKLAILDETDSGLDIDALRIVAEGVNKlRSPDRGILIITHyqRILDYIKPDFVHVLVDGRIVKSGG-KELALELE 232
|
|
| ABC_6TM_ABCB8_like |
cd18574 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ... |
103-290 |
3.09e-20 |
|
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B member 8, mitochondrial, and similar proteins; This group includes ABCB8, which is one of the three ATP-binding cassette (ABC) transporters found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. ABCB8 is essential for maintenance of normal cardiac function, involves mitochondrial iron export, and plays a role in the maturation of cytosolic Fe/S cluster-containing enzymes. ABCB8 is a half-molecule ABC protein that contains one TMD fused to a NBD, which dimerize to form a functional transporter.
Pssm-ID: 350018 [Multi-domain] Cd Length: 295 Bit Score: 92.61 E-value: 3.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 103 TRTGERQAARMREKYLRAVLRQDVGYFDLHvtSTSDVITSISSDslvIQDF-------LSEKLPNFLMNASAFVASYIVS 175
Cdd:cd18574 67 SVVGERVAARLRNDLFSSLLRQDIAFFDTH--RTGELVNRLTAD---VQEFkssfkqcVSQGLRSVTQTVGCVVSLYLIS 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 176 FilmwRLTI---VGFPFIILLlvpGLMYGRALVSISRKIHEQYNEAGSIAEQAISSVRTVYAFGSENKMIGKFST----A 248
Cdd:cd18574 142 P----KLTLlllVIVPVVVLV---GTLYGSFLRKLSRRAQAQVAKATGVADEALGNIRTVRAFAMEDRELELYEEevekA 214
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 15232977 249 LRGSVKLGLRQGLAKGIT-IGSNGVTHAIwaflTWYGSRLVMN 290
Cdd:cd18574 215 AKLNEKLGLGIGIFQGLSnLALNGIVLGV----LYYGGSLVSR 253
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
54-332 |
3.94e-20 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350008 [Multi-domain] Cd Length: 307 Bit Score: 92.58 E-value: 3.94e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 54 FIFNTLLNNLGTSSSNNKTFMQTISKnvVALLYVACGSWV--------ICFLEGYCWTRTGERQAARMREKYLRAVLRQD 125
Cdd:cd18564 24 VVIDDVLGDKPLPGLLGLAPLLGPDP--LALLLLAAAALVgiallrglASYAGTYLTALVGQRVVLDLRRDLFAHLQRLS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 126 VGYFDLHvtSTSDVITSISSDSLVIQDFLSEKLPNFLMNASAFVASYIVSFILMWRLTIVGFPFIILLLVPGLMYGRALV 205
Cdd:cd18564 102 LSFHDRR--RTGDLLSRLTGDVGAIQDLLVSGVLPLLTNLLTLVGMLGVMFWLDWQLALIALAVAPLLLLAARRFSRRIK 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 206 SISRKIHEQYNEAGSIAEQAISSVRTVYAFGSENKMIGKFSTALRGSVKLGLRQ-GLAKGITIGSNGVTHAIWAFLTWYG 284
Cdd:cd18564 180 EASREQRRREGALASVAQESLSAIRVVQAFGREEHEERRFARENRKSLRAGLRAaRLQALLSPVVDVLVAVGTALVLWFG 259
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15232977 285 SRLVMNHG-SKGG-TVFVvisciTYggvslgqsLSNL--------KY---FSEAFVAWERI 332
Cdd:cd18564 260 AWLVLAGRlTPGDlLVFL-----AY--------LKNLykpvrdlaKLtgrIAKASASAERV 307
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
691-929 |
4.31e-20 |
|
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, member 10) and similar proteins; This group includes the 6-TM subunit of the ABC10 (also known as ABC mitochondrial erythroid, ABC-me, mABC2, or ABCBA), which is one of the three ATP-binding cassette (ABC) transporters found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. In mammals, ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane.
Pssm-ID: 350017 [Multi-domain] Cd Length: 294 Bit Score: 92.19 E-value: 4.31e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 691 YSAGSVISVFFLTSHDQIKEKTRIYVLLFVGLAIFSF--LVNISQHYGFAYMGEYLTKRIREQMLSKILTFEVNWFDidD 768
Cdd:cd18573 17 FAIGKLIDVASKESGDIEIFGLSLKTFALALLGVFVVgaAANFGRVYLLRIAGERIVARLRKRLFKSILRQDAAFFD--K 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 769 NSSGAICSRLAKDANVVRSMVGDRMSLLVQTISAVIIACIIGLVIAWRLAIVMISVQPLIVVCFYTQRVLLKSLSEKASK 848
Cdd:cd18573 95 NKTGELVSRLSSDTSVVGKSLTQNLSDGLRSLVSGVGGIGMMLYISPKLTLVMLLVVPPIAVGAVFYGRYVRKLSKQVQD 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 849 AQDESSKLAAEAVSNIRTITAFSSQERIIKLLKKVQEGPRRESVHRSWLAGIVLGTSRSLITCTSALNFWYGGRLIADGK 928
Cdd:cd18573 175 ALADATKVAEERLSNIRTVRAFAAERKEVERYAKKVDEVFDLAKKEALASGLFFGSTGFSGNLSLLSVLYYGGSLVASGE 254
|
.
gi 15232977 929 I 929
Cdd:cd18573 255 L 255
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1016-1221 |
4.90e-20 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 90.41 E-value: 4.90e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1016 FSIEIDEGKSTAIVGTSGSGKSTIIGLIERFYDPLKGTVKIDGRDirsyHLRS--LRKYISLVSQEPMLFAG-TIRENIM 1092
Cdd:PRK10771 18 FDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQD----HTTTppSRRPVSMLFQENNLFSHlTVAQNIG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1093 YG---G---TSDKIDESEIIeaAKAANAHDFITSLSNgydtncgdkgvQLSGGQKQRIAIARAVLKNPSVLLLDEATSAL 1166
Cdd:PRK10771 94 LGlnpGlklNAAQREKLHAI--ARQMGIEDLLARLPG-----------QLSGGQRQRVALARCLVREQPILLLDEPFSAL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15232977 1167 DSKSERVVQDALERVMVGR--TSIMIAHRLS-TIQNCDMIVVLGKGKIVESGTHSSLL 1221
Cdd:PRK10771 161 DPALRQEMLTLVSQVCQERqlTLLMVSHSLEdAARIAPRSLVVADGRIAWDGPTDELL 218
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
716-941 |
5.08e-20 |
|
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 350020 [Multi-domain] Cd Length: 289 Bit Score: 91.78 E-value: 5.08e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 716 VLLFVGLAIFSFLvnisQHYGFAYMGEYLTKRIREQMLSKILTFEVNWFDidDNSSGAICSRLAKDANVVRSMVGDRMSL 795
Cdd:cd18576 43 LGLFLLQAVFSFF----RIYLFARVGERVVADLRKDLYRHLQRLPLSFFH--ERRVGELTSRLSNDVTQIQDTLTTTLAE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 796 LVQTISAVIIACIIGLVIAWRLAIVMISVQPLIVVCFYTQRVLLKSLSEKASKAQDESSKLAAEAVSNIRTITAFSSQER 875
Cdd:cd18576 117 FLRQILTLIGGVVLLFFISWKLTLLMLATVPVVVLVAVLFGRRIRKLSKKVQDELAEANTIVEETLQGIRVVKAFTREDY 196
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15232977 876 IIKLLKKVQEGPRRESVHRSWLAGIVLGTSRSLITCTSALNFWYGGRLIADGKIVSKAFFEiFLIF 941
Cdd:cd18576 197 EIERYRKALERVVKLALKRARIRALFSSFIIFLLFGAIVAVLWYGGRLVLAGELTAGDLVA-FLLY 261
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
365-583 |
5.24e-20 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 90.41 E-value: 5.24e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 365 KFTYLSRPETTIFDdlcLKIPAGKTVALVGGSGSGKSTVISLLQRFYDPIAGEILIDGV-----SIDKLQVNWLrsqmgl 439
Cdd:PRK10771 6 DITWLYHHLPMRFD---LTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQdhtttPPSRRPVSML------ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 440 vSQEPVLFA-TSITENILFG-----KEDASLDEVVEA-AKASNAHTFISQFPlgyktqvgergVQMSGGQKQRIAIARAI 512
Cdd:PRK10771 77 -FQENNLFShLTVAQNIGLGlnpglKLNAAQREKLHAiARQMGIEDLLARLP-----------GQLSGGQRQRVALARCL 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15232977 513 IKSPKILLLDEATSALD----SESERVVQESLDNASIgrTTIVIAHRLS-TIRNADVICVIHNGQIVETGSHEELL 583
Cdd:PRK10771 145 VREQPILLLDEPFSALDpalrQEMLTLVSQVCQERQL--TLLMVSHSLEdAARIAPRSLVVADGRIAWDGPTDELL 218
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
369-583 |
6.16e-20 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 93.75 E-value: 6.16e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 369 LSRPETTIFDDLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYDPIAGEILIDGVSIDKLQVNWLRSQMGLVSQEPVL-F 447
Cdd:PRK09536 11 VEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDTSLsF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 448 ATSITENI---------LFGKEDASLDEVVEAAKASnahTFISQFplgyktqvGERGV-QMSGGQKQRIAIARAIIKSPK 517
Cdd:PRK09536 91 EFDVRQVVemgrtphrsRFDTWTETDRAAVERAMER---TGVAQF--------ADRPVtSLSGGERQRVLLARALAQATP 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15232977 518 ILLLDEATSALDSESE----RVVQESLDNasiGRTTIVIAHRLS-TIRNADVICVIHNGQIVETGSHEELL 583
Cdd:PRK09536 160 VLLLDEPTASLDINHQvrtlELVRRLVDD---GKTAVAAIHDLDlAARYCDELVLLADGRVRAAGPPADVL 227
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1006-1220 |
6.27e-20 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 89.55 E-value: 6.27e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1006 TRPDVVIFENFSIEIDEGKSTAIVGTSGSGKSTIIGLIERFYDPLKGTVKIDGRDIRSYHLRSLRKYISlvSQEPMLFAG 1085
Cdd:PRK13539 11 VRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACHYLG--HRNAMKPAL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1086 TIRENI-----MYGGtsdkiDESEIIEAAKAANAHDfITSLSNGYdtncgdkgvqLSGGQKQRIAIARAVLKNPSVLLLD 1160
Cdd:PRK13539 89 TVAENLefwaaFLGG-----EELDIAAALEAVGLAP-LAHLPFGY----------LSAGQKRRVALARLLVSNRPIWILD 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1161 EATSALDSKSERVVQDalervmvgrtsIMIAHrlstiqncdmivvLGKGKIVESGTHSSL 1220
Cdd:PRK13539 153 EPTAALDAAAVALFAE-----------LIRAH-------------LAQGGIVIAATHIPL 188
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
1014-1194 |
7.08e-20 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 91.00 E-value: 7.08e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1014 ENFSIEIDEGKSTAIVGTSGSGKSTIIGLIERFYDPLKGtVKIDGRDIrsYHLRSL----------RKYISLVSQEPMLF 1083
Cdd:PRK14243 27 KNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLIPG-FRVEGKVT--FHGKNLyapdvdpvevRRRIGMVFQKPNPF 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1084 AGTIRENIMYGGTSD--KIDESEIIEAA--KAAnahdfitsLSNGYDTNCGDKGVQLSGGQKQRIAIARAVLKNPSVLLL 1159
Cdd:PRK14243 104 PKSIYDNIAYGARINgyKGDMDELVERSlrQAA--------LWDEVKDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILM 175
|
170 180 190
....*....|....*....|....*....|....*
gi 15232977 1160 DEATSALDSKSERVVQDALERVMVGRTSIMIAHRL 1194
Cdd:PRK14243 176 DEPCSALDPISTLRIEELMHELKEQYTIIIVTHNM 210
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
359-621 |
8.67e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 90.82 E-value: 8.67e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 359 VEFNHVKFTYlsrPE-TTIFDDLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYDPIAGEILIDGVSI-DKLQVNWLRSQ 436
Cdd:PRK13644 2 IRLENVSYSY---PDgTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTgDFSKLQGIRKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 437 MGLVSQEP--VLFATSITENILFGKEDASLDEVVEAAKASNAhtfISQFPLG-YKTQVGErgvQMSGGQKQRIAIARAII 513
Cdd:PRK13644 79 VGIVFQNPetQFVGRTVEEDLAFGPENLCLPPIEIRKRVDRA---LAEIGLEkYRHRSPK---TLSGGQGQCVALAGILT 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 514 KSPKILLLDEATSALDSESERVVQESLDNA-SIGRTTIVIAHRLSTIRNADVICVIHNGQIVETGSHEELLKRIDGQYTS 592
Cdd:PRK13644 153 MEPECLIFDEVTSMLDPDSGIAVLERIKKLhEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLSDVSLQTLG 232
|
250 260
....*....|....*....|....*....
gi 15232977 593 LVSLQQMENEESNVNINVSVTKDQVMSLS 621
Cdd:PRK13644 233 LTPPSLIELAENLKMHGVVIPWENTSSPS 261
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
373-603 |
9.17e-20 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 94.77 E-value: 9.17e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 373 ETTIFDDLCLKIPAGKTVALVGGSGSGKS-TVISLLQRFYDP----IAGEILIDGVSI---DKLQVNWLR-SQMGLVSQE 443
Cdd:PRK15134 21 VRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPpvvyPSGDIRFHGESLlhaSEQTLRGVRgNKIAMIFQE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 444 PVlfatsITENILFGKEDaSLDEVV--------EAAKAS-----------NAHTFISQFPLgyktqvgergvQMSGGQKQ 504
Cdd:PRK15134 101 PM-----VSLNPLHTLEK-QLYEVLslhrgmrrEAARGEilncldrvgirQAAKRLTDYPH-----------QLSGGERQ 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 505 RIAIARAIIKSPKILLLDEATSALDSESE-------RVVQESLdNASIgrttIVIAHRLSTIRN-ADVICVIHNGQIVET 576
Cdd:PRK15134 164 RVMIAMALLTRPELLIADEPTTALDVSVQaqilqllRELQQEL-NMGL----LFITHNLSIVRKlADRVAVMQNGRCVEQ 238
|
250 260
....*....|....*....|....*..
gi 15232977 577 GSHEELLKRIDGQYTslvslQQMENEE 603
Cdd:PRK15134 239 NRAATLFSAPTHPYT-----QKLLNSE 260
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
998-1221 |
1.05e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 90.11 E-value: 1.05e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 998 LNVDFAYPTRPDVVIFENFSIEIDEGKSTAIVGTSGSGKSTIIGLIERFYDPLKGTVKIDGR------DIRSYHLRSLRK 1071
Cdd:PRK14246 11 FNISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKvlyfgkDIFQIDAIKLRK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1072 YISLVSQEPMLFAG-TIRENIMY----GGTSDKIDESEIIEAAKAA-----NAHDFITSLSNgydtncgdkgvQLSGGQK 1141
Cdd:PRK14246 91 EVGMVFQQPNPFPHlSIYDNIAYplksHGIKEKREIKKIVEECLRKvglwkEVYDRLNSPAS-----------QLSGGQQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1142 QRIAIARAVLKNPSVLLLDEATSALDSKSERVVQDALERVMVGRTSIMIAHRLSTIQN-CDMIVVLGKGKIVESGTHSSL 1220
Cdd:PRK14246 160 QRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARvADYVAFLYNGELVEWGSSNEI 239
|
.
gi 15232977 1221 L 1221
Cdd:PRK14246 240 F 240
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1001-1216 |
1.16e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 90.63 E-value: 1.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1001 DFAYPTRPDVVIFENFSIEIDEGKSTAIVGTSGSGKSTIIGLIERFYDPLKGTVKIDGRDIRSYHLRSLRKYISLVSQEP 1080
Cdd:PRK13652 8 DLCYSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLVFQNP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1081 --MLFAGTIRENIMYGGTSDKIDESEII----EAAKAANAHDFITSLSNgydtncgdkgvQLSGGQKQRIAIARAVLKNP 1154
Cdd:PRK13652 88 ddQIFSPTVEQDIAFGPINLGLDEETVAhrvsSALHMLGLEELRDRVPH-----------HLSGGEKKRVAIAGVIAMEP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15232977 1155 SVLLLDEATSALDSKSERVVQDALERVMV--GRTSIMIAHRLSTI-QNCDMIVVLGKGKIVESGT 1216
Cdd:PRK13652 157 QVLVLDEPTAGLDPQGVKELIDFLNDLPEtyGMTVIFSTHQLDLVpEMADYIYVMDKGRIVAYGT 221
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
998-1216 |
1.48e-19 |
|
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: 93.98 E-value: 1.48e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 998 LNVDFAYPTRPDVVIfENFSIEIDEGKSTAIVGTSGSGKS----TIIGLIERFYDPLKGTVKIDGRDIRSYHLRSLRKY- 1072
Cdd:COG4172 12 LSVAFGQGGGTVEAV-KGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERELRRIr 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1073 ---ISLVSQEPM-----LFagTIRENIM-----YGGTSDKIDESEIIE---------AAKAANA--Hdfitslsngydtn 1128
Cdd:COG4172 91 gnrIAMIFQEPMtslnpLH--TIGKQIAevlrlHRGLSGAAARARALEllervgipdPERRLDAypH------------- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1129 cgdkgvQLSGGQKQRIAIARAVLKNPSVLLLDEATSALDskserV-VQ-------DALERVMvGRTSIMIAHRLSTIQN- 1199
Cdd:COG4172 156 ------QLSGGQRQRVMIAMALANEPDLLIADEPTTALD-----VtVQaqildllKDLQREL-GMALLLITHDLGVVRRf 223
|
250
....*....|....*..
gi 15232977 1200 CDMIVVLGKGKIVESGT 1216
Cdd:COG4172 224 ADRVAVMRQGEIVEQGP 240
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
373-582 |
1.59e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 91.07 E-value: 1.59e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 373 ETTIFDDLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYDPIAGEILI-DGVSIDKLQVNW---------------LRSQ 436
Cdd:PRK13631 38 ELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVgDIYIGDKKNNHElitnpyskkiknfkeLRRR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 437 MGLVSQEP--VLFATSITENILFG-------KEDASLDEVVEAAKASNAHTFISQFPLGyktqvgergvqMSGGQKQRIA 507
Cdd:PRK13631 118 VSMVFQFPeyQLFKDTIEKDIMFGpvalgvkKSEAKKLAKFYLNKMGLDDSYLERSPFG-----------LSGGQKRRVA 186
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15232977 508 IARAIIKSPKILLLDEATSALDSESER-VVQESLDNASIGRTTIVIAHRLSTIRN-ADVICVIHNGQIVETGSHEEL 582
Cdd:PRK13631 187 IAGILAIQPEILIFDEPTAGLDPKGEHeMMQLILDAKANNKTVFVITHTMEHVLEvADEVIVMDKGKILKTGTPYEI 263
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
377-554 |
1.71e-19 |
|
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: 88.65 E-value: 1.71e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 377 FDDLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYDPIAGEIL-------IDGVSIDKLQVNWLRSQ-MGLVSQepvlFA 448
Cdd:COG4778 27 LDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILvrhdggwVDLAQASPREILALRRRtIGYVSQ----FL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 449 TSI----TENILfgkEDASLDEVVEAAKASN-AHTFISQFplgyktQVGERGVQM-----SGGQKQRIAIARAIIKSPKI 518
Cdd:COG4778 103 RVIprvsALDVV---AEPLLERGVDREEARArARELLARL------NLPERLWDLppatfSGGEQQRVNIARGFIADPPL 173
|
170 180 190
....*....|....*....|....*....|....*..
gi 15232977 519 LLLDEATSALDSESERVVQESLDNASIGRTTIV-IAH 554
Cdd:COG4778 174 LLLDEPTASLDAANRAVVVELIEEAKARGTAIIgIFH 210
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
355-574 |
1.84e-19 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 94.41 E-value: 1.84e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 355 MKGEVEFNHVKFTYLSRPETT-IFDDLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYDPIAGEILIDGVSIDKLQVNWL 433
Cdd:PRK10535 1 MTALLELKDIRRSYPSGEEQVeVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 434 ----RSQMGLVSQEPVLFA-TSITENILFGKEDASLDEvveAAKASNAHTFISQfpLGYKTQVGERGVQMSGGQKQRIAI 508
Cdd:PRK10535 81 aqlrREHFGFIFQRYHLLShLTAAQNVEVPAVYAGLER---KQRLLRAQELLQR--LGLEDRVEYQPSQLSGGQQQRVSI 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15232977 509 ARAIIKSPKILLLDEATSALDSESERVVQESLDN-ASIGRTTIVIAHRLSTIRNADVICVIHNGQIV 574
Cdd:PRK10535 156 ARALMNGGQVILADEPTGALDSHSGEEVMAILHQlRDRGHTVIIVTHDPQVAAQAERVIEIRDGEIV 222
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1012-1216 |
2.05e-19 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 89.45 E-value: 2.05e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1012 IFENFSIEIDEGKSTAIVGTSGSGKSTIIGLIERFYDPLKGTVKIDGRDIRSYHLRSLRKYISLVSQEPML-FAGTIREN 1090
Cdd:PRK13548 17 LLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVLPQHSSLsFPFTVEEV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1091 I-M--YGGTSDKIDESEIIEAAKAANAhdfITSLSNGYDTncgdkgvQLSGGQKQRIAIARaVL-------KNPSVLLLD 1160
Cdd:PRK13548 97 VaMgrAPHGLSRAEDDALVAAALAQVD---LAHLAGRDYP-------QLSGGEQQRVQLAR-VLaqlwepdGPPRWLLLD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15232977 1161 EATSALD-SKSERVVQDALERVMV-GRTSIMIAHRLS-TIQNCDMIVVLGKGKIVESGT 1216
Cdd:PRK13548 166 EPTSALDlAHQHHVLRLARQLAHErGLAVIVVLHDLNlAARYADRIVLLHQGRLVADGT 224
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
714-960 |
2.15e-19 |
|
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349986 [Multi-domain] Cd Length: 292 Bit Score: 90.18 E-value: 2.15e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 714 IYVLLFVGLAIFSFLVNISQHYGFAYMGEYLTKRIREQMLSKILTFEVNWFDidDNSSGAICSRLAKDANVVRSMVGDRM 793
Cdd:cd18542 40 LLALLILGVALLRGVFRYLQGYLAEKASQKVAYDLRNDLYDHLQRLSFSFHD--KARTGDLMSRCTSDVDTIRRFLAFGL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 794 SLLVQTISAVIIACIIGLVIAWRLAIVMISVQPLIVVCFYTQRVLLKSLSEKASKAQDESSKLAAEAVSNIRTITAFSSQ 873
Cdd:cd18542 118 VELVRAVLLFIGALIIMFSINWKLTLISLAIIPFIALFSYVFFKKVRPAFEEIREQEGELNTVLQENLTGVRVVKAFARE 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 874 ERIIKLLKKVQEGPRRESVHRSWLAGIVLGTSRSLITCTSALNFWYGGRLIADGKIVSKAFFeIFLIFVTT--------G 945
Cdd:cd18542 198 DYEIEKFDKENEEYRDLNIKLAKLLAKYWPLMDFLSGLQIVLVLWVGGYLVINGEITLGELV-AFISYLWMliwpvrqlG 276
|
250
....*....|....*
gi 15232977 946 RVIADAGTMTTDLAR 960
Cdd:cd18542 277 RLINDMSRASASAER 291
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
1017-1222 |
2.42e-19 |
|
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: 88.37 E-value: 2.42e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1017 SIEIDEGKSTAIVGTSGSGKSTIIGLIERFYDPLKGTVKIDGRDIRSYHL-RSLRKYISLVSQEPMLFAG-TIRENIMYG 1094
Cdd:cd03218 20 SLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMhKRARLGIGYLPQEASIFRKlTVEENILAV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1095 GTSDKIDESEIIEAAKAAnAHDF-ITSLSNgydtncgDKGVQLSGGQKQRIAIARAVLKNPSVLLLDEATSALDSKS--- 1170
Cdd:cd03218 100 LEIRGLSKKEREEKLEEL-LEEFhITHLRK-------SKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVDPIAvqd 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15232977 1171 -ERVVQDALERVMvgrtSIMIA-HRLS-TIQNCDMIVVLGKGKIVESGTHSSLLE 1222
Cdd:cd03218 172 iQKIIKILKDRGI----GVLITdHNVReTLSITDRAYIIYEGKVLAEGTPEEIAA 222
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1005-1215 |
2.56e-19 |
|
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: 88.19 E-value: 2.56e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1005 PTRPDVVIFENFSIEIDEGKSTAIVGTSGSGKSTIIGLIERFYDPLKGTVKIDGRDIRSYHLRSLRKyISLVSQEPMLFA 1084
Cdd:cd03266 13 DVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARRR-LGFVSDSTGLYD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1085 G-TIRENIMYGGTsdkideseiIEAAKAANAHDFITSLSNGYDTN--CGDKGVQLSGGQKQRIAIARAVLKNPSVLLLDE 1161
Cdd:cd03266 92 RlTARENLEYFAG---------LYGLKGDELTARLEELADRLGMEelLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDE 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 15232977 1162 ATSALDSKSERVVQDALERVM-VGRTSIMIAHRLSTIQN-CDMIVVLGKGKIVESG 1215
Cdd:cd03266 163 PTTGLDVMATRALREFIRQLRaLGKCILFSTHIMQEVERlCDRVVVLHRGRVVYEG 218
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
359-587 |
2.93e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 89.79 E-value: 2.93e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 359 VEFNHVKFTYlsRPETTIFD----DLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYDPI-----AGEILIDGVSIDKlQ 429
Cdd:PRK13643 2 IKFEKVNYTY--QPNSPFASralfDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTegkvtVGDIVVSSTSKQK-E 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 430 VNWLRSQMGLVSQEP--VLFATSITENILFGKEDASLDEVvEAAKASNAHTFIsqfpLGYKTQVGERG-VQMSGGQKQRI 506
Cdd:PRK13643 79 IKPVRKKVGVVFQFPesQLFEETVLKDVAFGPQNFGIPKE-KAEKIAAEKLEM----VGLADEFWEKSpFELSGGQMRRV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 507 AIARAIIKSPKILLLDEATSALDSESERVVQESLDNA-SIGRTTIVIAHRLSTIRN-ADVICVIHNGQIVETGSHEELLK 584
Cdd:PRK13643 154 AIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIhQSGQTVVLVTHLMDDVADyADYVYLLEKGHIISCGTPSDVFQ 233
|
...
gi 15232977 585 RID 587
Cdd:PRK13643 234 EVD 236
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1006-1221 |
3.60e-19 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 88.98 E-value: 3.60e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1006 TRPDVVIFENFSIEIDEGKSTAIVGTSGSGKSTIIGLIERFYDPLKGTVKIDGRDI----RSYHlRSLRKYISLVSQEPm 1081
Cdd:PRK10419 21 KHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLaklnRAQR-KAFRRDIQMVFQDS- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1082 LFAGTIRENImyggtSDKIDE-----SEIIEAAKAANAHDFITSLsnGYDTNCGDK-GVQLSGGQKQRIAIARAVLKNPS 1155
Cdd:PRK10419 99 ISAVNPRKTV-----REIIREplrhlLSLDKAERLARASEMLRAV--DLDDSVLDKrPPQLSGGQLQRVCLARALAVEPK 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15232977 1156 VLLLDEATSALDskseRVVQ----DALERVM--VGRTSIMIAHRLSTIQN-CDMIVVLGKGKIVESGTHSSLL 1221
Cdd:PRK10419 172 LLILDEAVSNLD----LVLQagviRLLKKLQqqFGTACLFITHDLRLVERfCQRVMVMDNGQIVETQPVGDKL 240
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
378-582 |
4.48e-19 |
|
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: 87.43 E-value: 4.48e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 378 DDLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYDPIAGEILIDGVSIDKLQVNwLRSQMGLVSQEPVLfatsitENILF 457
Cdd:cd03265 17 RGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPRE-VRRRIGIVFQDLSV------DDELT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 458 GKED----ASLDEVVEAAKASNAHTFISQFPLGyktQVGERGVQ-MSGGQKQRIAIARAIIKSPKILLLDEATSALDSES 532
Cdd:cd03265 90 GWENlyihARLYGVPGAERRERIDELLDFVGLL---EAADRLVKtYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQT 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15232977 533 ERVVQESLD--NASIGRTTIVIAHRLSTIRN-ADVICVIHNGQIVETGSHEEL 582
Cdd:cd03265 167 RAHVWEYIEklKEEFGMTILLTTHYMEEAEQlCDRVAIIDHGRIIAEGTPEEL 219
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
1003-1206 |
4.89e-19 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 86.52 E-value: 4.89e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1003 AYPTRPdvvIFENFSIEIDEGKSTAIVGTSGSGKSTIIGLIERFYDPLKGTVKidgrdirsyhlRSLRKYISLVSQ---E 1079
Cdd:NF040873 1 GYGGRP---VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVR-----------RAGGARVAYVPQrseV 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1080 PMLFAGTIRENIMYG--------GTSDKIDESEIIEAAKAANAHDFIT-SLSngydtncgdkgvQLSGGQKQRIAIARAV 1150
Cdd:NF040873 67 PDSLPLTVRDLVAMGrwarrglwRRLTRDDRAAVDDALERVGLADLAGrQLG------------ELSGGQRQRALLAQGL 134
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15232977 1151 LKNPSVLLLDEATSALDSKSERVVQDAL-ERVMVGRTSIMIAHRLSTIQNCDMIVVL 1206
Cdd:NF040873 135 AQEADLLLLDEPTTGLDAESRERIIALLaEEHARGATVVVVTHDLELVRRADPCVLL 191
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
371-584 |
4.94e-19 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 92.80 E-value: 4.94e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 371 RPETTIFDDLCLKIPAGKTVALVGGSGSGKSTVISLLQrFYDP----IAGEILIDGVSIDKlqvnwlrSQMGLVS---QE 443
Cdd:TIGR00955 35 RPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALA-FRSPkgvkGSGSVLLNGMPIDA-------KEMRAISayvQQ 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 444 PVLFATSIT--ENILFG-----KEDASLDEVVEAAKA--------SNAHTFIsqfplgyktQVGERGVQMSGGQKQRIAI 508
Cdd:TIGR00955 107 DDLFIPTLTvrEHLMFQahlrmPRRVTKKEKRERVDEvlqalglrKCANTRI---------GVPGRVKGLSGGERKRLAF 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15232977 509 ARAIIKSPKILLLDEATSALDSES-ERVVQESLDNASIGRTTIVIAHRLST--IRNADVICVIHNGQIVETGSHEELLK 584
Cdd:TIGR00955 178 ASELLTDPPLLFCDEPTSGLDSFMaYSVVQVLKGLAQKGKTIICTIHQPSSelFELFDKIILMAEGRVAYLGSPDQAVP 256
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1015-1216 |
4.97e-19 |
|
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: 88.17 E-value: 4.97e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1015 NFSIEIDEGKSTAIVGTSGSGKSTIIGLIERFYDPLKGTVKIDGRDI---RSYHLRSL---RKYislvsQEPMLFAG-TI 1087
Cdd:COG0411 22 DVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDItglPPHRIARLgiaRTF-----QNPRLFPElTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1088 RENIMYGGT---------------SDKIDESEIIEAAKAANAhdfITSLSNGYDTNCGDkgvqLSGGQKQRIAIARAVLK 1152
Cdd:COG0411 97 LENVLVAAHarlgrgllaallrlpRARREEREARERAEELLE---RVGLADRADEPAGN----LSYGQQRRLEIARALAT 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15232977 1153 NPSVLLLDEATSALDSK-SERVVqDALERV--MVGRTSIMIAHRLSTIQN-CDMIVVLGKGKIVESGT 1216
Cdd:COG0411 170 EPKLLLLDEPAAGLNPEeTEELA-ELIRRLrdERGITILLIEHDMDLVMGlADRIVVLDFGRVIAEGT 236
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
702-929 |
5.78e-19 |
|
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349985 [Multi-domain] Cd Length: 293 Bit Score: 89.01 E-value: 5.78e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 702 LTSHDQIKEKTRIYVLLFVGLAIFSFLVNISQHYGFAYMGEYLTKRIREQMLSKILTFEVNWFDidDNSSGAICSRLAKD 781
Cdd:cd18541 29 LTAGTLTASQLLRYALLILLLALLIGIFRFLWRYLIFGASRRIEYDLRNDLFAHLLTLSPSFYQ--KNRTGDLMARATND 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 782 ANVVRSMVGDRMSLLVQTISAVIIACIIGLVIAWRLAIVMISVQPLIVVCFYTQRVLLKSLSEKASKAQDESSKLAAEAV 861
Cdd:cd18541 107 LNAVRMALGPGILYLVDALFLGVLVLVMMFTISPKLTLIALLPLPLLALLVYRLGKKIHKRFRKVQEAFSDLSDRVQESF 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15232977 862 SNIRTITAFSSQERIIKLLKKVQEGPRRESVHRSWLAGIVLGTSRSLITCTSALNFWYGGRLIADGKI 929
Cdd:cd18541 187 SGIRVIKAFVQEEAEIERFDKLNEEYVEKNLRLARVDALFFPLIGLLIGLSFLIVLWYGGRLVIRGTI 254
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
305-555 |
7.33e-19 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 91.79 E-value: 7.33e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 305 ITYGGVS-----LGQSLSNLKYFSEAF---VAW----ERI---LEVIKRVPDIDSNkkEGQILERMKGEVEFNHVKftyL 369
Cdd:COG4178 296 ITLGGLMqaasaFGQVQGALSWFVDNYqslAEWratvDRLagfEEALEAADALPEA--ASRIETSEDGALALEDLT---L 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 370 SRPE-TTIFDDLCLKIPAGKTVALVGGSGSGKST---VISLLQRFYDpiaGEILI-DGvsidklqvnwlrSQMGLVSQEP 444
Cdd:COG4178 371 RTPDgRPLLEDLSLSLKPGERLLITGPSGSGKSTllrAIAGLWPYGS---GRIARpAG------------ARVLFLPQRP 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 445 VLFATSITENILF--GKEDASLDEVVEAAKASNAHTFISQFplgykTQVGERGVQMSGGQKQRIAIARAIIKSPKILLLD 522
Cdd:COG4178 436 YLPLGTLREALLYpaTAEAFSDAELREALEAVGLGHLAERL-----DEEADWDQVLSLGEQQRLAFARLLLHKPDWLFLD 510
|
250 260 270
....*....|....*....|....*....|....*..
gi 15232977 523 EATSALDSESE----RVVQESLDNASIgrttIVIAHR 555
Cdd:COG4178 511 EATSALDEENEaalyQLLREELPGTTV----ISVGHR 543
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
989-1221 |
1.21e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 87.46 E-value: 1.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 989 EKIKGQITFLNVDFAYPTRPDV---------VIFENFSIEIDEGKSTAIVGTSGSGKSTIIGLIERFYDPLKG-----TV 1054
Cdd:PRK14271 4 ERLGGQSGAADVDAAAPAMAAVnltlgfagkTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1055 KIDGRDIRSYH-LRSLRKYISLVSQEPMLFAGTIRENIMYGGTSDKIDESEiiEAAKAANAHDFITSLSNGYDTNCGDKG 1133
Cdd:PRK14271 84 LLGGRSIFNYRdVLEFRRRVGMLFQRPNPFPMSIMDNVLAGVRAHKLVPRK--EFRGVAQARLTEVGLWDAVKDRLSDSP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1134 VQLSGGQKQRIAIARAVLKNPSVLLLDEATSALDSKSERVVQDALERVMVGRTSIMIAHRLSTIQN-CDMIVVLGKGKIV 1212
Cdd:PRK14271 162 FRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAQAARiSDRAALFFDGRLV 241
|
....*....
gi 15232977 1213 ESGTHSSLL 1221
Cdd:PRK14271 242 EEGPTEQLF 250
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
1014-1215 |
1.45e-18 |
|
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: 85.35 E-value: 1.45e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1014 ENFSIEIDEGKSTAIVGTSGSGKSTIIGLIERFYDPLKGTVKIDGRDIRsyHLRSLRKYISLVSQEPMLFAG-TIRENIM 1092
Cdd:cd03268 17 DDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQ--KNIEALRRIGALIEAPGFYPNlTARENLR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1093 YGGTSDKIDESEIIEAAKAANAHDFitslsngydtncGDKGV-QLSGGQKQRIAIARAVLKNPSVLLLDEATSALDSKSE 1171
Cdd:cd03268 95 LLARLLGIRKKRIDEVLDVVGLKDS------------AKKKVkGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPDGI 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 15232977 1172 RVVQDALERVM-VGRTSIMIAHRLSTIQN-CDMIVVLGKGKIVESG 1215
Cdd:cd03268 163 KELRELILSLRdQGITVLISSHLLSEIQKvADRIGIINKGKLIEEG 208
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
364-587 |
1.81e-18 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 86.74 E-value: 1.81e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 364 VKFTYLSRPETTIFDDLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYDPIAGEILIDGVSIDKLQVNWL---RSQMGLV 440
Cdd:PRK11831 10 MRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLytvRKRMSML 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 441 SQEPVLFA-TSITENILFG-KEDASLDEVVeaakasnAHTFIsqfpLGYKTQVGERGV------QMSGGQKQRIAIARAI 512
Cdd:PRK11831 90 FQSGALFTdMNVFDNVAYPlREHTQLPAPL-------LHSTV----MMKLEAVGLRGAaklmpsELSGGMARRAALARAI 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15232977 513 IKSPKILLLDEATSALDSESERVVQESLD--NASIGRTTIVIAHRLSTIRN-ADVICVIHNGQIVETGSHEELLKRID 587
Cdd:PRK11831 159 ALEPDLIMFDEPFVGQDPITMGVLVKLISelNSALGVTCVVVSHDVPEVLSiADHAYIVADKKIVAHGSAQALQANPD 236
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
386-582 |
1.86e-18 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 90.50 E-value: 1.86e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 386 AGKTVALVGGSGSGKSTVISLLQRFYDPIAGEILIDGVSIDKLQVNwLRSQMG--LVSQEPVLFAT-SITENILFG--KE 460
Cdd:PRK15439 36 AGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPA-KAHQLGiyLVPQEPLLFPNlSVKENILFGlpKR 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 461 DASLDEVVEAAKASNAHtfisqfpLGYKTQVGERGVqmsgGQKQRIAIARAIIKSPKILLLDEATSALD-SESERVVQE- 538
Cdd:PRK15439 115 QASMQKMKQLLAALGCQ-------LDLDSSAGSLEV----ADRQIVEILRGLMRDSRILILDEPTASLTpAETERLFSRi 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 15232977 539 -SLDNASIGrttIV-IAHRLSTIRN-ADVICVIHNGQIVETGSHEEL 582
Cdd:PRK15439 184 rELLAQGVG---IVfISHKLPEIRQlADRISVMRDGTIALSGKTADL 227
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
369-583 |
2.52e-18 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 86.43 E-value: 2.52e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 369 LSRPETTIFDDLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYDPIAGEILIDGvsiDKLQ------------------V 430
Cdd:COG4167 21 FRRQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILING---HKLEygdykyrckhirmifqdpN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 431 NWL--RSQMGLVSQEPVLFATSITENilfgkedASLDEVVEAAKasnahtfisqfplgyktQVG------ERGVQM-SGG 501
Cdd:COG4167 98 TSLnpRLNIGQILEEPLRLNTDLTAE-------EREERIFATLR-----------------LVGllpehaNFYPHMlSSG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 502 QKQRIAIARAIIKSPKILLLDEATSALDSeSERV--------VQESLdnasiGRTTIVIAHRLSTIRN-ADVICVIHNGQ 572
Cdd:COG4167 154 QKQRVALARALILQPKIIIADEALAALDM-SVRSqiinlmleLQEKL-----GISYIYVSQHLGIVKHiSDKVLVMHQGE 227
|
250
....*....|.
gi 15232977 573 IVETGSHEELL 583
Cdd:COG4167 228 VVEYGKTAEVF 238
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
360-540 |
2.99e-18 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 86.07 E-value: 2.99e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 360 EFNHVKFTY-LSRPETTIFDDLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYDPIAGEILIDGVSIDKLQVNwlRsqmG 438
Cdd:COG4525 5 TVRHVSVRYpGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGAD--R---G 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 439 LVSQEPVLFA-TSITENILFGKEdasLDEVVEAAKASNAHTFISQFPLGyktQVGERGV-QMSGGQKQRIAIARAIIKSP 516
Cdd:COG4525 80 VVFQKDALLPwLNVLDNVAFGLR---LRGVPKAERRARAEELLALVGLA---DFARRRIwQLSGGMRQRVGIARALAADP 153
|
170 180
....*....|....*....|....
gi 15232977 517 KILLLDEATSALDSESERVVQESL 540
Cdd:COG4525 154 RFLLMDEPFGALDALTREQMQELL 177
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
999-1167 |
3.25e-18 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 89.74 E-value: 3.25e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 999 NVDFAYPTRPdvvIFENFSIEIDEGKSTAIVGTSGSGKSTIIGLIERFYDPLKGTVKIDgRDIRsyhlrslrkyISLVSQ 1078
Cdd:COG0488 3 NLSKSFGGRP---LLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIP-KGLR----------IGYLPQ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1079 EPMLFAG-TIRENIMYG--GTSDKIDESEIIEAA---------KAANAHDFITSLsNGYD---------------TNCGD 1131
Cdd:COG0488 69 EPPLDDDlTVLDTVLDGdaELRALEAELEELEAKlaepdedleRLAELQEEFEAL-GGWEaearaeeilsglgfpEEDLD 147
|
170 180 190
....*....|....*....|....*....|....*..
gi 15232977 1132 KGV-QLSGGQKQRIAIARAVLKNPSVLLLDEATSALD 1167
Cdd:COG0488 148 RPVsELSGGWRRRVALARALLSEPDLLLLDEPTNHLD 184
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1012-1216 |
3.63e-18 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 87.83 E-value: 3.63e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1012 IFENFSIEIDEGKSTAIVGTSGSGKSTIIGLIERFYDPLKGTVKIDGRDIRSYHLRSLRkyISLVSQEPMLFAG-TIREN 1090
Cdd:PRK10851 17 VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDRK--VGFVFQHYALFRHmTVFDN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1091 IMYGGT----SDKIDESEIieAAKAANAHDFI--TSLSNGYDTncgdkgvQLSGGQKQRIAIARAVLKNPSVLLLDEATS 1164
Cdd:PRK10851 95 IAFGLTvlprRERPNAAAI--KAKVTQLLEMVqlAHLADRYPA-------QLSGGQKQRVALARALAVEPQILLLDEPFG 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15232977 1165 ALDSKservVQDALERVM------VGRTSIMIAH-RLSTIQNCDMIVVLGKGKIVESGT 1216
Cdd:PRK10851 166 ALDAQ----VRKELRRWLrqlheeLKFTSVFVTHdQEEAMEVADRVVVMSQGNIEQAGT 220
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
359-580 |
3.83e-18 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 87.19 E-value: 3.83e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 359 VEFNHVKFTYLSRPettIFDDLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYDPIAGEILIDGVSIDKlQVNWLRSQMG 438
Cdd:PRK13536 42 IDLAGVSKSYGDKA---VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPA-RARLARARIG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 439 LVSQEPVL-FATSITENIL-----FGKEDASLDEVV----EAAKASNahtfisqfplgyktQVGERGVQMSGGQKQRIAI 508
Cdd:PRK13536 118 VVPQFDNLdLEFTVRENLLvfgryFGMSTREIEAVIpsllEFARLES--------------KADARVSDLSGGMKRRLTL 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15232977 509 ARAIIKSPKILLLDEATSALDSESERVVQESLDN-ASIGRTTIVIAHRLSTI-RNADVICVIHNG-QIVETGSHE 580
Cdd:PRK13536 184 ARALINDPQLLILDEPTTGLDPHARHLIWERLRSlLARGKTILLTTHFMEEAeRLCDRLCVLEAGrKIAEGRPHA 258
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
359-585 |
4.22e-18 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 86.78 E-value: 4.22e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 359 VEFNHVKFTYlsrPETTIFDDLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYDPIAGEILIDGVSIDKlQVNWLRSQMG 438
Cdd:PRK13537 8 IDFRNVEKRY---GDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPS-RARHARQRVG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 439 LVSQ----EPVLfatSITENIL-----FGKEDASLDEVV----EAAKASNAHtfisqfplgyKTQVGErgvqMSGGQKQR 505
Cdd:PRK13537 84 VVPQfdnlDPDF---TVRENLLvfgryFGLSAAAARALVppllEFAKLENKA----------DAKVGE----LSGGMKRR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 506 IAIARAIIKSPKILLLDEATSALDSESERVVQESLDN-ASIGRTTIVIAHRLSTI-RNADVICVIHNGQIVETGSHEELL 583
Cdd:PRK13537 147 LTLARALVNDPDVLVLDEPTTGLDPQARHLMWERLRSlLARGKTILLTTHFMEEAeRLCDRLCVIEEGRKIAEGAPHALI 226
|
..
gi 15232977 584 KR 585
Cdd:PRK13537 227 ES 228
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
359-582 |
4.53e-18 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 87.45 E-value: 4.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 359 VEFNHVKfTYLSRpeTTIFDDLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYDPIAGEILIDGVSIDKLQVNwlRSQMG 438
Cdd:PRK10851 3 IEIANIK-KSFGR--TQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHAR--DRKVG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 439 LVSQEPVLFA-TSITENILFG----------------KEDASLDEVVEAAKASNahtfisQFPlgyktqvgergVQMSGG 501
Cdd:PRK10851 78 FVFQHYALFRhMTVFDNIAFGltvlprrerpnaaaikAKVTQLLEMVQLAHLAD------RYP-----------AQLSGG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 502 QKQRIAIARAIIKSPKILLLDEATSALDSESERVVQESLDN--ASIGRTTIVIAH-RLSTIRNADVICVIHNGQIVETGS 578
Cdd:PRK10851 141 QKQRVALARALAVEPQILLLDEPFGALDAQVRKELRRWLRQlhEELKFTSVFVTHdQEEAMEVADRVVVMSQGNIEQAGT 220
|
....
gi 15232977 579 HEEL 582
Cdd:PRK10851 221 PDQV 224
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
369-583 |
5.20e-18 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 85.21 E-value: 5.20e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 369 LSRPETTIFDDLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYDPIAGEILIDGVSIDKLQVnWLRSQM-GLVSQEPVL- 446
Cdd:PRK13548 10 VRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSP-AELARRrAVLPQHSSLs 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 447 FATSITENILFGK-----EDASLDEVVEAAKASnahTFISQFplgyktqvGERGV-QMSGGQKQRIAIARAII------K 514
Cdd:PRK13548 89 FPFTVEEVVAMGRaphglSRAEDDALVAAALAQ---VDLAHL--------AGRDYpQLSGGEQQRVQLARVLAqlwepdG 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15232977 515 SPKILLLDEATSALD-SESERVVQ--ESLDNASiGRTTIVIAHRLS-TIRNADVICVIHNGQIVETGSHEELL 583
Cdd:PRK13548 158 PPRWLLLDEPTSALDlAHQHHVLRlaRQLAHER-GLAVIVVLHDLNlAARYADRIVLLHQGRLVADGTPAEVL 229
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
995-1218 |
5.95e-18 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 84.68 E-value: 5.95e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 995 ITFLNVDFAYPTRPdvvIFENFSIEIDEGKSTAIVGTSGSGKSTIIGLIERFYDPLKGTVKIDG------RDIRSYHLRS 1068
Cdd:COG4161 3 IQLKNINCFYGSHQ---ALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGhqfdfsQKPSEKAIRL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1069 LRKYISLVSQE----PMLfagTIRENIMYGGTS-DKIDESEIIEAAKAANAHDFITSLSNGYDtncgdkgVQLSGGQKQR 1143
Cdd:COG4161 80 LRQKVGMVFQQynlwPHL---TVMENLIEAPCKvLGLSKEQAREKAMKLLARLRLTDKADRFP-------LHLSGGQQQR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15232977 1144 IAIARAVLKNPSVLLLDEATSALDSK-SERVVQDALERVMVGRTSIMIAHRLSTIQNCDMIVV-LGKGKIVESGTHS 1218
Cdd:COG4161 150 VAIARALMMEPQVLLFDEPTAALDPEiTAQVVEIIRELSQTGITQVIVTHEVEFARKVASQVVyMEKGRIIEQGDAS 226
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
374-583 |
6.19e-18 |
|
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: 84.52 E-value: 6.19e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 374 TTIFDDLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYDPIAGEILIDGVSIDKLQVNwLRSQMGL--VSQEPVLFAT-S 450
Cdd:cd03218 13 RKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMH-KRARLGIgyLPQEASIFRKlT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 451 ITENILFGKEDASLDEvveAAKASNAHTFISQFPLgyKTQVGERGVQMSGGQKQRIAIARAIIKSPKILLLDEATSALD- 529
Cdd:cd03218 92 VEENILAVLEIRGLSK---KEREEKLEELLEEFHI--THLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVDp 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15232977 530 ---SESERVVQEsLDNASIG--------RTTIVIAHRlstirnadvICVIHNGQIVETGSHEELL 583
Cdd:cd03218 167 iavQDIQKIIKI-LKDRGIGvlitdhnvRETLSITDR---------AYIIYEGKVLAEGTPEEIA 221
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
81-332 |
6.95e-18 |
|
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349986 [Multi-domain] Cd Length: 292 Bit Score: 85.56 E-value: 6.95e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 81 VVALLYVACGSWVICFLEGYCWTRTGERQAARMREKYLRAVLRQDVGYFDLhvTSTSDVITSISSDSLVIQDFLSEKLPN 160
Cdd:cd18542 42 ALLILGVALLRGVFRYLQGYLAEKASQKVAYDLRNDLYDHLQRLSFSFHDK--ARTGDLMSRCTSDVDTIRRFLAFGLVE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 161 FLMNASAFVASYIVSFILMWRLTIVGFPFIILLLVPGLMYGRALVSISRKIHEQYNEAGSIAEQAISSVRTVYAFGSENK 240
Cdd:cd18542 120 LVRAVLLFIGALIIMFSINWKLTLISLAIIPFIALFSYVFFKKVRPAFEEIREQEGELNTVLQENLTGVRVVKAFAREDY 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 241 MIGKFSTALRGSVKLGLRQGLAKGITIG-SNGVTHAIWAFLTWYGSRLVMNHGSKGGTVFVVISCITYggVS-----LGQ 314
Cdd:cd18542 200 EIEKFDKENEEYRDLNIKLAKLLAKYWPlMDFLSGLQIVLVLWVGGYLVINGEITLGELVAFISYLWM--LIwpvrqLGR 277
|
250
....*....|....*...
gi 15232977 315 SLSNlkyFSEAFVAWERI 332
Cdd:cd18542 278 LIND---MSRASASAERI 292
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
999-1222 |
9.11e-18 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 84.84 E-value: 9.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 999 NVDFAYPTRpdvVIFENFSIEIDEGKSTAIVGTSGSGKSTIIGLIERFYDPLKGTVKIDGRDIRSYHLRSL-RKYISLVS 1077
Cdd:PRK10575 16 NVSFRVPGR---TLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFaRKVAYLPQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1078 QEPMLFAGTIRENIMYG-----------GTSD--KIDESEIIEAAKAAnAHDFITSlsngydtncgdkgvqLSGGQKQRI 1144
Cdd:PRK10575 93 QLPAAEGMTVRELVAIGrypwhgalgrfGAADreKVEEAISLVGLKPL-AHRLVDS---------------LSGGERQRA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1145 AIARAVLKNPSVLLLDEATSALDSKSERVVQDALERV--MVGRTSIMIAHRLS-TIQNCDMIVVLGKGKIVESGTHSSLL 1221
Cdd:PRK10575 157 WIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLsqERGLTVIAVLHDINmAARYCDYLVALRGGEMIAQGTPAELM 236
|
.
gi 15232977 1222 E 1222
Cdd:PRK10575 237 R 237
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
1017-1220 |
1.00e-17 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 83.73 E-value: 1.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1017 SIEIDEGKSTAIVGTSGSGKST----IIGLIerfyDPLKGTVKIDGRDI--RSYHLRSlRKYISLVSQEPMLFAG-TIRE 1089
Cdd:TIGR03410 20 SLEVPKGEVTCVLGRNGVGKTTllktLMGLL----PVKSGSIRLDGEDItkLPPHERA-RAGIAYVPQGREIFPRlTVEE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1090 NIMYGGTSDKIDESEIIeaakaanahDFITSLSNGYDTNCGDKGVQLSGGQKQRIAIARAVLKNPSVLLLDEATSALDSK 1169
Cdd:TIGR03410 95 NLLTGLAALPRRSRKIP---------DEIYELFPVLKEMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDEPTEGIQPS 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15232977 1170 serVVQDalervmVGRTSIMIAHR--LSTI---QN-------CDMIVVLGKGKIVESGTHSSL 1220
Cdd:TIGR03410 166 ---IIKD------IGRVIRRLRAEggMAILlveQYldfarelADRYYVMERGRVVASGAGDEL 219
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
999-1219 |
1.05e-17 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 83.91 E-value: 1.05e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 999 NVDFAYPTrpDVVIFeNFSIEIDEGKSTAIVGTSGSGKSTIIGLIERFYDPLKGTVKIDG------RDIRSYHLRSLRKY 1072
Cdd:PRK11124 7 GINCFYGA--HQALF-DITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGnhfdfsKTPSDKAIRELRRN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1073 ISLVSQE----PMLfagTIRENIMYGGTS-DKIDESEIIEAAKAANAHDFITSLSNGYDtncgdkgVQLSGGQKQRIAIA 1147
Cdd:PRK11124 84 VGMVFQQynlwPHL---TVQQNLIEAPCRvLGLSKDQALARAEKLLERLRLKPYADRFP-------LHLSGGQQQRVAIA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15232977 1148 RAVLKNPSVLLLDEATSALDSK-SERVVQDALERVMVGRTSIMIAHRLSTIQNCDMIVV-LGKGKIVESGTHSS 1219
Cdd:PRK11124 154 RALMMEPQVLLFDEPTAALDPEiTAQIVSIIRELAETGITQVIVTHEVEVARKTASRVVyMENGHIVEQGDASC 227
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
32-523 |
1.06e-17 |
|
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: 88.32 E-value: 1.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 32 WILMALGLIGAVGDGFITPVVVFIfNTLLNnlGTSSSNNKTFMQTIsknVVALLYVACGSWVICFLegycwTRTGERQAA 111
Cdd:COG4615 13 WLLLLALLLGLLSGLANAGLIALI-NQALN--ATGAALARLLLLFA---GLLVLLLLSRLASQLLL-----TRLGQHAVA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 112 RMREKYLRAVLRQDvgYFDLHVTSTSDVITSISSDSLVIQDFLSeKLPNFLMNASAFVASyivsFILMWRLTIVGFPFII 191
Cdd:COG4615 82 RLRLRLSRRILAAP--LERLERIGAARLLAALTEDVRTISQAFV-RLPELLQSVALVLGC----LAYLAWLSPPLFLLTL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 192 LLLVPGLMYGRALVSISRKIHEQYNEAgsiaeqaissvrtvyafgsENKMIGKFSTALRGSVKLGL----RQGLAKG--- 264
Cdd:COG4615 155 VLLGLGVAGYRLLVRRARRHLRRAREA-------------------EDRLFKHFRALLEGFKELKLnrrrRRAFFDEdlq 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 265 ----------ITIGSNGVTHAIWAFLTWYGsrlVMnhgskGGTVFVV-----ISCITYGGVSL---------GQSLSNLK 320
Cdd:COG4615 216 ptaeryrdlrIRADTIFALANNWGNLLFFA---LI-----GLILFLLpalgwADPAVLSGFVLvllflrgplSQLVGALP 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 321 YFSEAFVAWERILEVIKRVPDIDSNKKEGQILERMKG--EVEFNHVKFTYLSRPETTIFD----DLclKIPAGKTVALVG 394
Cdd:COG4615 288 TLSRANVALRKIEELELALAAAEPAAADAAAPPAPADfqTLELRGVTYRYPGEDGDEGFTlgpiDL--TIRRGELVFIVG 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 395 GSGSGKSTVISLLQRFYDPIAGEILIDGVSIDKLQVNWLRSQMGLVSQEPVLFATsiteniLFGKEDASLDEVVEAakas 474
Cdd:COG4615 366 GNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAYRQLFSAVFSDFHLFDR------LLGLDGEADPARARE---- 435
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 15232977 475 nahtFISQFPLGYKTQVgERG----VQMSGGQKQRIAIARAIIKSPKILLLDE 523
Cdd:COG4615 436 ----LLERLELDHKVSV-EDGrfstTDLSQGQRKRLALLVALLEDRPILVFDE 483
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
373-587 |
1.12e-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: 82.57 E-value: 1.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 373 ETTIFDDLCLKIPAGKTVALVGGSGSGKSTVISLLQRF--YDPIAGEILIDGVSIDKLQVNwLRSQMG--LVSQEPVLFA 448
Cdd:cd03217 12 GKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLPPE-ERARLGifLAFQYPPEIP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 449 TSITENILfgkedasldevveaakasnahtfisqfplgyktqvgeRGVQM--SGGQKQRIAIARAIIKSPKILLLDEATS 526
Cdd:cd03217 91 GVKNADFL-------------------------------------RYVNEgfSGGEKKRNEILQLLLLEPDLAILDEPDS 133
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15232977 527 ALDSESERVVQESLDN-ASIGRTTIVIAH--RLSTIRNADVICVIHNGQIVETGShEELLKRID 587
Cdd:cd03217 134 GLDIDALRLVAEVINKlREEGKSVLIITHyqRLLDYIKPDRVHVLYDGRIVKSGD-KELALEIE 196
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
1006-1167 |
1.14e-17 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 82.91 E-value: 1.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1006 TRPDVVIFENFSIEIDEGKSTAIVGTSGSGKSTIIGLIERFYDP---LKGTVKIDGRDIRsyHLRSLRKYISLVSQEPML 1082
Cdd:COG4136 10 TLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLT--ALPAEQRRIGILFQDDLL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1083 FAG-TIRENIMYGgTSDKIDESE----IIEAAKAANAHDFitslsngydtncGDKGV-QLSGGQKQRIAIARAVLKNPSV 1156
Cdd:COG4136 88 FPHlSVGENLAFA-LPPTIGRAQrrarVEQALEEAGLAGF------------ADRDPaTLSGGQRARVALLRALLAEPRA 154
|
170
....*....|.
gi 15232977 1157 LLLDEATSALD 1167
Cdd:COG4136 155 LLLDEPFSKLD 165
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
373-586 |
1.14e-17 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 83.98 E-value: 1.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 373 ETTIFDDLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYDPIAGEILIDGVSIDKLQVNWLRSQMGLVSQEPVlFATSIT 452
Cdd:COG4604 13 GKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLAILRQENH-INSRLT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 453 --ENILFG----------KEDaslDEVVEAAkasnahtfISQFPLgykTQVGERGV-QMSGGQKQRIAIARAIIKSPKIL 519
Cdd:COG4604 92 vrELVAFGrfpyskgrltAED---REIIDEA--------IAYLDL---EDLADRYLdELSGGQRQRAFIAMVLAQDTDYV 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15232977 520 LLDEATSALDSESERVVQESLDNAS--IGRTTIVIAHRLstirN-----ADVICVIHNGQIVETGS-----HEELLKRI 586
Cdd:COG4604 158 LLDEPLNNLDMKHSVQMMKLLRRLAdeLGKTVVIVLHDI----NfascyADHIVAMKDGRVVAQGTpeeiiTPEVLSDI 232
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
1009-1215 |
1.16e-17 |
|
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: 83.10 E-value: 1.16e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1009 DVVIFENFSIEIDEGKSTAIVGTSGSGKSTIIGLIERFYDPLKGTVKIDGRDIRSYHlrslRKYISLVSQEPMLFAG-TI 1087
Cdd:cd03269 12 RVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAA----RNRIGYLPEERGLYPKmKV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1088 RENIMYGGTSDKIDESEIieaakAANAHDFITSLSNGydtNCGDKGV-QLSGGQKQRIAIARAVLKNPSVLLLDEATSAL 1166
Cdd:cd03269 88 IDQLVYLAQLKGLKKEEA-----RRRIDEWLERLELS---EYANKRVeELSKGNQQKVQFIAAVIHDPELLILDEPFSGL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 15232977 1167 DSKSERVVQDAL-ERVMVGRTSIMIAHRLSTIQN-CDMIVVLGKGKIVESG 1215
Cdd:cd03269 160 DPVNVELLKDVIrELARAGKTVILSTHQMELVEElCDRVLLLNKGRAVLYG 210
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
1014-1192 |
1.40e-17 |
|
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: 83.28 E-value: 1.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1014 ENFSIEIDEGKSTAIVGTSGSGKSTIIGLIERFYDPLKGTVKIDGRDIRSYHLRSLrkyisLVSQEPMLFAG-TIRENIM 1092
Cdd:TIGR01184 2 KGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRM-----VVFQNYSLLPWlTVRENIA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1093 YGGTSDKIDESEIiEAAKAANAHDFITSLSNGYDTNCGdkgvQLSGGQKQRIAIARAVLKNPSVLLLDEATSALDSKSER 1172
Cdd:TIGR01184 77 LAVDRVLPDLSKS-ERRAIVEEHIALVGLTEAADKRPG----QLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRG 151
|
170 180
....*....|....*....|..
gi 15232977 1173 VVQDALERVM--VGRTSIMIAH 1192
Cdd:TIGR01184 152 NLQEELMQIWeeHRVTVLMVTH 173
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
370-553 |
1.69e-17 |
|
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: 82.02 E-value: 1.69e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 370 SRPETTIFDDLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYDPIAGEILIDGVSIDKLQVNWLRSQMGLVSQEPVLFAT 449
Cdd:TIGR01189 9 SRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYLGHLPGLKPEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 450 SITENILFGKED-ASLDEVVEAAKASNAHTFISQFPLGyktqvgergvQMSGGQKQRIAIARAIIKSPKILLLDEATSAL 528
Cdd:TIGR01189 89 SALENLHFWAAIhGGAQRTIEDALAAVGLTGFEDLPAA----------QLSAGQQRRLALARLWLSRRPLWILDEPTTAL 158
|
170 180
....*....|....*....|....*
gi 15232977 529 DSESERVVQESLDnASIGRTTIVIA 553
Cdd:TIGR01189 159 DKAGVALLAGLLR-AHLARGGIVLL 182
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1007-1216 |
1.93e-17 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 83.21 E-value: 1.93e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1007 RPDVVIFENFSIEIDEGKSTAIVGTSGSGKSTIIGLIERFYDPLKGTVKIDGRdirsyhlrslrkyislVSqePML-FAG 1085
Cdd:COG1134 36 REEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGR----------------VS--ALLeLGA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1086 ------TIRENI-----MYGGTSDKIDE--SEIIEaakAANAHDFItslsngydtncgDKGVQ-LSGGQKQRIAIARAVL 1151
Cdd:COG1134 98 gfhpelTGRENIylngrLLGLSRKEIDEkfDEIVE---FAELGDFI------------DQPVKtYSSGMRARLAFAVATA 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1152 KNPSVLLLDEATSALDS----KSERVVQDALERvmvGRTSIMIAHRLSTIQN-CDMIVVLGKGKIVESGT 1216
Cdd:COG1134 163 VDPDILLVDEVLAVGDAafqkKCLARIRELRES---GRTVIFVSHSMGAVRRlCDRAIWLEKGRLVMDGD 229
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
359-559 |
2.01e-17 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 82.62 E-value: 2.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 359 VEFNHVKFTYLSRPETTIFDDLCLKipAGKTVALVGGSGSGKSTVISLLQRFYDPIAGEILIDGVSIDKL---QVNWLRS 435
Cdd:PRK10908 2 IRFEHVSKAYLGGRQALQGVTFHMR--PGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLknrEVPFLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 436 QMGLVSQE---------------PVLFATSITENILfGKEDASLDEVVEAAKASNahtfisqFPlgyktqvgergVQMSG 500
Cdd:PRK10908 80 QIGMIFQDhhllmdrtvydnvaiPLIIAGASGDDIR-RRVSAALDKVGLLDKAKN-------FP-----------IQLSG 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 501 GQKQRIAIARAIIKSPKILLLDEATSALDSE-SERVVQESLDNASIGRTTIVIAHRLSTI 559
Cdd:PRK10908 141 GEQQRVGIARAVVNKPAVLLADEPTGNLDDAlSEGILRLFEEFNRVGVTVLMATHDIGLI 200
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
351-582 |
2.16e-17 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 86.91 E-value: 2.16e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 351 ILErMKGEV-EFNHVKftylsrpettIFDDLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYdPIA---GEILIDGvsiD 426
Cdd:PRK13549 5 LLE-MKNITkTFGGVK----------ALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PHGtyeGEIIFEG---E 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 427 KLQVNWLR--SQMGLV--SQEPVLFAT-SITENILFGKEDASLDEVVEAAKASNAHTFISQFPLGYK--TQVGERGvqms 499
Cdd:PRK13549 70 ELQASNIRdtERAGIAiiHQELALVKElSVLENIFLGNEITPGGIMDYDAMYLRAQKLLAQLKLDINpaTPVGNLG---- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 500 GGQKQRIAIARAIIKSPKILLLDEATSALdSESERVVQESL--DNASIGRTTIVIAHRLSTIRN-ADVICVIHNGQIVET 576
Cdd:PRK13549 146 LGQQQLVEIAKALNKQARLLILDEPTASL-TESETAVLLDIirDLKAHGIACIYISHKLNEVKAiSDTICVIRDGRHIGT 224
|
....*.
gi 15232977 577 GSHEEL 582
Cdd:PRK13549 225 RPAAGM 230
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
1007-1236 |
2.27e-17 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 87.41 E-value: 2.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1007 RPDVVIFENFSIEIDEGKSTAIVGTSGSGKSTIIGLIErFYDP----LKGTVKIDGRDIRSYHLRSLRKYIslvsQEPML 1082
Cdd:TIGR00955 35 RPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALA-FRSPkgvkGSGSVLLNGMPIDAKEMRAISAYV----QQDDL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1083 FAG--TIRENIMY--------GGTSDKIDE--SEIIEAakaanahdfiTSLSNGYDTNCGDKGVQ--LSGGQKQRIAIAR 1148
Cdd:TIGR00955 110 FIPtlTVREHLMFqahlrmprRVTKKEKRErvDEVLQA----------LGLRKCANTRIGVPGRVkgLSGGERKRLAFAS 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1149 AVLKNPSVLLLDEATSALDSKS-ERVVQDALERVMVGRTSIMIAHRLST--IQNCDMIVVLGKGKIVESGTHSSLLEkgp 1225
Cdd:TIGR00955 180 ELLTDPPLLFCDEPTSGLDSFMaYSVVQVLKGLAQKGKTIICTIHQPSSelFELFDKIILMAEGRVAYLGSPDQAVP--- 256
|
250
....*....|.
gi 15232977 1226 tgtYFSLAGIQ 1236
Cdd:TIGR00955 257 ---FFSDLGHP 264
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
714-929 |
2.75e-17 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350007 [Multi-domain] Cd Length: 296 Bit Score: 84.10 E-value: 2.75e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 714 IYVLLFVGLAIFSFLVNISQHYGFAYMGEYLTKRIREQMLSKILTFEVNWFDidDNSSGAICSRLAKDANVVRSMVGDRM 793
Cdd:cd18563 44 LLVLGLAGAYVLSALLGILRGRLLARLGERITADLRRDLYEHLQRLSLSFFD--KRQTGSLMSRVTSDTDRLQDFLSDGL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 794 -SLLVQTISAVIIACIIgLVIAWRLAIVMISVQPLIVVCFYTQRVLLKSLSEKASKAQDESSKLAAEAVSNIRTITAFSS 872
Cdd:cd18563 122 pDFLTNILMIIGIGVVL-FSLNWKLALLVLIPVPLVVWGSYFFWKKIRRLFHRQWRRWSRLNSVLNDTLPGIRVVKAFGQ 200
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 873 QERIIKLLKKVQEGPRRES--VHRSWLA-GIVLGTsrsLITCTSALNFWYGGRLIADGKI 929
Cdd:cd18563 201 EKREIKRFDEANQELLDANirAEKLWATfFPLLTF---LTSLGTLIVWYFGGRQVLSGTM 257
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
371-591 |
3.00e-17 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 87.22 E-value: 3.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 371 RPETTIFDDLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYDPIAGEILIDGVSIDKL--QVNWLRSQ------------ 436
Cdd:PRK10261 26 QQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRRRsrQVIELSEQsaaqmrhvrgad 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 437 MGLVSQEPV-----LFAT--SITENIL----FGKEDASLD--EVVEAAKASNAHTFISQFPLgyktqvgergvQMSGGQK 503
Cdd:PRK10261 106 MAMIFQEPMtslnpVFTVgeQIAESIRlhqgASREEAMVEakRMLDQVRIPEAQTILSRYPH-----------QLSGGMR 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 504 QRIAIARAIIKSPKILLLDEATSALDSESE-------RVVQESLdnaSIGrtTIVIAHRLSTIRN-ADVICVIHNGQIVE 575
Cdd:PRK10261 175 QRVMIAMALSCRPAVLIADEPTTALDVTIQaqilqliKVLQKEM---SMG--VIFITHDMGVVAEiADRVLVMYQGEAVE 249
|
250
....*....|....*.
gi 15232977 576 TGSHEELLKRIDGQYT 591
Cdd:PRK10261 250 TGSVEQIFHAPQHPYT 265
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
33-332 |
3.60e-17 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350007 [Multi-domain] Cd Length: 296 Bit Score: 83.71 E-value: 3.60e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 33 ILMALGLIGAVGDGFITPVV--VFIFNTLLNNLGTSSSnnKTFMQTIsknvVALLYVACGSWVICFLEGYCWTRTGERQA 110
Cdd:cd18563 2 ILGFLLMLLGTALGLVPPYLtkILIDDVLIQLGPGGNT--SLLLLLV----LGLAGAYVLSALLGILRGRLLARLGERIT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 111 ARMREKYLRAVLRQDVGYFDLHvtSTSDVITSISSDSLVIQDFLSEKLPNFLMNASAFVASYIVSFILMWRLTIVGF--- 187
Cdd:cd18563 76 ADLRRDLYEHLQRLSLSFFDKR--QTGSLMSRVTSDTDRLQDFLSDGLPDFLTNILMIIGIGVVLFSLNWKLALLVLipv 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 188 PFIILLLVpglMYGRALVSISRKIHEQYNEAGSIAEQAISSVRTVYAFGSENKMIGKFSTALRGSVKLGLRqglakgiti 267
Cdd:cd18563 154 PLVVWGSY---FFWKKIRRLFHRQWRRWSRLNSVLNDTLPGIRVVKAFGQEKREIKRFDEANQELLDANIR--------- 221
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15232977 268 gSNGVTHAIWAFLT-----------WYGSRLVMNHGSKGGTVFVVISCIT--YGGVslgQSLSNL-KYFSEAFVAWERI 332
Cdd:cd18563 222 -AEKLWATFFPLLTfltslgtlivwYFGGRQVLSGTMTLGTLVAFLSYLGmfYGPL---QWLSRLnNWITRALTSAERI 296
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
378-586 |
3.73e-17 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 86.39 E-value: 3.73e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 378 DDLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYDPIAGEILI----DGVSIDKLQVNwLRSQ----MGLVSQEPVLFA- 448
Cdd:TIGR03269 301 DNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdEWVDMTKPGPD-GRGRakryIGILHQEYDLYPh 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 449 TSITENIlfgKEDASLDEVVEAAKASNAHTFISQ-FPLGYKTQVGERGV-QMSGGQKQRIAIARAIIKSPKILLLDEATS 526
Cdd:TIGR03269 380 RTVLDNL---TEAIGLELPDELARMKAVITLKMVgFDEEKAEEILDKYPdELSEGERHRVALAQVLIKEPRIVILDEPTG 456
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15232977 527 ALDSESERVVQESLDNA--SIGRTTIVIAHRLSTIRN-ADVICVIHNGQIVETGSHEELLKRI 586
Cdd:TIGR03269 457 TMDPITKVDVTHSILKAreEMEQTFIIVSHDMDFVLDvCDRAALMRDGKIVKIGDPEEIVEEL 519
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
995-1193 |
3.97e-17 |
|
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: 80.28 E-value: 3.97e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 995 ITFLNVDFAYPTrpDVVIFENFSIEIDEGKSTAIVGTSGSGKSTIIGLIERFYDPLKGTVKIDGRDirsyhlRSLrkyis 1074
Cdd:cd03223 1 IELENLSLATPD--GRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEGE------DLL----- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1075 LVSQEPMLFAGTIRENIMYggTSDKIdeseiieaakaanahdfitslsngydtncgdkgvqLSGGQKQRIAIARAVLKNP 1154
Cdd:cd03223 68 FLPQRPYLPLGTLREQLIY--PWDDV-----------------------------------LSGGEQQRLAFARLLLHKP 110
|
170 180 190
....*....|....*....|....*....|....*....
gi 15232977 1155 SVLLLDEATSALDSKSERVVQDALERVMVgrTSIMIAHR 1193
Cdd:cd03223 111 KFVFLDEATSALDEESEDRLYQLLKELGI--TVISVGHR 147
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
372-584 |
4.68e-17 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 82.53 E-value: 4.68e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 372 PETTIFDDLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYDPIAGEILIDGVSIDKL-------QVNWLRSQM----GLV 440
Cdd:PRK10575 22 PGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWsskafarKVAYLPQQLpaaeGMT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 441 SQEPVLFATSITENIL--FGKEDasldevveAAKASNAHTFISQFPLgyktqvGERGV-QMSGGQKQRIAIARAIIKSPK 517
Cdd:PRK10575 102 VRELVAIGRYPWHGALgrFGAAD--------REKVEEAISLVGLKPL------AHRLVdSLSGGERQRAWIAMLVAQDSR 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 518 ILLLDEATSALDseservvqesldnasIGRTTIVIA--HRLSTIRNADVICVIHN----------------GQIVETGSH 579
Cdd:PRK10575 168 CLLLDEPTSALD---------------IAHQVDVLAlvHRLSQERGLTVIAVLHDinmaarycdylvalrgGEMIAQGTP 232
|
....*
gi 15232977 580 EELLK 584
Cdd:PRK10575 233 AELMR 237
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
373-591 |
4.98e-17 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 85.91 E-value: 4.98e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 373 ETTIFDDLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYdPIAGEILIDGVSIDKL---QVNWLRSQMGLVSQEP----- 444
Cdd:PRK15134 298 HNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLI-NSQGEIWFDGQPLHNLnrrQLLPVRHRIQVVFQDPnssln 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 445 ------------------VLFATSITENILFGKEDASLDevveaakASNAHTFISQFplgyktqvgergvqmSGGQKQRI 506
Cdd:PRK15134 377 prlnvlqiieeglrvhqpTLSAAQREQQVIAVMEEVGLD-------PETRHRYPAEF---------------SGGQRQRI 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 507 AIARAIIKSPKILLLDEATSALDseseRVVQ-------ESLDNASiGRTTIVIAHRLSTIRNA--DVIcVIHNGQIVETG 577
Cdd:PRK15134 435 AIARALILKPSLIILDEPTSSLD----KTVQaqilallKSLQQKH-QLAYLFISHDLHVVRALchQVI-VLRQGEVVEQG 508
|
250
....*....|....
gi 15232977 578 SHEELLKRIDGQYT 591
Cdd:PRK15134 509 DCERVFAAPQQEYT 522
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1007-1232 |
5.75e-17 |
|
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: 87.38 E-value: 5.75e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1007 RPDVvifENFSIEIDEGKSTAIVGTSGSGKSTIIGLIERFYDPLKGTVKIDGRDIRSyHLRSLRKYISLVSQEPMLFAG- 1085
Cdd:TIGR01257 943 RPAV---DRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIET-NLDAVRQSLGMCPQHNILFHHl 1018
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1086 TIRENIM-YGGTSDKIDESEIIEAAkaANAHDfiTSLSNGYDTNCGDkgvqLSGGQKQRIAIARAVLKNPSVLLLDEATS 1164
Cdd:TIGR01257 1019 TVAEHILfYAQLKGRSWEEAQLEME--AMLED--TGLHHKRNEEAQD----LSGGMQRKLSVAIAFVGDAKVVVLDEPTS 1090
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15232977 1165 ALDSKSERVVQDALERVMVGRTSIMIAHRLSTIQNC-DMIVVLGKGKIVESGTHSSLLEKGPTGTYFSL 1232
Cdd:TIGR01257 1091 GVDPYSRRSIWDLLLKYRSGRTIIMSTHHMDEADLLgDRIAIISQGRLYCSGTPLFLKNCFGTGFYLTL 1159
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
382-598 |
5.91e-17 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 82.37 E-value: 5.91e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 382 LKIPAGKTVALVGGSGSGKSTVISLLQRfydpiageiLIDGVSIDKLQVNWL-----------------RSQMGLVSQEP 444
Cdd:PRK09984 25 LNIHHGEMVALLGPSGSGKSTLLRHLSG---------LITGDKSAGSHIELLgrtvqregrlardirksRANTGYIFQQF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 445 VLF-ATSITENILFG--------KEDASLDEVVEAAKASNAHTFISQFPLGYktqvgERGVQMSGGQKQRIAIARAIIKS 515
Cdd:PRK09984 96 NLVnRLSVLENVLIGalgstpfwRTCFSWFTREQKQRALQALTRVGMVHFAH-----QRVSTLSGGQQQRVAIARALMQQ 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 516 PKILLLDEATSALDSESERVVQESLD--NASIGRTTIVIAHRLS-TIRNADVICVIHNGQIVETGSHEEL-LKRIDGQYT 591
Cdd:PRK09984 171 AKVILADEPIASLDPESARIVMDTLRdiNQNDGITVVVTLHQVDyALRYCERIVALRQGHVFYDGSSQQFdNERFDHLYR 250
|
....*..
gi 15232977 592 SLVSLQQ 598
Cdd:PRK09984 251 SINRVEE 257
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
369-532 |
6.04e-17 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 85.50 E-value: 6.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 369 LSRPETTIFDDLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYDPIAGEILIDGvsidklqvNWlrsQMGLVSQEPVLFA 448
Cdd:COG0488 6 KSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK--------GL---RIGYLPQEPPLDD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 449 T-SITENILFG----------------KEDASLDEVVEAAKA-------------SNAHTFISQfpLGYKTQVGERGV-Q 497
Cdd:COG0488 75 DlTVLDTVLDGdaelraleaeleeleaKLAEPDEDLERLAELqeefealggweaeARAEEILSG--LGFPEEDLDRPVsE 152
|
170 180 190
....*....|....*....|....*....|....*
gi 15232977 498 MSGGQKQRIAIARAIIKSPKILLLDEATSALDSES 532
Cdd:COG0488 153 LSGGWRRRVALARALLSEPDLLLLDEPTNHLDLES 187
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
999-1219 |
6.14e-17 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 86.32 E-value: 6.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 999 NVDFAYPT-RPDVVIFENFSIEIDEGKSTAIVGTSGSGKSTIIGLIERFYDPLKGTVKIDGRDIRSYHLRSL----RKYI 1073
Cdd:PRK10535 9 DIRRSYPSgEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALaqlrREHF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1074 SLVSQEPMLFAG-TIRENI----MYGGTSDKideseiieaAKAANAHDFITSLsnGYDTNCGDKGVQLSGGQKQRIAIAR 1148
Cdd:PRK10535 89 GFIFQRYHLLSHlTAAQNVevpaVYAGLERK---------QRLLRAQELLQRL--GLEDRVEYQPSQLSGGQQQRVSIAR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15232977 1149 AVLKNPSVLLLDEATSALDSKSERVVQDALERVM-VGRTSIMIAHRLSTIQNCDMIVVLGKGKIV-ESGTHSS 1219
Cdd:PRK10535 158 ALMNGGQVILADEPTGALDSHSGEEVMAILHQLRdRGHTVIIVTHDPQVAAQAERVIEIRDGEIVrNPPAQEK 230
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
714-929 |
6.42e-17 |
|
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 350019 [Multi-domain] Cd Length: 289 Bit Score: 82.53 E-value: 6.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 714 IYVLLFVGLAIFSFLvnisQHYGFAYMGEYLTKRIREQMLSKILTFEVNWFDidDNSSGAICSRLAKDANVVRSMVGDRM 793
Cdd:cd18575 41 LLLAVALVLALASAL----RFYLVSWLGERVVADLRKAVFAHLLRLSPSFFE--TTRTGEVLSRLTTDTTLIQTVVGSSL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 794 SLLVQTiSAVIIACIIGLVI-AWRLAIVMISVQPLIVV--CFYTQRVllKSLSEKASKAQDESSKLAAEAVSNIRTITAF 870
Cdd:cd18575 115 SIALRN-LLLLIGGLVMLFItSPKLTLLVLLVIPLVVLpiILFGRRV--RRLSRASQDRLADLSAFAEETLSAIKTVQAF 191
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15232977 871 SSQERIIKLLKKVQEGPRRESVH----RSWLAGIVLGTSRSLITCTsalnFWYGGRLIADGKI 929
Cdd:cd18575 192 TREDAERQRFATAVEAAFAAALRriraRALLTALVIFLVFGAIVFV----LWLGAHDVLAGRM 250
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1012-1222 |
7.63e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 81.81 E-value: 7.63e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1012 IFENFSIEIDEGKSTAIVGTSGSGKSTIIGLIERFYD-----PLKGTVKIDGRDIRSYHLRSL--RKYISLVSQEPMLFA 1084
Cdd:PRK14267 19 VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElneeaRVEGEVRLFGRNIYSPDVDPIevRREVGMVFQYPNPFP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1085 G-TIRENIMYGGTSDKIDES-----EIIE-AAKAANAHDFITSLSNGYDTNcgdkgvqLSGGQKQRIAIARAVLKNPSVL 1157
Cdd:PRK14267 99 HlTIYDNVAIGVKLNGLVKSkkeldERVEwALKKAALWDEVKDRLNDYPSN-------LSGGQRQRLVIARALAMKPKIL 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15232977 1158 LLDEATSALDSKSERVVQDALERVMVGRTSIMIAH------RLStiqncDMIVVLGKGKIVESGTHSSLLE 1222
Cdd:PRK14267 172 LMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHspaqaaRVS-----DYVAFLYLGKLIEVGPTRKVFE 237
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
991-1223 |
7.84e-17 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 83.34 E-value: 7.84e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 991 IKGQITFLNVDFAYPTRP--DVVIFENFSIEIDEGKSTAIVGTSGSGKSTIIGLIERFYDPLKGTVKIDGRDIRSyHLRS 1068
Cdd:PRK13536 33 IPGSMSTVAIDLAGVSKSygDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPA-RARL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1069 LRKYISLVSQEPML-FAGTIRENIM----YGGTSDKIDESEI---IEAAKaanahdfitsLSNGYDTNCGDkgvqLSGGQ 1140
Cdd:PRK13536 112 ARARIGVVPQFDNLdLEFTVRENLLvfgrYFGMSTREIEAVIpslLEFAR----------LESKADARVSD----LSGGM 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1141 KQRIAIARAVLKNPSVLLLDEATSALDSKSERVVQDALERVMV-GRTSIMIAHRLSTIQN-CDMIVVLGKG-KIVESGTH 1217
Cdd:PRK13536 178 KRRLTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSLLArGKTILLTTHFMEEAERlCDRLCVLEAGrKIAEGRPH 257
|
....*.
gi 15232977 1218 SSLLEK 1223
Cdd:PRK13536 258 ALIDEH 263
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
370-533 |
7.90e-17 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 80.23 E-value: 7.90e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 370 SRPETTIFDDLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYDPIAGEILIDGVSIDKLQVNWLRSQMGLVSQEPVLFAT 449
Cdd:cd03231 9 ERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 450 SITENILFGKEDASlDEVVEAAKAsnahtfisqfplgyktQVGERGV------QMSGGQKQRIAIARAIIKSPKILLLDE 523
Cdd:cd03231 89 SVLENLRFWHADHS-DEQVEEALA----------------RVGLNGFedrpvaQLSAGQQRRVALARLLLSGRPLWILDE 151
|
170
....*....|
gi 15232977 524 ATSALDSESE 533
Cdd:cd03231 152 PTTALDKAGV 161
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
1011-1215 |
8.91e-17 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 81.96 E-value: 8.91e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1011 VIFENFSIEIDEGKSTAIVGTSGSGKSTIIGLIERFYDPLKGTVKIDGRDIRSYHLRSLRKYISLVSQEPMLFAG-TIRE 1089
Cdd:PRK10253 21 TVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTPGDiTVQE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1090 NIMYGGTSD--------KIDESEIIEAAKAANahdfITSLSN-GYDTncgdkgvqLSGGQKQRIAIARAVLKNPSVLLLD 1160
Cdd:PRK10253 101 LVARGRYPHqplftrwrKEDEEAVTKAMQATG----ITHLADqSVDT--------LSGGQRQRAWIAMVLAQETAIMLLD 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1161 EATSALDSKSERVVQDALERV--MVGRTSIMIAHRLStiQNC---DMIVVLGKGKIVESG 1215
Cdd:PRK10253 169 EPTTWLDISHQIDLLELLSELnrEKGYTLAAVLHDLN--QACryaSHLIALREGKIVAQG 226
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
378-582 |
9.20e-17 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 85.08 E-value: 9.20e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 378 DDLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYDPIAGEILIDG--VSID------KLQVnwlrsqmGLVSQEPVLFAT 449
Cdd:COG3845 22 DDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGkpVRIRsprdaiALGI-------GMVHQHFMLVPN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 450 -SITENILFGKEDA-----SLDEVVEAAKAsnahtfISQ---FPLGYKTQVGergvQMSGGQKQRIAIARAIIKSPKILL 520
Cdd:COG3845 95 lTVAENIVLGLEPTkggrlDRKAARARIRE------LSErygLDVDPDAKVE----DLSVGEQQRVEILKALYRGARILI 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 521 LDEATSAL-DSESERVVqESLDN-ASIGRTTIVIAHRLSTIR-NADVICVIHNGQIVETG-----SHEEL 582
Cdd:COG3845 165 LDEPTAVLtPQEADELF-EILRRlAAEGKSIIFITHKLREVMaIADRVTVLRRGKVVGTVdtaetSEEEL 233
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
714-929 |
9.50e-17 |
|
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349989 [Multi-domain] Cd Length: 293 Bit Score: 82.13 E-value: 9.50e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 714 IYVLLFVGLAIFSFLVNISQHYGFAYMGEYLTKRIREQMLSKILTFEVNWFdiDDNSSGAICSRLAKDANVVRSMV-GDR 792
Cdd:cd18545 41 IIALLFLALNLVNWVASRLRIYLMAKVGQRILYDLRQDLFSHLQKLSFSFF--DSRPVGKILSRVINDVNSLSDLLsNGL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 793 MSLLVQTISAVIIAcIIGLVIAWRLAIVMISVQP-LIVVCFYTQRVLLKS---LSEKASKAqdeSSKLaAEAVSNIRTIT 868
Cdd:cd18545 119 INLIPDLLTLVGIV-IIMFSLNVRLALVTLAVLPlLVLVVFLLRRRARKAwqrVRKKISNL---NAYL-HESISGIRVIQ 193
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15232977 869 AFSSQERIIKLLKKVQEGPRRESVHRSWLAGIVLGTSRSLITCTSALNFWYGGRLIADGKI 929
Cdd:cd18545 194 SFAREDENEEIFDELNRENRKANMRAVRLNALFWPLVELISALGTALVYWYGGKLVLGGAI 254
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
1017-1220 |
1.29e-16 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 82.45 E-value: 1.29e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1017 SIEIDEGKSTAIVGTSGSGKST----IIGLIErfydPLKGTVKIDGRDIRSY---HLRSLRKYISLVSQEP-------ML 1082
Cdd:PRK15079 41 TLRLYEGETLGVVGESGCGKSTfaraIIGLVK----ATDGEVAWLGKDLLGMkddEWRAVRSDIQMIFQDPlaslnprMT 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1083 FAGTIRE--NIMYggtsDKIDESEIIEAAKAANAH-DFITSLSNGYDTncgdkgvQLSGGQKQRIAIARAVLKNPSVLLL 1159
Cdd:PRK15079 117 IGEIIAEplRTYH----PKLSRQEVKDRVKAMMLKvGLLPNLINRYPH-------EFSGGQCQRIGIARALILEPKLIIC 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15232977 1160 DEATSALD-SKSERVVQ--DALERVMvGRTSIMIAHRLSTIQN-CDMIVVLGKGKIVESGTHSSL 1220
Cdd:PRK15079 186 DEPVSALDvSIQAQVVNllQQLQREM-GLSLIFIAHDLAVVKHiSDRVLVMYLGHAVELGTYDEV 249
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1010-1209 |
1.38e-16 |
|
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: 80.17 E-value: 1.38e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1010 VVIFENFSIEIDEGKSTAIVGTSGSGKSTIIGLIERFYDPLKGTV------------KIDGRDIrsYHLRslRKYISLVS 1077
Cdd:COG4778 24 LPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSIlvrhdggwvdlaQASPREI--LALR--RRTIGYVS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1078 Q---------------EPMLFAGtirenimyggtsdkIDESEIIEAAKAANAHDFI-TSLSNGYDTNcgdkgvqLSGGQK 1141
Cdd:COG4778 100 QflrviprvsaldvvaEPLLERG--------------VDREEARARARELLARLNLpERLWDLPPAT-------FSGGEQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1142 QRIAIARAVLKNPSVLLLDEATSALDSKSERVVQDALERVMV-GRTSIMIAHRLSTIQN-CDMIVVLGKG 1209
Cdd:COG4778 159 QRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKArGTAIIGIFHDEEVREAvADRVVDVTPF 228
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
1007-1215 |
1.62e-16 |
|
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: 80.01 E-value: 1.62e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1007 RPDVVIFENFSIEIDEGKSTAIVGTSGSGKSTIIGLIERFYDPLK---GTVKIDGRDIRSYhlrSLRKYISLVSQEPMLF 1083
Cdd:cd03234 17 NKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGttsGQILFNGQPRKPD---QFQKCVAYVRQDDILL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1084 AG-TIRENIMYGG-------TSDKIDESEiieaakaanahDFITSLSNGYDTNCGDKGVQ-LSGGQKQRIAIARAVLKNP 1154
Cdd:cd03234 94 PGlTVRETLTYTAilrlprkSSDAIRKKR-----------VEDVLLRDLALTRIGGNLVKgISGGERRRVSIAVQLLWDP 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15232977 1155 SVLLLDEATSALDSKSERVVQDALERVMV-GRTSIMIAH--RLSTIQNCDMIVVLGKGKIVESG 1215
Cdd:cd03234 163 KVLILDEPTSGLDSFTALNLVSTLSQLARrNRIVILTIHqpRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
360-540 |
1.74e-16 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 80.51 E-value: 1.74e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 360 EFNHVKFTYLSRPettIFDDLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYDPIAGEILIDGVSIDKLQvnwlrSQMGL 439
Cdd:PRK11248 3 QISHLYADYGGKP---ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPG-----AERGV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 440 VSQ-EPVLFATSITENILFGKEdasLDEVVEAAKASNAHTFISQFPLgykTQVGERGV-QMSGGQKQRIAIARAIIKSPK 517
Cdd:PRK11248 75 VFQnEGLLPWRNVQDNVAFGLQ---LAGVEKMQRLEIAHQMLKKVGL---EGAEKRYIwQLSGGQRQRVGIARALAANPQ 148
|
170 180
....*....|....*....|...
gi 15232977 518 ILLLDEATSALDSESERVVQESL 540
Cdd:PRK11248 149 LLLLDEPFGALDAFTREQMQTLL 171
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
387-591 |
1.87e-16 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 84.52 E-value: 1.87e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 387 GKTVALVGGSGSGKSTVISLLQRFYDPIAGEILIDGVSIDKL---QVNWLRSQMGLVSQEPvlFAT---------SITE- 453
Cdd:PRK10261 350 GETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLspgKLQALRRDIQFIFQDP--YASldprqtvgdSIMEp 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 454 ----NILFGKEDAS-LDEVVEAAKASNAHTFisQFPLgyktqvgergvQMSGGQKQRIAIARAIIKSPKILLLDEATSAL 528
Cdd:PRK10261 428 lrvhGLLPGKAAAArVAWLLERVGLLPEHAW--RYPH-----------EFSGGQRQRICIARALALNPKVIIADEAVSAL 494
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15232977 529 D-SESERVVQESLD-NASIGRTTIVIAHRLSTI-RNADVICVIHNGQIVETGSHEELLKRIDGQYT 591
Cdd:PRK10261 495 DvSIRGQIINLLLDlQRDFGIAYLFISHDMAVVeRISHRVAVMYLGQIVEIGPRRAVFENPQHPYT 560
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1009-1230 |
1.88e-16 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 81.31 E-value: 1.88e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1009 DVVIFENFSIEIDEGKSTAIVGTSGSGKSTIIGLIERFYDPLKGTVKIDGRDIRsyhlRSLRKYISLVSQEPMLFAG-TI 1087
Cdd:COG4152 13 DKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLD----PEDRRRIGYLPEERGLYPKmKV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1088 RENIMY-----GgtsdkIDESEIIEAAKA-ANAHDfITSLSNgydtncgDKGVQLSGGQKQRIAIARAVLKNPSVLLLDE 1161
Cdd:COG4152 89 GEQLVYlarlkG-----LSKAEAKRRADEwLERLG-LGDRAN-------KKVEELSKGNQQKVQLIAALLHDPELLILDE 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15232977 1162 ATSALDSKSERVVQDAL-ERVMVGRTSIMIAHRLSTIQN-CDMIVVLGKGKIVESGTHSSLLEKGPTGTYF 1230
Cdd:COG4152 156 PFSGLDPVNVELLKDVIrELAAKGTTVIFSSHQMELVEElCDRIVIINKGRKVLSGSVDEIRRQFGRNTLR 226
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
378-591 |
1.99e-16 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 82.06 E-value: 1.99e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 378 DDLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYDPIAGEILIDGVSIDKL-QVNWL--RSQMGLVSQEPV-------LF 447
Cdd:PRK15079 38 DGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMkDDEWRavRSDIQMIFQDPLaslnprmTI 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 448 ATSITENILFGKEDASLDEVVEAAKASNAHT-----FISQFPLgyktqvgergvQMSGGQKQRIAIARAIIKSPKILLLD 522
Cdd:PRK15079 118 GEIIAEPLRTYHPKLSRQEVKDRVKAMMLKVgllpnLINRYPH-----------EFSGGQCQRIGIARALILEPKLIICD 186
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15232977 523 EATSALD-SESERVVQ--ESLdNASIGRTTIVIAHRLSTIRN-ADVICVIHNGQIVETGSHEELLKRIDGQYT 591
Cdd:PRK15079 187 EPVSALDvSIQAQVVNllQQL-QREMGLSLIFIAHDLAVVKHiSDRVLVMYLGHAVELGTYDEVYHNPLHPYT 258
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
1017-1216 |
2.32e-16 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 81.93 E-value: 2.32e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1017 SIEIDEGKSTAIVGTSGSGKSTI---IGLIERfydPLKGTVKIDGRDIRSY---HLRSLRKYISLVSQEPmlfagtiren 1090
Cdd:PRK11308 35 SFTLERGKTLAVVGESGCGKSTLarlLTMIET---PTGGELYYQGQDLLKAdpeAQKLLRQKIQIVFQNP---------- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1091 imYGG------TSDKIDESEIIE-----AAKAANAHDFITSLsnGYDTNCGDKGVQL-SGGQKQRIAIARAVLKNPSVLL 1158
Cdd:PRK11308 102 --YGSlnprkkVGQILEEPLLINtslsaAERREKALAMMAKV--GLRPEHYDRYPHMfSGGQRQRIAIARALMLDPDVVV 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15232977 1159 LDEATSALD-SKSERV------VQDALervmvGRTSIMIAHRLSTIQN-CDMIVVLGKGKIVESGT 1216
Cdd:PRK11308 178 ADEPVSALDvSVQAQVlnlmmdLQQEL-----GLSYVFISHDLSVVEHiADEVMVMYLGRCVEKGT 238
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
994-1220 |
2.33e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 81.29 E-value: 2.33e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 994 QITFLNVDFAYPTRPDVVI--FENFSIEIDEGKSTAIVGTSGSGKSTIIGLIERFYDPLKGTVKIDGRDIRSYH------ 1065
Cdd:PRK13651 2 QIKVKNIVKIFNKKLPTELkaLDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKKktkeke 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1066 ------------------LRSLRKYISLVSQ--EPMLFAGTIRENIMYGGTSDKIDESEIIEAAKaanahDFITSLsnGY 1125
Cdd:PRK13651 82 kvleklviqktrfkkikkIKEIRRRVGVVFQfaEYQLFEQTIEKDIIFGPVSMGVSKEEAKKRAA-----KYIELV--GL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1126 DTNCGDKG-VQLSGGQKQRIAIARAVLKNPSVLLLDEATSALDSKSERVVQDALERV-MVGRTSIMIAHRL-STIQNCDM 1202
Cdd:PRK13651 155 DESYLQRSpFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLnKQGKTIILVTHDLdNVLEWTKR 234
|
250
....*....|....*....
gi 15232977 1203 IVVLGKGKIVESG-THSSL 1220
Cdd:PRK13651 235 TIFFKDGKIIKDGdTYDIL 253
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
378-554 |
2.77e-16 |
|
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: 79.43 E-value: 2.77e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 378 DDLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYDPIAGEILIDGVSIDKLQVNWLrsqmgLVSQEPVLFA-TSITENIL 456
Cdd:TIGR01184 2 KGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRM-----VVFQNYSLLPwLTVRENIA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 457 FgkedaSLDEVVEAAKASNAHTFISQFP--LGYKTQVGERGVQMSGGQKQRIAIARAIIKSPKILLLDEATSALDSESER 534
Cdd:TIGR01184 77 L-----AVDRVLPDLSKSERRAIVEEHIalVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRG 151
|
170 180
....*....|....*....|..
gi 15232977 535 VVQESLDN--ASIGRTTIVIAH 554
Cdd:TIGR01184 152 NLQEELMQiwEEHRVTVLMVTH 173
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
1009-1216 |
2.86e-16 |
|
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: 79.34 E-value: 2.86e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1009 DVVIFENFSIEIDEGKSTAIVGTSGSGKSTIIGLIERFYDPLKGTVKIDGRDIRSyHLRSLRKYISLVSQEPMLFAG-TI 1087
Cdd:cd03265 12 DFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR-EPREVRRRIGIVFQDLSVDDElTG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1088 RENI-----MYGGTSDKIDEsEIIEAAKAANAHDFITSLSNGYdtncgdkgvqlSGGQKQRIAIARAVLKNPSVLLLDEA 1162
Cdd:cd03265 91 WENLyiharLYGVPGAERRE-RIDELLDFVGLLEAADRLVKTY-----------SGGMRRRLEIARSLVHRPEVLFLDEP 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15232977 1163 TSALDSKSERVVQDALERVM--VGRTSIMIAHRLSTI-QNCDMIVVLGKGKIVESGT 1216
Cdd:cd03265 159 TIGLDPQTRAHVWEYIEKLKeeFGMTILLTTHYMEEAeQLCDRVAIIDHGRIIAEGT 215
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
995-1215 |
2.93e-16 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 82.00 E-value: 2.93e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 995 ITFLNVDFAYPtrpDVVIFENFSIEIDEGKSTAIVGTSGSGKSTIIGLIERFYDPLKGTVKIDGRdiRSYHLRSLRKYIS 1074
Cdd:PRK11000 4 VTLRNVTKAYG---DVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEK--RMNDVPPAERGVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1075 LVSQEPMLFAG-TIRENIMYGGTSDKIDESEIieaAKAANAHDFITSLSNGYDTncgdKGVQLSGGQKQRIAIARAVLKN 1153
Cdd:PRK11000 79 MVFQSYALYPHlSVAENMSFGLKLAGAKKEEI---NQRVNQVAEVLQLAHLLDR----KPKALSGGQRQRVAIGRTLVAE 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15232977 1154 PSVLLLDEATSALDSkSERV---VQDALERVMVGRTSIMIAH-RLSTIQNCDMIVVLGKGKIVESG 1215
Cdd:PRK11000 152 PSVFLLDEPLSNLDA-ALRVqmrIEISRLHKRLGRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVG 216
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
376-577 |
4.61e-16 |
|
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: 78.85 E-value: 4.61e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 376 IFDDLCLKIPAGKTVALVGGSGSGKST---VISLLQRFYDPIAGEILIDGVSIDKLQVnwlRSQMGLVSQEPVlFATSIT 452
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTlldAISGRVEGGGTTSGQILFNGQPRKPDQF---QKCVAYVRQDDI-LLPGLT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 453 --ENILFG--------KEDASLDEVVEAAKASNAHTfisqfplgykTQVGERGVQ-MSGGQKQRIAIARAIIKSPKILLL 521
Cdd:cd03234 98 vrETLTYTailrlprkSSDAIRKKRVEDVLLRDLAL----------TRIGGNLVKgISGGERRRVSIAVQLLWDPKVLIL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15232977 522 DEATSALDSESERVVQESLDN-ASIGRTTIVIAH--RLSTIRNADVICVIHNGQIVETG 577
Cdd:cd03234 168 DEPTSGLDSFTALNLVSTLSQlARRNRIVILTIHqpRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1004-1161 |
4.90e-16 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 78.92 E-value: 4.90e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1004 YPTRPdVVifENFSIEIDEGKSTAIVGTSGSGKST----IIGLIErfydPLKGTVKIDGRDIRSY--HLRSlRKYISLVS 1077
Cdd:COG1137 13 YGKRT-VV--KDVSLEVNQGEIVGLLGPNGAGKTTtfymIVGLVK----PDSGRIFLDGEDITHLpmHKRA-RLGIGYLP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1078 QEPMLFAG-TIRENIM-----YGGTSDKIDE--SEIIEaakaanahDF-ITSLSNgydtncgDKGVQLSGGQKQRIAIAR 1148
Cdd:COG1137 85 QEASIFRKlTVEDNILavlelRKLSKKEREErlEELLE--------EFgITHLRK-------SKAYSLSGGERRRVEIAR 149
|
170
....*....|...
gi 15232977 1149 AVLKNPSVLLLDE 1161
Cdd:COG1137 150 ALATNPKFILLDE 162
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
374-557 |
4.94e-16 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 78.70 E-value: 4.94e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 374 TTIFDDLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYDPIAGEILIDGVSIDKLQVNW---LRSQ-MGLVSQ-EPVLFA 448
Cdd:PRK11629 22 TDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAkaeLRNQkLGFIYQfHHLLPD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 449 TSITENI----LFGKedasldeVVEAAKASNAHTFISQFPLGYKTQvgERGVQMSGGQKQRIAIARAIIKSPKILLLDEA 524
Cdd:PRK11629 102 FTALENVamplLIGK-------KKPAEINSRALEMLAAVGLEHRAN--HRPSELSGGERQRVAIARALVNNPRLVLADEP 172
|
170 180 190
....*....|....*....|....*....|....*
gi 15232977 525 TSALDSESERVVQESLD--NASIGRTTIVIAHRLS 557
Cdd:PRK11629 173 TGNLDARNADSIFQLLGelNRLQGTAFLVVTHDLQ 207
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
677-929 |
5.50e-16 |
|
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (TrmA) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349988 [Multi-domain] Cd Length: 294 Bit Score: 80.12 E-value: 5.50e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 677 LSAALVGVLQPVsaysagsVISVF---FLTSHDQIKEKTRIYVLLFVGLAIFSFLVNISQHYGFAYMGEYLTKRIREQML 753
Cdd:cd18544 9 LLATALELLGPL-------LIKRAiddYIVPGQGDLQGLLLLALLYLGLLLLSFLLQYLQTYLLQKLGQRIIYDLRRDLF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 754 SKILTFEVNWFdiDDNSSGAICSRLAKDANVVRSMVgdrMSLLVQTISAVIIacIIGLVIA-----WRLAIVMISVQPLI 828
Cdd:cd18544 82 SHIQRLPLSFF--DRTPVGRLVTRVTNDTEALNELF---TSGLVTLIGDLLL--LIGILIAmfllnWRLALISLLVLPLL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 829 VVCFYTQRVLLKSLSEKASKAQdesSKLAA---EAVSNIRTITAFSSQERIIKLLKKVQEGPRRESVHRSWLAGIVLGTS 905
Cdd:cd18544 155 LLATYLFRKKSRKAYREVREKL---SRLNAflqESISGMSVIQLFNREKREFEEFDEINQEYRKANLKSIKLFALFRPLV 231
|
250 260
....*....|....*....|....
gi 15232977 906 RSLITCTSALNFWYGGRLIADGKI 929
Cdd:cd18544 232 ELLSSLALALVLWYGGGQVLSGAV 255
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
373-582 |
6.87e-16 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 80.84 E-value: 6.87e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 373 ETTIFDDLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYDPIAGEILIDGVSIDklQVNWLRSQMGLVSQEPVLFA-TSI 451
Cdd:PRK11000 15 DVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMN--DVPPAERGVGMVFQSYALYPhLSV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 452 TENILFGKEDASLDEVvEAAKASNAHTFISQfpLGYKTQvgERGVQMSGGQKQRIAIARAIIKSPKILLLDEATSALDSe 531
Cdd:PRK11000 93 AENMSFGLKLAGAKKE-EINQRVNQVAEVLQ--LAHLLD--RKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDA- 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15232977 532 SERV---VQESLDNASIGRTTIVIAH-RLSTIRNADVICVIHNGQIVETGSHEEL 582
Cdd:PRK11000 167 ALRVqmrIEISRLHKRLGRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVGKPLEL 221
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
366-585 |
7.73e-16 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 79.28 E-value: 7.73e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 366 FTYLSRPettIFDDLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYDPIAGEILIDGVSID--KLQVNWLRSQMGLVSQE 443
Cdd:PRK13638 9 FRYQDEP---VLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDysKRGLLALRQQVATVFQD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 444 P--VLFATSITENILFGKEDASLDEVVEAAKASNAHTFISQfpLGYKTQvgerGVQ-MSGGQKQRIAIARAIIKSPKILL 520
Cdd:PRK13638 86 PeqQIFYTDIDSDIAFSLRNLGVPEAEITRRVDEALTLVDA--QHFRHQ----PIQcLSHGQKKRVAIAGALVLQARYLL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15232977 521 LDEATSALDSES--------ERVVQEsldnasiGRTTIVIAHRLSTIRN-ADVICVIHNGQIVETGSHEELLKR 585
Cdd:PRK13638 160 LDEPTAGLDPAGrtqmiaiiRRIVAQ-------GNHVIISSHDIDLIYEiSDAVYVLRQGQILTHGAPGEVFAC 226
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
378-585 |
8.62e-16 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 79.38 E-value: 8.62e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 378 DDLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYDPIAGEILIDGVSIDKLQvnwlRSQMGLVSQEPVLFAT-SITENIL 456
Cdd:COG4152 18 DDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPED----RRRIGYLPEERGLYPKmKVGEQLV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 457 -FGK-EDASLDEVVEAAKAsnahtFISQFPLG--YKTQVGErgvqMSGGQKQRIAIARAIIKSPKILLLDEATSALDSES 532
Cdd:COG4152 94 yLARlKGLSKAEAKRRADE-----WLERLGLGdrANKKVEE----LSKGNQQKVQLIAALLHDPELLILDEPFSGLDPVN 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15232977 533 -ERVVQESLDNASIGRTTIVIAHRLSTI-RNADVICVIHNGQIVETGSHEELLKR 585
Cdd:COG4152 165 vELLKDVIRELAAKGTTVIFSSHQMELVeELCDRIVIINKGRKVLSGSVDEIRRQ 219
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
994-1168 |
1.07e-15 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 78.37 E-value: 1.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 994 QITFLNVDFAYP-TRPDVVIFENFSIEIDEGKSTAIVGTSGSGKSTIIGLIERFYDPLKGTVKIDGRDI------RSyhl 1066
Cdd:COG4525 3 MLTVRHVSVRYPgGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVtgpgadRG--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1067 rslrkyisLVSQEPMLFAG-TIRENIMYGGTSDKIDESEIIEAAKAANA----HDFitslsngydtncGDKGV-QLSGGQ 1140
Cdd:COG4525 80 --------VVFQKDALLPWlNVLDNVAFGLRLRGVPKAERRARAEELLAlvglADF------------ARRRIwQLSGGM 139
|
170 180
....*....|....*....|....*...
gi 15232977 1141 KQRIAIARAVLKNPSVLLLDEATSALDS 1168
Cdd:COG4525 140 RQRVGIARALAADPRFLLMDEPFGALDA 167
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
375-588 |
1.53e-15 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 78.10 E-value: 1.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 375 TIFDDLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYDPIAGEILIDGVSIDKLQVNWLRSQMGLVSQEPVLFA-TSITE 453
Cdd:PRK10253 21 TVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTPGdITVQE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 454 NILFG------------KEDAslDEVVEAAKASNAhtfisqfplgykTQVGERGVQ-MSGGQKQRIAIARAIIKSPKILL 520
Cdd:PRK10253 101 LVARGryphqplftrwrKEDE--EAVTKAMQATGI------------THLADQSVDtLSGGQRQRAWIAMVLAQETAIML 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15232977 521 LDEATSALDSESERVVQESLD--NASIGRTTIVIAHRLS-TIRNADVICVIHNGQIVETGSHEE-----LLKRIDG 588
Cdd:PRK10253 167 LDEPTTWLDISHQIDLLELLSelNREKGYTLAAVLHDLNqACRYASHLIALREGKIVAQGAPKEivtaeLIERIYG 242
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1009-1223 |
2.33e-15 |
|
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: 80.62 E-value: 2.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1009 DVVIFENFSIEIDEGKSTAIVGTSGSGKSTIIGLIERF--YDPLKGTV-------------------------------- 1054
Cdd:TIGR03269 12 GKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIiyhvalcekcgyverpskvgepcpvcggtlep 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1055 -KIDGRDIRSYHLRSLRKYISLVSQEPMLFAG--TIRENIM-------YGGTSDKIDESEIIEAAKAANAhdfITSLSNg 1124
Cdd:TIGR03269 92 eEVDFWNLSDKLRRRIRKRIAIMLQRTFALYGddTVLDNVLealeeigYEGKEAVGRAVDLIEMVQLSHR---ITHIAR- 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1125 ydtncgdkgvQLSGGQKQRIAIARAVLKNPSVLLLDEATSALDSKSERVVQDALERVMV--GRTSIMIAHRLSTIQN-CD 1201
Cdd:TIGR03269 168 ----------DLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKasGISMVLTSHWPEVIEDlSD 237
|
250 260
....*....|....*....|..
gi 15232977 1202 MIVVLGKGKIVESGTHSSLLEK 1223
Cdd:TIGR03269 238 KAIWLENGEIKEEGTPDEVVAV 259
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
378-585 |
2.57e-15 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 77.05 E-value: 2.57e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 378 DDLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYDP----IAGEILIDGVSIDKLQvnwLRSQM-GLVSQEP-------V 445
Cdd:PRK10418 20 HGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGRVLLDGKPVAPCA---LRGRKiATIMQNPrsafnplH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 446 LFATSITENIL-FGKE--DASLDEVVEAAKASNAHTFISQFPLgyktqvgergvQMSGGQKQRIAIARAIIKSPKILLLD 522
Cdd:PRK10418 97 TMHTHARETCLaLGKPadDATLTAALEAVGLENAARVLKLYPF-----------EMSGGMLQRMMIALALLCEAPFIIAD 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15232977 523 EATSALDSES--------ERVVQESldnasiGRTTIVIAHRLSTI-RNADVICVIHNGQIVETGSHEELLKR 585
Cdd:PRK10418 166 EPTTDLDVVAqarildllESIVQKR------ALGMLLVTHDMGVVaRLADDVAVMSHGRIVEQGDVETLFNA 231
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
375-576 |
2.94e-15 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 80.25 E-value: 2.94e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 375 TIFDDLCLKIPAGKTVALVGGSGSGKSTVISLLQRFY--DPIAGEILIDGVSIDKLQV-NWLRSQMGLVSQEPVLFAT-S 450
Cdd:TIGR02633 15 KALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYphGTWDGEIYWSGSPLKASNIrDTERAGIVIIHQELTLVPElS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 451 ITENILFGKE------DASLDEVVEAAKASNAHTFISQFPLgyKTQVGERGvqmsGGQKQRIAIARAIIKSPKILLLDEA 524
Cdd:TIGR02633 95 VAENIFLGNEitlpggRMAYNAMYLRAKNLLRELQLDADNV--TRPVGDYG----GGQQQLVEIAKALNKQARLLILDEP 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15232977 525 TSAL-DSESERVVQESLDNASIGRTTIVIAHRLSTIRN-ADVICVIHNGQIVET 576
Cdd:TIGR02633 169 SSSLtEKETEILLDIIRDLKAHGVACVYISHKLNEVKAvCDTICVIRDGQHVAT 222
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
373-554 |
3.15e-15 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 76.36 E-value: 3.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 373 ETTIFDDLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYDPIAGEILIDGVSIDKL---QVNWLRSQ-MGLVSQEPVLFA 448
Cdd:PRK10584 22 ELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMdeeARAKLRAKhVGFVFQSFMLIP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 449 T-SITENIlfgKEDASLDEVVEAAKASNAHTFISQFPLGYKtqVGERGVQMSGGQKQRIAIARAIIKSPKILLLDEATSA 527
Cdd:PRK10584 102 TlNALENV---ELPALLRGESSRQSRNGAKALLEQLGLGKR--LDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGN 176
|
170 180 190
....*....|....*....|....*....|
gi 15232977 528 LDSES-ERVVQE--SLdNASIGRTTIVIAH 554
Cdd:PRK10584 177 LDRQTgDKIADLlfSL-NREHGTTLILVTH 205
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1008-1212 |
3.29e-15 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 80.07 E-value: 3.29e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1008 PDVVIFENFSIEIDEGKSTAIVGTSGSGKSTIIGLIERFYDPLKGTVKIDGRDIRsyhLRS----LRKYISLVSQEPMLF 1083
Cdd:COG3845 16 GGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVR---IRSprdaIALGIGMVHQHFMLV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1084 AG-TIRENIMYG---GTSDKIDESEIIEAakaanahdfITSLSNGYdtncG-----DKGV-QLSGGQKQRIAIARAVLKN 1153
Cdd:COG3845 93 PNlTVAENIVLGlepTKGGRLDRKAARAR---------IRELSERY----GldvdpDAKVeDLSVGEQQRVEILKALYRG 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15232977 1154 PSVLLLDEATSALdSKSErvVQDALE--RVMV--GRTSIMIAHRLSTI-QNCDMIVVLGKGKIV 1212
Cdd:COG3845 160 ARILILDEPTAVL-TPQE--ADELFEilRRLAaeGKSIIFITHKLREVmAIADRVTVLRRGKVV 220
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
386-583 |
3.40e-15 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 77.14 E-value: 3.40e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 386 AGKTVALVGGSGSGKSTVISLLQRFYDPIAGEILIDGVSIDKLQVNWlRSQ-MGLVSQEPvlfATSItenilfgkedasl 464
Cdd:PRK15112 38 EGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSY-RSQrIRMIFQDP---STSL------------- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 465 devveaakasNAHTFISQ---FPLGYKT----------------QVGERGVQ-------MSGGQKQRIAIARAIIKSPKI 518
Cdd:PRK15112 101 ----------NPRQRISQildFPLRLNTdlepeqrekqiietlrQVGLLPDHasyyphmLAPGQKQRLGLARALILRPKV 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15232977 519 LLLDEATSALD-SESERVVQESLD-NASIGRTTIVIAHRLSTIRN-ADVICVIHNGQIVETGSHEELL 583
Cdd:PRK15112 171 IIADEALASLDmSMRSQLINLMLElQEKQGISYIYVTQHLGMMKHiSDQVLVMHQGEVVERGSTADVL 238
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
995-1210 |
3.61e-15 |
|
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: 73.64 E-value: 3.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 995 ITFLNVDFAYPTRPdvvIFENFSIEIDEGKSTAIVGTSGSGKSTIIGLIERFYDPLKGTVKIdGRDIRSYHLRslrkyis 1074
Cdd:cd03221 1 IELENLSKTYGGKL---LLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTW-GSTVKIGYFE------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1075 lvsqepmlfagtirenimyggtsdkideseiieaakaanahdfitslsngydtncgdkgvQLSGGQKQRIAIARAVLKNP 1154
Cdd:cd03221 70 ------------------------------------------------------------QLSGGEKMRLALAKLLLENP 89
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15232977 1155 SVLLLDEATSALDSKServvQDALERVMVG--RTSIMIAHRLSTIQN-CDMIVVLGKGK 1210
Cdd:cd03221 90 NLLLLDEPTNHLDLES----IEALEEALKEypGTVILVSHDRYFLDQvATKIIELEDGK 144
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
74-332 |
4.33e-15 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349994 [Multi-domain] Cd Length: 294 Bit Score: 77.52 E-value: 4.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 74 MQTISKNVVALLYVACGSWVICFLEGYCWTRTGERQAARMREKYLRAVLRQDVGYFDlhVTSTSDVITSISSDSLVIQDF 153
Cdd:cd18550 35 LGLLVLLALGMVAVAVASALLGVVQTYLSARIGQGVMYDLRVQLYAHLQRMSLAFFT--RTRTGEIQSRLNNDVGGAQSV 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 154 LSEKLPNFLMNASAFVASYIVSFILMWRLTIVGFPFIILLLVPGLMYGRALVSISRKIHEQYNEAGSIAEQ--AISSVRT 231
Cdd:cd18550 113 VTGTLTSVVSNVVTLVATLVAMLALDWRLALLSLVLLPLFVLPTRRVGRRRRKLTREQQEKLAELNSIMQEtlSVSGALL 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 232 VYAFGSENKMIGKFSTALRGSVKLGLRQGLAKGITIGSNGVTHAIW-AFLTWYGSRLVMNHGSKGGTVFVVISCIT--YG 308
Cdd:cd18550 193 VKLFGREDDEAARFARRSRELRDLGVRQALAGRWFFAALGLFTAIGpALVYWVGGLLVIGGGLTIGTLVAFTALLGrlYG 272
|
250 260
....*....|....*....|....*
gi 15232977 309 GVslgQSLSNLKY-FSEAFVAWERI 332
Cdd:cd18550 273 PL---TQLLNIQVdLMTSLALFERI 294
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
365-577 |
5.53e-15 |
|
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: 75.65 E-value: 5.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 365 KFTYLSRPETTIFDDLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYDPIAGEILIDGvsidklQVNWLrsqMGL-VSQE 443
Cdd:cd03220 26 LGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG------RVSSL---LGLgGGFN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 444 PVLfatSITENILF-----GKEDASLDEVVEaakasnahtFISQFplgykTQVGERGVQ----MSGGQKQRIAIARAIIK 514
Cdd:cd03220 97 PEL---TGRENIYLngrllGLSRKEIDEKID---------EIIEF-----SELGDFIDLpvktYSSGMKARLAFAIATAL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15232977 515 SPKILLLDEATSALDSE----SERVVQESLDNasiGRTTIVIAHRLSTIRN-ADVICVIHNGQIVETG 577
Cdd:cd03220 160 EPDILLIDEVLAVGDAAfqekCQRRLRELLKQ---GKTVILVSHDPSSIKRlCDRALVLEKGKIRFDG 224
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
378-576 |
8.13e-15 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 78.68 E-value: 8.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 378 DDLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYdPIA---GEILIDGvsiDKLQVNWLRS--QMGLV--SQE----PVL 446
Cdd:NF040905 18 DDVNLSVREGEIHALCGENGAGKSTLMKVLSGVY-PHGsyeGEILFDG---EVCRFKDIRDseALGIViiHQElaliPYL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 447 fatSITENILFGKEDASL-----DEVVEAAKASNAHTFISQFPlgyKTQVGERGVqmsgGQKQRIAIARAIIKSPKILLL 521
Cdd:NF040905 94 ---SIAENIFLGNERAKRgvidwNETNRRARELLAKVGLDESP---DTLVTDIGV----GKQQLVEIAKALSKDVKLLIL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15232977 522 DEATSAL-DSESERVVQESLDNASIGRTTIVIAHRLSTIRN-ADVICVIHNGQIVET 576
Cdd:NF040905 164 DEPTAALnEEDSAALLDLLLELKAQGITSIIISHKLNEIRRvADSITVLRDGRTIET 220
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
994-1221 |
1.11e-14 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 75.64 E-value: 1.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 994 QITFLNVDFAYPT----RPDVVIFENFSIEIDEGKSTAIVGTSGSGKST----IIGLIErfydPLKGTVKIDGR--DIRS 1063
Cdd:COG4167 6 EVRNLSKTFKYRTglfrRQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTlakmLAGIIE----PTSGEILINGHklEYGD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1064 YHLRSlrKYISLVSQE------PMLFAGTIRENIMYGGTsdKIDESE----IIEAAK-----AANAHDFITslsngydtn 1128
Cdd:COG4167 82 YKYRC--KHIRMIFQDpntslnPRLNIGQILEEPLRLNT--DLTAEEreerIFATLRlvgllPEHANFYPH--------- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1129 cgdkgvQLSGGQKQRIAIARAVLKNPSVLLLDEATSALDS--KSERV-----VQDALervmvGRTSIMIAHRLSTIQNC- 1200
Cdd:COG4167 149 ------MLSSGQKQRVALARALILQPKIIIADEALAALDMsvRSQIInlmleLQEKL-----GISYIYVSQHLGIVKHIs 217
|
250 260
....*....|....*....|.
gi 15232977 1201 DMIVVLGKGKIVESGTHSSLL 1221
Cdd:COG4167 218 DKVLVMHQGEVVEYGKTAEVF 238
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
1009-1224 |
1.12e-14 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 75.10 E-value: 1.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1009 DVVIFENFSIEIDEGKSTAIVGTSGSGKST----IIGlIERfYDPLKGTVKIDGRDI-------RSyhlrslRKYISLVS 1077
Cdd:COG0396 12 GKEILKGVNLTIKPGEVHAIMGPNGSGKSTlakvLMG-HPK-YEVTSGSILLDGEDIlelspdeRA------RAGIFLAF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1078 QEPMLFAG-TIRE------NIMYGGTSDKID-ESEIIEAAKAAN-AHDFIT-SLSNGydtncgdkgvqLSGGQKQRIAIA 1147
Cdd:COG0396 84 QYPVEIPGvSVSNflrtalNARRGEELSAREfLKLLKEKMKELGlDEDFLDrYVNEG-----------FSGGEKKRNEIL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1148 RAVLKNPSVLLLDEATSALDSKSERVVQDALERVMV-GRTSIMIAH--RLSTIQNCDMIVVLGKGKIVESGTHS---SLL 1221
Cdd:COG0396 153 QMLLLEPKLAILDETDSGLDIDALRIVAEGVNKLRSpDRGILIITHyqRILDYIKPDFVHVLVDGRIVKSGGKElalELE 232
|
...
gi 15232977 1222 EKG 1224
Cdd:COG0396 233 EEG 235
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
368-563 |
1.13e-14 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 73.81 E-value: 1.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 368 YLSRPettIFDDLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYDPIAGEILIDGvsidKLQVNWLRSQMGLVSQEPVLF 447
Cdd:NF040873 2 YGGRP---VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG----GARVAYVPQRSEVPDSLPLTV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 448 ATSIT-----ENILFGKEDASLDEVVEAA-KASNAHTFIsqfplgyKTQVGErgvqMSGGQKQRIAIARAIIKSPKILLL 521
Cdd:NF040873 75 RDLVAmgrwaRRGLWRRLTRDDRAAVDDAlERVGLADLA-------GRQLGE----LSGGQRQRALLAQGLAQEADLLLL 143
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 15232977 522 DEATSALDSESERVVQESLDNASI-GRTTIVIAHRLSTIRNAD 563
Cdd:NF040873 144 DEPTTGLDAESRERIIALLAEEHArGATVVVVTHDLELVRRAD 186
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1008-1220 |
1.30e-14 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 78.03 E-value: 1.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1008 PDVVIFENFSIEIDEGKSTAIVGTSGSGKSTIIGLIERFYDPLKGTVKIDGRDIRSYHLR-SLRKYISLVSQE----PML 1082
Cdd:PRK11288 15 PGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTaALAAGVAIIYQElhlvPEM 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1083 fagTIRENIMYGGTSDK---IDESEIIEAAKAANAHdfitslsNGYDTNCGDKGVQLSGGQKQRIAIARAVLKNPSVLLL 1159
Cdd:PRK11288 95 ---TVAENLYLGQLPHKggiVNRRLLNYEAREQLEH-------LGVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAF 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15232977 1160 DEATSALDSK-SERvvqdaLERVMV-----GRTSIMIAHRLSTI-QNCDMIVVLGKGKIVEsgTHSSL 1220
Cdd:PRK11288 165 DEPTSSLSAReIEQ-----LFRVIRelraeGRVILYVSHRMEEIfALCDAITVFKDGRYVA--TFDDM 225
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1014-1222 |
1.39e-14 |
|
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: 78.31 E-value: 1.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1014 ENFSIEIDEGKSTAIVGTSGSGKSTIIGLIERFYDPLKGTVK-------IDGRDIRSYHLRSLRKYISLVSQEPMLFA-G 1085
Cdd:TIGR03269 301 DNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNvrvgdewVDMTKPGPDGRGRAKRYIGILHQEYDLYPhR 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1086 TIRENIMYGGTSDKIDESEIIEAAkaanahdfITSLSNGYDTncgDKGV--------QLSGGQKQRIAIARAVLKNPSVL 1157
Cdd:TIGR03269 381 TVLDNLTEAIGLELPDELARMKAV--------ITLKMVGFDE---EKAEeildkypdELSEGERHRVALAQVLIKEPRIV 449
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15232977 1158 LLDEATSALDSKSERVVQDAL--ERVMVGRTSIMIAHRLSTIQN-CDMIVVLGKGKIVESGTHSSLLE 1222
Cdd:TIGR03269 450 ILDEPTGTMDPITKVDVTHSIlkAREEMEQTFIIVSHDMDFVLDvCDRAALMRDGKIVKIGDPEEIVE 517
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1023-1212 |
1.51e-14 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 74.14 E-value: 1.51e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1023 GKSTAIVGTSGSGKSTIIGLIERFYDPLKGTVKIDGRDI---RSYHLRSLRKYISLVSQEP-MLFAGTIREN-----IMY 1093
Cdd:PRK10908 28 GEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDItrlKNREVPFLRRQIGMIFQDHhLLMDRTVYDNvaiplIIA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1094 GGTSDKIDEseiieaaKAANAHDFITSLsngydtncgDKG----VQLSGGQKQRIAIARAVLKNPSVLLLDEATSALDSK 1169
Cdd:PRK10908 108 GASGDDIRR-------RVSAALDKVGLL---------DKAknfpIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDA 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 15232977 1170 -SERVVQDALERVMVGRTSIMIAHRLSTIQNCDM-IVVLGKGKIV 1212
Cdd:PRK10908 172 lSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYrMLTLSDGHLH 216
|
|
| ABC_6TM_ABCB8_like |
cd18574 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ... |
677-929 |
1.54e-14 |
|
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B member 8, mitochondrial, and similar proteins; This group includes ABCB8, which is one of the three ATP-binding cassette (ABC) transporters found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. ABCB8 is essential for maintenance of normal cardiac function, involves mitochondrial iron export, and plays a role in the maturation of cytosolic Fe/S cluster-containing enzymes. ABCB8 is a half-molecule ABC protein that contains one TMD fused to a NBD, which dimerize to form a functional transporter.
Pssm-ID: 350018 [Multi-domain] Cd Length: 295 Bit Score: 75.66 E-value: 1.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 677 LSAALVGVLQPVSAYSAGSVISVFFLTSH----DQIKEKTRIYVLLFVGLAIFSFlVNIsqhYGFAYMGEYLTKRIREQM 752
Cdd:cd18574 6 LAAALVNIQIPLLLGDLVNVISRSLKETNgdfiEDLKKPALKLLGLYLLQSLLTF-AYI---SLLSVVGERVAARLRNDL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 753 LSKILTFEVNWFDIddNSSGAICSRLAKDanvvrsmVGDRMSLLVQTIS------AVIIACIIGLV-IAWRLAIVMISVQ 825
Cdd:cd18574 82 FSSLLRQDIAFFDT--HRTGELVNRLTAD-------VQEFKSSFKQCVSqglrsvTQTVGCVVSLYlISPKLTLLLLVIV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 826 PLIVVCFYTQRVLLKSLSEKASKAQDESSKLAAEAVSNIRTITAFSSQERIIKL----LKKVQEGPRRESVHRSW----- 896
Cdd:cd18574 153 PVVVLVGTLYGSFLRKLSRRAQAQVAKATGVADEALGNIRTVRAFAMEDRELELyeeeVEKAAKLNEKLGLGIGIfqgls 232
|
250 260 270
....*....|....*....|....*....|....*.
gi 15232977 897 ---LAGIVLGTsrslitctsalnFWYGGRLIADGKI 929
Cdd:cd18574 233 nlaLNGIVLGV------------LYYGGSLVSRGEL 256
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
983-1215 |
1.81e-14 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 77.82 E-value: 1.81e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 983 PDGYVAEKIKGQITFLNVD---FAYPTRPDV--------VIFENFSIEIDEGKSTAIVGTSGSGKST----IIGLIerfy 1047
Cdd:PRK15134 261 PSGDPVPLPEPASPLLDVEqlqVAFPIRKGIlkrtvdhnVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLI---- 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1048 dPLKGTVKIDGRDIRSYHLRSL---RKYISLVSQEP-------MLFAGTIRE--NIMYGGTSDKIDESEIIEAAK----- 1110
Cdd:PRK15134 337 -NSQGEIWFDGQPLHNLNRRQLlpvRHRIQVVFQDPnsslnprLNVLQIIEEglRVHQPTLSAAQREQQVIAVMEevgld 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1111 AANAHDFITslsngydtncgdkgvQLSGGQKQRIAIARAVLKNPSVLLLDEATSALDskseRVVQD---ALERVMVGR-- 1185
Cdd:PRK15134 416 PETRHRYPA---------------EFSGGQRQRIAIARALILKPSLIILDEPTSSLD----KTVQAqilALLKSLQQKhq 476
|
250 260 270
....*....|....*....|....*....|..
gi 15232977 1186 -TSIMIAHRLSTIQN-CDMIVVLGKGKIVESG 1215
Cdd:PRK15134 477 lAYLFISHDLHVVRAlCHQVIVLRQGEVVEQG 508
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
362-604 |
2.03e-14 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 78.90 E-value: 2.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 362 NHVK-FTYLSRPETtifDDLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYDPIAGEILIDGVSIDKlQVNWLRSQMGLV 440
Cdd:TIGR01257 933 NLVKiFEPSGRPAV---DRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIET-NLDAVRQSLGMC 1008
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 441 SQEPVLFA-TSITENILFGKE--DASLDEVVEAAKASNAHTfisqfplGYKTQVGERGVQMSGGQKQRIAIARAIIKSPK 517
Cdd:TIGR01257 1009 PQHNILFHhLTVAEHILFYAQlkGRSWEEAQLEMEAMLEDT-------GLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAK 1081
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 518 ILLLDEATSALDSESERVVQESLDNASIGRTTIVIAHRLStirNADV----ICVIHNGQIVETGShEELLKRIDGQYTSL 593
Cdd:TIGR01257 1082 VVVLDEPTSGVDPYSRRSIWDLLLKYRSGRTIIMSTHHMD---EADLlgdrIAIISQGRLYCSGT-PLFLKNCFGTGFYL 1157
|
250
....*....|.
gi 15232977 594 VSLQQMENEES 604
Cdd:TIGR01257 1158 TLVRKMKNIQS 1168
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
972-1213 |
2.05e-14 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 77.41 E-value: 2.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 972 LDRCTTIEPKNPDGYV-----AEKIKGQ--ITFLNVDFAYPtrpDVVIFENFSIEIDEGKSTAIVGTSGSGKSTIIGLIE 1044
Cdd:COG0488 286 LEKLEREEPPRRDKTVeirfpPPERLGKkvLELEGLSKSYG---DKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLA 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1045 RFYDPLKGTVKIdGRDIRsyhlrslrkyISLVSQEPMLFAG--TIRENIMYGgtSDKIDESEIIeaakaanahdfitsls 1122
Cdd:COG0488 363 GELEPDSGTVKL-GETVK----------IGYFDQHQEELDPdkTVLDELRDG--APGGTEQEVR---------------- 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1123 nGY-----------DTNCGDkgvqLSGGQKQRIAIARAVLKNPSVLLLDEATSALDSKSERVVQDALER----Vmvgrts 1187
Cdd:COG0488 414 -GYlgrflfsgddaFKPVGV----LSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALDDfpgtV------ 482
|
250 260
....*....|....*....|....*....
gi 15232977 1188 IMIAH-R--LSTIqnCDMIVVLGKGKIVE 1213
Cdd:COG0488 483 LLVSHdRyfLDRV--ATRILEFEDGGVRE 509
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1018-1216 |
2.51e-14 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 74.66 E-value: 2.51e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1018 IEIDEGKSTAIVGTSGSGKSTII----GLI------ERFYDPLKGTVKIDGRDIRSyhLRSLRKYISLVSQEPMLFAG-T 1086
Cdd:PRK09984 25 LNIHHGEMVALLGPSGSGKSTLLrhlsGLItgdksaGSHIELLGRTVQREGRLARD--IRKSRANTGYIFQQFNLVNRlS 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1087 IRENIMYGGTSDKIDESEIIEAAKAANAHDFITSLSN-GYDTNCGDKGVQLSGGQKQRIAIARAVLKNPSVLLLDEATSA 1165
Cdd:PRK09984 103 VLENVLIGALGSTPFWRTCFSWFTREQKQRALQALTRvGMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVILADEPIAS 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15232977 1166 LDSKSERVVQDALERVMV--GRTSIMIAHRLS-TIQNCDMIVVLGKGKIVESGT 1216
Cdd:PRK09984 183 LDPESARIVMDTLRDINQndGITVVVTLHQVDyALRYCERIVALRQGHVFYDGS 236
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
994-1192 |
2.51e-14 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 74.35 E-value: 2.51e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 994 QITFLNVDfaYPTRPdvvIFENFSIEIDEGKSTAIVGTSGSGKSTIIGLIERFYDPLKGTVKIDGRDIRSYHLRSlrkyi 1073
Cdd:PRK11248 3 QISHLYAD--YGGKP---ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAER----- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1074 SLVSQ-EPMLFAGTIRENIMYGGTSDKIDESEIIEAAKAANA--------HDFITslsngydtncgdkgvQLSGGQKQRI 1144
Cdd:PRK11248 73 GVVFQnEGLLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKkvglegaeKRYIW---------------QLSGGQRQRV 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15232977 1145 AIARAVLKNPSVLLLDEATSALDSKSERVVQDALERVM--VGRTSIMIAH 1192
Cdd:PRK11248 138 GIARALAANPQLLLLDEPFGALDAFTREQMQTLLLKLWqeTGKQVLLITH 187
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1008-1210 |
3.25e-14 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 76.89 E-value: 3.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1008 PDVVIFENFSIEIDEGKSTAIVGTSGSGKSTIIGLIERFYdP---LKGTVKIDGRDIRSYHLR-SLRKYISLVSQEPMLF 1083
Cdd:PRK13549 16 GGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PhgtYEGEIIFEGEELQASNIRdTERAGIAIIHQELALV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1084 AG-TIRENIMYGgtsDKIDESEIIE-AAKAANAHDFITSLsnGYDTNCGDKGVQLSGGQKQRIAIARAVLKNPSVLLLDE 1161
Cdd:PRK13549 95 KElSVLENIFLG---NEITPGGIMDyDAMYLRAQKLLAQL--KLDINPATPVGNLGLGQQQLVEIAKALNKQARLLILDE 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15232977 1162 ATSALDSKSERV----VQDALERvmvGRTSIMIAHRLSTIQN-CDMIVVLGKGK 1210
Cdd:PRK13549 170 PTASLTESETAVlldiIRDLKAH---GIACIYISHKLNEVKAiSDTICVIRDGR 220
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
371-538 |
3.72e-14 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 72.60 E-value: 3.72e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 371 RPETTIFDDLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYDPIAGEILIDGVSIDKLQVnwlRSQMGLVSQ----EPVL 446
Cdd:PRK13539 12 RGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDV---AEACHYLGHrnamKPAL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 447 fatSITENILF-----GKEDASLDEVVEAAKASN-AHTfisqfPLGYktqvgergvqMSGGQKQRIAIARAIIKSPKILL 520
Cdd:PRK13539 89 ---TVAENLEFwaaflGGEELDIAAALEAVGLAPlAHL-----PFGY----------LSAGQKRRVALARLLVSNRPIWI 150
|
170
....*....|....*...
gi 15232977 521 LDEATSALDSESERVVQE 538
Cdd:PRK13539 151 LDEPTAALDAAAVALFAE 168
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
358-585 |
4.63e-14 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 76.55 E-value: 4.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 358 EVEFNHVKFTYlsrpETTIFD--DLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYDPIAGEILIDGVSIDKLQVNWLRS 435
Cdd:PRK10522 322 TLELRNVTFAY----QDNGFSvgPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRK 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 436 qmglvsqepvLFATSITENILFgkeDASLDEVVEAAKASNAHTFISQFPLGYKTQVGE---RGVQMSGGQKQRIAIARAI 512
Cdd:PRK10522 398 ----------LFSAVFTDFHLF---DQLLGPEGKPANPALVEKWLERLKMAHKLELEDgriSNLKLSKGQKKRLALLLAL 464
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15232977 513 IKSPKILLLDEATSALDSESERVVQESLDNA--SIGRTTIVIAHRLSTIRNADVICVIHNGQIVE-TGSHEELLKR 585
Cdd:PRK10522 465 AEERDILLLDEWAADQDPHFRREFYQVLLPLlqEMGKTIFAISHDDHYFIHADRLLEMRNGQLSElTGEERDAASR 540
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
1026-1215 |
4.69e-14 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 75.30 E-value: 4.69e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1026 TAIVGTSGSGKSTIIGLIERFYDPLKGTVKIDGR---DIRS-YHLRSLRKYISLVSQEPMLFAG-TIRENIMYGgtsdki 1100
Cdd:PRK11144 27 TAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRvlfDAEKgICLPPEKRRIGYVFQDARLFPHyKVRGNLRYG------ 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1101 deseiieAAKAANAH-DFITSLSngydtncgdkGVQ---------LSGGQKQRIAIARAVLKNPSVLLLDEATSALDSKS 1170
Cdd:PRK11144 101 -------MAKSMVAQfDKIVALL----------GIEplldrypgsLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPR 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 15232977 1171 ERVVQDALERvMVGRTSIMI---AHRLSTI-QNCDMIVVLGKGKIVESG 1215
Cdd:PRK11144 164 KRELLPYLER-LAREINIPIlyvSHSLDEIlRLADRVVVLEQGKVKAFG 211
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
359-555 |
5.08e-14 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 71.03 E-value: 5.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 359 VEFNHVkfTYLSRPETTIFDDLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYdPIAGEilidgvSIDKLQvnwlRSQMG 438
Cdd:cd03223 1 IELENL--SLATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLW-PWGSG------RIGMPE----GEDLL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 439 LVSQEPVLFATSITENILFgkedaSLDEVveaakasnahtfisqfplgyktqvgergvqMSGGQKQRIAIARAIIKSPKI 518
Cdd:cd03223 68 FLPQRPYLPLGTLREQLIY-----PWDDV------------------------------LSGGEQQRLAFARLLLHKPKF 112
|
170 180 190
....*....|....*....|....*....|....*..
gi 15232977 519 LLLDEATSALDSESERVVQESLDNASIgrTTIVIAHR 555
Cdd:cd03223 113 VFLDEATSALDEESEDRLYQLLKELGI--TVISVGHR 147
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
995-1222 |
5.08e-14 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 74.46 E-value: 5.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 995 ITFLNVDFAYPtrpDVVIFENFSIEIDEGKSTAIVGTSGSGKSTIIGLIERFYDPLKGTVKIDGRDIRSyHLRSLRKYIS 1074
Cdd:PRK13537 8 IDFRNVEKRYG---DKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPS-RARHARQRVG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1075 LVSQEPML---FagTIRENIM-----YGGTSDKIDE--SEIIEAAKaanahdfitsLSNGYDTNCGDkgvqLSGGQKQRI 1144
Cdd:PRK13537 84 VVPQFDNLdpdF--TVRENLLvfgryFGLSAAAARAlvPPLLEFAK----------LENKADAKVGE----LSGGMKRRL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1145 AIARAVLKNPSVLLLDEATSALDSKSERVVQDALERVMV-GRTSIMIAHRLSTIQN-CDMIVVLGKGKIVESGTHSSLLE 1222
Cdd:PRK13537 148 TLARALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLLArGKTILLTTHFMEEAERlCDRLCVIEEGRKIAEGAPHALIE 227
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
359-572 |
5.20e-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: 70.56 E-value: 5.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 359 VEFNHVKFTYLSRPettIFDDLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYDPIAGEILIDgvsidklqvnwlrsqmg 438
Cdd:cd03221 1 IELENLSKTYGGKL---LLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWG----------------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 439 lvsqepvlfatsitenilfgkedasldevveaakasnAHTFISQFPlgyktqvgergvQMSGGQKQRIAIARAIIKSPKI 518
Cdd:cd03221 61 -------------------------------------STVKIGYFE------------QLSGGEKMRLALAKLLLENPNL 91
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15232977 519 LLLDEATSALDSESERVVQESLDNasIGRTTIVIAHRLSTIRN-ADVICVIHNGQ 572
Cdd:cd03221 92 LLLDEPTNHLDLESIEALEEALKE--YPGTVILVSHDRYFLDQvATKIIELEDGK 144
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
373-587 |
6.02e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 73.97 E-value: 6.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 373 ETTIFDDLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYDPIAGEI------------------LIDGVSIDKL------ 428
Cdd:PRK13651 19 ELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewifkdeknkkktkekekVLEKLVIQKTrfkkik 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 429 QVNWLRSQMGLVSQ--EPVLFATSITENILFGKEDASLDEVvEAAKASNAHTFISQFPLGYKtqvgERG-VQMSGGQKQR 505
Cdd:PRK13651 99 KIKEIRRRVGVVFQfaEYQLFEQTIEKDIIFGPVSMGVSKE-EAKKRAAKYIELVGLDESYL----QRSpFELSGGQKRR 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 506 IAIARAIIKSPKILLLDEATSALDSESERVVQESLDNA-SIGRTTIVIAHRL-STIRNADVICVIHNGQIVETGSHEELL 583
Cdd:PRK13651 174 VALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLnKQGKTIILVTHDLdNVLEWTKRTIFFKDGKIIKDGDTYDIL 253
|
....
gi 15232977 584 KRID 587
Cdd:PRK13651 254 SDNK 257
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
1009-1215 |
6.82e-14 |
|
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: 71.79 E-value: 6.82e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1009 DVVIFENFSIEIDEGKSTAIVGTSGSGKSTIIGLIERF--YDPLKGTVKIDGRDIR--SYHLRSlRKYISLVSQEPMLFA 1084
Cdd:cd03217 12 GKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITdlPPEERA-RLGIFLAFQYPPEIP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1085 G-TIRenimyggtsdkideseiieaakaanahDFITSLSNGydtncgdkgvqLSGGQKQRIAIARAVLKNPSVLLLDEAT 1163
Cdd:cd03217 91 GvKNA---------------------------DFLRYVNEG-----------FSGGEKKRNEILQLLLLEPDLAILDEPD 132
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15232977 1164 SALDSKSERVVQDALERVM-VGRTSIMIAH--RLSTIQNCDMIVVLGKGKIVESG 1215
Cdd:cd03217 133 SGLDIDALRLVAEVINKLReEGKSVLIITHyqRLLDYIKPDRVHVLYDGRIVKSG 187
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
994-1216 |
8.42e-14 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 74.49 E-value: 8.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 994 QITFLNVDFAYPTRPDVVifENFSIEIDEGKSTAIVGTSGSGKST----IIGLiERFYDplkGTVKIDGRDIRsyHLRSL 1069
Cdd:PRK11650 3 GLKLQAVRKSYDGKTQVI--KGIDLDVADGEFIVLVGPSGCGKSTllrmVAGL-ERITS---GEIWIGGRVVN--ELEPA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1070 RKYISLVSQEPMLFAG-TIRENIMYG----GTS-DKIDEsEIIEAAKAANAHDFITSlsngydtncgdKGVQLSGGQKQR 1143
Cdd:PRK11650 75 DRDIAMVFQNYALYPHmSVRENMAYGlkirGMPkAEIEE-RVAEAARILELEPLLDR-----------KPRELSGGQRQR 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15232977 1144 IAIARAVLKNPSVLLLDEATSALDSK---SERVVQDALERVMvGRTSIMIAH-RLSTIQNCDMIVVLGKGKIVESGT 1216
Cdd:PRK11650 143 VAMGRAIVREPAVFLFDEPLSNLDAKlrvQMRLEIQRLHRRL-KTTSLYVTHdQVEAMTLADRVVVMNGGVAEQIGT 218
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
359-575 |
9.31e-14 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 75.49 E-value: 9.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 359 VEFNHVKFTYlsrPETTIFDDLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYDPIAGEILIdGVSIdklqvnwlrsQMG 438
Cdd:COG0488 316 LELEGLSKSY---GDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETV----------KIG 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 439 LVSQEpvlfatsiTENIlfgKEDASLDEVVEAAKASNAHTFISQFpLGY--------KTQVGErgvqMSGGQKQRIAIAR 510
Cdd:COG0488 382 YFDQH--------QEEL---DPDKTVLDELRDGAPGGTEQEVRGY-LGRflfsgddaFKPVGV----LSGGEKARLALAK 445
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15232977 511 AIIKSPKILLLDEATSALDSESERVVQESLDNASiGrTTIVIAH-R--LSTIrnADVICVIHNGQIVE 575
Cdd:COG0488 446 LLLSPPNVLLLDEPTNHLDIETLEALEEALDDFP-G-TVLLVSHdRyfLDRV--ATRILEFEDGGVRE 509
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1023-1215 |
9.54e-14 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 75.47 E-value: 9.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1023 GKSTAIVGTSGSGKSTIIGLIERFYDPLKGTVKIDGRdiRSYHLRSLRKY---ISLVSQEPMLFAG-TIRENIMYGGTSD 1098
Cdd:PRK15439 37 GEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGN--PCARLTPAKAHqlgIYLVPQEPLLFPNlSVKENILFGLPKR 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1099 KIDESEIIEAAKAANAHdfitsLSngYDTNCGdkgvQLSGGQKQRIAIARAVLKNPSVLLLDEATSALD-SKSERVVQDA 1177
Cdd:PRK15439 115 QASMQKMKQLLAALGCQ-----LD--LDSSAG----SLEVADRQIVEILRGLMRDSRILILDEPTASLTpAETERLFSRI 183
|
170 180 190
....*....|....*....|....*....|....*....
gi 15232977 1178 LERVMVGRTSIMIAHRLSTI-QNCDMIVVLGKGKIVESG 1215
Cdd:PRK15439 184 RELLAQGVGIVFISHKLPEIrQLADRISVMRDGTIALSG 222
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
375-584 |
9.66e-14 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 72.37 E-value: 9.66e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 375 TIFDDLCLKIPAGKTVALVGGSGSGKSTVisllqrFY------DPIAGEILIDGVSIDKLQVnWLRSQMGL--VSQEPVL 446
Cdd:COG1137 17 TVVKDVSLEVNQGEIVGLLGPNGAGKTTT------FYmivglvKPDSGRIFLDGEDITHLPM-HKRARLGIgyLPQEASI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 447 FAT-SITENILfgkedASLdEVVEAAKA---SNAHTFISQFPLGY--KTqvgeRGVQMSGGQKQRIAIARAIIKSPKILL 520
Cdd:COG1137 90 FRKlTVEDNIL-----AVL-ELRKLSKKereERLEELLEEFGITHlrKS----KAYSLSGGERRRVEIARALATNPKFIL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15232977 521 LDEATSALD----SESERVVQEsLDNASIG--------RTTIVIAHRlstirnadvICVIHNGQIVETGSHEELLK 584
Cdd:COG1137 160 LDEPFAGVDpiavADIQKIIRH-LKERGIGvlitdhnvRETLGICDR---------AYIISEGKVLAEGTPEEILN 225
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
998-1216 |
9.68e-14 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 73.99 E-value: 9.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 998 LNVDFAYPTrPDVVIFENFSIEIDEGKSTAIVGTSGSGKS----TIIGLIERfYDPLKGTVKIDGRDI---RSYHLRSLR 1070
Cdd:PRK09473 18 LRVTFSTPD-GDVTAVNDLNFSLRAGETLGIVGESGSGKSqtafALMGLLAA-NGRIGGSATFNGREIlnlPEKELNKLR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1071 -KYISLVSQEPML-------FAGTIRENIMYG---GTSDKIDES-EIIEAAKAANAHDFITSLSNgydtncgdkgvQLSG 1138
Cdd:PRK09473 96 aEQISMIFQDPMTslnpymrVGEQLMEVLMLHkgmSKAEAFEESvRMLDAVKMPEARKRMKMYPH-----------EFSG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1139 GQKQRIAIARAVLKNPSVLLLDEATSALDSkserVVQ-------DALERVMvGRTSIMIAHRLSTIQN-CDMIVVLGKGK 1210
Cdd:PRK09473 165 GMRQRVMIAMALLCRPKLLIADEPTTALDV----TVQaqimtllNELKREF-NTAIIMITHDLGVVAGiCDKVLVMYAGR 239
|
....*.
gi 15232977 1211 IVESGT 1216
Cdd:PRK09473 240 TMEYGN 245
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
81-250 |
1.20e-13 |
|
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349987 [Multi-domain] Cd Length: 291 Bit Score: 72.90 E-value: 1.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 81 VVALLYVACGSWVICFLEGYCWTRTGERQAARMREKYLRAVLRQDVGYFDlhVTSTSDVITSISSDSLVIQDFLSeKLPN 160
Cdd:cd18543 42 VLLLLALGVAEAVLSFLRRYLAGRLSLGVEHDLRTDLFAHLQRLDGAFHD--RWQSGQLLSRATSDLSLVQRFLA-FGPF 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 161 FLMNASAFVASYIVSFILMWRLTIVGFPFIILLLVPGLMYGRALVSISRKIHEQYNEAGSIAEQAISSVRTVYAFGSENK 240
Cdd:cd18543 119 LLGNLLTLVVGLVVMLVLSPPLALVALASLPPLVLVARRFRRRYFPASRRAQDQAGDLATVVEESVTGIRVVKAFGRERR 198
|
170
....*....|
gi 15232977 241 MIGKFSTALR 250
Cdd:cd18543 199 ELDRFEAAAR 208
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
370-585 |
1.48e-13 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 71.65 E-value: 1.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 370 SRPETTIFDDLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYDPIAGEILIDGvsidklQVNWLRS-QMGlvsqepvlFA 448
Cdd:COG1134 35 RREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNG------RVSALLElGAG--------FH 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 449 TSIT--ENILFG--------KE-DASLDEVVEaakasnahtF--ISQF---PLG-YktqvgergvqmSGGQKQRIAIARA 511
Cdd:COG1134 101 PELTgrENIYLNgrllglsrKEiDEKFDEIVE---------FaeLGDFidqPVKtY-----------SSGMRARLAFAVA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15232977 512 IIKSPKILLLDEATSALDSE----SERVVQESLDNasiGRTTIVIAHRLSTIRN-ADVICVIHNGQIVETGSHEELLKR 585
Cdd:COG1134 161 TAVDPDILLVDEVLAVGDAAfqkkCLARIRELRES---GRTVIFVSHSMGAVRRlCDRAIWLEKGRLVMDGDPEEVIAA 236
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1013-1211 |
1.75e-13 |
|
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: 70.15 E-value: 1.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1013 FENFSIEIDEGKSTAIVGTSGSGKS----TIIGLIErfydPLKGTVKIDGRDIRSYHLRSLRKY-ISLVSQEPM---LFA 1084
Cdd:cd03215 16 VRDVSFEVRAGEIVGIAGLVGNGQTelaeALFGLRP----PASGEITLDGKPVTRRSPRDAIRAgIAYVPEDRKregLVL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1085 G-TIRENImyggtsdkideseiieaakaanahdFITSLsngydtncgdkgvqLSGGQKQRIAIARAVLKNPSVLLLDEAT 1163
Cdd:cd03215 92 DlSVAENI-------------------------ALSSL--------------LSGGNQQKVVLARWLARDPRVLILDEPT 132
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15232977 1164 SALD--SKSE--RVVQDALERvmvGRTSIMIahrlST-----IQNCDMIVVLGKGKI 1211
Cdd:cd03215 133 RGVDvgAKAEiyRLIRELADA---GKAVLLI----SSeldelLGLCDRILVMYEGRI 182
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
1012-1170 |
1.94e-13 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 71.39 E-value: 1.94e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1012 IFENFSIEIDEGKSTAIVGTSGSGKSTIIGLIERFYDPLKGTVKIDGRDIRSYHLRS---LR-KYISLVSQEPMLFAG-T 1086
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAkaeLRnQKLGFIYQFHHLLPDfT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1087 IRENIMYGGTSDKIDESEIIEaakaaNAHDFITSLsnGYDTNCGDKGVQLSGGQKQRIAIARAVLKNPSVLLLDEATSAL 1166
Cdd:PRK11629 104 ALENVAMPLLIGKKKPAEINS-----RALEMLAAV--GLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNL 176
|
....
gi 15232977 1167 DSKS 1170
Cdd:PRK11629 177 DARN 180
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
369-555 |
2.29e-13 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 70.76 E-value: 2.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 369 LSRPETTIFDDLCLKIPAGKTVALVGGSGSGKSTVISLLQRFY--DPIAGEILIDGVSIDklqvnwlrsqmglvsQEpvl 446
Cdd:COG2401 38 LRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDVPDNQFG---------------RE--- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 447 faTSITENILfgkEDASLDEVVE---AAKASNAHTFISQFPlgyktqvgergvQMSGGQKQRIAIARAIIKSPKILLLDE 523
Cdd:COG2401 100 --ASLIDAIG---RKGDFKDAVEllnAVGLSDAVLWLRRFK------------ELSTGQKFRFRLALLLAERPKLLVIDE 162
|
170 180 190
....*....|....*....|....*....|....
gi 15232977 524 ATSALDSESERVVQESLDNAS--IGRTTIVIAHR 555
Cdd:COG2401 163 FCSHLDRQTAKRVARNLQKLArrAGITLVVATHH 196
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
379-581 |
2.95e-13 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 72.60 E-value: 2.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 379 DLCLKI----PAGKTVALVGGSGSGKSTVISLLQRFYDPIAGEILIDG-VSIDKLQVNWL---RSQMGLVSQEPVLFA-T 449
Cdd:PRK11144 12 DLCLTVnltlPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGrVLFDAEKGICLppeKRRIGYVFQDARLFPhY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 450 SITENILFG---KEDASLDEVV-----EAakasnahtFISQFPLGyktqvgergvqMSGGQKQRIAIARAIIKSPKILLL 521
Cdd:PRK11144 92 KVRGNLRYGmakSMVAQFDKIVallgiEP--------LLDRYPGS-----------LSGGEKQRVAIGRALLTAPELLLM 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15232977 522 DEATSALDSESERVVQESLDNAS--IGRTTIVIAHRLSTI-RNADVICVIHNGQIVETGSHEE 581
Cdd:PRK11144 153 DEPLASLDLPRKRELLPYLERLAreINIPILYVSHSLDEIlRLADRVVVLEQGKVKAFGPLEE 215
|
|
| ABC_6TM_exporter_like |
cd18540 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
669-929 |
4.01e-13 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349984 [Multi-domain] Cd Length: 295 Bit Score: 71.36 E-value: 4.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 669 WKHALYGCLSAALVGVLQPVSAYSAGSVISVFFLtshDQIKEKTRIYVLLFVGLAIFSFLVNisqhYGFAYMG----EYL 744
Cdd:cd18540 1 KKLLILLIILMLLVALLDAVFPLLTKYAIDHFIT---PGTLDGLTGFILLYLGLILIQALSV----FLFIRLAgkieMGV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 745 TKRIREQMLSKILTFEVNWFDidDNSSGAICSRLAKDANVVRSMVGDRMSLLVQTISAVIIACIIGLVIAWRLA-IVMIS 823
Cdd:cd18540 74 SYDLRKKAFEHLQTLSFSYFD--KTPVGWIMARVTSDTQRLGEIISWGLVDLVWGITYMIGILIVMLILNWKLAlIVLAV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 824 VQPLIVVCFYTQRVLLKSlsekASKAQDESSKLAA---EAVSNIRTITAFSSQERIIKLLKKVQEGPRRESVHRSWLAGI 900
Cdd:cd18540 152 VPVLAVVSIYFQKKILKA----YRKVRKINSRITGafnEGITGAKTTKTLVREEKNLREFKELTEEMRRASVRAARLSAL 227
|
250 260
....*....|....*....|....*....
gi 15232977 901 VLGTSRSLITCTSALNFWYGGRLIADGKI 929
Cdd:cd18540 228 FLPIVLFLGSIATALVLWYGGILVLAGAI 256
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
1008-1215 |
4.46e-13 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 70.50 E-value: 4.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1008 PDVVIFENFSIEIDEGKSTAIVGTSGSGKS----TIIGLIERFYDPLKGTVKIDGRDIRSYHLRSlrKYISLVSQEP--- 1080
Cdd:PRK10418 14 AAQPLVHGVSLTLQRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGRVLLDGKPVAPCALRG--RKIATIMQNPrsa 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1081 ----MLFAGTIRENIM-YGGTSDKIDESEIIEAAKAANAHDFITSLSngydtncgdkgVQLSGGQKQRIAIARAVLKNPS 1155
Cdd:PRK10418 92 fnplHTMHTHARETCLaLGKPADDATLTAALEAVGLENAARVLKLYP-----------FEMSGGMLQRMMIALALLCEAP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15232977 1156 VLLLDEATSALDSKSERVVQDALERVMVGRTS--IMIAHRLSTIQNC-DMIVVLGKGKIVESG 1215
Cdd:PRK10418 161 FIIADEPTTDLDVVAQARILDLLESIVQKRALgmLLVTHDMGVVARLaDDVAVMSHGRIVEQG 223
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
375-597 |
5.13e-13 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 71.68 E-value: 5.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 375 TIFDDLCLKIPAGKTVALVGGSGSGKS-TVISLLQRFYDP--IAGEILIDGVSIDKL---QVNWLRS-QMGLVSQEPVlf 447
Cdd:PRK09473 30 TAVNDLNFSLRAGETLGIVGESGSGKSqTAFALMGLLAANgrIGGSATFNGREILNLpekELNKLRAeQISMIFQDPM-- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 448 aTS------ITENIL--------FGKEDASLDEV--VEAAKASNAHTFISQFPLgyktqvgergvQMSGGQKQRIAIARA 511
Cdd:PRK09473 108 -TSlnpymrVGEQLMevlmlhkgMSKAEAFEESVrmLDAVKMPEARKRMKMYPH-----------EFSGGMRQRVMIAMA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 512 IIKSPKILLLDEATSALDSESERVVQESLD------NASIgrttIVIAHRLSTIRN-ADVICVIHNGQIVETGSHEE--- 581
Cdd:PRK09473 176 LLCRPKLLIADEPTTALDVTVQAQIMTLLNelkrefNTAI----IMITHDLGVVAGiCDKVLVMYAGRTMEYGNARDvfy 251
|
250 260
....*....|....*....|....*...
gi 15232977 582 ---------LLK---RIDGQYTSLVSLQ 597
Cdd:PRK09473 252 qpshpysigLLNavpRLDAEGESLLTIP 279
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
1007-1220 |
9.90e-13 |
|
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: 68.15 E-value: 9.90e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1007 RPDVVIFENFSIEIDEGKSTAIVGTSGSGKSTIIGLIERFYDPLKGTVKIDGRDIRSyhLRSLRkyislvsQEPMLFAG- 1085
Cdd:TIGR01189 10 RGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAE--QRDEP-------HENILYLGh 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1086 --------TIRENIMYGgTSDKIDESEIIEAAKAAnahdfiTSLSNGYDTNCGdkgvQLSGGQKQRIAIARAVLKNPSVL 1157
Cdd:TIGR01189 81 lpglkpelSALENLHFW-AAIHGGAQRTIEDALAA------VGLTGFEDLPAA----QLSAGQQRRLALARLWLSRRPLW 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15232977 1158 LLDEATSALDSKSERVVqdalervmvgrTSIMIAHrlstiqncdmivvLGKGKIVESGTHSSL 1220
Cdd:TIGR01189 150 ILDEPTTALDKAGVALL-----------AGLLRAH-------------LARGGIVLLTTHQDL 188
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
373-580 |
1.04e-12 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 69.29 E-value: 1.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 373 ETTIFDDLCLKIPAGKTVALVGGSGSGKSTVISLL--QRFYDPIAGEILIDGVSIDKLQVNwLRSQMGL----------- 439
Cdd:CHL00131 19 ENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIagHPAYKILEGDILFKGESILDLEPE-ERAHLGIflafqypieip 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 440 -VSQEPVLFATSITENILFGKEDAS----LDEVVEAAKASN-AHTFISqfplgyktqvgeRGVQ--MSGGQKQRIAIARA 511
Cdd:CHL00131 98 gVSNADFLRLAYNSKRKFQGLPELDplefLEIINEKLKLVGmDPSFLS------------RNVNegFSGGEKKRNEILQM 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15232977 512 IIKSPKILLLDEATSALDSESERVVQESLDN-ASIGRTTIVIAH--RLSTIRNADVICVIHNGQIVETGSHE 580
Cdd:CHL00131 166 ALLDSELAILDETDSGLDIDALKIIAEGINKlMTSENSIILITHyqRLLDYIKPDYVHVMQNGKIIKTGDAE 237
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
995-1210 |
1.21e-12 |
|
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: 72.47 E-value: 1.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 995 ITFLNVDFAYPTRpDVVIfENFSIEIDEGKSTAIVGTSGSGKSTIIGLIERFYDPLKGTVKIDGRDIRSYhlrslrkyis 1074
Cdd:TIGR00954 452 IKFENIPLVTPNG-DVLI-ESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPAKGKLFY---------- 519
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1075 lVSQEPMLFAGTIRENIMYGGTSDK-----IDESEIIEAAKAANAHDFITSlSNGYDTNCGDKGVqLSGGQKQRIAIARA 1149
Cdd:TIGR00954 520 -VPQRPYMTLGTLRDQIIYPDSSEDmkrrgLSDKDLEQILDNVQLTHILER-EGGWSAVQDWMDV-LSGGEKQRIAMARL 596
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15232977 1150 VLKNPSVLLLDEATSALDSKSERVVQDALERvmVGRTSIMIAHRLSTIQNCDMIVVL-GKGK 1210
Cdd:TIGR00954 597 FYHKPQFAILDECTSAVSVDVEGYMYRLCRE--FGITLFSVSHRKSLWKYHEYLLYMdGRGG 656
|
|
| ABC_6TM_TAP2 |
cd18590 |
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ... |
90-321 |
1.46e-12 |
|
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen processing 2 (TAP2); This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350034 [Multi-domain] Cd Length: 289 Bit Score: 69.67 E-value: 1.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 90 GSWVICFLEGYCWTRTGERQAARMREKYLRAVLRQDVGYFDlhVTSTSDVITSISSDSlviqDFLSEKLPnflMNASAFV 169
Cdd:cd18590 48 GSSLSAGLRGGLFMCTLSRLNLRLRHQLFSSLVQQDIGFFE--KTKTGDLTSRLSTDT----TLMSRSVA---LNANVLL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 170 AS-------YIVSFILMWRLTIVGFPFIILLLVPGLMYGRALVSISRKIHEQYNEAGSIAEQAISSVRTVYAFGSENKMI 242
Cdd:cd18590 119 RSlvktlgmLGFMLSLSWQLTLLTLIEMPLTAIAQKVYNTYHQKLSQAVQDSIAKAGELAREAVSSIRTVRSFKAEEEEA 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 243 GKFSTALRGSVKLGLRQGLAKGITIGSNGVTH-AIWAFLTWYGSRLVMN-HGSKGGTVfvviSCITYGGvSLGQSLSNLK 320
Cdd:cd18590 199 CRYSEALERTYNLKDRRDTVRAVYLLVRRVLQlGVQVLMLYCGRQLIQSgHLTTGSLV----SFILYQK-NLGSYVRTLV 273
|
.
gi 15232977 321 Y 321
Cdd:cd18590 274 Y 274
|
|
| ABC_6TM_TAP2 |
cd18590 |
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ... |
737-929 |
1.90e-12 |
|
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen processing 2 (TAP2); This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350034 [Multi-domain] Cd Length: 289 Bit Score: 69.29 E-value: 1.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 737 FAYMGEYLTKRIREQMLSKILTFEVNWFDidDNSSGAICSRLAKDANVVRSMVGDRMSLLVQTISAVIIACIIGLVIAWR 816
Cdd:cd18590 60 FMCTLSRLNLRLRHQLFSSLVQQDIGFFE--KTKTGDLTSRLSTDTTLMSRSVALNANVLLRSLVKTLGMLGFMLSLSWQ 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 817 LAIVMISVQPLIVVcfyTQRV---LLKSLSEKASKAQDESSKLAAEAVSNIRTITAFSSQERIIKLLKKVQEGPRRESVH 893
Cdd:cd18590 138 LTLLTLIEMPLTAI---AQKVyntYHQKLSQAVQDSIAKAGELAREAVSSIRTVRSFKAEEEEACRYSEALERTYNLKDR 214
|
170 180 190
....*....|....*....|....*....|....*.
gi 15232977 894 RSWLAGIVLGTSRSLITCTSALNFWYGGRLIADGKI 929
Cdd:cd18590 215 RDTVRAVYLLVRRVLQLGVQVLMLYCGRQLIQSGHL 250
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
83-305 |
2.00e-12 |
|
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (TrmA) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349988 [Multi-domain] Cd Length: 294 Bit Score: 69.34 E-value: 2.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 83 ALLYVAC--GSWVICFLEGYCWTRTGERQAARMREKYLRAVLRQDVGYFDLhvTSTSDVITSISSDSLVIQDFLSEKLPN 160
Cdd:cd18544 44 ALLYLGLllLSFLLQYLQTYLLQKLGQRIIYDLRRDLFSHIQRLPLSFFDR--TPVGRLVTRVTNDTEALNELFTSGLVT 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 161 FLMNASAFVASYIVSFILMWRLTIVGFPFIILLLVPGLMYGRALVSISRKIHEQYNEA-GSIAEQaISSVRTVYAFGSEN 239
Cdd:cd18544 122 LIGDLLLLIGILIAMFLLNWRLALISLLVLPLLLLATYLFRKKSRKAYREVREKLSRLnAFLQES-ISGMSVIQLFNREK 200
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15232977 240 KMIGKFSTALRGSVKLGLRQglakgITIGS------NGVTHAIWAFLTWYGSRLVMNHGSKGGTVFVVISCI 305
Cdd:cd18544 201 REFEEFDEINQEYRKANLKS-----IKLFAlfrplvELLSSLALALVLWYGGGQVLSGAVTLGVLYAFIQYI 267
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
715-929 |
2.17e-12 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349994 [Multi-domain] Cd Length: 294 Bit Score: 69.43 E-value: 2.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 715 YVLLFVGLAIFSFLVNISQHYGFAYMGEYLTKRIREQMLSKILTFEVNWFDidDNSSGAICSRLAKDANVVRSMVGDRMS 794
Cdd:cd18550 41 LALGMVAVAVASALLGVVQTYLSARIGQGVMYDLRVQLYAHLQRMSLAFFT--RTRTGEIQSRLNNDVGGAQSVVTGTLT 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 795 LLVQTISAVIIACIIGLVIAWRLAIVMISVQPLIVVCfyTQRV--LLKSLSEKASKAQDESSKLAAE--AVSNIRTITAF 870
Cdd:cd18550 119 SVVSNVVTLVATLVAMLALDWRLALLSLVLLPLFVLP--TRRVgrRRRKLTREQQEKLAELNSIMQEtlSVSGALLVKLF 196
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 871 SSQERIIKLLKKVQEGPRRESVhRSWLAGIVLGTSRSLIT-CTSALNFWYGGRLIADGKI 929
Cdd:cd18550 197 GREDDEAARFARRSRELRDLGV-RQALAGRWFFAALGLFTaIGPALVYWVGGLLVIGGGL 255
|
|
| ABC_6TM_ABCB9_like |
cd18784 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ... |
744-968 |
2.18e-12 |
|
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and similar proteins; ATP-binding cassette sub-family B member 9 is also known as transporter associated with antigen processing, TAP-like protein, TAPL, and ABCB9. It is a half transporter comprises a homodimeric lysosomal peptide transport complex. It belongs to the ABC_6TM_TAP_ABCB8_10_like subgroup of the ABC_6TM exporter family. The ABC_6TM exporter family represents the six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in the ABC_6TM exporter family. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs. The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting chemical diversity of the translocated substrates, whereas NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional unit.
Pssm-ID: 350057 [Multi-domain] Cd Length: 289 Bit Score: 69.26 E-value: 2.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 744 LTKRIREQMLSKILTFEVNWFDidDNSSGAICSRLAKDANVVRSMVGDRMSLLVQTISAVIIACIIGLVIAWRLAIVMIS 823
Cdd:cd18784 67 LNIRIRNLLFRSIVSQEIGFFD--TVKTGDITSRLTSDTTTMSDTVSLNLNIFLRSLVKAIGVIVFMFKLSWQLSLVTLI 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 824 VQPLI--VVCFYTQrvLLKSLSEKASKAQDESSKLAAEAVSNIRTITAFSSQE----RIIKLLKKVQEGPRREsvhrSWL 897
Cdd:cd18784 145 GLPLIaiVSKVYGD--YYKKLSKAVQDSLAKANEVAEETISSIRTVRSFANEDgeanRYSEKLKDTYKLKIKE----ALA 218
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15232977 898 AGIVLGTSRSLITCTSALNFWYGGRLIADGKIVSKAFFEIFLIFVTTGRVIADAGTMTTDLARGLDAVGSV 968
Cdd:cd18784 219 YGGYVWSNELTELALTVSTLYYGGHLVITGQISGGNLISFILYQLELGSCLESVGSVYTGLMQAVGAAEKV 289
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
1023-1210 |
2.21e-12 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 71.45 E-value: 2.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1023 GKSTAIVGTSGSGKSTIIGLIE-RFY-DPLKGTVKIDGRDIRsyhlRSLRKYISLVSQEPMLFAG-TIRENIMYGGT--- 1096
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAgRIQgNNFTGTILANNRKPT----KQILKRTGFVTQDDILYPHlTVRETLVFCSLlrl 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1097 SDKIDESEIIEAAKAANAHDFITSLSNGYDTNCGDKGVqlSGGQKQRIAIARAVLKNPSVLLLDEATSALDSKSE-RVVQ 1175
Cdd:PLN03211 170 PKSLTKQEKILVAESVISELGLTKCENTIIGNSFIRGI--SGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAyRLVL 247
|
170 180 190
....*....|....*....|....*....|....*..
gi 15232977 1176 DALERVMVGRTSIMIAHRLST--IQNCDMIVVLGKGK 1210
Cdd:PLN03211 248 TLGSLAQKGKTIVTSMHQPSSrvYQMFDSVLVLSEGR 284
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1014-1222 |
2.26e-12 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 71.42 E-value: 2.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1014 ENFSIEIDEGKSTAIVGTSGSGKSTIIGLIERFYDPLKGTVKIDGRDIRS---YHLRSLRKYISLVSQEPmlFAG----- 1085
Cdd:PRK10261 341 EKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTlspGKLQALRRDIQFIFQDP--YASldprq 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1086 TIRENIMyggtsDKIDESEIIEAAKAANAHDFITSLSNGYDTNCGDKGVQLSGGQKQRIAIARAVLKNPSVLLLDEATSA 1165
Cdd:PRK10261 419 TVGDSIM-----EPLRVHGLLPGKAAAARVAWLLERVGLLPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSA 493
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15232977 1166 LD-SKSERVVQ---DaLERVMvGRTSIMIAHRLSTIQNCD-MIVVLGKGKIVESGTHSSLLE 1222
Cdd:PRK10261 494 LDvSIRGQIINlllD-LQRDF-GIAYLFISHDMAVVERIShRVAVMYLGQIVEIGPRRAVFE 553
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
1015-1237 |
2.27e-12 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 68.76 E-value: 2.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1015 NFSIEIDEGKSTAIVGTSGSGKSTIIGLIERFYDPLKGTVKIDGRDIRSYHLRSLRKYISLVSQEPMLFAGTIRENIMYG 1094
Cdd:PRK15056 25 DASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNLVAYVPQSEEVDWSFPVLVEDVVMMG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1095 GTSD-------KIDESEIIEAAKAAnahdfiTSLSNGYDTNCGdkgvQLSGGQKQRIAIARAVLKNPSVLLLDEATSALD 1167
Cdd:PRK15056 105 RYGHmgwlrraKKRDRQIVTAALAR------VDMVEFRHRQIG----ELSGGQKKRVFLARAIAQQGQVILLDEPFTGVD 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15232977 1168 SKSE-RVVQDALERVMVGRTSIMIAHRLSTIQN-CDMIVVLgKGKIVESgthssllekGPTGTYFSLAGIQR 1237
Cdd:PRK15056 175 VKTEaRIISLLRELRDEGKTMLVSTHNLGSVTEfCDYTVMV-KGTVLAS---------GPTETTFTAENLEL 236
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
375-583 |
2.42e-12 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 68.38 E-value: 2.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 375 TIFDDLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYDPIAGEILIDGVSIDKLQVNW-LRSQMGLVSQEPVLFAT-SIT 452
Cdd:PRK10895 17 RVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHArARRGIGYLPQEASIFRRlSVY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 453 ENILfgkedASL---DEVVEAAKASNAHTFISQFPLGY-KTQVGErgvQMSGGQKQRIAIARAIIKSPKILLLDEATSAL 528
Cdd:PRK10895 97 DNLM-----AVLqirDDLSAEQREDRANELMEEFHIEHlRDSMGQ---SLSGGERRRVEIARALAANPKFILLDEPFAGV 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15232977 529 DSES----ERVVQESLDNasiGRTTIVIAHrlsTIRNADVIC----VIHNGQIVETGSHEELL 583
Cdd:PRK10895 169 DPISvidiKRIIEHLRDS---GLGVLITDH---NVRETLAVCerayIVSQGHLIAHGTPTEIL 225
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
376-585 |
2.62e-12 |
|
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: 70.99 E-value: 2.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 376 IFDDLCLKIPAGKTVALVGGSGSGKSTVISLLQRF--YDPIAGEIL-----------IDGVSIDKLQVNWLRSQMGLVSQ 442
Cdd:TIGR03269 15 VLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIyhvalcekcgyVERPSKVGEPCPVCGGTLEPEEV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 443 EPVLFATSITENI-------------LFGkEDASLDEVVEA-------AKAS--NAHTFISQFPLGYKTQVGERgvQMSG 500
Cdd:TIGR03269 95 DFWNLSDKLRRRIrkriaimlqrtfaLYG-DDTVLDNVLEAleeigyeGKEAvgRAVDLIEMVQLSHRITHIAR--DLSG 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 501 GQKQRIAIARAIIKSPKILLLDEATSALDSESERVVQESLDNASI--GRTTIVIAHRLSTIRN-ADVICVIHNGQIVETG 577
Cdd:TIGR03269 172 GEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKasGISMVLTSHWPEVIEDlSDKAIWLENGEIKEEG 251
|
....*...
gi 15232977 578 SHEELLKR 585
Cdd:TIGR03269 252 TPDEVVAV 259
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1002-1215 |
2.71e-12 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 68.50 E-value: 2.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1002 FAYPTRPdvvIFENFSIEIDEGKSTAIVGTSGSGKSTIIGLIERFYDPLKGTVKIDGR--DIRSYHLRSLRKYISLVSQE 1079
Cdd:PRK13638 9 FRYQDEP---VLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKplDYSKRGLLALRQQVATVFQD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1080 P--MLFAGTIRENIMYGGTSDKIDESEII----EAAKAANAHDFitslsNGYDTNCgdkgvqLSGGQKQRIAIARAVLKN 1153
Cdd:PRK13638 86 PeqQIFYTDIDSDIAFSLRNLGVPEAEITrrvdEALTLVDAQHF-----RHQPIQC------LSHGQKKRVAIAGALVLQ 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15232977 1154 PSVLLLDEATSALDSKSERVVQDALERVMV-GRTSIMIAHRLSTI-QNCDMIVVLGKGKIVESG 1215
Cdd:PRK13638 155 ARYLLLDEPTAGLDPAGRTQMIAIIRRIVAqGNHVIISSHDIDLIyEISDAVYVLRQGQILTHG 218
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
716-929 |
3.73e-12 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350008 [Multi-domain] Cd Length: 307 Bit Score: 68.69 E-value: 3.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 716 VLLFVGLAIFSFLVNISQHYGFAYMGEYLTKRIREQMLSKILTFEVNWFDidDNSSGAICSRLAKDANVVRSMVgdrMSL 795
Cdd:cd18564 57 AAALVGIALLRGLASYAGTYLTALVGQRVVLDLRRDLFAHLQRLSLSFHD--RRRTGDLLSRLTGDVGAIQDLL---VSG 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 796 LVQTISAVIIacIIGLVIA-----WRLAIVMISVQPL--IVVCFYTQRVllKSLSEKASKAQDESSKLAAEAVSNIRTIT 868
Cdd:cd18564 132 VLPLLTNLLT--LVGMLGVmfwldWQLALIALAVAPLllLAARRFSRRI--KEASREQRRREGALASVAQESLSAIRVVQ 207
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15232977 869 AFSSQERIIKLLKKVQEGPRRESVH----RSWLAGIVLGtsrsLITCTSALNFWYGGRLIADGKI 929
Cdd:cd18564 208 AFGREEHEERRFARENRKSLRAGLRaarlQALLSPVVDV----LVAVGTALVLWFGAWLVLAGRL 268
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
1016-1216 |
3.73e-12 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 67.65 E-value: 3.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1016 FSIEIDEGKSTAIVGTSGSGKSTII----GLIerfydPLKGTVKIDGRDIRSYHLRSL---RKYisLVSQEPMLFAGTIR 1088
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLarmaGLL-----PGSGSIQFAGQPLEAWSAAELarhRAY--LSQQQTPPFAMPVF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1089 ENI---MYGGTSDKIDESEIIEAAKAANAHDFITSLSNgydtncgdkgvQLSGGQKQRIAIARAVLK-----NPS--VLL 1158
Cdd:PRK03695 88 QYLtlhQPDKTRTEAVASALNEVAEALGLDDKLGRSVN-----------QLSGGEWQRVRLAAVVLQvwpdiNPAgqLLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15232977 1159 LDEATSALDskserVVQD-ALERVMV-----GRTSIMIAHRLS-TIQNCDMIVVLGKGKIVESGT 1216
Cdd:PRK03695 157 LDEPMNSLD-----VAQQaALDRLLSelcqqGIAVVMSSHDLNhTLRHADRVWLLKQGKLLASGR 216
|
|
| ABC_6TM_TAP1 |
cd18589 |
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ... |
81-296 |
3.82e-12 |
|
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen processing 1 (TAP1); This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350033 [Multi-domain] Cd Length: 289 Bit Score: 68.65 E-value: 3.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 81 VVALLYVAcgSWVICFLEGYCWTRTGERQAARMREKYLRAVLRQDVGYFDlhVTSTSDVITSISSDSLVIQDFLSEKLPN 160
Cdd:cd18589 41 VMSLLTIA--SAVSEFVCDLIYNITMSRIHSRLQGLVFAAVLRQEIAFFD--SNQTGDIVSRVTTDTEDMSESLSENLSL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 161 FLMNASAFVASYIVSFILMWRL---TIVGFPfiILLLVPGLMyGRALVSISRKIHEQYNEAGSIAEQAISSVRTVYAFGS 237
Cdd:cd18589 117 LMWYLARGLFLFIFMLWLSPKLallTALGLP--LLLLVPKFV-GKFQQSLAVQVQKSLARANQVAVETFSAMKTVRSFAN 193
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 238 ENKMIGKFSTALRGSVKLGLRQGLAKGITIGSNGVTH-AIWAFLTWYGSRLVMNHGSKGG 296
Cdd:cd18589 194 EEGEAQRYRQRLQKTYRLNKKEAAAYAVSMWTSSFSGlALKVGILYYGGQLVTAGTVSSG 253
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
369-584 |
4.26e-12 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 67.93 E-value: 4.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 369 LSRPETTIFDDLCLKIPAGKTVALVGGSGSGKSTVISLLQ-RFYDPIA-------GEILIDG---VSIDKLQVNWLRSQM 437
Cdd:PRK13547 9 VARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAgDLTGGGAprgarvtGDVTLNGeplAAIDAPRLARLRAVL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 438 GLVSQEPvlFATSITENILFGKedasLDEVVEAAKASNAHTFISQFPL---GYKTQVGERGVQMSGGQKQRIAIARAI-- 512
Cdd:PRK13547 89 PQAAQPA--FAFSAREIVLLGR----YPHARRAGALTHRDGEIAWQALalaGATALVGRDVTTLSGGELARVQFARVLaq 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 513 -------IKSPKILLLDEATSALDSESERVVQESLDNAS----IGRTTIVIAHRLSTiRNADVICVIHNGQIVETGSHEE 581
Cdd:PRK13547 163 lwpphdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLArdwnLGVLAIVHDPNLAA-RHADRIAMLADGAIVAHGAPAD 241
|
...
gi 15232977 582 LLK 584
Cdd:PRK13547 242 VLT 244
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
378-577 |
4.50e-12 |
|
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: 67.36 E-value: 4.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 378 DDLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYDPIAGEILIDGVSIDKLQVNWLRsQMGLV--SQEPVLFATSITENI 455
Cdd:cd03267 38 KGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLR-RIGVVfgQKTQLWWDLPVIDSF 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 456 LFGKEDASLDEvvEAAKASNAHtFISQFPLG--YKTQVgeRgvQMSGGQKQRIAIARAIIKSPKILLLDEATSALDSESE 533
Cdd:cd03267 117 YLLAAIYDLPP--ARFKKRLDE-LSELLDLEelLDTPV--R--QLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQ 189
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 15232977 534 RVVQESLD--NASIGRTTIVIAHRLSTI-RNADVICVIHNGQIVETG 577
Cdd:cd03267 190 ENIRNFLKeyNRERGTTVLLTSHYMKDIeALARRVLVIDKGRLLYDG 236
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
377-573 |
5.02e-12 |
|
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: 65.92 E-value: 5.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 377 FDDLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYDPIAGEILIDGVSIDKLQV-NWLRSQMGLVSQEPV---LFAT-SI 451
Cdd:cd03215 16 VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPrDAIRAGIAYVPEDRKregLVLDlSV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 452 TENILFGkedasldevveaakasnahtfisqfplgyktqvgergVQMSGGQKQRIAIARAIIKSPKILLLDEATSALDSE 531
Cdd:cd03215 96 AENIALS-------------------------------------SLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVG 138
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 15232977 532 SERVVQESL-DNASIGRTTIVIahrlST-----IRNADVICVIHNGQI 573
Cdd:cd03215 139 AKAEIYRLIrELADAGKAVLLI----SSeldelLGLCDRILVMYEGRI 182
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
716-929 |
5.95e-12 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350051 [Multi-domain] Cd Length: 293 Bit Score: 67.95 E-value: 5.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 716 VLLFVGLAIFSFLVNISQHYgfayMGEYLTKRIREQMLSKILTFEVNWFDidDNSSGAICSRLAKDANVVRSMVGDrmsL 795
Cdd:cd18778 47 LGAYLLRALLNFLRIYLNHV----AEQKVVADLRSDLYDKLQRLSLRYFD--DRQTGDLMSRVINDVANVERLIAD---G 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 796 LVQTISAV---IIACIIGLVIAWRLAIVMISVQPLIVVC--FYTQRVllkslSEKASKAQDESSKLAA---EAVSNIRTI 867
Cdd:cd18778 118 IPQGITNVltlVGVAIILFSINPKLALLTLIPIPFLALGawLYSKKV-----RPRYRKVREALGELNAllqDNLSGIREI 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15232977 868 TAFSSQERIIKLLKKVQEGPRRESVHRSWLAGIVLGTSRSLITCTSALNFWYGGRLIADGKI 929
Cdd:cd18778 193 QAFGREEEEAKRFEALSRRYRKAQLRAMKLWAIFHPLMEFLTSLGTVLVLGFGGRLVLAGEL 254
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
1012-1213 |
6.79e-12 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 66.52 E-value: 6.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1012 IFENFSIEIDEGKSTAIVGTSGSGKSTIIGLIERFY--DPLKGTVKIDGRDIrsyhlrslrkyislvSQEpmlfaGTIRE 1089
Cdd:COG2401 45 VLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDVPDNQF---------------GRE-----ASLID 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1090 NImyGGTSDKIDESEIIEAAKAANAHDFITSLSNgydtncgdkgvqLSGGQKQRIAIARAVLKNPSVLLLDEATSALDSK 1169
Cdd:COG2401 105 AI--GRKGDFKDAVELLNAVGLSDAVLWLRRFKE------------LSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQ 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 15232977 1170 SERVVQDALERVM--VGRTSIMIAHR---LSTIQNcDMIVVLGKGKIVE 1213
Cdd:COG2401 171 TAKRVARNLQKLArrAGITLVVATHHydvIDDLQP-DLLIFVGYGGVPE 218
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
378-582 |
7.04e-12 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 66.94 E-value: 7.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 378 DDLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYDPIAGEILIDGVSIDKL---QVnwlrSQMGLVS--QEPVLFAT-SI 451
Cdd:PRK11300 22 NNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLpghQI----ARMGVVRtfQHVRLFREmTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 452 TENILFGKEDASLDEVV------------EAAKASNAHTFISQFPLgykTQVGERGV-QMSGGQKQRIAIARAIIKSPKI 518
Cdd:PRK11300 98 IENLLVAQHQQLKTGLFsgllktpafrraESEALDRAATWLERVGL---LEHANRQAgNLAYGQQRRLEIARCMVTQPEI 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15232977 519 LLLDEATSALDSESERVVQESLDN--ASIGRTTIVIAHRLSTIRN-ADVICVIHNGQIVETGSHEEL 582
Cdd:PRK11300 175 LMLDEPAAGLNPKETKELDELIAElrNEHNVTVLLIEHDMKLVMGiSDRIYVVNQGTPLANGTPEEI 241
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
360-576 |
7.11e-12 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 69.55 E-value: 7.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 360 EFNHVKFTYlsrPETTIFDDLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYDPIAGEILIDGVsidklQVNW------L 433
Cdd:PRK11288 6 SFDGIGKTF---PGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQ-----EMRFasttaaL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 434 RSQMGLVSQE----PVLfatSITENILFGKEDASL-----DEVVEAAKASNAHTFIS---QFPLGYktqvgergvqMSGG 501
Cdd:PRK11288 78 AAGVAIIYQElhlvPEM---TVAENLYLGQLPHKGgivnrRLLNYEAREQLEHLGVDidpDTPLKY----------LSIG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 502 QKQRIAIARAIIKSPKILLLDEATSALDS-ESE---RVVQESLDNasiGRTTIVIAHRLSTI-RNADVICVIHNGQIVET 576
Cdd:PRK11288 145 QRQMVEIAKALARNARVIAFDEPTSSLSArEIEqlfRVIRELRAE---GRVILYVSHRMEEIfALCDAITVFKDGRYVAT 221
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
998-1216 |
8.32e-12 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 69.50 E-value: 8.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 998 LNVDFaYPTRPDVVIFENFSIEIDEGKSTAIVGTSGSGKSTIIGLIERFYDPLKGTVK-------------IDGRDIRSY 1064
Cdd:PRK10261 18 LNIAF-MQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQcdkmllrrrsrqvIELSEQSAA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1065 HLRSLRKY-ISLVSQEPML-----------FAGTIRENIMYGGTSDKIDESEIIEAAKAANAHDFITSLSNgydtncgdk 1132
Cdd:PRK10261 97 QMRHVRGAdMAMIFQEPMTslnpvftvgeqIAESIRLHQGASREEAMVEAKRMLDQVRIPEAQTILSRYPH--------- 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1133 gvQLSGGQKQRIAIARAVLKNPSVLLLDEATSALD-SKSERVVQdaLERVMVGRTS---IMIAHRLSTIQN-CDMIVVLG 1207
Cdd:PRK10261 168 --QLSGGMRQRVMIAMALSCRPAVLIADEPTTALDvTIQAQILQ--LIKVLQKEMSmgvIFITHDMGVVAEiADRVLVMY 243
|
....*....
gi 15232977 1208 KGKIVESGT 1216
Cdd:PRK10261 244 QGEAVETGS 252
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1006-1220 |
8.40e-12 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 67.10 E-value: 8.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1006 TRPDVVIFENFSIEIDEGKSTAIVGTSGSGKSTIIGLIERFYDPLKGTVKIDGRDI----RSyHLRSLRKYISLVSQEPM 1081
Cdd:PRK11831 16 TRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIpamsRS-RLYTVRKRMSMLFQSGA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1082 LFAG-TIRENIMY-----GGTSDKIDESEI---IEAAKAANAHDFITSlsngydtncgdkgvQLSGGQKQRIAIARAVLK 1152
Cdd:PRK11831 95 LFTDmNVFDNVAYplrehTQLPAPLLHSTVmmkLEAVGLRGAAKLMPS--------------ELSGGMARRAALARAIAL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15232977 1153 NPSVLLLDEATSALDSKSERVVQ---DALERVMvGRTSIMIAHRLSTIQN-CDMIVVLGKGKIVESGTHSSL 1220
Cdd:PRK11831 161 EPDLIMFDEPFVGQDPITMGVLVkliSELNSAL-GVTCVVVSHDVPEVLSiADHAYIVADKKIVAHGSAQAL 231
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
1020-1213 |
9.07e-12 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 66.34 E-value: 9.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1020 IDEGKSTAIVGTSGSGKSTIIGLIERFYDPLKGTVKIDGRDIRSYH------LRSlrKYISLVSQEPMLFAG-TIRENI- 1091
Cdd:PRK10584 33 VKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDeearakLRA--KHVGFVFQSFMLIPTlNALENVe 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1092 ---MYGGTSDKIDESEIIEAAKAANAHDFITSLSngydtncgdkgVQLSGGQKQRIAIARAVLKNPSVLLLDEATSALDS 1168
Cdd:PRK10584 111 lpaLLRGESSRQSRNGAKALLEQLGLGKRLDHLP-----------AQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDR 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 15232977 1169 KSERVVQD---ALERVMvGRTSIMIAHRLSTIQNCDMIVVLGKGKIVE 1213
Cdd:PRK10584 180 QTGDKIADllfSLNREH-GTTLILVTHDLQLAARCDRRLRLVNGQLQE 226
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
51-332 |
1.01e-11 |
|
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette transporters; This group includes the 6-TMD of the peptidase-containing ATP-binding cassette transporters (PCATs) such as Clostridium thermocellum PCAT1, a polypeptide processing and secretion transporter, and LagD, a bacteriocin ABC transporter from Lactococcus lactis. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs. The transporters involved in protein secretion often contain additional peptidase domains essential for substrate processing. These peptidase domains belong to the cysteine protease superfamily, classified as family C39, bacteriocin-processing peptidase. LagD is highly similar to the peptidase-containing ATP-binding cassette transporters (PCATs). In Gram-positive bacteria, the PCATs are responsible for exporting quorum-sensing or antimicrobial peptides called bacteriocins.
Pssm-ID: 350014 [Multi-domain] Cd Length: 294 Bit Score: 67.09 E-value: 1.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 51 VVVFIFNTLLNNLGTSSS-------------NNKTFMQTISknvVALLYVACGSWVICFLEGYCWTRTGERQAARMREKY 117
Cdd:cd18570 5 ILILLLSLLITLLGIAGSfffqiliddiipsGDINLLNIIS---IGLILLYLFQSLLSYIRSYLLLKLSQKLDIRLILGY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 118 LRAVLRQDVGYFDLHvtSTSDVITSISsDSLVIQDFLSEKLPNFLMNASAFVASYIVSFILMWRLTIVGFPFIILLLVPG 197
Cdd:cd18570 82 FKHLLKLPLSFFETR--KTGEIISRFN-DANKIREAISSTTISLFLDLLMVIISGIILFFYNWKLFLITLLIIPLYILII 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 198 LMYGRALVSISRKIHEQYNEAGSIAEQAISSVRTVYAFGSENKMIGKFSTALRGSVKLGLRQGLAKGITIGSNGVTHAIW 277
Cdd:cd18570 159 LLFNKPFKKKNREVMESNAELNSYLIESLKGIETIKSLNAEEQFLKKIEKKFSKLLKKSFKLGKLSNLQSSIKGLISLIG 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 15232977 278 -AFLTWYGSRLVMNHGSKGGTVFVVISCITYGGVSLgQSLSNL-KYFSEAFVAWERI 332
Cdd:cd18570 239 sLLILWIGSYLVIKGQLSLGQLIAFNALLGYFLGPI-ENLINLqPKIQEAKVAADRL 294
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1014-1216 |
1.19e-11 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 67.46 E-value: 1.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1014 ENFSIEIDEGKSTAIVGTSGSGKS----TIIGLIERFYDPLKGTVKIDGRDIRSYHLRSLRKYI----SLVSQEPMLFAG 1085
Cdd:PRK11022 24 DRISYSVKQGEVVGIVGESGSGKSvsslAIMGLIDYPGRVMAEKLEFNGQDLQRISEKERRNLVgaevAMIFQDPMTSLN 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1086 ---TIRENIM-----YGGTSDKIDESEIIEAAKAANAHDFITSLSNgYDTncgdkgvQLSGGQKQRIAIARAVLKNPSVL 1157
Cdd:PRK11022 104 pcyTVGFQIMeaikvHQGGNKKTRRQRAIDLLNQVGIPDPASRLDV-YPH-------QLSGGMSQRVMIAMAIACRPKLL 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15232977 1158 LLDEATSALDSKSERVVQDAL------ERVMVgrtsIMIAHRLSTI-QNCDMIVVLGKGKIVESGT 1216
Cdd:PRK11022 176 IADEPTTALDVTIQAQIIELLlelqqkENMAL----VLITHDLALVaEAAHKIIVMYAGQVVETGK 237
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1013-1212 |
1.27e-11 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 68.51 E-value: 1.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1013 FENFSIEIDEGKSTAIVGTSGSGKS----TIIGLierfYDPLKGTVKIDGR--DIRSYHlRSLRKYISLVSQEPM---LF 1083
Cdd:COG1129 268 VRDVSFSVRAGEILGIAGLVGAGRTelarALFGA----DPADSGEIRLDGKpvRIRSPR-DAIRAGIAYVPEDRKgegLV 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1084 AG-TIRENIM---YGGTSDK--IDESEIIEAAKaanahDFITSLS---NGYDTNCGdkgvQLSGGQKQRIAIARAVLKNP 1154
Cdd:COG1129 343 LDlSIRENITlasLDRLSRGglLDRRRERALAE-----EYIKRLRiktPSPEQPVG----NLSGGNQQKVVLAKWLATDP 413
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15232977 1155 SVLLLDEATSALD--SKSE--RVVQDALERvmvGRTSIMIahrlST-----IQNCDMIVVLGKGKIV 1212
Cdd:COG1129 414 KVLILDEPTRGIDvgAKAEiyRLIRELAAE---GKAVIVI----SSelpelLGLSDRILVMREGRIV 473
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
999-1221 |
1.32e-11 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 66.07 E-value: 1.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 999 NVDFAYPTRPdvvIFENFSIEIDEGKSTAIVGTSGSGKST----IIGLIERFydplKGTVKIDGRDIR--SYHLRSlRKY 1072
Cdd:PRK10895 8 NLAKAYKGRR---VVEDVSLTVNSGEIVGLLGPNGAGKTTtfymVVGIVPRD----AGNIIIDDEDISllPLHARA-RRG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1073 ISLVSQEPMLFAG-TIRENIM-YGGTSDKIDESEIIEAAKAANAHDFITSLSNGYdtncgdkGVQLSGGQKQRIAIARAV 1150
Cdd:PRK10895 80 IGYLPQEASIFRRlSVYDNLMaVLQIRDDLSAEQREDRANELMEEFHIEHLRDSM-------GQSLSGGERRRVEIARAL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15232977 1151 LKNPSVLLLDEATSALDSKSERVVQDALERVMVGRTSIMIA-HRL-STIQNCDMIVVLGKGKIVESGTHSSLL 1221
Cdd:PRK10895 153 AANPKFILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITdHNVrETLAVCERAYIVSQGHLIAHGTPTEIL 225
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
378-577 |
2.01e-11 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 67.89 E-value: 2.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 378 DDLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYDPIAGEILIDGVSIDKLQvNWLRSQMG--LVSQE-PVLFATSITEN 454
Cdd:PRK09700 22 KSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLD-HKLAAQLGigIIYQElSVIDELTVLEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 455 ILFG----KEDASLDEVVEAAKASNAHTFISQfpLGYKTQVGERGVQMSGGQKQRIAIARAIIKSPKILLLDEATSAL-D 529
Cdd:PRK09700 101 LYIGrhltKKVCGVNIIDWREMRVRAAMMLLR--VGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLtN 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 15232977 530 SESERV--VQESLDNAsiGRTTIVIAHRLSTIRN-ADVICVIHNGQIVETG 577
Cdd:PRK09700 179 KEVDYLflIMNQLRKE--GTAIVYISHKLAEIRRiCDRYTVMKDGSSVCSG 227
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1014-1221 |
2.15e-11 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 67.81 E-value: 2.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1014 ENFSIEIDEGKSTAIVGTSGSGKS-TIIGLIERFYDP----LKGTVKIDGRDIRSYHLRSLRKY----ISLVSQEPMLFA 1084
Cdd:PRK15134 26 NDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPpvvyPSGDIRFHGESLLHASEQTLRGVrgnkIAMIFQEPMVSL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1085 G---TIRENI-----MYGGTSDKIDESEIIEAAKAANAHDFITSLSngydtncgDKGVQLSGGQKQRIAIARAVLKNPSV 1156
Cdd:PRK15134 106 NplhTLEKQLyevlsLHRGMRREAARGEILNCLDRVGIRQAAKRLT--------DYPHQLSGGERQRVMIAMALLTRPEL 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15232977 1157 LLLDEATSALDSKSERVVQDALE--RVMVGRTSIMIAHRLSTI-QNCDMIVVLGKGKIVESGTHSSLL 1221
Cdd:PRK15134 178 LIADEPTTALDVSVQAQILQLLRelQQELNMGLLFITHNLSIVrKLADRVAVMQNGRCVEQNRAATLF 245
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
378-572 |
2.19e-11 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 67.72 E-value: 2.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 378 DDLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYDPIAGEILIDGvsiDKLQVNWLR-SQ---MGLVSQEPVLFAT-SIT 452
Cdd:PRK10762 21 SGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLG---KEVTFNGPKsSQeagIGIIHQELNLIPQlTIA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 453 ENILFGKEDAS------LDEVVEAAKASNAHTFISQFPlgyKTQVGErgvqMSGGQKQRIAIARAIIKSPKILLLDEATS 526
Cdd:PRK10762 98 ENIFLGREFVNrfgridWKKMYAEADKLLARLNLRFSS---DKLVGE----LSIGEQQMVEIAKVLSFESKVIIMDEPTD 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 15232977 527 AL-DSESE---RVVQESLDNasiGRTTIVIAHRLSTIRN-ADVICVIHNGQ 572
Cdd:PRK10762 171 ALtDTETEslfRVIRELKSQ---GRGIVYISHRLKEIFEiCDDVTVFRDGQ 218
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
378-591 |
2.20e-11 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 66.69 E-value: 2.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 378 DDLCLKIPAGKTVALVGGSGSGKStVISLlqrfydPIAGeiLID---GVSIDKLQVN--------------WLRSQMGLV 440
Cdd:PRK11022 24 DRISYSVKQGEVVGIVGESGSGKS-VSSL------AIMG--LIDypgRVMAEKLEFNgqdlqrisekerrnLVGAEVAMI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 441 SQEPVlfaTSITENILFGKEdasldeVVEAAKA--SNAHTFISQFPLGYKTQVG------ERGV---QMSGGQKQRIAIA 509
Cdd:PRK11022 95 FQDPM---TSLNPCYTVGFQ------IMEAIKVhqGGNKKTRRQRAIDLLNQVGipdpasRLDVyphQLSGGMSQRVMIA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 510 RAIIKSPKILLLDEATSALDSESERVVQESL------DNASIgrttIVIAHRLSTI-RNADVICVIHNGQIVETGSHEEL 582
Cdd:PRK11022 166 MAIACRPKLLIADEPTTALDVTIQAQIIELLlelqqkENMAL----VLITHDLALVaEAAHKIIVMYAGQVVETGKAHDI 241
|
....*....
gi 15232977 583 LKRIDGQYT 591
Cdd:PRK11022 242 FRAPRHPYT 250
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1009-1212 |
2.27e-11 |
|
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: 67.93 E-value: 2.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1009 DVVIFENFSIEIDEGKSTAIVGTSGSGKSTIIGLIERFY--DPLKGTVKIDGRDIRSYHLRSL-RKYISLVSQEPMLFAG 1085
Cdd:TIGR02633 13 GVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYphGTWDGEIYWSGSPLKASNIRDTeRAGIVIIHQELTLVPE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1086 -TIRENIMYGG----TSDKIDESEIIEaakaaNAHDFITSLSNGYDTNCGDKGvQLSGGQKQRIAIARAVLKNPSVLLLD 1160
Cdd:TIGR02633 93 lSVAENIFLGNeitlPGGRMAYNAMYL-----RAKNLLRELQLDADNVTRPVG-DYGGGQQQLVEIAKALNKQARLLILD 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15232977 1161 EATSALDSKSERVVQDALERVMV-GRTSIMIAHRLSTIQN-CDMIVVLGKGKIV 1212
Cdd:TIGR02633 167 EPSSSLTEKETEILLDIIRDLKAhGVACVYISHKLNEVKAvCDTICVIRDGQHV 220
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
1012-1211 |
2.37e-11 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 65.47 E-value: 2.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1012 IFENFSIEIDEGKSTAIVGTSGSGKSTIIGLIERFYDPLKGTVkIDGrdirSYHLRSLRKYISLVSQEPMLFA-GTIREN 1090
Cdd:PRK11247 27 VLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL-LAG----TAPLAEAREDTRLMFQDARLLPwKKVIDN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1091 IMYGGTSDKIDES-EIIEAAKAAN-AHDFITSLSngydtncgdkgvqlsGGQKQRIAIARAVLKNPSVLLLDEATSALDS 1168
Cdd:PRK11247 102 VGLGLKGQWRDAAlQALAAVGLADrANEWPAALS---------------GGQKQRVALARALIHRPGLLLLDEPLGALDA 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 15232977 1169 KSERVVQDALERVMV--GRTSIMIAHRLS-TIQNCDMIVVLGKGKI 1211
Cdd:PRK11247 167 LTRIEMQDLIESLWQqhGFTVLLVTHDVSeAVAMADRVLLIEEGKI 212
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1015-1221 |
2.57e-11 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 64.90 E-value: 2.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1015 NFSIEIDEGKSTAIVGTSGSGKSTIIGLIERFYDPLKGTVKIDGRDIRSYHL-RSLRKYISLVSQEPMLFAG-TIRENIM 1092
Cdd:PRK11614 23 EVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTaKIMREAVAIVPEGRRVFSRmTVEENLA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1093 YGGT-SDKIDESEIIEaakaaNAHDFITSLSNGYDTNCGdkgvQLSGGQKQRIAIARAVLKNPSVLLLDEATSALDSKSE 1171
Cdd:PRK11614 103 MGGFfAERDQFQERIK-----WVYELFPRLHERRIQRAG----TMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPIII 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15232977 1172 RVVQDALERVMVGRTSIMIAHRLS--TIQNCDMIVVLGKGKIVESGTHSSLL 1221
Cdd:PRK11614 174 QQIFDTIEQLREQGMTIFLVEQNAnqALKLADRGYVLENGHVVLEDTGDALL 225
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
380-584 |
3.05e-11 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 64.95 E-value: 3.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 380 LCLKIPAGKTVALVGGSGSGKSTVIS----LLqrfydPIAGEILIDGVSIDKLQVNWLRSQMG-LVSQEPVLFATSIten 454
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLArmagLL-----PGSGSIQFAGQPLEAWSAAELARHRAyLSQQQTPPFAMPV--- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 455 ilFGKEDASL-DEVVEAAKASNAHTFISQFPLGYKTqvgERGV-QMSGGQKQRIAIARAIIK-SPKI------LLLDEAT 525
Cdd:PRK03695 87 --FQYLTLHQpDKTRTEAVASALNEVAEALGLDDKL---GRSVnQLSGGEWQRVRLAAVVLQvWPDInpagqlLLLDEPM 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15232977 526 SALDseserVVQES-LDN-----ASIGRTTIVIAHRLS-TIRNADVICVIHNGQIVETGSHEELLK 584
Cdd:PRK03695 162 NSLD-----VAQQAaLDRllselCQQGIAVVMSSHDLNhTLRHADRVWLLKQGKLLASGRRDEVLT 222
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
355-583 |
3.10e-11 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 64.90 E-value: 3.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 355 MKGEVEFNHVKFTYlsrPETTIFDDLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYDPIAGEILIDGVSIDKLQV-NWL 433
Cdd:PRK11614 2 EKVMLSFDKVSAHY---GKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTaKIM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 434 RSQMGLVSQEPVLFA-TSITENILFGKEDASLDEVVEAAKasnahTFISQFPLGYKTQVgERGVQMSGGQKQRIAIARAI 512
Cdd:PRK11614 79 REAVAIVPEGRRVFSrMTVEENLAMGGFFAERDQFQERIK-----WVYELFPRLHERRI-QRAGTMSGGEQQMLAIGRAL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15232977 513 IKSPKILLLDEATSALdseSERVVQESLDNASIGRT---TIVIAHRLS--TIRNADVICVIHNGQIVETGSHEELL 583
Cdd:PRK11614 153 MSQPRLLLLDEPSLGL---APIIIQQIFDTIEQLREqgmTIFLVEQNAnqALKLADRGYVLENGHVVLEDTGDALL 225
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
715-1161 |
3.85e-11 |
|
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: 67.13 E-value: 3.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 715 YVLLFVGLAIFSFLVNISQHYGFAYMGEYLTKRIREQMLSKILTfeVNWFDIDDNSSGAICSRLAKDANVVrSMVGDRMS 794
Cdd:COG4615 50 LLLLFAGLLVLLLLSRLASQLLLTRLGQHAVARLRLRLSRRILA--APLERLERIGAARLLAALTEDVRTI-SQAFVRLP 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 795 LLVQTIsAVIIACIIGL-VIAWRLAIVMISVQPLIVVCFYTQRVLLKSLSEKASKAQDessklaaeavsnirtitafssq 873
Cdd:COG4615 127 ELLQSV-ALVLGCLAYLaWLSPPLFLLTLVLLGLGVAGYRLLVRRARRHLRRAREAED---------------------- 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 874 eRIIKLLKKVQEG--------PRRESVHRSWLAGIVlGTSRSLITctSALNFWyggrliADGKIVSKAFFEIF---LIFV 942
Cdd:COG4615 184 -RLFKHFRALLEGfkelklnrRRRRAFFDEDLQPTA-ERYRDLRI--RADTIF------ALANNWGNLLFFALiglILFL 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 943 TTGRVIADAGTMTT--------------------DLARG---LDAVGSVFAVLDRCTTIEPKNPDGYVAEKIKgQITFLN 999
Cdd:COG4615 254 LPALGWADPAVLSGfvlvllflrgplsqlvgalpTLSRAnvaLRKIEELELALAAAEPAAADAAAPPAPADFQ-TLELRG 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1000 VDFAYPTRPDVVIFE--NFSIEIDEGKSTAIVGTSGSGKSTIIGLIERFYDPLKGTVKIDGRDIRSYHLRSLRKYISLVS 1077
Cdd:COG4615 333 VTYRYPGEDGDEGFTlgPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAYRQLFSAVF 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1078 QEPMLFAGtireniMYGGTSDKIDEseiieaakAANAH------DFITSLSNGYDTNcgdkgVQLSGGQKQRIAIARAVL 1151
Cdd:COG4615 413 SDFHLFDR------LLGLDGEADPA--------RARELlerlelDHKVSVEDGRFST-----TDLSQGQRKRLALLVALL 473
|
490
....*....|
gi 15232977 1152 KNPSVLLLDE 1161
Cdd:COG4615 474 EDRPILVFDE 483
|
|
| ABC_6TM_TAP1 |
cd18589 |
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ... |
747-931 |
4.12e-11 |
|
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen processing 1 (TAP1); This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350033 [Multi-domain] Cd Length: 289 Bit Score: 65.19 E-value: 4.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 747 RIREQMLSKILTFEVNWFDidDNSSGAICSRLAKDANVVRSMVGDRMSLLVQTISAVIIACIIGLVIAWRLAIVMISVQP 826
Cdd:cd18589 70 RLQGLVFAAVLRQEIAFFD--SNQTGDIVSRVTTDTEDMSESLSENLSLLMWYLARGLFLFIFMLWLSPKLALLTALGLP 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 827 LIVVCFYTQRVLLKSLSEKASKAQDESSKLAAEAVSNIRTITAFSSQE----RIIKLLKKVQEGPRRESVhrSWLAGIVL 902
Cdd:cd18589 148 LLLLVPKFVGKFQQSLAVQVQKSLARANQVAVETFSAMKTVRSFANEEgeaqRYRQRLQKTYRLNKKEAA--AYAVSMWT 225
|
170 180
....*....|....*....|....*....
gi 15232977 903 GTSRSLITCTSALnfWYGGRLIADGKIVS 931
Cdd:cd18589 226 SSFSGLALKVGIL--YYGGQLVTAGTVSS 252
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
362-580 |
4.29e-11 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 64.90 E-value: 4.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 362 NHVKFTYlsRPETTIFDDLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYDPIAGEILIDGVSIDK-LQVNWLrsqmGLV 440
Cdd:PRK15056 10 NDVTVTW--RNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQaLQKNLV----AYV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 441 SQE-------PVLfatsITENILFGK---------EDASLDEVVEAAKASnahtfISQFPLGYKtQVGErgvqMSGGQKQ 504
Cdd:PRK15056 84 PQSeevdwsfPVL----VEDVVMMGRyghmgwlrrAKKRDRQIVTAALAR-----VDMVEFRHR-QIGE----LSGGQKK 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15232977 505 RIAIARAIIKSPKILLLDEATSALDSESE-RVVQESLDNASIGRTTIVIAHRLSTIRNADVICVIHNGQIVETGSHE 580
Cdd:PRK15056 150 RVFLARAIAQQGQVILLDEPFTGVDVKTEaRIISLLRELRDEGKTMLVSTHNLGSVTEFCDYTVMVKGTVLASGPTE 226
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
353-558 |
4.91e-11 |
|
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: 66.88 E-value: 4.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 353 ERMKGEV-EFNHVKFTYLSRpetTIFDDLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYDPIAGEILIdGVSIDKLQVN 431
Cdd:TIGR03719 316 PRLGDKViEAENLTKAFGDK---LLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETVKLAYVD 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 432 WLRSQMglvsqEPvlfATSITENILFGkedasLDEVVEAAKASNAHTFISQFplGYKTQVGERGV-QMSGGQKQRIAIAR 510
Cdd:TIGR03719 392 QSRDAL-----DP---NKTVWEEISGG-----LDIIKLGKREIPSRAYVGRF--NFKGSDQQKKVgQLSGGERNRVHLAK 456
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15232977 511 AIIKSPKILLLDEATSALDSESERVVQESLDNasIGRTTIVIAH------RLST 558
Cdd:TIGR03719 457 TLKSGGNVLLLDEPTNDLDVETLRALEEALLN--FAGCAVVISHdrwfldRIAT 508
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
715-929 |
5.56e-11 |
|
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349987 [Multi-domain] Cd Length: 291 Bit Score: 64.81 E-value: 5.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 715 YVLLFVGLAIFSFLVNISQHY---GFAYMGEYltkRIREQMLSKILTFEVNWFDidDNSSGAICSRLAKDANVVRSMVGD 791
Cdd:cd18543 41 LVLLLLALGVAEAVLSFLRRYlagRLSLGVEH---DLRTDLFAHLQRLDGAFHD--RWQSGQLLSRATSDLSLVQRFLAF 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 792 RMSLLVQTISAVIIACIIgLVIAWRLA-IVMISVQPLIVVCFYTQRVLLKSlsekASKAQDESSKLAA---EAVSNIRTI 867
Cdd:cd18543 116 GPFLLGNLLTLVVGLVVM-LVLSPPLAlVALASLPPLVLVARRFRRRYFPA----SRRAQDQAGDLATvveESVTGIRVV 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15232977 868 TAFSSQERIIKLLKKVQEGPRRESVHRSWLAGIVLGTSRSLITCTSALNFWYGGRLIADGKI 929
Cdd:cd18543 191 KAFGRERRELDRFEAAARRLRATRLRAARLRARFWPLLEALPELGLAAVLALGGWLVANGSL 252
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1002-1221 |
6.27e-11 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 64.43 E-value: 6.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1002 FAYPT----RPDVVIFENFSIEIDEGKSTAIVGTSGSGKSTIIGLIERFYDPLKGTVKIDGRDIR--SYHLRSLRkyISL 1075
Cdd:PRK15112 14 FRYRTgwfrRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHfgDYSYRSQR--IRM 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1076 VSQEP-----------MLFAGTIRENIMYGGTSDkidESEIIEAAKAANahdFITSLSNGYDTncgdkgvQLSGGQKQRI 1144
Cdd:PRK15112 92 IFQDPstslnprqrisQILDFPLRLNTDLEPEQR---EKQIIETLRQVG---LLPDHASYYPH-------MLAPGQKQRL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1145 AIARAVLKNPSVLLLDEATSALD-SKSERVVQDALE-RVMVGRTSIMIAHRLSTIQN-CDMIVVLGKGKIVESGTHSSLL 1221
Cdd:PRK15112 159 GLARALILRPKVIIADEALASLDmSMRSQLINLMLElQEKQGISYIYVTQHLGMMKHiSDQVLVMHQGEVVERGSTADVL 238
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
371-586 |
6.62e-11 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 65.11 E-value: 6.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 371 RPETTIF---DDLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYDPIAGEILIDGVSIDKLQVNWLRsQMGLV----SQ- 442
Cdd:COG4586 29 RREYREVeavDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPFKRRKEFAR-RIGVVfgqrSQl 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 443 ---EPVL--FAtsiteniLFGKedasLDEVVEAAKASNAHTFISQFPLG--YKTQVgeRgvQMSGGQKQRIAIARAIIKS 515
Cdd:COG4586 108 wwdLPAIdsFR-------LLKA----IYRIPDAEYKKRLDELVELLDLGelLDTPV--R--QLSLGQRMRCELAAALLHR 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15232977 516 PKILLLDEATSALDSESERVVQESLD--NASIGRTTIVIAHRLSTIRN-ADVICVIHNGQIVETGSHEELLKRI 586
Cdd:COG4586 173 PKILFLDEPTIGLDVVSKEAIREFLKeyNRERGTTILLTSHDMDDIEAlCDRVIVIDHGRIIYDGSLEELKERF 246
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
941-1211 |
6.70e-11 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 66.81 E-value: 6.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 941 FVTTGRVIADAGTMTTDLARGLDAVGSVFAVL-DRCTTIEPKNPDGYVAEKIkgqITFLNVDFAYPTRPdvVIFENFSIE 1019
Cdd:PLN03073 457 FIDKFRYNAKRASLVQSRIKALDRLGHVDAVVnDPDYKFEFPTPDDRPGPPI---ISFSDASFGYPGGP--LLFKNLNFG 531
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1020 IDEGKSTAIVGTSGSGKSTIIGLIERFYDPLKGTVkidgrdirsyhLRSLRKYISLVSQE----------PMLFAGTIre 1089
Cdd:PLN03073 532 IDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTV-----------FRSAKVRMAVFSQHhvdgldlssnPLLYMMRC-- 598
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1090 nimYGGtsdkideseIIEAAKAANAHDFITSlsngydtncGDKGVQ----LSGGQKQRIAIARAVLKNPSVLLLDEATSA 1165
Cdd:PLN03073 599 ---FPG---------VPEQKLRAHLGSFGVT---------GNLALQpmytLSGGQKSRVAFAKITFKKPHILLLDEPSNH 657
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 15232977 1166 LDskservvQDALERVMVGRT-----SIMIAHRLSTIQ-NCDMIVVLGKGKI 1211
Cdd:PLN03073 658 LD-------LDAVEALIQGLVlfqggVLMVSHDEHLISgSVDELWVVSEGKV 702
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
998-1179 |
7.69e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 63.05 E-value: 7.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 998 LNVDFAYPTRPdvvIFENFSIEIDEGKSTAIVGTSGSGKSTIIGLIERFYDPLKGTVKIDGRDIRsyhlRSLRKYislvs 1077
Cdd:PRK13540 5 IELDFDYHDQP---LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIK----KDLCTY----- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1078 QEPMLFAG---------TIRENIMYG--GTSDKIDESEIIEaakaanahdfITSLSNGYDTNCGdkgvQLSGGQKQRIAI 1146
Cdd:PRK13540 73 QKQLCFVGhrsginpylTLRENCLYDihFSPGAVGITELCR----------LFSLEHLIDYPCG----LLSSGQKRQVAL 138
|
170 180 190
....*....|....*....|....*....|...
gi 15232977 1147 ARAVLKNPSVLLLDEATSALDSKSERVVQDALE 1179
Cdd:PRK13540 139 LRLWMSKAKLWLLDEPLVALDELSLLTIITKIQ 171
|
|
| ABC_6TM_YOR1_D2_like |
cd18606 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC ... |
714-882 |
8.57e-11 |
|
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC subfamily; This group includes the six-transmembrane domain 1 (TMD1) of the yeast Yor1p, an oligomycin resistance ABC transporter, and similar proteins. Members of this group belong to the MRP (multidrug resistance-associated protein) subfamily (ABCC). In addition to Yor1p, yeast ABCC (also termed MRP/CFTR) subfamily also comprises five other members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p, and Vmr1p), which are not included in this group. Yor1p is a plasma membrane ATP-binding transporter that mediates export of many different organic anions including oligomycin. While Yor1p has been shown to localize to the plasma membrane, the other 4 members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p and Vmr1p) have been shown to localize to the vacuolar membrane.
Pssm-ID: 350050 [Multi-domain] Cd Length: 290 Bit Score: 64.42 E-value: 8.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 714 IYVLLFVGLAIFSFLVNISqhygFAYMGEYLTKRIREQMLSKILTFEVNWFDIddNSSGAICSRLAKDANVVRSMVGDRM 793
Cdd:cd18606 40 IYAGLGVLQAIFLFLFGLL----LAYLGIRASKRLHNKALKRVLRAPMSFFDT--TPLGRILNRFSKDTDVLDNELPDSL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 794 SLLVQTISAVIiaCIIGLVIA---WrLAIVMIsvqPLIVVCFYTQRVLLKSlsekaskAQD----ES---SKLAA---EA 860
Cdd:cd18606 114 RMFLYTLSSII--GTFILIIIylpW-FAIALP---PLLVLYYFIANYYRAS-------SRElkrlESilrSFVYAnfsES 180
|
170 180
....*....|....*....|..
gi 15232977 861 VSNIRTITAFSSQERIIKLLKK 882
Cdd:cd18606 181 LSGLSTIRAYGAQDRFIKKNEK 202
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1008-1215 |
9.15e-11 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 65.96 E-value: 9.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1008 PDVVIFENFSIEIDEGKSTAIVGTSGSGKSTIIGLIERFYDPLKGTVKIDGRDI-RSYHLRSLRKYISLVSQE-PMLFAG 1085
Cdd:PRK09700 16 GPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYnKLDHKLAAQLGIGIIYQElSVIDEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1086 TIRENIMYGGTSDK-------IDESEIIEAAKaanahdfITSLSNGYDTNCGDKGVQLSGGQKQRIAIARAVLKNPSVLL 1158
Cdd:PRK09700 96 TVLENLYIGRHLTKkvcgvniIDWREMRVRAA-------MMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVII 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15232977 1159 LDEATSALDSKServvQDALERVM-----VGRTSIMIAHRLSTIQN-CDMIVVLGKGKIVESG 1215
Cdd:PRK09700 169 MDEPTSSLTNKE----VDYLFLIMnqlrkEGTAIVYISHKLAEIRRiCDRYTVMKDGSSVCSG 227
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
1007-1171 |
9.46e-11 |
|
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: 62.51 E-value: 9.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1007 RPDVVIFENFSIEIDEGKSTAIVGTSGSGKSTIIGLIERFYDPLKGTVKIDGRDIRSYHLRSLRKYISLVSQEPMLFAGT 1086
Cdd:cd03231 10 RDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTLS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1087 IRENIMYggTSDKIDESEIIEAAKAANAhdfitslsNGY-DTNCGdkgvQLSGGQKQRIAIARAVLKNPSVLLLDEATSA 1165
Cdd:cd03231 90 VLENLRF--WHADHSDEQVEEALARVGL--------NGFeDRPVA----QLSAGQQRRVALARLLLSGRPLWILDEPTTA 155
|
....*.
gi 15232977 1166 LDSKSE 1171
Cdd:cd03231 156 LDKAGV 161
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
363-563 |
1.25e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 62.27 E-value: 1.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 363 HVKFTYLSRPettIFDDLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYDPIAGEILIDGVSIDKLQVNWlRSQMGLVSQ 442
Cdd:PRK13540 6 ELDFDYHDQP---LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTY-QKQLCFVGH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 443 E----PVLfatSITENILFGKEDAS----LDEVVEAAKASNahtfISQFPLGYktqvgergvqMSGGQKQRIAIARAIIK 514
Cdd:PRK13540 82 RsginPYL---TLRENCLYDIHFSPgavgITELCRLFSLEH----LIDYPCGL----------LSSGQKRQVALLRLWMS 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15232977 515 SPKILLLDEATSALDSES-ERVVQESLDNASIGRTTIVIAHRLSTIRNAD 563
Cdd:PRK13540 145 KAKLWLLDEPLVALDELSlLTIITKIQEHRAKGGAVLLTSHQDLPLNKAD 194
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
715-878 |
1.34e-10 |
|
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm288) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349991 [Multi-domain] Cd Length: 298 Bit Score: 63.96 E-value: 1.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 715 YVLLFVGLAIFSFLVNISQHYGFAYMGEYLTKRIREQMLSKILTFEVNWFDidDNSSGAICSRLAKDANVVRSMVGDRMS 794
Cdd:cd18547 47 ILLLLLGLYLLSALFSYLQNRLMARVSQRTVYDLRKDLFEKLQRLPLSYFD--THSHGDIMSRVTNDVDNISQALSQSLT 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 795 LLVQTISAVIIACIIGLVIAWRLAIVMISVQPLIVvcfytqrVLLKSLSEKASKA----QDESSKLAA---EAVSNIRTI 867
Cdd:cd18547 125 QLISSILTIVGTLIMMLYISPLLTLIVLVTVPLSL-------LVTKFIAKRSQKYfrkqQKALGELNGyieEMISGQKVV 197
|
170
....*....|.
gi 15232977 868 TAFSSQERIIK 878
Cdd:cd18547 198 KAFNREEEAIE 208
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
1001-1215 |
1.53e-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: 61.89 E-value: 1.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1001 DFAYPTRPDVVIFENFSIEIDEGKSTAIVGTSGSGKST----IIGLIERFYDPlKGTVKIDGRDIRSYHLRSLRKYIsLV 1076
Cdd:cd03233 11 FTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTllkaLANRTEGNVSV-EGDIHYNGIPYKEFAEKYPGEII-YV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1077 SQEPMLFAG-TIREnimyggtsdkideseIIEAAKAANAHDFItslsngydtncgdKGVqlSGGQKQRIAIARAVLKNPS 1155
Cdd:cd03233 89 SEEDVHFPTlTVRE---------------TLDFALRCKGNEFV-------------RGI--SGGERKRVSIAEALVSRAS 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15232977 1156 VLLLDEATSALDSKServvqdALERVMVGRTsimIAH--RLSTIQNC-----------DMIVVLGKGKIVESG 1215
Cdd:cd03233 139 VLCWDNSTRGLDSST------ALEILKCIRT---MADvlKTTTFVSLyqasdeiydlfDKVLVLYEGRQIYYG 202
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
716-927 |
1.97e-10 |
|
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349990 [Multi-domain] Cd Length: 292 Bit Score: 63.28 E-value: 1.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 716 VLLFVGLAIFSFLVNISQHYGFAYMGEYLTKRIREQMLSKILTFEVNWFDidDNSSGAICSRLAKDANVVRSMVGDRM-S 794
Cdd:cd18546 42 AAAYLAVVLAGWVAQRAQTRLTGRTGERLLYDLRLRVFAHLQRLSLDFHE--RETSGRIMTRMTSDIDALSELLQTGLvQ 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 795 LLVQTISAVIIACIIgLVIAWRLAIVMISVQPLIVVCFYTQRVLlkslSEKA-SKAQDESSKLAA---EAVSNIRTITAF 870
Cdd:cd18546 120 LVVSLLTLVGIAVVL-LVLDPRLALVALAALPPLALATRWFRRR----SSRAyRRARERIAAVNAdlqETLAGIRVVQAF 194
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15232977 871 SSQERIIKLLKKVQEGPRRESVHRSWLAGIVLGTSRSLITCTSALNFWYGGRLIADG 927
Cdd:cd18546 195 RRERRNAERFAELSDDYRDARLRAQRLVAIYFPGVELLGNLATAAVLLVGAWRVAAG 251
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
715-929 |
2.10e-10 |
|
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm287) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349992 [Multi-domain] Cd Length: 292 Bit Score: 63.19 E-value: 2.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 715 YVLLFVGLAIFSFLVNISQHYGFAYMGEYLTKRIREQMLSKILTFEVNwfDIDDNSSGAICSRLAKDANVVRSMVGDRMS 794
Cdd:cd18548 41 TGLLMLLLALLGLIAGILAGYFAAKASQGFGRDLRKDLFEKIQSFSFA--EIDKFGTSSLITRLTNDVTQVQNFVMMLLR 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 795 LLVQTISAVIIACIIGLVIAWRLAIVMISVQPLIVVCFYTqrVLLKS--LSEKASKAQDESSKLAAEAVSNIRTITAFSS 872
Cdd:cd18548 119 MLVRAPIMLIGAIIMAFRINPKLALILLVAIPILALVVFL--IMKKAipLFKKVQKKLDRLNRVVRENLTGIRVIRAFNR 196
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15232977 873 QERIIKLLKKVQEGPRRESVHrswlAGIVLGTSRSLIT----CTSALNFWYGGRLIADGKI 929
Cdd:cd18548 197 EDYEEERFDKANDDLTDTSLK----AGRLMALLNPLMMlimnLAIVAILWFGGHLINAGSL 253
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
706-929 |
2.30e-10 |
|
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette transporters; This group includes the 6-TMD of the peptidase-containing ATP-binding cassette transporters (PCATs) such as Clostridium thermocellum PCAT1, a polypeptide processing and secretion transporter, and LagD, a bacteriocin ABC transporter from Lactococcus lactis. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs. The transporters involved in protein secretion often contain additional peptidase domains essential for substrate processing. These peptidase domains belong to the cysteine protease superfamily, classified as family C39, bacteriocin-processing peptidase. LagD is highly similar to the peptidase-containing ATP-binding cassette transporters (PCATs). In Gram-positive bacteria, the PCATs are responsible for exporting quorum-sensing or antimicrobial peptides called bacteriocins.
Pssm-ID: 350014 [Multi-domain] Cd Length: 294 Bit Score: 63.23 E-value: 2.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 706 DQIKEKTRIYVLLFVGLAIFSFLVNISQHYGFAYMGEYLTKRIREQMLSKILTFEVNWFDidDNSSGAICSRLaKDANVV 785
Cdd:cd18570 35 SGDINLLNIISIGLILLYLFQSLLSYIRSYLLLKLSQKLDIRLILGYFKHLLKLPLSFFE--TRKTGEIISRF-NDANKI 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 786 RSMVGDRM-SLLVQTISAVIIACIIgLVIAWRLAIVMISVQPLIVVCFYtqrVLLKSLSEKASKAQDESSKLAA---EAV 861
Cdd:cd18570 112 REAISSTTiSLFLDLLMVIISGIIL-FFYNWKLFLITLLIIPLYILIIL---LFNKPFKKKNREVMESNAELNSyliESL 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15232977 862 SNIRTITAFSSQERIIKLLKKVQEGpRRESVHRSWLAGIVLGTSRSLI-TCTSALNFWYGGRLIADGKI 929
Cdd:cd18570 188 KGIETIKSLNAEEQFLKKIEKKFSK-LLKKSFKLGKLSNLQSSIKGLIsLIGSLLILWIGSYLVIKGQL 255
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
373-558 |
2.47e-10 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 64.90 E-value: 2.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 373 ETTIFDDLCLKIPAGKTVALVGGSGSGKSTVISLLQ-RFY-DPIAGEILIDGVSIDKLqvnwLRSQMGLVSQEPVLFA-T 449
Cdd:PLN03211 80 ERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAgRIQgNNFTGTILANNRKPTKQ----ILKRTGFVTQDDILYPhL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 450 SITENILFGKEDASLDEVVEAAKASNAHTFISQFPLGY--KTQVGE---RGVqmSGGQKQRIAIARAIIKSPKILLLDEA 524
Cdd:PLN03211 156 TVRETLVFCSLLRLPKSLTKQEKILVAESVISELGLTKceNTIIGNsfiRGI--SGGERKRVSIAHEMLINPSLLILDEP 233
|
170 180 190
....*....|....*....|....*....|....*
gi 15232977 525 TSALDSESE-RVVQESLDNASIGRTTIVIAHRLST 558
Cdd:PLN03211 234 TSGLDATAAyRLVLTLGSLAQKGKTIVTSMHQPSS 268
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
377-595 |
2.76e-10 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 62.25 E-value: 2.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 377 FDDLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYDPIAGEILI---DGVSIDKLQVN------WLRSQMGLVSQEP--- 444
Cdd:PRK11701 22 CRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYrmrDGQLRDLYALSeaerrrLLRTEWGFVHQHPrdg 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 445 ----VLFATSITENIL------FGK-EDASLD--EVVEAAKASnahtfISQFPLGYktqvgergvqmSGGQKQRIAIARA 511
Cdd:PRK11701 102 lrmqVSAGGNIGERLMavgarhYGDiRATAGDwlERVEIDAAR-----IDDLPTTF-----------SGGMQQRLQIARN 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 512 IIKSPKILLLDEATSALDSEservVQESLDN------ASIGRTTIVIAHRLSTIRN-ADVICVIHNGQIVETGSHEELLK 584
Cdd:PRK11701 166 LVTHPRLVFMDEPTGGLDVS----VQARLLDllrglvRELGLAVVIVTHDLAVARLlAHRLLVMKQGRVVESGLTDQVLD 241
|
250
....*....|....
gi 15232977 585 riDGQ--YTS-LVS 595
Cdd:PRK11701 242 --DPQhpYTQlLVS 253
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
1003-1176 |
2.77e-10 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 64.57 E-value: 2.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1003 AYPtrPDVVIFENFSIEIDEGKSTAIVGTSGSGKSTIiglierfydpLKGTVKIDgRDIRSYHLRSLRKYISLVSQEPML 1082
Cdd:TIGR03719 13 VVP--PKKEILKDISLSFFPGAKIGVLGLNGAGKSTL----------LRIMAGVD-KDFNGEARPQPGIKVGYLPQEPQL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1083 FAG-TIRENIMYG-----GTSDKIDE-------------------SEIIEAAKAANAHDFITSLSNGYDT-NC--GDKGV 1134
Cdd:TIGR03719 80 DPTkTVRENVEEGvaeikDALDRFNEisakyaepdadfdklaaeqAELQEIIDAADAWDLDSQLEIAMDAlRCppWDADV 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 15232977 1135 Q-LSGGQKQRIAIARAVLKNPSVLLLDEATSALDSKS----ERVVQD 1176
Cdd:TIGR03719 160 TkLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESvawlERHLQE 206
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
1001-1215 |
4.16e-10 |
|
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: 61.58 E-value: 4.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1001 DFAYPTRPDVVIFENFSIEIDEGKSTAIVGTSGSGKSTIIGLIERFYDPLKGTVKIDGRDIRSYHLRSLRKyISLV--SQ 1078
Cdd:cd03267 25 SLFKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLRR-IGVVfgQK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1079 EPMLFAGTIRENI-----MYGgtsdkideseiIEAAKAANAHDFITSLsngydTNCG---DKGV-QLSGGQKQRIAIARA 1149
Cdd:cd03267 104 TQLWWDLPVIDSFyllaaIYD-----------LPPARFKKRLDELSEL-----LDLEellDTPVrQLSLGQRMRAEIAAA 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15232977 1150 VLKNPSVLLLDEATSALDSKSERVVQDALERVMVGR--TSIMIAHRLSTIQN-CDMIVVLGKGKIVESG 1215
Cdd:cd03267 168 LLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERgtTVLLTSHYMKDIEAlARRVLVIDKGRLLYDG 236
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
338-560 |
5.46e-10 |
|
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: 63.61 E-value: 5.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 338 RVPDIDSNKKEGQILERMKG----EVEFNHVKFTY--LSRPETTIF-DDLCLKIPAGKTVALVGGSGSGKSTVISLLQRF 410
Cdd:TIGR00954 422 RVEEIESGREGGRNSNLVPGrgivEYQDNGIKFENipLVTPNGDVLiESLSFEVPSGNNLLICGPNGCGKSSLFRILGEL 501
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 411 YDPIAGEILIDgvSIDKLQVNWLRSQMGLVS-QEPVLFATSITENILFGKEDASLDEVVEAAKasnahtfisqfpLGY-- 487
Cdd:TIGR00954 502 WPVYGGRLTKP--AKGKLFYVPQRPYMTLGTlRDQIIYPDSSEDMKRRGLSDKDLEQILDNVQ------------LTHil 567
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15232977 488 KTQVGERGVQ-----MSGGQKQRIAIARAIIKSPKILLLDEATSALDSESERVVQESLDNASIgrTTIVIAHRLSTIR 560
Cdd:TIGR00954 568 EREGGWSAVQdwmdvLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLCREFGI--TLFSVSHRKSLWK 643
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
1007-1180 |
7.13e-10 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 60.20 E-value: 7.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1007 RPDVVIFENFSIEIDEGKSTAIVGTSGSGKSTIIGLIERFYDPLKGTVKIDGRDIR----SYHlrslrkyislvsQEpML 1082
Cdd:PRK13538 11 RDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRrqrdEYH------------QD-LL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1083 FAG---------TIRENI-MYGGTSDKIDESEIIEAAKAANAHDFitslsngYDTNCGdkgvQLSGGQKQRIAIARAVLK 1152
Cdd:PRK13538 78 YLGhqpgiktelTALENLrFYQRLHGPGDDEALWEALAQVGLAGF-------EDVPVR----QLSAGQQRRVALARLWLT 146
|
170 180
....*....|....*....|....*...
gi 15232977 1153 NPSVLLLDEATSALDSKSERVVQDALER 1180
Cdd:PRK13538 147 RAPLWILDEPFTAIDKQGVARLEALLAQ 174
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
1006-1214 |
7.74e-10 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 62.88 E-value: 7.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1006 TRPDVVIFENFSIEIDEGKSTAIVGTSGSGKSTIIGLIERFYdP---LKGTVKIDG-----RDIRSyhlrSLRKYISLVS 1077
Cdd:NF040905 10 TFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVY-PhgsYEGEILFDGevcrfKDIRD----SEALGIVIIH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1078 QE----PMLfagTIRENIMYG---GTSDKIDESEIIEAAKAANAHdfiTSLSNGYDTNCGDKGVqlsgGQKQRIAIARAV 1150
Cdd:NF040905 85 QElaliPYL---SIAENIFLGnerAKRGVIDWNETNRRARELLAK---VGLDESPDTLVTDIGV----GKQQLVEIAKAL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15232977 1151 LKNPSVLLLDEATSAL-DSKSERVVQDALERVMVGRTSIMIAHRLSTI-QNCDMIVVLGKGKIVES 1214
Cdd:NF040905 155 SKDVKLLILDEPTAALnEEDSAALLDLLLELKAQGITSIIISHKLNEIrRVADSITVLRDGRTIET 220
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
370-529 |
9.11e-10 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 59.82 E-value: 9.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 370 SRPETTIFDDLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYDPIAGEILIDGVSIDKL------QVNWLRSQMGLvsqE 443
Cdd:PRK13538 10 ERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQrdeyhqDLLYLGHQPGI---K 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 444 PVLFAtsiTENILFGKEDASL--DEVVEAAKAsnahtfisqfplgyktQVGERGV------QMSGGQKQRIAIARAIIKS 515
Cdd:PRK13538 87 TELTA---LENLRFYQRLHGPgdDEALWEALA----------------QVGLAGFedvpvrQLSAGQQRRVALARLWLTR 147
|
170
....*....|....
gi 15232977 516 PKILLLDEATSALD 529
Cdd:PRK13538 148 APLWILDEPFTAID 161
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
387-585 |
1.15e-09 |
|
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: 59.18 E-value: 1.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 387 GKTVALVGGSGSGKSTVISLL-QRFYD-PIAGEILIDGVSIDKlqvNWLRSqMGLVSQEPVLFATS-ITENILFgkeDAS 463
Cdd:cd03232 33 GTLTALMGESGAGKTTLLDVLaGRKTAgVITGEILINGRPLDK---NFQRS-TGYVEQQDVHSPNLtVREALRF---SAL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 464 LdevveaakasnahtfisqfplgyktqvgeRGvqMSGGQKQRIAIARAIIKSPKILLLDEATSALDSESERVVQESLDN- 542
Cdd:cd03232 106 L-----------------------------RG--LSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFLKKl 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 15232977 543 ASIGRTtiviahrlstirnadVICVIH--NGQIVETGSHEELLKR 585
Cdd:cd03232 155 ADSGQA---------------ILCTIHqpSASIFEKFDRLLLLKR 184
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1013-1215 |
1.46e-09 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 60.32 E-value: 1.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1013 FENFSIEIDEGKSTAIVGTSGSGKSTIIGLIERFYDPLKGTVKIDGRDIRSYHLRSL---------RKYISLVSQEPM-- 1081
Cdd:PRK11701 22 CRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYALseaerrrllRTEWGFVHQHPRdg 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1082 ----LFAG-TIRENIM------YGG----TSDKIDESEIieaakAANAHDfitslsngydtncgDKGVQLSGGQKQRIAI 1146
Cdd:PRK11701 102 lrmqVSAGgNIGERLMavgarhYGDiratAGDWLERVEI-----DAARID--------------DLPTTFSGGMQQRLQI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1147 ARAVLKNPSVLLLDEATSALD-SKSER--------VVQDALERVM------VGRtsiMIAHRLstiqncdmiVVLGKGKI 1211
Cdd:PRK11701 163 ARNLVTHPRLVFMDEPTGGLDvSVQARlldllrglVRELGLAVVIvthdlaVAR---LLAHRL---------LVMKQGRV 230
|
....
gi 15232977 1212 VESG 1215
Cdd:PRK11701 231 VESG 234
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
995-1209 |
1.49e-09 |
|
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: 58.79 E-value: 1.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 995 ITFLNVDFAYPT-RPDVVIFENFSIEIDEGKSTAIVGTSGSGKST---------IIGLIErfydplkGTVKIDGRDIRSy 1064
Cdd:cd03232 4 LTWKNLNYTVPVkGGKRQLLNNISGYVKPGTLTALMGESGAGKTTlldvlagrkTAGVIT-------GEILINGRPLDK- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1065 hlrSLRKYISLVSQEPMLFAG-TIRENIMYggtsdkideseiieaakAANAHDfitslsngydtncgdkgvqLSGGQKQR 1143
Cdd:cd03232 76 ---NFQRSTGYVEQQDVHSPNlTVREALRF-----------------SALLRG-------------------LSVEQRKR 116
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15232977 1144 IAIARAVLKNPSVLLLDEATSALDSKSERVVQDALERV-MVGRTSIMIAHRLS--TIQNCDMIVVLGKG 1209
Cdd:cd03232 117 LTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFLKKLaDSGQAILCTIHQPSasIFEKFDRLLLLKRG 185
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
1023-1198 |
1.62e-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: 57.77 E-value: 1.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1023 GKSTAIVGTSGSGKSTIIGLIERFYDPLKGTVK-IDGRDIRSYHLRSLRKYISlvsqepmlfagtirenimyggtsdkid 1101
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIyIDGEDILEEVLDQLLLIIV--------------------------- 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1102 eseiieaakaanahdfitslsngydtncGDKGVQLSGGQKQRIAIARAVLKNPSVLLLDEATSALDSKSERVVQDALE-- 1179
Cdd:smart00382 55 ----------------------------GGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEElr 106
|
170 180
....*....|....*....|....
gi 15232977 1180 -----RVMVGRTSIMIAHRLSTIQ 1198
Cdd:smart00382 107 lllllKSEKNLTVILTTNDEKDLG 130
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
994-1213 |
1.65e-09 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 61.91 E-value: 1.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 994 QITFLNVDFAYPTrpdvvifENFS-----IEIDEGKSTAIVGTSGSGKSTIIGLIERFYDPLKGTVKIDGRDIRSYHLRS 1068
Cdd:PRK10522 322 TLELRNVTFAYQD-------NGFSvgpinLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPED 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1069 LRKYISLVSQEPMLFAGTIRENimyGGTSDKIDESEIIEAAKAANAhdfiTSLSNGYDTNcgdkgVQLSGGQKQRIAIAR 1148
Cdd:PRK10522 395 YRKLFSAVFTDFHLFDQLLGPE---GKPANPALVEKWLERLKMAHK----LELEDGRISN-----LKLSKGQKKRLALLL 462
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15232977 1149 AVLKNPSVLLLDEATSALDSKSERVV-QDALERVM-VGRTSIMIAHRLSTIQNCDMIVVLGKGKIVE 1213
Cdd:PRK10522 463 ALAEERDILLLDEWAADQDPHFRREFyQVLLPLLQeMGKTIFAISHDDHYFIHADRLLEMRNGQLSE 529
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1008-1214 |
1.81e-09 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 61.56 E-value: 1.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1008 PDVVIFENFSIEIDEGKSTAIVGTSGSGKSTIIGLIERFYDPLKGTVKIDGRDIRSYHLR-SLRKYISLVSQEPMLFAG- 1085
Cdd:PRK10762 15 PGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKsSQEAGIGIIHQELNLIPQl 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1086 TIRENIMYG----GTSDKIDESEIIEAAKAANAHdfiTSLSNGYDTNCGDkgvqLSGGQKQRIAIARAVLKNPSVLLLDE 1161
Cdd:PRK10762 95 TIAENIFLGrefvNRFGRIDWKKMYAEADKLLAR---LNLRFSSDKLVGE----LSIGEQQMVEIAKVLSFESKVIIMDE 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15232977 1162 ATSAL-DSKSE---RVVQDALERvmvGRTSIMIAHRLSTI-QNCDMIVVLGKGK-IVES 1214
Cdd:PRK10762 168 PTDALtDTETEslfRVIRELKSQ---GRGIVYISHRLKEIfEICDDVTVFRDGQfIAER 223
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
361-574 |
2.04e-09 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 58.81 E-value: 2.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 361 FNHVKFTYLSRPETTIFDDLCLKIPAGKTVALVGGSGSGKST---VISLLQRFYDPIAGEILIDGVSIDKLQvNWLRSQM 437
Cdd:cd03233 7 RNISFTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTllkALANRTEGNVSVEGDIHYNGIPYKEFA-EKYPGEI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 438 GLVSQEPVLFATSITEnilfgkedasldEVVEAAKASNAHTFIsqfplgyktqvgeRGVqmSGGQKQRIAIARAIIKSPK 517
Cdd:cd03233 86 IYVSEEDVHFPTLTVR------------ETLDFALRCKGNEFV-------------RGI--SGGERKRVSIAEALVSRAS 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15232977 518 ILLLDEATSALDSEServvqeSLDNASIGR--------TTIVIAHRLS-TIRNA-DVICVIHNGQIV 574
Cdd:cd03233 139 VLCWDNSTRGLDSST------ALEILKCIRtmadvlktTTFVSLYQASdEIYDLfDKVLVLYEGRQI 199
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
1015-1216 |
2.56e-09 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 59.55 E-value: 2.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1015 NFSIEIDEGKSTAIVGTSGSGKSTIIG--LIERFYDPLKGTVKIDGRDIRSYHLRSLRKYIsLVSQEPMlfAGTIREN-I 1091
Cdd:cd03271 13 NIDVDIPLGVLTCVTGVSGSGKSSLINdtLYPALARRLHLKKEQPGNHDRIEGLEHIDKVI-VIDQSPI--GRTPRSNpA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1092 MYGGTSDKIDE------------SEIIE------------AAKAANAHDF---ITSLSNGYDTNC---------GDKGVQ 1135
Cdd:cd03271 90 TYTGVFDEIRElfcevckgkrynRETLEvrykgksiadvlDMTVEEALEFfenIPKIARKLQTLCdvglgyiklGQPATT 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1136 LSGGQKQRIAIARAVLK---NPSVLLLDEATSALDSKSERVVQDALER-VMVGRTSIMIAHRLSTIQNCDMIVVLGK--- 1208
Cdd:cd03271 170 LSGGEAQRIKLAKELSKrstGKTLYILDEPTTGLHFHDVKKLLEVLQRlVDKGNTVVVIEHNLDVIKCADWIIDLGPegg 249
|
250
....*....|.
gi 15232977 1209 ---GKIVESGT 1216
Cdd:cd03271 250 dggGQVVASGT 260
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1009-1223 |
3.18e-09 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 59.27 E-value: 3.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1009 DVVIFENFSIEIDEGKSTAIVGTSGSGKSTIIGLIERF--YDPLKGTVKIDGRDIRSY--HLRSlRKYISLVSQEPMLFA 1084
Cdd:CHL00131 19 ENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHpaYKILEGDILFKGESILDLepEERA-HLGIFLAFQYPIEIP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1085 GTIREN---IMYGGTSDKIDESEI--IEAAKAANAHDFITSLSNGYDTNCGDKGvqLSGGQKQRIAIARAVLKNPSVLLL 1159
Cdd:CHL00131 98 GVSNADflrLAYNSKRKFQGLPELdpLEFLEIINEKLKLVGMDPSFLSRNVNEG--FSGGEKKRNEILQMALLDSELAIL 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15232977 1160 DEATSALDSKSERVVQDALERVMVGRTSI-MIAH--RLSTIQNCDMIVVLGKGKIVESGTHS--SLLEK 1223
Cdd:CHL00131 176 DETDSGLDIDALKIIAEGINKLMTSENSIiLITHyqRLLDYIKPDYVHVMQNGKIIKTGDAElaKELEK 244
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
1015-1215 |
3.99e-09 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 60.67 E-value: 3.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1015 NFSIEIDEGKSTAIVGTSGSGKSTIIGLIERFYDPLKGTVKIDGrdirSYHLrslrkyISLVSQEPMLFAGTirENI--- 1091
Cdd:PRK13545 42 NISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKG----SAAL------IAISSGLNGQLTGI--ENIelk 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1092 --MYGGTSDKIDE--SEIIEAAKAANahdFITSLSNGYdtncgdkgvqlSGGQKQRIAIARAVLKNPSVLLLDEATSALD 1167
Cdd:PRK13545 110 glMMGLTKEKIKEiiPEIIEFADIGK---FIYQPVKTY-----------SSGMKSRLGFAISVHINPDILVIDEALSVGD 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15232977 1168 SK-SERVVQDALERVMVGRTSIMIAHRLSTIQN-CDMIVVLGKGKIVESG 1215
Cdd:PRK13545 176 QTfTKKCLDKMNEFKEQGKTIFFISHSLSQVKSfCTKALWLHYGQVKEYG 225
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
372-538 |
4.05e-09 |
|
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: 60.72 E-value: 4.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 372 PETTIFDDLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYDPIAGEILI-DGVSIdklqvnwlrsqmGLVSQEPVLFAT- 449
Cdd:TIGR03719 16 PKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPqPGIKV------------GYLPQEPQLDPTk 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 450 SITENI-------------------LFGKEDASLD-------EVVEAAKASNAHTFISQF---------PLGyKTQVGEr 494
Cdd:TIGR03719 84 TVRENVeegvaeikdaldrfneisaKYAEPDADFDklaaeqaELQEIIDAADAWDLDSQLeiamdalrcPPW-DADVTK- 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 15232977 495 gvqMSGGQKQRIAIARAIIKSPKILLLDEATSALDSES----ERVVQE 538
Cdd:TIGR03719 162 ---LSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESvawlERHLQE 206
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
1022-1194 |
5.16e-09 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 60.59 E-value: 5.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1022 EGKSTAIVGTSGSGKSTII---------------------GLIERFydplKGTVKIDG-RDIRSYHLRSLRK--YISLVs 1077
Cdd:PRK13409 98 EGKVTGILGPNGIGKTTAVkilsgelipnlgdyeeepswdEVLKRF----RGTELQNYfKKLYNGEIKVVHKpqYVDLI- 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1078 qePMLFAGTIRENIMyggtsdKIDESEIIEaakaanahDFITSLSNgydTNCGDKGV-QLSGGQKQRIAIARAVLKNPSV 1156
Cdd:PRK13409 173 --PKVFKGKVRELLK------KVDERGKLD--------EVVERLGL---ENILDRDIsELSGGELQRVAIAAALLRDADF 233
|
170 180 190
....*....|....*....|....*....|....*....
gi 15232977 1157 LLLDEATSALDSKsERV-VQDALERVMVGRTSIMIAHRL 1194
Cdd:PRK13409 234 YFFDEPTSYLDIR-QRLnVARLIRELAEGKYVLVVEHDL 271
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
1020-1215 |
5.42e-09 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 60.89 E-value: 5.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1020 IDEGKSTAIVGTSGSGKST----IIGLIERFYDPLKGTVKIDG---RDIRSyHLRSLRKYIS--------LVSQEPMLFA 1084
Cdd:TIGR00956 84 IKPGELTVVLGRPGSGCSTllktIASNTDGFHIGVEGVITYDGitpEEIKK-HYRGDVVYNAetdvhfphLTVGETLDFA 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1085 GTIRE-NIMYGGTSDKIDESEIIEAAKAanahdfITSLSNGYDTNCGDKGVQ-LSGGQKQRIAIARAVLKNPSVLLLDEA 1162
Cdd:TIGR00956 163 ARCKTpQNRPDGVSREEYAKHIADVYMA------TYGLSHTRNTKVGNDFVRgVSGGERKRVSIAEASLGGAKIQCWDNA 236
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15232977 1163 TSALDSKServvqdALERVMVGRTSIMIAHR--LSTIQNC--------DMIVVLGKGKIVESG 1215
Cdd:TIGR00956 237 TRGLDSAT------ALEFIRALKTSANILDTtpLVAIYQCsqdayelfDKVIVLYEGYQIYFG 293
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
68-291 |
6.22e-09 |
|
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349985 [Multi-domain] Cd Length: 293 Bit Score: 58.58 E-value: 6.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 68 SNNKTFMQTISKNVVALLYVACGSWVICFLEGYCWTRTGERQAARMREKYLRAVLRQDVGYFDLHvtSTSDVITSISSDS 147
Cdd:cd18541 30 TAGTLTASQLLRYALLILLLALLIGIFRFLWRYLIFGASRRIEYDLRNDLFAHLLTLSPSFYQKN--RTGDLMARATNDL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 148 LVIQDFLSeklPNFLMNASAFVAsYIVSFILM----WRLTIVGF-PFIILLLVpGLMYGRALVSISRKIHEQYNEAGSIA 222
Cdd:cd18541 108 NAVRMALG---PGILYLVDALFL-GVLVLVMMftisPKLTLIALlPLPLLALL-VYRLGKKIHKRFRKVQEAFSDLSDRV 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15232977 223 EQAISSVRTVYAFGSENKMIGKFSTALRGSVKLGLR----QGLAKGITIGSNGVTHAIwafLTWYGSRLVMNH 291
Cdd:cd18541 183 QESFSGIRVIKAFVQEEAEIERFDKLNEEYVEKNLRlarvDALFFPLIGLLIGLSFLI---VLWYGGRLVIRG 252
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
998-1221 |
6.35e-09 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 58.30 E-value: 6.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 998 LNVDFAYPTRPDVVIFENFSIEIDEGKSTAIVGTSGSGKSTIIG-LIERFYDP-------LKGTVKIDGRDIRSYHLRSL 1069
Cdd:PRK13547 2 LTADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKaLAGDLTGGgaprgarVTGDVTLNGEPLAAIDAPRL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1070 RKYISLVSQ--EPMlFAGTIRENIMYG-------GTSDKIDESEIIEAAKAAnahdfitslsNGYDTNCGDKGVQLSGGQ 1140
Cdd:PRK13547 82 ARLRAVLPQaaQPA-FAFSAREIVLLGrypharrAGALTHRDGEIAWQALAL----------AGATALVGRDVTTLSGGE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1141 KQRIAIARAVLK---------NPSVLLLDEATSALDSKSERVVQDALERVM----VGRTSIMIAHRLSTiQNCDMIVVLG 1207
Cdd:PRK13547 151 LARVQFARVLAQlwpphdaaqPPRYLLLDEPTAALDLAHQHRLLDTVRRLArdwnLGVLAIVHDPNLAA-RHADRIAMLA 229
|
250
....*....|....
gi 15232977 1208 KGKIVESGTHSSLL 1221
Cdd:PRK13547 230 DGAIVAHGAPADVL 243
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
714-878 |
6.92e-09 |
|
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group represents the six-transmembrane domain 2 (TMD2) of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The type 3 ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. All ABC transporters share a common architecture of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. By contrast, bacterial ABC exporters are typically assembled from dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are comprised of two identical TMDs and two identical NBDs.
Pssm-ID: 350024 [Multi-domain] Cd Length: 294 Bit Score: 58.67 E-value: 6.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 714 IYVLLFVGLAIFSFLVNISqhygFAYMGEYLTKRIREQMLSKILTFEVNWFDidDNSSGAICSRLAKDANVVRSMVGDRM 793
Cdd:cd18580 44 YAALLVLASVLLVLLRWLL----FVLAGLRASRRLHDKLLRSVLRAPMSFFD--TTPSGRILNRFSKDIGLIDEELPLAL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 794 SLLVQTISAVIIACIIGLVIAWRLAIVMIsvqPLIVVCFYTQRVLLKSLSEkaSKAQDESSK-----LAAEAVSNIRTIT 868
Cdd:cd18580 118 LDFLQSLFSVLGSLIVIAIVSPYFLIVLP---PLLVVYYLLQRYYLRTSRQ--LRRLESESRsplysHFSETLSGLSTIR 192
|
170
....*....|
gi 15232977 869 AFSSQERIIK 878
Cdd:cd18580 193 AFGWQERFIE 202
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1015-1216 |
7.19e-09 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 58.08 E-value: 7.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1015 NFSIEIDEGKSTAIVGTSGSGKSTIIGLIERFYDPLKGTVKIDGRDI--------------RSY-HLRSLRKYIS----L 1075
Cdd:PRK11300 23 NVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIeglpghqiarmgvvRTFqHVRLFREMTVienlL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1076 VSQ----EPMLFAGTIREnimyggTSDKIDESEIIEaaKAANAHDFI--TSLSNGYDTNcgdkgvqLSGGQKQRIAIARA 1149
Cdd:PRK11300 103 VAQhqqlKTGLFSGLLKT------PAFRRAESEALD--RAATWLERVglLEHANRQAGN-------LAYGQQRRLEIARC 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1150 VLKNPSVLLLDEATSALDSKSERVVQDALE--RVMVGRTSIMIAHRLSTIQN-CDMIVVLGKGKIVESGT 1216
Cdd:PRK11300 168 MVTQPEILMLDEPAAGLNPKETKELDELIAelRNEHNVTVLLIEHDMKLVMGiSDRIYVVNQGTPLANGT 237
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
387-573 |
7.78e-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: 55.84 E-value: 7.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 387 GKTVALVGGSGSGKSTVISLLQRFYDPIAGEILIDGVSIDKLQVNWLRSQMGlvsqepvlfatsitenilfgkedaslde 466
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLII---------------------------- 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 467 vveaakasnahtfisqfplgyktqVGERGVQMSGGQKQRIAIARAIIKSPKILLLDEATSALDSESERVVQESLDNASI- 545
Cdd:smart00382 54 ------------------------VGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLLl 109
|
170 180 190
....*....|....*....|....*....|....*...
gi 15232977 546 ------GRTTIVIAHRLSTIRNADVI----CVIHNGQI 573
Cdd:smart00382 110 llksekNLTVILTTNDEKDLGPALLRrrfdRRIVLLLI 147
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
373-605 |
9.39e-09 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 59.80 E-value: 9.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 373 ETTIFDDLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYDPIAGEI-LIDGVSIDKL---QVNWLRSQMGLVsQEPVLFA 448
Cdd:PRK10636 324 DRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIgLAKGIKLGYFaqhQLEFLRADESPL-QHLARLA 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 449 TSITENILfgkedasldevveaakasnaHTFISQFplGYK-TQVGERGVQMSGGQKQRIAIARAIIKSPKILLLDEATSA 527
Cdd:PRK10636 403 PQELEQKL--------------------RDYLGGF--GFQgDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNH 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 528 LDSESERVVQESL---DNAsigrtTIVIAHRLSTIRN-ADVICVIHNGQIvetgshEELLKRIDGQYTSLVSLQQMENEE 603
Cdd:PRK10636 461 LDLDMRQALTEALidfEGA-----LVVVSHDRHLLRStTDDLYLVHDGKV------EPFDGDLEDYQQWLSDVQKQENQT 529
|
..
gi 15232977 604 SN 605
Cdd:PRK10636 530 DE 531
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
369-582 |
1.35e-08 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 58.88 E-value: 1.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 369 LSRPETtiFDDLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYDPIAGEILIDGVSIDKLQVN-WLRSQMGLVS----QE 443
Cdd:COG1129 262 LSVGGV--VRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRdAIRAGIAYVPedrkGE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 444 PVLFATSITENILFgkedASLDEVV------EAAKASNAHTFISQfpLGYKTQVGERGVQ-MSGGQKQRIAIARAIIKSP 516
Cdd:COG1129 340 GLVLDLSIRENITL----ASLDRLSrgglldRRRERALAEEYIKR--LRIKTPSPEQPVGnLSGGNQQKVVLAKWLATDP 413
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15232977 517 KILLLDEATSALD----SESERVVQESLDNasiGRTTIVIahrlST-----IRNADVICVIHNGQIVETGSHEEL 582
Cdd:COG1129 414 KVLILDEPTRGIDvgakAEIYRLIRELAAE---GKAVIVI----SSelpelLGLSDRILVMREGRIVGELDREEA 481
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1014-1223 |
1.38e-08 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 58.17 E-value: 1.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1014 ENFSIEIDEGKSTAIVGTSGSGKSTII----GLIErfydPLKGTVKIDGRDI---RSYHLRSlrkyISLV----SQepmL 1082
Cdd:COG4586 39 DDISFTIEPGEIVGFIGPNGAGKSTTIkmltGILV----PTSGEVRVLGYVPfkrRKEFARR----IGVVfgqrSQ---L 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1083 ---------FAgTIREniMYGgtsdkIDESE----IIEAAKAANAHDFItslsngydtncgDKGV-QLSGGQKQRIAIAR 1148
Cdd:COG4586 108 wwdlpaidsFR-LLKA--IYR-----IPDAEykkrLDELVELLDLGELL------------DTPVrQLSLGQRMRCELAA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1149 AVLKNPSVLLLDEATSALDSKSERVVQDAL-----ERvmvGRTSIMIAHRLSTIQN-CDMIVVLGKGKIVESGTHSSLLE 1222
Cdd:COG4586 168 ALLHRPKILFLDEPTIGLDVVSKEAIREFLkeynrER---GTTILLTSHDMDDIEAlCDRVIVIDHGRIIYDGSLEELKE 244
|
.
gi 15232977 1223 K 1223
Cdd:COG4586 245 R 245
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
1003-1170 |
1.98e-08 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 58.59 E-value: 1.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1003 AYPtrPDVVIFENFSIEIDEGKSTAIVGTSGSGKSTIiglierfydpLK---GTVK-IDGRDIRSYHLRslrkyISLVSQ 1078
Cdd:PRK11819 15 VVP--PKKQILKDISLSFFPGAKIGVLGLNGAGKSTL----------LRimaGVDKeFEGEARPAPGIK-----VGYLPQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1079 EPMLFAG-TIRENIMYG--GTSDKIDESEII----------------EAAK------AANAHDFITSLSNGYDT-NC--G 1130
Cdd:PRK11819 78 EPQLDPEkTVRENVEEGvaEVKAALDRFNEIyaayaepdadfdalaaEQGElqeiidAADAWDLDSQLEIAMDAlRCppW 157
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 15232977 1131 DKGV-QLSGGQKQRIAIARAVLKNPSVLLLDEATSALDSKS 1170
Cdd:PRK11819 158 DAKVtKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAES 198
|
|
| ABC_6TM_SUR1_D2_like |
cd18602 |
Six-transmembrane helical domain 2 (TMD2) of the sulphonylurea receptors SUR1/2; This group ... |
704-882 |
2.08e-08 |
|
Six-transmembrane helical domain 2 (TMD2) of the sulphonylurea receptors SUR1/2; This group represents the six-transmembrane domain 2 (TMD2) of the sulphonylurea receptors SUR1/2 (ABCC8), which function as a modulator of ATP-sensitive potassium channels and insulin release, and belong to the ABCC subfamily. The ATP-sensitive (K-ATP) channel is an octameric complex of four pore-forming Kir6.2 subunits and four regulatory SUR subunits. Thus, in contrast to other ABC transporters, the SUR serves as the regulatory subunit of an ion channel. Mutations and deficiencies in the SUR proteins have been observed in patients with hyperinsulinemic hypoglycemia of infancy, an autosomal recessive disorder of unregulated and high insulin secretion. Mutations have also been associated with non-insulin-dependent diabetes mellitus type 2, an autosomal dominant disease of defective insulin secretion.
Pssm-ID: 350046 [Multi-domain] Cd Length: 307 Bit Score: 57.23 E-value: 2.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 704 SHDQIKEKTRIYVLLFVGLAIFSFLVNISQHYgfayMGEYLTKRIREQMLSKILTFEVNWFDIddNSSGAICSRLAKDAN 783
Cdd:cd18602 45 EDDEVSYYISVYAGLSLGAVILSLVTNLAGEL----AGLRAARRLHDRMLRNIVRAPMRFFDT--TPIGRILNRFSSDTN 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 784 VVRSMVGDRMSLLVQTISAVIIACIIGLVIAWRLAIVMIsvqPLIVVCFYTQRVLLKSLSEkaskAQ--DESSKL----- 856
Cdd:cd18602 119 VIDQKLPTTLERLLRFLLLCLSAIIVNAIVTPYFLIALI---PIIIVYYFLQKFYRASSRE----LQrlDNITKSpvfsh 191
|
170 180
....*....|....*....|....*.
gi 15232977 857 AAEAVSNIRTITAFSSQERIIKLLKK 882
Cdd:cd18602 192 FSETLGGLTTIRAFRQQARFTQQMLE 217
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
80-332 |
2.18e-08 |
|
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349989 [Multi-domain] Cd Length: 293 Bit Score: 57.09 E-value: 2.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 80 NVVALLYVAC--GSWVICFLEGYCWTRTGERQAARMREKYLRAVLRQDVGYFDlhVTSTSDVITSISSDSLVIQDFLSEK 157
Cdd:cd18545 40 LIIALLFLALnlVNWVASRLRIYLMAKVGQRILYDLRQDLFSHLQKLSFSFFD--SRPVGKILSRVINDVNSLSDLLSNG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 158 LPNFLMNASAFVASYIVSFILMWRLTIVGFPFIILLLVpglmygrALVSISRKIHEQYNEA--------GSIAEqAISSV 229
Cdd:cd18545 118 LINLIPDLLTLVGIVIIMFSLNVRLALVTLAVLPLLVL-------VVFLLRRRARKAWQRVrkkisnlnAYLHE-SISGI 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 230 RTVYAFGSENKMIGKFSTALRGSVKLGLRQGLAKGI------TIGSNGVthaiwAFLTWYGSRLVMNHGSkggTVFVVIS 303
Cdd:cd18545 190 RVIQSFAREDENEEIFDELNRENRKANMRAVRLNALfwplveLISALGT-----ALVYWYGGKLVLGGAI---TVGVLVA 261
|
250 260 270
....*....|....*....|....*....|....*..
gi 15232977 304 CITYggvsLG------QSLSNLkY--FSEAFVAWERI 332
Cdd:cd18545 262 FIGY----VGrfwqpiRNLSNF-YnqLQSAMASAERI 293
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
1015-1215 |
2.22e-08 |
|
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: 55.02 E-value: 2.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1015 NFSIEIDEGKSTAIVGTSGSGKSTIigLIERFYDPLKgtvkidgrdirsyhlRSLRKYISLVSQEPMLFAGTIRenimyg 1094
Cdd:cd03238 13 NLDVSIPLNVLVVVTGVSGSGKSTL--VNEGLYASGK---------------ARLISFLPKFSRNKLIFIDQLQ------ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1095 gtsdkideseiieaakaanahdFITSLSNGYDTnCGDKGVQLSGGQKQRIAIARAVLKNP--SVLLLDEATSALDSKSER 1172
Cdd:cd03238 70 ----------------------FLIDVGLGYLT-LGQKLSTLSGGELQRVKLASELFSEPpgTLFILDEPSTGLHQQDIN 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15232977 1173 VVQDALER-VMVGRTSIMIAHRLSTIQNCDMIVVLGK------GKIVESG 1215
Cdd:cd03238 127 QLLEVIKGlIDLGNTVILIEHNLDVLSSADWIIDFGPgsgksgGKVVFSG 176
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
1016-1185 |
2.87e-08 |
|
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: 56.26 E-value: 2.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1016 FSIEIDEGKST-----AIVGTSGSGKSTIIGLIERFYDPLKGTVKIDGRDIrSYHlrslRKYISLVSQepmlfaGTIRE- 1089
Cdd:cd03237 13 FTLEVEGGSISeseviGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTV-SYK----PQYIKADYE------GTVRDl 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1090 --NIMYGGTSDKIDESEIIEAAKaanahdfITSLsngYDTNCGDkgvqLSGGQKQRIAIARAVLKNPSVLLLDEATSALD 1167
Cdd:cd03237 82 lsSITKDFYTHPYFKTEIAKPLQ-------IEQI---LDREVPE----LSGGELQRVAIAACLSKDADIYLLDEPSAYLD 147
|
170
....*....|....*...
gi 15232977 1168 SKservvqdalERVMVGR 1185
Cdd:cd03237 148 VE---------QRLMASK 156
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
995-1194 |
3.04e-08 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 56.28 E-value: 3.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 995 ITFLNVDFAYPTRpdvVIFENFSIEIDEGKSTAIVGTSGSGKSTIIGLIERFYDPLKGTVKidgrdiRSYHLRslrkyIS 1074
Cdd:PRK09544 5 VSLENVSVSFGQR---RVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK------RNGKLR-----IG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1075 LVSQ----EPMLFAGTIRENIMYGGTSDkideSEIIEAAKAANAHDFItslsngydtncgDKGVQ-LSGGQKQRIAIARA 1149
Cdd:PRK09544 71 YVPQklylDTTLPLTVNRFLRLRPGTKK----EDILPALKRVQAGHLI------------DAPMQkLSGGETQRVLLARA 134
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 15232977 1150 VLKNPSVLLLDEATSALDSKSERVVQDALE--RVMVGRTSIMIAHRL 1194
Cdd:PRK09544 135 LLNRPQLLVLDEPTQGVDVNGQVALYDLIDqlRRELDCAVLMVSHDL 181
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
1022-1203 |
3.08e-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: 57.87 E-value: 3.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1022 EGKSTAIVGTSGSGKSTIIGL---------------------IERFydplKGTVKIDG-RDIRSYHLRSLRK--YISLVs 1077
Cdd:COG1245 98 KGKVTGILGPNGIGKSTALKIlsgelkpnlgdydeepswdevLKRF----RGTELQDYfKKLANGEIKVAHKpqYVDLI- 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1078 qePMLFAGTIRENIMyggtsdKIDE----SEIIEAakaanahdfiTSLSNGYDTNCGDkgvqLSGGQKQRIAIARAVLKN 1153
Cdd:COG1245 173 --PKVFKGTVRELLE------KVDErgklDELAEK----------LGLENILDRDISE----LSGGELQRVAIAAALLRD 230
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15232977 1154 PSVLLLDEATSALDSK----SERVVQDALERvmvGRTSIMIAHRLSTIqncDMI 1203
Cdd:COG1245 231 ADFYFFDEPSSYLDIYqrlnVARLIRELAEE---GKYVLVVEHDLAIL---DYL 278
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
33-245 |
3.77e-08 |
|
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm288) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349991 [Multi-domain] Cd Length: 298 Bit Score: 56.26 E-value: 3.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 33 ILMALGLIGAVGDGFITPVVVFIFNTLLNNLGTSSSNNktfMQTISKNVVALLYVACGSWVICFLEGYCWTRTGERQAAR 112
Cdd:cd18547 3 LVIILAIISTLLSVLGPYLLGKAIDLIIEGLGGGGGVD---FSGLLRILLLLLGLYLLSALFSYLQNRLMARVSQRTVYD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 113 MREKYLRAVLRQDVGYFDLHvtSTSDVITSISSDSLVIQDFLSEKLPNFLMNASAFVASYIVSFILMWRLTIVGFPFIIL 192
Cdd:cd18547 80 LRKDLFEKLQRLPLSYFDTH--SHGDIMSRVTNDVDNISQALSQSLTQLISSILTIVGTLIMMLYISPLLTLIVLVTVPL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15232977 193 LLVpglmYGRALVSISRKI-HEQYNEAGSI---AEQAISSVRTVYAFGSENKMIGKF 245
Cdd:cd18547 158 SLL----VTKFIAKRSQKYfRKQQKALGELngyIEEMISGQKVVKAFNREEEAIEEF 210
|
|
| ABC_6TM_HetC_like |
cd18568 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ... |
32-291 |
4.14e-08 |
|
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS (type 1 secretion systems), such as heterocyst differentiation protein HetC. HetC is similar to ABC protein exporters of T1SS (type 1 secretion systems) and is involved in early regulation of heterocyst differentiation in the filamentous cynobacterium Anabaena sp. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. ABC-transporter proteins in this group carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion.
Pssm-ID: 350012 [Multi-domain] Cd Length: 294 Bit Score: 56.41 E-value: 4.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 32 WILMALGLIGAVGdgFITPVVV-FIFNTLLNNlgtsssNNKTFMQTIsknVVALLYVACGSWVICFLEGYCWTRTGERQA 110
Cdd:cd18568 6 EILLASLLLQLLG--LALPLFTqIILDRVLVH------KNISLLNLI---LIGLLIVGIFQILLSAVRQYLLDYFANRID 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 111 ARMREKYLRAVLRQDVGYFDLHvtSTSDVITSISsDSLVIQDFLSEKLPNFLMNasafVASYIVSFILM----WRLTIVG 186
Cdd:cd18568 75 LSLLSDFYKHLLSLPLSFFASR--KVGDIITRFQ-ENQKIRRFLTRSALTTILD----LLMVFIYLGLMfyynLQLTLIV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 187 FPFIILLLVPGLMYGRALVSISRKIHEQYNEAGSIAEQAISSVRTVYAFGSENKMIGKFSTALRGSVKLGLR-QGLAKGI 265
Cdd:cd18568 148 LAFIPLYVLLTLLSSPKLKRNSREIFQANAEQQSFLVEALTGIATIKALAAERPIRWRWENKFAKALNTRFRgQKLSIVL 227
|
250 260
....*....|....*....|....*.
gi 15232977 266 TIGSNGVTHAIWAFLTWYGSRLVMNH 291
Cdd:cd18568 228 QLISSLINHLGTIAVLWYGAYLVISG 253
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
378-582 |
4.95e-08 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 56.96 E-value: 4.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 378 DDLCLKIPAGKTVALVGGSGSGKSTVISLL--QRfyDPIAGEILIDGVSIDKLQVNWLRsQMGL--VSQEPVLFAT---- 449
Cdd:COG3845 275 KDVSLEVRAGEILGIAGVAGNGQSELAEALagLR--PPASGSIRLDGEDITGLSPRERR-RLGVayIPEDRLGRGLvpdm 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 450 SITENILFGKEDAS-------LDEvvEAAKAsNAHTFISQF---PLGYKTQVGergvQMSGGQKQRIAIARAIIKSPKIL 519
Cdd:COG3845 352 SVAENLILGRYRRPpfsrggfLDR--KAIRA-FAEELIEEFdvrTPGPDTPAR----SLSGGNQQKVILARELSRDPKLL 424
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15232977 520 LLDEATSALDSES-ERVVQESLDNASIGRTTIVIAHRLSTIRN-ADVICVIHNGQIVETGSHEEL 582
Cdd:COG3845 425 IAAQPTRGLDVGAiEFIHQRLLELRDAGAAVLLISEDLDEILAlSDRIAVMYEGRIVGEVPAAEA 489
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
96-238 |
7.16e-08 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350009 [Multi-domain] Cd Length: 313 Bit Score: 55.65 E-value: 7.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 96 FLEGYCWTRTGERQAARMREKYLRAVLRQDVGYFDLHvtSTSDVITSISSDSLVIQDFLSEKLPNFLMNASAFVASYIVS 175
Cdd:cd18565 72 YLSGVLWRRFAQRVQHDLRTDTYDHVQRLDMAFFEDR--QTGDLMSVLNNDVNQLERFLDDGANSIIRVVVTVLGIGAIL 149
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15232977 176 FILMWRLTIVGFPFIILLLVPGLMYGRALVSISRKIHEQYNEAGSIAEQAISSVRTVYAFGSE 238
Cdd:cd18565 150 FYLNWQLALVALLPVPLIIAGTYWFQRRIEPRYRAVREAVGDLNARLENNLSGIAVIKAFTAE 212
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
369-608 |
7.82e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 56.56 E-value: 7.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 369 LSRPETTIFDDLCLKipAGKTVALVGGSGSGKSTVISLLQRFYDPIAGEIL-----IDGVSIDKLQ----VNWLRSQMGL 439
Cdd:PRK10938 13 LSDTKTLQLPSLTLN--AGDSWAFVGANGSGKSALARALAGELPLLSGERQsqfshITRLSFEQLQklvsDEWQRNNTDM 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 440 VSQEPVLFATSITENILFGKEDASLDEVVEAakasnahtfisQFplGYKTQVGERGVQMSGGQKQRIAIARAIIKSPKIL 519
Cdd:PRK10938 91 LSPGEDDTGRTTAEIIQDEVKDPARCEQLAQ-----------QF--GITALLDRRFKYLSTGETRKTLLCQALMSEPDLL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 520 LLDEATSALDSESERVVQESLDN-ASIGRTTIVIAHRLSTIRN-ADVICVIHNGQIVETGSHEELLKRidgqytSLVslQ 597
Cdd:PRK10938 158 ILDEPFDGLDVASRQQLAELLASlHQSGITLVLVLNRFDEIPDfVQFAGVLADCTLAETGEREEILQQ------ALV--A 229
|
250
....*....|.
gi 15232977 598 QMENEESNVNI 608
Cdd:PRK10938 230 QLAHSEQLEGV 240
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
379-578 |
8.27e-08 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 54.93 E-value: 8.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 379 DLCLKIPAGKTVALVGGSGSGKSTVI------SLLQRFYdpIAGEILIDGVSIDKLQ-VNWLRsqmgLVSQEPV------ 445
Cdd:cd03271 13 NIDVDIPLGVLTCVTGVSGSGKSSLIndtlypALARRLH--LKKEQPGNHDRIEGLEhIDKVI----VIDQSPIgrtprs 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 446 -------LFaTSITEniLF-----GK-----------EDASLDEVVEAAkASNAHTFISQFP-------------LGYkT 489
Cdd:cd03271 87 npatytgVF-DEIRE--LFcevckGKrynretlevryKGKSIADVLDMT-VEEALEFFENIPkiarklqtlcdvgLGY-I 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 490 QVGERGVQMSGGQKQRIAIARAIIK---SPKILLLDEATSALDSESER----VVQESLDNasiGRTTIVIAHRLSTIRNA 562
Cdd:cd03271 162 KLGQPATTLSGGEAQRIKLAKELSKrstGKTLYILDEPTTGLHFHDVKklleVLQRLVDK---GNTVVVIEHNLDVIKCA 238
|
250 260
....*....|....*....|..
gi 15232977 563 DVICVI------HNGQIVETGS 578
Cdd:cd03271 239 DWIIDLgpeggdGGGQVVASGT 260
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
372-532 |
1.37e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 55.90 E-value: 1.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 372 PETTIFDDLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYDPIAGE-ILIDGVSIdklqvnwlrsqmGLVSQEPVLFAT- 449
Cdd:PRK11819 18 PKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEaRPAPGIKV------------GYLPQEPQLDPEk 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 450 SITENI-------------------LFGKEDASLDEVV-EAAK------ASNAHTFISQF---------PLGyKTQVGer 494
Cdd:PRK11819 86 TVRENVeegvaevkaaldrfneiyaAYAEPDADFDALAaEQGElqeiidAADAWDLDSQLeiamdalrcPPW-DAKVT-- 162
|
170 180 190
....*....|....*....|....*....|....*...
gi 15232977 495 gvQMSGGQKQRIAIARAIIKSPKILLLDEATSALDSES 532
Cdd:PRK11819 163 --KLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAES 198
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
368-561 |
1.38e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 55.73 E-value: 1.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 368 YLSRPETTIFDDLCLKIPAGKTVALVGGSGSGKSTVISLLqrfydpiAGEILID--------GVSIDKLQVNWLRSQMGL 439
Cdd:PRK11147 10 WLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKIL-------NGEVLLDdgriiyeqDLIVARLQQDPPRNVEGT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 440 V------------------SQEPVLFATSITENILfgKEDASLDEVVEAAKA----SNAHTFISQFPLGYKTQVGErgvq 497
Cdd:PRK11147 83 VydfvaegieeqaeylkryHDISHLVETDPSEKNL--NELAKLQEQLDHHNLwqleNRINEVLAQLGLDPDAALSS---- 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15232977 498 MSGGQKQRIAIARAIIKSPKILLLDEATSALDSESERVVQESLDN--ASIgrttIVIAHRLSTIRN 561
Cdd:PRK11147 157 LSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTfqGSI----IFISHDRSFIRN 218
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
716-927 |
1.83e-07 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350009 [Multi-domain] Cd Length: 313 Bit Score: 54.49 E-value: 1.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 716 VLLFVGLAIFSFLvnisQHYGFAYMGEYLTKRIREQMLSKILTFEVNWFDidDNSSGAICSRLAKDANVVRSMVGDRMSL 795
Cdd:cd18565 61 VAAFLLESLFQYL----SGVLWRRFAQRVQHDLRTDTYDHVQRLDMAFFE--DRQTGDLMSVLNNDVNQLERFLDDGANS 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 796 LVQTISAVIIACIIGLVIAWRLAIVMISVQPLIVVC-FYTQRVLLKSLSEKASKAQDESSKLaAEAVSNIRTITAFSSQE 874
Cdd:cd18565 135 IIRVVVTVLGIGAILFYLNWQLALVALLPVPLIIAGtYWFQRRIEPRYRAVREAVGDLNARL-ENNLSGIAVIKAFTAED 213
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15232977 875 RIIKLLKKVQEGPRRESVHRSWLAGIVLGTSRSLITCTSALNFWYGGRLIADG 927
Cdd:cd18565 214 FERERVADASEEYRDANWRAIRLRAAFFPVIRLVAGAGFVATFVVGGYWVLDG 266
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
382-569 |
2.20e-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: 53.52 E-value: 2.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 382 LKIPA-GKTVALVGGSGSGKSTVISLLQ--------RFYDPIAGEILIDGVSIDKLQVNWLRSQMG---------LVSQE 443
Cdd:cd03236 20 LPVPReGQVLGLVGPNGIGKSTALKILAgklkpnlgKFDDPPDWDEILDEFRGSELQNYFTKLLEGdvkvivkpqYVDLI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 444 PVLFATSITENILFGKEDASLDEVVEaakasnahtfisQFPLgykTQVGERGV-QMSGGQKQRIAIARAIIKSPKILLLD 522
Cdd:cd03236 100 PKAVKGKVGELLKKKDERGKLDELVD------------QLEL---RHVLDRNIdQLSGGELQRVAIAAALARDADFYFFD 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15232977 523 EATSALDSESE----RVVQESLDNasiGRTTIVIAHRLSTIRN-ADVICVIH 569
Cdd:cd03236 165 EPSSYLDIKQRlnaaRLIRELAED---DNYVLVVEHDLAVLDYlSDYIHCLY 213
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
1008-1212 |
2.55e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 54.74 E-value: 2.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1008 PDVVIFENFSIEIDEGKSTAIVGTSGSGKSTIIGLIERFYDPLKGTVKIDGRDIR-SYHLRSLRKYISLVSQE-PMLFAG 1085
Cdd:PRK10982 9 PGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfKSSKEALENGISMVHQElNLVLQR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1086 TIRENIMYGGTSDK---IDESEIIEAAKAANAHDFItslsngyDTNCGDKGVQLSGGQKQRIAIARAVLKNPSVLLLDEA 1162
Cdd:PRK10982 89 SVMDNMWLGRYPTKgmfVDQDKMYRDTKAIFDELDI-------DIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEP 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15232977 1163 TSALDSKSE----RVVQDALERvmvGRTSIMIAHRLSTI-QNCDMIVVLGKGKIV 1212
Cdd:PRK10982 162 TSSLTEKEVnhlfTIIRKLKER---GCGIVYISHKMEEIfQLCDEITILRDGQWI 213
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
370-582 |
2.64e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 54.74 E-value: 2.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 370 SRPETTIFDDLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYDPIAGEILIDGVSID-KLQVNWLRSQMGLVSQE-PVLF 447
Cdd:PRK10982 7 SFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfKSSKEALENGISMVHQElNLVL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 448 ATSITENILFGKEDASlDEVVEAAKASNAHTFISQfPLGYKTQVGERGVQMSGGQKQRIAIARAIIKSPKILLLDEATSA 527
Cdd:PRK10982 87 QRSVMDNMWLGRYPTK-GMFVDQDKMYRDTKAIFD-ELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSS 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15232977 528 LdseSERVVQ------ESLDNASIGrtTIVIAHRLSTIRN-ADVICVIHNGQIVETGSHEEL 582
Cdd:PRK10982 165 L---TEKEVNhlftiiRKLKERGCG--IVYISHKMEEIFQlCDEITILRDGQWIATQPLAGL 221
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
382-529 |
2.84e-07 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 54.08 E-value: 2.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 382 LKIPAGKTVALVGGSGSGKSTvislLQRFydpIAG-------EILIDGVSIDKLqvnwlrsqmglvsqEP------VLFA 448
Cdd:PRK11650 25 LDVADGEFIVLVGPSGCGKST----LLRM---VAGleritsgEIWIGGRVVNEL--------------EPadrdiaMVFQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 449 T-------SITENILFGKEDASLDE------VVEAAKASNAHTFISQFPlgyktqvgeRgvQMSGGQKQRIAIARAIIKS 515
Cdd:PRK11650 84 NyalyphmSVRENMAYGLKIRGMPKaeieerVAEAARILELEPLLDRKP---------R--ELSGGQRQRVAMGRAIVRE 152
|
170
....*....|....
gi 15232977 516 PKILLLDEATSALD 529
Cdd:PRK11650 153 PAVFLFDEPLSNLD 166
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
355-529 |
3.79e-07 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 52.81 E-value: 3.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 355 MKGEVEFNHVKFTYLSRpetTIFDDLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYDPIAGEILIDgvsiDKLQVNWLR 434
Cdd:PRK09544 1 MTSLVSLENVSVSFGQR---RVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRN----GKLRIGYVP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 435 SQMGLvsqEPVLFATsiTENILFGKEDASLDEVVEAAKASNAHTFIsQFPLGyktqvgergvQMSGGQKQRIAIARAIIK 514
Cdd:PRK09544 74 QKLYL---DTTLPLT--VNRFLRLRPGTKKEDILPALKRVQAGHLI-DAPMQ----------KLSGGETQRVLLARALLN 137
|
170
....*....|....*
gi 15232977 515 SPKILLLDEATSALD 529
Cdd:PRK09544 138 RPQLLVLDEPTQGVD 152
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
81-332 |
3.93e-07 |
|
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349990 [Multi-domain] Cd Length: 292 Bit Score: 53.26 E-value: 3.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 81 VVALLYVACG--SWVICFLEGYCWTRTGERQAARMREKYLRAVLRQDVGYFDlhvTSTSD-VITSISSDSLVIQDFLSEK 157
Cdd:cd18546 40 LAAAAYLAVVlaGWVAQRAQTRLTGRTGERLLYDLRLRVFAHLQRLSLDFHE---RETSGrIMTRMTSDIDALSELLQTG 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 158 LPNFLMNASAFVASYIVSFILMWRLTIVGFPFIILLLVPGLMYGRALVSISRKIHEQYneAGSIAE--QAISSVRTVYAF 235
Cdd:cd18546 117 LVQLVVSLLTLVGIAVVLLVLDPRLALVALAALPPLALATRWFRRRSSRAYRRARERI--AAVNADlqETLAGIRVVQAF 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 236 GSENKMIGKFSTALRGSVKLGLRQGLAKGITI-GSNGVTHAIWAFLTWYGSRLVMNHGSkggTVFVVISCITYGGVSLG- 313
Cdd:cd18546 195 RRERRNAERFAELSDDYRDARLRAQRLVAIYFpGVELLGNLATAAVLLVGAWRVAAGTL---TVGVLVAFLLYLRRFFAp 271
|
250 260
....*....|....*....|..
gi 15232977 314 -QSLSNLkY--FSEAFVAWERI 332
Cdd:cd18546 272 iQQLSQV-FdsYQQARAALEKI 292
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1006-1213 |
4.39e-07 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 54.02 E-value: 4.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1006 TRPDVVIFENFSIEIDEGKSTAIVGTSGSGKSTIIGLIerF-YDPLK-GTVKIDGRDIR-SYHLRSLRKYISLVSQ---E 1079
Cdd:PRK09700 272 TSRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCL--FgVDKRAgGEIRLNGKDISpRSPLDAVKKGMAYITEsrrD 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1080 PMLFAG-TIRENIM---------YGGTSDKIDESEiiEAAKAANAHDFITSLSNGYDTNCGdkgvQLSGGQKQRIAIARA 1149
Cdd:PRK09700 350 NGFFPNfSIAQNMAisrslkdggYKGAMGLFHEVD--EQRTAENQRELLALKCHSVNQNIT----ELSGGNQQKVLISKW 423
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15232977 1150 VLKNPSVLLLDEATSALD--SKSE--RVVQDALERvmvGRTSIMIAHRLSTIQN-CDMIVVLGKGKIVE 1213
Cdd:PRK09700 424 LCCCPEVIIFDEPTRGIDvgAKAEiyKVMRQLADD---GKVILMVSSELPEIITvCDRIAVFCEGRLTQ 489
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
387-554 |
5.06e-07 |
|
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: 52.41 E-value: 5.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 387 GKTVALVGGSGSGKSTVISLLQRFYDPIAGEILIDGVSID-KLQVNWLRSQMGLvsqepvlfatsitENILFGKEDASLD 465
Cdd:cd03237 25 SEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSyKPQYIKADYEGTV-------------RDLLSSITKDFYT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 466 EV---VEAAKasnahtfisqfPLGYKtQVGERGV-QMSGGQKQRIAIARAIIKSPKILLLDEATSALDSESE----RVVQ 537
Cdd:cd03237 92 HPyfkTEIAK-----------PLQIE-QILDREVpELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRlmasKVIR 159
|
170
....*....|....*..
gi 15232977 538 ESLDNASigRTTIVIAH 554
Cdd:cd03237 160 RFAENNE--KTAFVVEH 174
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1015-1212 |
5.70e-07 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 53.49 E-value: 5.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1015 NFSIEIDEGKSTAIVGTSGSGKS----TIIGLIErfydPLKGTVKIDGRDIRSYHLRSLRKY-ISLVSQEPM---LFAG- 1085
Cdd:COG3845 276 DVSLEVRAGEILGIAGVAGNGQSelaeALAGLRP----PASGSIRLDGEDITGLSPRERRRLgVAYIPEDRLgrgLVPDm 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1086 TIRENIMYGGTSDK-------IDESEIIEAAKAanahdfitsLSNGYDTNCGDKGV---QLSGGQKQRIAIARAVLKNPS 1155
Cdd:COG3845 352 SVAENLILGRYRRPpfsrggfLDRKAIRAFAEE---------LIEEFDVRTPGPDTparSLSGGNQQKVILARELSRDPK 422
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15232977 1156 VLLLDEATSALDSKSERVVQDAL-ERVMVGRTSIMIAHRLSTIQN-CDMIVVLGKGKIV 1212
Cdd:COG3845 423 LLIAAQPTRGLDVGAIEFIHQRLlELRDAGAAVLLISEDLDEILAlSDRIAVMYEGRIV 481
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
485-582 |
7.39e-07 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 53.86 E-value: 7.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 485 LGYkTQVGERGVQMSGGQKQRIAIARAIIK---SPKILLLDEATSALDSESER----VVQESLDNasiGRTTIVIAHRLS 557
Cdd:TIGR00630 818 LGY-IRLGQPATTLSGGEAQRIKLAKELSKrstGRTLYILDEPTTGLHFDDIKklleVLQRLVDK---GNTVVVIEHNLD 893
|
90 100 110
....*....|....*....|....*....|...
gi 15232977 558 TIRNADviCVI--------HNGQIVETGSHEEL 582
Cdd:TIGR00630 894 VIKTAD--YIIdlgpeggdGGGTVVASGTPEEV 924
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
1012-1224 |
7.53e-07 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 51.72 E-value: 7.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1012 IFENFSIEIDEGKSTAIVGTSGSGKSTIIGLI--ERFYDPLKGTVKIDGRDIRSYHLRSLR-KYISLVSQEPMLFAGTir 1088
Cdd:PRK09580 16 ILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLagREDYEVTGGTVEFKGKDLLELSPEDRAgEGIFMAFQYPVEIPGV-- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1089 ENIMYGGTS-------------DKIDESEIIEaakaanahDFITSLSNGYDTNCGDKGVQLSGGQKQRIAIARAVLKNPS 1155
Cdd:PRK09580 94 SNQFFLQTAlnavrsyrgqeplDRFDFQDLME--------EKIALLKMPEDLLTRSVNVGFSGGEKKRNDILQMAVLEPE 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15232977 1156 VLLLDEATSALDSKSERVVQDALERVMVG-RTSIMIAH--RLSTIQNCDMIVVLGKGKIVESGTHS---SLLEKG 1224
Cdd:PRK09580 166 LCILDESDSGLDIDALKIVADGVNSLRDGkRSFIIVTHyqRILDYIKPDYVHVLYQGRIVKSGDFTlvkQLEEQG 240
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
369-565 |
7.65e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 51.03 E-value: 7.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 369 LSRPETTIFDdLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYDPIAGEILIDGVSIDKLQ---VNWLRSQMGLVSQEPV 445
Cdd:PRK13541 9 FNIEQKNLFD-LSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAkpyCTYIGHNLGLKLEMTV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 446 LfatsitENILFGKEDASLDEVVEAAkasnahtfISQFPLGYktQVGERGVQMSGGQKQRIAIARAIIKSPKILLLDEAT 525
Cdd:PRK13541 88 F------ENLKFWSEIYNSAETLYAA--------IHYFKLHD--LLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVE 151
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 15232977 526 SALDSESERVVQESLD-NASIGRTTIVIAHRLSTIRNADVI 565
Cdd:PRK13541 152 TNLSKENRDLLNNLIVmKANSGGIVLLSSHLESSIKSAQIL 192
|
|
| ABC_6TM_YwjA_like |
cd18549 |
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ... |
111-245 |
7.87e-07 |
|
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar proteins; This group represents the six-transmembrane helical domain of an uncharacterized ABC transporter YwjA from Bacillus subtilis and similar proteins. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349993 [Multi-domain] Cd Length: 295 Bit Score: 52.45 E-value: 7.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 111 ARMREKYLRAVLRQDVGYFDLHvtSTSDVITSISSDSLVIQDFLSEKLPNFLMNASAFVASYIVSFILMWRLTIVGFPFI 190
Cdd:cd18549 75 TDMRRDLFEHLQKLSFSFFDNN--KTGQLMSRITNDLFDISELAHHGPEDLFISIITIIGSFIILLTINVPLTLIVFALL 152
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 15232977 191 ILLLVPGLMYGRALVSISRKIHEQYNEAGSIAEQAISSVRTVYAFGSENKMIGKF 245
Cdd:cd18549 153 PLMIIFTIYFNKKMKKAFRRVREKIGEINAQLEDSLSGIRVVKAFANEEYEIEKF 207
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
1013-1203 |
8.81e-07 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 53.25 E-value: 8.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1013 FENFSIEIDEGK-----STAIVGTSGSGKSTII----GLIERFYDPLKGTVKIdgrdirSYhlrslrK--YISlVSQEpm 1081
Cdd:COG1245 351 YGGFSLEVEGGEiregeVLGIVGPNGIGKTTFAkilaGVLKPDEGEVDEDLKI------SY------KpqYIS-PDYD-- 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1082 lfaGTIREnIMYGGTSDKIDES----EIIEAakaanahdfiTSLSNGYDTNCGDkgvqLSGGQKQRIAIARAVLKNPSVL 1157
Cdd:COG1245 416 ---GTVEE-FLRSANTDDFGSSyyktEIIKP----------LGLEKLLDKNVKD----LSGGELQRVAIAACLSRDADLY 477
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 15232977 1158 LLDEATSALDSkSERV-VQDALERVMVGR--TSIMIAHRLSTIqncDMI 1203
Cdd:COG1245 478 LLDEPSAHLDV-EQRLaVAKAIRRFAENRgkTAMVVDHDIYLI---DYI 522
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
378-556 |
1.03e-06 |
|
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: 53.48 E-value: 1.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 378 DDLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYDPIAGEILIDGVSIdKLQVNWLRSQMGLVSQEPVLfatsitENILF 457
Cdd:TIGR01257 1956 DRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSI-LTNISDVHQNMGYCPQFDAI------DDLLT 2028
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 458 GKEDASLDEVVEAAKASNAHTFI--SQFPLGYKTQVGERGVQMSGGQKQRIAIARAIIKSPKILLLDEATSALDSESERV 535
Cdd:TIGR01257 2029 GREHLYLYARLRGVPAEEIEKVAnwSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRM 2108
|
170 180
....*....|....*....|....
gi 15232977 536 VQESLdnASI---GRTTIVIAHRL 556
Cdd:TIGR01257 2109 LWNTI--VSIireGRAVVLTSHSM 2130
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
1022-1195 |
1.10e-06 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 51.60 E-value: 1.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1022 EGKSTAIVGTSGSGKSTIIGLIE--------RFYDPLKGTVKID---GRDIRSYHLRSLRKYISL------VSQEPMLFA 1084
Cdd:cd03236 25 EGQVLGLVGPNGIGKSTALKILAgklkpnlgKFDDPPDWDEILDefrGSELQNYFTKLLEGDVKVivkpqyVDLIPKAVK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1085 GTIRENImyggtsDKIDES----EIIEAakaanahdfiTSLSNGYDTNCGdkgvQLSGGQKQRIAIARAVLKNPSVLLLD 1160
Cdd:cd03236 105 GKVGELL------KKKDERgkldELVDQ----------LELRHVLDRNID----QLSGGELQRVAIAAALARDADFYFFD 164
|
170 180 190
....*....|....*....|....*....|....*....
gi 15232977 1161 EATSALDSKSE----RVVQdalERVMVGRTSIMIAHRLS 1195
Cdd:cd03236 165 EPSSYLDIKQRlnaaRLIR---ELAEDDNYVLVVEHDLA 200
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
384-578 |
1.40e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 52.80 E-value: 1.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 384 IPAGKTVALVGGSGSGKST----VISLLQRFYDPIAGEILIDGVSIDKLqVNWLRSQMGLVSQEPVLFAT-SITENILF- 457
Cdd:TIGR00956 84 IKPGELTVVLGRPGSGCSTllktIASNTDGFHIGVEGVITYDGITPEEI-KKHYRGDVVYNAETDVHFPHlTVGETLDFa 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 458 ------GKEDASLDEVVEAAKAsnAHTFISQFPLG--YKTQVGE---RGVqmSGGQKQRIAIARAIIKSPKILLLDEATS 526
Cdd:TIGR00956 163 arcktpQNRPDGVSREEYAKHI--ADVYMATYGLShtRNTKVGNdfvRGV--SGGERKRVSIAEASLGGAKIQCWDNATR 238
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 527 ALDS----ESERVVQESldnASIGRTTIVIAhRLSTIRNA----DVICVIHNGQIVETGS 578
Cdd:TIGR00956 239 GLDSatalEFIRALKTS---ANILDTTPLVA-IYQCSQDAyelfDKVIVLYEGYQIYFGP 294
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
497-591 |
1.56e-06 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 51.73 E-value: 1.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 497 QMSGGQKQRIAIARAIIKSPKILLLDEATSALDSESERVVQESLD--NASIGRTTIVIAHRLSTIRN-ADVICVIHNGQI 573
Cdd:PRK15093 158 ELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTrlNQNNNTTILLISHDLQMLSQwADKINVLYCGQT 237
|
90
....*....|....*...
gi 15232977 574 VETGSHEELLKRIDGQYT 591
Cdd:PRK15093 238 VETAPSKELVTTPHHPYT 255
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
1015-1216 |
1.71e-06 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 52.71 E-value: 1.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1015 NFSIEIDEGKSTAIVGTSGSGKSTII------GLIERFYdpLKGTVKIDGRDIRSY-HL------------RSLRK---- 1071
Cdd:TIGR00630 626 NITVSIPLGLFTCITGVSGSGKSTLIndtlypALANRLN--GAKTVPGRYTSIEGLeHLdkvihidqspigRTPRSnpat 703
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1072 YISLVSQEPMLFA------------------------------GTI--------------------REN-----IMYGGT 1096
Cdd:TIGR00630 704 YTGVFDEIRELFAetpeakvrgytpgrfsfnvkggrceacqgdGVIkiemhflpdvyvpcevckgkRYNretleVKYKGK 783
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1097 SdkIdeSEIIEAAkAANAHDF---ITSLSNGYDTNCgDKGVQ----------LSGGQKQRIAIARAVLK---NPSVLLLD 1160
Cdd:TIGR00630 784 N--I--ADVLDMT-VEEAYEFfeaVPSISRKLQTLC-DVGLGyirlgqpattLSGGEAQRIKLAKELSKrstGRTLYILD 857
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15232977 1161 EATSALDSKSERVVQDALER-VMVGRTSIMIAHRLSTIQNCDMIVVLGK------GKIVESGT 1216
Cdd:TIGR00630 858 EPTTGLHFDDIKKLLEVLQRlVDKGNTVVVIEHNLDVIKTADYIIDLGPeggdggGTVVASGT 920
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
387-583 |
2.62e-06 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 52.16 E-value: 2.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 387 GKTVALVGGSGSGKSTVISLL--QRFYDPIAGEILIDGVSidKLQVNWLR-----SQMGLVS-----QEPVLFATSITEN 454
Cdd:PLN03140 906 GVLTALMGVSGAGKTTLMDVLagRKTGGYIEGDIRISGFP--KKQETFARisgycEQNDIHSpqvtvRESLIYSAFLRLP 983
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 455 ILFGKEDAS--LDEVVEAAKASNAHTFIsqfplgyktqVGERGVQ-MSGGQKQRIAIARAIIKSPKILLLDEATSALDSE 531
Cdd:PLN03140 984 KEVSKEEKMmfVDEVMELVELDNLKDAI----------VGLPGVTgLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDAR 1053
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15232977 532 SERVVQESLDNA-SIGRTtiviahrlstirnadVICVIHNGQIVETGSHEELL 583
Cdd:PLN03140 1054 AAAIVMRTVRNTvDTGRT---------------VVCTIHQPSIDIFEAFDELL 1091
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
714-929 |
3.12e-06 |
|
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 secretion systems, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) and similar proteins. These transporter subunits include HylB, PrtD, CyaB, CvaB, RsaD, HasD, LipB, and LapB, among many others. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). Most targeted proteins are not cleaved at the N terminus, but rather carry signals located toward the extreme C terminus to direct type I secretion. However, the 10 kDa Escherichia coli colicin V (CvaB) targets the ABC transporter using a cleaved, N-terminal signal sequence. Almost all transport substrates of the type I system have critical functions in attacking host cells either directly or by being essential for host colonization. The ABC-dependent T1SS transports various molecules, from ions, drugs, to proteins of various sizes up to 900 kDa. The molecules secreted vary in size from the small Escherichia coli peptide colicin V, (10 kDa) to the Pseudomonas fluorescens cell adhesion protein LapA of 520 kDa. The best characterized are the RTX toxins such as the adenylate cyclase (CyaA) toxin from Bordetella pertussis, the causative agent of whooping cough, and the lipases such as LipA. Type I secretion is also involved in export of non-protein substrates such as cyclic beta-glucans and polysaccharides.
Pssm-ID: 349999 [Multi-domain] Cd Length: 294 Bit Score: 50.59 E-value: 3.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 714 IYVLLFVGLAIFSFLVNISQHYGFAYMGEYLTKRIREQMLSKILTFEVNWFDIddNSSGAICSRlAKDANVVRSMVGDRM 793
Cdd:cd18555 43 VLGIGILILFLLYGLFSFLRGYIIIKLQTKLDKSLMSDFFEHLLKLPYSFFEN--RSSGDLLFR-ANSNVYIRQILSNQV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 794 SLLVQTISAVIIACIIGLVIAWRLAIVMISVQPLIVVCFYTQRVLLKSLSEKASKAQDESSKLAAEAVSNIRTITAFSSQ 873
Cdd:cd18555 120 ISLIIDLLLLVIYLIYMLYYSPLLTLIVLLLGLLIVLLLLLTRKKIKKLNQEEIVAQTKVQSYLTETLYGIETIKSLGSE 199
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 15232977 874 ERIIKLLKKVQEGPRRESVHRSWLAGIVLGTSRSLITCTSALNFWYGGRLIADGKI 929
Cdd:cd18555 200 KNIYKKWENLFKKQLKAFKKKERLSNILNSISSSIQFIAPLLILWIGAYLVINGEL 255
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
1008-1203 |
3.23e-06 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 51.35 E-value: 3.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1008 PDVVI-FENFSIEIDEGKS-----TAIVGTSGSGKSTIIGLIERFYDPLKGTVKIDgrdIR-SYhlrslrK--YISlVSQ 1078
Cdd:PRK13409 344 PDLTKkLGDFSLEVEGGEIyegevIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE---LKiSY------KpqYIK-PDY 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1079 EpmlfaGTIRENIMygGTSDKIDES----EIIEAakaanahdfiTSLSNGYDTNCGDkgvqLSGGQKQRIAIARAVLKNP 1154
Cdd:PRK13409 414 D-----GTVEDLLR--SITDDLGSSyyksEIIKP----------LQLERLLDKNVKD----LSGGELQRVAIAACLSRDA 472
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15232977 1155 SVLLLDEATSALDSkSERV-VQDALERVMVGR--TSIMIAHRLSTIqncDMI 1203
Cdd:PRK13409 473 DLYLLDEPSAHLDV-EQRLaVAKAIRRIAEEReaTALVVDHDIYMI---DYI 520
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
364-589 |
4.19e-06 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 49.79 E-value: 4.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 364 VKFTYLSRPETTIFDDLCLKIPAGKTVALVGGSGSGKSTVISLL--QRFYDPIAGEILIDGVSIDKLQVNwLRSQMG--L 439
Cdd:PRK09580 4 IKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLagREDYEVTGGTVEFKGKDLLELSPE-DRAGEGifM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 440 VSQEPV--------LFATSITENILFGKEDASLDEVvEAAKASNAHTFISQFPLGYKTQvgERGVQMSGGQKQRIAIARA 511
Cdd:PRK09580 83 AFQYPVeipgvsnqFFLQTALNAVRSYRGQEPLDRF-DFQDLMEEKIALLKMPEDLLTR--SVNVGFSGGEKKRNDILQM 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 512 IIKSPKILLLDEATSALDSESERVVQESLDNASIG-RTTIVIAH--RLSTIRNADVICVIHNGQIVETGSHeELLKRIDG 588
Cdd:PRK09580 160 AVLEPELCILDESDSGLDIDALKIVADGVNSLRDGkRSFIIVTHyqRILDYIKPDYVHVLYQGRIVKSGDF-TLVKQLEE 238
|
.
gi 15232977 589 Q 589
Cdd:PRK09580 239 Q 239
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
379-577 |
8.59e-06 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 47.70 E-value: 8.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 379 DLCLKIPAGKTVALVGGSGSGKST-------------VISLLQRFYDPIAgeilidgVSIDKLQvnwlrsqmglvsqepv 445
Cdd:cd03238 13 NLDVSIPLNVLVVVTGVSGSGKSTlvneglyasgkarLISFLPKFSRNKL-------IFIDQLQ---------------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 446 lfatsitenilfgkedasldevveaakasnahtFISQFPLGYKTqVGERGVQMSGGQKQRIAIARAIIKSPK--ILLLDE 523
Cdd:cd03238 70 ---------------------------------FLIDVGLGYLT-LGQKLSTLSGGELQRVKLASELFSEPPgtLFILDE 115
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15232977 524 ATSALDSESERVVQESLDN-ASIGRTTIVIAHRLSTIRNADVICVI------HNGQIVETG 577
Cdd:cd03238 116 PSTGLHQQDINQLLEVIKGlIDLGNTVILIEHNLDVLSSADWIIDFgpgsgkSGGKVVFSG 176
|
|
| ABC_6TM_MRP7_D2_like |
cd18605 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and ... |
689-878 |
8.96e-06 |
|
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and similar proteins; This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated protein 7 (MRP7), which belongs to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350049 [Multi-domain] Cd Length: 300 Bit Score: 49.07 E-value: 8.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 689 SAYSAGSVISVFFLTSHDQIKektriYVLLFVGLAIFSFLVNISQHYGFAYMGEYLTKRIREQMLSKILTFEVNWFDIdd 768
Cdd:cd18605 23 SYWVSHSNNSFFNFINDSFNF-----FLTVYGFLAGLNSLFTLLRAFLFAYGGLRAARRLHNKLLSSILFAKMSFFDK-- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 769 NSSGAICSRLAKDANvvrsMVGDRMS-----LLVQTISAVIIACIIGLVIAWrLAIVMIsvqPLIVVCFYTQRVL----- 838
Cdd:cd18605 96 TPVGRILNRFSSDVY----TIDDSLPfilniLLAQLFGLLGYLVVICYQLPW-LLLLLL---PLAFIYYRIQRYYratsr 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 15232977 839 -LKSLSEKAskaqdeSSKLAA---EAVSNIRTITAFSSQERIIK 878
Cdd:cd18605 168 eLKRLNSVN------LSPLYThfsETLKGLVTIRAFRKQERFLK 205
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
1023-1195 |
1.13e-05 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 49.84 E-value: 1.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1023 GKSTAIVGTSGSGKSTII---------GLIErfydplkGTVKIDGRDIRSYHLRSLRKYI--------SLVSQEPMLFAG 1085
Cdd:PLN03140 906 GVLTALMGVSGAGKTTLMdvlagrktgGYIE-------GDIRISGFPKKQETFARISGYCeqndihspQVTVRESLIYSA 978
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1086 TIRENIMYGGTSDKIDESEIIEAAKAANAHDFITSLSngydtncGDKGvqLSGGQKQRIAIARAVLKNPSVLLLDEATSA 1165
Cdd:PLN03140 979 FLRLPKEVSKEEKMMFVDEVMELVELDNLKDAIVGLP-------GVTG--LSTEQRKRLTIAVELVANPSIIFMDEPTSG 1049
|
170 180 190
....*....|....*....|....*....|.
gi 15232977 1166 LDSKSERVVQDALER-VMVGRTSIMIAHRLS 1195
Cdd:PLN03140 1050 LDARAAAIVMRTVRNtVDTGRTVVCTIHQPS 1080
|
|
| ABC_6TM_ABCC |
cd18559 |
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents ... |
697-898 |
1.23e-05 |
|
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents the 6-transmembrane (6TM) domain of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The type 3 ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides.
Pssm-ID: 350003 [Multi-domain] Cd Length: 290 Bit Score: 48.75 E-value: 1.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 697 ISVFFLTSHDQIKEKTRIYVLLFVGLAIFSFLVNISQHYGFAYMGEYLTKRIREQMLSKILTFEVNWFDidDNSSGAICS 776
Cdd:cd18559 22 LLLWFDDPVNGPQEHGQVYLSVLGALAILQGITVFQYSMAVSIGGIFASRAVHLDLYHKALRSPISFFE--RTPSGELVN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 777 RLAKDANVVRSMVGDRMSLLVQTISAVIIACIIglviaWRLAIVMISVQ-PLIVVCFYTQRVL---LKSLSEKASKAQDE 852
Cdd:cd18559 100 LFSKDLDRVDSMAPQVIKMWMGPLQNVIGLYLL-----ILLAGPMAAVGiPLGLLYVPVNRVYaasSRQLKRLESVSKDP 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 15232977 853 SSKLAAEAVSNIRTITAFSSQERII-KLLKKVQE--GPRRESVHRSWLA 898
Cdd:cd18559 175 RYKLFNETLLGISVIKAFEWEEAFIrQVDAKRDNelAYLPSIVYLRALA 223
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
1009-1179 |
1.25e-05 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 49.55 E-value: 1.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1009 DVVIFENFSIEIDEGKSTAIVGTSGSGKSTIIGLIERFYDPLKGTVKIdGRDIRsyhlrslrkyISLVSQEpmlfagtiR 1088
Cdd:TIGR03719 334 DKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETVK----------LAYVDQS--------R 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1089 ENImyggTSDKIDESEIieaakaANAHDFITSlsNGYDTN----CGD---KGV-------QLSGGQKQRIAIARAVLKNP 1154
Cdd:TIGR03719 395 DAL----DPNKTVWEEI------SGGLDIIKL--GKREIPsrayVGRfnfKGSdqqkkvgQLSGGERNRVHLAKTLKSGG 462
|
170 180
....*....|....*....|....*
gi 15232977 1155 SVLLLDEATSALDSKSERVVQDALE 1179
Cdd:TIGR03719 463 NVLLLDEPTNDLDVETLRALEEALL 487
|
|
| ABC_6TM_MRP4_D2_like |
cd18601 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4) ... |
706-966 |
1.54e-05 |
|
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4) and similar proteins; This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4), which belongs to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350045 [Multi-domain] Cd Length: 314 Bit Score: 48.47 E-value: 1.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 706 DQIKEKTRIYVLLFVGLAIFSFLVNISQHYGFAYMGEYLTKRIREQMLSKILTFEVNWFDIddNSSGAICSRLAKDANVV 785
Cdd:cd18601 52 DIEDLDRDFNLGIYAGLTAATFVFGFLRSLLFFHVAVSASKNLHNKMFASVLRAPIRFFDT--NPIGRILNRFSKDIGHL 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 786 RSMVG----DRMSLLVQTISAVIIACIiglVIAWrlaiVMISVQPLIVVCFYTQRVLLKSLSE-KASKAQDES---SKLA 857
Cdd:cd18601 130 DDLLPltflDFLQLLLQVVGVVLLAVV---VNPW----VLIPVIPLVILFLFLRRYYLKTSREvKRIEGTTRSpvfSHLS 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 858 AeAVSNIRTITAFSSQERIIKLLKKVQEgprresVH-RSWLAgiVLGTSRslitctsalnfWYGGRLiadgkivsKAFFE 936
Cdd:cd18601 203 S-TLQGLWTIRAYSAQERFQEEFDAHQD------LHsEAWFL--FLATSR-----------WLAVRL--------DALCA 254
|
250 260 270
....*....|....*....|....*....|..
gi 15232977 937 IFLIFVTTGRVIadagtmttdLARGLDA--VG 966
Cdd:cd18601 255 LFVTVVAFGSLF---------LAESLDAglVG 277
|
|
| ABC_6TM_VMR1_D2_like |
cd18604 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
715-883 |
2.52e-05 |
|
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; This group includes the six-transmembrane domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1, all of which are ABC transporters of the MRP (multidrug resistance-associated protein) subfamily (ABCC). Yeast ABCC (also termed MRP/CFTR) subfamily includes six members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p, Vmr1p, and Yor1p), of which three members (Ycf1p, Bpt1P and Yor1p) are not included here. While Yor1p, an oligomycin resistance ABC transporter, has been shown to localize to the plasma membrane, the other 4 members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p and Vmr1p) have been shown to localize to the vacuolar membrane. Ybt1p is originally identified as a bile acid transporter and regulates membrane fusion through Ca2+ transport modulation. Ybt1p also plays a part in ade2 pigment transport. Moreover, Ybt1p has been recently shown to translocate phosphatidylcholine from the outer leaflet of the vacuole to the inner leaflet for degradation and choline recycling. Vmr1p, a vacuolar membrane protein, participates in the export of numerous growth inhibitors from the cell, such as cycloheximide, 2,4-dinitrophenole, cadmium and other toxic metals. Nft1p is not well-characterized, but it is proposed to be regulate Ycf1p, which is involved in heavy metal detoxification.
Pssm-ID: 350048 [Multi-domain] Cd Length: 297 Bit Score: 47.46 E-value: 2.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 715 YVLLFVGLAIFSFLVNISQHYGFAYMGEYLTKRIREQMLSKILTFEVNWFDIddNSSGAICSRLAKDANVVRSMVGDRMS 794
Cdd:cd18604 45 YLGIYALISLLSVLLGTLRYLLFFFGSLRASRKLHERLLHSVLRAPLRWLDT--TPVGRILNRFSKDIETIDSELADSLS 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 795 LLVQTISAVIIACIIGLVIAWRLAIVMIsvqPLIVVCFYTQRVLLK-SLSEKaskaQDESSKLA------AEAVSNIRTI 867
Cdd:cd18604 123 SLLESTLSLLVILIAIVVVSPAFLLPAV---VLAALYVYIGRLYLRaSRELK----RLESVARSpilshfGETLAGLVTI 195
|
170
....*....|....*..
gi 15232977 868 TAFSSQERIIK-LLKKV 883
Cdd:cd18604 196 RAFGAEERFIEeMLRRI 212
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1136-1212 |
2.86e-05 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 48.41 E-value: 2.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1136 LSGGQKQRIAIARAVLKNPSVLLLDEATSALDSKServvQDALERVMVG-RTSIM-IAHRLSTIQNcdM---IVVLGKGK 1210
Cdd:PRK11147 157 LSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIET----IEWLEGFLKTfQGSIIfISHDRSFIRN--MatrIVDLDRGK 230
|
..
gi 15232977 1211 IV 1212
Cdd:PRK11147 231 LV 232
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
999-1211 |
2.94e-05 |
|
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: 48.28 E-value: 2.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 999 NVDFAYPTRPDVVIFENFSIEIDEGKSTAIVGTSGSGKSTIIGLIERFYD-PLKGTVKIDGR--DIRSyHLRSLRKYISL 1075
Cdd:TIGR02633 262 NLTCWDVINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPgKFEGNVFINGKpvDIRN-PAQAIRAGIAM 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1076 VSQE-------PMLFAGtirENIMYGGTSDKIDESEIIEAAKAANAHDFITSLSngYDTNCGDKGV-QLSGGQKQRIAIA 1147
Cdd:TIGR02633 341 VPEDrkrhgivPILGVG---KNITLSVLKSFCFKMRIDAAAELQIIGSAIQRLK--VKTASPFLPIgRLSGGNQQKAVLA 415
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1148 RAVLKNPSVLLLDEATSALD--SKSE---RVVQDALERVMVgrtsIMIAHRLSTIQN-CDMIVVLGKGKI 1211
Cdd:TIGR02633 416 KMLLTNPRVLILDEPTRGVDvgAKYEiykLINQLAQEGVAI----IVVSSELAEVLGlSDRVLVIGEGKL 481
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
995-1197 |
4.04e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 47.70 E-value: 4.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 995 ITFLNVDFAYPTRPdvvIFENFSIEIDEGKSTAIVGTSGSGKSTIIGLIERfyDPLKG---TVKIDGR---------DIR 1062
Cdd:PRK10938 261 IVLNNGVVSYNDRP---ILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITG--DHPQGysnDLTLFGRrrgsgetiwDIK 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1063 syhlrslrKYISLVSQEPML---FAGTIReNIMYGGTSDKIDESEIIEAAKAANAHDFITSLsnGYDTNCGDKGVQ-LSG 1138
Cdd:PRK10938 336 --------KHIGYVSSSLHLdyrVSTSVR-NVILSGFFDSIGIYQAVSDRQQKLAQQWLDIL--GIDKRTADAPFHsLSW 404
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15232977 1139 GQkQRIA-IARAVLKNPSVLLLDEATSALDSKSERVVQDALErVMV--GRTSIM------------IAHRLSTI 1197
Cdd:PRK10938 405 GQ-QRLAlIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVD-VLIseGETQLLfvshhaedapacITHRLEFV 476
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
359-537 |
4.19e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 47.93 E-value: 4.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 359 VEFNHVKFTYLSRPetTIFDDLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYDPIAGEILidgvsidklqvnwlRS--- 435
Cdd:PLN03073 509 ISFSDASFGYPGGP--LLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVF--------------RSakv 572
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 436 QMGLVSQEPVlfatsitenilfgkedASLDevveaaKASNAHTFISQ-FP----------LGYKTQVGERGVQ----MSG 500
Cdd:PLN03073 573 RMAVFSQHHV----------------DGLD------LSSNPLLYMMRcFPgvpeqklrahLGSFGVTGNLALQpmytLSG 630
|
170 180 190
....*....|....*....|....*....|....*...
gi 15232977 501 GQKQRIAIARAIIKSPKILLLDEATSALDSES-ERVVQ 537
Cdd:PLN03073 631 GQKSRVAFAKITFKKPHILLLDEPSNHLDLDAvEALIQ 668
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
1134-1197 |
4.65e-05 |
|
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: 45.26 E-value: 4.65e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15232977 1134 VQLSGGQKQRIAIARAVLKNPSVLLLDEATSALDSKSERVVQDALERVMV--GRTSIMIAHRLSTI 1197
Cdd:cd03222 70 IDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEegKKTALVVEHDLAVL 135
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
378-573 |
6.58e-05 |
|
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: 47.13 E-value: 6.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 378 DDLCLKIPAGKTVALVGGSGSGKSTVISLLQRFYD-PIAGEILIDGVSID-KLQVNWLRSQMGLVSQE-------PVL-F 447
Cdd:TIGR02633 277 DDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPgKFEGNVFINGKPVDiRNPAQAIRAGIAMVPEDrkrhgivPILgV 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 448 ATSITENIL--FGK-----EDASLDEVVEAAKASNAHTFISQFPLGyktqvgergvQMSGGQKQRIAIARAIIKSPKILL 520
Cdd:TIGR02633 357 GKNITLSVLksFCFkmridAAAELQIIGSAIQRLKVKTASPFLPIG----------RLSGGNQQKAVLAKMLLTNPRVLI 426
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15232977 521 LDEATSALDSESERVVQESLDN-ASIGRTTIVIAHRLSTIRN-ADVICVIHNGQI 573
Cdd:TIGR02633 427 LDEPTRGVDVGAKYEIYKLINQlAQEGVAIIVVSSELAEVLGlSDRVLVIGEGKL 481
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
374-534 |
8.37e-05 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 47.04 E-value: 8.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 374 TTIFDDLCLKIPAGKTVALVGGSGSGKSTVISLlqrfydpIAG-EILIDGvsidklQVNWLRSQM--------------- 437
Cdd:NF033858 14 TVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSL-------IAGaRKIQQG------RVEVLGGDMadarhrravcpriay 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 438 ---GLVSQepvLFAT-SITENI-----LFG---KE-DASLDEVVEAakasnahTFISQFPlgyktqvgER--GvQMSGGQ 502
Cdd:NF033858 81 mpqGLGKN---LYPTlSVFENLdffgrLFGqdaAErRRRIDELLRA-------TGLAPFA--------DRpaG-KLSGGM 141
|
170 180 190
....*....|....*....|....*....|..
gi 15232977 503 KQRIAIARAIIKSPKILLLDEATSALDSESER 534
Cdd:NF033858 142 KQKLGLCCALIHDPDLLILDEPTTGVDPLSRR 173
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1005-1211 |
8.84e-05 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 46.46 E-value: 8.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1005 PTRPDVVIFENFSIEIDEGKSTAIVGTSGSGK----STIIGLIERFYdplKGTVKIDGR--DIRSYHlRSLRKYISLVSQ 1078
Cdd:PRK13549 270 PVNPHIKRVDDVSFSLRRGEILGIAGLVGAGRtelvQCLFGAYPGRW---EGEIFIDGKpvKIRNPQ-QAIAQGIAMVPE 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1079 E-------PMLFAGtirENIMYGGTSDKIDESEIIEAAKAANAHDFITSLSngYDTNCGDKGV-QLSGGQKQRIAIARAV 1150
Cdd:PRK13549 346 DrkrdgivPVMGVG---KNITLAALDRFTGGSRIDDAAELKTILESIQRLK--VKTASPELAIaRLSGGNQQKAVLAKCL 420
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15232977 1151 LKNPSVLLLDEATSALD--SKSE--RVVQDALERvmvGRTSIMIAHRLSTIQN-CDMIVVLGKGKI 1211
Cdd:PRK13549 421 LLNPKILILDEPTRGIDvgAKYEiyKLINQLVQQ---GVAIIVISSELPEVLGlSDRVLVMHEGKL 483
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
486-584 |
1.01e-04 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 46.26 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 486 GYKTQVGergvQMSGGQKQRIAIARAIIKSPKILLLDEATSALDSESE-RVVQESLDNASIGRTTIVIAHRLSTIRN-AD 563
Cdd:PRK10982 384 GHRTQIG----SLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKfEIYQLIAELAKKDKGIIIISSEMPELLGiTD 459
|
90 100
....*....|....*....|....*.
gi 15232977 564 VICVIHNGQ---IVETG--SHEELLK 584
Cdd:PRK10982 460 RILVMSNGLvagIVDTKttTQNEILR 485
|
|
| ABC_6TM_HetC_like |
cd18568 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ... |
771-929 |
1.09e-04 |
|
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS (type 1 secretion systems), such as heterocyst differentiation protein HetC. HetC is similar to ABC protein exporters of T1SS (type 1 secretion systems) and is involved in early regulation of heterocyst differentiation in the filamentous cynobacterium Anabaena sp. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. ABC-transporter proteins in this group carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion.
Pssm-ID: 350012 [Multi-domain] Cd Length: 294 Bit Score: 45.63 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 771 SGAICSRLAKDANVVRSMVGDRMSLLVQTISAVIIACIIgLVIAWRLAIVMISVQPLIVVCFYTQRVLLKSLSEKASKAQ 850
Cdd:cd18568 98 VGDIITRFQENQKIRRFLTRSALTTILDLLMVFIYLGLM-FYYNLQLTLIVLAFIPLYVLLTLLSSPKLKRNSREIFQAN 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 851 DESSKLAAEAVSNIRTITAFSS--------QERIIKLLKKvqegprresVHRSWLAGIVLGTSRSLI-TCTSALNFWYGG 921
Cdd:cd18568 177 AEQQSFLVEALTGIATIKALAAerpirwrwENKFAKALNT---------RFRGQKLSIVLQLISSLInHLGTIAVLWYGA 247
|
....*...
gi 15232977 922 RLIADGKI 929
Cdd:cd18568 248 YLVISGQL 255
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
1006-1167 |
1.94e-04 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 44.07 E-value: 1.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1006 TRPDVVIFENFSIEIDEGKSTAIVGTSGSGKSTIIGLIERFYDPLKGTVKIDGRDIRSYHlRSlrKYISLVSQEPMLFAG 1085
Cdd:PRK13543 20 SRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGD-RS--RFMAYLGHLPGLKAD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1086 -TIRENIMYGGTSDKIDESEIIEAAKAanahdfITSLSNGYDTNCGdkgvQLSGGQKQRIAIARAVLKNPSVLLLDEATS 1164
Cdd:PRK13543 97 lSTLENLHFLCGLHGRRAKQMPGSALA------IVGLAGYEDTLVR----QLSAGQKKRLALARLWLSPAPLWLLDEPYA 166
|
...
gi 15232977 1165 ALD 1167
Cdd:PRK13543 167 NLD 169
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
485-591 |
1.96e-04 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 45.83 E-value: 1.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 485 LGYkTQVGERGVQMSGGQKQRIAIARAIIKSP--KIL-LLDEATSALDSESER----VVQESLDNasiGRTTIVIAHRLS 557
Cdd:PRK00349 819 LGY-IKLGQPATTLSGGEAQRVKLAKELSKRStgKTLyILDEPTTGLHFEDIRklleVLHRLVDK---GNTVVVIEHNLD 894
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 15232977 558 TIRNADVIcvI--------HNGQIVETGSHEELLKrIDGQYT 591
Cdd:PRK00349 895 VIKTADWI--IdlgpeggdGGGEIVATGTPEEVAK-VEASYT 933
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
995-1221 |
2.02e-04 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 45.18 E-value: 2.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 995 ITFLNVDFAYPTRPdVVIFENFSIEIDEGKSTAIVGTSGSGKS----TIIGLIERFYDPLKGTVKIDGRDIRSYHLRSLR 1070
Cdd:PRK15093 6 IRNLTIEFKTSDGW-VKAVDRVSMTLTEGEIRGLVGESGSGKSliakAICGVTKDNWRVTADRMRFDDIDLLRLSPRERR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1071 KYI----SLVSQEP---MLFAGTIRENIM-------YGG------TSDKIDESEIIEAAKAANAHDFITSLSngydtncg 1130
Cdd:PRK15093 85 KLVghnvSMIFQEPqscLDPSERVGRQLMqnipgwtYKGrwwqrfGWRKRRAIELLHRVGIKDHKDAMRSFP-------- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1131 dkgVQLSGGQKQRIAIARAVLKNPSVLLLDEATSALDSKSERVVQDALERVMV--GRTSIMIAHRLSTI-QNCDMIVVLG 1207
Cdd:PRK15093 157 ---YELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQnnNTTILLISHDLQMLsQWADKINVLY 233
|
250
....*....|....
gi 15232977 1208 KGKIVESGTHSSLL 1221
Cdd:PRK15093 234 CGQTVETAPSKELV 247
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1014-1167 |
2.16e-04 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 45.38 E-value: 2.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1014 ENFSIEIDEGKSTAIVGTSGSGKSTIIGLIERFYDPLKGTVKIDGRDIRSYH----LRSLRKYISLVSQEPMLFAG-TIR 1088
Cdd:PRK10762 269 NDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSpqdgLANGIVYISEDRKRDGLVLGmSVK 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1089 ENI---------MYGGTSDKIDESEIIEaakaanahDFITsLSNgYDTNCGDKGV-QLSGGQKQRIAIARAVLKNPSVLL 1158
Cdd:PRK10762 349 ENMsltalryfsRAGGSLKHADEQQAVS--------DFIR-LFN-IKTPSMEQAIgLLSGGNQQKVAIARGLMTRPKVLI 418
|
....*....
gi 15232977 1159 LDEATSALD 1167
Cdd:PRK10762 419 LDEPTRGVD 427
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
74-303 |
2.25e-04 |
|
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm287) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349992 [Multi-domain] Cd Length: 292 Bit Score: 44.70 E-value: 2.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 74 MQTISKNVVALLYVACGSWVICFLEGYCWTRTGERQAARMREKYLRAVLRQDVGYFDlHVtSTSDVITSISSDSLVIQDF 153
Cdd:cd18548 35 LSYILRTGLLMLLLALLGLIAGILAGYFAAKASQGFGRDLRKDLFEKIQSFSFAEID-KF-GTSSLITRLTNDVTQVQNF 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 154 LSEKLPNFLMNASAFVASYIVSFILMWRLTIVGFPFIILLLVPGLMYGRALVSISRKIHEQYNEAGSIAEQAISSVRTVY 233
Cdd:cd18548 113 VMMLLRMLVRAPIMLIGAIIMAFRINPKLALILLVAIPILALVVFLIMKKAIPLFKKVQKKLDRLNRVVRENLTGIRVIR 192
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15232977 234 AFGSENKMIGKF---STALRG-SVKLGLRQGLAK-GITIGSNGVThaiwAFLTWYGSRLVMNHGSKGGTVFVVIS 303
Cdd:cd18548 193 AFNREDYEEERFdkaNDDLTDtSLKAGRLMALLNpLMMLIMNLAI----VAILWFGGHLINAGSLQVGDLVAFIN 263
|
|
| ABC_6TM_MRP7_D2_like |
cd18605 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and ... |
55-334 |
2.70e-04 |
|
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and similar proteins; This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated protein 7 (MRP7), which belongs to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350049 [Multi-domain] Cd Length: 300 Bit Score: 44.44 E-value: 2.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 55 IFNTLLNNLGTSSSNNKTFMQTisknvvaLLYVACGSWVICFLEGYCWTRTGERQAARMREKYLRAVLRQDVGYFDlhVT 134
Cdd:cd18605 26 VSHSNNSFFNFINDSFNFFLTV-------YGFLAGLNSLFTLLRAFLFAYGGLRAARRLHNKLLSSILFAKMSFFD--KT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 135 STSDVITSISSDSLVIQDFLSEKLpNFLMNASAFVASYIVsfilmwrLTIVGFPFIILLLVP-GLMYG------------ 201
Cdd:cd18605 97 PVGRILNRFSSDVYTIDDSLPFIL-NILLAQLFGLLGYLV-------VICYQLPWLLLLLLPlAFIYYriqryyratsre 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 202 -RALVSISR-KIHEQYNEagsiaeqAISSVRTVYAFGSENKMIGKFSTALRGSVK-----------LGLRqglakgITIG 268
Cdd:cd18605 169 lKRLNSVNLsPLYTHFSE-------TLKGLVTIRAFRKQERFLKEYLEKLENNQRaqlasqaasqwLSIR------LQLL 235
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15232977 269 SNGVTHAIwAFLTwygsrlVMNHGSKGGTVFVVIS-CITYgGVSLGQSLSNL-KYFSE---AFVAWERILE 334
Cdd:cd18605 236 GVLIVTFV-ALTA------VVQHFFGLSIDAGLIGlALSY-ALPITGLLSGLlNSFTEtekEMVSVERVRQ 298
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
47-334 |
2.85e-04 |
|
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group represents the six-transmembrane domain 2 (TMD2) of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The type 3 ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. All ABC transporters share a common architecture of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. By contrast, bacterial ABC exporters are typically assembled from dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are comprised of two identical TMDs and two identical NBDs.
Pssm-ID: 350024 [Multi-domain] Cd Length: 294 Bit Score: 44.42 E-value: 2.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 47 FITPVVVFIFNTLLNNLGTSSSNNKTFMQTISKNVVALLYVACGSWVICFLEGYCWTRTGERQAARMREKYLRAVLRQDV 126
Cdd:cd18580 8 LLLLAFLSQFSNIWLDWWSSDWSSSPNSSSGYYLGVYAALLVLASVLLVLLRWLLFVLAGLRASRRLHDKLLRSVLRAPM 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 127 GYFDlhVTSTSDVITSISSDslviQDFLSEKLPNFLMNASAFVASYIVSFILM----WRLTIVGFPFIILLLVPGLMYGR 202
Cdd:cd18580 88 SFFD--TTPSGRILNRFSKD----IGLIDEELPLALLDFLQSLFSVLGSLIVIaivsPYFLIVLPPLLVVYYLLQRYYLR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 203 A------LVSISRK-IHEQYNEagSIaeQAISSVRtvyAFGSENKMIGKFSTALRGSVK-----------LGLRQGLakg 264
Cdd:cd18580 162 TsrqlrrLESESRSpLYSHFSE--TL--SGLSTIR---AFGWQERFIEENLRLLDASQRafylllavqrwLGLRLDL--- 231
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15232977 265 ITIGSNGVThaiwAFLTwygsrLVMNHGSKGGTVFVVISCItyggVSLGQSLSNL-KYFSE---AFVAWERILE 334
Cdd:cd18580 232 LGALLALVV----ALLA-----VLLRSSISAGLVGLALTYA----LSLTGSLQWLvRQWTEletSMVSVERILE 292
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
474-589 |
2.94e-04 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 44.73 E-value: 2.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 474 SNAHTFISQFPLgyKTQVGERGVQMSGGQKQRIAIARAIIKSPKILLLDEATSALDSESERVVQESLDN-ASIGRTTIVI 552
Cdd:NF000106 123 ARADELLERFSL--TEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSmVRDGATVLLT 200
|
90 100 110
....*....|....*....|....*....|....*...
gi 15232977 553 AHRLSTIRN-ADVICVIHNGQIVETGSHEELLKRIDGQ 589
Cdd:NF000106 201 TQYMEEAEQlAHELTVIDRGRVIADGKVDELKTKVGGR 238
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18566 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ... |
716-929 |
3.84e-04 |
|
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350010 [Multi-domain] Cd Length: 294 Bit Score: 44.11 E-value: 3.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 716 VLLFVGLAIFSFLVNISQHYGFAYMGEYLTKRIREQMLSKILTFEVNWFDidDNSSGAICSRLaKDANVVRSMVGDRMSL 795
Cdd:cd18566 45 VIGVVIAILLESLLRLLRSYILAWIGARFDHRLSNAAFEHLLSLPLSFFE--REPSGAHLERL-NSLEQIREFLTGQALL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 796 LVQTISAVIIACIIGLVIAWRLAIVMISVQPLIVVCFYTQRVLLKSLSEKASKAQDESSKLAAEAVSNIRTITAFSSQER 875
Cdd:cd18566 122 ALLDLPFVLIFLGLIWYLGGKLVLVPLVLLGLFVLVAILLGPILRRALKERSRADERRQNFLIETLTGIHTIKAMAMEPQ 201
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15232977 876 IIKLLKKVQEGPRRESVHRSWLAGIVLGTSRSLITCTSALNFWYGGRLIADGKI 929
Cdd:cd18566 202 MLRRYERLQANAAYAGFKVAKINAVAQTLGQLFSQVSMVAVVAFGALLVINGDL 255
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
1130-1223 |
3.99e-04 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 44.34 E-value: 3.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1130 GDKGVQLSGGQKQRIAIARAVLKNPSVLLLDEATSALDSKSERVVQDALeRVMV--GRTSIMIAHRLSTI-QNCDMIVVL 1206
Cdd:NF000106 139 GRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEV-RSMVrdGATVLLTTQYMEEAeQLAHELTVI 217
|
90
....*....|....*..
gi 15232977 1207 GKGKIVESGTHSSLLEK 1223
Cdd:NF000106 218 DRGRVIADGKVDELKTK 234
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
436-710 |
4.49e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 44.82 E-value: 4.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 436 QMGLvsQEPVLFATSITEnilfgkEDASLDEVVEAAKasNAHTFISQFPLGYKTQvgERGVQ-MSGGQKQRIAIARA--- 511
Cdd:PRK00635 426 QMSL--QELFIFLSQLPS------KSLSIEEVLQGLK--SRLSILIDLGLPYLTP--ERALAtLSGGEQERTALAKHlga 493
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 512 -------IIKSPKILLLDEATSALdsesERVVQESLDNasiGRTTIVIAHRLSTIRNAD-VICV-----IHNGQIVETGS 578
Cdd:PRK00635 494 eligityILDEPSIGLHPQDTHKL----INVIKKLRDQ---GNTVLLVEHDEQMISLADrIIDIgpgagIFGGEVLFNGS 566
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 579 HEELLKRIDgqytSLVSlqQMENEESNVNINVSVTKDQ-VMSLSKDFKYSQHN---SIGSTSSSIVTNV-----SDLIpn 649
Cdd:PRK00635 567 PREFLAKSD----SLTA--KYLRQELTIPIPEKRTNSLgTLTLSKATKHNLKDltiSLPLGRLTVVTGVsgsgkSSLI-- 638
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15232977 650 dNQPLVPSFTRLMVMNRPEWKHALYGCLSaALVGVLQPVSAYSAGSvISVFFLTSHDQIKE 710
Cdd:PRK00635 639 -NDTLVPAVEEFIEQGFCSNLSIQWGAIS-RLVHITRDLPGRSQRS-IPLTYIKAFDDLRE 696
|
|
| ABC_6TM_PrtD_like |
cd18586 |
Six-transmembrane helical domain (6TM) domain of the ABC subunit (PrtD) in the T1SS ... |
716-929 |
4.83e-04 |
|
Six-transmembrane helical domain (6TM) domain of the ABC subunit (PrtD) in the T1SS metalloprotease secretion system, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) such as PrtD, which is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. The Aquifex aeolicus PrtDEF of T1SS is composed of an inner-membrane ABC transporter (PrtD), a periplasmic membrane-fusion protein (PrtE), and an outer-membrane porin (PrtF). These three components assemble into complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides
Pssm-ID: 350030 [Multi-domain] Cd Length: 291 Bit Score: 43.75 E-value: 4.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 716 VLLFVGLAIFSFLVNISQHYGFAYMGEYLTKRIREQMLSKI--LTFEVNwfdiddnSSGAICSRLaKDANVVRSMVGDRM 793
Cdd:cd18586 45 TLGMVVLLAFDGLLRQVRSRILQRVGLRLDVELGRRVFRAVleLPLESR-------PSGYWQQLL-RDLDTLRNFLTGPS 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 794 SLLVQTISAVIIACIIGLVIAWRLAIVMISVQPLIVVCFYTQRVLLKSLSEKASKAQDESSKLAAEAVSNIRTITAFSSQ 873
Cdd:cd18586 117 LFAFFDLPWAPLFLAVIFLIHPPLGWVALVGAPVLVGLAWLNHRATRKPLGEANEAQAARDALAAETLRNAETIKALGML 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 15232977 874 ERIIKLLKKVQEGPRRESVHRSWLAGIVLGTSRSLITCTSALNFWYGGRLIADGKI 929
Cdd:cd18586 197 GNLRRRWEARHAETLELQIRASDLAGAISAIGKTLRMALQSLILGVGAYLVIDGEL 252
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
113-332 |
5.27e-04 |
|
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 secretion systems, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) and similar proteins. These transporter subunits include HylB, PrtD, CyaB, CvaB, RsaD, HasD, LipB, and LapB, among many others. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). Most targeted proteins are not cleaved at the N terminus, but rather carry signals located toward the extreme C terminus to direct type I secretion. However, the 10 kDa Escherichia coli colicin V (CvaB) targets the ABC transporter using a cleaved, N-terminal signal sequence. Almost all transport substrates of the type I system have critical functions in attacking host cells either directly or by being essential for host colonization. The ABC-dependent T1SS transports various molecules, from ions, drugs, to proteins of various sizes up to 900 kDa. The molecules secreted vary in size from the small Escherichia coli peptide colicin V, (10 kDa) to the Pseudomonas fluorescens cell adhesion protein LapA of 520 kDa. The best characterized are the RTX toxins such as the adenylate cyclase (CyaA) toxin from Bordetella pertussis, the causative agent of whooping cough, and the lipases such as LipA. Type I secretion is also involved in export of non-protein substrates such as cyclic beta-glucans and polysaccharides.
Pssm-ID: 349999 [Multi-domain] Cd Length: 294 Bit Score: 43.65 E-value: 5.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 113 MREKYLRAVLRQDVGYFDLHvtSTSDVITSISSDSlVIQDFLSEKLPNFLMNASAFVASYIVSFILMWRLTIVGFPFIIL 192
Cdd:cd18555 77 LMSDFFEHLLKLPYSFFENR--SSGDLLFRANSNV-YIRQILSNQVISLIIDLLLLVIYLIYMLYYSPLLTLIVLLLGLL 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 193 LLVPGLMYGRALVSISRKIHEQYNEAGSIAEQAISSVRTVYAFGSENKMI----GKFSTALRGSVKLGLRQGLakgITIG 268
Cdd:cd18555 154 IVLLLLLTRKKIKKLNQEEIVAQTKVQSYLTETLYGIETIKSLGSEKNIYkkweNLFKKQLKAFKKKERLSNI---LNSI 230
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 269 SNGVTHAIWAFLTWYGSRLVMNHGSKGGTvfvVISCITYGG------VSLGQSLSNLKYFSEAFvawERI 332
Cdd:cd18555 231 SSSIQFIAPLLILWIGAYLVINGELTLGE---LIAFSSLAGsfltpiVSLINSYNQFILLKSYL---ERL 294
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
498-592 |
5.65e-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: 44.23 E-value: 5.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 498 MSGGQKQRIAIARAIIK--SPKILLLDEATSAL-DSESERVVQESLDNASIGRTTIVIAHRLSTIRNADVICVI------ 568
Cdd:TIGR00630 489 LSGGEAQRIRLATQIGSglTGVLYVLDEPSIGLhQRDNRRLINTLKRLRDLGNTLIVVEHDEDTIRAADYVIDIgpgage 568
|
90 100
....*....|....*....|....*..
gi 15232977 569 HNGQIVETGSHEELLKR---IDGQYTS 592
Cdd:TIGR00630 569 HGGEVVASGTPEEILANpdsLTGQYLS 595
|
|
| ABC_6TM_VMR1_D2_like |
cd18604 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
32-245 |
5.70e-04 |
|
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; This group includes the six-transmembrane domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1, all of which are ABC transporters of the MRP (multidrug resistance-associated protein) subfamily (ABCC). Yeast ABCC (also termed MRP/CFTR) subfamily includes six members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p, Vmr1p, and Yor1p), of which three members (Ycf1p, Bpt1P and Yor1p) are not included here. While Yor1p, an oligomycin resistance ABC transporter, has been shown to localize to the plasma membrane, the other 4 members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p and Vmr1p) have been shown to localize to the vacuolar membrane. Ybt1p is originally identified as a bile acid transporter and regulates membrane fusion through Ca2+ transport modulation. Ybt1p also plays a part in ade2 pigment transport. Moreover, Ybt1p has been recently shown to translocate phosphatidylcholine from the outer leaflet of the vacuole to the inner leaflet for degradation and choline recycling. Vmr1p, a vacuolar membrane protein, participates in the export of numerous growth inhibitors from the cell, such as cycloheximide, 2,4-dinitrophenole, cadmium and other toxic metals. Nft1p is not well-characterized, but it is proposed to be regulate Ycf1p, which is involved in heavy metal detoxification.
Pssm-ID: 350048 [Multi-domain] Cd Length: 297 Bit Score: 43.23 E-value: 5.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 32 WILMALGLIGAVgdgfitpvVVFIFNTLLnnLGTSSSNNKTFMQTISKNVVALLYVA-----CGSWVICFLEGYCWTRTG 106
Cdd:cd18604 1 WALLLLLFVLSQ--------LLSVGQSWW--LGIWASAYETSSALPPSEVSVLYYLGiyaliSLLSVLLGTLRYLLFFFG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 107 ERQAAR-MREKYLRAVLRQDVGYFDlhVTSTSDVITSISSDSLVIQDFLSEKLPNFLMNASAFVASYIVSFILMWRLTIV 185
Cdd:cd18604 71 SLRASRkLHERLLHSVLRAPLRWLD--TTPVGRILNRFSKDIETIDSELADSLSSLLESTLSLLVILIAIVVVSPAFLLP 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15232977 186 GFPFIILLLVPGLMYGRA------LVSISRK-IHEQYNEAGSiaeqAISSVRtvyAFGSENKMIGKF 245
Cdd:cd18604 149 AVVLAALYVYIGRLYLRAsrelkrLESVARSpILSHFGETLA----GLVTIR---AFGAEERFIEEM 208
|
|
| ABC_6TM_MRP1_2_3_6_D2_like |
cd18603 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, ... |
714-885 |
5.83e-04 |
|
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, 2, 3 and 6; This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, 2, 3 and 6, all of which are belonging to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350047 [Multi-domain] Cd Length: 296 Bit Score: 43.24 E-value: 5.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 714 IYVLLFVGLAIFSFLVNISqhygFAYMGEYLTKRIREQMLSKILTFEVNWFDIddNSSGAICSRLAKDANVVRSMVGDRM 793
Cdd:cd18603 46 VYGALGLGQAIFVFLGSLA----LALGCVRASRNLHNKLLHNILRAPMSFFDT--TPLGRILNRFSKDIDTVDNTLPQNI 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 794 SLLVQTISAVIIACIiglVIAWRLAIVMISVQPLIVVCFYTQRVL------LKSLsEKASKaqdeSSKLA--AEAVSNIR 865
Cdd:cd18603 120 RSFLNCLFQVISTLV---VISISTPIFLVVIIPLAILYFFIQRFYvatsrqLKRL-ESVSR----SPIYShfSETLQGAS 191
|
170 180
....*....|....*....|.
gi 15232977 866 TITAFSSQER-IIKLLKKVQE 885
Cdd:cd18603 192 TIRAYGVQERfIRESDRRVDE 212
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
1013-1040 |
7.14e-04 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 39.12 E-value: 7.14e-04
10 20
....*....|....*....|....*...
gi 15232977 1013 FENFSIEIDEGKSTAIVGTSGSGKSTII 1040
Cdd:pfam13555 12 FDGHTIPIDPRGNTLLTGPSGSGKSTLL 39
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
379-577 |
7.40e-04 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 42.63 E-value: 7.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 379 DLCLKIPAGKTVALVGGSGSGKS-----TVISLLQRFY--------------------DPIAGeiLIDGVSID-KLQVNW 432
Cdd:cd03270 13 NVDVDIPRNKLVVITGVSGSGKSslafdTIYAEGQRRYveslsayarqflgqmdkpdvDSIEG--LSPAIAIDqKTTSRN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 433 LRSQMGlvsqepvlfatSITE-----NILFGKedASLDEVVEaakasnahtFISQFPLGYKTqVGERGVQMSGGQKQRIA 507
Cdd:cd03270 91 PRSTVG-----------TVTEiydylRLLFAR--VGIRERLG---------FLVDVGLGYLT-LSRSAPTLSGGEAQRIR 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15232977 508 IARAIIK--SPKILLLDEATSALDSESERVVQESLDN-ASIGRTTIVIAHRLSTIRNAD-VICV-----IHNGQIVETG 577
Cdd:cd03270 148 LATQIGSglTGVLYVLDEPSIGLHPRDNDRLIETLKRlRDLGNTVLVVEHDEDTIRAADhVIDIgpgagVHGGEIVAQG 226
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
487-569 |
8.04e-04 |
|
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: 41.79 E-value: 8.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 487 YKTQVgergVQMSGGQKQRIAIARAIIKSPKILLLDEATSALDSE----SERVVQESLDNASigRTTIVIAHRLSTIRN- 561
Cdd:cd03222 65 YKPQY----IDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEqrlnAARAIRRLSEEGK--KTALVVEHDLAVLDYl 138
|
....*...
gi 15232977 562 ADVICVIH 569
Cdd:cd03222 139 SDRIHVFE 146
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
372-573 |
8.36e-04 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 43.38 E-value: 8.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 372 PETTIFDDLCLKIPAGKTVALVGGSGSGKS-TVISLLQRFYDPIAGEILIDG--VSIDKLQvNWLRSQMGLVSQE----- 443
Cdd:PRK13549 273 PHIKRVDDVSFSLRRGEILGIAGLVGAGRTeLVQCLFGAYPGRWEGEIFIDGkpVKIRNPQ-QAIAQGIAMVPEDrkrdg 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 444 --PVLfatSITENILFgkedASLDEVV------EAAKASNAHTFISQfpLGYKTQVGERGV-QMSGGQKQRIAIARAIIK 514
Cdd:PRK13549 352 ivPVM---GVGKNITL----AALDRFTggsridDAAELKTILESIQR--LKVKTASPELAIaRLSGGNQQKAVLAKCLLL 422
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15232977 515 SPKILLLDEATSALD--SESE------RVVQEsldnasiGRTTIVIAHRLSTIRN-ADVICVIHNGQI 573
Cdd:PRK13549 423 NPKILILDEPTRGIDvgAKYEiyklinQLVQQ-------GVAIIVISSELPEVLGlSDRVLVMHEGKL 483
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1137-1223 |
9.61e-04 |
|
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: 43.85 E-value: 9.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1137 SGGQKQRIAIARAVLKNPSVLLLDEATSALDSKSERVVQDALERVM-VGRTSIMIAHRLSTIQN-CDMIVVLGKGKIVES 1214
Cdd:TIGR01257 2072 SGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIrEGRAVVLTSHSMEECEAlCTRLAIMVKGAFQCL 2151
|
....*....
gi 15232977 1215 GTHSSLLEK 1223
Cdd:TIGR01257 2152 GTIQHLKSK 2160
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
496-565 |
9.85e-04 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 41.19 E-value: 9.85e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15232977 496 VQMSGGQKQRIAIA-----RAIIKSPkILLLDEATSALDSESER----VVQESLDNasiGRTTIVIAHRLSTIRNADVI 565
Cdd:cd03227 76 LQLSGGEKELSALAlilalASLKPRP-LYILDEIDRGLDPRDGQalaeAILEHLVK---GAQVIVITHLPELAELADKL 150
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
1135-1167 |
1.02e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 43.31 E-value: 1.02e-03
10 20 30
....*....|....*....|....*....|...
gi 15232977 1135 QLSGGQKQRIAIARAVLKNPSVLLLDEATSALD 1167
Cdd:PLN03073 344 TFSGGWRMRIALARALFIEPDLLLLDEPTNHLD 376
|
|
| ABC_6TM_exporter_like |
cd18540 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
128-306 |
1.35e-03 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349984 [Multi-domain] Cd Length: 295 Bit Score: 42.08 E-value: 1.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 128 YFDlhVTSTSDVITSISSDSLVIQDFLSEKLPNFLMNASAFVASYIVSFILMWRLTIvgfpfIILLLVPGLmygrALVSI 207
Cdd:cd18540 92 YFD--KTPVGWIMARVTSDTQRLGEIISWGLVDLVWGITYMIGILIVMLILNWKLAL-----IVLAVVPVL----AVVSI 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 208 ---------SRKIHEQ-------YNEagsiaeqAISSVRTVYAFGSENKMIGKF---STALRG-SVKLGLRQGLAKGI-- 265
Cdd:cd18540 161 yfqkkilkaYRKVRKInsritgaFNE-------GITGAKTTKTLVREEKNLREFkelTEEMRRaSVRAARLSALFLPIvl 233
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 15232977 266 TIGSNGVthaiwAFLTWYGSRLVMNHGSKGGTVFVVISCIT 306
Cdd:cd18540 234 FLGSIAT-----ALVLWYGGILVLAGAITIGTLVAFISYAT 269
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
497-529 |
1.37e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 42.92 E-value: 1.37e-03
10 20 30
....*....|....*....|....*....|...
gi 15232977 497 QMSGGQKQRIAIARAIIKSPKILLLDEATSALD 529
Cdd:PLN03073 344 TFSGGWRMRIALARALFIEPDLLLLDEPTNHLD 376
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
1011-1208 |
1.42e-03 |
|
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: 40.81 E-value: 1.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1011 VIFENFSIEIDEGKSTAIVGTSGSGKSTIIglierfydplkgtvkidgrdirsyhlrslrkyislvsqEPMLFAGTIREN 1090
Cdd:cd03227 9 SYFVPNDVTFGEGSLTIITGPNGSGKSTIL--------------------------------------DAIGLALGGAQS 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1091 IMYGGTSDKIDEseiIEAAKAAnahDFITSLsngydtncgdkgVQLSGGQKQRIAIARAV----LKNPSVLLLDEATSAL 1166
Cdd:cd03227 51 ATRRRSGVKAGC---IVAAVSA---ELIFTR------------LQLSGGEKELSALALILalasLKPRPLYILDEIDRGL 112
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 15232977 1167 DSKSERVVQDALERVMV-GRTSIMIAHRLSTIQNCDMIVVLGK 1208
Cdd:cd03227 113 DPRDGQALAEAILEHLVkGAQVIVITHLPELAELADKLIHIKK 155
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
1124-1218 |
1.44e-03 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 42.79 E-value: 1.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1124 GYDTNCGdkgvQLSGGQKQRIAIARAVLKNPSVLLLDEATSALD--SKSErVVQDALERVMVGRTSIMIAHRLSTIQN-C 1200
Cdd:PRK10982 384 GHRTQIG----SLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDvgAKFE-IYQLIAELAKKDKGIIIISSEMPELLGiT 458
|
90 100
....*....|....*....|.
gi 15232977 1201 DMIVVLGKGK---IVESGTHS 1218
Cdd:PRK10982 459 DRILVMSNGLvagIVDTKTTT 479
|
|
| ABC_6TM_AarD_CydD |
cd18584 |
Six-transmembrane helical domain (6TM) of the CydD, a component of the ABC cysteine/GSH ... |
672-889 |
1.48e-03 |
|
Six-transmembrane helical domain (6TM) of the CydD, a component of the ABC cysteine/GSH transporter, and a homolog AarD; The CydD protein, together with the CydC protein, constitutes a bacterial heterodimeric ATP-binding cassette (ABC) transporter complex required for formation of the functional cytochrome bd oxidase in both gram-positive and gram-negative aerobic bacteria. In Escherichia coli, the biogenesis of both cytochrome bd-type quinol oxidases and periplasmic cytochromes requires the ABC-type cysteine/GSH transporter CydDC, which exports cysteine and glutathione from the cytoplasm to the periplasm to maintain redox homeostasis. Mutations in AarD, a homolog from Providencia stuartii, also show phenotypic characteristic consistent with a defect in the cytochrome d oxidase. The CydDC forms a heterodimeric ABC transporter with two transmembrane domains (TMDs), each predicted to comprise six TM alpha-helices and two nucleotide binding domains (NBDs).
Pssm-ID: 350028 [Multi-domain] Cd Length: 290 Bit Score: 42.01 E-value: 1.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 672 ALYGCLSAALVgVLQpvsAYSAGSVISVFFLTSHDQikEKTRIYVLLFVGLAIF-SFLVNISQHYGFAyMGEYLTKRIRE 750
Cdd:cd18584 2 VLLGLLAALLI-IAQ---AWLLARIIAGVFLEGAGL--AALLPLLLLLLAALLLrALLAWAQERLAAR-AAARVKAELRR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 751 QMLSKILTFEVNWfdIDDNSSGAICSRLAK--DAnvvrsmVGDRMSL-LVQTISAVIIACIIGLVIA---WRLAIVMISV 824
Cdd:cd18584 75 RLLARLLALGPAL--LRRQSSGELATLLTEgvDA------LDGYFARyLPQLVLAAIVPLLILVAVFpldWVSALILLVT 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15232977 825 QPLIVVcFYtqrVLLKSLSEKASKAQ-DESSKLAA---EAVSNIRTITAFSSQERIIKLLKKVQEGPRR 889
Cdd:cd18584 147 APLIPL-FM---ILIGKAAQAASRRQwAALSRLSGhflDRLRGLPTLKLFGRARAQAARIARASEDYRR 211
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
714-869 |
1.82e-03 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; Uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350055 [Multi-domain] Cd Length: 294 Bit Score: 41.81 E-value: 1.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 714 IYVLLFVGLAIFSFLVNISQHYGFAYMGEYLTKRIREQMLSKILTFEVNWFDidDNSSGAICSRLAkDANVVRSMVGDRM 793
Cdd:cd18782 43 VIGVVMLVAALLEAVLTALRTYLFTDTANRIDLELGGTIIDHLLRLPLGFFD--KRPVGELSTRIS-ELDTIRGFLTGTA 119
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15232977 794 SLLVQTISAVIIACIIGLVIAWRLAIVMISVQPLIV-VCFYTQRVLLKSLSEKASKAQDESSKLaAEAVSNIRTITA 869
Cdd:cd18782 120 LTTLLDVLFSVIYIAVLFSYSPLLTLVVLATVPLQLlLTFLFGPILRRQIRRRAEASAKTQSYL-VESLTGIQTVKA 195
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
498-529 |
1.91e-03 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 42.30 E-value: 1.91e-03
10 20 30
....*....|....*....|....*....|..
gi 15232977 498 MSGGQKQRIAIARAIIKSPKILLLDEATSALD 529
Cdd:PRK10762 396 LSGGNQQKVAIARGLMTRPKVLILDEPTRGVD 427
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
1139-1190 |
2.19e-03 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 42.19 E-value: 2.19e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 15232977 1139 GQKQRIAIARAVLKNPSVLLLDEATSALDSKSERvvqdALERVMVGRTSIMI 1190
Cdd:PRK15064 159 GWKLRVLLAQALFSNPDILLLDEPTNNLDINTIR----WLEDVLNERNSTMI 206
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
497-569 |
2.78e-03 |
|
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: 41.69 E-value: 2.78e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15232977 497 QMSGGQKQRIAIARAIIKSPKILLLDEATSALD----SESERVVQESldnASIGRTTIVIAHRLSTIRN-ADVICVIH 569
Cdd:COG1245 212 ELSGGELQRVAIAAALLRDADFYFFDEPSSYLDiyqrLNVARLIREL---AEEGKYVLVVEHDLAILDYlADYVHILY 286
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1135-1203 |
3.36e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 41.97 E-value: 3.36e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15232977 1135 QLSGGQKQRIAIAR--AVLK-NPSVL-LLDEATSALD-SKSERVVQdaLERVMVGRTS-IMIAHRLSTIQNCDMI 1203
Cdd:TIGR02168 1089 LLSGGEKALTALALlfAIFKvKPAPFcILDEVDAPLDdANVERFAN--LLKEFSKNTQfIVITHNKGTMEVADQL 1161
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
497-565 |
3.79e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 41.50 E-value: 3.79e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15232977 497 QMSGGQKQRIAIA--RAIIK---SPkILLLDEATSALD-SESERVVQ---ESLDNASIgrttIVIAHRLSTIRNADVI 565
Cdd:pfam02463 1077 LLSGGEKTLVALAliFAIQKykpAP-FYLLDEIDAALDdQNVSRVANllkELSKNAQF----IVISLREEMLEKADKL 1149
|
|
| ABC_6TM_YOR1_D2_like |
cd18606 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC ... |
47-249 |
4.19e-03 |
|
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC subfamily; This group includes the six-transmembrane domain 1 (TMD1) of the yeast Yor1p, an oligomycin resistance ABC transporter, and similar proteins. Members of this group belong to the MRP (multidrug resistance-associated protein) subfamily (ABCC). In addition to Yor1p, yeast ABCC (also termed MRP/CFTR) subfamily also comprises five other members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p, and Vmr1p), which are not included in this group. Yor1p is a plasma membrane ATP-binding transporter that mediates export of many different organic anions including oligomycin. While Yor1p has been shown to localize to the plasma membrane, the other 4 members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p and Vmr1p) have been shown to localize to the vacuolar membrane.
Pssm-ID: 350050 [Multi-domain] Cd Length: 290 Bit Score: 40.54 E-value: 4.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 47 FITPVVVFIFNTLLNNLGTSSSNNKTFMqtISKNVVALLYVA--CGSWVICFLEGYCWTRTGERQAARMREKYLRAVLRQ 124
Cdd:cd18606 4 LLLLLILSQFAQVFTNLWLSFWTEDFFG--LSQGFYIGIYAGlgVLQAIFLFLFGLLLAYLGIRASKRLHNKALKRVLRA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 125 DVGYFDlhVTSTSDVITSISSDSLVIQDFLSEKLPNFLMNASAFVASYIVSFILM-WrlTIVGFPFIILLLVPGLMYGRA 203
Cdd:cd18606 82 PMSFFD--TTPLGRILNRFSKDTDVLDNELPDSLRMFLYTLSSIIGTFILIIIYLpW--FAIALPPLLVLYYFIANYYRA 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15232977 204 -------LVSISR-KIHEQYNEagsiaeqAISSVRTVYAFGSENKMIGKFSTAL 249
Cdd:cd18606 158 ssrelkrLESILRsFVYANFSE-------SLSGLSTIRAYGAQDRFIKKNEKLI 204
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
377-559 |
4.26e-03 |
|
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: 41.31 E-value: 4.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 377 FDDLCLKIPAGK-----TVALVGGSGSGKSTVISLLqrfydpiAGEILIDGVSIDKlQVNwlrsqmglVSQEPvlfatsi 451
Cdd:COG1245 351 YGGFSLEVEGGEiregeVLGIVGPNGIGKTTFAKIL-------AGVLKPDEGEVDE-DLK--------ISYKP------- 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 452 teNILFGKEDASLDEVVEAAkasNAHTFISQFplgYKTQVGER-GVQ---------MSGGQKQRIAIARAIIKSPKILLL 521
Cdd:COG1245 408 --QYISPDYDGTVEEFLRSA---NTDDFGSSY---YKTEIIKPlGLEklldknvkdLSGGELQRVAIAACLSRDADLYLL 479
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 15232977 522 DEATSALDSES--------ERVVQESldnasiGRTTIVIAHRLSTI 559
Cdd:COG1245 480 DEPSAHLDVEQrlavakaiRRFAENR------GKTAMVVDHDIYLI 519
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
1005-1212 |
4.78e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 40.93 E-value: 4.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1005 PTRPDVVIFENFSIEIDEGKSTAIVGTSGSGKS----TIIGlieRFYDP-LKGTVKIDGRDIRsyhLRSLRKYIS----- 1074
Cdd:NF040905 268 PLHPERKVVDDVSLNVRRGEIVGIAGLMGAGRTelamSVFG---RSYGRnISGTVFKDGKEVD---VSTVSDAIDaglay 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1075 ---------LVSQEpmlfagTIRENIM---YGGTSDK--IDESEIIEAAKaanahDFITSL---SNGYDTNCGdkgvQLS 1137
Cdd:NF040905 342 vtedrkgygLNLID------DIKRNITlanLGKVSRRgvIDENEEIKVAE-----EYRKKMnikTPSVFQKVG----NLS 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 1138 GGQKQRIAIARAVLKNPSVLLLDEATSALD--SKSE--RVVQDALERvmvGRTSIMIAHRL-STIQNCDMIVVLGKGKIV 1212
Cdd:NF040905 407 GGNQQKVVLSKWLFTDPDVLILDEPTRGIDvgAKYEiyTIINELAAE---GKGVIVISSELpELLGMCDRIYVMNEGRIT 483
|
|
| ABC_6TM_ABCC_D1 |
cd18579 |
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group ... |
716-915 |
6.45e-03 |
|
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group represents the six-transmembrane domain 1 (TMD1)of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The type 3 ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. By contrast, bacterial ABC exporters are typically assembled from dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are comprised of two identical TMDs and two identical NBDs.
Pssm-ID: 350023 [Multi-domain] Cd Length: 289 Bit Score: 40.16 E-value: 6.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 716 VLLFVGLAIFSFLVNISQHYGFaYMGEYLTKRIREQMLS----KILTfeVNWFDIDDNSSGAICSRLAKDANvvrsMVGD 791
Cdd:cd18579 39 YLLALALFLVSLLQSLLLHQYF-FLSFRLGMRVRSALSSliyrKALR--LSSSARQETSTGEIVNLMSVDVQ----RIED 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232977 792 RMSLLVQTISAVIIAcIIGLVIAWRL----AIVMISVqplIVVCFYTQRVL---LKSLSEKASKAQDESSKLAAEAVSNI 864
Cdd:cd18579 112 FFLFLHYLWSAPLQI-IVALYLLYRLlgwaALAGLGV---LLLLIPLQAFLaklISKLRKKLMKATDERVKLTNEILSGI 187
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 15232977 865 RTITAFSSQERIIKLLKKVqegpRRESVHRSWLAGIVLGTSRSLITCTSAL 915
Cdd:cd18579 188 KVIKLYAWEKPFLKRIEEL----RKKELKALRKFGYLRALNSFLFFSTPVL 234
|
|
| AAA_15 |
pfam13175 |
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ... |
1013-1046 |
9.42e-03 |
|
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily.
Pssm-ID: 433011 [Multi-domain] Cd Length: 392 Bit Score: 39.89 E-value: 9.42e-03
10 20 30
....*....|....*....|....*....|....
gi 15232977 1013 FENFSIEIDEGKsTAIVGTSGSGKSTIIGLIERF 1046
Cdd:pfam13175 14 LKDTEIDLDEDL-TVLIGKNNSGKSSILEALDIF 46
|
|
| |
