|
Name |
Accession |
Description |
Interval |
E-value |
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1-495 |
0e+00 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 937.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 1 MKPLLEARQIRKQFSGVAVLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDSGELTIGERAFARLNPALAHQLG 80
Cdd:PRK15439 8 APPLLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQLG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 81 IYLVPQEPMLFPNLSVRENILFRLPKRADTTARLQEKLQQLNCQINLDASASTLEVADQQMVEILRGLMREARILILDEP 160
Cdd:PRK15439 88 IYLVPQEPLLFPNLSVKENILFGLPKRQASMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILILDEP 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 161 TASLTPGETERLFSQIRALQALDVGIVFISHKLPEIRQLASHVSVMRDGAVVLSGETAGYGDQQLISAMTPASRDHALSD 240
Cdd:PRK15439 168 TASLTPAETERLFSRIRELLAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTADLSTDDIIQAITPAAREKSLSA 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 241 TQKLWLALPGNRRTQAQDFPVLRVEDLTGEGFIDLSLEIRAGEIVGLAGLVGSGRTEFAETLYGLRPPRAGRIWLENREI 320
Cdd:PRK15439 248 SQKLWLELPGNRRQQAAGAPVLTVEDLTGEGFRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEI 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 321 SQESTRARLASGLVYLPEDRQVSGLFLDAPVRWNTV--MFNQPSWWQQGKREAAVVERYHRALGIKLADGDQPVRTLSGG 398
Cdd:PRK15439 328 NALSTAQRLARGLVYLPEDRQSSGLYLDAPLAWNVCalTHNRRGFWIKPARENAVLERYRRALNIKFNHAEQAARTLSGG 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 399 NQQKVLLARCLEANPLLLIVDEPTRGVDVSARADIYQLLKSVAAQNVAVLMISSDVEEFVGLADRVLVMHQGRHSGELAR 478
Cdd:PRK15439 408 NQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIAAQNVAVLFISSDLEEIEQMADRVLVMHQGEISGALTG 487
|
490
....*....|....*..
gi 2095916338 479 QAVTVDRMMTLAFGGQA 495
Cdd:PRK15439 488 AAINVDTIMRLAFGEHQ 504
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-495 |
0e+00 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 633.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 1 MKPLLEARQIRKQFSGVAVLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDSGELTIGERAFARLNPALAHQLG 80
Cdd:COG1129 1 AEPLLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDAQAAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 81 IYLVPQEPMLFPNLSVRENILF-RLPKR------ADTTARLQEKLQQLNCQINLDASASTLEVADQQMVEILRGLMREAR 153
Cdd:COG1129 81 IAIIHQELNLVPNLSVAENIFLgREPRRgglidwRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRDAR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 154 ILILDEPTASLTPGETERLFSQIRALQALDVGIVFISHKLPEIRQLASHVSVMRDGAVVLSGETAGYGDQQLISAMTPas 233
Cdd:COG1129 161 VLILDEPTASLTEREVERLFRIIRRLKAQGVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVAELTEDELVRLMVG-- 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 234 rdHALSDTQKlwlalpgnRRTQAQDFPVLRVEDLTGEGFI-DLSLEIRAGEIVGLAGLVGSGRTEFAETLYGLRPPRAGR 312
Cdd:COG1129 239 --RELEDLFP--------KRAAAPGEVVLEVEGLSVGGVVrDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGE 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 313 IWLENREISQESTRARLASGLVYLPEDRQVSGLFLDAPVRWNTVMFNQPSWWQQG----KREAAVVERYHRALGIKLADG 388
Cdd:COG1129 309 IRLDGKPVRIRSPRDAIRAGIAYVPEDRKGEGLVLDLSIRENITLASLDRLSRGGlldrRRERALAEEYIKRLRIKTPSP 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 389 DQPVRTLSGGNQQKVLLARCLEANPLLLIVDEPTRGVDVSARADIYQLLKSVAAQNVAVLMISSDVEEFVGLADRVLVMH 468
Cdd:COG1129 389 EQPVGNLSGGNQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAEGKAVIVISSELPELLGLSDRILVMR 468
|
490 500
....*....|....*....|....*..
gi 2095916338 469 QGRHSGELARQAVTVDRMMTLAFGGQA 495
Cdd:COG1129 469 EGRIVGELDREEATEEAIMAAATGGAA 495
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-488 |
7.51e-168 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 483.37 E-value: 7.51e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 1 MKPLLEARQIRKQFSGVAVLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDSGELTIGERAFARLNPALAHQLG 80
Cdd:COG3845 2 MPPALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRDAIALG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 81 IYLVPQEPMLFPNLSVRENIL-------FRLPKRADTTARLQEKLQQLNCQINLDASASTLEVADQQMVEILRGLMREAR 153
Cdd:COG3845 82 IGMVHQHFMLVPNLTVAENIVlgleptkGGRLDRKAARARIRELSERYGLDVDPDAKVEDLSVGEQQRVEILKALYRGAR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 154 ILILDEPTASLTPGETERLFSQIRALQALDVGIVFISHKLPEIRQLASHVSVMRDGAVVLSGETAGYGDQQLISAMTpaS 233
Cdd:COG3845 162 ILILDEPTAVLTPQEADELFEILRRLAAEGKSIIFITHKLREVMAIADRVTVLRRGKVVGTVDTAETSEEELAELMV--G 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 234 RDhalsdtqklwLALPGNRRTQAQDFPVLRVEDLT------GEGFIDLSLEIRAGEIVGLAGLVGSGRTEFAETLYGLRP 307
Cdd:COG3845 240 RE----------VLLRVEKAPAEPGEVVLEVENLSvrddrgVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRP 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 308 PRAGRIWLENREISQESTRARLASGLVYLPEDRQVSGLFLDAPVRWNTVM--FNQPSWWQQG--KREAA------VVERY 377
Cdd:COG3845 310 PASGSIRLDGEDITGLSPRERRRLGVAYIPEDRLGRGLVPDMSVAENLILgrYRRPPFSRGGflDRKAIrafaeeLIEEF 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 378 hralGIKLADGDQPVRTLSGGNQQKVLLARCLEANPLLLIVDEPTRGVDVSARADIYQLLKSVAAQNVAVLMISSDVEEF 457
Cdd:COG3845 390 ----DVRTPGPDTPARSLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVLLISEDLDEI 465
|
490 500 510
....*....|....*....|....*....|....
gi 2095916338 458 VGLADRVLVMHQGRHSGELARQAVTVDR---MMT 488
Cdd:COG3845 466 LALSDRIAVMYEGRIVGEVPAAEATREEiglLMA 499
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1-490 |
6.84e-130 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 386.19 E-value: 6.84e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 1 MKPLLEARQIRKQFSGVAVLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDSGELTIG--ERAFARLNPALAHq 78
Cdd:PRK11288 1 SSPYLSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDgqEMRFASTTAALAA- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 79 lGIYLVPQEPMLFPNLSVRENI-LFRLP------KRADTTARLQEKLQQLNCQINLDASASTLEVADQQMVEILRGLMRE 151
Cdd:PRK11288 80 -GVAIIYQELHLVPEMTVAENLyLGQLPhkggivNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 152 ARILILDEPTASLTPGETERLFSQIRALQALDVGIVFISHKLPEIRQLASHVSVMRDGAVVLSGET-AGYGDQQLISAMT 230
Cdd:PRK11288 159 ARVIAFDEPTSSLSAREIEQLFRVIRELRAEGRVILYVSHRMEEIFALCDAITVFKDGRYVATFDDmAQVDRDQLVQAMV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 231 paSRDhaLSDtqkLWlalpGNRRTQAQDfPVLRVEDLTGEGFI-DLSLEIRAGEIVGLAGLVGSGRTEFAETLYGLRPPR 309
Cdd:PRK11288 239 --GRE--IGD---IY----GYRPRPLGE-VRLRLDGLKGPGLRePISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRT 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 310 AGRIWLENREISQESTRARLASGLVYLPEDRQVSGLFLDAPVRWNTVM-----FNQPSWWQQGKREAAVVERYHRALGIK 384
Cdd:PRK11288 307 AGQVYLDGKPIDIRSPRDAIRAGIMLCPEDRKAEGIIPVHSVADNINIsarrhHLRAGCLINNRWEAENADRFIRSLNIK 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 385 LADGDQPVRTLSGGNQQKVLLARCLEANPLLLIVDEPTRGVDVSARADIYQLLKSVAAQNVAVLMISSDVEEFVGLADRV 464
Cdd:PRK11288 387 TPSREQLIMNLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYELAAQGVAVLFVSSDLPEVLGVADRI 466
|
490 500
....*....|....*....|....*.
gi 2095916338 465 LVMHQGRHSGELARQAVTVDRMMTLA 490
Cdd:PRK11288 467 VVMREGRIAGELAREQATERQALSLA 492
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-495 |
6.23e-127 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 378.89 E-value: 6.23e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 1 MKPLLEARQIRKQFSGVAVLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVeTPD---SGELTI-GERAFARlNPALA 76
Cdd:PRK13549 2 MEYLLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGV-YPHgtyEGEIIFeGEELQAS-NIRDT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 77 HQLGIYLVPQEPMLFPNLSVRENI-LFRLPKR------ADTTARLQEKLQQLNCQINLDASASTLEVADQQMVEILRGLM 149
Cdd:PRK13549 80 ERAGIAIIHQELALVKELSVLENIfLGNEITPggimdyDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 150 REARILILDEPTASLTPGETERLFSQIRALQALDVGIVFISHKLPEIRQLASHVSVMRDGAVVLSGETAGYGDQQLISAM 229
Cdd:PRK13549 160 KQARLLILDEPTASLTESETAVLLDIIRDLKAHGIACIYISHKLNEVKAISDTICVIRDGRHIGTRPAAGMTEDDIITMM 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 230 TPasrdhalsdtqklwlalpgnrRTQAQDFP---------VLRVEDLTGEGFI--------DLSLEIRAGEIVGLAGLVG 292
Cdd:PRK13549 240 VG---------------------RELTALYPrephtigevILEVRNLTAWDPVnphikrvdDVSFSLRRGEILGIAGLVG 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 293 SGRTEFAETLYGLRPPR-AGRIWLENREISQESTRARLASGLVYLPEDRQVSGLFLDAPVRWNTVMFNQPSWWQQGK--- 368
Cdd:PRK13549 299 AGRTELVQCLFGAYPGRwEGEIFIDGKPVKIRNPQQAIAQGIAMVPEDRKRDGIVPVMGVGKNITLAALDRFTGGSRidd 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 369 -REAAVVERYHRALGIKLADGDQPVRTLSGGNQQKVLLARCLEANPLLLIVDEPTRGVDVSARADIYQLLKSVAAQNVAV 447
Cdd:PRK13549 379 aAELKTILESIQRLKVKTASPELAIARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQGVAI 458
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 2095916338 448 LMISSDVEEFVGLADRVLVMHQGRHSGELARQAVTVDRMMTLAFGGQA 495
Cdd:PRK13549 459 IVISSELPEVLGLSDRVLVMHEGKLKGDLINHNLTQEQVMEAALRSEH 506
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1-494 |
1.62e-124 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 372.80 E-value: 1.62e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 1 MKPLLEARQIRKQFSGVAVLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDSGELT-IG-ERAFArlNPALAHQ 78
Cdd:PRK10762 1 MQALLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILyLGkEVTFN--GPKSSQE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 79 LGIYLVPQEPMLFPNLSVRENI-LFRLPKRA-------DTTARLQEKLQQLNCQINLDASASTLEVADQQMVEILRGLMR 150
Cdd:PRK10762 79 AGIGIIHQELNLIPQLTIAENIfLGREFVNRfgridwkKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 151 EARILILDEPTASLTPGETERLFSQIRALQALDVGIVFISHKLPEIRQLASHVSVMRDGAVVLSGETAGYGDQQLISAMT 230
Cdd:PRK10762 159 ESKVIIMDEPTDALTDTETESLFRVIRELKSQGRGIVYISHRLKEIFEICDDVTVFRDGQFIAEREVADLTEDSLIEMMV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 231 pasrdhalsdTQKLWLALPgnRRTQAQDFPVLRVEDLTGEGFIDLSLEIRAGEIVGLAGLVGSGRTEFAETLYGLRPPRA 310
Cdd:PRK10762 239 ----------GRKLEDQYP--RLDKAPGEVRLKVDNLSGPGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTS 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 311 GRIWLENREISQESTRARLASGLVYLPEDRQVSGLFLDAPVRWNTVM-----FNQPSWWQQGKREAAVVERYHRALGIKL 385
Cdd:PRK10762 307 GYVTLDGHEVVTRSPQDGLANGIVYISEDRKRDGLVLGMSVKENMSLtalryFSRAGGSLKHADEQQAVSDFIRLFNIKT 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 386 ADGDQPVRTLSGGNQQKVLLARCLEANPLLLIVDEPTRGVDVSARADIYQLLKSVAAQNVAVLMISSDVEEFVGLADRVL 465
Cdd:PRK10762 387 PSMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAEGLSIILVSSEMPEVLGMSDRIL 466
|
490 500
....*....|....*....|....*....
gi 2095916338 466 VMHQGRHSGELARQAVTVDRMMTLAFGGQ 494
Cdd:PRK10762 467 VMHEGRISGEFTREQATQEKLMAAAVGKL 495
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-490 |
4.09e-118 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 356.40 E-value: 4.09e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 1 MKPLLEARQIRKQFSGVAVLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDSGELTIGERAFARLNPALAHQLG 80
Cdd:PRK09700 2 ATPYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 81 IYLVPQEPMLFPNLSVRENILF-RLPKR----------ADTTARLQEKLQQLNCQINLDASASTLEVADQQMVEILRGLM 149
Cdd:PRK09700 82 IGIIYQELSVIDELTVLENLYIgRHLTKkvcgvniidwREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 150 REARILILDEPTASLTPGETERLFSQIRALQALDVGIVFISHKLPEIRQLASHVSVMRDGAVVLSGETAGYGDQQLISAM 229
Cdd:PRK09700 162 LDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDVSNDDIVRLM 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 230 TPasrdhalSDTQKLWLALPGNRRTQAQDfPVLRVEDLTGEGF---IDLSLEIRAGEIVGLAGLVGSGRTEFAETLYGLR 306
Cdd:PRK09700 242 VG-------RELQNRFNAMKENVSNLAHE-TVFEVRNVTSRDRkkvRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 307 PPRAGRIWLENREISQESTRARLASGLVYLPEDRQVSGLFLDAPVRWNTVMFNQ--PSWWQ------QGKREAAVVERYH 378
Cdd:PRK09700 314 KRAGGEIRLNGKDISPRSPLDAVKKGMAYITESRRDNGFFPNFSIAQNMAISRSlkDGGYKgamglfHEVDEQRTAENQR 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 379 RALGIKLADGDQPVRTLSGGNQQKVLLARCLEANPLLLIVDEPTRGVDVSARADIYQLLKSVAAQNVAVLMISSDVEEFV 458
Cdd:PRK09700 394 ELLALKCHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEII 473
|
490 500 510
....*....|....*....|....*....|...
gi 2095916338 459 GLADRVLVMHQGRHSGEL-ARQAVTVDRMMTLA 490
Cdd:PRK09700 474 TVCDRIAVFCEGRLTQILtNRDDMSEEEIMAWA 506
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
4-489 |
4.45e-111 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 337.92 E-value: 4.45e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 4 LLEARQIRKQFSGVAVLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDSGELTI----GERAFARLNPAlaHQL 79
Cdd:NF040905 1 ILEMRGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGSYEGEIlfdgEVCRFKDIRDS--EAL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 80 GIYLVPQEPMLFPNLSVRENIL-------FRLPKRADTTARLQEKLQQLNCQINLDASASTLEVADQQMVEILRGLMREA 152
Cdd:NF040905 79 GIVIIHQELALIPYLSIAENIFlgnerakRGVIDWNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 153 RILILDEPTASLTPGETERLFSQIRALQALDVGIVFISHKLPEIRQLASHVSVMRDGAVV--LSGETAGYGDQQLISAMT 230
Cdd:NF040905 159 KLLILDEPTAALNEEDSAALLDLLLELKAQGITSIIISHKLNEIRRVADSITVLRDGRTIetLDCRADEVTEDRIIRGMV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 231 PASRDHALSDtqklwlalpgnrRTQAQDFPVLRVEDLT-------GEGFID-LSLEIRAGEIVGLAGLVGSGRTEFAETL 302
Cdd:NF040905 239 GRDLEDRYPE------------RTPKIGEVVFEVKNWTvyhplhpERKVVDdVSLNVRRGEIVGIAGLMGAGRTELAMSV 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 303 YGlrppRA------GRIWLENREISQESTRARLASGLVYLPEDRQVSGLFLDAPVRWNTVMFNQPS----WWQQGKREAA 372
Cdd:NF040905 307 FG----RSygrnisGTVFKDGKEVDVSTVSDAIDAGLAYVTEDRKGYGLNLIDDIKRNITLANLGKvsrrGVIDENEEIK 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 373 VVERYHRALGIKLADGDQPVRTLSGGNQQKVLLARCLEANPLLLIVDEPTRGVDVSARADIYQLLKSVAAQNVAVLMISS 452
Cdd:NF040905 383 VAEEYRKKMNIKTPSVFQKVGNLSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAEGKGVIVISS 462
|
490 500 510
....*....|....*....|....*....|....*..
gi 2095916338 453 DVEEFVGLADRVLVMHQGRHSGELARQAVTVDRMMTL 489
Cdd:NF040905 463 ELPELLGMCDRIYVMNEGRITGELPREEASQERIMRL 499
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
4-490 |
7.73e-103 |
|
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: 316.77 E-value: 7.73e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 4 LLEARQIRKQFSGVAVLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDS--GELTIGERAFARLNPALAHQLGI 81
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTwdGEIYWSGSPLKASNIRDTERAGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 82 YLVPQEPMLFPNLSVRENILF----RLPKRADTTARLQEKLQQLNCQINLDASASTLEVAD-----QQMVEILRGLMREA 152
Cdd:TIGR02633 81 VIIHQELTLVPELSVAENIFLgneiTLPGGRMAYNAMYLRAKNLLRELQLDADNVTRPVGDygggqQQLVEIAKALNKQA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 153 RILILDEPTASLTPGETERLFSQIRALQALDVGIVFISHKLPEIRQLASHVSVMRDGAVVLSGETAGYGDQQLISAMTpa 232
Cdd:TIGR02633 161 RLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQHVATKDMSTMSEDDIITMMV-- 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 233 SRDHAlsdtqklwlALPGNRRTQAQDfPVLRVEDLTGEGFI--------DLSLEIRAGEIVGLAGLVGSGRTEFAETLYG 304
Cdd:TIGR02633 239 GREIT---------SLYPHEPHEIGD-VILEARNLTCWDVInphrkrvdDVSFSLRRGEILGVAGLVGAGRTELVQALFG 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 305 LRPPR-AGRIWLENREISQESTRARLASGLVYLPEDRQVSGLFLDAPVRWNTVMFNQPSWWQQGKREAA----VVERYHR 379
Cdd:TIGR02633 309 AYPGKfEGNVFINGKPVDIRNPAQAIRAGIAMVPEDRKRHGIVPILGVGKNITLSVLKSFCFKMRIDAAaelqIIGSAIQ 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 380 ALGIKLADGDQPVRTLSGGNQQKVLLARCLEANPLLLIVDEPTRGVDVSARADIYQLLKSVAAQNVAVLMISSDVEEFVG 459
Cdd:TIGR02633 389 RLKVKTASPFLPIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLG 468
|
490 500 510
....*....|....*....|....*....|.
gi 2095916338 460 LADRVLVMHQGRHSGELARQAVTVDRMMTLA 490
Cdd:TIGR02633 469 LSDRVLVIGEGKLKGDFVNHALTQEQVLAAA 499
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
10-490 |
5.36e-91 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 285.86 E-value: 5.36e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 10 IRKQFSGVAVLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDSGELTI--GERAFARLNPALAHqlGIYLVPQE 87
Cdd:PRK10982 4 ISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFqgKEIDFKSSKEALEN--GISMVHQE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 88 PMLFPNLSVRENI-LFRLPKRA----------DTTARLQEklqqLNCQINLDASASTLEVADQQMVEILRGLMREARILI 156
Cdd:PRK10982 82 LNLVLQRSVMDNMwLGRYPTKGmfvdqdkmyrDTKAIFDE----LDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 157 LDEPTASLTPGETERLFSQIRALQALDVGIVFISHKLPEIRQLASHVSVMRDGAVVLSGETAGYGDQQLISAMTPasrdh 236
Cdd:PRK10982 158 MDEPTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQWIATQPLAGLTMDKIIAMMVG----- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 237 alsdtqklwlalpgnrRTQAQDFP---------VLRVEDLTG---EGFIDLSLEIRAGEIVGLAGLVGSGRTEFAETLYG 304
Cdd:PRK10982 233 ----------------RSLTQRFPdkenkpgevILEVRNLTSlrqPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFG 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 305 LRPPRAGRIWLENREISQESTRARLASGLVYLPEDRQVSGLFLDAPVRWNTVMFNQPSWWQQ-----GKREAAVVERYHR 379
Cdd:PRK10982 297 IREKSAGTITLHGKKINNHNANEAINHGFALVTEERRSTGIYAYLDIGFNSLISNIRNYKNKvglldNSRMKSDTQWVID 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 380 ALGIKLADGDQPVRTLSGGNQQKVLLARCLEANPLLLIVDEPTRGVDVSARADIYQLLKSVAAQNVAVLMISSDVEEFVG 459
Cdd:PRK10982 377 SMRVKTPGHRTQIGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLG 456
|
490 500 510
....*....|....*....|....*....|.
gi 2095916338 460 LADRVLVMHQGRHSGELARQAVTVDRMMTLA 490
Cdd:PRK10982 457 ITDRILVMSNGLVAGIVDTKTTTQNEILRLA 487
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
260-471 |
3.77e-79 |
|
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: 244.65 E-value: 3.77e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 260 PVLRVEDLTGEGFI-DLSLEIRAGEIVGLAGLVGSGRTEFAETLYGLRPPRAGRIWLENREISQESTRARLASGLVYLPE 338
Cdd:cd03215 3 PVLEVRGLSVKGAVrDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAGIAYVPE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 339 DRQVSGLFLDAPVRWNTVMfnqpswwqqgkreaavveryhralgikladgdqpVRTLSGGNQQKVLLARCLEANPLLLIV 418
Cdd:cd03215 83 DRKREGLVLDLSVAENIAL----------------------------------SSLLSGGNQQKVVLARWLARDPRVLIL 128
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2095916338 419 DEPTRGVDVSARADIYQLLKSVAAQNVAVLMISSDVEEFVGLADRVLVMHQGR 471
Cdd:cd03215 129 DEPTRGVDVGAKAEIYRLIRELADAGKAVLLISSELDELLGLCDRILVMYEGR 181
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
5-214 |
1.45e-72 |
|
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: 226.93 E-value: 1.45e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 5 LEARQIRKQFSGVAVLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDSGELTIGERAFARLNPALAHQLGIYLV 84
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDARRAGIAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 85 PQepmlfpnlsvrenilfrlpkradttarlqeklqqlncqinldasastLEVADQQMVEILRGLMREARILILDEPTASL 164
Cdd:cd03216 81 YQ-----------------------------------------------LSVGERQMVEIARALARNARLLILDEPTAAL 113
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2095916338 165 TPGETERLFSQIRALQALDVGIVFISHKLPEIRQLASHVSVMRDGAVVLS 214
Cdd:cd03216 114 TPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRVVGT 163
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-471 |
5.68e-65 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 218.62 E-value: 5.68e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 1 MKPLLEARQIRKQFSG--VAVLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPD---SGELTIGERAFARLNPAL 75
Cdd:COG1123 1 MTPLLEVRDLSVRYPGgdVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 76 AHQLgIYLVPQEPM--LFPnLSVRENILF----RLPKRADTTARLQEKLQQLNCQINLDASASTLEVADQQMVEILRGLM 149
Cdd:COG1123 81 RGRR-IGMVFQDPMtqLNP-VTVGDQIAEalenLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 150 REARILILDEPTASLTPGETERLFSQIRALQA-LDVGIVFISHKLPEIRQLASHVSVMRDGAVVLSGETAgygdqQLISA 228
Cdd:COG1123 159 LDPDLLIADEPTTALDVTTQAEILDLLRELQReRGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPE-----EILAA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 229 MTpasrdhALSDTQKLWLALPGNRRTQAQDFPVLRVEDLT-------GEGFI---DLSLEIRAGEIVGLAGLVGSGRTEF 298
Cdd:COG1123 234 PQ------ALAAVPRLGAARGRAAPAAAAAEPLLEVRNLSkrypvrgKGGVRavdDVSLTLRRGETLGLVGESGSGKSTL 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 299 AETLYGLRPPRAGRIWLENREISQESTRARLASGlvylpedRQVSGLF------LDAPVR-WNTVMFnqPSWWQQGKREA 371
Cdd:COG1123 308 ARLLLGLLRPTSGSILFDGKDLTKLSRRSLRELR-------RRVQMVFqdpyssLNPRMTvGDIIAE--PLRLHGLLSRA 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 372 AVVERYHRAL---GIKLADGDQPVRTLSGGNQQKVLLARCLEANPLLLIVDEPTRGVDVSARADIYQLLKSVAAQ-NVAV 447
Cdd:COG1123 379 ERRERVAELLervGLPPDLADRYPHELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRElGLTY 458
|
490 500
....*....|....*....|....*..
gi 2095916338 448 LMISSD---VEEfvgLADRVLVMHQGR 471
Cdd:COG1123 459 LFISHDlavVRY---IADRVAVMYDGR 482
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
5-218 |
6.66e-49 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 167.93 E-value: 6.66e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 5 LEARQIRKQFSGVAVLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDSGELTIGERAFARLNPALAHQLGIylV 84
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRRIGY--V 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 85 PQEPMLFPNLSVRENI-----LFRLPKRaDTTARLQEKLQQLNCQINLDASASTLEVADQQMVEILRGLMREARILILDE 159
Cdd:COG1131 79 PQEPALYPDLTVRENLrffarLYGLPRK-EARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDE 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2095916338 160 PTASLTPGETERLFSQIRALQALDVGIVFISHKLPEIRQLASHVSVMRDGAVVLSGETA 218
Cdd:COG1131 158 PTSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPD 216
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-215 |
1.30e-47 |
|
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: 165.21 E-value: 1.30e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 1 MKPLLEARQIRKQFSGVAVLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDSGELTIGERAFARLNPALAHQLG 80
Cdd:COG0411 1 SDPLLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIARLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 81 I---YlvpQEPMLFPNLSVRENI---------------LFRLPKRADTTARLQEKLQQLNCQINL----DASASTLEVAD 138
Cdd:COG0411 81 IartF---QNPRLFPELTVLENVlvaaharlgrgllaaLLRLPRARREEREARERAEELLERVGLadraDEPAGNLSYGQ 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2095916338 139 QQMVEILRGLMREARILILDEPTASLTPGETERLFSQIRALQA-LDVGIVFISHKLPEIRQLASHVSVMRDGAVVLSG 215
Cdd:COG0411 158 QRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDeRGITILLIEHDMDLVMGLADRIVVLDFGRVIAEG 235
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
4-219 |
3.65e-46 |
|
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: 160.79 E-value: 3.65e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 4 LLEARQIRKQFSGVAVLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDSGELTIGERAFARLNPALAHQLGIyl 83
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQIGV-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 84 VPQEPMLFPNLSVRENILF----RLPKRADTTARLQEKLQQLNCQINLDASASTLEVADQQMVEILRGLMREARILILDE 159
Cdd:COG4555 79 LPDERGLYDRLTVRENIRYfaelYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDE 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 160 PTASLTPGETERLFSQIRALQALDVGIVFISHKLPEIRQLASHVSVMRDGAVVLSGETAG 219
Cdd:COG4555 159 PTNGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDE 218
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
5-215 |
6.93e-46 |
|
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: 159.91 E-value: 6.93e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 5 LEARQIRKQFSGVAVLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDSGELTIGERAFARLNPALAHQLGIYLV 84
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARLGIGRT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 85 PQEPMLFPNLSVRENIL----------FRLPKRADTTARLQEKLQQLNCQINL----DASASTLEVADQQMVEILRGLMR 150
Cdd:cd03219 81 FQIPRLFPELTVLENVMvaaqartgsgLLLARARREEREARERAEELLERVGLadlaDRPAGELSYGQQRRLEIARALAT 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2095916338 151 EARILILDEPTASLTPGETERLFSQIRALQALDVGIVFISHKLPEIRQLASHVSVMRDGAVVLSG 215
Cdd:cd03219 161 DPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEG 225
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
5-215 |
6.46e-44 |
|
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: 153.83 E-value: 6.46e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 5 LEARQIRKQFSGVAVLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDSGELTIGERAFARLNPalaHQLGIYLV 84
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPP---ERRNIGMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 85 PQEPMLFPNLSVRENILF----RLPKRADTTARLQEKLQQLNCQINLDASASTLEVADQQMVEILRGLMREARILILDEP 160
Cdd:cd03259 78 FQDYALFPHLTVAENIAFglklRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2095916338 161 TASLTPGETERLFSQIRALQ-ALDVGIVFISHKLPEIRQLASHVSVMRDGAVVLSG 215
Cdd:cd03259 158 LSALDAKLREELREELKELQrELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
3-218 |
8.06e-43 |
|
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: 151.67 E-value: 8.06e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 3 PLLEARQIRKQFSGVAVLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDSGELTIGERAFARLNPALAHQLGIY 82
Cdd:COG0410 2 PMLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIARLGIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 83 LVPQEPMLFPNLSVRENIL---FRLPKRADTTA----------RLQEKLQQLncqinldasASTL---EvadQQMVEILR 146
Cdd:COG0410 82 YVPEGRRIFPSLTVEENLLlgaYARRDRAEVRAdlervyelfpRLKERRRQR---------AGTLsggE---QQMLAIGR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2095916338 147 GLMREARILILDEPTASLTPGETERLFSQIRALQALDVGIVFISHKLPEIRQLASHVSVMRDGAVVLSGETA 218
Cdd:COG0410 150 ALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNREGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAA 221
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
5-218 |
1.14e-42 |
|
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: 151.05 E-value: 1.14e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 5 LEARQIRKQFSGVAVLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDSGELTIGERAFARLNPALAHQLGIYLV 84
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARAGIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 85 PQEPMLFPNLSVRENIL---FRLPKRADTTA---------RLQEKLQQLncqinldasASTLEVADQQMVEILRGLMREA 152
Cdd:cd03224 81 PEGRRIFPELTVEENLLlgaYARRRAKRKARlervyelfpRLKERRKQL---------AGTLSGGEQQMLAIARALMSRP 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2095916338 153 RILILDEPTASLTPGETERLFSQIRALQALDVGIVFISHKLPEIRQLASHVSVMRDGAVVLSGETA 218
Cdd:cd03224 152 KLLLLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAA 217
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
5-209 |
4.25e-40 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 142.54 E-value: 4.25e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 5 LEARQIRKQFSGVAVLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDSGELTIGERAFARLNPALAHQLGIylV 84
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKRRIGY--L 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 85 PQEPMLFPNLSVRENIlfRLPKRadttarlqeklqqlncqinldasastlevaDQQMVEILRGLMREARILILDEPTASL 164
Cdd:cd03230 79 PEEPSLYENLTVRENL--KLSGG------------------------------MKQRLALAQALLHDPELLILDEPTSGL 126
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2095916338 165 TPGETERLFSQIRALQALDVGIVFISHKLPEIRQLASHVSVMRDG 209
Cdd:cd03230 127 DPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNG 171
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-212 |
4.76e-37 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 135.94 E-value: 4.76e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 1 MKPLLEARQIRKQF----SGVAVLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDSGELTIGERAFARLNPA-L 75
Cdd:COG1136 1 MSPLLELRNLTKSYgtgeGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSEReL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 76 A----HQLGIylVPQEPMLFPNLSVRENILfrLP------KRADTTARLQEKLQQLNCQINLDASASTLEVADQQMVEIL 145
Cdd:COG1136 81 ArlrrRHIGF--VFQFFNLLPELTALENVA--LPlllagvSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2095916338 146 RGLMREARILILDEPTASLTPGETERLFSQIRAL-QALDVGIVFISHKlPEIRQLASHVSVMRDGAVV 212
Cdd:COG1136 157 RALVNRPKLILADEPTGNLDSKTGEEVLELLRELnRELGTTIVMVTHD-PELAARADRVIRLRDGRIV 223
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
5-218 |
6.17e-36 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 136.43 E-value: 6.17e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 5 LEARQIRKQFSGVAVLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDSGELTIGER-AFARLNPalaHQLGIYL 83
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRdLFTNLPP---RERRVGF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 84 VPQEPMLFPNLSVRENILFRLPKRADTTARLQEKLQQLNCQINLDasastlEVAD----------QQMVEILRGLMREAR 153
Cdd:COG1118 80 VFQHYALFPHMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLE------GLADrypsqlsggqRQRVALARALAVEPE 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2095916338 154 ILILDEP----TASLTPgETERLFSQIraLQALDVGIVFISHKLPEIRQLASHVSVMRDGAVVLSGETA 218
Cdd:COG1118 154 VLLLDEPfgalDAKVRK-ELRRWLRRL--HDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPD 219
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
5-305 |
7.88e-36 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 134.85 E-value: 7.88e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 5 LEARQIRKQFSGVAVLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDSGELTI-GErafaRLNPALAHQLGiYL 83
Cdd:COG4152 2 LELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWdGE----PLDPEDRRRIG-YL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 84 vPQEPMLFPNLSVRENILF--RLP--KRADTTARLQEKLQQLNCQINLDASASTLEVADQQMVEILRGLMREARILILDE 159
Cdd:COG4152 77 -PEERGLYPKMKVGEQLVYlaRLKglSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLILDE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 160 PTASLTPGETERLFSQIRALQALDVGIVFISHKLPEIRQLASHVSVMRDGAVVLSGET----AGYGdqqlisamtpasrd 235
Cdd:COG4152 156 PFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVdeirRQFG-------------- 221
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2095916338 236 halsdTQKLWLALPGNRRTQAQDFPVLRVEDLTGEGFIDLSLEIRAGEIvgLAGLVGSGR-TEFAETLYGL 305
Cdd:COG4152 222 -----RNTLRLEADGDAGWLRALPGVTVVEEDGDGAELKLEDGADAQEL--LRALLARGPvREFEEVRPSL 285
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
2-218 |
8.14e-36 |
|
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: 139.27 E-value: 8.14e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 2 KPLLEARQIRKQF-----SGVAVLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDSGELTIGERAFARLNP--- 73
Cdd:COG1123 258 EPLLEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRrsl 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 74 -ALAHQLGIylVPQEP--MLFPNLSVRENI-----LFRLPKRADTTARLQEKLQQLncqiNLDAsastlEVAD------- 138
Cdd:COG1123 338 rELRRRVQM--VFQDPysSLNPRMTVGDIIaeplrLHGLLSRAERRERVAELLERV----GLPP-----DLADryphels 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 139 ---QQMVEILRGLMREARILILDEPTASLTPGETERLFSQIRALQA-LDVGIVFISHKLPEIRQLASHVSVMRDGAVVLS 214
Cdd:COG1123 407 ggqRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQReLGLTYLFISHDLAVVRYIADRVAVMYDGRIVED 486
|
....
gi 2095916338 215 GETA 218
Cdd:COG1123 487 GPTE 490
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
4-218 |
2.04e-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: 132.47 E-value: 2.04e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 4 LLEARQIRKQFSGVAVLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDSGELTIGERAFARLNP-ALAHQLGiy 82
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRrELARRIA-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 83 LVPQEPMLFPNLSVRENIL---------FRLPKRADtTARLQEKLQQLNCQINLDASASTL---EvadQQMVEILRGLMR 150
Cdd:COG1120 79 YVPQEPPAPFGLTVRELVAlgryphlglFGRPSAED-REAVEEALERTGLEHLADRPVDELsggE---RQRVLIARALAQ 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2095916338 151 EARILILDEPTASLTPGETERLFSQIRAL-QALDVGIVFISHKLPEIRQLASHVSVMRDGAVVLSGETA 218
Cdd:COG1120 155 EPPLLLLDEPTSHLDLAHQLEVLELLRRLaRERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPE 223
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
262-471 |
1.92e-34 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 129.03 E-value: 1.92e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 262 LRVEDLT---GEGFI--DLSLEIRAGEIVGLAGLVGSGRTEFAETLYGLRPPRAGRIWLENREISQESTRARLASGlvYL 336
Cdd:COG1131 1 IEVRGLTkryGDKTAldGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRRIG--YV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 337 PEDrqvSGLFLDAPVRWNTVMFnqpsWWQQGKREAAVVERYHRALGI-KLAD-GDQPVRTLSGGNQQKVLLARCLEANPL 414
Cdd:COG1131 79 PQE---PALYPDLTVRENLRFF----ARLYGLPRKEARERIDELLELfGLTDaADRKVGTLSGGMKQRLGLALALLHDPE 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 415 LLIVDEPTRGVDVSARADIYQLLKSVAAQNVAVLMIS---SDVEEfvgLADRVLVMHQGR 471
Cdd:COG1131 152 LLILDEPTSGLDPEARRELWELLRELAAEGKTVLLSThylEEAER---LCDRVAIIDKGR 208
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
20-162 |
2.35e-34 |
|
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: 126.22 E-value: 2.35e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 20 LKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDSGELTIGERAFARLNPALAHQlGIYLVPQEPMLFPNLSVREN 99
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRK-EIGYVFQDPQLFPRLTVREN 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2095916338 100 ILFRL----PKRADTTARLQEKLQQLNcQIN-----LDASASTLEVADQQMVEILRGLMREARILILDEPTA 162
Cdd:pfam00005 80 LRLGLllkgLSKREKDARAEEALEKLG-LGDladrpVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
16-218 |
5.06e-34 |
|
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: 127.83 E-value: 5.06e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 16 GVAVLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDSGELTIGERAFARLNP-ALAHQLGIylVPQEP--MLFp 92
Cdd:COG1122 13 GTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLrELRRKVGL--VFQNPddQLF- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 93 NLSVRENILF-----RLPkRADTTARLQEKLQQLNCQINLDASASTLEVADQQMVEILRGLMREARILILDEPTASLTPG 167
Cdd:COG1122 90 APTVEEDVAFgpenlGLP-REEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPR 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2095916338 168 ETERLFSQIRALQALDVGIVFISHKLPEIRQLASHVSVMRDGAVVLSGETA 218
Cdd:COG1122 169 GRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPR 219
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
5-211 |
6.15e-34 |
|
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: 127.22 E-value: 6.15e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 5 LEARQIRKQFSG----VAVLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDSGELTIGERAFARLNPA-----L 75
Cdd:cd03255 1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKelaafR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 76 AHQLGIylVPQEPMLFPNLSVRENILfrLP------KRADTTARLQEKLQQLNCQINLDASASTLEVADQQMVEILRGLM 149
Cdd:cd03255 81 RRHIGF--VFQSFNLLPDLTALENVE--LPlllagvPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2095916338 150 REARILILDEPTASLTPGETERLFSQIRALQALD-VGIVFISHKlPEIRQLASHVSVMRDGAV 211
Cdd:cd03255 157 NDPKIILADEPTGNLDSETGKEVMELLRELNKEAgTTIVVVTHD-PELAEYADRIIELRDGKI 218
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
6-209 |
1.62e-33 |
|
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: 126.04 E-value: 1.62e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 6 EARQIRKQFSG--VAVLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDSGELTIGERAFARLNPALAHQLgIYL 83
Cdd:cd03225 1 ELKNLSFSYPDgaRPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRK-VGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 84 VPQEP--MLFpNLSVRENILFRLP----KRADTTARLQEKLQQLNCQINLDASASTLEVADQQMVEILRGLMREARILIL 157
Cdd:cd03225 80 VFQNPddQFF-GPTVEEEVAFGLEnlglPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2095916338 158 DEPTASLTPGETERLFSQIRALQALDVGIVFISHKLPEIRQLASHVSVMRDG 209
Cdd:cd03225 159 DEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDG 210
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
5-215 |
1.79e-33 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 125.79 E-value: 1.79e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 5 LEARQIRKQFSGVAVLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDSGELTIGERAFARLNPALAHqLGIYLv 84
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALRR-IGALI- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 85 pQEPMLFPNLSVRENI-----LFRLPKRadttaRLQEKLQQLNCQINLDASASTLEVADQQMVEILRGLMREARILILDE 159
Cdd:cd03268 79 -EAPGFYPNLTARENLrllarLLGIRKK-----RIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDE 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2095916338 160 PTASLTPGETERLFSQIRALQALDVGIVFISHKLPEIRQLASHVSVMRDGAVVLSG 215
Cdd:cd03268 153 PTNGLDPDGIKELRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
260-472 |
1.81e-33 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 126.74 E-value: 1.81e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 260 PVLRVEDLT---GEGFI--DLSLEIRAGEIVGLAGLVGSGRTEFAETLYGLRPPRAGRIWLENREISQEstRARLAsglv 334
Cdd:COG1121 5 PAIELENLTvsyGGRPVleDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRA--RRRIG---- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 335 YLPEDRQVSGLFldaPVR-WNTVM---FNQPSWWQQ-GKREAAVVERYHRALGI-KLADgdQPVRTLSGGNQQKVLLARC 408
Cdd:COG1121 79 YVPQRAEVDWDF---PITvRDVVLmgrYGRRGLFRRpSRADREAVDEALERVGLeDLAD--RPIGELSGGQQQRVLLARA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2095916338 409 LEANPLLLIVDEPTRGVDVSARADIYQLLKSVAAQNVAVLMISSDVEEFVGLADRVLVMHQGRH 472
Cdd:COG1121 154 LAQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLLNRGLV 217
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
15-209 |
3.37e-33 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 123.65 E-value: 3.37e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 15 SGVAVLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDSGELTIGERAFARLNPALAHQLgIYLVPQEPMLFpNL 94
Cdd:cd03228 13 RPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKN-IAYVPQDPFLF-SG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 95 SVRENILfrlpkradttarlqeklqqlncqinldasaSTLEvadQQMVEILRGLMREARILILDEPTASLTPgETERLFs 174
Cdd:cd03228 91 TIRENIL------------------------------SGGQ---RQRIAIARALLRDPPILILDEATSALDP-ETEALI- 135
|
170 180 190
....*....|....*....|....*....|....*..
gi 2095916338 175 qIRALQALDVG--IVFISHKLPEIRQlASHVSVMRDG 209
Cdd:cd03228 136 -LEALRALAKGktVIVIAHRLSTIRD-ADRIIVLDDG 170
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-212 |
1.16e-32 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 127.52 E-value: 1.16e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 1 MKPLLEARQIRKQFSGVAVLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDSGELTIGERAFARLNPalaHQLG 80
Cdd:COG3842 2 AMPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPP---EKRN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 81 IYLVPQEPMLFPNLSVRENILF----RLPKRADTTARLQEKLQQLncqiNLDASASTLeVAD-----QQMVEILRGLMRE 151
Cdd:COG3842 79 VGMVFQDYALFPHLTVAENVAFglrmRGVPKAEIRARVAELLELV----GLEGLADRY-PHQlsggqQQRVALARALAPE 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2095916338 152 ARILILDEPTASLTPGETERLFSQIRALQAlDVGI--VFISHKLPEIRQLASHVSVMRDGAVV 212
Cdd:COG3842 154 PRVLLLDEPLSALDAKLREEMREELRRLQR-ELGItfIYVTHDQEEALALADRIAVMNDGRIE 215
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
5-209 |
1.30e-32 |
|
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: 122.30 E-value: 1.30e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 5 LEARQIRKQFSGVAVLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDSGELTIGERAFARLNPAL-AHQLGIYL 83
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELpPLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 84 VPQEPMLFPNLSVRENILFRLpkradttarlqeklqqlncqinldaSAstlevADQQMVEILRGLMREARILILDEPTAS 163
Cdd:cd03229 81 VFQDFALFPHLTVLENIALGL-------------------------SG-----GQQQRVALARALAMDPDVLLLDEPTSA 130
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2095916338 164 LTPGETERLFSQIRALQA-LDVGIVFISHKLPEIRQLASHVSVMRDG 209
Cdd:cd03229 131 LDPITRREVRALLKSLQAqLGITVVLVTHDLDEAARLADRVVVLRDG 177
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
3-191 |
1.78e-32 |
|
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: 122.97 E-value: 1.78e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 3 PLLEARQIRKQFSGVAVLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDSGELTIGERAFARLNPALAHQLGIy 82
Cdd:COG4133 1 MMLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRRLAY- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 83 lVPQEPMLFPNLSVRENILF--RLPKRADTTARLQEKLQQLNCQINLDASASTLEVADQQMVEILRGLMREARILILDEP 160
Cdd:COG4133 80 -LGHADGLKPELTVRENLRFwaALYGLRADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEP 158
|
170 180 190
....*....|....*....|....*....|.
gi 2095916338 161 TASLTPGETERLFSQIRALQALDVGIVFISH 191
Cdd:COG4133 159 FTALDAAGVALLAELIAAHLARGGAVLLTTH 189
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-471 |
1.97e-32 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 129.80 E-value: 1.97e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 1 MKPLLEARQIRKQFSG----VAVLKGIDFTLCAGQVHALMGGNGAGKS----TLMKIIAGVETPDSGELTIGERAFARLN 72
Cdd:COG4172 3 SMPLLSVEDLSVAFGQgggtVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 73 PALAHQL---GIYLVPQEPM--LFPNLSVRENI--LFRLPKRADTTARLQEKLQQLNcQINLDASASTLEV-------AD 138
Cdd:COG4172 83 ERELRRIrgnRIAMIFQEPMtsLNPLHTIGKQIaeVLRLHRGLSGAAARARALELLE-RVGIPDPERRLDAyphqlsgGQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 139 QQMVEILRGLMREARILILDEPTASL--TpgeterLFSQI----RALQA-LDVGIVFISHKLPEIRQLASHVSVMRDGAV 211
Cdd:COG4172 162 RQRVMIAMALANEPDLLIADEPTTALdvT------VQAQIldllKDLQReLGMALLLITHDLGVVRRFADRVAVMRQGEI 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 212 VLSGETAgygdqQLISAMTpasrdHALsdTQKLWLALPGN--RRTQAQDFPVLRVEDL-----TGEGFI----------- 273
Cdd:COG4172 236 VEQGPTA-----ELFAAPQ-----HPY--TRKLLAAEPRGdpRPVPPDAPPLLEARDLkvwfpIKRGLFrrtvghvkavd 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 274 DLSLEIRAGEIVGLAGLVGSGRTEFAETLYGLRPPRaGRIWLENREISQESTRARLAsglvyLPEDRQVsgLFLD----- 348
Cdd:COG4172 304 GVSLTLRRGETLGLVGESGSGKSTLGLALLRLIPSE-GEIRFDGQDLDGLSRRALRP-----LRRRMQV--VFQDpfgsl 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 349 APvRWnTVM--------FNQPSwWQQGKREAAVVEryhrAL---GIKLADGDQPVRTLSGGNQQKVLLARCLEANPLLLI 417
Cdd:COG4172 376 SP-RM-TVGqiiaeglrVHGPG-LSAAERRARVAE----ALeevGLDPAARHRYPHEFSGGQRQRIAIARALILEPKLLV 448
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 2095916338 418 VDEPTRGVDVSARADIYQLLKSV-AAQNVAVLMISSD---VEEfvgLADRVLVMHQGR 471
Cdd:COG4172 449 LDEPTSALDVSVQAQILDLLRDLqREHGLAYLFISHDlavVRA---LAHRVMVMKDGK 503
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-218 |
2.16e-32 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 124.05 E-value: 2.16e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 1 MKPLLEARQIRKQFSGVAVLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDSGELTIGERAFARLNPALAhqlg 80
Cdd:COG1121 3 MMPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARRRIG---- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 81 iYlVPQEPML---FPnLSVRENI---------LFRLPKRADtTARLQEKLQQLNCQinldasastlEVADQQM------- 141
Cdd:COG1121 79 -Y-VPQRAEVdwdFP-ITVRDVVlmgrygrrgLFRRPSRAD-REAVDEALERVGLE----------DLADRPIgelsggq 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 142 ---VEILRGLMREARILILDEPTASLTPGETERLFSQIRALQALDVGIVFISHKLPEIRQLASHVSVMRDGaVVLSGETA 218
Cdd:COG1121 145 qqrVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLLNRG-LVAHGPPE 223
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-215 |
2.51e-32 |
|
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: 123.55 E-value: 2.51e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 1 MKPLLEARQIRKQFSGVAVLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDSGELTIGERAFARLNP----ALA 76
Cdd:COG1127 2 SEPMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEkelyELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 77 HQLGIylVPQEPMLFPNLSVRENILF------RLPkRADTTARLQEKLQQLNcqinldasastLEVADQQM--------- 141
Cdd:COG1127 82 RRIGM--LFQGGALFDSLTVFENVAFplrehtDLS-EAEIRELVLEKLELVG-----------LPGAADKMpselsggmr 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2095916338 142 --VEILRGLMREARILILDEPTASLTPGETERLFSQIRALQ-ALDVGIVFISHKLPEIRQLASHVSVMRDGAVVLSG 215
Cdd:COG1127 148 krVALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRdELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEG 224
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
2-211 |
1.72e-31 |
|
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: 119.46 E-value: 1.72e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 2 KPLLEARQIrkqfSGVAVLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDSGELTIGERAFARLNPALAHQLGI 81
Cdd:cd03215 2 EPVLEVRGL----SVKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 82 YLVPQEPM---LFPNLSVRENILFRlpkradttarlqeklQQL---NcqinldasastlevadQQMVEILRGLMREARIL 155
Cdd:cd03215 78 AYVPEDRKregLVLDLSVAENIALS---------------SLLsggN----------------QQKVVLARWLARDPRVL 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2095916338 156 ILDEPTASLTPGETERLFSQIRALQALDVGIVFISHKLPEIRQLASHVSVMRDGAV 211
Cdd:cd03215 127 ILDEPTRGVDVGAKAEIYRLIRELADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
5-212 |
2.63e-31 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 123.64 E-value: 2.63e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 5 LEARQIRKQFSGVAVLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDSGELTIGERAFARLNPAlahQLGIYLV 84
Cdd:COG3839 4 LELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPK---DRNIAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 85 PQEPMLFPNLSVRENILF-----RLPKrADTTARLQE-----KLQQLncqinLDASASTLEVADQQMVEILRGLMREARI 154
Cdd:COG3839 81 FQSYALYPHMTVYENIAFplklrKVPK-AEIDRRVREaaellGLEDL-----LDRKPKQLSGGQRQRVALGRALVREPKV 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2095916338 155 LILDEPTASLTPGETERLFSQIRALQA-LDVGIVFISHKLPEIRQLASHVSVMRDGAVV 212
Cdd:COG3839 155 FLLDEPLSNLDAKLRVEMRAEIKRLHRrLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQ 213
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
4-212 |
3.78e-31 |
|
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: 119.92 E-value: 3.78e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 4 LLEARQIRKQFSG----VAVLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDSGELTIGERAFARLNPALAHQL 79
Cdd:cd03257 1 LLEVKNLSVSFPTgggsVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 80 G--IYLVPQEPM--LFPNLSVRENIL--FRLPKRADTTARLQEKLQQLNCQINLDAsastlEVAD----------QQMVE 143
Cdd:cd03257 81 RkeIQMVFQDPMssLNPRMTIGEQIAepLRIHGKLSKKEARKEAVLLLLVGVGLPE-----EVLNryphelsggqRQRVA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2095916338 144 ILRGLMREARILILDEPTASL---TPGETERLFSQIRalQALDVGIVFISHKLPEIRQLASHVSVMRDGAVV 212
Cdd:cd03257 156 IARALALNPKLLIADEPTSALdvsVQAQILDLLKKLQ--EELGLTLLFITHDLGVVAKIADRVAVMYAGKIV 225
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
261-471 |
3.86e-31 |
|
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: 120.53 E-value: 3.86e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 261 VLRVEDLT---GEGFI--DLSLEIRAGEIVGLAGLVGSGRTEFAETLYGLRPPRAGRIWLENREISQESTRARlASGLVY 335
Cdd:COG1120 1 MLEAENLSvgyGGRPVldDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRREL-ARRIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 336 LPEDRQVSGLFldaPVRwNTVMF----NQPSWWQQGKREAAVVERYHRALGI-KLADgdQPVRTLSGGNQQKVLLARCLE 410
Cdd:COG1120 80 VPQEPPAPFGL---TVR-ELVALgrypHLGLFGRPSAEDREAVEEALERTGLeHLAD--RPVDELSGGERQRVLIARALA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2095916338 411 ANPLLLIVDEPTRGVDVSARADIYQLLKSVAA-QNVAVLMISSDVEEFVGLADRVLVMHQGR 471
Cdd:COG1120 154 QEPPLLLLDEPTSHLDLAHQLEVLELLRRLAReRGRTVVMVLHDLNLAARYADRLVLLKDGR 215
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
5-215 |
4.98e-31 |
|
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: 119.96 E-value: 4.98e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 5 LEARQIRKQFSGVAVLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDSGELTIGERAFARLNPALAHQLGIYLV 84
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRARLGIGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 85 PQEPMLFPNLSVRENILFRLPKRADTTARLQEKLQQL----NCQINLDASASTLEVADQQMVEILRGLMREARILILDEP 160
Cdd:cd03218 81 PQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELleefHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2095916338 161 TASLTP---GETERLfsqIRALQALDVGIVFISHKLPEIRQLASHVSVMRDGAVVLSG 215
Cdd:cd03218 161 FAGVDPiavQDIQKI---IKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEG 215
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
5-215 |
7.98e-31 |
|
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: 118.54 E-value: 7.98e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 5 LEARQIRKQFSGVAVLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDSGELTIGERAFArlnPALAHQLGiYLv 84
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLD---IAARNRIG-YL- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 85 PQEPMLFPNLSVRENILF--RLP--KRADTTARLQEKLQQLNCQINLDASASTLEVADQQMVEILRGLMREARILILDEP 160
Cdd:cd03269 76 PEERGLYPKMKVIDQLVYlaQLKglKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEP 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2095916338 161 TASLTPGETERLFSQIRALQALDVGIVFISHKLPEIRQLASHVSVMRDGAVVLSG 215
Cdd:cd03269 156 FSGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
6-209 |
1.22e-30 |
|
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: 116.19 E-value: 1.22e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 6 EARQIRKQFSGVAVLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDSGELTIGERAFARLNPALAHQlGIYLVP 85
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRR-RIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 86 QepmlfpnLSVREnilfrlpkradttarlqeklqqlncqinldasastlevadQQMVEILRGLMREARILILDEPTASLT 165
Cdd:cd00267 80 Q-------LSGGQ----------------------------------------RQRVALARALLLNPDLLLLDEPTSGLD 112
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2095916338 166 PGETERLFSQIRALQALDVGIVFISHKLPEIRQLASHVSVMRDG 209
Cdd:cd00267 113 PASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDG 156
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
262-474 |
1.25e-30 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 118.31 E-value: 1.25e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 262 LRVEDL-TGEGFI----DLSLEIRAGEIVGLAGLVGSGRTEFAETLYGLRPPRAGRIWLENREISQESTRARLASGLVYL 336
Cdd:cd03224 1 LEVENLnAGYGKSqilfGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARAGIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 337 PEDRQVsglFLDAPVRWNTVMfnqpswWQQGKREAAVVERYHRALGI--KLAD-GDQPVRTLSGGNQQKVLLARCLEANP 413
Cdd:cd03224 81 PEGRRI---FPELTVEENLLL------GAYARRRAKRKARLERVYELfpRLKErRKQLAGTLSGGEQQMLAIARALMSRP 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2095916338 414 LLLIVDEPTRGVDVSARADIYQLLKSVAAQNVAVLMISSDVEEFVGLADRVLVMHQGR--HSG 474
Cdd:cd03224 152 KLLLLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRvvLEG 214
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
5-216 |
1.38e-30 |
|
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: 118.59 E-value: 1.38e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 5 LEARQIRKQFsGVAVLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDSGELTIGERAFARLNPalaHQLGIYLV 84
Cdd:cd03299 1 LKVENLSKDW-KEFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPP---EKRDISYV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 85 PQEPMLFPNLSVRENILFRLPKRADTTARLQEKLQQLNCQIN----LDASASTLEVADQQMVEILRGLMREARILILDEP 160
Cdd:cd03299 77 PQNYALFPHMTVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGidhlLNRKPETLSGGEQQRVAIARALVVNPKILLLDEP 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2095916338 161 TASLTPGETERLFSQIRALQ-ALDVGIVFISHKLPEIRQLASHVSVMRDGAVVLSGE 216
Cdd:cd03299 157 FSALDVRTKEKLREELKKIRkEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGK 213
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
262-471 |
1.40e-30 |
|
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: 116.73 E-value: 1.40e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 262 LRVEDLT---GEGFI--DLSLEIRAGEIVGLAGLVGSGRTEFAETLYGLRPPRAGRIWLENREISQESTRARLASGlvYL 336
Cdd:cd03230 1 IEVRNLSkryGKKTAldDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKRRIG--YL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 337 PEDrqvSGLFLDApvrwnTVMFNqpswwqqgkreaavveryhralgIKLadgdqpvrtlSGGNQQKVLLARCLEANPLLL 416
Cdd:cd03230 79 PEE---PSLYENL-----TVREN-----------------------LKL----------SGGMKQRLALAQALLHDPELL 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2095916338 417 IVDEPTRGVDVSARADIYQLLKSVAAQNVAVLMISSDVEEFVGLADRVLVMHQGR 471
Cdd:cd03230 118 ILDEPTSGLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGR 172
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
15-215 |
1.92e-30 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 125.33 E-value: 1.92e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 15 SGVAVLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDSGELTIGERAFARLNPA-LAHQLGiyLVPQEPMLFpN 93
Cdd:COG2274 486 DSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPAsLRRQIG--VVLQDVFLF-S 562
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 94 LSVRENILFRLPKRADttARLQEKLQQLncqiNLDASASTL------EVADQ---------QMVEILRGLMREARILILD 158
Cdd:COG2274 563 GTIRENITLGDPDATD--EEIIEAARLA----GLHDFIEALpmgydtVVGEGgsnlsggqrQRLAIARALLRNPRILILD 636
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2095916338 159 EPTASLTPgETERLFsqIRALQALDVG--IVFISHKLPEIRqLASHVSVMRDGAVVLSG 215
Cdd:COG2274 637 EATSALDA-ETEAII--LENLRRLLKGrtVIIIAHRLSTIR-LADRIIVLDKGRIVEDG 691
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
9-215 |
2.24e-30 |
|
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: 117.40 E-value: 2.24e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 9 QIRKQFSGVAvLKgIDFTlCAGQVHALMGGNGAGKSTLMKIIAGVETPDSGELTIGERAF--ARLNPALA-HQLGIYLVP 85
Cdd:cd03297 5 DIEKRLPDFT-LK-IDFD-LNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLfdSRKKINLPpQQRKIGLVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 86 QEPMLFPNLSVRENILFRLPKRADTTARLQ--EKLQQLNCQINLDASASTLEVADQQMVEILRGLMREARILILDEPTAS 163
Cdd:cd03297 82 QQYALFPHLNVRENLAFGLKRKRNREDRISvdELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2095916338 164 LTPGETERLFSQIRALQA-LDVGIVFISHKLPEIRQLASHVSVMRDGAVVLSG 215
Cdd:cd03297 162 LDRALRLQLLPELKQIKKnLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
260-477 |
3.38e-30 |
|
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: 117.39 E-value: 3.38e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 260 PVLRVEDLT---GEGFI--DLSLEIRAGEIVGLAGLVGSGRTEFAETLYGLRPPRAGRIWLENREISQESTRARLASGLV 334
Cdd:COG0410 2 PMLEVENLHagyGGIHVlhGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIARLGIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 335 YLPEDRQVsglFLDAPVRWNTVM--FNQPSWWQQGKREAAVVERYHRalgikLAD-GDQPVRTLSGGNQQKVLLARCLEA 411
Cdd:COG0410 82 YVPEGRRI---FPSLTVEENLLLgaYARRDRAEVRADLERVYELFPR-----LKErRRQRAGTLSGGEQQMLAIGRALMS 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2095916338 412 NPLLLIVDEPTRGVDVSARADIYQLLKSVAAQNVAVLMISSDVEEFVGLADRVLVMHQGR--HSGELA 477
Cdd:COG0410 154 RPKLLLLDEPSLGLAPLIVEEIFEIIRRLNREGVTILLVEQNARFALEIADRAYVLERGRivLEGTAA 221
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
5-215 |
3.62e-30 |
|
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: 117.60 E-value: 3.62e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 5 LEARQIRKQFSGVAVLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDSGELTIGERAFARLNPA----LAHQLG 80
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAelyrLRRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 81 IylVPQEPMLFPNLSVRENILF------RLPKRaDTTARLQEKLQQLNcqinldasastLEVADQQM-----------VE 143
Cdd:cd03261 81 M--LFQSGALFDSLTVFENVAFplrehtRLSEE-EIREIVLEKLEAVG-----------LRGAEDLYpaelsggmkkrVA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2095916338 144 ILRGLMREARILILDEPTASLTP---GETERLfsqIRALQ-ALDVGIVFISHKLPEIRQLASHVSVMRDGAVVLSG 215
Cdd:cd03261 147 LARALALDPELLLYDEPTAGLDPiasGVIDDL---IRSLKkELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEG 219
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
262-471 |
4.94e-30 |
|
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: 117.15 E-value: 4.94e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 262 LRVEDLT---GeGFI---DLSLEIRAGEIVGLAGLVGSGRTEFAETLYGLRPPRAGRIWLENREISQESTRARLASGLVy 335
Cdd:cd03219 1 LEVRGLTkrfG-GLValdDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARLGIG- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 336 lpedR--QVSGLFLDAPVRWNtVM-------FNQPSWWQQGKREAAVVERYHRALG-IKLAD-GDQPVRTLSGGNQQKVL 404
Cdd:cd03219 79 ----RtfQIPRLFPELTVLEN-VMvaaqartGSGLLLARARREEREARERAEELLErVGLADlADRPAGELSYGQQRRLE 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2095916338 405 LARCLEANPLLLIVDEPTRGVDVSARADIYQLLKSVAAQNVAVLMISSDVEeFV-GLADRVLVMHQGR 471
Cdd:cd03219 154 IARALATDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMD-VVmSLADRVTVLDQGR 220
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
4-215 |
5.54e-30 |
|
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: 116.70 E-value: 5.54e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 4 LLEARQIRKQFS----GVAVLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDSGELTIGERAFARlNPALAhQL 79
Cdd:cd03266 1 MITADALTKRFRdvkkTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVK-EPAEA-RR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 80 GIYLVPQEPMLFPNLSVRENILF--RLP--KRADTTARLQEKLQQLNCQINLDASASTLEVADQQMVEILRGLMREARIL 155
Cdd:cd03266 79 RLGFVSDSTGLYDRLTARENLEYfaGLYglKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 156 ILDEPTASLTPGETERLFSQIRALQALDVGIVFISHKLPEIRQLASHVSVMRDGAVVLSG 215
Cdd:cd03266 159 LLDEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
274-467 |
1.22e-29 |
|
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: 115.32 E-value: 1.22e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 274 DLSLEIRAGEIVGLAGLVGSGRTEFAETLYGLRPPRAGRIWLENREISQEstRARLAsglvYLPEDRQVSglfLDAPVR- 352
Cdd:cd03235 17 DVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKE--RKRIG----YVPQRRSID---RDFPISv 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 353 WNTVM---FNQPSWWQ-QGKREAAVVERYHRALGI-KLADgdQPVRTLSGGNQQKVLLARCLEANPLLLIVDEPTRGVDV 427
Cdd:cd03235 88 RDVVLmglYGHKGLFRrLSKADKAKVDEALERVGLsELAD--RQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDP 165
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2095916338 428 SARADIYQLLKSVAAQNVAVLMISSDVEEFVGLADRVLVM 467
Cdd:cd03235 166 KTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRVLLL 205
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
5-215 |
3.99e-29 |
|
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: 114.64 E-value: 3.99e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 5 LEARQIRKQFSGVAVLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDSGELTIGERAFARLNPalaHQLGIYLV 84
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPP---HKRPVNTV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 85 PQEPMLFPNLSVRENILFRLP----KRADTTARLQEKLQQLNCQINLDASASTLEVADQQMVEILRGLMREARILILDEP 160
Cdd:cd03300 78 FQNYALFPHLTVFENIAFGLRlkklPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2095916338 161 TASLTPGETERLFSQIRALQAlDVGI--VFISHKLPEIRQLASHVSVMRDGAVVLSG 215
Cdd:cd03300 158 LGALDLKLRKDMQLELKRLQK-ELGItfVFVTHDQEEALTMSDRIAVMNKGKIQQIG 213
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
4-217 |
6.59e-29 |
|
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: 113.83 E-value: 6.59e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 4 LLEARQIRKQFSG----VAVLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDSGELTIGERAFARLNPA----L 75
Cdd:cd03258 1 MIELKNVSKVFGDtggkVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKelrkA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 76 AHQLGiyLVPQEPMLFPNLSVRENILFRLP----KRADTTARLQEKLQQLNCQINLDASASTLEVADQQMVEILRGLMRE 151
Cdd:cd03258 81 RRRIG--MIFQHFNLLSSRTVFENVALPLEiagvPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANN 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2095916338 152 ARILILDEPTASLTPGETE---RLFSQIRalQALDVGIVFISHKLPEIRQLASHVSVMRDGAVVLSGET 217
Cdd:cd03258 159 PKVLLCDEATSALDPETTQsilALLRDIN--RELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTV 225
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
274-471 |
8.05e-29 |
|
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: 113.58 E-value: 8.05e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 274 DLSLEIRAGEIVGLAGLVGSGRTEFAETLYGLRPPRAGRIWLENREISQESTRA-RLASGLV--YlPEDrQvsgLFldAP 350
Cdd:COG1122 19 DVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRElRRKVGLVfqN-PDD-Q---LF--AP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 351 VRWNTVMF---NQpswwqqGKREAAVVERYHRAL---GI-KLADgdQPVRTLSGGNQQKVLLARCLEANPLLLIVDEPTR 423
Cdd:COG1122 92 TVEEDVAFgpeNL------GLPREEIRERVEEALelvGLeHLAD--RPPHELSGGQKQRVAIAGVLAMEPEVLVLDEPTA 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2095916338 424 GVDVSARADIYQLLKSVAAQNVAVLMISSDVEEFVGLADRVLVMHQGR 471
Cdd:COG1122 164 GLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGR 211
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
261-471 |
8.14e-29 |
|
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: 113.37 E-value: 8.14e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 261 VLRVEDL-----TGEGFI----DLSLEIRAGEIVGLAGLVGSGRTEFAETLYGLRPPRAGRIWLENREISQESTRARLAS 331
Cdd:cd03257 1 LLEVKNLsvsfpTGGGSVkaldDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 332 GlvylpedRQVSGLFLDAPVRWNTVM-----FNQPSW-WQQGKREAAVVERYHRAL-GIKLADG--DQPVRTLSGGNQQK 402
Cdd:cd03257 81 R-------KEIQMVFQDPMSSLNPRMtigeqIAEPLRiHGKLSKKEARKEAVLLLLvGVGLPEEvlNRYPHELSGGQRQR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 403 VLLARCLEANPLLLIVDEPTRGVDVSARADIYQLLKSVAAQ-NVAVLMISSDVEEFVGLADRVLVMHQGR 471
Cdd:cd03257 154 VAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEElGLTLLFITHDLGVVAKIADRVAVMYAGK 223
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
16-215 |
1.08e-28 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 119.48 E-value: 1.08e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 16 GVAVLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDSGELTIGERAFARLNPA-LAHQLGiyLVPQEPMLFPnL 94
Cdd:COG4988 349 GRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPAsWRRQIA--WVPQNPYLFA-G 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 95 SVRENILFRLP-------KRADTTARLQEKLQQLNCQIN--LDASASTLEVADQQMVEILRGLMREARILILDEPTASLT 165
Cdd:COG4988 426 TIRENLRLGRPdasdeelEAALEAAGLDEFVAALPDGLDtpLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLD 505
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2095916338 166 PgETERLFsqIRALQAL--DVGIVFISHKLPEIRQlASHVSVMRDGAVVLSG 215
Cdd:COG4988 506 A-ETEAEI--LQALRRLakGRTVILITHRLALLAQ-ADRILVLDDGRIVEQG 553
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
5-212 |
1.14e-28 |
|
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: 112.95 E-value: 1.14e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 5 LEARQIRKQFSG----VAVLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDSGELTIGERAFARLNPALAhqlg 80
Cdd:cd03293 1 LEVRNVSKTYGGgggaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPDRG---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 81 iyLVPQEPMLFPNLSVRENILFRLPKRADTTARLQEKLQQLNCQINLDASA----STLEVADQQMVEILRGLMREARILI 156
Cdd:cd03293 77 --YVFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFEnaypHQLSGGMRQRVALARALAVDPDVLL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2095916338 157 LDEPTASL---TPGETERLFSQIraLQALDVGIVFISHKLPEIRQLASHVSVM--RDGAVV 212
Cdd:cd03293 155 LDEPFSALdalTREQLQEELLDI--WRETGKTVLLVTHDIDEAVFLADRVVVLsaRPGRIV 213
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
274-471 |
1.43e-28 |
|
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: 112.18 E-value: 1.43e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 274 DLSLEIRAGEIVGLAGLVGSGRTEFAETLYGLRPPRAGRIWLENREISQESTRA-RLASGLVYLPEDRQVSGLfldapvr 352
Cdd:cd03225 19 DISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKElRRKVGLVFQNPDDQFFGP------- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 353 wnTV----MFNQPswwQQGKREAAVVERYHRALGIKLADG--DQPVRTLSGGNQQKVLLARCLEANPLLLIVDEPTRGVD 426
Cdd:cd03225 92 --TVeeevAFGLE---NLGLPEEEIEERVEEALELVGLEGlrDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLD 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2095916338 427 VSARADIYQLLKSVAAQNVAVLMISSDVEEFVGLADRVLVMHQGR 471
Cdd:cd03225 167 PAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
4-215 |
1.78e-28 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 113.29 E-value: 1.78e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 4 LLEARQIRKQFSGVAVLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDSGELTIGERAFARLNP-ALAHQLGIy 82
Cdd:COG4559 1 MLEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPwELARRRAV- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 83 lVPQE-PMLFPnLSVRENILF-RLP---KRADTTARLQEKLQQLNCQINLDASASTLEVADQQMVEILRGL-------MR 150
Cdd:COG4559 80 -LPQHsSLAFP-FTVEEVVALgRAPhgsSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLaqlwepvDG 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2095916338 151 EARILILDEPTASLTPGETERLFSQIRALQALDVGIVFISHKLPEIRQLASHVSVMRDGAVVLSG 215
Cdd:COG4559 158 GPRWLFLDEPTSALDLAHQHAVLRLARQLARRGGGVVAVLHDLNLAAQYADRILLLHQGRLVAQG 222
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
23-218 |
2.95e-28 |
|
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: 115.20 E-value: 2.95e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 23 IDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDSGELTIGERAF----ARLN-PalAHQLGIYLVPQEPMLFPNLSVR 97
Cdd:COG4148 18 VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLqdsaRGIFlP--PHRRRIGYVFQEARLFPHLSVR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 98 ENILF---RLPKRADtTARLQEKLQQLNCQINLDASASTLEVADQQMVEILRGLMREARILILDEPTASLTPGETERLFS 174
Cdd:COG4148 96 GNLLYgrkRAPRAER-RISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAEILP 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2095916338 175 QIRAL-QALDVGIVFISHKLPEIRQLASHVSVMRDGAVVLSGETA 218
Cdd:COG4148 175 YLERLrDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLA 219
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
7-471 |
6.91e-28 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 116.70 E-value: 6.91e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 7 ARQIRKQFSGVAVLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDSGELTIGERAfarlnpalahQLGiYLvPQ 86
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGL----------RIG-YL-PQ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 87 EPMLFPNLSVRENI------LFRLPKR--------ADTT------ARLQEKLQQLNcQINLDASASTL--------EVAD 138
Cdd:COG0488 69 EPPLDDDLTVLDTVldgdaeLRALEAEleeleaklAEPDedlerlAELQEEFEALG-GWEAEARAEEIlsglgfpeEDLD 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 139 QQM----------VEILRGLMREARILILDEPT-----ASltpgeTERL--FsqiraLQALDVGIVFISHKLPEIRQLAS 201
Cdd:COG0488 148 RPVselsggwrrrVALARALLSEPDLLLLDEPTnhldlES-----IEWLeeF-----LKNYPGTVLVVSHDRYFLDRVAT 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 202 HVSVMRDGAVVL-SGetaGYGDQQLISAMTPASRDHALSDTQKL------WLA---LPGNRRTQAQ-------------- 257
Cdd:COG0488 218 RILELDRGKLTLyPG---NYSAYLEQRAERLEQEAAAYAKQQKKiakeeeFIRrfrAKARKAKQAQsrikaleklereep 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 258 ---------DFP--------VLRVEDLT-GEG----FIDLSLEIRAGEIVGLAGLVGSGRTEFAETLYGLRPPRAGRIWL 315
Cdd:COG0488 295 prrdktveiRFPpperlgkkVLELEGLSkSYGdktlLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 316 enreisqeSTRARLAsglvYLPEDRQVsgLFLDAPVrWNTVmfnqpSWWQQGKREAAVveryhRA-LGIKLADGDQ---P 391
Cdd:COG0488 375 --------GETVKIG----YFDQHQEE--LDPDKTV-LDEL-----RDGAPGGTEQEV-----RGyLGRFLFSGDDafkP 429
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 392 VRTLSGGNQQKVLLARCLEANPLLLIVDEPTRGVDVSARADIYQLLKSVAAqnvAVLMISSDvEEFV-GLADRVLVMHQG 470
Cdd:COG0488 430 VGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALDDFPG---TVLLVSHD-RYFLdRVATRILEFEDG 505
|
.
gi 2095916338 471 R 471
Cdd:COG0488 506 G 506
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
5-218 |
2.82e-27 |
|
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: 109.13 E-value: 2.82e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 5 LEARQIRKQFSG--VAVLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDSGELTIGERAFARlNPALAHQ-LGI 81
Cdd:cd03263 1 LQIRNLTKTYKKgtKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT-DRKAARQsLGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 82 ylVPQEPMLFPNLSVRENILF--RLPKRADTTARLQ--EKLQQLNCQINLDASASTLEVADQQMVEILRGLMREARILIL 157
Cdd:cd03263 80 --CPQFDALFDELTVREHLRFyaRLKGLPKSEIKEEveLLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2095916338 158 DEPTASLTPGETERLFSQIRALQAlDVGIVFISHKLPEIRQLASHVSVMRDGAVVLSGETA 218
Cdd:cd03263 158 DEPTSGLDPASRRAIWDLILEVRK-GRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQ 217
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
5-212 |
3.82e-27 |
|
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: 108.50 E-value: 3.82e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 5 LEARQIRKQFSGVAVLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDSGELTIGERAFARLNPAlahQLGIYLV 84
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPK---DRDIAMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 85 PQEPMLFPNLSVRENILFRLP----KRADTTARLQEKLQQLNCQINLDASASTLEVADQQMVEILRGLMREARILILDEP 160
Cdd:cd03301 78 FQNYALYPHMTVYDNIAFGLKlrkvPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2095916338 161 TASLTPGETERLFSQIRALQA-LDVGIVFISHKLPEIRQLASHVSVMRDGAVV 212
Cdd:cd03301 158 LSNLDAKLRVQMRAELKRLQQrLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQ 210
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
3-470 |
9.62e-27 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 113.26 E-value: 9.62e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 3 PLLEARQI----RKQFSGVAVLKGIDFTLCAGQVHALMGGNGAGKS-TLMKIIAGVETPD----SGELTI-GERAFARLN 72
Cdd:PRK15134 4 PLLAIENLsvafRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPvvypSGDIRFhGESLLHASE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 73 PALAHQLG--IYLVPQEPMLFPN-LSVRENILF----------RLPKRADTTARLqEKLQQLNCQINLDASASTLEVADQ 139
Cdd:PRK15134 84 QTLRGVRGnkIAMIFQEPMVSLNpLHTLEKQLYevlslhrgmrREAARGEILNCL-DRVGIRQAAKRLTDYPHQLSGGER 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 140 QMVEILRGLMREARILILDEPTASLTPGETERLFSQIRAL-QALDVGIVFISHKLPEIRQLASHVSVMRDGAVVLSGETa 218
Cdd:PRK15134 163 QRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELqQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRA- 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 219 gygdQQLISAmtPAsrdHALsdTQKLWLALPGNRRT--QAQDFPVLRVEDL--------------TGEGFI--DLSLEIR 280
Cdd:PRK15134 242 ----ATLFSA--PT---HPY--TQKLLNSEPSGDPVplPEPASPLLDVEQLqvafpirkgilkrtVDHNVVvkNISFTLR 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 281 AGEIVGLAGLVGSGRTEFAETLYGLRPPRaGRIWLENREISQESTRArlasglvYLPEDRQVSGLFLDAPVRWNTVM--- 357
Cdd:PRK15134 311 PGETLGLVGESGSGKSTTGLALLRLINSQ-GEIWFDGQPLHNLNRRQ-------LLPVRHRIQVVFQDPNSSLNPRLnvl 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 358 --------FNQPSwWQQGKREAAVVERYHRaLGIKLADGDQPVRTLSGGNQQKVLLARCLEANPLLLIVDEPTRGVDVSA 429
Cdd:PRK15134 383 qiieeglrVHQPT-LSAAQREQQVIAVMEE-VGLDPETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTV 460
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 2095916338 430 RADIYQLLKSVAAQN-VAVLMISSDVEEFVGLADRVLVMHQG 470
Cdd:PRK15134 461 QAQILALLKSLQQKHqLAYLFISHDLHVVRALCHQVIVLRQG 502
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
274-471 |
1.49e-26 |
|
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: 105.73 E-value: 1.49e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 274 DLSLEIRAGEIVGLAGLVGSGRTEFAETLYGLRPPRAGRIWLENREISQESTRARlasglvylPEDRQVSGLFLD-APVR 352
Cdd:cd03229 18 DVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELP--------PLRRRIGMVFQDfALFP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 353 WNTVMFNqpswwqqgkreaavveryhRALGikladgdqpvrtLSGGNQQKVLLARCLEANPLLLIVDEPTRGVDVSARAD 432
Cdd:cd03229 90 HLTVLEN-------------------IALG------------LSGGQQQRVALARALAMDPDVLLLDEPTSALDPITRRE 138
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2095916338 433 IYQLLKSVAAQ-NVAVLMISSDVEEFVGLADRVLVMHQGR 471
Cdd:cd03229 139 VRALLKSLQAQlGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
6-215 |
1.71e-26 |
|
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: 105.60 E-value: 1.71e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 6 EARQIRKQFSGVAVLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDSGELTIGERAFARLNP-ALAHQLGIylV 84
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPkELARKIAY--V 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 85 PQepmlfpnlsvrenilfrlpkradttarlqeKLQQLNCQINLDASASTLEVADQQMVEILRGLMREARILILDEPTASL 164
Cdd:cd03214 79 PQ------------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHL 128
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2095916338 165 TPGETERLFSQIRAL-QALDVGIVFISHKLPEIRQLASHVSVMRDGAVVLSG 215
Cdd:cd03214 129 DIAHQIELLELLRRLaRERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
274-471 |
2.69e-26 |
|
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: 106.44 E-value: 2.69e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 274 DLSLEIRAGEIVGLAGLVGSGRTEFAETLYGLRPPRAGRIWLENREISQESTRARLASGlvYLPEDRqvsGLFLDAPVRW 353
Cdd:cd03263 20 DLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAARQSLG--YCPQFD---ALFDELTVRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 354 NTVMFNQpswwQQGKREA---AVVERYHRALGIKlADGDQPVRTLSGGNQQKVLLARCLEANPLLLIVDEPTRGVDVSAR 430
Cdd:cd03263 95 HLRFYAR----LKGLPKSeikEEVELLLRVLGLT-DKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPASR 169
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2095916338 431 ADIYQLLKSVaAQNVAVLMISSDVEEFVGLADRVLVMHQGR 471
Cdd:cd03263 170 RAIWDLILEV-RKGRSIILTTHSMDEAEALCDRIAIMSDGK 209
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
5-215 |
3.99e-26 |
|
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: 105.74 E-value: 3.99e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 5 LEARQIRKQFSGVAVLKGIDFTLCAGqVHALMGGNGAGKSTLMKIIAGVETPDSGELTIGERAFARLNPALAHQLGiYLv 84
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRRIG-YL- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 85 PQEPMLFPNLSVRE-----NILFRLPKRaDTTARLQEKLQQLNCQINLDASASTLEVADQQMVEILRGLMREARILILDE 159
Cdd:cd03264 78 PQEFGVYPNFTVREfldyiAWLKGIPSK-EVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2095916338 160 PTASLTPGETERlFSQIRALQALDVGIVFISHKLPEIRQLASHVSVMRDGAVVLSG 215
Cdd:cd03264 157 PTAGLDPEERIR-FRNLLSELGEDRIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
274-471 |
7.67e-26 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 105.32 E-value: 7.67e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 274 DLSLEIRAGEIVGLAGLVGSGRTEFAETLYGLRPPRAGRIWLENREISQE--STRARLasGLVYLPedrQVSGLFLDAPV 351
Cdd:cd03218 18 GVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLpmHKRARL--GIGYLP---QEASIFRKLTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 352 RWNTV----MFNQPSWWQQGKREAAVVEryhraLGI-KLADgdQPVRTLSGGNQQKVLLARCLEANPLLLIVDEPTRGVD 426
Cdd:cd03218 93 EENILavleIRGLSKKEREEKLEELLEE-----FHItHLRK--SKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVD 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2095916338 427 VSARADIYQLLKSVAAQNVAVLMISSDVEEFVGLADRVLVMHQGR 471
Cdd:cd03218 166 PIAVQDIQKIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGK 210
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
262-471 |
9.93e-26 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 104.51 E-value: 9.93e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 262 LRVEDLT-----GEGFIDLSLEIRAGEIVGLAGLVGSGRTEFAETLYGLRPPRAGRIWLENREISQ---ESTRARLAsgl 333
Cdd:COG4619 1 LELEGLSfrvggKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAmppPEWRRQVA--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 334 vYLPedrQVSGLFlDAPVRWNtvmFNQPSWWQQGKREAAVVERYHRALGIKLADGDQPVRTLSGGNQQKVLLARCLEANP 413
Cdd:COG4619 78 -YVP---QEPALW-GGTVRDN---LPFPFQLRERKFDRERALELLERLGLPPDILDKPVERLSGGERQRLALIRALLLQP 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2095916338 414 LLLIVDEPTRGVDVSARADIYQLLKS-VAAQNVAVLMISSDVEEFVGLADRVLVMHQGR 471
Cdd:COG4619 150 DVLLLDEPTSALDPENTRRVEELLREyLAEEGRAVLWVSHDPEQIERVADRVLTLEAGR 208
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
23-218 |
9.98e-26 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 105.22 E-value: 9.98e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 23 IDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDSGELTIGERAFARLNPAlahQLGIYLVPQEPMLFPNLSVRENILF 102
Cdd:COG3840 18 FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPA---ERPVSMLFQENNLFPHLTVAQNIGL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 103 ----RLPKRADTTARLQEKLQQLNCQINLDASASTLEVADQQMVEILRGLMREARILILDEPTASLTPG---ETERLFSQ 175
Cdd:COG3840 95 glrpGLKLTAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDPAlrqEMLDLVDE 174
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2095916338 176 IRALQALDVgiVFISHKLPEIRQLASHVSVMRDGAVVLSGETA 218
Cdd:COG3840 175 LCRERGLTV--LMVTHDPEDAARIADRVLLVADGRIAADGPTA 215
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
5-217 |
1.24e-25 |
|
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: 104.57 E-value: 1.24e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 5 LEARQIRKQFSGVAVLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAG-----VETPDSGELTI-GERAFARLNPALAHQ 78
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRlndliPGAPDEGEVLLdGKDIYDLDVDVLELR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 79 LGIYLVPQEPMLFPnLSVRENILFRLP-----KRADTTARLQEKLQQ--LNCQINLDASASTLEVADQQMVEILRGLMRE 151
Cdd:cd03260 81 RRVGMVFQKPNPFP-GSIYDNVAYGLRlhgikLKEELDERVEEALRKaaLWDEVKDRLHALGLSGGQQQRLCLARALANE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2095916338 152 ARILILDEPTASLTPGETERLFSQIRALQAlDVGIVFISHKLPEIRQLASHVSVMRDGAVVLSGET 217
Cdd:cd03260 160 PEVLLLDEPTSALDPISTAKIEELIAELKK-EYTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPT 224
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
17-215 |
1.51e-25 |
|
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: 104.21 E-value: 1.51e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 17 VAVLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDSGELTIGERAFARLNPA-LAHQLGIylVPQEPMLFpNLS 95
Cdd:cd03245 17 IPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPAdLRRNIGY--VPQDVTLF-YGT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 96 VRENILFRLPkrADTTARLQE--KLQQLNCQINLDASASTLEVADQ---------QMVEILRGLMREARILILDEPTASL 164
Cdd:cd03245 94 LRDNITLGAP--LADDERILRaaELAGVTDFVNKHPNGLDLQIGERgrglsggqrQAVALARALLNDPPILLLDEPTSAM 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2095916338 165 TPGETERLFSQIRALQAlDVGIVFISHKLPeIRQLASHVSVMRDGAVVLSG 215
Cdd:cd03245 172 DMNSEERLKERLRQLLG-DKTLIIITHRPS-LLDLVDRIIVMDSGRIVADG 220
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
24-215 |
1.82e-25 |
|
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: 103.73 E-value: 1.82e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 24 DFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDSGELTIGERAFARLNPAlahQLGIYLVPQEPMLFPNLSVRENILFR 103
Cdd:cd03298 18 DLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPA---DRPVSMLFQENNLFAHLTVEQNVGLG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 104 LPKRADTTARLQEKLQQLNCQINLDAS----ASTLEVADQQMVEILRGLMREARILILDEPTASLTPG---ETERLFSQI 176
Cdd:cd03298 95 LSPGLKLTAEDRQAIEVALARVGLAGLekrlPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPAlraEMLDLVLDL 174
|
170 180 190
....*....|....*....|....*....|....*....
gi 2095916338 177 RALQALDVgiVFISHKLPEIRQLASHVSVMRDGAVVLSG 215
Cdd:cd03298 175 HAETKMTV--LMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
3-216 |
1.92e-25 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 107.61 E-value: 1.92e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 3 PLLEARQIRKQFSGVAVLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDSGELTIGERAFARLNPalaHQLGIY 82
Cdd:PRK11607 18 PLLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPP---YQRPIN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 83 LVPQEPMLFPNLSVRENILF-----RLPKrADTTARLQEKLQQLNCQINLDASASTLEVADQQMVEILRGLMREARILIL 157
Cdd:PRK11607 95 MMFQSYALFPHMTVEQNIAFglkqdKLPK-AEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLL 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2095916338 158 DEPTASLTPGETERLfsQIRALQALD-VGI--VFISHKLPEIRQLASHVSVMRDGAVVLSGE 216
Cdd:PRK11607 174 DEPMGALDKKLRDRM--QLEVVDILErVGVtcVMVTHDQEEAMTMAGRIAIMNRGKFVQIGE 233
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
5-211 |
2.18e-25 |
|
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: 103.38 E-value: 2.18e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 5 LEARQIRKQFSGVAVLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDSGELTI-GERAFARLNPALAHQLGIYL 83
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIdGLKLTDDKKNINELRQKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 84 VPQEPMLFPNLSVRENILFRLPK-----RADTTARLQEKLQQLNCQINLDASASTLEVADQQMVEILRGLMREARILILD 158
Cdd:cd03262 81 VFQQFNLFPHLTVLENITLAPIKvkgmsKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2095916338 159 EPTASLTPGETERLFSQIRALQALDVGIVFISHKLPEIRQLASHVSVMRDGAV 211
Cdd:cd03262 161 EPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
5-471 |
3.01e-25 |
|
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: 108.74 E-value: 3.01e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 5 LEARQIRKQFSGVAVLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVET--PDSGELT-----------------IGE 65
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQyePTSGRIIyhvalcekcgyverpskVGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 66 RA-------------FARLNPALAHQLG--IYLVPQEPM-LFPNLSVRENILFRLP----KRADTTARLQEKLQQLNCQI 125
Cdd:TIGR03269 81 PCpvcggtlepeevdFWNLSDKLRRRIRkrIAIMLQRTFaLYGDDTVLDNVLEALEeigyEGKEAVGRAVDLIEMVQLSH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 126 NLDASASTLEVADQQMVEILRGLMREARILILDEPTASLTPGETERLFSQIR-ALQALDVGIVFISHkLPE-IRQLASHV 203
Cdd:TIGR03269 161 RITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEeAVKASGISMVLTSH-WPEvIEDLSDKA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 204 SVMRDGAVVLSGETagygDQQLISAMtpasrdHALSDTQKLWLALPGNrrtqaqdfPVLRVEDLTG------EGFI---- 273
Cdd:TIGR03269 240 IWLENGEIKEEGTP----DEVVAVFM------EGVSEVEKECEVEVGE--------PIIKVRNVSKryisvdRGVVkavd 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 274 DLSLEIRAGEIVGLAGLVGSGRTEFAETLYGLRPPRAGRIWLENREISQEST--------RARLASGLVYlpedrQVSGL 345
Cdd:TIGR03269 302 NVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRVGDEWVDMTkpgpdgrgRAKRYIGILH-----QEYDL 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 346 FLDAPVRWN---TVMFNQPSwwQQGKREAAVV-------ERYHRALGIKLADgdqpvrTLSGGNQQKVLLARCLEANPLL 415
Cdd:TIGR03269 377 YPHRTVLDNlteAIGLELPD--ELARMKAVITlkmvgfdEEKAEEILDKYPD------ELSEGERHRVALAQVLIKEPRI 448
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 2095916338 416 LIVDEPTRGVDVSARADI-YQLLKSVAAQNVAVLMISSDVEEFVGLADRVLVMHQGR 471
Cdd:TIGR03269 449 VILDEPTGTMDPITKVDVtHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGK 505
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
3-215 |
4.56e-25 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 103.57 E-value: 4.56e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 3 PLLEARQIRKQFSGVAVLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDSGELTIGERAFARLNPALAHQLGI- 81
Cdd:COG1137 2 MTLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMHKRARLGIg 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 82 YLvPQEPMLFPNLSVRENIL----FRLPKRADTTARLQEKLQQLNCQINLDASASTLEVADQQMVEILRGLMREARILIL 157
Cdd:COG1137 82 YL-PQEASIFRKLTVEDNILavleLRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKFILL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2095916338 158 DEPTASLTP---GETERLfsqIRALQALDVGIVFISHKLPEIRQLASHVSVMRDGAVVLSG 215
Cdd:COG1137 161 DEPFAGVDPiavADIQKI---IRHLKERGIGVLITDHNVRETLGICDRAYIISEGKVLAEG 218
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
274-471 |
4.97e-25 |
|
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: 101.36 E-value: 4.97e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 274 DLSLEIRAGEIVGLAGLVGSGRTEFAETLYGLRPPRAGRIWLENREISQESTRARlASGLVYLPedrqvsglfldapvrw 353
Cdd:cd03214 17 DLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKEL-ARKIAYVP---------------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 354 nTVMfnqpswwqqgkreaavveryhRALGI-KLADgdQPVRTLSGGNQQKVLLARCLEANPLLLIVDEPTRGVDVSARAD 432
Cdd:cd03214 80 -QAL---------------------ELLGLaHLAD--RPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQIE 135
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2095916338 433 IYQLLKSVAAQ-NVAVLMISSDVEEFVGLADRVLVMHQGR 471
Cdd:cd03214 136 LLELLRRLARErGKTVVMVLHDLNLAARYADRVILLKDGR 175
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
19-215 |
7.03e-25 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 107.94 E-value: 7.03e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 19 VLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDSGELTIGERAFARLNPA-LAHQLGIylVPQEPMLFpNLSVR 97
Cdd:COG1132 355 VLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLEsLRRQIGV--VPQDTFLF-SGTIR 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 98 ENILFRLPKRADttARLQEKLQQLNCqinlDASASTLE------VADQ---------QMVEILRGLMREARILILDEPTA 162
Cdd:COG1132 432 ENIRYGRPDATD--EEVEEAAKAAQA----HEFIEALPdgydtvVGERgvnlsggqrQRIAIARALLKDPPILILDEATS 505
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2095916338 163 SLTPgETERLfsqI-RALQALDVG--IVFISHKLPEIRQlASHVSVMRDGAVVLSG 215
Cdd:COG1132 506 ALDT-ETEAL---IqEALERLMKGrtTIVIAHRLSTIRN-ADRILVLDDGRIVEQG 556
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
13-215 |
7.14e-25 |
|
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: 102.69 E-value: 7.14e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 13 QFS---GVAVLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDSGELTIGERAFARLNPALAHQLgIYLVPQEPM 89
Cdd:cd03254 9 NFSydeKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSM-IGVVLQDTF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 90 LFPNlSVRENILFRLP-------KRADTTARLQEKLQQL--NCQINLDASASTLEVADQQMVEILRGLMREARILILDEP 160
Cdd:cd03254 88 LFSG-TIMENIRLGRPnatdeevIEAAKEAGAHDFIMKLpnGYDTVLGENGGNLSQGERQLLAIARAMLRDPKILILDEA 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2095916338 161 TASLTPgETERLFSQirALQALDVG--IVFISHKLPEIRQlASHVSVMRDGAVVLSG 215
Cdd:cd03254 167 TSNIDT-ETEKLIQE--ALEKLMKGrtSIIIAHRLSTIKN-ADKILVLDDGKIIEEG 219
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
19-215 |
8.42e-25 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 102.79 E-value: 8.42e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 19 VLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDSGELTIGERAF---ARLNPALAHQL--GIYLVPQEPMLFPN 93
Cdd:PRK11124 17 ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFdfsKTPSDKAIRELrrNVGMVFQQYNLWPH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 94 LSVRENiLFRLPKR------ADTTARLQEKLQQLNCQINLDASASTLEVADQQMVEILRGLMREARILILDEPTASLTPG 167
Cdd:PRK11124 97 LTVQQN-LIEAPCRvlglskDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPE 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2095916338 168 ETERLFSQIRALQALDVGIVFISHKLPEIRQLASHVSVMRDGAVVLSG 215
Cdd:PRK11124 176 ITAQIVSIIRELAETGITQVIVTHEVEVARKTASRVVYMENGHIVEQG 223
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
262-471 |
9.38e-25 |
|
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: 100.01 E-value: 9.38e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 262 LRVEDLTGEGFIDLSLEIRAGEIVGLAGLVGSGRTEFAETLYGLRPPRAGRIWLENREISQESTRaRLASGLVYLPEdrq 341
Cdd:cd00267 5 LSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLE-ELRRRIGYVPQ--- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 342 vsglfldapvrwntvmfnqpswwqqgkreaavveryhralgikladgdqpvrtLSGGNQQKVLLARCLEANPLLLIVDEP 421
Cdd:cd00267 81 -----------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEP 107
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2095916338 422 TRGVDVSARADIYQLLKSVAAQNVAVLMISSDVEEFVGLADRVLVMHQGR 471
Cdd:cd00267 108 TSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
19-212 |
1.05e-24 |
|
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: 101.56 E-value: 1.05e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 19 VLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDSGELTIGERAFarlnPALAHQLGIYLVPQEP--MLFPNlSV 96
Cdd:cd03226 15 ILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPI----KAKERRKSIGYVMQDVdyQLFTD-SV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 97 RENILFRLPKRADTTARLQEKLQQLNCQINLDASASTLEVADQQMVEILRGLMREARILILDEPTASLTPGETERLFSQI 176
Cdd:cd03226 90 REELLLGLKELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNMERVGELI 169
|
170 180 190
....*....|....*....|....*....|....*.
gi 2095916338 177 RALQALDVGIVFISHKLPEIRQLASHVSVMRDGAVV 212
Cdd:cd03226 170 RELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
3-218 |
1.98e-24 |
|
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: 101.70 E-value: 1.98e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 3 PLLEARQIRKQFSGVAVLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDSG-ELTI-GERaFARLN-------- 72
Cdd:COG1119 2 PLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLfGER-RGGEDvwelrkri 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 73 ----PALAHQLGiylvpqepmlfPNLSVRENIL---------FRLPKRADtTARLQEKLQQLNCQINLDASASTLEVADQ 139
Cdd:COG1119 81 glvsPALQLRFP-----------RDETVLDVVLsgffdsiglYREPTDEQ-RERARELLELLGLAHLADRPFGTLSQGEQ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 140 QMVEILRGLMREARILILDEPTASLTPGETERLFSQIRAL-QALDVGIVFISHKLPEIRQLASHVSVMRDGAVVLSGETA 218
Cdd:COG1119 149 RRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLaAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRVVAAGPKE 228
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
5-216 |
2.14e-24 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 101.75 E-value: 2.14e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 5 LEARQIRKQFSGVAVLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDSGELTIGE---------RAFARLNPAL 75
Cdd:PRK11264 4 IEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDitidtarslSQQKGLIRQL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 76 AHQLGiyLVPQEPMLFPNLSVRENIL-----FRLPKRADTTARLQEKLQQLNCQINLDASASTLEVADQQMVEILRGLMR 150
Cdd:PRK11264 84 RQHVG--FVFQNFNLFPHRTVLENIIegpviVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAM 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2095916338 151 EARILILDEPTASLTPGETERLFSQIRALQALDVGIVFISHKLPEIRQLASHVSVMRDGAVVLSGE 216
Cdd:PRK11264 162 RPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGP 227
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
274-471 |
2.42e-24 |
|
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: 2.42e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 274 DLSLEIRAGEIVGLAGLVGSGRTEFAETLYGLRPPRAGRIWLENREIsQESTRARLAsglvYLPEDRqvsGLFLDAPVRW 353
Cdd:cd03269 18 DISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPL-DIAARNRIG----YLPEER---GLYPKMKVID 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 354 NTVMFNQPSwwQQGKREAAV-VERYHRALGIKlADGDQPVRTLSGGNQQKVLLARCLEANPLLLIVDEPTRGVDVSARAD 432
Cdd:cd03269 90 QLVYLAQLK--GLKKEEARRrIDEWLERLELS-EYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVNVEL 166
|
170 180 190
....*....|....*....|....*....|....*....
gi 2095916338 433 IYQLLKSVAAQNVAVLMISSDVEEFVGLADRVLVMHQGR 471
Cdd:cd03269 167 LKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGR 205
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
5-215 |
3.00e-24 |
|
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: 100.52 E-value: 3.00e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 5 LEARQIRKQFSGVAVLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDSGELTIGERAFARLNPALAHQLGIylV 84
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREVRRRIGI--V 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 85 PQEPMLFPNLSVRENILF--RLP--KRADTTARLQEKLQQLNCQINLDASASTLEVADQQMVEILRGLMREARILILDEP 160
Cdd:cd03265 79 FQDLSVDDELTGWENLYIhaRLYgvPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEP 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2095916338 161 TASLTPGETERLFSQIRALQA-LDVGIVFISHKLPEIRQLASHVSVMRDGAVVLSG 215
Cdd:cd03265 159 TIGLDPQTRAHVWEYIEKLKEeFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEG 214
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
15-225 |
3.15e-24 |
|
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: 101.11 E-value: 3.15e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 15 SGVAVLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDSGELTIGERAFARLNP----ALAHQLGiyLVPQEPML 90
Cdd:cd03256 12 NGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGkalrQLRRQIG--MIFQQFNL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 91 FPNLSVRENILF-RLPKRA--DTTARL---QEKLQQLNC--QINLD----ASASTLEVADQQMVEILRGLMREARILILD 158
Cdd:cd03256 90 IERLSVLENVLSgRLGRRStwRSLFGLfpkEEKQRALAAleRVGLLdkayQRADQLSGGQQQRVAIARALMQQPKLILAD 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2095916338 159 EPTASLTPGETERLFSQIRALqALDVGI-VFIS-HKLPEIRQLASHVSVMRDGAVVLSGETAGYGDQQL 225
Cdd:cd03256 170 EPVASLDPASSRQVMDLLKRI-NREEGItVIVSlHQVDLAREYADRIVGLKDGRIVFDGPPAELTDEVL 237
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
274-471 |
4.31e-24 |
|
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: 99.87 E-value: 4.31e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 274 DLSLEIRAGEIVGLAGLVGSGRTEFAETLYGLRPPRAGRIWLENREISQESTRARLA-----SGLVYlpedrQVSGLFLD 348
Cdd:cd03255 22 GVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAfrrrhIGFVF-----QSFNLLPD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 349 APVRWNtVMFnqPSWWQqGKREAAVVERYHRALG-IKLADG-DQPVRTLSGGNQQKVLLARCLEANPLLLIVDEPTRGVD 426
Cdd:cd03255 97 LTALEN-VEL--PLLLA-GVPKKERRERAEELLErVGLGDRlNHYPSELSGGQQQRVAIARALANDPKIILADEPTGNLD 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2095916338 427 VSARADIYQLLKSVAAQ-NVAVLMISSDvEEFVGLADRVLVMHQGR 471
Cdd:cd03255 173 SETGKEVMELLRELNKEaGTTIVVVTHD-PELAEYADRIIELRDGK 217
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
14-215 |
6.33e-24 |
|
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: 99.53 E-value: 6.33e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 14 FSGVAVLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDSGELTIgeraFARlnPALAHQLGIYLVPQEPML--- 90
Cdd:cd03235 9 YGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRV----FGK--PLEKERKRIGYVPQRRSIdrd 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 91 FPnLSVRENIL---------FRLPKRADtTARLQEKLQQLNCQINLDASASTLEVADQQMVEILRGLMREARILILDEPT 161
Cdd:cd03235 83 FP-ISVRDVVLmglyghkglFRRLSKAD-KAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPF 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2095916338 162 ASLTPGETERLFSQIRALQALDVGIVFISHKLPEIRQLASHVsVMRDGAVVLSG 215
Cdd:cd03235 161 AGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRV-LLLNRTVVASG 213
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
19-211 |
6.84e-24 |
|
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: 98.06 E-value: 6.84e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 19 VLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDSGELTIGERAFARLNPAlahQLG--IYLVPQEPMLFPNlSV 96
Cdd:cd03246 17 VLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPN---ELGdhVGYLPQDDELFSG-SI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 97 RENILFRlpkradttarlqeklqqlncqinldasastlevADQQMVEILRGLMREARILILDEPTASLTPGETERLFSQI 176
Cdd:cd03246 93 AENILSG---------------------------------GQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQAI 139
|
170 180 190
....*....|....*....|....*....|....*
gi 2095916338 177 RALQALDVGIVFISHKlPEIRQLASHVSVMRDGAV 211
Cdd:cd03246 140 AALKAAGATRIVIAHR-PETLASADRILVLEDGRV 173
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
11-215 |
9.10e-24 |
|
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: 99.71 E-value: 9.10e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 11 RKQFSGVAVLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDSGELTI-GERAFARlNPALAHQLGIyLVPQEPM 89
Cdd:cd03267 28 KRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVaGLVPWKR-RKKFLRRIGV-VFGQKTQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 90 LFPNLSVRENI-----LFRLPKrADTTARLQEKLQQLNCQINLDASASTLEVADQQMVEILRGLMREARILILDEPTASL 164
Cdd:cd03267 106 LWWDLPVIDSFyllaaIYDLPP-ARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGL 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2095916338 165 TPGETERLFSQIRALQAL-DVGIVFISHKLPEIRQLASHVSVMRDGAVVLSG 215
Cdd:cd03267 185 DVVAQENIRNFLKEYNRErGTTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
5-211 |
1.04e-23 |
|
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: 99.72 E-value: 1.04e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 5 LEARQIRKQFSGVAVLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDSGELTIGERAFARLNPalaHQLGIYLV 84
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPV---QERNVGFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 85 PQEPMLFPNLSVRENILF--RLPKRAD--TTARLQEKLQQLNCQINLDASA----STLEVADQQMVEILRGLMREARILI 156
Cdd:cd03296 80 FQHYALFRHMTVFDNVAFglRVKPRSErpPEAEIRAKVHELLKLVQLDWLAdrypAQLSGGQRQRVALARALAVEPKVLL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2095916338 157 LDEPTASLTPGETERLFSQIRALQ-ALDVGIVFISHKLPEIRQLASHVSVMRDGAV 211
Cdd:cd03296 160 LDEPFGALDAKVRKELRRWLRRLHdELHVTTVFVTHDQEEALEVADRVVVMNKGRI 215
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
16-215 |
1.17e-23 |
|
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: 99.54 E-value: 1.17e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 16 GVAVLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDSGELTIGERAFARLNP-ALAHQLGIylVPQEPMLFPNl 94
Cdd:cd03249 15 DVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLrWLRSQIGL--VSQEPVLFDG- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 95 SVRENILFRLPKRADTTArlQEKLQQLNC-----------QINLDASASTLEVADQQMVEILRGLMREARILILDEPTAS 163
Cdd:cd03249 92 TIAENIRYGKPDATDEEV--EEAAKKANIhdfimslpdgyDTLVGERGSQLSGGQKQRIAIARALLRNPKILLLDEATSA 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2095916338 164 LTpGETERLFSQirALQALDVG--IVFISHKLPEIRQlASHVSVMRDGAVVLSG 215
Cdd:cd03249 170 LD-AESEKLVQE--ALDRAMKGrtTIVIAHRLSTIRN-ADLIAVLQNGQVVEQG 219
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
274-471 |
2.42e-23 |
|
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: 98.21 E-value: 2.42e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 274 DLSLEIRAGEIVGLAGLVGSGRTEFAETLYGLRPPRAGRIWLENREISQESTRARLASGLV--YLPEDRQVSGlfldapv 351
Cdd:cd03265 18 GVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREVRRRIGIVfqDLSVDDELTG------- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 352 RWNTVMFNQpswwQQGKREAAVVERYHRAL-GIKLAD-GDQPVRTLSGGNQQKVLLARCLEANPLLLIVDEPTRGVDVSA 429
Cdd:cd03265 91 WENLYIHAR----LYGVPGAERRERIDELLdFVGLLEaADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQT 166
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2095916338 430 RADIYQLLKS-VAAQNVAVLMISSDVEEFVGLADRVLVMHQGR 471
Cdd:cd03265 167 RAHVWEYIEKlKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGR 209
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
260-471 |
4.47e-23 |
|
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: 96.78 E-value: 4.47e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 260 PVLRVEDLT---GEG--FIDLSLEIRAGEIVGLAGLVGSGRTEFAETLYGLRPPRAGRIWLENREISQEstRARLASGLV 334
Cdd:COG4133 1 MMLEAENLScrrGERllFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDA--REDYRRRLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 335 YLPEDrqvSGLFLDAPVRWNTvmfnqpSWWQQGKREAAVVERYHRAL-GIKLAD-GDQPVRTLSGGNQQKVLLARCLEAN 412
Cdd:COG4133 79 YLGHA---DGLKPELTVRENL------RFWAALYGLRADREAIDEALeAVGLAGlADLPVRQLSAGQKRRVALARLLLSP 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2095916338 413 PLLLIVDEPTRGVDVSARADIYQLLKSVAAQNVAVLMISSDVEEFvgLADRVLVMHQGR 471
Cdd:COG4133 150 APLWLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTTHQPLEL--AAARVLDLGDFK 206
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
10-225 |
5.63e-23 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 99.91 E-value: 5.63e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 10 IRKQFSGVAVLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDSGELTI-GERAFARlnpALAHQLGIYLVPQEP 88
Cdd:PRK13536 47 VSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVlGVPVPAR---ARLARARIGVVPQFD 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 89 MLFPNLSVRENIL-----FRLPKRaDTTARLQEKLQQLNCQINLDASASTLEVADQQMVEILRGLMREARILILDEPTAS 163
Cdd:PRK13536 124 NLDLEFTVRENLLvfgryFGMSTR-EIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTG 202
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2095916338 164 LTPGETERLFSQIRALQALDVGIVFISHKLPEIRQLASHVSVMRDGAVVLSGETAGYGDQQL 225
Cdd:PRK13536 203 LDPHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHALIDEHI 264
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
2-209 |
7.89e-23 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 100.02 E-value: 7.89e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 2 KPLLEARQIRKQFSGVAVLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDSGELTIGERAFARLNPALAHqlgI 81
Cdd:PRK09452 12 SPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAENRH---V 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 82 YLVPQEPMLFPNLSVRENILF--RLPKR--ADTTARLQEKLQQLNCQINLDASASTLEVADQQMVEILRGLMREARILIL 157
Cdd:PRK09452 89 NTVFQSYALFPHMTVFENVAFglRMQKTpaAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLL 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2095916338 158 DEPTASLTPGETERLFSQIRALQ-ALDVGIVFISHKLPEIRQLASHVSVMRDG 209
Cdd:PRK09452 169 DESLSALDYKLRKQMQNELKALQrKLGITFVFVTHDQEEALTMSDRIVVMRDG 221
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
262-471 |
9.13e-23 |
|
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: 96.80 E-value: 9.13e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 262 LRVEDLT---GEGFI--DLSLEIRAGEIVGLAGLVGSGRTEFAETLYGLRPPRAGRIWLENREISQES----TRARLASG 332
Cdd:cd03261 1 IELRGLTksfGGRTVlkGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSeaelYRLRRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 333 LVYlpedrQVSGLFLDAPVRWNtVMF------NQPSWWQQGKreaaVVERYHrALGIKlADGDQPVRTLSGGNQQKVLLA 406
Cdd:cd03261 81 MLF-----QSGALFDSLTVFEN-VAFplrehtRLSEEEIREI----VLEKLE-AVGLR-GAEDLYPAELSGGMKKRVALA 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2095916338 407 RCLEANPLLLIVDEPTRGVDVSARADIYQLLKSV-AAQNVAVLMISSDVEEFVGLADRVLVMHQGR 471
Cdd:cd03261 149 RALALDPELLLYDEPTAGLDPIASGVIDDLIRSLkKELGLTSIMVTHDLDTAFAIADRIAVLYDGK 214
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
5-211 |
1.41e-22 |
|
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: 95.55 E-value: 1.41e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 5 LEARQIRKQF-SGVAVLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDSGELTIGERAFARLN----PALAHQL 79
Cdd:cd03292 1 IEFINVTKTYpNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRgraiPYLRRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 80 GIylVPQEPMLFPNLSVRENILFRL----PKRADTTARLQEKLQQLNCQINLDASASTLEVADQQMVEILRGLMREARIL 155
Cdd:cd03292 81 GV--VFQDFRLLPDRNVYENVAFALevtgVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTIL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2095916338 156 ILDEPTASLTPGETERLFSQIRALQALDVGIVFISHKLPEIRQLASHVSVMRDGAV 211
Cdd:cd03292 159 IADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
274-471 |
1.46e-22 |
|
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: 96.25 E-value: 1.46e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 274 DLSLEIRAGEIVGLAGLVGSGRTEFAETLYGLRPPRAGRIWLENREISQESTRARlASGLVYlpedrQVSGLFLDAPVRW 353
Cdd:cd03296 20 DVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQER-NVGFVF-----QHYALFRHMTVFD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 354 NtVMFN---QPSwwQQGKREAAVVERYHRALGIKLADG--DQPVRTLSGGNQQKVLLARCLEANPLLLIVDEPTRGVDVS 428
Cdd:cd03296 94 N-VAFGlrvKPR--SERPPEAEIRAKVHELLKLVQLDWlaDRYPAQLSGGQRQRVALARALAVEPKVLLLDEPFGALDAK 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2095916338 429 ARADIYQLLKSVAAQ-NVAVLMISSDVEEFVGLADRVLVMHQGR 471
Cdd:cd03296 171 VRKELRRWLRRLHDElHVTTVFVTHDQEEALEVADRVVVMNKGR 214
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
16-212 |
1.69e-22 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 95.50 E-value: 1.69e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 16 GVAVLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDSGELTIGERAFARLN----PALAHQLGIylVPQEPMLF 91
Cdd:COG2884 14 GREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKrreiPYLRRRIGV--VFQDFRLL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 92 PNLSVRENILFRL----PKRADTTARLQEKLQQLNCQINLDASASTLEVADQQMVEILRGLMREARILILDEPTASLTPG 167
Cdd:COG2884 92 PDRTVYENVALPLrvtgKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLLADEPTGNLDPE 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2095916338 168 ETERLFSQIRALQALDVGIVFISHKLPEIRQLASHVSVMRDGAVV 212
Cdd:COG2884 172 TSWEIMELLEEINRRGTTVLIATHDLELVDRMPKRVLELEDGRLV 216
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
19-215 |
2.43e-22 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 95.90 E-value: 2.43e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 19 VLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVE--TPDSG----------ELTIGERAfarlnpalahQLGIYLVPQ 86
Cdd:COG0396 15 ILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPkyEVTSGsilldgedilELSPDERA----------RAGIFLAFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 87 EPMLFPNLSVReNILfrlpkRADTTARLQEKLQQLNCQINLDASASTLEVaDQQMV----------------EILRGLMR 150
Cdd:COG0396 85 YPVEIPGVSVS-NFL-----RTALNARRGEELSAREFLKLLKEKMKELGL-DEDFLdryvnegfsggekkrnEILQMLLL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2095916338 151 EARILILDEPTA-----SLtpgeteRLFSQ-IRALQALDVGIVFISHK---LPEIRqlASHVSVMRDGAVVLSG 215
Cdd:COG0396 158 EPKLAILDETDSgldidAL------RIVAEgVNKLRSPDRGILIITHYqriLDYIK--PDFVHVLVDGRIVKSG 223
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
17-215 |
3.30e-22 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 100.18 E-value: 3.30e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 17 VAVLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDSGELTIGERAFARLNPALAHQlGIYLVPQEPMLFpNLSV 96
Cdd:TIGR00958 494 VPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHR-QVALVGQEPVLF-SGSV 571
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 97 RENILFRLPKRADttARLQEKLQQLNCQ-----------INLDASASTLEVADQQMVEILRGLMREARILILDEPTASLT 165
Cdd:TIGR00958 572 RENIAYGLTDTPD--EEIMAAAKAANAHdfimefpngydTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALD 649
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2095916338 166 pGETERLFSQIRALQALDVgiVFISHKLPEIRQlASHVSVMRDGAVVLSG 215
Cdd:TIGR00958 650 -AECEQLLQESRSRASRTV--LLIAHRLSTVER-ADQILVLKKGSVVEMG 695
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1-209 |
3.83e-22 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 95.44 E-value: 3.83e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 1 MKPLLEARQIRKQFSGVAVLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDSGELTIGERAFARLNPALAHQLG 80
Cdd:PRK11300 2 SQPLLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIARMG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 81 IYLVPQEPMLFPNLSVRENI---------------LFRLP--KRADTTA--RLQEKLQQLNCQINLDASASTLEVADQQM 141
Cdd:PRK11300 82 VVRTFQHVRLFREMTVIENLlvaqhqqlktglfsgLLKTPafRRAESEAldRAATWLERVGLLEHANRQAGNLAYGQQRR 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2095916338 142 VEILRGLMREARILILDEPTASLTPGETERLFSQIRAL-QALDVGIVFISHKLPEIRQLASHVSVMRDG 209
Cdd:PRK11300 162 LEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELrNEHNVTVLLIEHDMKLVMGISDRIYVVNQG 230
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
261-471 |
4.53e-22 |
|
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: 96.66 E-value: 4.53e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 261 VLRVEDL-----TGEGFI----DLSLEIRAGEIVGLAGLVGSGRTEFAETLYGLRPPRA---GRIWLENREISQESTRA- 327
Cdd:COG0444 1 LLEVRNLkvyfpTRRGVVkavdGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPGitsGEILFDGEDLLKLSEKEl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 328 RLASGlvylpedRQVSGLFLDA-----PVRwnTV--MFNQPSWWQQGKREAAVVERYHRAL---GIkladgDQPVRT--- 394
Cdd:COG0444 81 RKIRG-------REIQMIFQDPmtslnPVM--TVgdQIAEPLRIHGGLSKAEARERAIELLervGL-----PDPERRldr 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 395 ----LSGGNQQKVLLARCLEANPLLLIVDEPTRGVDVSARADIYQLLKSVAAQ-NVAVLMISSD---VEEFvglADRVLV 466
Cdd:COG0444 147 ypheLSGGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRElGLAILFITHDlgvVAEI---ADRVAV 223
|
....*
gi 2095916338 467 MHQGR 471
Cdd:COG0444 224 MYAGR 228
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
262-491 |
5.43e-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: 97.10 E-value: 5.43e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 262 LRVEDLTGEGFIDLSLEIRAGEIVGLAGLVGSGRTEFAETLYGLRPPRAGRIWLeNREISQEStrarlASGLVYLPEDRQ 341
Cdd:TIGR02142 3 ARFSKRLGDFSLDADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVL-NGRTLFDS-----RKGIFLPPEKRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 342 VSGLFLDA------PVRWNtvmFNQPSWWQQGKREAAVVERYHRALGIK-LADgdQPVRTLSGGNQQKVLLARCLEANPL 414
Cdd:TIGR02142 77 IGYVFQEArlfphlSVRGN---LRYGMKRARPSERRISFERVIELLGIGhLLG--RLPGRLSGGEKQRVAIGRALLSSPR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2095916338 415 LLIVDEPTRGVDVSARADIYQLLKSVAAQ-NVAVLMISSDVEEFVGLADRVLVMHQGRHSGELARQAVTVDRMMTLAF 491
Cdd:TIGR02142 152 LLLMDEPLAALDDPRKYEILPYLERLHAEfGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPDLPWLA 229
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
19-215 |
5.96e-22 |
|
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: 92.76 E-value: 5.96e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 19 VLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDSGELTIGERAFARLNPALAHQLGIylVPQEPMLFpNLSVRE 98
Cdd:cd03247 17 VLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSLISV--LNQRPYLF-DTTLRN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 99 NILFRLPKradttarlqeklqqlncqinldasastlevADQQMVEILRGLMREARILILDEPTASLTPgETER-----LF 173
Cdd:cd03247 94 NLGRRFSG------------------------------GERQRLALARILLQDAPIVLLDEPTVGLDP-ITERqllslIF 142
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2095916338 174 SQIRalqalDVGIVFISHKLPEIRQlASHVSVMRDGAVVLSG 215
Cdd:cd03247 143 EVLK-----DKTLIWITHHLTGIEH-MDKILFLENGKIIMQG 178
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
274-470 |
6.98e-22 |
|
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: 93.48 E-value: 6.98e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 274 DLSLEIRAGEIVGLAGLVGSGRTEFAETLYGLRPPRAGRIWLENREISQeSTRARlASGLVYLPEDRQvsgLFLDApVrW 353
Cdd:cd03226 18 DLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKA-KERRK-SIGYVMQDVDYQ---LFTDS-V-R 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 354 NTVMFNQPswwqQGKREAAVVERYHRALGIKLADGDQPvRTLSGGNQQKVLLARCLEANPLLLIVDEPTRGVDVSARADI 433
Cdd:cd03226 91 EELLLGLK----ELDAGNEQAETVLKDLDLYALKERHP-LSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNMERV 165
|
170 180 190
....*....|....*....|....*....|....*..
gi 2095916338 434 YQLLKSVAAQNVAVLMISSDVEEFVGLADRVLVMHQG 470
Cdd:cd03226 166 GELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANG 202
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
253-471 |
7.19e-22 |
|
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: 94.48 E-value: 7.19e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 253 RTQAQDFPVLRvedltgegfiDLSLEIRAGEIVGLAGLVGSGRTEFAETLYGLRPPRAGRIWLENREISQESTRARLasg 332
Cdd:COG1124 12 GQGGRRVPVLK----------DVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFR--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 333 lvylpedRQVSGLFLDAPV----RWnTV--MFNQPSWWQQGKREAAVVERYHRALGIKLADGDQPVRTLSGGNQQKVLLA 406
Cdd:COG1124 79 -------RRVQMVFQDPYAslhpRH-TVdrILAEPLRIHGLPDREERIAELLEQVGLPPSFLDRYPHQLSGGQRQRVAIA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2095916338 407 RCLEANPLLLIVDEPTRGVDVSARADIYQLLKSV-AAQNVAVLMISSDVeEFVG-LADRVLVMHQGR 471
Cdd:COG1124 151 RALILEPELLLLDEPTSALDVSVQAEILNLLKDLrEERGLTYLFVSHDL-AVVAhLCDRVAVMQNGR 216
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
3-215 |
7.24e-22 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 94.84 E-value: 7.24e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 3 PLLEARQIRKQFSGVAVLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDSGELTIGERAFARLNPA-LAHQLGI 81
Cdd:PRK13548 1 AMLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAeLARRRAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 82 ylVPQEPML-FPnLSVRENI-LFRLP---KRADTTARLQEKLQQLNCQINLDASASTLEVADQQMVEILRGLMR------ 150
Cdd:PRK13548 81 --LPQHSSLsFP-FTVEEVVaMGRAPhglSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAQlwepdg 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2095916338 151 EARILILDEPTASLTPGETERLFSQIRAL-QALDVGIVFISHKLPEIRQLASHVSVMRDGAVVLSG 215
Cdd:PRK13548 158 PPRWLLLDEPTSALDLAHQHHVLRLARQLaHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADG 223
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
274-422 |
1.32e-21 |
|
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: 91.17 E-value: 1.32e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 274 DLSLEIRAGEIVGLAGLVGSGRTEFAETLYGLRPPRAGRIWLENREISQESTRARLAsGLVYLPEDrqvSGLFLDAPVRW 353
Cdd:pfam00005 3 NVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRK-EIGYVFQD---PQLFPRLTVRE 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2095916338 354 NtVMFNQPSWWQQGKREAAVVERYHRALGIKLADG---DQPVRTLSGGNQQKVLLARCLEANPLLLIVDEPT 422
Cdd:pfam00005 79 N-LRLGLLLKGLSKREKDARAEEALEKLGLGDLADrpvGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
274-475 |
1.81e-21 |
|
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: 90.95 E-value: 1.81e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 274 DLSLEIRAGEIVGLAGLVGSGRTEFAETLYGLRPPRAGRIWLENREISqestrarlasglvylpedrqvsglfldapvrw 353
Cdd:cd03216 18 GVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVS-------------------------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 354 ntvmFNQPswwqqgkREAavveryhRALGIkladgdQPVRTLSGGNQQKVLLARCLEANPLLLIVDEPTRGVDVSARADI 433
Cdd:cd03216 66 ----FASP-------RDA-------RRAGI------AMVYQLSVGERQMVEIARALARNARLLILDEPTAALTPAEVERL 121
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2095916338 434 YQLLKSVAAQNVAVLMISSDVEEFVGLADRVLVMHQGRHSGE 475
Cdd:cd03216 122 FKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRVVGT 163
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
7-215 |
2.04e-21 |
|
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: 93.86 E-value: 2.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 7 ARQIRKQFSGVAVLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDSGELTIGERAFARLNPALAHQL---GIYL 83
Cdd:cd03294 27 KEEILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRELrrkKISM 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 84 VPQEPMLFPNLSVRENILFRLP----KRADTTARLQEKLQQLNCQINLDASASTLEVADQQMVEILRGLMREARILILDE 159
Cdd:cd03294 107 VFQSFALLPHRTVLENVAFGLEvqgvPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDE 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2095916338 160 PTASLTPGETERLFSQIRALQA-LDVGIVFISHKLPEIRQLASHVSVMRDGAVVLSG 215
Cdd:cd03294 187 AFSALDPLIRREMQDELLRLQAeLQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVG 243
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
262-471 |
2.47e-21 |
|
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: 92.78 E-value: 2.47e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 262 LRVEDLT---GEGFI-DLSLEIRAGEIVGLAGLVGSGRTEFAETLYGLRPPRAGRIWLENREISQESTRARlasGLVYLP 337
Cdd:cd03299 1 LKVENLSkdwKEFKLkNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEKR---DISYVP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 338 EDRqvsGLFLDAPVRWNTVMFNQPSWWQQGKREAAVVErYHRALGIK--LadgDQPVRTLSGGNQQKVLLARCLEANPLL 415
Cdd:cd03299 78 QNY---ALFPHMTVYKNIAYGLKKRKVDKKEIERKVLE-IAEMLGIDhlL---NRKPETLSGGEQQRVAIARALVVNPKI 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2095916338 416 LIVDEPTRGVDVSARADIYQLLKSVAAQ-NVAVLMISSDVEEFVGLADRVLVMHQGR 471
Cdd:cd03299 151 LLLDEPFSALDVRTKEKLREELKKIRKEfGVTVLHVTHDFEEAWALADKVAIMLNGK 207
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
5-180 |
6.21e-21 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 91.00 E-value: 6.21e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 5 LEARQIRKQfsGVAVLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPD---SGELTIGERAFARLNPalaHQLGI 81
Cdd:COG4136 4 LENLTITLG--GRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRLTALPA---EQRRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 82 YLVPQEPMLFPNLSVRENILFRLP---KRADTTARLQEKLQQLNCQINLDASASTLEVADQQMVEILRGLMREARILILD 158
Cdd:COG4136 79 GILFQDDLLFPHLSVGENLAFALPptiGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLD 158
|
170 180
....*....|....*....|....*.
gi 2095916338 159 EPTASLTPGETERL----FSQIRALQ 180
Cdd:COG4136 159 EPFSKLDAALRAQFrefvFEQIRQRG 184
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-215 |
7.50e-21 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 92.95 E-value: 7.50e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 1 MKPLLEARQIRKQFSGVAVLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDSGELTIGERAFARLNPALAHQLG 80
Cdd:PRK13537 4 SVAPIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQRVG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 81 IylVPQEPMLFPNLSVRENIL-----FRLPKrADTTARLQEKLQQLNCQINLDASASTLEVADQQMVEILRGLMREARIL 155
Cdd:PRK13537 84 V--VPQFDNLDPDFTVRENLLvfgryFGLSA-AAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 156 ILDEPTASLTPGETERLFSQIRALQALDVGIVFISHKLPEIRQLASHVSVMRDGAVVLSG 215
Cdd:PRK13537 161 VLDEPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEG 220
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
2-206 |
8.45e-21 |
|
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: 95.43 E-value: 8.45e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 2 KPLLEARQIRKQFSGV--------AVLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDSGELTIGERAFARLNP 73
Cdd:TIGR02857 312 APVTAAPASSLEFSGVsvaypgrrPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADA 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 74 ALAHQlGIYLVPQEPMLFPNlSVRENILFRLP-------KRADTTARLQEKLQQLNCQIN--LDASASTLEVADQQMVEI 144
Cdd:TIGR02857 392 DSWRD-QIAWVPQHPFLFAG-TIAENIRLARPdasdaeiREALERAGLDEFVAALPQGLDtpIGEGGAGLSGGQAQRLAL 469
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2095916338 145 LRGLMREARILILDEPTASLTPgETERLFsqIRALQALDVG--IVFISHKlPEIRQLASHVSVM 206
Cdd:TIGR02857 470 ARAFLRDAPLLLLDEPTAHLDA-ETEAEV--LEALRALAQGrtVLLVTHR-LALAALADRIVVL 529
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
5-212 |
9.14e-21 |
|
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: 91.21 E-value: 9.14e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 5 LEARQIRKQFSGV-AVLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDSGELTIGERAFARLNP-ALAHQLGiY 82
Cdd:cd03295 1 IEFENVTKRYGGGkKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPvELRRKIG-Y 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 83 lVPQEPMLFPNLSVRENILFrLPK-----RADTTARLQEKLQQLNCQIN--LDASASTLEVADQQMVEILRGLMREARIL 155
Cdd:cd03295 80 -VIQQIGLFPHMTVEENIAL-VPKllkwpKEKIRERADELLALVGLDPAefADRYPHELSGGQQQRVGVARALAADPPLL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2095916338 156 ILDEPTASLTPGETERLFSQIRALQ-ALDVGIVFISHKLPEIRQLASHVSVMRDGAVV 212
Cdd:cd03295 158 LMDEPFGALDPITRDQLQEEFKRLQqELGKTIVFVTHDIDEAFRLADRIAIMKNGEIV 215
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
274-471 |
1.07e-20 |
|
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: 90.27 E-value: 1.07e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 274 DLSLEIRAGEIVGLAGLVGSGRTEFAETLYGLRPPRAGRIWLENREISQEStrarlasglvylPEDRQVSGLFLDApvrw 353
Cdd:cd03259 18 DLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVP------------PERRNIGMVFQDY---- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 354 ntVMFNQPSWWQ--------QGKREAAVVERYHRAL---GIkLADGDQPVRTLSGGNQQKVLLARCLEANPLLLIVDEPT 422
Cdd:cd03259 82 --ALFPHLTVAEniafglklRGVPKAEIRARVRELLelvGL-EGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2095916338 423 RGVDVSARADIYQLLKSV-AAQNVAVLMISSDVEEFVGLADRVLVMHQGR 471
Cdd:cd03259 159 SALDAKLREELREELKELqRELGITTIYVTHDQEEALALADRIAVMNEGR 208
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
5-217 |
1.43e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 90.74 E-value: 1.43e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 5 LEARQIRKQFSGVAVLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGV-----ETPDSGELTIGERAFARLnPALAHQL 79
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQDIFKM-DVIELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 80 GIYLVPQEPMLFPNLSVRENI-----LFRLPK-RADTTARLQEKLQ--QLNCQIN--LDASASTLEVADQQMVEILRGLM 149
Cdd:PRK14247 83 RVQMVFQIPNPIPNLSIFENValglkLNRLVKsKKELQERVRWALEkaQLWDEVKdrLDAPAGKLSGGQQQRLCIARALA 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2095916338 150 REARILILDEPTASLTPGETERLFSQIRALQAlDVGIVFISHKLPEIRQLASHVSVMRDGAVVLSGET 217
Cdd:PRK14247 163 FQPEVLLADEPTANLDPENTAKIESLFLELKK-DMTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPT 229
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
274-471 |
1.73e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 91.65 E-value: 1.73e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 274 DLSLEIRAGEIVGLAGLVGSGRTEFAETLYGLRPPRAGRIWLENREISQES---TRARLASGLVY-LPEDRqvsgLFLDA 349
Cdd:PRK13637 25 NVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKvklSDIRKKVGLVFqYPEYQ----LFEET 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 350 PVRwnTVMFNqPSwwQQGKREAAVVERYHRAL---GIKLAD-GDQPVRTLSGGNQQKVLLARCLEANPLLLIVDEPTRGV 425
Cdd:PRK13637 101 IEK--DIAFG-PI--NLGLSEEEIENRVKRAMnivGLDYEDyKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGL 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2095916338 426 DVSARADIYQLLKSVAAQ-NVAVLMISSDVEEFVGLADRVLVMHQGR 471
Cdd:PRK13637 176 DPKGRDEILNKIKELHKEyNMTIILVSHSMEDVAKLADRIIVMNKGK 222
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
262-471 |
1.92e-20 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 90.20 E-value: 1.92e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 262 LRVEDLTG--EGFI-DLSLEIRAGEIVGLAGLVGSGRTEFAETLYGLRPPRAGRIWLENREISQestrarlasglvYLPE 338
Cdd:COG3840 2 LRLDDLTYryGDFPlRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTA------------LPPA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 339 DRQVSGLFLDapvrwNTvMFNQPSWWQQ--------GKREAAVVERYHRALG-IKLAD-GDQPVRTLSGGNQQKVLLARC 408
Cdd:COG3840 70 ERPVSMLFQE-----NN-LFPHLTVAQNiglglrpgLKLTAEQRAQVEQALErVGLAGlLDRLPGQLSGGQRQRVALARC 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2095916338 409 L-EANPLLLIvDEPTRGVDVSARADIYQLLKSVAA-QNVAVLMISSDVEEFVGLADRVLVMHQGR 471
Cdd:COG3840 144 LvRKRPILLL-DEPFSALDPALRQEMLDLVDELCReRGLTVLMVTHDPEDAARIADRVLLVADGR 207
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
274-467 |
1.98e-20 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 88.83 E-value: 1.98e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 274 DLSLEIRAGEIVGLAGLVGSGRTEFAETLYGLRPPRAGRIwlenreisqestRARLASGLVYLPEDRQVSGLFlDAPVRw 353
Cdd:NF040873 10 GVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTV------------RRAGGARVAYVPQRSEVPDSL-PLTVR- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 354 NTVM---FNQPSWWQQGKREA-AVVERYHRALGikLAD-GDQPVRTLSGGNQQKVLLARCLEANPLLLIVDEPTRGVDVS 428
Cdd:NF040873 76 DLVAmgrWARRGLWRRLTRDDrAAVDDALERVG--LADlAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAE 153
|
170 180 190
....*....|....*....|....*....|....*....
gi 2095916338 429 ARADIYQLLKSVAAQNVAVLMISSDVEEfVGLADRVLVM 467
Cdd:NF040873 154 SRERIIALLAEEHARGATVVVVTHDLEL-VRRADPCVLL 191
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-210 |
2.37e-20 |
|
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: 89.80 E-value: 2.37e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 1 MKPLLEARQIRKQFS-------GVAVLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDSGELTIgERAFARLNP 73
Cdd:COG4778 1 MTTLLEVENLSKTFTlhlqggkRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILV-RHDGGWVDL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 74 ALA--HQLgIYL-------VPQepmlF----PNLS----VRENILFRLPKRADTTARLQEKLQQLNCQINL-DASASTLE 135
Cdd:COG4778 80 AQAspREI-LALrrrtigyVSQ----FlrviPRVSaldvVAEPLLERGVDREEARARARELLARLNLPERLwDLPPATFS 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2095916338 136 VADQQMVEILRGLMREARILILDEPTASLTPGETERLFSQIRALQALDVGIVFISHKLPEIRQLASHVSVMRDGA 210
Cdd:COG4778 155 GGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVREAVADRVVDVTPFS 229
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
16-215 |
3.44e-20 |
|
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: 88.35 E-value: 3.44e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 16 GVAVLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVE--TPDSGELTIGERAFARLNPALAHQLGIYLVPQEPMLFPN 93
Cdd:cd03217 12 GKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKGEDITDLPPEERARLGIFLAFQYPPEIPG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 94 LSVREniLFRlpkradttarlqeklqqlncqiNLDASASTLEVadqQMVEILRGLMREARILILDEPTASLTPGETERLF 173
Cdd:cd03217 92 VKNAD--FLR----------------------YVNEGFSGGEK---KRNEILQLLLLEPDLAILDEPDSGLDIDALRLVA 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2095916338 174 SQIRALQALDVGIVFISHKlpeiRQLASH-----VSVMRDGAVVLSG 215
Cdd:cd03217 145 EVINKLREEGKSVLIITHY----QRLLDYikpdrVHVLYDGRIVKSG 187
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
261-481 |
3.70e-20 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 91.02 E-value: 3.70e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 261 VLRVEDLTGEGFI--DLSLEIRAGEIVGLAGLVGSGRTEFAETLYGLRPPRAGRIWLENREISQESTRARLASGLVylpe 338
Cdd:PRK13537 10 FRNVEKRYGDKLVvdGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQRVGVV---- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 339 dRQVSGLFLDAPVRWNTVMFNQpswwQQGKREAAVVERYHRALGI-KLAD-GDQPVRTLSGGNQQKVLLARCLEANPLLL 416
Cdd:PRK13537 86 -PQFDNLDPDFTVRENLLVFGR----YFGLSAAAARALVPPLLEFaKLENkADAKVGELSGGMKRRLTLARALVNDPDVL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2095916338 417 IVDEPTRGVDVSARADIYQLLKSVAAQNVAVLMISSDVEEFVGLADRVLVMHQGRHSGELARQAV 481
Cdd:PRK13537 161 VLDEPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHAL 225
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
16-215 |
3.71e-20 |
|
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: 89.21 E-value: 3.71e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 16 GVAVLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDSGELTIGERAFARLN-PALAHQLGIylVPQEPMLFpNL 94
Cdd:cd03251 14 GPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTlASLRRQIGL--VSQDVFLF-ND 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 95 SVRENILFRLP-------KRADTTARLQEKLQQL--NCQINLDASASTLEVADQQMVEILRGLMREARILILDEPTASLT 165
Cdd:cd03251 91 TVAENIAYGRPgatreevEEAARAANAHEFIMELpeGYDTVIGERGVKLSGGQRQRIAIARALLKDPPILILDEATSALD 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2095916338 166 pGETERLFSQ-IRALQALDVGIVfISHKLPEIRQlASHVSVMRDGAVVLSG 215
Cdd:cd03251 171 -TESERLVQAaLERLMKNRTTFV-IAHRLSTIEN-ADRIVVLEDGKIVERG 218
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
5-234 |
4.27e-20 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 91.68 E-value: 4.27e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 5 LEARQIRKQFSGVAVLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDSGELTIGERAFARLNpALAHQLGiyLV 84
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLH-ARDRKVG--FV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 85 PQEPMLFPNLSVRENILF---RLPKRA-DTTARLQEKLQQLNCQINLDASA----STLEVADQQMVEILRGLMREARILI 156
Cdd:PRK10851 80 FQHYALFRHMTVFDNIAFgltVLPRRErPNAAAIKAKVTQLLEMVQLAHLAdrypAQLSGGQKQRVALARALAVEPQILL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2095916338 157 LDEPTASLTPGETERLFSQIRAL-QALDVGIVFISHKLPEIRQLASHVSVMRDGAVvlsgETAGYGDQQLisaMTPASR 234
Cdd:PRK10851 160 LDEPFGALDAQVRKELRRWLRQLhEELKFTSVFVTHDQEEAMEVADRVVVMSQGNI----EQAGTPDQVW---REPATR 231
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
260-471 |
6.03e-20 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 88.56 E-value: 6.03e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 260 PVLRVEDLT-----GEGFI----DLSLEIRAGEIVGLAGLVGSGRTEFAETLYGLRPPRAGRIWLENREISQ--ESTRAR 328
Cdd:COG1136 3 PLLELRNLTksygtGEGEVtalrGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSlsERELAR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 329 L---ASGLVYlpedrQVSGLFLDAPVRWNtVMFnqPSWWQqGKREAAVVERYHRALG-IKLAD-GDQPVRTLSGGNQQKV 403
Cdd:COG1136 83 LrrrHIGFVF-----QFFNLLPELTALEN-VAL--PLLLA-GVSRKERRERARELLErVGLGDrLDHRPSQLSGGQQQRV 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2095916338 404 LLARCLEANPLLLIVDEPTRGVDVSARADIYQLLKSVAAQ-NVAVLMISSDvEEFVGLADRVLVMHQGR 471
Cdd:COG1136 154 AIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRElGTTIVMVTHD-PELAARADRVIRLRDGR 221
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
19-218 |
6.61e-20 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 88.99 E-value: 6.61e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 19 VLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDSGELTIGErafaRLNPALAHQLGIYlvpqepmlfPNLSVRE 98
Cdd:COG1134 41 ALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNG----RVSALLELGAGFH---------PELTGRE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 99 NILFR-----LPkRADTTARLQEklqqlncqInldASASTL-EVADQQMveilR----GlMReAR------------ILI 156
Cdd:COG1134 108 NIYLNgrllgLS-RKEIDEKFDE--------I---VEFAELgDFIDQPV----KtyssG-MR-ARlafavatavdpdILL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2095916338 157 LDEPTASltpGET---ERLFSQIRALQALDVGIVFISHKLPEIRQLASHVSVMRDGAVVLSGETA 218
Cdd:COG1134 170 VDEVLAV---GDAafqKKCLARIRELRESGRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPE 231
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
24-234 |
7.85e-20 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 88.49 E-value: 7.85e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 24 DFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDSGELTIGERAFARLNPAlahQLGIYLVPQEPMLFPNLSVRENILFR 103
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPS---RRPVSMLFQENNLFSHLTVAQNIGLG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 104 LPKRADTTARLQEKLQQLNCQINLDASASTLEVA----DQQMVEILRGLMREARILILDEPTASLTP---GETERLFSQI 176
Cdd:PRK10771 96 LNPGLKLNAAQREKLHAIARQMGIEDLLARLPGQlsggQRQRVALARCLVREQPILLLDEPFSALDPalrQEMLTLVSQV 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2095916338 177 RALQALDvgIVFISHKLPEIRQLASHVSVMRDGAVVLSGETagygdQQLISAMTPASR 234
Cdd:PRK10771 176 CQERQLT--LLMVSHSLEDAARIAPRSLVVADGRIAWDGPT-----DELLSGKASASA 226
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
274-471 |
8.84e-20 |
|
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: 86.28 E-value: 8.84e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 274 DLSLEIRAGEIVGLAGLVGSGRTEFAETLYGLRPPRAGRIWLEN---REISQESTRARLAsglvYLPedrQVSGLFLDap 350
Cdd:cd03228 20 DVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGvdlRDLDLESLRKNIA----YVP---QDPFLFSG-- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 351 vrwnTVMFNqpswwqqgkreaavveryhralgIkladgdqpvrtLSGGNQQKVLLARCLEANPLLLIVDEPTRGVDVSAR 430
Cdd:cd03228 91 ----TIREN-----------------------I-----------LSGGQRQRIAIARALLRDPPILILDEATSALDPETE 132
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2095916338 431 ADIYQLLKSvAAQNVAVLMISSDVEEfVGLADRVLVMHQGR 471
Cdd:cd03228 133 ALILEALRA-LAKGKTVIVIAHRLST-IRDADRIIVLDDGR 171
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
274-484 |
1.01e-19 |
|
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: 87.53 E-value: 1.01e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 274 DLSLEIRAGEIVGLAGLVGSGRTEFAETLYGLRPPRAGRIWLENREISQESTRArlasGLVYlpedrQVSGLFldaPvrW 353
Cdd:cd03293 22 DISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPDR----GYVF-----QQDALL---P--W 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 354 NTVMFN-------QpswWQQGKREAAVVERYHRALGIKLADGDQPvRTLSGGNQQKVLLARCLEANPLLLIVDEPTRGVD 426
Cdd:cd03293 88 LTVLDNvalglelQ---GVPKAEARERAEELLELVGLSGFENAYP-HQLSGGMRQRVALARALAVDPDVLLLDEPFSALD 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2095916338 427 VSARADIYQ-LLKSVAAQNVAVLMISSDVEEFVGLADRVLVMhqGRHSGELARQaVTVD 484
Cdd:cd03293 164 ALTREQLQEeLLDIWRETGKTVLLVTHDIDEAVFLADRVVVL--SARPGRIVAE-VEVD 219
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
5-178 |
1.29e-19 |
|
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: 86.78 E-value: 1.29e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 5 LEARQIRKQFSGVAVLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDSGELTIGERAFARLNPALAHqlGIYLV 84
Cdd:cd03231 1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIAR--GLLYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 85 PQEPMLFPNLSVRENILFRLPKRADTTarLQEKLQQLNCQINLDASASTLEVADQQMVEILRGLMREARILILDEPTASL 164
Cdd:cd03231 79 GHAPGIKTTLSVLENLRFWHADHSDEQ--VEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTAL 156
|
170
....*....|....
gi 2095916338 165 TPGETERLFSQIRA 178
Cdd:cd03231 157 DKAGVARFAEAMAG 170
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
270-471 |
1.30e-19 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 87.42 E-value: 1.30e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 270 EGFIDLSLEIRAGEIVGLAGLVGSGRTEFAETLYGLRPPRAGRIWLENREISQESTRA----RLASGLVY----LPEDRQ 341
Cdd:COG2884 16 EALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREipylRRRIGVVFqdfrLLPDRT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 342 VS---GLFLDApvrwntvmfnqpswwqQGKREAAVVERYHRALG-IKLAD-GDQPVRTLSGGNQQKVLLARCLEANPLLL 416
Cdd:COG2884 96 VYenvALPLRV----------------TGKSRKEIRRRVREVLDlVGLSDkAKALPHELSGGEQQRVAIARALVNRPELL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2095916338 417 IVDEPTRGVDVSARADIYQLLKSVAAQNVAVLMISSDVEEFVGLADRVLVMHQGR 471
Cdd:COG2884 160 LADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLELVDRMPKRVLELEDGR 214
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
274-471 |
1.35e-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: 87.42 E-value: 1.35e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 274 DLSLEIRAGEIVGLAGLVGSGRTEFAETLYGLRPPRAGRIWLENREISQESTRARLASGLVylPEDRqvsGLFLDAPVRW 353
Cdd:cd03266 23 GVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARRRLGFV--SDST---GLYDRLTARE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 354 NTVMFNQPSWWQQGKREAAVVERYHRaLGIKlADGDQPVRTLSGGNQQKVLLARCLEANPLLLIVDEPTRGVDVSARADI 433
Cdd:cd03266 98 NLEYFAGLYGLKGDELTARLEELADR-LGME-ELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRAL 175
|
170 180 190
....*....|....*....|....*....|....*...
gi 2095916338 434 YQLLKSVAAQNVAVLMISSDVEEFVGLADRVLVMHQGR 471
Cdd:cd03266 176 REFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGR 213
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
274-471 |
1.49e-19 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 87.78 E-value: 1.49e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 274 DLSLEIRAGEIVGLAGLVGSGRTefaETLY---GLRPPRAGRIWLENREISQES--TRARLasGLVYLPedrQVSGLFLD 348
Cdd:COG1137 21 DVSLEVNQGEIVGLLGPNGAGKT---TTFYmivGLVKPDSGRIFLDGEDITHLPmhKRARL--GIGYLP---QEASIFRK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 349 APVRWNTVMFNQpswwQQGKREAavvERYHRA------LGI-KLAdgDQPVRTLSGGNQQKVLLARCLEANPLLLIVDEP 421
Cdd:COG1137 93 LTVEDNILAVLE----LRKLSKK---EREERLeelleeFGItHLR--KSKAYSLSGGERRRVEIARALATNPKFILLDEP 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2095916338 422 TRGVDVSARADIYQLLKSVAAQNVAVLMISSDVEEFVGLADRVLVMHQGR 471
Cdd:COG1137 164 FAGVDPIAVADIQKIIRHLKERGIGVLITDHNVRETLGICDRAYIISEGK 213
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
16-191 |
1.76e-19 |
|
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 130234 [Multi-domain] Cd Length: 190 Bit Score: 86.32 E-value: 1.76e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 16 GVAVLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDSGELTIGERAFARLNPAL-AHQLGIYLVPQEP--MLFP 92
Cdd:TIGR01166 4 GPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPLDYSRKGLlERRQRVGLVFQDPddQLFA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 93 NlSVRENILFRLP----KRADTTARLQEKLQQLNCQINLDASASTLEVADQQMVEILRGLMREARILILDEPTASLTPGE 168
Cdd:TIGR01166 84 A-DVDQDVAFGPLnlglSEAEVERRVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAGLDPAG 162
|
170 180
....*....|....*....|...
gi 2095916338 169 TERLFSQIRALQALDVGIVFISH 191
Cdd:TIGR01166 163 REQMLAILRRLRAEGMTVVISTH 185
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
223-475 |
1.80e-19 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 89.50 E-value: 1.80e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 223 QQLISAMTPASRDHALSDTQKLWL-----ALPGNRRTQAQDFPVLRvEDLTGEGFID-LSLEIRAGEIVGLAGLVGSGRT 296
Cdd:PRK13536 3 TRAVAEEAPRRLELSPIERKHQGIseakaSIPGSMSTVAIDLAGVS-KSYGDKAVVNgLSFTVASGECFGLLGPNGAGKS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 297 EFAETLYGLRPPRAGRIWLENREISQESTRARLASGLVylpedRQVSGLFLDAPVRWNTVMFNQPSWWQQGKREAAVVER 376
Cdd:PRK13536 82 TIARMILGMTSPDAGKITVLGVPVPARARLARARIGVV-----PQFDNLDLEFTVRENLLVFGRYFGMSTREIEAVIPSL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 377 YHRALGIKLADGdqPVRTLSGGNQQKVLLARCLEANPLLLIVDEPTRGVDVSARADIYQLLKSVAAQNVAVLMISSDVEE 456
Cdd:PRK13536 157 LEFARLESKADA--RVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSLLARGKTILLTTHFMEE 234
|
250
....*....|....*....
gi 2095916338 457 FVGLADRVLVMHQGRHSGE 475
Cdd:PRK13536 235 AERLCDRLCVLEAGRKIAE 253
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
8-218 |
2.12e-19 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 89.37 E-value: 2.12e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 8 RQIRKQFSG----VAVLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDSGELTIGERAFARLNPAlahQL---- 79
Cdd:COG1135 5 ENLSKTFPTkggpVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSER---ELraar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 80 -GIYLVPQEPMLFPNLSVRENILFRL-----PKrADTTARLQEkLQQLncqINL----DASASTLEVADQQMVEILRGLM 149
Cdd:COG1135 82 rKIGMIFQHFNLLSSRTVAENVALPLeiagvPK-AEIRKRVAE-LLEL---VGLsdkaDAYPSQLSGGQKQRVGIARALA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2095916338 150 REARILILDEPTASLTPGETE---RLFSQIRalQALDVGIVFISHKLPEIRQLASHVSVMRDGAVVLSGETA 218
Cdd:COG1135 157 NNPKVLLCDEATSALDPETTRsilDLLKDIN--RELGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVL 226
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
247-471 |
3.26e-19 |
|
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: 90.58 E-value: 3.26e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 247 ALPGNRRtqaqdfPVLRvedltgegfiDLSLEIRAGEIVGLAGLVGSGRTEFAETLYGLRPPRAGRIWLENREISQeSTR 326
Cdd:COG4618 339 VPPGSKR------PILR----------GVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQ-WDR 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 327 ARLASGLVYLPEDrqvSGLFlDAPVRWNTVMFNQPSwwqqgkrEAAVVERYHRAlGI-----KLADG-DQPV----RTLS 396
Cdd:COG4618 402 EELGRHIGYLPQD---VELF-DGTIAENIARFGDAD-------PEKVVAAAKLA-GVhemilRLPDGyDTRIgeggARLS 469
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2095916338 397 GGNQQKVLLARCLEANPLLLIVDEPTRGVDVSARADIYQLLKSVAAQNVAVLMISSDVeEFVGLADRVLVMHQGR 471
Cdd:COG4618 470 GGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKARGATVVVITHRP-SLLAAVDKLLVLRDGR 543
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
2-208 |
3.66e-19 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 86.31 E-value: 3.66e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 2 KPLLEARQIRKQFSGVAVLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDSGELTIGERAFARLNPALAHQLGI 81
Cdd:PRK10247 5 SPLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 82 YLVpQEPMLFPNlSVRENILF--RLPKRADTTARLQEKLQQLNCQIN-LDASASTLEVADQQMVEILRGLMREARILILD 158
Cdd:PRK10247 85 YCA-QTPTLFGD-TVYDNLIFpwQIRNQQPDPAIFLDDLERFALPDTiLTKNIAELSGGEKQRISLIRNLQFMPKVLLLD 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2095916338 159 EPTASLTPGETERLFSQI-RALQALDVGIVFISHKLPEIRQ------LASHVSVMRD 208
Cdd:PRK10247 163 EITSALDESNKHNVNEIIhRYVREQNIAVLWVTHDKDEINHadkvitLQPHAGEMQE 219
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1-212 |
3.77e-19 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 90.55 E-value: 3.77e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 1 MKPLLEARQIRKQF-SG---VAVLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDSGELTIGERAFARLNP-AL 75
Cdd:PRK10535 1 MTALLELKDIRRSYpSGeeqVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDAdAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 76 A-----HQLGIYlvpQEPMLFPNLSVRENI----LFRLPKRADTTARLQEKLQQLNCQINLDASASTLEVADQQMVEILR 146
Cdd:PRK10535 81 AqlrreHFGFIF---QRYHLLSHLTAAQNVevpaVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIAR 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2095916338 147 GLMREARILILDEPTASLTPGETERLFSQIRALQALDVGIVFISHKlPEIRQLASHVSVMRDGAVV 212
Cdd:PRK10535 158 ALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHD-PQVAAQAERVIEIRDGEIV 222
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
4-215 |
4.57e-19 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 86.30 E-value: 4.57e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 4 LLEARQIRKQFSGVAVLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDSGELTI------GERAFARLnpaLAH 77
Cdd:PRK09493 1 MIEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVdglkvnDPKVDERL---IRQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 78 QLGiyLVPQEPMLFPNLSVRENILF-----RLPKRADTTARLQEKLQQLNCQINLDASASTLEVADQQMVEILRGLMREA 152
Cdd:PRK09493 78 EAG--MVFQQFYLFPHLTALENVMFgplrvRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2095916338 153 RILILDEPTASLTPGETERLFSQIRALQALDVGIVFISHKLPEIRQLASHVSVMRDGAVVLSG 215
Cdd:PRK09493 156 KLMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDG 218
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-213 |
4.64e-19 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 86.09 E-value: 4.64e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 1 MKPLLEARQIRKQFSGVAVLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDSGELTIGERAFARLNPALAHQLG 80
Cdd:PRK11614 2 EKVMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMREA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 81 IYLVPQEPMLFPNLSVRENILF------------RLPKRADTTARLQEKLQQlncqinldaSASTLEVADQQMVEILRGL 148
Cdd:PRK11614 82 VAIVPEGRRVFSRMTVEENLAMggffaerdqfqeRIKWVYELFPRLHERRIQ---------RAGTMSGGEQQMLAIGRAL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2095916338 149 MREARILILDEPTASLTPGETERLFSQIRALQALDVGIVFISHKLPEIRQLASHVSVMRDGAVVL 213
Cdd:PRK11614 153 MSQPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHVVL 217
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
3-215 |
4.92e-19 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 89.13 E-value: 4.92e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 3 PLLEARQIRKQFSGVAVLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDSGELTIGERAFARLNPALAHQLgIY 82
Cdd:PRK09536 2 PMIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRR-VA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 83 LVPQEPMLFPNLSVRENI-LFRLPKR--------ADTTArLQEKLQQLNCQINLDASASTLEVADQQMVEILRGLMREAR 153
Cdd:PRK09536 81 SVPQDTSLSFEFDVRQVVeMGRTPHRsrfdtwteTDRAA-VERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2095916338 154 ILILDEPTASLTPGETERLFSQIRALQALDVGIVFISHKLPEIRQLASHVSVMRDGAVVLSG 215
Cdd:PRK09536 160 VLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAG 221
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
274-471 |
5.70e-19 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 85.33 E-value: 5.70e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 274 DLSLEIRAGEIVGLAGLVGSGRTEFAETLYGLRPPRAGRIWLENREISQEStRARLASGLVYLPEDrqvSGLFLdAPVRW 353
Cdd:cd03245 22 NVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLD-PADLRRNIGYVPQD---VTLFY-GTLRD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 354 NTVMFNQPSwwqqgkrEAAVVERYHRALGI-----KLADG-DQPV----RTLSGGNQQKVLLARCLEANPLLLIVDEPTR 423
Cdd:cd03245 97 NITLGAPLA-------DDERILRAAELAGVtdfvnKHPNGlDLQIgergRGLSGGQRQAVALARALLNDPPILLLDEPTS 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2095916338 424 GVDVSARADIYQLLKSVAAQNvaVLMISSDVEEFVGLADRVLVMHQGR 471
Cdd:cd03245 170 AMDMNSEERLKERLRQLLGDK--TLIIITHRPSLLDLVDRIIVMDSGR 215
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
274-471 |
6.01e-19 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 86.10 E-value: 6.01e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 274 DLSLEIRAGEIVGLAGLVGSGRTEFAETLYGLRPPRAGRIWLENREISQESTRARLASGLVYLPedrQVSGLFLDAPVRW 353
Cdd:PRK10895 21 DVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRGIGYLP---QEASIFRRLSVYD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 354 NTVMFNQP----SWWQQGKREAAVVERYHRAlgiklADGDQPVRTLSGGNQQKVLLARCLEANPLLLIVDEPTRGVDVSA 429
Cdd:PRK10895 98 NLMAVLQIrddlSAEQREDRANELMEEFHIE-----HLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPIS 172
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2095916338 430 RADIYQLLKSVAAQNVAVLMISSDVEEFVGLADRVLVMHQGR 471
Cdd:PRK10895 173 VIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGH 214
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
274-471 |
7.72e-19 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 85.94 E-value: 7.72e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 274 DLSLEIRAGEIVGLAGLVGSGRTEFAETLYGLRPPRAGRIWLENREISQESTRArLASGLVYLPedrQVSGLFLDAPVRw 353
Cdd:COG4559 19 DVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWE-LARRRAVLP---QHSSLAFPFTVE- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 354 NTVMFNQPSWWQQGKREAAVVERYHRALGIkLADGDQPVRTLSGGNQQKVLLARCL-------EANPLLLIVDEPTRGVD 426
Cdd:COG4559 94 EVVALGRAPHGSSAAQDRQIVREALALVGL-AHLAGRSYQTLSGGEQQRVQLARVLaqlwepvDGGPRWLFLDEPTSALD 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2095916338 427 VSARADIYQLLKSVAAQNVAVLMISSDVEEFVGLADRVLVMHQGR 471
Cdd:COG4559 173 LAHQHAVLRLARQLARRGGGVVAVLHDLNLAAQYADRILLLHQGR 217
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
274-471 |
1.09e-18 |
|
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: 89.12 E-value: 1.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 274 DLSLEIRAGEIVGLAGLVGSGRTEFAETLYGLRPPRAGRIWLENREISQESTRArLASGLVYLPEDrqvsGLFLDAPVRW 353
Cdd:COG2274 493 NISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPAS-LRRQIGVVLQD----VFLFSGTIRE 567
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 354 NTVMFNqpswwqqgkrEAAVVERYHRAL---GI-----KLADG-DQPV----RTLSGGNQQKVLLARCLEANPLLLIVDE 420
Cdd:COG2274 568 NITLGD----------PDATDEEIIEAArlaGLhdfieALPMGyDTVVgeggSNLSGGQRQRLAIARALLRNPRILILDE 637
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2095916338 421 PTRGVDVSARADIYQLLKSvAAQNVAVLMISSDvEEFVGLADRVLVMHQGR 471
Cdd:COG2274 638 ATSALDAETEAIILENLRR-LLKGRTVIIIAHR-LSTIRLADRIIVLDKGR 686
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
1-232 |
1.16e-18 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 86.94 E-value: 1.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 1 MKPLLEARQIRKQ-------FSGVAVLK---GIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDSGELTIGERAFAR 70
Cdd:PRK11308 2 QQPLLQAIDLKKHypvkrglFKPERLVKaldGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 71 LNPALAHQL--GIYLVPQEPmlFPNLSVRENILFRL--PKRADTT---ARLQEKLQQLNCQINLDAsastlEVAD----- 138
Cdd:PRK11308 82 ADPEAQKLLrqKIQIVFQNP--YGSLNPRKKVGQILeePLLINTSlsaAERREKALAMMAKVGLRP-----EHYDryphm 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 139 -----QQMVEILRGLMREARILILDEPTASLTpgeterlfSQIRA--------LQA-LDVGIVFISHKLPEIRQLASHVS 204
Cdd:PRK11308 155 fsggqRQRIAIARALMLDPDVVVADEPVSALD--------VSVQAqvlnlmmdLQQeLGLSYVFISHDLSVVEHIADEVM 226
|
250 260 270
....*....|....*....|....*....|....*
gi 2095916338 205 VMRDGAVVLSGETAG-YGD------QQLISAmTPA 232
Cdd:PRK11308 227 VMYLGRCVEKGTKEQiFNNprhpytQALLSA-TPR 260
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
260-492 |
1.41e-18 |
|
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: 85.14 E-value: 1.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 260 PVLRVEDLT---GEGFI--DLSLEIRAGEIVGLAGLVGSGRTEFAETLYGLRPPRAG-RIWLENREISQEST---RARLa 330
Cdd:COG1119 2 PLLELRNVTvrrGGKTIldDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRGGEDVwelRKRI- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 331 sGLV------YLPED---RQV--SGLFlDAPVRWNtvmfnQPSWWQQGKreaavVERYHRALGIK-LADgdQPVRTLSGG 398
Cdd:COG1119 81 -GLVspalqlRFPRDetvLDVvlSGFF-DSIGLYR-----EPTDEQRER-----ARELLELLGLAhLAD--RPFGTLSQG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 399 NQQKVLLARCLEANPLLLIVDEPTRGVDVSARADIYQLLKSVAAQ-NVAVLMISSDVEEFVGLADRVLVMHQGR--HSGE 475
Cdd:COG1119 147 EQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEgAPTLVLVTHHVEEIPPGITHVLLLKDGRvvAAGP 226
|
250
....*....|....*..
gi 2095916338 476 LArqAVTVDRMMTLAFG 492
Cdd:COG1119 227 KE--EVLTSENLSEAFG 241
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
260-471 |
1.89e-18 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 85.45 E-value: 1.89e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 260 PVLRVEDLTGE-------GFIDLSLEIRAGEIVGLAGLVGSGRTEFAETLYGLRPPRAGRIWLENREISQEST---RARL 329
Cdd:PRK13635 4 EIIRVEHISFRypdaatyALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVwdvRRQV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 330 asGLVYLPEDRQvsglFLDAPVRwNTVMFnqpSWWQQGKREAAVVERYHRAL---GIKLADGDQPVRtLSGGNQQKVLLA 406
Cdd:PRK13635 84 --GMVFQNPDNQ----FVGATVQ-DDVAF---GLENIGVPREEMVERVDQALrqvGMEDFLNREPHR-LSGGQKQRVAIA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2095916338 407 RCLEANPLLLIVDEPTRGVDVSARADIYQLLKSVAAQ-NVAVLMISSDVEEfVGLADRVLVMHQGR 471
Cdd:PRK13635 153 GVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQkGITVLSITHDLDE-AAQADRVIVMNKGE 217
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
254-471 |
2.03e-18 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 86.32 E-value: 2.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 254 TQAQDFPVLRVEDL-----TGEGFI----DLSLEIRAGEIVGLAGLVGSGRTEFAETLYGLRPpRAGRI----WLENREI 320
Cdd:PRK09473 5 AQQQADALLDVKDLrvtfsTPDGDVtavnDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLA-ANGRIggsaTFNGREI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 321 sqestrarlasglVYLPEDR-------QVSGLFLDAPVRWNTVMfnqpswwQQGKREAAVVeRYHRALGIKLAdGDQPVR 393
Cdd:PRK09473 84 -------------LNLPEKElnklraeQISMIFQDPMTSLNPYM-------RVGEQLMEVL-MLHKGMSKAEA-FEESVR 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 394 TL-------------------SGGNQQKVLLARCLEANPLLLIVDEPTRGVDVSARADIYQLLKSVAAQ-NVAVLMISSD 453
Cdd:PRK09473 142 MLdavkmpearkrmkmyphefSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHD 221
|
250
....*....|....*...
gi 2095916338 454 VEEFVGLADRVLVMHQGR 471
Cdd:PRK09473 222 LGVVAGICDKVLVMYAGR 239
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
274-471 |
2.03e-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: 83.81 E-value: 2.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 274 DLSLEIRAGEIVGLAGLVGSGRTEFAETLYGLRPPRAGRIWLenreisqestrarLASGLVYLPEDRQVSGLFLDAP--- 350
Cdd:cd03268 18 DISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITF-------------DGKSYQKNIEALRRIGALIEAPgfy 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 351 ----VRWNTVMFNQpswwQQGKREAAvVERYHRALGIKlADGDQPVRTLSGGNQQKVLLARCLEANPLLLIVDEPTRGVD 426
Cdd:cd03268 85 pnltARENLRLLAR----LLGIRKKR-IDEVLDVVGLK-DSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLD 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2095916338 427 VSARADIYQLLKSVAAQNVAVLMISSDVEEFVGLADRVLVMHQGR 471
Cdd:cd03268 159 PDGIKELRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGK 203
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
274-471 |
2.04e-18 |
|
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: 84.66 E-value: 2.04e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 274 DLSLEIRAGEIVGLAGLVGSGRTEFAETLYGLRPPRAGRIWLENREISQES-TRARLASGLVYlpedrQVSGLFLDAPVR 352
Cdd:cd03295 19 NLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDpVELRRKIGYVI-----QQIGLFPHMTVE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 353 WNTVMFNQPSWWQQGKREAAVVERyhralgIKLAD------GDQPVRTLSGGNQQKVLLARCLEANPLLLIVDEPTRGVD 426
Cdd:cd03295 94 ENIALVPKLLKWPKEKIRERADEL------LALVGldpaefADRYPHELSGGQQQRVGVARALAADPPLLLMDEPFGALD 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2095916338 427 VSARADIYQLLKSVAAQ-NVAVLMISSDVEEFVGLADRVLVMHQGR 471
Cdd:cd03295 168 PITRDQLQEEFKRLQQElGKTIVFVTHDIDEAFRLADRIAIMKNGE 213
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
2-218 |
2.04e-18 |
|
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: 87.94 E-value: 2.04e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 2 KPLLEARQIRKQFSGV--AVLK---GIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDSGELT--IGER--AFARLN 72
Cdd:TIGR03269 277 EPIIKVRNVSKRYISVdrGVVKavdNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNvrVGDEwvDMTKPG 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 73 PALAHQLGIYL--VPQEPMLFPNLSVREN----ILFRLPK-----RADTTARL----QEKLQQLncqinLDASASTLEVA 137
Cdd:TIGR03269 357 PDGRGRAKRYIgiLHQEYDLYPHRTVLDNlteaIGLELPDelarmKAVITLKMvgfdEEKAEEI-----LDKYPDELSEG 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 138 DQQMVEILRGLMREARILILDEPTASLTPGETERLFSQI-RALQALDVGIVFISHKLPEIRQLASHVSVMRDGAVVLSGE 216
Cdd:TIGR03269 432 ERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSIlKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGD 511
|
..
gi 2095916338 217 TA 218
Cdd:TIGR03269 512 PE 513
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
5-166 |
2.25e-18 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 84.75 E-value: 2.25e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 5 LEARQIRKQF-SG----VAVLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDSGELTIGERAFARLNpalAHQL 79
Cdd:COG1101 2 LELKNLSKTFnPGtvneKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLP---EYKR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 80 GIYL--VPQEPML--FPNLSVRENIL----------FRLPKRADTTARLQEKLQQLNCQIN--LDASASTLEVADQQMVE 143
Cdd:COG1101 79 AKYIgrVFQDPMMgtAPSMTIEENLAlayrrgkrrgLRRGLTKKRRELFRELLATLGLGLEnrLDTKVGLLSGGQRQALS 158
|
170 180
....*....|....*....|...
gi 2095916338 144 ILRGLMREARILILDEPTASLTP 166
Cdd:COG1101 159 LLMATLTKPKLLLLDEHTAALDP 181
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
5-199 |
2.25e-18 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 83.18 E-value: 2.25e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 5 LEARQIRKQFSGVAVLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDSGELTIGERAFARLNPALAHQLgIYLV 84
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENI-LYLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 85 PQePMLFPNLSVRENILFRLPKRADTTARLQEKLQQLNCQINLDASASTLEVADQQMVEILRGLMREARILILDEPTASL 164
Cdd:TIGR01189 80 HL-PGLKPELSALENLHFWAAIHGGAQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTAL 158
|
170 180 190
....*....|....*....|....*....|....*...
gi 2095916338 165 TPGETERLFSQIRALQALDVGIVFISHK---LPEIRQL 199
Cdd:TIGR01189 159 DKAGVALLAGLLRAHLARGGIVLLTTHQdlgLVEAREL 196
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
271-471 |
2.76e-18 |
|
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: 84.62 E-value: 2.76e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 271 GFIDLSLEIRAGEIVGLAGLVGSGRTEFAETLYGLRPPRAGRIWLENREISQESTRA-----RLASGLVYlpedrQVSGL 345
Cdd:cd03294 39 GVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKElrelrRKKISMVF-----QSFAL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 346 FLDAPVRWNTVMfnqpSWWQQGKREAAVVERYHRAL---GIKlADGDQPVRTLSGGNQQKVLLARCLEANPLLLIVDEPT 422
Cdd:cd03294 114 LPHRTVLENVAF----GLEVQGVPRAEREERAAEALelvGLE-GWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAF 188
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2095916338 423 RGVDVSARADIY-QLLKSVAAQNVAVLMISSDVEEFVGLADRVLVMHQGR 471
Cdd:cd03294 189 SALDPLIRREMQdELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGR 238
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
260-471 |
2.80e-18 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 85.92 E-value: 2.80e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 260 PVLRVEDLT---GEGFI--DLSLEIRAGEIVGLAGLVGSGRTEFAETLYGLRPPRAGRIWLENREISqestraRLAsglv 334
Cdd:COG3842 4 PALELENVSkryGDVTAldDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVT------GLP---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 335 ylPEDRQVS------GLFldaP---VRWNtVMF--NQpswwqQGKREAAVVERYHRALG-IKLAD-GDQPVRTLSGGNQQ 401
Cdd:COG3842 74 --PEKRNVGmvfqdyALF---PhltVAEN-VAFglRM-----RGVPKAEIRARVAELLElVGLEGlADRYPHQLSGGQQQ 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2095916338 402 KVLLARCLEANPLLLIVDEPTRGVDVSARADIYQLLKSV-AAQNVAVLMISSDVEEFVGLADRVLVMHQGR 471
Cdd:COG3842 143 RVALARALAPEPRVLLLDEPLSALDAKLREEMREELRRLqRELGITFIYVTHDQEEALALADRIAVMNDGR 213
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
260-471 |
2.82e-18 |
|
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: 83.88 E-value: 2.82e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 260 PVLRVEDLT---GEGFI--DLSLEIRAGEIVGLAGLVGSGRTEFAETLYGLRPPRAGRIWLENREISQESTRARLA---- 330
Cdd:COG1127 4 PMIEVRNLTksfGDRVVldGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYElrrr 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 331 SGLVYlpedrQVSGLFLDAPVRWNtVMFnqPswwqqgkreaavvERYHRALGIKLAD---------------GDQPVRTL 395
Cdd:COG1127 84 IGMLF-----QGGALFDSLTVFEN-VAF--P-------------LREHTDLSEAEIRelvleklelvglpgaADKMPSEL 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2095916338 396 SGGNQQKVLLARCLEANPLLLIVDEPTRGVD-VSARAdIYQLLKSVAAQ-NVAVLMISSDVEEFVGLADRVLVMHQGR 471
Cdd:COG1127 143 SGGMRKRVALARALALDPEILLYDEPTAGLDpITSAV-IDELIRELRDElGLTSVVVTHDLDSAFAIADRVAVLADGK 219
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
249-471 |
3.19e-18 |
|
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: 87.51 E-value: 3.19e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 249 PGNRRTQAQDFPVLRVEDLT----GEGFI--DLSLEIRAGEIVGLAGLVGSGRTEFAETLYGLRPPRAGRIWLENREISQ 322
Cdd:COG4988 324 AGTAPLPAAGPPSIELEDVSfsypGGRPAldGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSD 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 323 EStRARLASGLVYLPedrQVSGLFlDAPVRWNTVMfnqpswwqqGKREA--AVVERYHRALGI-----KLADG-DQPV-- 392
Cdd:COG4988 404 LD-PASWRRQIAWVP---QNPYLF-AGTIRENLRL---------GRPDAsdEELEAALEAAGLdefvaALPDGlDTPLge 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 393 --RTLSGGNQQKVLLARCLEANPLLLIVDEPTRGVDVSARADIYQLLKSvAAQNVAVLMISSDvEEFVGLADRVLVMHQG 470
Cdd:COG4988 470 ggRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRR-LAKGRTVILITHR-LALLAQADRILVLDDG 547
|
.
gi 2095916338 471 R 471
Cdd:COG4988 548 R 548
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
260-471 |
3.29e-18 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 84.05 E-value: 3.29e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 260 PVLRVEDLT---GEGFI--DLSLEIRAGEIVGLAGLVGSGRTEFAETLYGLRPPRAGRIWLENREISQESTRArLASGLV 334
Cdd:PRK13548 1 AMLEARNLSvrlGGRTLldDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAE-LARRRA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 335 YLPedrQVSGLFLDAPVRWNTVMFNQPsWWQQGKREAAVVERYHRALGIkLADGDQPVRTLSGGNQQKVLLARCL----- 409
Cdd:PRK13548 80 VLP---QHSSLSFPFTVEEVVAMGRAP-HGLSRAEDDALVAAALAQVDL-AHLAGRDYPQLSGGEQQRVQLARVLaqlwe 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2095916338 410 -EANPLLLIVDEPTRGVDVSARADIYQLLKSVA-AQNVAVLMISSDVEEFVGLADRVLVMHQGR 471
Cdd:PRK13548 155 pDGPPRWLLLDEPTSALDLAHQHHVLRLARQLAhERGLAVIVVLHDLNLAARYADRIVLLHQGR 218
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
23-215 |
3.83e-18 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 85.70 E-value: 3.83e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 23 IDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDSGELTIGERAfarLNPAlahQLGIYLVP---------QEPMLFPN 93
Cdd:PRK11144 17 VNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRV---LFDA---EKGICLPPekrrigyvfQDARLFPH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 94 LSVRENILFRLpkRADTTARLQEKLQQLNCQINLDASASTLEVADQQMVEILRGLMREARILILDEPTASL-TPGETERL 172
Cdd:PRK11144 91 YKVRGNLRYGM--AKSMVAQFDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLdLPRKRELL 168
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2095916338 173 FSQIRALQALDVGIVFISHKLPEIRQLASHVSVMRDGAVVLSG 215
Cdd:PRK11144 169 PYLERLAREINIPILYVSHSLDEILRLADRVVVLEQGKVKAFG 211
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
272-471 |
3.85e-18 |
|
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: 81.88 E-value: 3.85e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 272 FIDLSLEIRAGEIVGLAGLVGSGRTEFAETLYGLRPPRAGRIWLENREISQEStRARLASGLVYLPEDrqvsglfldapv 351
Cdd:cd03246 18 LRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWD-PNELGDHVGYLPQD------------ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 352 rwntvmfnqpswwqqgkreaavveryhralgIKLADGDQPVRTLSGGNQQKVLLARCLEANPLLLIVDEPTRGVDVSARA 431
Cdd:cd03246 85 -------------------------------DELFSGSIAENILSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGER 133
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2095916338 432 DIYQLLKSVAAQNVAVLMISSDvEEFVGLADRVLVMHQGR 471
Cdd:cd03246 134 ALNQAIAALKAAGATRIVIAHR-PETLASADRILVLEDGR 172
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
2-215 |
4.11e-18 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 83.92 E-value: 4.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 2 KPLLEARQIRKQFSGVAVLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGveTPD----SGELTIGERAFARLNPALAH 77
Cdd:CHL00131 5 KPILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG--HPAykilEGDILFKGESILDLEPEERA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 78 QLGIYLVPQEPMLFPNLSvreNILF-RLpkrADTTARLQEKLQQLNC------------QINLDASASTLEVAD------ 138
Cdd:CHL00131 83 HLGIFLAFQYPIEIPGVS---NADFlRL---AYNSKRKFQGLPELDPlefleiineklkLVGMDPSFLSRNVNEgfsgge 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 139 QQMVEILRGLMREARILILDEPTASLTPGETERLFSQIRALQALDVGIVFISHK---LPEIRqlASHVSVMRDGAVVLSG 215
Cdd:CHL00131 157 KKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIILITHYqrlLDYIK--PDYVHVMQNGKIIKTG 234
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
274-471 |
4.89e-18 |
|
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: 82.63 E-value: 4.89e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 274 DLSLEIRAGeIVGLAGLVGSGRTEFAETLYGLRPPRAGRIWLENREISQESTRARLASGlvYLPEDrqvsglFLDAPvRW 353
Cdd:cd03264 18 GVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRRIG--YLPQE------FGVYP-NF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 354 NTVMFNQPSWWQQGKREAAVVERYHRALG-IKLAD-GDQPVRTLSGGNQQKVLLARCLEANPLLLIVDEPTRGVDVSARA 431
Cdd:cd03264 88 TVREFLDYIAWLKGIPSKEVKARVDEVLElVNLGDrAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDPEERI 167
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2095916338 432 DIYQLLKSVAAQNVAVLM--ISSDVEefvGLADRVLVMHQGR 471
Cdd:cd03264 168 RFRNLLSELGEDRIVILSthIVEDVE---SLCNQVAVLNKGK 206
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
3-232 |
4.94e-18 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 83.97 E-value: 4.94e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 3 PLLEARQIRKQFSGV---------AVLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDSGELTIGERAFARLNP 73
Cdd:PRK10419 2 TLLNVSGLSHHYAHGglsgkhqhqTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 74 A--LAHQLGIYLVPQEPM--LFPNLSVRENI------LFRLpKRADTTARLQEKLQqlncQINLDAsastlEVADQ---- 139
Cdd:PRK10419 82 AqrKAFRRDIQMVFQDSIsaVNPRKTVREIIreplrhLLSL-DKAERLARASEMLR----AVDLDD-----SVLDKrppq 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 140 ------QMVEILRGLMREARILILDEPTASLTPGETERLFSQIRALQA-LDVGIVFISHKLPEIRQLASHVSVMRDGAVV 212
Cdd:PRK10419 152 lsggqlQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQqFGTACLFITHDLRLVERFCQRVMVMDNGQIV 231
|
250 260
....*....|....*....|....*....
gi 2095916338 213 lsgETAGYGD---------QQLISAMTPA 232
Cdd:PRK10419 232 ---ETQPVGDkltfsspagRVLQNAVLPA 257
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
4-215 |
8.82e-18 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 82.63 E-value: 8.82e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 4 LLEARQIRKQFSGVAVLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDSGELTIGERAFARLNPALAHQLGIYL 83
Cdd:PRK10895 3 TLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRGIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 84 VPQEPMLFPNLSVRENILFRLPKRADTTA-----RLQEKLQQLNCQINLDASASTLEVADQQMVEILRGLMREARILILD 158
Cdd:PRK10895 83 LPQEASIFRRLSVYDNLMAVLQIRDDLSAeqredRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLD 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2095916338 159 EPTASLTPGETERLFSQIRALQALDVGIVFISHKLPEIRQLASHVSVMRDGAVVLSG 215
Cdd:PRK10895 163 EPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHG 219
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
17-215 |
1.00e-17 |
|
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: 82.20 E-value: 1.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 17 VAVLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDSGELTIGErafaRLNPALAHQLGIYlvpqepmlfPNLSV 96
Cdd:cd03220 35 FWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG----RVSSLLGLGGGFN---------PELTG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 97 RENILFRLP----KRADTTARLQEKLQ--QLNcqinldasastlEVADQQMVEILRG-LMR---------EARILILDEP 160
Cdd:cd03220 102 RENIYLNGRllglSRKEIDEKIDEIIEfsELG------------DFIDLPVKTYSSGmKARlafaiatalEPDILLIDEV 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2095916338 161 TASltpGET---ERLFSQIRALQALDVGIVFISHKLPEIRQLASHVSVMRDGAVVLSG 215
Cdd:cd03220 170 LAV---GDAafqEKCQRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
273-471 |
1.03e-17 |
|
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: 81.57 E-value: 1.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 273 IDLSLEIRaGEIVGLAGLVGSGRTEFAETLYGLRPPRAGRIWLENReISQESTRarlasGLVYLPEDRQVSGLFLDAP-- 350
Cdd:cd03297 15 LKIDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGT-VLFDSRK-----KINLPPQQRKIGLVFQQYAlf 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 351 ----VRWNTVM-FNQPSWWQQGKREAAVVERyhraLGI-KLadGDQPVRTLSGGNQQKVLLARCLEANPLLLIVDEPTRG 424
Cdd:cd03297 88 phlnVRENLAFgLKRKRNREDRISVDELLDL----LGLdHL--LNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSA 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2095916338 425 VDVSARADIYQLLKSVAAQ-NVAVLMISSDVEEFVGLADRVLVMHQGR 471
Cdd:cd03297 162 LDRALRLQLLPELKQIKKNlNIPVIFVTHDLSEAEYLADRIVVMEDGR 209
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
274-471 |
1.07e-17 |
|
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: 81.69 E-value: 1.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 274 DLSLEIRAGEIVGLAGLVGSGRTEFAETLYGLRPPRAGRIWLENREISQESTRA----RLASGLVYlpedrQVSGLFLDA 349
Cdd:cd03292 19 GINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAipylRRKIGVVF-----QDFRLLPDR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 350 PVRWNtVMF------NQPSWWQqgKREAAVVERyhraLGIKLADGDQPVRtLSGGNQQKVLLARCLEANPLLLIVDEPTR 423
Cdd:cd03292 94 NVYEN-VAFalevtgVPPREIR--KRVPAALEL----VGLSHKHRALPAE-LSGGEQQRVAIARAIVNSPTILIADEPTG 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2095916338 424 GVDVSARADIYQLLKSVAAQNVAVLMISSDVEEFVGLADRVLVMHQGR 471
Cdd:cd03292 166 NLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRHRVIALERGK 213
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
19-215 |
1.08e-17 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 82.75 E-value: 1.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 19 VLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDSGELTIGERAFARLNP-ALAHQLGiyLVPQEPMLFPNLSVR 97
Cdd:PRK11231 17 ILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSrQLARRLA--LLPQHHLTPEGITVR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 98 ENILF-RLPK-------RADTTARLQEKLQQLNCQINLDASASTLEVADQQMVEILRGLMREARILILDEPTASLTPGET 169
Cdd:PRK11231 95 ELVAYgRSPWlslwgrlSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDINHQ 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2095916338 170 ERLFSQIRALQALDVGIVFISHKLPEIRQLASHVSVMRDGAVVLSG 215
Cdd:PRK11231 175 VELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQG 220
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
262-470 |
1.28e-17 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 83.80 E-value: 1.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 262 LRVEDLTGEGFI----DLSLEIRAGEIVGLAGLVGSGRTEFAETLYGLRPPR----AGRIWLENREISQESTRARlasgl 333
Cdd:COG4170 9 LTIEIDTPQGRVkavdRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDNwhvtADRFRWNGIDLLKLSPRER----- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 334 vylpedRQVSG-----LF------LDAPVRWNT-VMFNQPS------WWQQGK-REAAVVERYHRaLGIKlaDGDQPVRT 394
Cdd:COG4170 84 ------RKIIGreiamIFqepsscLDPSAKIGDqLIEAIPSwtfkgkWWQRFKwRKKRAIELLHR-VGIK--DHKDIMNS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 395 ----LSGGNQQKVLLARCLEANPLLLIVDEPTRGVDVSARADIYQLLKSVAA-QNVAVLMISSDVEEFVGLADRVLVMHQ 469
Cdd:COG4170 155 ypheLTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQlQGTSILLISHDLESISQWADTITVLYC 234
|
.
gi 2095916338 470 G 470
Cdd:COG4170 235 G 235
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
274-471 |
1.29e-17 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 82.81 E-value: 1.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 274 DLSLEIRAGEIVGLAGLVGSGRTEFAETLYGLRPPRAGRIWLENREISQESTRARLASglvylpeDRQVSGLFLDAP--- 350
Cdd:PRK10419 30 NVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQRKAF-------RRDIQMVFQDSIsav 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 351 -----VRWntvMFNQPSWWQQGKREAAVVERYH---RALGIKLADGDQPVRTLSGGNQQKVLLARCLEANPLLLIVDEPT 422
Cdd:PRK10419 103 nprktVRE---IIREPLRHLLSLDKAERLARASemlRAVDLDDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAV 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2095916338 423 RGVDVSARADIYQLLKSVAAQ-NVAVLMISSD---VEEFvglADRVLVMHQGR 471
Cdd:PRK10419 180 SNLDLVLQAGVIRLLKKLQQQfGTACLFITHDlrlVERF---CQRVMVMDNGQ 229
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
260-471 |
1.56e-17 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 82.28 E-value: 1.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 260 PVLRVEDLT-----GEGFIDLSLEIRAGEIVGLAGLVGSGRTEFAETLYGLRPPRAGRIWLENREISQ-------ESTRA 327
Cdd:PRK11701 5 PLLSVRGLTklygpRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLrdlyalsEAERR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 328 RLAS---GLVYL-PEDrqvsGLFLDAPVRWNTvmfnqpswwqqGKREAAVVERYH---RALG--------IKLADGDQPV 392
Cdd:PRK11701 85 RLLRtewGFVHQhPRD----GLRMQVSAGGNI-----------GERLMAVGARHYgdiRATAgdwlerveIDAARIDDLP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 393 RTLSGGNQQKVLLARCLEANPLLLIVDEPTRGVDVSARADIYQLLKS-VAAQNVAVLMISSDVEEFVGLADRVLVMHQGR 471
Cdd:PRK11701 150 TTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGlVRELGLAVVIVTHDLAVARLLAHRLLVMKQGR 229
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
19-211 |
1.97e-17 |
|
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: 81.36 E-value: 1.97e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 19 VLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDSGELTIGERAFARLNPALAHQLgIYLVPQEPMLFPNlSVRE 98
Cdd:cd03248 29 VLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSK-VSLVGQEPVLFAR-SLQD 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 99 NILFRLP-------KRADTTARLQEKLQQLNCQINLDA--SASTLEVADQQMVEILRGLMREARILILDEPTASLTpGET 169
Cdd:cd03248 107 NIAYGLQscsfecvKEAAQKAHAHSFISELASGYDTEVgeKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALD-AES 185
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2095916338 170 ERLFSQIRALQALDVGIVFISHKLPEIRQlASHVSVMRDGAV 211
Cdd:cd03248 186 EQQVQQALYDWPERRTVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
275-492 |
1.98e-17 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 84.88 E-value: 1.98e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 275 LSLEIRAGEIVGLAGLVGSGRTEFAETLYGLRP--PRAGRIWLENREISQESTRARLASGLVYLpedRQVSGLFLDAPVR 352
Cdd:TIGR02633 20 IDLEVRPGECVGLCGENGAGKSTLMKILSGVYPhgTWDGEIYWSGSPLKASNIRDTERAGIVII---HQELTLVPELSVA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 353 WNTVMFNQPSWWQQGKREAAVVERYH---RALGIKLADGDQPVRTLSGGNQQKVLLARCLEANPLLLIVDEPTRGVDVSA 429
Cdd:TIGR02633 97 ENIFLGNEITLPGGRMAYNAMYLRAKnllRELQLDADNVTRPVGDYGGGQQQLVEIAKALNKQARLLILDEPSSSLTEKE 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2095916338 430 RADIYQLLKSVAAQNVAVLMISSDVEEFVGLADRVLVMHQGRHSGELARQAVTVDRMMTLAFG 492
Cdd:TIGR02633 177 TEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQHVATKDMSTMSEDDIITMMVG 239
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
258-471 |
1.98e-17 |
|
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: 81.04 E-value: 1.98e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 258 DFPVLRvedltgegfiDLSLEIRAGEIVGLAGLVGSGRTEFAETLYGLRPPRAGRIWLENREISQEST-----RARLasG 332
Cdd:cd03262 12 DFHVLK----------GIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKninelRQKV--G 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 333 LVYlpedrQVSGLF-----LD----APVrwntvmfnqpswWQQGKREAAVVERYHRALG-IKLAD-GDQPVRTLSGGNQQ 401
Cdd:cd03262 80 MVF-----QQFNLFphltvLEnitlAPI------------KVKGMSKAEAEERALELLEkVGLADkADAYPAQLSGGQQQ 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 402 KVLLARCLEANPLLLIVDEPTRGVDVSARADIYQLLKSVAAQNVAVLMISSDVEEFVGLADRVLVMHQGR 471
Cdd:cd03262 143 RVAIARALAMNPKVMLFDEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDGR 212
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
254-471 |
2.17e-17 |
|
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: 84.82 E-value: 2.17e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 254 TQAQDFPVLRVEDLT----GEGFI---DLSLEIRAGEIVGLAGLVGSGRTEFAETLYGLRPPRAGRIWLENREISQEStR 326
Cdd:COG4987 326 APAPGGPSLELEDVSfrypGAGRPvldGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLD-E 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 327 ARLASGLVYLPEDrqvSGLFlDAPVRWNTVMFnqpswwqqgkREAAVVERYHRALGI--------KLADG-DQPV----R 393
Cdd:COG4987 405 DDLRRRIAVVPQR---PHLF-DTTLRENLRLA----------RPDATDEELWAALERvglgdwlaALPDGlDTWLgeggR 470
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2095916338 394 TLSGGNQQKVLLARCLEANPLLLIVDEPTRGVDVSARADIYQLLKSvAAQNVAVLMISSDVEEfVGLADRVLVMHQGR 471
Cdd:COG4987 471 RLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLE-ALAGRTVLLITHRLAG-LERMDRILVLEDGR 546
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
274-471 |
2.26e-17 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 82.46 E-value: 2.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 274 DLSLEIRAGEIVGLAGLVGSGRTEFAETLYGLRPPRAGRIWLENREISQEsTRARLAsglvYLPEDRqvsGLFLDAPVRW 353
Cdd:COG4152 19 DVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPE-DRRRIG----YLPEER---GLYPKMKVGE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 354 NTVMFNQ----PSwwQQGKREA-AVVERyhraLGIKlADGDQPVRTLSGGNQQKVLLARCLEANPLLLIVDEPTRGVDVS 428
Cdd:COG4152 91 QLVYLARlkglSK--AEAKRRAdEWLER----LGLG-DRANKKVEELSKGNQQKVQLIAALLHDPELLILDEPFSGLDPV 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2095916338 429 ARADIYQLLKSVAAQNVAVLMiSS----DVEEfvgLADRVLVMHQGR 471
Cdd:COG4152 164 NVELLKDVIRELAAKGTTVIF-SShqmeLVEE---LCDRIVIINKGR 206
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
19-194 |
2.43e-17 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 80.38 E-value: 2.43e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 19 VLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDSGELTIGERAFARLNPALAHQLgiYLVPQEPMLFPNLSVRE 98
Cdd:PRK13540 16 LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKQL--CFVGHRSGINPYLTLRE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 99 NILFRLpKRADTTARLQEKLQQLNCQINLDASASTLEVADQQMVEILRGLMREARILILDEPTASLTPGETERLFSQIRA 178
Cdd:PRK13540 94 NCLYDI-HFSPGAVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTIITKIQE 172
|
170
....*....|....*..
gi 2095916338 179 LQALDVGIVFISH-KLP 194
Cdd:PRK13540 173 HRAKGGAVLLTSHqDLP 189
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
275-471 |
2.50e-17 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 81.52 E-value: 2.50e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 275 LSLEIRAGEIVGLAGLVGSGRTEFAETLYGLRPpRAGRIWLENREISQESTrARLASGLVYLPEdrQVSGLFLdAPVrWN 354
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLLP-GSGSIQFAGQPLEAWSA-AELARHRAYLSQ--QQTPPFA-MPV-FQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 355 TVMFNQPSWWQQGKREAAVVERYHR-ALGIKLAdgdQPVRTLSGGNQQKVLLAR-CL----EANPL--LLIVDEPTRGVD 426
Cdd:PRK03695 89 YLTLHQPDKTRTEAVASALNEVAEAlGLDDKLG---RSVNQLSGGEWQRVRLAAvVLqvwpDINPAgqLLLLDEPMNSLD 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2095916338 427 VSARADIYQLLKSVAAQNVAVLMISSDVEEFVGLADRVLVMHQGR 471
Cdd:PRK03695 166 VAQQAALDRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGK 210
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
16-215 |
3.02e-17 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 84.51 E-value: 3.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 16 GVAVLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVeTPDSGELTIGERAFARLNPALAHQLgIYLVPQEPMLFPNlS 95
Cdd:PRK11174 362 GKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGF-LPYQGSLKINGIELRELDPESWRKH-LSWVGQNPQLPHG-T 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 96 VRENILFRLPKRADttARLQEKLQQ-------------LNCQINlDASAsTLEVADQQMVEILRGLMREARILILDEPTA 162
Cdd:PRK11174 439 LRDNVLLGNPDASD--EQLQQALENawvseflpllpqgLDTPIG-DQAA-GLSVGQAQRLALARALLQPCQLLLLDEPTA 514
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2095916338 163 SLTpGETERLFSQirALQALDVG--IVFISHKLPEIRQLaSHVSVMRDGAVVLSG 215
Cdd:PRK11174 515 SLD-AHSEQLVMQ--ALNAASRRqtTLMVTHQLEDLAQW-DQIWVMQDGQIVQQG 565
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
253-467 |
3.05e-17 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 81.29 E-value: 3.05e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 253 RTQAQDFPVLRvedltgegfiDLSLEIRAGEIVGLAGLVGSGRTefaeTL----YGLRPPRAGRIWLENREISQESTRAr 328
Cdd:COG1116 18 PTGGGGVTALD----------DVSLTVAAGEFVALVGPSGCGKS----TLlrliAGLEKPTSGEVLVDGKPVTGPGPDR- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 329 lasGLVYlpedrQVSGLFldaPvrWNTV----MFNQPswwQQGKREAAVVERYHRALG-IKLAD-GDQPVRTLSGGNQQK 402
Cdd:COG1116 83 ---GVVF-----QEPALL---P--WLTVldnvALGLE---LRGVPKAERRERARELLElVGLAGfEDAYPHQLSGGMRQR 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2095916338 403 VLLARCLEANPLLLIVDEPTRGVDVSARADIYQLLKSV-AAQNVAVLMISSDVEEFVGLADRVLVM 467
Cdd:COG1116 147 VAIARALANDPEVLLMDEPFGALDALTRERLQDELLRLwQETGKTVLFVTHDVDEAVFLADRVVVL 212
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
4-215 |
3.05e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 81.82 E-value: 3.05e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 4 LLEARQIRKQFS-GVAVLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDSGELTIGERAFARLNPALAH-QLGI 81
Cdd:PRK13636 5 ILKVEELNYNYSdGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRKGLMKlRESV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 82 YLVPQEP--MLFpNLSVRENILF-----RLPKRaDTTARLQEKLQQLNCQINLDASASTLEVADQQMVEILRGLMREARI 154
Cdd:PRK13636 85 GMVFQDPdnQLF-SASVYQDVSFgavnlKLPED-EVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKV 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2095916338 155 LILDEPTASLTP-GETERLFSQIRALQALDVGIVFISHKLPEIRQLASHVSVMRDGAVVLSG 215
Cdd:PRK13636 163 LVLDEPTAGLDPmGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQG 224
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
274-471 |
3.37e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 81.58 E-value: 3.37e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 274 DLSLEIRAGEIVGLAGLVGSGRTEFAETLYGLRPPRAGRIWLENREISQES-TRARLASGLVYLPEDRQVSGLFLDAPVR 352
Cdd:PRK13632 27 NVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENlKEIRKKIGIIFQNPDNQFIGATVEDDIA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 353 WNTVMFNQPSwwqqgKREAAVVERYHRALGIKLADGDQPvRTLSGGNQQKVLLARCLEANPLLLIVDEPTRGVDVSARAD 432
Cdd:PRK13632 107 FGLENKKVPP-----KKMKDIIDDLAKKVGMEDYLDKEP-QNLSGGQKQRVAIASVLALNPEIIIFDESTSMLDPKGKRE 180
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2095916338 433 IYQLLKSVAAQNVAVLM-ISSDVEEFVgLADRVLVMHQGR 471
Cdd:PRK13632 181 IKKIMVDLRKTRKKTLIsITHDMDEAI-LADKVIVFSEGK 219
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
19-215 |
3.99e-17 |
|
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: 80.74 E-value: 3.99e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 19 VLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDSGELTIGERAFARLN-PALAHQLGIylVPQEPMLFpNLSVR 97
Cdd:cd03253 16 VLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTlDSLRRAIGV--VPQDTVLF-NDTIG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 98 ENILFRLPK-------RADTTARLQEKLQQLNCQINLDASASTLEVA--DQQMVEILRGLMREARILILDEPTASLTPgE 168
Cdd:cd03253 93 YNIRYGRPDatdeeviEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSggEKQRVAIARAILKNPPILLLDEATSALDT-H 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2095916338 169 TERLFsqIRALQALDVG--IVFISHKLPEIRQlASHVSVMRDGAVVLSG 215
Cdd:cd03253 172 TEREI--QAALRDVSKGrtTIVIAHRLSTIVN-ADKIIVLKDGRIVERG 217
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
258-471 |
7.00e-17 |
|
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: 79.97 E-value: 7.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 258 DFPVLRvedltgegfiDLSLEIRAGEIVGLAGLVGSGRTEFAETLYGLRPPRAGRIWLEN---REISQESTRARLAsglv 334
Cdd:cd03253 13 GRPVLK----------DVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGqdiREVTLDSLRRAIG---- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 335 YLPEDrqvSGLFLDapvrwnTVMFN----QPSWWQQGKREAAVVERYHRALgIKLADGDQPV---R--TLSGGNQQKVLL 405
Cdd:cd03253 79 VVPQD---TVLFND------TIGYNirygRPDATDEEVIEAAKAAQIHDKI-MRFPDGYDTIvgeRglKLSGGEKQRVAI 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2095916338 406 ARCLEANPLLLIVDEPTRGVDVSARADIYQLLKSVAAqNVAVLMISSDVEEFVGlADRVLVMHQGR 471
Cdd:cd03253 149 ARAILKNPPILLLDEATSALDTHTEREIQAALRDVSK-GRTTIVIAHRLSTIVN-ADKIIVLKDGR 212
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
19-427 |
7.04e-17 |
|
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: 83.45 E-value: 7.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 19 VLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDSGEltigerafARLNPalahqlGI---YLvPQEPMLFPNLS 95
Cdd:TIGR03719 20 ILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGE--------ARPQP------GIkvgYL-PQEPQLDPTKT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 96 VRENI-------------------LFRLP-----KRADTTARLQEKLQ-----QLNCQINL----------DASASTLEV 136
Cdd:TIGR03719 85 VRENVeegvaeikdaldrfneisaKYAEPdadfdKLAAEQAELQEIIDaadawDLDSQLEIamdalrcppwDADVTKLSG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 137 ADQQMVEILRGLMREARILILDEPTASLTPGETERLfsqIRALQALDVGIVFISHKlpeiRQLASHVS-----VMRDGAV 211
Cdd:TIGR03719 165 GERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWL---ERHLQEYPGTVVAVTHD----RYFLDNVAgwileLDRGRGI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 212 VLSGETAGYGDQQL----ISAMTPASRDHALSDTQKLWLALPGNRRT------------QAQDFP--------------- 260
Cdd:TIGR03719 238 PWEGNYSSWLEQKQkrleQEEKEESARQKTLKRELEWVRQSPKGRQAkskarlaryeelLSQEFQkrnetaeiyippgpr 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 261 ----VLRVEDLT-GEG----FIDLSLEIRAGEIVGLAGLVGSGRTEFAETLYGLRPPRAGRIwlenrEISqESTRarlas 331
Cdd:TIGR03719 318 lgdkVIEAENLTkAFGdkllIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTI-----EIG-ETVK----- 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 332 gLVYLPEDRQVsglfLDAPvrwNTVmfnqpswWQQ----------GKREaaVVER-YHRALGIKLADGDQPVRTLSGGNQ 400
Cdd:TIGR03719 387 -LAYVDQSRDA----LDPN---KTV-------WEEisggldiiklGKRE--IPSRaYVGRFNFKGSDQQKKVGQLSGGER 449
|
490 500
....*....|....*....|....*....
gi 2095916338 401 QKVLLARCLE--ANPLLLivDEPTRGVDV 427
Cdd:TIGR03719 450 NRVHLAKTLKsgGNVLLL--DEPTNDLDV 476
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
2-212 |
7.39e-17 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 83.19 E-value: 7.39e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 2 KPLLEARQIRKQFSGVAVLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDSGELTIGERAfarlnpalahQLGI 81
Cdd:COG0488 313 KKVLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGETV----------KIGY 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 82 YlvPQEP-MLFPNLSVRENILFRLPKRADTTARlqeklqqlncqinldasaSTLE----VADQQM--VEILRG------- 147
Cdd:COG0488 383 F--DQHQeELDPDKTVLDELRDGAPGGTEQEVR------------------GYLGrflfSGDDAFkpVGVLSGgekarla 442
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2095916338 148 ----LMREARILILDEPT-----ASLtpgetERLfsqIRALQALDVGIVFISH--KLpeIRQLASHVSVMRDGAVV 212
Cdd:COG0488 443 laklLLSPPNVLLLDEPTnhldiETL-----EAL---EEALDDFPGTVLLVSHdrYF--LDRVATRILEFEDGGVR 508
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
274-471 |
7.61e-17 |
|
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: 79.55 E-value: 7.61e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 274 DLSLEIRAGEIVGLAGLVGSGRTEFAETLYGLRPPRAGRIWLENREISQESTR----ARLASGLVYlpedrQVSGLFLDA 349
Cdd:cd03258 23 DVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKelrkARRRIGMIF-----QHFNLLSSR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 350 PVRWNtVMFNQPSWwqqGKREAAVVERYHRALG-IKLAD-GDQPVRTLSGGNQQKVLLARCLEANPLLLIVDEPTRGVDV 427
Cdd:cd03258 98 TVFEN-VALPLEIA---GVPKAEIEERVLELLElVGLEDkADAYPAQLSGGQKQRVGIARALANNPKVLLCDEATSALDP 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2095916338 428 SARADIYQLLKSVAAQ-NVAVLMISSDVEEFVGLADRVLVMHQGR 471
Cdd:cd03258 174 ETTQSILALLRDINRElGLTIVLITHEMEVVKRICDRVAVMEKGE 218
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
274-469 |
1.29e-16 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 79.39 E-value: 1.29e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 274 DLSLEIRAGEIVGLAGLVGSGRTEFAETLYGLRPPRAGRIwlenreisQESTRARLAsglvYLPEDrqvsgLFLDA--PV 351
Cdd:PRK09544 22 DVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI--------KRNGKLRIG----YVPQK-----LYLDTtlPL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 352 RWNTVMFNQPswwqqGKREAAVVERYHRALGIKLADgdQPVRTLSGGNQQKVLLARCLEANPLLLIVDEPTRGVDVSARA 431
Cdd:PRK09544 85 TVNRFLRLRP-----GTKKEDILPALKRVQAGHLID--APMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQV 157
|
170 180 190
....*....|....*....|....*....|....*....
gi 2095916338 432 DIYQLLKSVAAQ-NVAVLMISSDVEEFVGLADRVLVMHQ 469
Cdd:PRK09544 158 ALYDLIDQLRRElDCAVLMVSHDLHLVMAKTDEVLCLNH 196
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
8-211 |
1.38e-16 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 81.23 E-value: 1.38e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 8 RQIRKQFSGVAVLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDSGELTIGERafaRLNPALAHQLGIYLVPQE 87
Cdd:PRK11000 7 RNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEK---RMNDVPPAERGVGMVFQS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 88 PMLFPNLSVRENILFRLP----KRADTTARLQEKLQQLNCQINLDASASTLEVADQQMVEILRGLMREARILILDEPTAS 163
Cdd:PRK11000 84 YALYPHLSVAENMSFGLKlagaKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSN 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2095916338 164 LTPGETERLFSQIRAL-QALDVGIVFISHKLPEIRQLASHVSVMRDGAV 211
Cdd:PRK11000 164 LDAALRVQMRIEISRLhKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRV 212
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
274-470 |
1.48e-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: 78.66 E-value: 1.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 274 DLSLEIRAGEIVGLAGLVGSGRTEFAETLYGLRPPRAGRIWLENREIsQESTRARLasgLVYlpedrQVSGLFLDAPVRW 353
Cdd:TIGR01184 3 GVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQI-TEPGPDRM---VVF-----QNYSLLPWLTVRE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 354 NTVMFNQPSWWQQGKREAAVVERYHRAL-GIKLAdGDQPVRTLSGGNQQKVLLARCLEANPLLLIVDEPTRGVDVSARAD 432
Cdd:TIGR01184 74 NIALAVDRVLPDLSKSERRAIVEEHIALvGLTEA-ADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGN 152
|
170 180 190
....*....|....*....|....*....|....*....
gi 2095916338 433 IY-QLLKSVAAQNVAVLMISSDVEEFVGLADRVLVMHQG 470
Cdd:TIGR01184 153 LQeELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
5-221 |
1.54e-16 |
|
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: 77.98 E-value: 1.54e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 5 LEARQIRKQ------FSGVAVLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAG--VETPDSGELTIGERAFARLNPALA 76
Cdd:cd03213 4 LSFRNLTVTvksspsKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGrrTGLGVSGEVLINGRPLDKRSFRKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 77 hqlgIYLVPQEPMLFPNLSVRENILFrlpkradtTARLQeklqqlncqinldaSASTLEvadQQMVEILRGLMREARILI 156
Cdd:cd03213 84 ----IGYVPQDDILHPTLTVRETLMF--------AAKLR--------------GLSGGE---RKRVSIALELVSNPSLLF 134
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2095916338 157 LDEPTASLTPGETERLFSQIRALQALDVGIVFISHklpeirQLASHVSVMRDGAVVLS-GETAGYG 221
Cdd:cd03213 135 LDEPTSGLDSSSALQVMSLLRRLADTGRTIICSIH------QPSSEIFELFDKLLLLSqGRVIYFG 194
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
274-471 |
1.82e-16 |
|
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: 78.53 E-value: 1.82e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 274 DLSLEIRAGEIVGLAGLVGSGRTEFAETLYGLRPPRAGRIwlenreisqestraRLAsGLVylPEDRQvsglflDAPVRW 353
Cdd:cd03267 39 GISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEV--------------RVA-GLV--PWKRR------KKFLRR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 354 NTVMFNQPS--WWQQGKREAAVV---------ERYHRALGiKLADG-------DQPVRTLSGGNQQKVLLARCLEANPLL 415
Cdd:cd03267 96 IGVVFGQKTqlWWDLPVIDSFYLlaaiydlppARFKKRLD-ELSELldleellDTPVRQLSLGQRMRAEIAAALLHEPEI 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2095916338 416 LIVDEPTRGVDVSARADIYQLLKS-VAAQNVAVLMISSDVEEFVGLADRVLVMHQGR 471
Cdd:cd03267 175 LFLDEPTIGLDVVAQENIRNFLKEyNRERGTTVLLTSHYMKDIEALARRVLVIDKGR 231
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
17-471 |
1.96e-16 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 82.21 E-value: 1.96e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 17 VAVLKGIDFTLCAGQVHALMGGNGAGKS----TLMKII--AGVETpDSGELTIGERA--FARLNPALAHQL------GIY 82
Cdd:PRK10261 29 IAAVRNLSFSLQRGETLAIVGESGSGKSvtalALMRLLeqAGGLV-QCDKMLLRRRSrqVIELSEQSAAQMrhvrgaDMA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 83 LVPQEPM--LFPNLSVRENIL--FRLPKRADTTARLQEKLQQLNcQINLDASASTLEVADQQM-------VEILRGLMRE 151
Cdd:PRK10261 108 MIFQEPMtsLNPVFTVGEQIAesIRLHQGASREEAMVEAKRMLD-QVRIPEAQTILSRYPHQLsggmrqrVMIAMALSCR 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 152 ARILILDEPTASLTPGETERLFSQIRALQA-LDVGIVFISHKLPEIRQLASHVSVMRDGAVVLSG--ETAGYGDQ----Q 224
Cdd:PRK10261 187 PAVLIADEPTTALDVTIQAQILQLIKVLQKeMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGsvEQIFHAPQhpytR 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 225 LISAMTP---ASRDHALSDTQKL-WLALPGNRRTQA-QDF-----PVLRVEDLTGE-----GFID-----------LSLE 278
Cdd:PRK10261 267 ALLAAVPqlgAMKGLDYPRRFPLiSLEHPAKQEPPIeQDTvvdgePILQVRNLVTRfplrsGLLNrvtrevhavekVSFD 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 279 IRAGEIVGLAGLVGSGRTEFAETLYGLRPPRAGRIWLENREISQESTRA--RLASGLVYLPED-------RQVSGLFLDA 349
Cdd:PRK10261 347 LWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKlqALRRDIQFIFQDpyasldpRQTVGDSIME 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 350 PVRWNTVMfnqpswwqQGKREAAVVERYHRALGIKLADGDQPVRTLSGGNQQKVLLARCLEANPLLLIVDEPTRGVDVSA 429
Cdd:PRK10261 427 PLRVHGLL--------PGKAAAARVAWLLERVGLLPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSI 498
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 2095916338 430 RADIYQLLKSVAAQ-NVAVLMISSDVEEFVGLADRVLVMHQGR 471
Cdd:PRK10261 499 RGQIINLLLDLQRDfGIAYLFISHDMAVVERISHRVAVMYLGQ 541
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
19-212 |
2.39e-16 |
|
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: 77.92 E-value: 2.39e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 19 VLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDSGELTIGERAFARLNP-ALAHQLGIylVPQEPMLFPNlSVR 97
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLhDLRSRISI--IPQDPVLFSG-TIR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 98 ENI----------LFRLPKRADTTARLQEKLQQLNCQInlDASASTLEVADQQMVEILRGLMREARILILDEPTASLTPg 167
Cdd:cd03244 96 SNLdpfgeysdeeLWQALERVGLKEFVESLPGGLDTVV--EEGGENLSVGQRQLLCLARALLRKSKILVLDEATASVDP- 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2095916338 168 ETERLFSQ-IRALQAlDVGIVFISHKLPEIrqLASH-VSVMRDGAVV 212
Cdd:cd03244 173 ETDALIQKtIREAFK-DCTVLTIAHRLDTI--IDSDrILVLDKGRVV 216
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
2-193 |
2.67e-16 |
|
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: 81.25 E-value: 2.67e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 2 KPLLEARQIRKQFSGVA-VLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDSGELTIGERAFARLNPALAHQLg 80
Cdd:TIGR02868 332 KPTLELRDLSAGYPGAPpVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRR- 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 81 IYLVPQEPMLFpNLSVRENILFRLPKRAD-------TTARLQEKLQQLNCQIN--LDASASTLEVADQQMVEILRGLMRE 151
Cdd:TIGR02868 411 VSVCAQDAHLF-DTTVRENLRLARPDATDeelwaalERVGLADWLRALPDGLDtvLGEGGARLSGGERQRLALARALLAD 489
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2095916338 152 ARILILDEPTASLTPGETERLFSQIraLQALD-VGIVFISHKL 193
Cdd:TIGR02868 490 APILLLDEPTEHLDAETADELLEDL--LAALSgRTVVLITHHL 530
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
6-105 |
3.53e-16 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 78.20 E-value: 3.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 6 EARQIRKQFSGVAVLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDSGELTIGERAFARLNPA-LAHQLGIylV 84
Cdd:COG4604 3 EIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSReLAKRLAI--L 80
|
90 100
....*....|....*....|..
gi 2095916338 85 PQEPMLFPNLSVRENILF-RLP 105
Cdd:COG4604 81 RQENHINSRLTVRELVAFgRFP 102
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
274-471 |
3.74e-16 |
|
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: 77.66 E-value: 3.74e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 274 DLSLEIRAGEIVGLAGLVGSGRTEFAETLYGLRPPRAGRIWLENREISQestrarlasglvYLPEDRQVSGLFldapvrW 353
Cdd:cd03300 18 GVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITN------------LPPHKRPVNTVF------Q 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 354 NTVMFNQPSWWQ--------QGKREAAVVERYHRALG-IKLAD-GDQPVRTLSGGNQQKVLLARCLEANPLLLIVDEPTR 423
Cdd:cd03300 80 NYALFPHLTVFEniafglrlKKLPKAEIKERVAEALDlVQLEGyANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLG 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2095916338 424 GVDVSARADIYQLLKSVAAQ-NVAVLMISSDVEEFVGLADRVLVMHQGR 471
Cdd:cd03300 160 ALDLKLRKDMQLELKRLQKElGITFVFVTHDQEEALTMSDRIAVMNKGK 208
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
19-215 |
4.91e-16 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 80.64 E-value: 4.91e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 19 VLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDSGELTIGERAFARLN-PALAHQlgIYLVPQEPMLFpNLSVR 97
Cdd:PRK11160 355 VLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSeAALRQA--ISVVSQRVHLF-SATLR 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 98 ENILFRLPKRADttARLQEKLQQLNCQINLDASAS----------TLEVADQQMVEILRGLMREARILILDEPTASLTPg 167
Cdd:PRK11160 432 DNLLLAAPNASD--EALIEVLQQVGLEKLLEDDKGlnawlgeggrQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDA- 508
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2095916338 168 ETERlfsQIRAL---QALDVGIVFISHKLPEIRQLaSHVSVMRDGAVVLSG 215
Cdd:PRK11160 509 ETER---QILELlaeHAQNKTVLMITHRLTGLEQF-DRICVMDNGQIIEQG 555
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
19-215 |
5.79e-16 |
|
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: 77.14 E-value: 5.79e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 19 VLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDSGELTIGERAFARLNPA-LAHQLGIYLvpQEPMLFpNLSVR 97
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAwLRRQVGVVL--QENVLF-NRSIR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 98 ENILFRLP----KRADTTARL---QEKLQQLNCQIN--LDASASTLEVADQQMVEILRGLMREARILILDEPTASLTPgE 168
Cdd:cd03252 94 DNIALADPgmsmERVIEAAKLagaHDFISELPEGYDtiVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATSALDY-E 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2095916338 169 TERLFsqIRALQALDVG--IVFISHKLPEIRQlASHVSVMRDGAVVLSG 215
Cdd:cd03252 173 SEHAI--MRNMHDICAGrtVIIIAHRLSTVKN-ADRIIVMEKGRIVEQG 218
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-225 |
5.91e-16 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 77.66 E-value: 5.91e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 1 MKPLLEARQIRKQFSGVAVLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDSGELTIGERA-----FARLNPAL 75
Cdd:PRK11701 3 DQPLLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDgqlrdLYALSEAE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 76 AHQL-----GIylVPQEPM--LFPNLSVRENILFRLPKRADTT-ARLQEKLQQLNCQINLDAS-----ASTLEVADQQMV 142
Cdd:PRK11701 83 RRRLlrtewGF--VHQHPRdgLRMQVSAGGNIGERLMAVGARHyGDIRATAGDWLERVEIDAAriddlPTTFSGGMQQRL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 143 EILRGLMREARILILDEPTASLTPGETERLFSQIRALQA-LDVGIVFISHKLPEIRQLASHVSVMRDGAVVLSGETagyg 221
Cdd:PRK11701 161 QIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVReLGLAVVIVTHDLAVARLLAHRLLVMKQGRVVESGLT---- 236
|
....
gi 2095916338 222 DQQL 225
Cdd:PRK11701 237 DQVL 240
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
30-466 |
6.45e-16 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 80.24 E-value: 6.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 30 GQVHALMGGNGAGKSTLMKIIAGVETPDSG----ELTIGE--RAFA--------------RLNPALAHQlgiYlVPQEPM 89
Cdd:PRK13409 99 GKVTGILGPNGIGKTTAVKILSGELIPNLGdyeeEPSWDEvlKRFRgtelqnyfkklyngEIKVVHKPQ---Y-VDLIPK 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 90 LFpNLSVREnilfrLPKRADTTARLQEKLQQLNCQINLDASASTLEVADQQMVEILRGLMREARILILDEPTASLTPGET 169
Cdd:PRK13409 175 VF-KGKVRE-----LLKKVDERGKLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRQR 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 170 ERLFSQIRALqALDVGIVFISHKLPEIRQLAshvsvmrDGAVVLSGETAGYGdqqLISamTPAS---------------- 233
Cdd:PRK13409 249 LNVARLIREL-AEGKYVLVVEHDLAVLDYLA-------DNVHIAYGEPGAYG---VVS--KPKGvrvgineylkgylpee 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 234 ----RDHALSDTQKlwlalPGNRRTQAQdfPVLRVEDLTGEgFIDLSL-----EIRAGEIVGLAGLVGSGRTEFAETLYG 304
Cdd:PRK13409 316 nmriRPEPIEFEER-----PPRDESERE--TLVEYPDLTKK-LGDFSLeveggEIYEGEVIGIVGPNGIGKTTFAKLLAG 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 305 LRPPRAGRIWLENReISqestrarlasglvYLPE------DRQVSGLFLDAPVRWNTvmfnqpSWWQQgkreaAVVERyh 378
Cdd:PRK13409 388 VLKPDEGEVDPELK-IS-------------YKPQyikpdyDGTVEDLLRSITDDLGS------SYYKS-----EIIKP-- 440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 379 raLGI-KLADgdQPVRTLSGGNQQKVLLARCL--EANplLLIVDEPTRGVDVSARADIYQLLKSVAAQN-VAVLMISSDV 454
Cdd:PRK13409 441 --LQLeRLLD--KNVKDLSGGELQRVAIAACLsrDAD--LYLLDEPSAHLDVEQRLAVAKAIRRIAEEReATALVVDHDI 514
|
490
....*....|..
gi 2095916338 455 EEFVGLADRVLV 466
Cdd:PRK13409 515 YMIDYISDRLMV 526
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
262-471 |
7.11e-16 |
|
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: 76.84 E-value: 7.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 262 LRVEDLT---GEGFI--DLSLEIRAGEIVGLAGLVGSGRTEFAETLYGLRP-----PRAGRIWLENREISQESTRarlas 331
Cdd:cd03260 1 IELRDLNvyyGDKHAlkDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIYDLDVD----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 332 gLVYLPedRQVSGLFLDAPVRWNTVMFN--QPSWWQQGKREAAVVERYHRALGI-----KLADgDQPVRTLSGGNQQKVL 404
Cdd:cd03260 76 -VLELR--RRVGMVFQKPNPFPGSIYDNvaYGLRLHGIKLKEELDERVEEALRKaalwdEVKD-RLHALGLSGGQQQRLC 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2095916338 405 LARCLEANPLLLIVDEPTRGVDVSARADIYQLLKSvAAQNVAVLMISSDVEEFVGLADRVLVMHQGR 471
Cdd:cd03260 152 LARALANEPEVLLLDEPTSALDPISTAKIEELIAE-LKKEYTIVIVTHNMQQAARVADRTAFLLNGR 217
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1-225 |
7.12e-16 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 77.36 E-value: 7.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 1 MKPLLEARQIRKQFSGVAVLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDS---------GELTIGERAFAR- 70
Cdd:PRK09984 1 MQTIIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKsagshiellGRTVQREGRLARd 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 71 LNPALAHQLGIYlvpQEPMLFPNLSVRENIL---------FRLPKRADTTARLQEKLQQLNcQINLDASA----STLEVA 137
Cdd:PRK09984 81 IRKSRANTGYIF---QQFNLVNRLSVLENVLigalgstpfWRTCFSWFTREQKQRALQALT-RVGMVHFAhqrvSTLSGG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 138 DQQMVEILRGLMREARILILDEPTASLTPGETERLFSQIRALQALD-VGIVFISHKLPEIRQLASHVSVMRDGAVVLSGE 216
Cdd:PRK09984 157 QQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDgITVVVTLHQVDYALRYCERIVALRQGHVFYDGS 236
|
....*....
gi 2095916338 217 TAGYGDQQL 225
Cdd:PRK09984 237 SQQFDNERF 245
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
273-494 |
8.92e-16 |
|
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: 78.60 E-value: 8.92e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 273 IDLSLEIRAGEIVGLAGLVGSGRTEFAETLYGLRPPRAGRIWLeNREISQESTRArlasglVYLP-EDRQVSGLFLDAP- 350
Cdd:COG4148 16 LDVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRL-GGEVLQDSARG------IFLPpHRRRIGYVFQEARl 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 351 -----VRWNtVMFNQPSWWQQGKRE--AAVVERyhraLGIK--LadgDQPVRTLSGGNQQKVLLARCLEANPLLLIVDEP 421
Cdd:COG4148 89 fphlsVRGN-LLYGRKRAPRAERRIsfDEVVEL----LGIGhlL---DRRPATLSGGERQRVAIGRALLSSPRLLLMDEP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 422 TRGVDVSARADIYQLLKSVAAQ-NVAVLMISSDVEEFVGLADRVLVMHQGR--HSGELA--------------RQAVTV- 483
Cdd:COG4148 161 LAALDLARKAEILPYLERLRDElDIPILYVSHSLDEVARLADHVVLLEQGRvvASGPLAevlsrpdllplaggEEAGSVl 240
|
250 260
....*....|....*....|.
gi 2095916338 484 ----------DRMMTLAFGGQ 494
Cdd:COG4148 241 eatvaahdpdYGLTRLALGGG 261
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
14-458 |
9.10e-16 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 79.99 E-value: 9.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 14 FSGVAVLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDSGELTI-GERAFARL--NP----------------- 73
Cdd:PRK11147 13 FSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYeQDLIVARLqqDPprnvegtvydfvaegie 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 74 ALAHQLGIY-----LVPQEPMlfpnlsvrENILFRLpkradttARLQEKLQQLNC------------QINLDASA--STL 134
Cdd:PRK11147 93 EQAEYLKRYhdishLVETDPS--------EKNLNEL-------AKLQEQLDHHNLwqlenrinevlaQLGLDPDAalSSL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 135 EVADQQMVEILRGLMREARILILDEPTASLTPGETERLFSQIRALQAldvGIVFISHKLPEIRQLASHVsVMRDGAVVLS 214
Cdd:PRK11147 158 SGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQG---SIIFISHDRSFIRNMATRI-VDLDRGKLVS 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 215 --GETAGYGDQQ----LISAMTPASRDHALSDtQKLWL----------------ALPGNRRTQAQDFPV-----LRVEDL 267
Cdd:PRK11147 234 ypGNYDQYLLEKeealRVEELQNAEFDRKLAQ-EEVWIrqgikarrtrnegrvrALKALRRERSERREVmgtakMQVEEA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 268 TGEGFI------------------DLSLEIRAGEIVGLAGLVGSGRTEFAETLYGLRPPRAGRIwlenreisQESTRARL 329
Cdd:PRK11147 313 SRSGKIvfemenvnyqidgkqlvkDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRI--------HCGTKLEV 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 330 AsglvYLPEDRQVsglfLDaPVRwnTVMFNqpswWQQGKREAAVVERYHRALGIkLAD-------GDQPVRTLSGGNQQK 402
Cdd:PRK11147 385 A----YFDQHRAE----LD-PEK--TVMDN----LAEGKQEVMVNGRPRHVLGY-LQDflfhpkrAMTPVKALSGGERNR 448
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 2095916338 403 VLLARCLEANPLLLIVDEPTRGVDVsaraDIYQLLKSVAAQNVAVLMISSDVEEFV 458
Cdd:PRK11147 449 LLLARLFLKPSNLLILDEPTNDLDV----ETLELLEELLDSYQGTVLLVSHDRQFV 500
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
3-215 |
1.18e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 77.10 E-value: 1.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 3 PLLEARQIRKQFSGVA--VLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDSGELTIGERAFARLN-PALAHQL 79
Cdd:PRK13648 6 SIIVFKNVSFQYQSDAsfTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNfEKLRKHI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 80 GIylVPQEP-MLFPNLSVRENILFRLPKRADTTARLQEKLQQLNCQINL----DASASTLEVADQQMVEILRGLMREARI 154
Cdd:PRK13648 86 GI--VFQNPdNQFVGSIVKYDVAFGLENHAVPYDEMHRRVSEALKQVDMleraDYEPNALSGGQKQRVAIAGVLALNPSV 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2095916338 155 LILDEPTASLTPGETERLFSQIRALQA-LDVGIVFISHKLPEIRQlASHVSVMRDGAVVLSG 215
Cdd:PRK13648 164 IILDEATSMLDPDARQNLLDLVRKVKSeHNITIISITHDLSEAME-ADHVIVMNKGTVYKEG 224
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
5-212 |
1.29e-15 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 78.22 E-value: 1.29e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 5 LEARQIRKQFSGVAVLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDSGELTI-GERAFARlnpaLAHQLGIYL 83
Cdd:PRK11432 7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIdGEDVTHR----SIQQRDICM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 84 VPQEPMLFPNLSVRENILFRLP----KRADTTARLQEKLQQLNCQINLDASASTLEVADQQMVEILRGLMREARILILDE 159
Cdd:PRK11432 83 VFQSYALFPHMSLGENVGYGLKmlgvPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDE 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2095916338 160 PTASLTPGETERLFSQIRALQ-ALDVGIVFISHKLPEIRQLASHVSVMRDGAVV 212
Cdd:PRK11432 163 PLSNLDANLRRSMREKIRELQqQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIM 216
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
4-215 |
1.37e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 76.77 E-value: 1.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 4 LLEARQIRKQFSG-VAVLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDSGELTIGERAFARLNPALAHQLgIY 82
Cdd:PRK13652 3 LIETRDLCYSYSGsKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKF-VG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 83 LVPQEP--MLFpNLSVRENILF---RLPKRADTTA-RLQEKLQQLNCQINLDASASTLEVADQQMVEILRGLMREARILI 156
Cdd:PRK13652 82 LVFQNPddQIF-SPTVEQDIAFgpiNLGLDEETVAhRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 157 LDEPTASLTPGETERLFSQIRAL-QALDVGIVFISHKLPEIRQLASHVSVMRDGAVVLSG 215
Cdd:PRK13652 161 LDEPTAGLDPQGVKELIDFLNDLpETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYG 220
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
274-471 |
1.45e-15 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 76.44 E-value: 1.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 274 DLSLEIRAGEIVGLAGLVGSGRTEFAETLYGLRPPRAGRIWLENREISQESTrarlasglvylpeDRQVsgLFL-DAPVR 352
Cdd:COG4525 25 DVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGA-------------DRGV--VFQkDALLP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 353 WNTVMFNQPSWWQ-QGKREAAVVERYHRALG-IKLAD-GDQPVRTLSGGNQQKVLLARCLEANPLLLIVDEPTRGVDVSA 429
Cdd:COG4525 90 WLNVLDNVAFGLRlRGVPKAERRARAEELLAlVGLADfARRRIWQLSGGMRQRVGIARALAADPRFLLMDEPFGALDALT 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2095916338 430 RADIYQLLKSV-AAQNVAVLMISSDVEEFVGLADRVLVM--HQGR 471
Cdd:COG4525 170 REQMQELLLDVwQRTGKGVFLITHSVEEALFLATRLVVMspGPGR 214
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
274-471 |
1.65e-15 |
|
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: 75.77 E-value: 1.65e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 274 DLSLEIRAGEIVGLAGLVGSGRTEFAETLYGLRPPRA---GRIWLENREISQESTRARLAsglvYLPE-DRQVSGLFLDA 349
Cdd:cd03234 25 DVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGttsGQILFNGQPRKPDQFQKCVA----YVRQdDILLPGLTVRE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 350 PVRWnTVMFNQPSWWQQGKREAAVVERYHRALGIKLAdGDQPVRTLSGGNQQKVLLARCLEANPLLLIVDEPTRGVDVSA 429
Cdd:cd03234 101 TLTY-TAILRLPRKSSDAIRKKRVEDVLLRDLALTRI-GGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFT 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2095916338 430 RADIYQLLKSVAAQNVAVLMI----SSDVEEfvgLADRVLVMHQGR 471
Cdd:cd03234 179 ALNLVSTLSQLARRNRIVILTihqpRSDLFR---LFDRILLLSSGE 221
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
20-216 |
1.76e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 76.62 E-value: 1.76e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 20 LKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDSGELTIGERAFARLNPALAH---QLGiyLVPQEP--MLFPNl 94
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKLSDirkKVG--LVFQYPeyQLFEE- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 95 SVRENILFRlPKR-----ADTTARLQE--KLQQLNCQINLDASASTLEVADQQMVEILRGLMREARILILDEPTASLTPG 167
Cdd:PRK13637 100 TIEKDIAFG-PINlglseEEIENRVKRamNIVGLDYEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPK 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2095916338 168 ETERLFSQIRALQ-ALDVGIVFISHKLPEIRQLASHVSVMRDGAVVLSGE 216
Cdd:PRK13637 179 GRDEILNKIKELHkEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGT 228
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
2-209 |
2.03e-15 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 75.62 E-value: 2.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 2 KPLLEARQIRKQFS----GVAVLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDSGELTIGERAFARLNPALA- 76
Cdd:PRK11629 3 KILLQCDNLCKRYQegsvQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKa 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 77 ----HQLG-IYlvpQEPMLFPNLSVRENILFRLPKRADTTARLQEKLQQLNCQINLDASA----STLEVADQQMVEILRG 147
Cdd:PRK11629 83 elrnQKLGfIY---QFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRAnhrpSELSGGERQRVAIARA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2095916338 148 LMREARILILDEPTASLTPGETERLFSQIRALQALD-VGIVFISHKLPEIRQLASHVSvMRDG 209
Cdd:PRK11629 160 LVNNPRLVLADEPTGNLDARNADSIFQLLGELNRLQgTAFLVVTHDLQLAKRMSRQLE-MRDG 221
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
2-218 |
2.03e-15 |
|
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: 78.57 E-value: 2.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 2 KPLLEARQIRKQFSG-----------VAVLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVEtPDSGELTIGERAFAR 70
Cdd:COG4172 273 PPLLEARDLKVWFPIkrglfrrtvghVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLI-PSEGEIRFDGQDLDG 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 71 LNP----ALAHQLGIylVPQEPM--LFPNLSVRE------NILFRLPKRADTTARLQEKLQQlncqINLDAsastlEVAD 138
Cdd:COG4172 352 LSRralrPLRRRMQV--VFQDPFgsLSPRMTVGQiiaeglRVHGPGLSAAERRARVAEALEE----VGLDP-----AARH 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 139 Q----------QMVEILRGLMREARILILDEPTASLtpgetERlfS---QI----RALQA-LDVGIVFISHKLPEIRQLA 200
Cdd:COG4172 421 RyphefsggqrQRIAIARALILEPKLLVLDEPTSAL-----DV--SvqaQIldllRDLQReHGLAYLFISHDLAVVRALA 493
|
250
....*....|....*...
gi 2095916338 201 SHVSVMRDGAVVLSGETA 218
Cdd:COG4172 494 HRVMVMKDGKVVEQGPTE 511
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
270-471 |
2.12e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 76.41 E-value: 2.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 270 EGFIDLSLEIRAGEIVGLAGLVGSGRTEFAETLYGLRPPRAGRIWLENREISQEST-----RARLASGLVY-LPEdrqvS 343
Cdd:PRK13641 21 KGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGnknlkKLRKKVSLVFqFPE----A 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 344 GLFLDAPVRwnTVMFNQPSWW--QQGKREAAVveRYHRALGIKLADGDQPVRTLSGGNQQKVLLARCLEANPLLLIVDEP 421
Cdd:PRK13641 97 QLFENTVLK--DVEFGPKNFGfsEDEAKEKAL--KWLKKVGLSEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEP 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2095916338 422 TRGVDVSARADIYQLLKSVAAQNVAVLMISSDVEEFVGLADRVLVMHQGR 471
Cdd:PRK13641 173 AAGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGK 222
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
3-228 |
2.31e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 76.29 E-value: 2.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 3 PLLEARQIRKQFSGVAVLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETP-----DSGELTIGERAFARLNPALAH 77
Cdd:PRK14271 20 PAMAAVNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKvsgyrYSGDVLLGGRSIFNYRDVLEF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 78 QLGIYLVPQEPMLFPnLSVRENIL-----FRLPKRADTTARLQEKLQQLN----CQINLDASASTLEVADQQMVEILRGL 148
Cdd:PRK14271 100 RRRVGMLFQRPNPFP-MSIMDNVLagvraHKLVPRKEFRGVAQARLTEVGlwdaVKDRLSDSPFRLSGGQQQLLCLARTL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 149 MREARILILDEPTASLTPGETERLFSQIRALqALDVGIVFISHKLPEIRQLASHVSVMRDGAVVLSGETagygdQQLISA 228
Cdd:PRK14271 179 AVNPEVLLLDEPTSALDPTTTEKIEEFIRSL-ADRLTVIIVTHNLAQAARISDRAALFFDGRLVEEGPT-----EQLFSS 252
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
274-471 |
2.61e-15 |
|
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: 74.60 E-value: 2.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 274 DLSLEIRAGEIVGLAGLVGSGRTEFAETLYGLRPPRAGRIWLENREISQEStrarlasglvylPEDRQVSGLFLDAPVRW 353
Cdd:cd03301 18 DLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLP------------PKDRDIAMVFQNYALYP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 354 NTVMFNQPSW--WQQGKREAAVVERYHRA---LGIK--LadgDQPVRTLSGGNQQKVLLARCLEANPLLLIVDEPTRGVD 426
Cdd:cd03301 86 HMTVYDNIAFglKLRKVPKDEIDERVREVaelLQIEhlL---DRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLD 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2095916338 427 ----VSARADIYQLLKsvaAQNVAVLMISSDVEEFVGLADRVLVMHQGR 471
Cdd:cd03301 163 aklrVQMRAELKRLQQ---RLGTTTIYVTHDQVEAMTMADRIAVMNDGQ 208
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
274-485 |
2.91e-15 |
|
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: 75.30 E-value: 2.91e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 274 DLSLEIRAGEIVGLAGLVGSGRTEFAETLYGLRPPRAGRIWLENREISQESTRA----RLASGLVY----LPEDRQV--- 342
Cdd:cd03256 19 DVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKAlrqlRRQIGMIFqqfnLIERLSVlen 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 343 --SGLFldapVRWNT--VMFNQPSwwQQGKREA-AVVERyhraLGIkLADGDQPVRTLSGGNQQKVLLARCLEANPLLLI 417
Cdd:cd03256 99 vlSGRL----GRRSTwrSLFGLFP--KEEKQRAlAALER----VGL-LDKAYQRADQLSGGQQQRVAIARALMQQPKLIL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2095916338 418 VDEPTRGVDVSARADIYQLLKSVAAQ-NVAVLMISSDVEEFVGLADRVLVMHQGRHSGELARQAVTVDR 485
Cdd:cd03256 168 ADEPVASLDPASSRQVMDLLKRINREeGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAELTDEV 236
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
5-209 |
3.13e-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: 72.48 E-value: 3.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 5 LEARQIRKQFSGVAVLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDSGELTIGERafarlnpalahqLGIYLV 84
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGST------------VKIGYF 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 85 PQepmlfpnLSvrenilfrlpkradttarlqeklqqlncqinldasastlevADQQM-VEILRGLMREARILILDEPTAS 163
Cdd:cd03221 69 EQ-------LS-----------------------------------------GGEKMrLALAKLLLENPNLLLLDEPTNH 100
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2095916338 164 LTpgeterLFSQ---IRALQALDVGIVFISHKLPEIRQLASHVSVMRDG 209
Cdd:cd03221 101 LD------LESIealEEALKEYPGTVILVSHDRYFLDQVATKIIELEDG 143
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-215 |
3.79e-15 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 75.82 E-value: 3.79e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 1 MKPLLEARQIRKQFSGVA--VLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDSGELTIGERAfarLNPA---- 74
Cdd:PRK13635 2 KEEIIRVEHISFRYPDAAtyALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMV---LSEEtvwd 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 75 LAHQLGIylVPQEP-MLFPNLSVRENILFRLPK----RADTTARLQEKLQQLNCQINLDASASTLEVADQQMVEILRGLM 149
Cdd:PRK13635 79 VRRQVGM--VFQNPdNQFVGATVQDDVAFGLENigvpREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2095916338 150 REARILILDEPTASLTPGETERLFSQIRAL-QALDVGIVFISHKLPEIRQlASHVSVMRDGAVVLSG 215
Cdd:PRK13635 157 LQPDIIILDEATSMLDPRGRREVLETVRQLkEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEG 222
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
274-470 |
3.95e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 75.56 E-value: 3.95e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 274 DLSLEIRAGEIVGLAGLVGSGRTEFAETLYGLRPPRAGRIWLENREISQES-TRARLASGLVYLPEDRQvsglFLDAPVR 352
Cdd:PRK13648 27 DVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNfEKLRKHIGIVFQNPDNQ----FVGSIVK 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 353 WNtVMF---NQPSWWQQGKREAAV----VERYHRAlgikladgDQPVRTLSGGNQQKVLLARCLEANPLLLIVDEPTRGV 425
Cdd:PRK13648 103 YD-VAFgleNHAVPYDEMHRRVSEalkqVDMLERA--------DYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSML 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2095916338 426 DVSARADIYQLLKSVAA-QNVAVLMISSDVEEFVGlADRVLVMHQG 470
Cdd:PRK13648 174 DPDARQNLLDLVRKVKSeHNITIISITHDLSEAME-ADHVIVMNKG 218
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1-218 |
4.47e-15 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 75.21 E-value: 4.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 1 MKPLLEARQIRKQF---------SGVAVLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDSGELTIGERAFARL 71
Cdd:PRK15112 1 VETLLEVRNLSKTFryrtgwfrrQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 72 NPALAHQLgIYLVPQEPMLFPNLSVRENILFRLPKRADTTARLQEKLQQLNC---QINLDASAST-----LEVADQQMVE 143
Cdd:PRK15112 81 DYSYRSQR-IRMIFQDPSTSLNPRQRISQILDFPLRLNTDLEPEQREKQIIEtlrQVGLLPDHASyyphmLAPGQKQRLG 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2095916338 144 ILRGLMREARILILDEPTASLTPGETERLFSQIRALQALD-VGIVFISHKLPEIRQLASHVSVMRDGAVVLSGETA 218
Cdd:PRK15112 160 LARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQgISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTA 235
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
274-471 |
4.47e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 75.54 E-value: 4.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 274 DLSLEIRAGEIVGLAGLVGSGRTEFAETLYGLRPPRAGRIWLENREISQEST-RARLASGLVYLPEDRQvsglFLDAPVR 352
Cdd:PRK13650 25 DVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVwDIRHKIGMVFQNPDNQ----FVGATVE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 353 wNTVMFNQPSwwqQGKREAAVVERYHRAL---GIKLADGDQPVRtLSGGNQQKVLLARCLEANPLLLIVDEPTRGVDVSA 429
Cdd:PRK13650 101 -DDVAFGLEN---KGIPHEEMKERVNEALelvGMQDFKEREPAR-LSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEG 175
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2095916338 430 RADIYQLLKSVAAQ-NVAVLMISSDVEEfVGLADRVLVMHQGR 471
Cdd:PRK13650 176 RLELIKTIKGIRDDyQMTVISITHDLDE-VALSDRVLVMKNGQ 217
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
24-426 |
4.86e-15 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 77.36 E-value: 4.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 24 DFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDSGELTIGERAFARLNpalAHQLGiYLVPQE------PMLFPN---- 93
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLS---FEQLQ-KLVSDEwqrnntDMLSPGeddt 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 94 -LSVRENILfrlpKRADTTARLQEKLQQLNCQINLDASASTLEVADQQMVEILRGLMREARILILDEPTASLTPGETERL 172
Cdd:PRK10938 99 gRTTAEIIQ----DEVKDPARCEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 173 FSQIRALQALDVGIVFISHKLPEIRQLASHVSVMRDGAVVLSGETAGYGDQQLISAMTPA--------------SRDHAL 238
Cdd:PRK10938 175 AELLASLHQSGITLVLVLNRFDEIPDFVQFAGVLADCTLAETGEREEILQQALVAQLAHSeqlegvqlpepdepSARHAL 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 239 SDTQKLWLALPGNrrTQAQDFPVLRvedltgegfiDLSLEIRAGE---IVG---------LAGLVGSGRTEFAE--TLYG 304
Cdd:PRK10938 255 PANEPRIVLNNGV--VSYNDRPILH----------NLSWQVNPGEhwqIVGpngagkstlLSLITGDHPQGYSNdlTLFG 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 305 LRPPRAGRIWLENREISQESTRARLasglvylpeDRQVSglfldAPVRwNTVM---FNQPSWWQQ-GKREAAVVERYHRA 380
Cdd:PRK10938 323 RRRGSGETIWDIKKHIGYVSSSLHL---------DYRVS-----TSVR-NVILsgfFDSIGIYQAvSDRQQKLAQQWLDI 387
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 2095916338 381 LGIKLADGDQPVRTLSGGNQQKVLLARCLEANPLLLIVDEPTRGVD 426
Cdd:PRK10938 388 LGIDKRTADAPFHSLSWGQQRLALIVRALVKHPTLLILDEPLQGLD 433
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
260-495 |
7.23e-15 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 76.42 E-value: 7.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 260 PVLRVEDLT---GEGFI--DLSLEIRAGEIVGLAGLVGSGRTEFAETLYGLRPPRAGRIWLENREIsqESTRARLASGLV 334
Cdd:PRK09536 2 PMIDVSDLSvefGDTTVldGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDV--EALSARAASRRV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 335 -YLPEDRQVSglfLDAPVRWNTVMFNQP-----SWWQQGKReaAVVERYHRALGIKlADGDQPVRTLSGGNQQKVLLARC 408
Cdd:PRK09536 80 aSVPQDTSLS---FEFDVRQVVEMGRTPhrsrfDTWTETDR--AAVERAMERTGVA-QFADRPVTSLSGGERQRVLLARA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 409 L-EANPLLLIvDEPTRGVDVSARADIYQLLKSVAAQNVAVLMISSDVEEFVGLADRVLVMHQGR-HSGELARQAVTVDRM 486
Cdd:PRK09536 154 LaQATPVLLL-DEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRvRAAGPPADVLTADTL 232
|
....*....
gi 2095916338 487 MTlAFGGQA 495
Cdd:PRK09536 233 RA-AFDART 240
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
276-471 |
7.75e-15 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 73.36 E-value: 7.75e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 276 SLEIRAGEIVGLAGLVGSGRTEFAETLYGLRPPRAGRIWLENREISQESTRARLASGLVylpedrQVSGLFLDAPVRWNT 355
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPYQRPVSMLF------QENNLFAHLTVRQNI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 356 VMFNQPSW----WQQGKREAAVveryhRALGIkladGDQPVR---TLSGGNQQKVLLARCL-EANPLLLIvDEPTRGVDV 427
Cdd:TIGR01277 92 GLGLHPGLklnaEQQEKVVDAA-----QQVGI----ADYLDRlpeQLSGGQRQRVALARCLvRPNPILLL-DEPFSALDP 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2095916338 428 SARADIYQLLKSVAAQ-NVAVLMISSDVEEFVGLADRVLVMHQGR 471
Cdd:TIGR01277 162 LLREEMLALVKQLCSErQRTLLMVTHHLSDARAIASQIAVVSQGK 206
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
274-471 |
1.03e-14 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 73.94 E-value: 1.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 274 DLSLEIRAGEIVGLAGLVGSGRTEFAETLYGLRPPRAGRIWLENREIS--QESTR-----ARLasglvyLPedrqvsglf 346
Cdd:PRK11247 30 QLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAeaREDTRlmfqdARL------LP--------- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 347 ldapvrWNTVMFN-----QPSWwqqgkREAAvveryHRAL-GIKLAD--GDQPVrTLSGGNQQKVLLARCLEANPLLLIV 418
Cdd:PRK11247 95 ------WKKVIDNvglglKGQW-----RDAA-----LQALaAVGLADraNEWPA-ALSGGQKQRVALARALIHRPGLLLL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2095916338 419 DEPTRGVDVSARADIYQLLKSVAAQ-NVAVLMISSDVEEFVGLADRVLVMHQGR 471
Cdd:PRK11247 158 DEPLGALDALTRIEMQDLIESLWQQhGFTVLLVTHDVSEAVAMADRVLLIEEGK 211
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
274-471 |
1.15e-14 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 75.18 E-value: 1.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 274 DLSLEIRAGEIVGLAGLVGSGRTefaeTL----YGLRPPRAGRIWLENREISqestrARLAsglvylPEDRQVSGLFLDA 349
Cdd:COG1118 20 DVSLEIASGELVALLGPSGSGKT----TLlriiAGLETPDSGRIVLNGRDLF-----TNLP------PRERRVGFVFQHY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 350 ---P---VRWNtVMF----NQPSwwqqgkrEAAVVERYHRALG-IKLAD-GDQPVRTLSGGNQQKVLLARCLEANPLLLI 417
Cdd:COG1118 85 alfPhmtVAEN-IAFglrvRPPS-------KAEIRARVEELLElVQLEGlADRYPSQLSGGQRQRVALARALAVEPEVLL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2095916338 418 VDEPTRGVDVSARADIYQLLKSV-AAQNVAVLMISSDVEEFVGLADRVLVMHQGR 471
Cdd:COG1118 157 LDEPFGALDAKVRKELRRWLRRLhDELGGTTVFVTHDQEEALELADRVVVMNQGR 211
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
30-466 |
1.19e-14 |
|
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: 76.36 E-value: 1.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 30 GQVHALMGGNGAGKSTLMKIIAGVETPDSG----ELTIGE--RAFA--------------RLNPALAHQLgIYLVPQepm 89
Cdd:COG1245 99 GKVTGILGPNGIGKSTALKILSGELKPNLGdydeEPSWDEvlKRFRgtelqdyfkklangEIKVAHKPQY-VDLIPK--- 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 90 lFPNLSVREnilfrLPKRADTTARLQEKLQQLNCQINLDASASTLEVADQQMVEILRGLMREARILILDEPTASLTPGET 169
Cdd:COG1245 175 -VFKGTVRE-----LLEKVDERGKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIYQR 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 170 ERLFSQIRALQALDVGIVFISHKLPEIRQLASHVsvmrdgaVVLSGETAGYG------------DQQL------------ 225
Cdd:COG1245 249 LNVARLIRELAEEGKYVLVVEHDLAILDYLADYV-------HILYGEPGVYGvvskpksvrvgiNQYLdgylpeenvrir 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 226 ---ISAMTPASRDHALSDTQKLWLALpgnrRTQAQDFpVLRVEdltgEGfidlslEIRAGEIVGLAGLVGSGRTEFAETL 302
Cdd:COG1245 322 depIEFEVHAPRREKEEETLVEYPDL----TKSYGGF-SLEVE----GG------EIREGEVLGIVGPNGIGKTTFAKIL 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 303 YGLRPPRAGRIWLENReISqestrarlasglvYLPE------DRQVSGLFLDApvrwNTVMFNQpSWWQqgkreAAVVER 376
Cdd:COG1245 387 AGVLKPDEGEVDEDLK-IS-------------YKPQyispdyDGTVEEFLRSA----NTDDFGS-SYYK-----TEIIKP 442
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 377 yhraLGI-KLADgdQPVRTLSGGNQQKVLLARCL--EANPLLLivDEPTRGVDVSARADIYQLLKSVAAQN-VAVLMISS 452
Cdd:COG1245 443 ----LGLeKLLD--KNVKDLSGGELQRVAIAACLsrDADLYLL--DEPSAHLDVEQRLAVAKAIRRFAENRgKTAMVVDH 514
|
490
....*....|....
gi 2095916338 453 DVEEFVGLADRVLV 466
Cdd:COG1245 515 DIYLIDYISDRLMV 528
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
6-218 |
1.25e-14 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 74.84 E-value: 1.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 6 EARQIRKQFSG----VAVLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDSGELTIGERAFARLNP----ALAH 77
Cdd:PRK11153 3 ELKNISKVFPQggrtIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEkelrKARR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 78 QLGiylvpqepMLFP--NL----SVRENILFRLP----KRADTTARLQEKLQQLNCQINLDASASTLEVADQQMVEILRG 147
Cdd:PRK11153 83 QIG--------MIFQhfNLlssrTVFDNVALPLElagtPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2095916338 148 LMREARILILDEPTASLTPgETER----LFSQIRalQALDVGIVFISHKLPEIRQLASHVSVMRDGAVVLSGETA 218
Cdd:PRK11153 155 LASNPKVLLCDEATSALDP-ATTRsileLLKDIN--RELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVS 226
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
274-471 |
1.36e-14 |
|
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: 73.03 E-value: 1.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 274 DLSLEIRAGEIVGLAGLVGSGRTEFAETLYGLRPPRAGRIWLENREISQeSTRARLASGLVYLPEDrqvSGLFLDApVRW 353
Cdd:cd03254 21 DINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRD-ISRKSLRSMIGVVLQD---TFLFSGT-IME 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 354 NTVMFNQPSwwqqgkrEAAVVERYHRALGI-----KLADGDQPV-----RTLSGGNQQKVLLARCLEANPLLLIVDEPTR 423
Cdd:cd03254 96 NIRLGRPNA-------TDEEVIEAAKEAGAhdfimKLPNGYDTVlgengGNLSQGERQLLAIARAMLRDPKILILDEATS 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2095916338 424 GVDVSARADIYQLLKSVaAQNVAVLMIS---SDVEEfvglADRVLVMHQGR 471
Cdd:cd03254 169 NIDTETEKLIQEALEKL-MKGRTSIIIAhrlSTIKN----ADKILVLDDGK 214
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
19-216 |
1.45e-14 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 73.89 E-value: 1.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 19 VLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDSGELTIGERAF---ARLNPALAHQLG-IYLVPQEPMLFPNL 94
Cdd:PRK13638 16 VLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLdysKRGLLALRQQVAtVFQDPEQQIFYTDI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 95 SvrENILFRLPK----RADTTARLQEKLQQLNCQINLDASASTLEVADQQMVEILRGLMREARILILDEPTASLTPGETE 170
Cdd:PRK13638 96 D--SDIAFSLRNlgvpEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRT 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2095916338 171 RLFSQIRALQALDVGIVFISHKLPEIRQLASHVSVMRDGAVVLSGE 216
Cdd:PRK13638 174 QMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGA 219
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
275-471 |
1.76e-14 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 72.99 E-value: 1.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 275 LSLEIRAGEIVGLAGLVGSGRTEFAETLYGlrPPRA--GRIWLENREISQESTRARLASGLVYLPEDRQVsglFLDAPVR 352
Cdd:PRK11614 24 VSLHINQGEIVTLIGANGAGKTTLLGTLCG--DPRAtsGRIVFDGKDITDWQTAKIMREAVAIVPEGRRV---FSRMTVE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 353 WNTVM---FNQPSWWQQgkREAAVVERYHRALGIKLadgdQPVRTLSGGNQQKVLLARCLEANPLLLIVDEPTRGVDVSA 429
Cdd:PRK11614 99 ENLAMggfFAERDQFQE--RIKWVYELFPRLHERRI----QRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPII 172
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2095916338 430 RADIYQLLKSVAAQNVAVLMISSDVEEFVGLADRVLVMHQGR 471
Cdd:PRK11614 173 IQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGH 214
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
15-215 |
2.28e-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: 76.21 E-value: 2.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 15 SGVAVLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDSGELTIGERAFARLNPALAHQLGiyLVPQEPMLFPNL 94
Cdd:TIGR01257 941 SGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDAVRQSLG--MCPQHNILFHHL 1018
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 95 SVRENILF--RLPKRADTTARLQEK--LQQLNCQINLDASASTLEVADQQMVEILRGLMREARILILDEPTASLTPGETE 170
Cdd:TIGR01257 1019 TVAEHILFyaQLKGRSWEEAQLEMEamLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRR 1098
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2095916338 171 RLFSQIRALQALDVgIVFISHKLPEIRQLASHVSVMRDGAVVLSG 215
Cdd:TIGR01257 1099 SIWDLLLKYRSGRT-IIMSTHHMDEADLLGDRIAIISQGRLYCSG 1142
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
37-161 |
2.29e-14 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 75.54 E-value: 2.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 37 GGNGAGKSTLMKIIAGVETPDSGEltigerafARLNPalahqlGI---YLvPQEPMLFPNLSVRENI------------- 100
Cdd:PRK11819 40 GLNGAGKSTLLRIMAGVDKEFEGE--------ARPAP------GIkvgYL-PQEPQLDPEKTVRENVeegvaevkaaldr 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 101 ------LFRLP-----KRADTTARLQEKLQQLNCQiNLDasaSTLEVA--------DQQMVEILRG-----------LMR 150
Cdd:PRK11819 105 fneiyaAYAEPdadfdALAAEQGELQEIIDAADAW-DLD---SQLEIAmdalrcppWDAKVTKLSGgerrrvalcrlLLE 180
|
170
....*....|.
gi 2095916338 151 EARILILDEPT 161
Cdd:PRK11819 181 KPDMLLLDEPT 191
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
18-217 |
2.32e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 73.16 E-value: 2.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 18 AVLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAG-VETPDS-----GE-LTIGERAFARLNPALAHQLGiyLVPQEPML 90
Cdd:PRK14246 24 AILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRlIEIYDSkikvdGKvLYFGKDIFQIDAIKLRKEVG--MVFQQPNP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 91 FPNLSVRENILFRLPKRADTTAR-----LQEKLQQL----NCQINLDASASTLEVADQQMVEILRGLMREARILILDEPT 161
Cdd:PRK14246 102 FPHLSIYDNIAYPLKSHGIKEKReikkiVEECLRKVglwkEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPT 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2095916338 162 ASL---TPGETERLFSQIRAlqalDVGIVFISHKLPEIRQLASHVSVMRDGAVVLSGET 217
Cdd:PRK14246 182 SMIdivNSQAIEKLITELKN----EIAIVIVSHNPQQVARVADYVAFLYNGELVEWGSS 236
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
262-471 |
2.52e-14 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 72.74 E-value: 2.52e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 262 LRVEDLT---GEGFI--DLSLEIRAGEIVGLAGLVGSGRTEFAETLYGLRPPRAGRIWLENREISQESTRaRLASGLVYL 336
Cdd:PRK11231 3 LRTENLTvgyGTKRIlnDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSR-QLARRLALL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 337 P------EDRQVSGLFLDAPVRWNTVmfnqpsWWQQGKREAAVVERYHRALGI-KLADgdQPVRTLSGGNQQKVLLARCL 409
Cdd:PRK11231 82 PqhhltpEGITVRELVAYGRSPWLSL------WGRLSAEDNARVNQAMEQTRInHLAD--RRLTDLSGGQRQRAFLAMVL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2095916338 410 EANPLLLIVDEPTRGVDVSARADIYQLLKSVAAQNVAVLMISSDVEEFVGLADRVLVMHQGR 471
Cdd:PRK11231 154 AQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGH 215
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
262-449 |
2.91e-14 |
|
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: 71.37 E-value: 2.91e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 262 LRVEDLTGEG-----FIDLSLEIRAGEIVGLAGLVGSGRTEFAETLYGLRPPRAGRIWLENREISQEstRARLASGLVYL 336
Cdd:cd03231 1 LEADELTCERdgralFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQ--RDSIARGLLYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 337 PEDRQVSGLFldapvrwnTVMFNQpSWWQQGKREAAVVERYHRA-LGiklADGDQPVRTLSGGNQQKVLLARCLEANPLL 415
Cdd:cd03231 79 GHAPGIKTTL--------SVLENL-RFWHADHSDEQVEEALARVgLN---GFEDRPVAQLSAGQQRRVALARLLLSGRPL 146
|
170 180 190
....*....|....*....|....*....|....
gi 2095916338 416 LIVDEPTRGVDVSARADIYQLLKSVAAQNVAVLM 449
Cdd:cd03231 147 WILDEPTTALDKAGVARFAEAMAGHCARGGMVVL 180
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
264-471 |
2.92e-14 |
|
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: 71.76 E-value: 2.92e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 264 VEDLTGEGFIDLSLEIRAGEIVGLAGLVGSGRTEFAETLYGLRPPRAGRIWLENREISQESTRARLASGLVylpedrQVS 343
Cdd:cd03298 6 IRFSYGEQPMHFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRPVSMLF------QEN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 344 GLFLDAPVRWNTVMFNQPSW----WQQGKREAAVveryhRALGIKLADGDQPvRTLSGGNQQKVLLARCLEANPLLLIVD 419
Cdd:cd03298 80 NLFAHLTVEQNVGLGLSPGLkltaEDRQAIEVAL-----ARVGLAGLEKRLP-GELSGGERQRVALARVLVRDKPVLLLD 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2095916338 420 EPTRGVDVSARADIYQLLKSVAAQN-VAVLMISSDVEEFVGLADRVLVMHQGR 471
Cdd:cd03298 154 EPFAALDPALRAEMLDLVLDLHAETkMTVLMVTHQPEDAKRLAQRVVFLDNGR 206
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
274-471 |
3.01e-14 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 73.99 E-value: 3.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 274 DLSLEIRAGEIVGLAGLVGSGRTEFAETLYGLRPPRAGRIWLENREISQESTRARLASgLVYlpedrQVSGLF----LDA 349
Cdd:PRK11432 24 NLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQRDIC-MVF-----QSYALFphmsLGE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 350 PVRWNTVMFNQPSwwqqgkreAAVVERYHRALgiKLAD----GDQPVRTLSGGNQQKVLLARCLEANPLLLIVDEPTRGV 425
Cdd:PRK11432 98 NVGYGLKMLGVPK--------EERKQRVKEAL--ELVDlagfEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSNL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2095916338 426 DV----SARADIYQLLKSVaaqNVAVLMISSDVEEFVGLADRVLVMHQGR 471
Cdd:PRK11432 168 DAnlrrSMREKIRELQQQF---NITSLYVTHDQSEAFAVSDTVIVMNKGK 214
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
14-216 |
3.24e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 72.85 E-value: 3.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 14 FSGVAvLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDSGELTIGERAFARLN-----PALAHQLGIYLVPQEP 88
Cdd:PRK13649 18 FEGRA-LFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSknkdiKQIRKKVGLVFQFPES 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 89 MLFPNlSVRENILFR------LPKRADTTARlqEKLQQLNCQINLdASASTLEVADQQM--VEILRGLMREARILILDEP 160
Cdd:PRK13649 97 QLFEE-TVLKDVAFGpqnfgvSQEEAEALAR--EKLALVGISESL-FEKNPFELSGGQMrrVAIAGILAMEPKILVLDEP 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2095916338 161 TASLTPGETERLFSQIRALQALDVGIVFISHKLPEIRQLASHVSVMRDGAVVLSGE 216
Cdd:PRK13649 173 TAGLDPKGRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGK 228
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
257-471 |
3.43e-14 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 72.73 E-value: 3.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 257 QDFPVLRvedltgegfiDLSLEIRAGEIVGLAGLVGSGRTEFAETLYGLRPPRAGRIWLENREISQeSTRARLA----SG 332
Cdd:PRK13638 12 QDEPVLK----------GLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDY-SKRGLLAlrqqVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 333 LVYLPEDRQVSGLFLDAPVRWntvmfnqpSWWQQGKREAAVVERYHRALGIKLADG--DQPVRTLSGGNQQKVLLARCLE 410
Cdd:PRK13638 81 TVFQDPEQQIFYTDIDSDIAF--------SLRNLGVPEAEITRRVDEALTLVDAQHfrHQPIQCLSHGQKKRVAIAGALV 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2095916338 411 ANPLLLIVDEPTRGVDVSARADIYQLLKSVAAQNVAVLMISSDVEEFVGLADRVLVMHQGR 471
Cdd:PRK13638 153 LQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQ 213
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
5-211 |
3.76e-14 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 73.72 E-value: 3.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 5 LEARQIRKQFSG-VAVLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDSGELTIGERAFARLNPAlahQLGIYL 83
Cdd:PRK11650 4 LKLQAVRKSYDGkTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPA---DRDIAM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 84 VPQEPMLFPNLSVRENILF-----RLPKrADTTARLQEKLQQLNCQINLDASASTLEVADQQMVEILRGLMREARILILD 158
Cdd:PRK11650 81 VFQNYALYPHMSVRENMAYglkirGMPK-AEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLFD 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2095916338 159 EPTASLTPgeteRLFSQ----IRALQA-LDVGIVFISHKLPEIRQLASHVSVMRDGAV 211
Cdd:PRK11650 160 EPLSNLDA----KLRVQmrleIQRLHRrLKTTSLYVTHDQVEAMTLADRVVVMNGGVA 213
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
260-471 |
5.16e-14 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 72.84 E-value: 5.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 260 PVLRVEDLT-----GEGFI-----------DLSLEIRAGEIVGLAGLVGSGRTEFAETLYGLRPPRAGRIWLENREISQE 323
Cdd:COG4608 6 PLLEVRDLKkhfpvRGGLFgrtvgvvkavdGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 324 STRARLAsglvyLPED--------------RQVSGLFLDAPVRWNTVMfnqpswwQQGKREAAVVE-------------R 376
Cdd:COG4608 86 SGRELRP-----LRRRmqmvfqdpyaslnpRMTVGDIIAEPLRIHGLA-------SKAERRERVAEllelvglrpehadR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 377 Y-HralgikladgdqpvrTLSGGNQQKVLLARCLEANPLLLIVDEPTRGVDVSARADIYQLLKSVAAQ-NVAVLMISSD- 453
Cdd:COG4608 154 YpH---------------EFSGGQRQRIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDElGLTYLFISHDl 218
|
250
....*....|....*....
gi 2095916338 454 -VEEFVglADRVLVMHQGR 471
Cdd:COG4608 219 sVVRHI--SDRVAVMYLGK 235
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
262-471 |
7.08e-14 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 72.53 E-value: 7.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 262 LRVEDLTGEGFID----LSLEIRAGEIVGLAGLVGSGRTEFAETLYGLRPPR----AGRIWLENREISQESTRARlaSGL 333
Cdd:PRK15093 9 LTIEFKTSDGWVKavdrVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDNwrvtADRMRFDDIDLLRLSPRER--RKL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 334 VylpeDRQVSGLF------LDAPVRWNT-VMFNQPS------WWQQ-GKREAAVVERYHRaLGIKlaDGDQPVRT----L 395
Cdd:PRK15093 87 V----GHNVSMIFqepqscLDPSERVGRqLMQNIPGwtykgrWWQRfGWRKRRAIELLHR-VGIK--DHKDAMRSfpyeL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2095916338 396 SGGNQQKVLLARCLEANPLLLIVDEPTRGVDVSARADIYQLLKSVAAQN-VAVLMISSDVEEFVGLADRVLVMHQGR 471
Cdd:PRK15093 160 TEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNnTTILLISHDLQMLSQWADKINVLYCGQ 236
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
274-471 |
7.15e-14 |
|
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: 70.98 E-value: 7.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 274 DLSLEIRAGEIVGLAGLVGSGRTEFAETLYGLRPPRAGRIWLENREIS---QESTRARLAsglVYLPEDrqvsgLFLDAP 350
Cdd:cd03252 20 NISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLAladPAWLRRQVG---VVLQEN-----VLFNRS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 351 VRWNTVMFNqPSWWQQGKREAAVVERYHR-----ALGIKLADGDQPVrTLSGGNQQKVLLARCLEANPLLLIVDEPTRGV 425
Cdd:cd03252 92 IRDNIALAD-PGMSMERVIEAAKLAGAHDfiselPEGYDTIVGEQGA-GLSGGQRQRIAIARALIHNPRILIFDEATSAL 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2095916338 426 DVSARADIYQLLKSVAAqNVAVLMISSDVEEfVGLADRVLVMHQGR 471
Cdd:cd03252 170 DYESEHAIMRNMHDICA-GRTVIIIAHRLST-VKNADRIIVMEKGR 213
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
20-215 |
8.04e-14 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 73.84 E-value: 8.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 20 LKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDSGELTIGERAFARLNPA-LAHQLGIylVPQEPMLFpNLSVRE 98
Cdd:PRK13657 351 VEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRAsLRRNIAV--VFQDAGLF-NRSIED 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 99 NI-----------LFRLPKRADTTARLQEKLQQLNCQINldASASTLEVADQQMVEILRGLMREARILILDEPTASLTpG 167
Cdd:PRK13657 428 NIrvgrpdatdeeMRAAAERAQAHDFIERKPDGYDTVVG--ERGRQLSGGERQRLAIARALLKDPPILILDEATSALD-V 504
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2095916338 168 ETERLFSQirALQALDVG--IVFISHKLPEIRQlASHVSVMRDGAVVLSG 215
Cdd:PRK13657 505 ETEAKVKA--ALDELMKGrtTFIIAHRLSTVRN-ADRILVFDNGRVVESG 551
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
3-164 |
8.17e-14 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 70.29 E-value: 8.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 3 PLLEARQIRKQFSGVAVLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDSGELTIGERAFARLNPALA-Hqlgi 81
Cdd:PRK13539 1 MMLEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEAcH---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 82 YLVPQEPMLfPNLSVRENILFRLPKRADTTARLQEKLQQLNCQINLDASASTLEVADQQMVEILRGLMREARILILDEPT 161
Cdd:PRK13539 77 YLGHRNAMK-PALTVAENLEFWAAFLGGEELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPT 155
|
...
gi 2095916338 162 ASL 164
Cdd:PRK13539 156 AAL 158
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
13-218 |
9.56e-14 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 71.02 E-value: 9.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 13 QFSGVAV---LKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVeTPDSGELTIGERAFARLNPA-LAHQLGiYLVPQEP 88
Cdd:COG4138 2 QLNDVAVagrLGPISAQVNAGELIHLIGPNGAGKSTLLARMAGL-LPGQGEILLNGRPLSDWSAAeLARHRA-YLSQQQS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 89 MLFpNLSVRENILFRLPKRADTTA---RLQEKLQQLNCQINLDASASTLEVADQQMVEILRGLMR-------EARILILD 158
Cdd:COG4138 80 PPF-AMPVFQYLALHQPAGASSEAveqLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLQvwptinpEGQLLLLD 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 159 EPTASLTPGETERLFSQIRALQALDVGIVFISHKLPEIRQLASHVSVMRDGAVVLSGETA 218
Cdd:COG4138 159 EPMNSLDVAQQAALDRLLRELCQQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETA 218
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
4-216 |
1.29e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 70.88 E-value: 1.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 4 LLEARQIRKQF-SGVAVLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDSGELTIGERAFARLNPALA---HQL 79
Cdd:PRK13639 1 ILETRDLKYSYpDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSLLevrKTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 80 GIylVPQEP--MLFPNlSVRENILF-----RLPKRaDTTARLQEKLQQLNCQINLDASASTLEVADQQMVEILRGLMREA 152
Cdd:PRK13639 81 GI--VFQNPddQLFAP-TVEEDVAFgplnlGLSKE-EVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2095916338 153 RILILDEPTASLTPGETERLFSQIRALQALDVGIVFISHKLPEIRQLASHVSVMRDGAVVLSGE 216
Cdd:PRK13639 157 EIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGT 220
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
8-215 |
1.51e-13 |
|
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: 69.99 E-value: 1.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 8 RQIRKQFSGVAVLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVEtpDSGELTIGERAFA--RLNPALAHQLGIYlVP 85
Cdd:cd03234 11 LKAKNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRV--EGGGTTSGQILFNgqPRKPDQFQKCVAY-VR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 86 QEPMLFPNLSVRENILF----RLPKRADTTARLQEKLQQLNCQINLDASASTLEVA----DQQMVEILRGLMREARILIL 157
Cdd:cd03234 88 QDDILLPGLTVRETLTYtailRLPRKSSDAIRKKRVEDVLLRDLALTRIGGNLVKGisggERRRVSIAVQLLWDPKVLIL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2095916338 158 DEPTASLTPGETERLFSQIRALQALDVGIVFISHK-LPEIRQLASHVSVMRDGAVVLSG 215
Cdd:cd03234 168 DEPTSGLDSFTALNLVSTLSQLARRNRIVILTIHQpRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
274-471 |
1.52e-13 |
|
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: 69.12 E-value: 1.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 274 DLSLEIRAGEIVGLAGLVGSGRTEFAETLYGLRPPRA--GRIWLENREISQESTRARLAsglvYLPEDRQVSGLFldapv 351
Cdd:cd03213 27 NVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLGvsGEVLINGRPLDKRSFRKIIG----YVPQDDILHPTL----- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 352 rwnTVmfnqpswwqqgkREAAvveRYHRALgikladgdqpvRTLSGGNQQKVLLARCLEANPLLLIVDEPTRGVDVSARA 431
Cdd:cd03213 98 ---TV------------RETL---MFAAKL-----------RGLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSAL 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2095916338 432 DIYQLLKSVAAQNVAVLMI----SSDVeefVGLADRVLVMHQGR 471
Cdd:cd03213 149 QVMSLLRRLADTGRTIICSihqpSSEI---FELFDKLLLLSQGR 189
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-193 |
1.72e-13 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 70.14 E-value: 1.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 1 MKPLLEARQIRKQFSGVAVLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDSGELtigERafarlnpalAHQLG 80
Cdd:PRK09544 1 MTSLVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI---KR---------NGKLR 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 81 IYLVPQEPMLFPNLSVRENILFRLP---KRADttarLQEKLQQLNCQINLDASASTLEVADQQMVEILRGLMREARILIL 157
Cdd:PRK09544 69 IGYVPQKLYLDTTLPLTVNRFLRLRpgtKKED----ILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVL 144
|
170 180 190
....*....|....*....|....*....|....*..
gi 2095916338 158 DEPTASLTPGETERLFSQIRAL-QALDVGIVFISHKL 193
Cdd:PRK09544 145 DEPTQGVDVNGQVALYDLIDQLrRELDCAVLMVSHDL 181
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
3-213 |
1.87e-13 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 70.09 E-value: 1.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 3 PLLeARQIRKQFSGVAVLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDSGELTIGerafarlNPALAH-QLGI 81
Cdd:PRK11247 12 PLL-LNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAG-------TAPLAEaREDT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 82 YLVPQEPMLFPNLSVRENILFRLpkRADTTARLQEKLQQLNCQINLDASASTLEVADQQMVEILRGLMREARILILDEPT 161
Cdd:PRK11247 84 RLMFQDARLLPWKKVIDNVGLGL--KGQWRDAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2095916338 162 A---SLTPGETERLFSQIRALQALDVGIVfiSHKLPEIRQLASHVSVMRDGAVVL 213
Cdd:PRK11247 162 GaldALTRIEMQDLIESLWQQHGFTVLLV--THDVSEAVAMADRVLLIEEGKIGL 214
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
13-218 |
1.88e-13 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 69.96 E-value: 1.88e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 13 QFSGVAV---LKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVeTPDSGELTIGERAFARLNPA-LAHQLGiYLVPQEP 88
Cdd:PRK03695 2 QLNDVAVstrLGPLSAEVRAGEILHLVGPNGAGKSTLLARMAGL-LPGSGSIQFAGQPLEAWSAAeLARHRA-YLSQQQT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 89 MLFpNLSVRENILFRLPKRADTTA---RLQEKLQQLNCQINLDASASTLEVADQQMV-------EILRGLMREARILILD 158
Cdd:PRK03695 80 PPF-AMPVFQYLTLHQPDKTRTEAvasALNEVAEALGLDDKLGRSVNQLSGGEWQRVrlaavvlQVWPDINPAGQLLLLD 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 159 EPTASLTPGETERLFSQIRALQALDVGIVFISHKLPEIRQLASHVSVMRDGAVVLSGETA 218
Cdd:PRK03695 159 EPMNSLDVAQQAALDRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRD 218
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
271-470 |
1.90e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 70.92 E-value: 1.90e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 271 GFIDLSLEIRAGEIVGLAGLVGSGRTEFAETLYGLRPP-----RAGRIWLENREISQESTRARLASGLVY-LPEdrqvSG 344
Cdd:PRK13643 21 ALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPtegkvTVGDIVVSSTSKQKEIKPVRKKVGVVFqFPE----SQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 345 LFLDAPVRwnTVMFNQPSWWQQGKREAAVVERYHRALGIKLADGDQPVRTLSGGNQQKVLLARCLEANPLLLIVDEPTRG 424
Cdd:PRK13643 97 LFEETVLK--DVAFGPQNFGIPKEKAEKIAAEKLEMVGLADEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAG 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2095916338 425 VDVSARADIYQLLKSVAAQNVAVLMISSDVEEFVGLADRVLVMHQG 470
Cdd:PRK13643 175 LDPKARIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKG 220
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
274-471 |
1.95e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 71.03 E-value: 1.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 274 DLSLEIRAGEIVGLAGLVGSGRTEFAETLYGLRPPRAGRIWLENREISQEST-----------------RARLASGLVY- 335
Cdd:PRK13631 44 NISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIGDKKNnhelitnpyskkiknfkELRRRVSMVFq 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 336 LPEDRqvsgLFLDAPVRwnTVMFNqPSWWQQGKREAAVVERYH-RALGIKLADGDQPVRTLSGGNQQKVLLARCLEANPL 414
Cdd:PRK13631 124 FPEYQ----LFKDTIEK--DIMFG-PVALGVKKSEAKKLAKFYlNKMGLDDSYLERSPFGLSGGQKRRVAIAGILAIQPE 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2095916338 415 LLIVDEPTRGVDVSARADIYQLLKSVAAQNVAVLMISSDVEEFVGLADRVLVMHQGR 471
Cdd:PRK13631 197 ILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGK 253
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
5-191 |
2.01e-13 |
|
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: 72.28 E-value: 2.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 5 LEARQIRKQFSGVAVLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDSGELTIGERAfarlnpalahQLGiYLV 84
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETV----------KLA-YVD 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 85 PQEPMLFPNLSVRENIlfrlpkradttARLQEKLQQLNCQINLDA--SASTLEVADQQ-MVEILRG-----------LMR 150
Cdd:TIGR03719 392 QSRDALDPNKTVWEEI-----------SGGLDIIKLGKREIPSRAyvGRFNFKGSDQQkKVGQLSGgernrvhlaktLKS 460
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2095916338 151 EARILILDEPTASLtpgeterlfsQIRALQALDVGI-------VFISH 191
Cdd:TIGR03719 461 GGNVLLLDEPTNDL----------DVETLRALEEALlnfagcaVVISH 498
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
248-467 |
2.08e-13 |
|
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: 72.32 E-value: 2.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 248 LPGNRRTQAQDFPVLRVEDLT------GEGFIDLSLEIRAGEIVGLAGLVGSGRTEFAETLYGLRPPRAGRIWLENREIs 321
Cdd:TIGR02857 308 LAGKAPVTAAPASSLEFSGVSvaypgrRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPL- 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 322 QESTRARLASGLVYLPedrQVSGLFlDAPVRWNtVMFNQPswwqqGKREAAVVERYHRA----------LGIKLADGDQP 391
Cdd:TIGR02857 387 ADADADSWRDQIAWVP---QHPFLF-AGTIAEN-IRLARP-----DASDAEIREALERAgldefvaalpQGLDTPIGEGG 456
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2095916338 392 VRtLSGGNQQKVLLARCLEANPLLLIVDEPTRGVDVSARADIYQLLKSvAAQNVAVLMISSDvEEFVGLADRVLVM 467
Cdd:TIGR02857 457 AG-LSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRA-LAQGRTVLLVTHR-LALAALADRIVVL 529
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
274-471 |
2.57e-13 |
|
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: 69.42 E-value: 2.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 274 DLSLEIRAGEIVGLAGLVGSGRTEFAETLYGLRPPRAGRIWLENREISQESTRarlasglvYLpeDRQVSgLFLDAPVRW 353
Cdd:cd03248 32 DVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHK--------YL--HSKVS-LVGQEPVLF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 354 NTVMFNQPSWWQQGKREAAVVE---RYHRALGI-KLADG-----DQPVRTLSGGNQQKVLLARCLEANPLLLIVDEPTRG 424
Cdd:cd03248 101 ARSLQDNIAYGLQSCSFECVKEaaqKAHAHSFIsELASGydtevGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSA 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2095916338 425 VDVSARADIYQLLKSvAAQNVAVLMIS---SDVEEfvglADRVLVMHQGR 471
Cdd:cd03248 181 LDAESEQQVQQALYD-WPERRTVLVIAhrlSTVER----ADQILVLDGGR 225
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
20-212 |
2.65e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 70.19 E-value: 2.65e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 20 LKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDSGELTIGERAFAR------LNPaLAHQLGIYLVPQEPMLFPN 93
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHktkdkyIRP-VRKRIGMVFQFPESQLFED 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 94 lSVRENILFRlPKR-----ADTTARLQEKLQQLNCQINLdASASTLEVADQQM--VEILRGLMREARILILDEPTASLTP 166
Cdd:PRK13646 102 -TVEREIIFG-PKNfkmnlDEVKNYAHRLLMDLGFSRDV-MSQSPFQMSGGQMrkIAIVSILAMNPDIIVLDEPTAGLDP 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2095916338 167 GETERLFSQIRALQALD-VGIVFISHKLPEIRQLASHVSVMRDGAVV 212
Cdd:PRK13646 179 QSKRQVMRLLKSLQTDEnKTIILVSHDMNEVARYADEVIVMKEGSIV 225
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
9-209 |
2.79e-13 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 69.13 E-value: 2.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 9 QIRKQF-SGVAVLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDSGELTIGERAFARLN----PALAHQLGiyL 83
Cdd:PRK10908 6 HVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKnrevPFLRRQIG--M 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 84 VPQEPMLFPNLSVRENILFRL----PKRADTTARLQEKLQQLNCqinLDASAS---TLEVADQQMVEILRGLMREARILI 156
Cdd:PRK10908 84 IFQDHHLLMDRTVYDNVAIPLiiagASGDDIRRRVSAALDKVGL---LDKAKNfpiQLSGGEQQRVGIARAVVNKPAVLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2095916338 157 LDEPTASLTPGETERLFSQIRALQALDVGIVFISHKLPEIRQLASHVSVMRDG 209
Cdd:PRK10908 161 ADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDG 213
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
5-211 |
2.96e-13 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 69.61 E-value: 2.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 5 LEARQIRKQFSGVAVLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDSGELTIGERAF-------ARLNPALAH 77
Cdd:PRK10619 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTInlvrdkdGQLKVADKN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 78 QLGIY-----LVPQEPMLFPNLSVRENILfRLPKR--ADTTARLQEKLQQLNCQINLDASA-----STLEVADQQMVEIL 145
Cdd:PRK10619 86 QLRLLrtrltMVFQHFNLWSHMTVLENVM-EAPIQvlGLSKQEARERAVKYLAKVGIDERAqgkypVHLSGGQQQRVSIA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2095916338 146 RGLMREARILILDEPTASLTP---GETERLFSQiraLQALDVGIVFISHKLPEIRQLASHVSVMRDGAV 211
Cdd:PRK10619 165 RALAMEPEVLLFDEPTSALDPelvGEVLRIMQQ---LAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKI 230
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
274-471 |
3.93e-13 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 70.75 E-value: 3.93e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 274 DLSLEIRAGEIVGLAGLVGSGRTEFAETLYGLRPPRAGRIWLENREISQEStrarlasglvylPEDRQVS------GLFL 347
Cdd:PRK09452 32 NLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVP------------AENRHVNtvfqsyALFP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 348 DAPVRWNtVMFnqpswwqqGKR-----EAAVVERYHRALG-IKLAD-GDQPVRTLSGGNQQKVLLARCLEANPLLLIVDE 420
Cdd:PRK09452 100 HMTVFEN-VAF--------GLRmqktpAAEITPRVMEALRmVQLEEfAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDE 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2095916338 421 PTRGVDVSARADIYQLLKSVAAQ-NVAVLMISSDVEEFVGLADRVLVMHQGR 471
Cdd:PRK09452 171 SLSALDYKLRKQMQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGR 222
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
276-481 |
4.00e-13 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 71.20 E-value: 4.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 276 SLEIRAGEIVGLAGLVGSGRTEFAETLYGLRPPRAG-------RIWLENREISQ---ESTRARLASGLVYLPED---RQV 342
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGerqsqfsHITRLSFEQLQklvSDEWQRNNTDMLSPGEDdtgRTT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 343 SGLFLDapvrwntvmfnqpswwqqGKREAAVVERYHRALGIKlADGDQPVRTLSGGNQQKVLLARCLEANPLLLIVDEPT 422
Cdd:PRK10938 103 AEIIQD------------------EVKDPARCEQLAQQFGIT-ALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPF 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2095916338 423 RGVDVSARADIYQLLKSVAAQNVAVLMIS---SDVEEFVG----LADRVLVmHQGRHSGELARQAV 481
Cdd:PRK10938 164 DGLDVASRQQLAELLASLHQSGITLVLVLnrfDEIPDFVQfagvLADCTLA-ETGEREEILQQALV 228
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
274-471 |
5.27e-13 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 71.35 E-value: 5.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 274 DLSLEIRAGEIVGLAGLVGSGRTEFAETLYGLRPPRAGRIWLEN---REISQESTRARLAsglvYLPEDrqvSGLFlDAP 350
Cdd:COG1132 358 DISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGvdiRDLTLESLRRQIG----VVPQD---TFLF-SGT 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 351 VRWNtVMFnqpswwqqGKREA--AVVERYHRALGI-----KLADG-DQPV----RTLSGGNQQKVLLARCLEANPLLLIV 418
Cdd:COG1132 430 IREN-IRY--------GRPDAtdEEVEEAAKAAQAhefieALPDGyDTVVgergVNLSGGQRQRIAIARALLKDPPILIL 500
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2095916338 419 DEPTRGVDVSARADIYQLLKSVaAQNVAVLMIS---SDVEEfvglADRVLVMHQGR 471
Cdd:COG1132 501 DEATSALDTETEALIQEALERL-MKGRTTIVIAhrlSTIRN----ADRILVLDDGR 551
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
260-471 |
6.45e-13 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 68.48 E-value: 6.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 260 PVLRVEDLT----GEGFID-LSLEIRAGEIVGLAGLVGSGRTEFAETLYGLRPPRAGRIWLENREI----SQESTR---- 326
Cdd:PRK11300 4 PLLSVSGLMmrfgGLLAVNnVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIeglpGHQIARmgvv 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 327 -----ARLASGLVYL-----PEDRQV-SGLFldapvrwnTVMFNQPSWwQQGKREAavVERYHRALG-IKLAD-GDQPVR 393
Cdd:PRK11300 84 rtfqhVRLFREMTVIenllvAQHQQLkTGLF--------SGLLKTPAF-RRAESEA--LDRAATWLErVGLLEhANRQAG 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2095916338 394 TLSGGNQQKVLLARCLEANPLLLIVDEPTRGVDVSARADIYQLLKSVAAQ-NVAVLMISSDVEEFVGLADRVLVMHQGR 471
Cdd:PRK11300 153 NLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEhNVTVLLIEHDMKLVMGISDRIYVVNQGT 231
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
262-479 |
6.72e-13 |
|
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: 67.55 E-value: 6.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 262 LRVEDLT---GEGFI--DLSLEIRAGEIVGLAGLVGSGRTEFAETLYGLRPPRA--GRIWLENREISQEStrarlasglv 334
Cdd:cd03217 1 LEIKDLHvsvGGKEIlkGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKYEVteGEILFKGEDITDLP---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 335 ylPEDRQVSGLFLdapvrwntvMFNQPswwqqgkreaavvERYHralGIKLADGDQPVR-TLSGGNQQKVLLARCLEANP 413
Cdd:cd03217 71 --PEERARLGIFL---------AFQYP-------------PEIP---GVKNADFLRYVNeGFSGGEKKRNEILQLLLLEP 123
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2095916338 414 LLLIVDEPTRGVDVSARADIYQLLKSVAAQNVAVLMIS--SDVEEFVgLADRVLVMHQGR--HSG--ELARQ 479
Cdd:cd03217 124 DLAILDEPDSGLDIDALRLVAEVINKLREEGKSVLIIThyQRLLDYI-KPDRVHVLYDGRivKSGdkELALE 194
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
274-471 |
7.16e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 69.11 E-value: 7.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 274 DLSLEIRAGEIVGLAGLVGSGRTEFAETLYGLRPPRAGRIWLENREISQEST---RARLASGLVYLPEDRQVSGLFLDAP 350
Cdd:PRK13636 24 GININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRKglmKLRESVGMVFQDPDNQLFSASVYQD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 351 VRWNTVMFNQPswwqqgkrEAAVVERYHRAL---GIKLADgDQPVRTLSGGNQQKVLLARCLEANPLLLIVDEPTRGVDV 427
Cdd:PRK13636 104 VSFGAVNLKLP--------EDEVRKRVDNALkrtGIEHLK-DKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDP 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2095916338 428 SARADIYQLLKSVAAQ-NVAVLMISSDVEEFVGLADRVLVMHQGR 471
Cdd:PRK13636 175 MGVSEIMKLLVEMQKElGLTIIIATHDIDIVPLYCDNVFVMKEGR 219
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
9-215 |
7.60e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 68.89 E-value: 7.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 9 QIRKQFSGVAvLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDSGELTIGERAFA------RLNPaLAHQLGIY 82
Cdd:PRK13634 13 QYKTPFERRA-LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITagkknkKLKP-LRKKVGIV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 83 LVPQEPMLFPNlSVRENILFRlP-----KRADTTARLQEKLQqlncQINLDA---SASTLEVADQQM--VEILRGLMREA 152
Cdd:PRK13634 91 FQFPEHQLFEE-TVEKDICFG-PmnfgvSEEDAKQKAREMIE----LVGLPEellARSPFELSGGQMrrVAIAGVLAMEP 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2095916338 153 RILILDEPTASLTP-GETE--RLFSQIRALQALDvgIVFISHKLPEIRQLASHVSVMRDGAVVLSG 215
Cdd:PRK13634 165 EVLVLDEPTAGLDPkGRKEmmEMFYKLHKEKGLT--TVLVTHSMEDAARYADQIVVMHKGTVFLQG 228
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
275-479 |
9.83e-13 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 67.59 E-value: 9.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 275 LSLEIRAGEIVGLAGLVGSGRTEFAETLYGLRPPRAGRIWLENREISQESTRA----RLASGLVYlpedrQVSGLFLDAP 350
Cdd:PRK10908 21 VTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREvpflRRQIGMIF-----QDHHLLMDRT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 351 VRWNTVM---FNQPSWWQQGKREAAVVERyhraLGIKLADGDQPVRtLSGGNQQKVLLARCLEANPLLLIVDEPTRGVDV 427
Cdd:PRK10908 96 VYDNVAIpliIAGASGDDIRRRVSAALDK----VGLLDKAKNFPIQ-LSGGEQQRVGIARAVVNKPAVLLADEPTGNLDD 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2095916338 428 SARADIYQLLKSVAAQNVAVLMISSDVEEFVGLADRVLVMHQGRHSGELARQ 479
Cdd:PRK10908 171 ALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHLHGGVGGE 222
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
15-215 |
1.07e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 68.29 E-value: 1.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 15 SGVAVLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDSGELTI----GERAFARLNPALAHQLGIylVPQEP-M 89
Cdd:PRK13640 18 SKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPNSKitvdGITLTAKTVWDIREKVGI--VFQNPdN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 90 LFPNLSVRENILFRLPKRADTTARLQEKLQQLNCQINL----DASASTLEVADQQMVEILRGLMREARILILDEPTASLT 165
Cdd:PRK13640 96 QFVGATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMldyiDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLD 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2095916338 166 PGETERLFSQIRALQA-LDVGIVFISHKLPEIRQlASHVSVMRDGAVVLSG 215
Cdd:PRK13640 176 PAGKEQILKLIRKLKKkNNLTVISITHDIDEANM-ADQVLVLDDGKLLAQG 225
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
260-471 |
1.35e-12 |
|
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: 67.07 E-value: 1.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 260 PVLRVEDLTG------------EGFIDLSLEIRAGEIVGLAGLVGSGRTEFAETLYGLRPPRAGRIWLENREisqesTRA 327
Cdd:COG4778 3 TLLEVENLSKtftlhlqggkrlPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDG-----GWV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 328 RLASGlvylpEDRQVSGL----------FLDAPVRWNT---VMfnQPSWWQQGKREAAV--VERYHRALGIKLADGDQPV 392
Cdd:COG4778 78 DLAQA-----SPREILALrrrtigyvsqFLRVIPRVSAldvVA--EPLLERGVDREEARarARELLARLNLPERLWDLPP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 393 RTLSGGNQQKVLLARCLEANPLLLIVDEPTRGVDVSARADIYQLLKSVAAQNVAVLMISSDvEEFV-GLADRVLVMHQGR 471
Cdd:COG4778 151 ATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHD-EEVReAVADRVVDVTPFS 229
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
17-164 |
1.37e-12 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 67.11 E-value: 1.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 17 VAVLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDSGELTIGERAFARLNPALAHQL---GIYLVPQEPMLFPN 93
Cdd:PRK10584 23 LSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKLrakHVGFVFQSFMLIPT 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2095916338 94 LSVRENI----LFRLPKRADTTARLQEKLQQLNCQINLDASASTLEVADQQMVEILRGLMREARILILDEPTASL 164
Cdd:PRK10584 103 LNALENVelpaLLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNL 177
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
19-216 |
1.40e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 67.71 E-value: 1.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 19 VLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDSGELTIGERAFARLN-PALAHQLGIylVPQEP-MLFPNLSV 96
Cdd:PRK13632 24 ALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENlKEIRKKIGI--IFQNPdNQFIGATV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 97 RENILFRLPKRADTTARLQEKLQQLNCQIN----LDASASTLEVADQQMVEILRGLMREARILILDEPTASLTPGETERL 172
Cdd:PRK13632 102 EDDIAFGLENKKVPPKKMKDIIDDLAKKVGmedyLDKEPQNLSGGQKQRVAIASVLALNPEIIIFDESTSMLDPKGKREI 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2095916338 173 FSQIRALQA-LDVGIVFISHKLPEIrQLASHVSVMRDGAVVLSGE 216
Cdd:PRK13632 182 KKIMVDLRKtRKKTLISITHDMDEA-ILADKVIVFSEGKLIAQGK 225
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
19-228 |
1.42e-12 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 69.75 E-value: 1.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 19 VLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDSGELTIGERAFARLNPALAHQlGIYLVPQEPM-----LFPN 93
Cdd:PRK10790 356 VLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQ-GVAMVQQDPVvladtFLAN 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 94 LSVRENILFRLPKRADTTARLQEKLQQLNCQIN--LDASASTLEVADQQMVEILRGLMREARILILDEPTASLTPGeTER 171
Cdd:PRK10790 435 VTLGRDISEEQVWQALETVQLAELARSLPDGLYtpLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSG-TEQ 513
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2095916338 172 LFSQirALQAL--DVGIVFISHKLPEIRQlASHVSVMRDGAVVLSGetagyGDQQLISA 228
Cdd:PRK10790 514 AIQQ--ALAAVreHTTLVVIAHRLSTIVE-ADTILVLHRGQAVEQG-----THQQLLAA 564
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
20-212 |
1.45e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 67.93 E-value: 1.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 20 LKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDSGELTIgerAFARLNP--------ALAHQLGIYLVPQEPMLF 91
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITI---AGYHITPetgnknlkKLRKKVSLVFQFPEAQLF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 92 PNlSVRENILFRLPKRADTTARLQEKLQQLNCQINLD---ASASTLEVADQQMVEI-LRGLMR-EARILILDEPTASLTP 166
Cdd:PRK13641 100 EN-TVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLSedlISKSPFELSGGQMRRVaIAGVMAyEPEILCLDEPAAGLDP 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2095916338 167 GETERLFSQIRALQALDVGIVFISHKLPEIRQLASHVSVMRDGAVV 212
Cdd:PRK13641 179 EGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLI 224
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
16-216 |
1.87e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 67.70 E-value: 1.87e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 16 GVAVLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDSGELTI-GERA--FARLnPALAHQLGIylVPQEP-MLF 91
Cdd:PRK13644 14 GTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVsGIDTgdFSKL-QGIRKLVGI--VFQNPeTQF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 92 PNLSVRENILFR-----LPKrADTTARLQEKLQQLNCQINLDASASTLEVADQQMVEILRGLMREARILILDEPTASLTP 166
Cdd:PRK13644 91 VGRTVEEDLAFGpenlcLPP-IEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDP 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2095916338 167 GETERLFSQIRALQALDVGIVFISHKLPEIrQLASHVSVMRDGAVVLSGE 216
Cdd:PRK13644 170 DSGIAVLERIKKLHEKGKTIVYITHNLEEL-HDADRIIVMDRGKIVLEGE 218
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
274-470 |
1.93e-12 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 68.57 E-value: 1.93e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 274 DLSLEIRAGEIVGLAGLVGSGRTEFAETLYGLRPPRAGRIWLENREISQESTRarlasglvylpeDRQVSGLFLD-APVR 352
Cdd:PRK10851 20 DISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHAR------------DRKVGFVFQHyALFR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 353 WNTVMFN------------QPSwwqqgkrEAAVVERYHRALGI----KLADgDQPVRtLSGGNQQKVLLARCLEANPLLL 416
Cdd:PRK10851 88 HMTVFDNiafgltvlprreRPN-------AAAIKAKVTQLLEMvqlaHLAD-RYPAQ-LSGGQKQRVALARALAVEPQIL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2095916338 417 IVDEPTRGVDVSARADIYQLLKSVAAQ-NVAVLMISSDVEEFVGLADRVLVMHQG 470
Cdd:PRK10851 159 LLDEPFGALDAQVRKELRRWLRQLHEElKFTSVFVTHDQEEAMEVADRVVVMSQG 213
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
274-471 |
1.94e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 67.70 E-value: 1.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 274 DLSLEIRAGEIVGLAGLVGSGRTEFAETLYGLRPPRAGRIWLENREISQEST--RARLASGLVYLPEDRQVSGLFLDAPV 351
Cdd:PRK13644 20 NINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKlqGIRKLVGIVFQNPETQFVGRTVEEDL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 352 RWNTVMFNQPSWWQQGKREAAVVEryhraLGIKLADGDQPvRTLSGGNQQKVLLARCLEANPLLLIVDEPTRGVDVSARA 431
Cdd:PRK13644 100 AFGPENLCLPPIEIRKRVDRALAE-----IGLEKYRHRSP-KTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGI 173
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2095916338 432 DIYQLLKSVAAQNVAVLMISSDVEEfVGLADRVLVMHQGR 471
Cdd:PRK13644 174 AVLERIKKLHEKGKTIVYITHNLEE-LHDADRIIVMDRGK 212
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
261-471 |
2.42e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 67.07 E-value: 2.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 261 VLRVEDLT------GEGFIDLSLEIRAGEIVGLAGLVGSGRTEFAETLYGLRPPRAGRIWLENREISQESTR-ARLASGL 333
Cdd:PRK13647 4 IIEVEDLHfrykdgTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKwVRSKVGL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 334 VYLPEDRQVSglfldAPVRWNTVMFNQPSwwqQGKREAAVVERYHRAL-GIKLAD-GDQPVRTLSGGNQQKVLLARCLEA 411
Cdd:PRK13647 84 VFQDPDDQVF-----SSTVWDDVAFGPVN---MGLDKDEVERRVEEALkAVRMWDfRDKPPYHLSYGQKKRVAIAGVLAM 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 412 NPLLLIVDEPTRGVDVSARADIYQLLKSVAAQNVAVLMISSDVEEFVGLADRVLVMHQGR 471
Cdd:PRK13647 156 DPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGR 215
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
18-232 |
3.01e-12 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 66.77 E-value: 3.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 18 AVLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGvETPDS---------GELTIGERAFARLNPALAHQLGIYLVPQEP 88
Cdd:PRK13547 15 AILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAG-DLTGGgaprgarvtGDVTLNGEPLAAIDAPRLARLRAVLPQAAQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 89 MLFPnLSVRENILF-RLPKRADTTARLQEKLQQLNCQINLdASASTL-----------EVADQQMVEILRGL------MR 150
Cdd:PRK13547 94 PAFA-FSAREIVLLgRYPHARRAGALTHRDGEIAWQALAL-AGATALvgrdvttlsggELARVQFARVLAQLwpphdaAQ 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 151 EARILILDEPTASLTPGETERLFSQIRAL-QALDVGIVFISHKLPEIRQLASHVSVMRDGAVVLSGETAGygdqqlisAM 229
Cdd:PRK13547 172 PPRYLLLDEPTAALDLAHQHRLLDTVRRLaRDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPAD--------VL 243
|
...
gi 2095916338 230 TPA 232
Cdd:PRK13547 244 TPA 246
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
260-471 |
3.04e-12 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 67.94 E-value: 3.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 260 PVLRVEDLT----GEGFID-LSLEIRAGEIVGLAGLVGSGRTEFAETLYGLRPPRAGRIWLENREISQESTRARLASGLV 334
Cdd:PRK11607 18 PLLEIRNLTksfdGQHAVDdVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQRPINMMF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 335 ylpedrQVSGLFLDAPVRWNtVMFNQPswwQQGKREAAVVERYHRALGI----KLAdGDQPvRTLSGGNQQKVLLARCLE 410
Cdd:PRK11607 98 ------QSYALFPHMTVEQN-IAFGLK---QDKLPKAEIASRVNEMLGLvhmqEFA-KRKP-HQLSGGQRQRVALARSLA 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2095916338 411 ANPLLLIVDEPTRGVDVSAR----ADIYQLLKSVAAQNVavlMISSDVEEFVGLADRVLVMHQGR 471
Cdd:PRK11607 166 KRPKLLLLDEPMGALDKKLRdrmqLEVVDILERVGVTCV---MVTHDQEEAMTMAGRIAIMNRGK 227
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
260-471 |
3.14e-12 |
|
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: 66.30 E-value: 3.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 260 PVLRVEDL-----TGEGFI----DLSLEIRAGEIVGLAGLVGSGRTEFAETLYGLRPPRAGRIWLENREISQ--ESTRAR 328
Cdd:COG4181 7 PIIELRGLtktvgTGAGELtilkGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFAldEDARAR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 329 LASGL-------------------VYLP-EDRQVSGLFldapvrwntvmfnqpswwqqgKREAAVVERY---HRAlgikl 385
Cdd:COG4181 87 LRARHvgfvfqsfqllptltalenVMLPlELAGRRDAR---------------------ARARALLERVglgHRL----- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 386 adGDQPvRTLSGGNQQKVLLARCLEANPLLLIVDEPTRGVDVSARADIYQLLKSV-AAQNVAVLMISSDVEefvgLA--- 461
Cdd:COG4181 141 --DHYP-AQLSGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELnRERGTTLVLVTHDPA----LAarc 213
|
250
....*....|
gi 2095916338 462 DRVLVMHQGR 471
Cdd:COG4181 214 DRVLRLRAGR 223
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
3-216 |
3.65e-12 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 68.58 E-value: 3.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 3 PLLEARQIRKQF---SGV--------AVLKGIDFTLCAGQVHALMGGNGAGKST----LMKIIAGvetpdSGELTIGERA 67
Cdd:PRK15134 274 PLLDVEQLQVAFpirKGIlkrtvdhnVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLINS-----QGEIWFDGQP 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 68 FARLNPA--LAHQLGIYLVPQEP--MLFPNLSVRENIL--FRLPKRADTTARLQEKLQQLNCQINLDASA-----STLEV 136
Cdd:PRK15134 349 LHNLNRRqlLPVRHRIQVVFQDPnsSLNPRLNVLQIIEegLRVHQPTLSAAQREQQVIAVMEEVGLDPETrhrypAEFSG 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 137 ADQQMVEILRGLMREARILILDEPTASLTPGETERLFSQIRALQAL-DVGIVFISHKLPEIRQLASHVSVMRDGAVVLSG 215
Cdd:PRK15134 429 GQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKhQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQG 508
|
.
gi 2095916338 216 E 216
Cdd:PRK15134 509 D 509
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
17-219 |
3.86e-12 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 67.03 E-value: 3.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 17 VAVLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDSGELTI-GERAFARlNPALAHQLGiyLV-PQEPMLFPNL 94
Cdd:COG4586 35 VEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVlGYVPFKR-RKEFARRIG--VVfGQRSQLWWDL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 95 SVRE--NIL---FRLPKradttARLQEKLQQLncqinldasASTLEVAD------------QQM-VEILRGLMREARILI 156
Cdd:COG4586 112 PAIDsfRLLkaiYRIPD-----AEYKKRLDEL---------VELLDLGElldtpvrqlslgQRMrCELAAALLHRPKILF 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 157 LDEPTASLTpgeterLFSQIRALQAL-------DVGIVFISHKLPEIRQLASHVSVMRDGAVVLSGETAG 219
Cdd:COG4586 178 LDEPTIGLD------VVSKEAIREFLkeynrerGTTILLTSHDMDDIEALCDRVIVIDHGRIIYDGSLEE 241
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
275-471 |
4.28e-12 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 66.15 E-value: 4.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 275 LSLEIRAGEIVGLAGLVGSGRTEFAETLYGLRPPRAGRIWLENREISQestrARLASGLVYLPEDRQVSGLFLDApvrwn 354
Cdd:PRK10619 24 VSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINL----VRDKDGQLKVADKNQLRLLRTRL----- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 355 TVMFNQPSWW--------------------QQGKREAAVveRYHRALGI-KLADGDQPVRtLSGGNQQKVLLARCLEANP 413
Cdd:PRK10619 95 TMVFQHFNLWshmtvlenvmeapiqvlglsKQEARERAV--KYLAKVGIdERAQGKYPVH-LSGGQQQRVSIARALAMEP 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2095916338 414 LLLIVDEPTRGVDVSARADIYQLLKSVAAQNVAVLMISSDVEEFVGLADRVLVMHQGR 471
Cdd:PRK10619 172 EVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGK 229
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-217 |
6.39e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 65.63 E-value: 6.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 1 MKPLLEARQIRKQFSGVAVLKGIDFTLCAGQVHALMGGNGAGKSTLMKI---------IAGVEtpdsGELTI-GERAFAR 70
Cdd:PRK14267 1 MKFAIETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTfnrllelneEARVE----GEVRLfGRNIYSP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 71 LNPALAHQLGIYLVPQEPMLFPNLSVRENI--------LFRLPKRADTTARLQEKLQQLNCQIN--LDASASTLEVADQQ 140
Cdd:PRK14267 77 DVDPIEVRREVGMVFQYPNPFPHLTIYDNVaigvklngLVKSKKELDERVEWALKKAALWDEVKdrLNDYPSNLSGGQRQ 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2095916338 141 MVEILRGLMREARILILDEPTASLTPGETERLFSQIRALQAlDVGIVFISHKLPEIRQLASHVSVMRDGAVVLSGET 217
Cdd:PRK14267 157 RLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKK-EYTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPT 232
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
274-471 |
7.39e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 65.88 E-value: 7.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 274 DLSLEIRAGEIVGLAGLVGSGRTEFAETLYGLRPPRAGRIWLENREISQEST--RARLASGLVYLPEDRQvsglfLDAPV 351
Cdd:PRK13633 28 DVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENlwDIRNKAGMVFQNPDNQ-----IVATI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 352 RWNTVMFNQPSWWQQGKREAAVVERYHRALGIkLADGDQPVRTLSGGNQQKVLLARCLEANPLLLIVDEPTRGVDVSARA 431
Cdd:PRK13633 103 VEEDVAFGPENLGIPPEEIRERVDESLKKVGM-YEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGRR 181
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2095916338 432 DIYQLLKSVAAQ-NVAVLMISSDVEEFVGlADRVLVMHQGR 471
Cdd:PRK13633 182 EVVNTIKELNKKyGITIILITHYMEEAVE-ADRIIVMDSGK 221
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
269-471 |
8.72e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 65.54 E-value: 8.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 269 GEGFIDLSLEIRAGEIVGLAGLVGSGRTEFAETLYGLRPPRAGRIWLENREISQESTRARLAS-----GLVY-LPEdrqv 342
Cdd:PRK13649 20 GRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNKDIKQirkkvGLVFqFPE---- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 343 SGLFLDAPVRwnTVMFNqPSWWQQGKREAAVVERYHRAL-GIKLADGDQPVRTLSGGNQQKVLLARCLEANPLLLIVDEP 421
Cdd:PRK13649 96 SQLFEETVLK--DVAFG-PQNFGVSQEEAEALAREKLALvGISESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEP 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2095916338 422 TRGVDVSARADIYQLLKSVAAQNVAVLMISSDVEEFVGLADRVLVMHQGR 471
Cdd:PRK13649 173 TAGLDPKGRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGK 222
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
12-209 |
8.98e-12 |
|
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: 64.41 E-value: 8.98e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 12 KQFSGVAVLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDSGELTIGERafarlnpalahqlgIYLVPQEPMLF 91
Cdd:cd03250 13 GEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS--------------IAYVSQEPWIQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 92 pNLSVRENILFRLPKRADttaRLQEKLQqlNCQinLDASASTLEVADQ---------------QMVEILRGLMREARILI 156
Cdd:cd03250 79 -NGTIRENILFGKPFDEE---RYEKVIK--ACA--LEPDLEILPDGDLteigekginlsggqkQRISLARAVYSDADIYL 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2095916338 157 LDEPTASLTPgETER-LFSQ-IRALQALDVGIVFISHKLPEIRQlASHVSVMRDG 209
Cdd:cd03250 151 LDDPLSAVDA-HVGRhIFENcILGLLLNNKTRILVTHQLQLLPH-ADQIVVLDNG 203
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
274-437 |
9.54e-12 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 65.39 E-value: 9.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 274 DLSLEIRAGEIVGLAGLVGSGRTEFAETLYGLRPPRAGRIWLENREISQESTR--AR---LASGLVYLPEDRQVSGLFld 348
Cdd:PRK10253 25 NLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKevARrigLLAQNATTPGDITVQELV-- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 349 APVRWNtvmfNQPSWWQQGKREAAVVERYHRALGI-KLADgdQPVRTLSGGNQQKVLLARCLEANPLLLIVDEPTRGVDV 427
Cdd:PRK10253 103 ARGRYP----HQPLFTRWRKEDEEAVTKAMQATGItHLAD--QSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDI 176
|
170
....*....|
gi 2095916338 428 SARADIYQLL 437
Cdd:PRK10253 177 SHQIDLLELL 186
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
5-65 |
1.23e-11 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 66.68 E-value: 1.23e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2095916338 5 LEARQIRKQFSGVAVLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDSGELTIGE 65
Cdd:PRK11819 325 IEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGE 385
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
15-203 |
1.34e-11 |
|
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: 62.94 E-value: 1.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 15 SGVAVLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDSGELTIGERAfarlnpalahqlGIYLVPQEPmLFPNL 94
Cdd:cd03223 12 DGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEGE------------DLLFLPQRP-YLPLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 95 SVRENILFrlpkradttarlqeklqqlncqinldASASTLEVADQQMVEILRGLMREARILILDEPTASLTPGETERLFs 174
Cdd:cd03223 79 TLREQLIY--------------------------PWDDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLY- 131
|
170 180
....*....|....*....|....*....
gi 2095916338 175 qiRALQALDVGIVFISHKlPEIRQLASHV 203
Cdd:cd03223 132 --QLLKELGITVISVGHR-PSLWKFHDRV 157
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
274-470 |
1.38e-11 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 64.72 E-value: 1.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 274 DLSLEIRAGEIVGLAGLVGSGRTEFAETLYGLRPPRAGRIWLENREISQESTRarlaSGLVYlpedrQVSGLfldapVRW 353
Cdd:PRK11248 19 DINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAE----RGVVF-----QNEGL-----LPW 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 354 NTVMFNQPSWWQ-QGKREAAVVERYHRALG-IKLADGDQ-PVRTLSGGNQQKVLLARCLEANPLLLIVDEPTRGVDVSAR 430
Cdd:PRK11248 85 RNVQDNVAFGLQlAGVEKMQRLEIAHQMLKkVGLEGAEKrYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTR 164
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2095916338 431 ADIYQLLKSV-AAQNVAVLMISSDVEEFVGLADRVLVMHQG 470
Cdd:PRK11248 165 EQMQTLLLKLwQETGKQVLLITHDIEEAVFMATELVLLSPG 205
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
274-477 |
1.41e-11 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 64.45 E-value: 1.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 274 DLSLEIRAGEIVGLAGLVGSGRTEFAETLYGLRPPRAGRIWLENREISQESTRARLAS-----GLVYlpedrQVSGLFLD 348
Cdd:PRK11629 27 NVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAELrnqklGFIY-----QFHHLLPD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 349 APVRWNTVMfnqpSWWQQGKREAAVVERYH---RALGIKLADGDQPVRtLSGGNQQKVLLARCLEANPLLLIVDEPTRGV 425
Cdd:PRK11629 102 FTALENVAM----PLLIGKKKPAEINSRALemlAAVGLEHRANHRPSE-LSGGERQRVAIARALVNNPRLVLADEPTGNL 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2095916338 426 DVSARADIYQLLKSV-AAQNVAVLMISSDVeEFVGLADRVLVMHQGRHSGELA 477
Cdd:PRK11629 177 DARNADSIFQLLGELnRLQGTAFLVVTHDL-QLAKRMSRQLEMRDGRLTAELS 228
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
4-224 |
1.48e-11 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 64.43 E-value: 1.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 4 LLEARQIRKQFSGVAVLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVE--TPDSGELTIGERAFARLNPALAHQLGI 81
Cdd:PRK09580 1 MLSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLELSPEDRAGEGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 82 YLVPQEPMLFPNLS-----------VRENILFRLPKRADTTARLQEKLQQLNCQINLDASASTLEVA--DQQMVEILRGL 148
Cdd:PRK09580 81 FMAFQYPVEIPGVSnqfflqtalnaVRSYRGQEPLDRFDFQDLMEEKIALLKMPEDLLTRSVNVGFSggEKKRNDILQMA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 149 MREARILILDEPTASLTPGETERLFSQIRALQALDVGIVFISHK---LPEIRqlASHVSVMRDGAVVLSG--------ET 217
Cdd:PRK09580 161 VLEPELCILDESDSGLDIDALKIVADGVNSLRDGKRSFIIVTHYqriLDYIK--PDYVHVLYQGRIVKSGdftlvkqlEE 238
|
250
....*....|
gi 2095916338 218 AGYG---DQQ 224
Cdd:PRK09580 239 QGYGwltEQQ 248
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
274-471 |
1.50e-11 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 66.65 E-value: 1.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 274 DLSLEIRAGEIVGLAGLVGSGRTEFAETLYGLRPpragriwlenreisqestrarlASGLVYLPEDRQVSG---LFLDAP 350
Cdd:PRK15134 27 DVSLQIEAGETLALVGESGSGKSVTALSILRLLP----------------------SPPVVYPSGDIRFHGeslLHASEQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 351 ----VRWNTV--MFNQP------------------SWWQQGKREAAVVE--RYHRALGIKLADG---DQPvRTLSGGNQQ 401
Cdd:PRK15134 85 tlrgVRGNKIamIFQEPmvslnplhtlekqlyevlSLHRGMRREAARGEilNCLDRVGIRQAAKrltDYP-HQLSGGERQ 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2095916338 402 KVLLARCLEANPLLLIVDEPTRGVDVSARADIYQLLKSVAAQ-NVAVLMISSDVEEFVGLADRVLVMHQGR 471
Cdd:PRK15134 164 RVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQElNMGLLFITHNLSIVRKLADRVAVMQNGR 234
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
275-488 |
1.73e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 64.73 E-value: 1.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 275 LSLEIRAGEIVGLAGLVGSGRTEFAETLYGLRPPRAGRIWLENREISQEST-RARLASGLVYLPEDRQVSGLFLDapvrw 353
Cdd:PRK13642 26 VSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVwNLRRKIGMVFQNPDNQFVGATVE----- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 354 NTVMFNQPSwwqQGKREAAVVERYHRAL-GIKLAD--GDQPVRtLSGGNQQKVLLARCLEANPLLLIVDEPTRGVDVSAR 430
Cdd:PRK13642 101 DDVAFGMEN---QGIPREEMIKRVDEALlAVNMLDfkTREPAR-LSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGR 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2095916338 431 ADIYQLLKSVAAQ-NVAVLMISSDVEEfVGLADRVLVMhqgrHSGELARQAVTVDRMMT 488
Cdd:PRK13642 177 QEIMRVIHEIKEKyQLTVLSITHDLDE-AASSDRILVM----KAGEIIKEAAPSELFAT 230
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
262-467 |
2.19e-11 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 63.27 E-value: 2.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 262 LRVEDLT-----GEGFIDLSLEIRAGEIVGLAGLVGSGRTEFAETLYGLRPPRA---GRIWLENREIsqestrARLAsgl 333
Cdd:COG4136 2 LSLENLTitlggRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAFsasGEVLLNGRRL------TALP--- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 334 vylPEDRQVSGLFLDAP------VrWNTVMFNQPSWWQQGKREAAVVEryhrAL-GIKLAD-GDQPVRTLSGGNQQKVLL 405
Cdd:COG4136 73 ---AEQRRIGILFQDDLlfphlsV-GENLAFALPPTIGRAQRRARVEQ----ALeEAGLAGfADRDPATLSGGQRARVAL 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2095916338 406 ARCLEANPLLLIVDEPTRGVDVSARADIYQLLKS-VAAQNVAVLMISSDVEEfVGLADRVLVM 467
Cdd:COG4136 145 LRALLAEPRALLLDEPFSKLDAALRAQFREFVFEqIRQRGIPALLVTHDEED-APAAGRVLDL 206
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
274-470 |
2.21e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 64.42 E-value: 2.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 274 DLSLEIRAGEIVGLAGLVGSGRTEFAETLYGLRPPRAGRIWLENREISQEST-----RARLASGLVY-LPEdrqvSGLFL 347
Cdd:PRK13646 25 DVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKdkyirPVRKRIGMVFqFPE----SQLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 348 DAPVRwnTVMFNqPSWWQQGKREaaVVERYHRAL---GIKLADGDQPVRTLSGGNQQKVLLARCLEANPLLLIVDEPTRG 424
Cdd:PRK13646 101 DTVER--EIIFG-PKNFKMNLDE--VKNYAHRLLmdlGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAG 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2095916338 425 VDVSARADIYQLLKSVAA-QNVAVLMISSDVEEFVGLADRVLVMHQG 470
Cdd:PRK13646 176 LDPQSKRQVMRLLKSLQTdENKTIILVSHDMNEVARYADEVIVMKEG 222
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
16-228 |
2.56e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 63.99 E-value: 2.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 16 GVAVLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDSGELTI-GERAFARLNPALAHQLGiyLVPQEP--MLFP 92
Cdd:PRK13647 17 GTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVmGREVNAENEKWVRSKVG--LVFQDPddQVFS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 93 NlSVRENILF-----RLpKRADTTARLQEKLQQLNCQINLDASASTLEVADQQMVEILRGLMREARILILDEPTASLTPG 167
Cdd:PRK13647 95 S-TVWDDVAFgpvnmGL-DKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPR 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2095916338 168 ETERLFSQIRALQALDVGIVFISHKLPEIRQLASHVSVMRDGAVVLSGETAGYGDQQLISA 228
Cdd:PRK13647 173 GQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKSLLTDEDIVEQ 233
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
19-212 |
2.91e-11 |
|
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: 62.81 E-value: 2.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 19 VLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDSGELTIGERAFARLN-PALAHQLGIylVPQEPMLFPNlSVR 97
Cdd:cd03369 23 VLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPlEDLRSSLTI--IPQDPTLFSG-TIR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 98 ENIlfrlpkraDTTARLQEKlqQLNCQINLDASASTLEVADQQMVEILRGLMREARILILDEPTASLTPgETERLFSQIR 177
Cdd:cd03369 100 SNL--------DPFDEYSDE--EIYGALRVSEGGLNLSQGQRQLLCLARALLKRPRVLVLDEATASIDY-ATDALIQKTI 168
|
170 180 190
....*....|....*....|....*....|....*
gi 2095916338 178 ALQALDVGIVFISHKLPEIRQLAShVSVMRDGAVV 212
Cdd:cd03369 169 REEFTNSTILTIAHRLRTIIDYDK-ILVMDAGEVK 202
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
4-162 |
3.72e-11 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 62.51 E-value: 3.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 4 LLEARQI------RKQFSGvavlkgIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDSGELTIGERAFARLNPA--- 74
Cdd:PRK13538 1 MLEARNLacerdeRILFSG------LSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEyhq 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 75 ----LAHQLGIYlvpqepmlfPNLSVRENILF--RLPKRADtTARLQEKLQQLNCQINLDASASTLEVADQQMVEILRGL 148
Cdd:PRK13538 75 dllyLGHQPGIK---------TELTALENLRFyqRLHGPGD-DEALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLW 144
|
170
....*....|....*
gi 2095916338 149 MREARILILDEP-TA 162
Cdd:PRK13538 145 LTRAPLWILDEPfTA 159
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
20-215 |
6.16e-11 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 64.68 E-value: 6.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 20 LKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPD---SGELTIGERafaRLNPALAHQLGIYlVPQEPMLFPNLSV 96
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGM---PIDAKEMRAISAY-VQQDDLFIPTLTV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 97 RENILF----RLPKRADTTARlQEKLQQLNCQINLDASASTLeVADQQMVEILRG-----------LMREARILILDEPT 161
Cdd:TIGR00955 117 REHLMFqahlRMPRRVTKKEK-RERVDEVLQALGLRKCANTR-IGVPGRVKGLSGgerkrlafaseLLTDPPLLFCDEPT 194
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2095916338 162 ASLtpgETERLFSQIRALQALDVG----IVFISHKLPEIRQLASHVSVMRDGAVVLSG 215
Cdd:TIGR00955 195 SGL---DSFMAYSVVQVLKGLAQKgktiICTIHQPSSELFELFDKIILMAEGRVAYLG 249
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
15-203 |
6.48e-11 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 64.44 E-value: 6.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 15 SGVAVLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDSGELTIgerafarlnPALAHQLgiyLVPQEPMLfPNL 94
Cdd:COG4178 374 DGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIAR---------PAGARVL---FLPQRPYL-PLG 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 95 SVRENILFRLPKRADTTARLQEKLQQLncqiNLDASASTLEVAD----------QQMVEILRGLMREARILILDEPTASL 164
Cdd:COG4178 441 TLREALLYPATAEAFSDAELREALEAV----GLGHLAERLDEEAdwdqvlslgeQQRLAFARLLLHKPDWLFLDEATSAL 516
|
170 180 190
....*....|....*....|....*....|....*....
gi 2095916338 165 TPGETERLFSQIRAlQALDVGIVFISHKlPEIRQLASHV 203
Cdd:COG4178 517 DEENEAALYQLLRE-ELPGTTVISVGHR-STLAAFHDRV 553
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
274-477 |
8.22e-11 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 63.19 E-value: 8.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 274 DLSLEIRAGEIVGLAGLVGSGRTEFAETLYGLRPPRAGRI-WL--ENREISQESTRARlasglvylPEDRQVsgLFLDAP 350
Cdd:PRK15079 39 GVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVaWLgkDLLGMKDDEWRAV--------RSDIQM--IFQDPL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 351 VRWNTVM-----FNQPSWWQQGKREAAVVERYHRALGIKLadGDQP------VRTLSGGNQQKVLLARCLEANPLLLIVD 419
Cdd:PRK15079 109 ASLNPRMtigeiIAEPLRTYHPKLSRQEVKDRVKAMMLKV--GLLPnlinryPHEFSGGQCQRIGIARALILEPKLIICD 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2095916338 420 EPTRGVDVSARADIYQLLKSVAAQ-NVAVLMISSDVEEFVGLADRVLVMHQGrHSGELA 477
Cdd:PRK15079 187 EPVSALDVSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVLVMYLG-HAVELG 244
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
30-215 |
8.48e-11 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 63.90 E-value: 8.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 30 GQVHALMGGNGAGKSTLMKIIAGVETPDSGELTIGERAFARLNPALAHQL---GIYLVPQEPMLFPNLSVRENILFRLPK 106
Cdd:PRK10070 54 GEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVrrkKIAMVFQSFALMPHMTVLDNTAFGMEL 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 107 RADTTARLQEKLQQLNCQINLDASA----STLEVADQQMVEILRGLMREARILILDEPTASLTPGETERLFSQIRALQAL 182
Cdd:PRK10070 134 AGINAEERREKALDALRQVGLENYAhsypDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQAK 213
|
170 180 190
....*....|....*....|....*....|....
gi 2095916338 183 -DVGIVFISHKLPEIRQLASHVSVMRDGAVVLSG 215
Cdd:PRK10070 214 hQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVG 247
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
23-215 |
9.01e-11 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 62.48 E-value: 9.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 23 IDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDSGELTI-GERAfarlnPALAHQlGIY-------LVPQEPMLFPNL 94
Cdd:PRK11831 26 ISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFdGENI-----PAMSRS-RLYtvrkrmsMLFQSGALFTDM 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 95 SVRENILFrlPKRADTtaRLQEKLQQLNCQINLDASAstLEVADQQMVEILRGLMR-----------EARILILDEPTAS 163
Cdd:PRK11831 100 NVFDNVAY--PLREHT--QLPAPLLHSTVMMKLEAVG--LRGAAKLMPSELSGGMArraalaraialEPDLIMFDEPFVG 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2095916338 164 LTPGETERLFSQIRAL-QALDVGIVFISHKLPEIRQLASHVSVMRDGAVVLSG 215
Cdd:PRK11831 174 QDPITMGVLVKLISELnSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHG 226
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
275-471 |
9.33e-11 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 62.07 E-value: 9.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 275 LSLEIRAGEIVGLAGLVGSGRTEFAETLYGLRPPRAGRIWL------ENREISQEST---RARLASGLVYlpedrQVSGL 345
Cdd:PRK11264 22 IDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVgditidTARSLSQQKGlirQLRQHVGFVF-----QNFNL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 346 FldaPVRwnTVMFN---QPSWWQQGKREAAVVERyhRALGIKLA---DGDQPVRTLSGGNQQKVLLARCLEANPLLLIVD 419
Cdd:PRK11264 97 F---PHR--TVLENiieGPVIVKGEPKEEATARA--RELLAKVGlagKETSYPRRLSGGQQQRVAIARALAMRPEVILFD 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2095916338 420 EPTRGVDVSARADIYQLLKSVAAQNVAVLMISSDVEEFVGLADRVLVMHQGR 471
Cdd:PRK11264 170 EPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGR 221
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
274-470 |
9.68e-11 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 62.50 E-value: 9.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 274 DLSLEIRAGEIVGLAGLVGSGRTEFAETLYGLRPPRAGRIWLENREI-----SQESTRARL-----ASGLvylpEDRQVS 343
Cdd:PRK15112 31 PLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLhfgdySYRSQRIRMifqdpSTSL----NPRQRI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 344 GLFLDAPVRWNTVMFNQpswwqqgKREAAVVERYhRALGIKLADGDQPVRTLSGGNQQKVLLARCLEANPLLLIVDEPTR 423
Cdd:PRK15112 107 SQILDFPLRLNTDLEPE-------QREKQIIETL-RQVGLLPDHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALA 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2095916338 424 GVDVSARADIYQL-LKSVAAQNVAVLMISSDVEEFVGLADRVLVMHQG 470
Cdd:PRK15112 179 SLDMSMRSQLINLmLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQG 226
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
17-471 |
1.18e-10 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 63.99 E-value: 1.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 17 VAVLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDSGELT-----IGERAF-ARLNPALAhqlgiYLvPQ--EP 88
Cdd:NF033858 14 TVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEvlggdMADARHrRAVCPRIA-----YM-PQglGK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 89 MLFPNLSVRENILF--RL--PKRADTTARLQEKLQQLNCQINLDASASTLEVADQQMVEILRGLMREARILILDEPTASL 164
Cdd:NF033858 88 NLYPTLSVFENLDFfgRLfgQDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCALIHDPDLLILDEPTTGV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 165 TPgeTER-----LFSQIRALQA-LDVgIV----------FishklpeirqlaSHVSVMRDGAVVLSGETA------GYG- 221
Cdd:NF033858 168 DP--LSRrqfweLIDRIRAERPgMSV-LVataymeeaerF------------DWLVAMDAGRVLATGTPAellartGADt 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 222 -DQQLIsAMTPAS--RDHALsdtqklwLALPgNRRTQAQDFPVLRVEDLT---GEgFI---DLSLEIRAGEIVGLAGLVG 292
Cdd:NF033858 233 lEAAFI-ALLPEEkrRGHQP-------VVIP-PRPADDDDEPAIEARGLTmrfGD-FTavdHVSFRIRRGEIFGFLGSNG 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 293 SGRTEFAETLYGLRPPRAGRIWLENREI--SQESTRARLAsglvYLpedRQVSGLFLDAPVRWNTVM----FNQPSwWQQ 366
Cdd:NF033858 303 CGKSTTMKMLTGLLPASEGEAWLFGQPVdaGDIATRRRVG----YM---SQAFSLYGELTVRQNLELharlFHLPA-AEI 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 367 GKREAAVVERYHralgikLAD-GDQPVRTLSGGNQQKVLLARCLEANPLLLIVDEPTRGVDVSARADIYQLLKSVAAQNV 445
Cdd:NF033858 375 AARVAEMLERFD------LADvADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVARDMFWRLLIELSREDG 448
|
490 500
....*....|....*....|....*....
gi 2095916338 446 AVLMISSdveEFVGLA---DRVLVMHQGR 471
Cdd:NF033858 449 VTIFIST---HFMNEAercDRISLMHAGR 474
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
272-449 |
1.30e-10 |
|
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: 60.84 E-value: 1.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 272 FIDLSLEIRAGEIVGLAGLVGSGRTEFAETLYGLRPPRAGRIWLENREISQesTRARLASGLVYLPedrQVSGLFLDAPV 351
Cdd:TIGR01189 16 FEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAE--QRDEPHENILYLG---HLPGLKPELSA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 352 RWNTVMFNQPSWWQQGKREAAVVEryhralgIKLAD-GDQPVRTLSGGNQQKVLLARCLEANPLLLIVDEPTRGVDVSAR 430
Cdd:TIGR01189 91 LENLHFWAAIHGGAQRTIEDALAA-------VGLTGfEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGV 163
|
170
....*....|....*....
gi 2095916338 431 ADIYQLLKSVAAQNVAVLM 449
Cdd:TIGR01189 164 ALLAGLLRAHLARGGIVLL 182
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
274-470 |
1.32e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 62.34 E-value: 1.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 274 DLSLEIRAGEIVGLAGLVGSGRTEFAETLYGLRPPRAGRIWLENREISQESTRARLAS-----GLVY-LPEdrqvSGLFL 347
Cdd:PRK13634 25 DVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKKNKKLKPlrkkvGIVFqFPE----HQLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 348 DapvrwnTVM----FNqPSWWQQGKREAavvERYHRALgIKLADGDQPVRT-----LSGGNQQKVLLARCLEANPLLLIV 418
Cdd:PRK13634 101 E------TVEkdicFG-PMNFGVSEEDA---KQKAREM-IELVGLPEELLArspfeLSGGQMRRVAIAGVLAMEPEVLVL 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2095916338 419 DEPTRGVDVSARADI----YQLLKSvaaQNVAVLMISSDVEEFVGLADRVLVMHQG 470
Cdd:PRK13634 170 DEPTAGLDPKGRKEMmemfYKLHKE---KGLTTVLVTHSMEDAARYADQIVVMHKG 222
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
4-164 |
1.38e-10 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 61.64 E-value: 1.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 4 LLEARQIRKQFSGVAVLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDSGELTIGERAFArlNPALAHQlgiyL 83
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVE--GPGAERG----V 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 84 VPQEPMLFPNLSVRENILFRLPKRADTTARLQEKLQQLNCQINLDASAS----TLEVADQQMVEILRGLMREARILILDE 159
Cdd:PRK11248 75 VFQNEGLLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKryiwQLSGGQRQRVGIARALAANPQLLLLDE 154
|
....*
gi 2095916338 160 PTASL 164
Cdd:PRK11248 155 PFGAL 159
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
258-471 |
1.55e-10 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 61.16 E-value: 1.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 258 DFPVLRvedltgegfiDLSLEIRAGEIVGLAGLVGSGRTEFAETLYGLRPPRAGRIWLENREISQEST---RARLASGLV 334
Cdd:COG1126 13 DLEVLK----------GISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKKdinKLRRKVGMV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 335 YlpedrQVSGLF-----LD----APVRwntVmfnqpswwqQGKREAAVVERYHRALG-IKLAD-GDQPVRTLSGGNQQKV 403
Cdd:COG1126 83 F-----QQFNLFphltvLEnvtlAPIK---V---------KKMSKAEAEERAMELLErVGLADkADAYPAQLSGGQQQRV 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2095916338 404 LLARCLEANPLLLIVDEPTrgvdvSA-----RADIYQLLKSVAAQNVAVLMIS------SDVeefvglADRVLVMHQGR 471
Cdd:COG1126 146 AIARALAMEPKVMLFDEPT-----SAldpelVGEVLDVMRDLAKEGMTMVVVThemgfaREV------ADRVVFMDGGR 213
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
242-471 |
1.61e-10 |
|
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: 61.01 E-value: 1.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 242 QKLWLALPGNRRTQAQDFPVLRvedltgegfiDLSLEIRAGEIVGLAGLVGSGRTEFAETLYGLRPPRAGRIWLENReis 321
Cdd:cd03220 18 SSLKKLGILGRKGEVGEFWALK----------DVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGR--- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 322 qesTRARLASGlvylpedrqvSGLFLDAPVRWNtVMFNQpSWWqqGKREAAVVERYHR-----ALGiklADGDQPVRTLS 396
Cdd:cd03220 85 ---VSSLLGLG----------GGFNPELTGREN-IYLNG-RLL--GLSRKEIDEKIDEiiefsELG---DFIDLPVKTYS 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2095916338 397 GGNQQKVLLARCLEANPLLLIVDEPTRGVDVSARADIYQLLKSVAAQNVAVLMISSDVEEFVGLADRVLVMHQGR 471
Cdd:cd03220 145 SGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGK 219
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
274-479 |
1.73e-10 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 63.20 E-value: 1.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 274 DLSLEIRAGEIVGLAGLVGSGRTEFAETLYGLRPPRAGRIWLENREISQESTRArLASGLVYLPEDRQVsglfLDAPVRW 353
Cdd:PRK10790 359 NINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSV-LRQGVAMVQQDPVV----LADTFLA 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 354 NTVM---FNQPSWWQqgKREAAVVERYHRAL--GIKLADGDQPvRTLSGGNQQKVLLARCLEANPLLLIVDEPTRGVDVS 428
Cdd:PRK10790 434 NVTLgrdISEEQVWQ--ALETVQLAELARSLpdGLYTPLGEQG-NNLSVGQKQLLALARVLVQTPQILILDEATANIDSG 510
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 429 ARADIYQLLKSVAAQNVAVLM---ISSDVEefvglADRVLVMH------QGRHSGELARQ 479
Cdd:PRK10790 511 TEQAIQQALAAVREHTTLVVIahrLSTIVE-----ADTILVLHrgqaveQGTHQQLLAAQ 565
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
274-471 |
1.74e-10 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 61.25 E-value: 1.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 274 DLSLEIRAGEIVGLAGLVGSGRTEFAETLYGLRPP----RAGRIWLENREISQESTRARLASglvylpedrqvsglflda 349
Cdd:PRK10418 21 GVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGRVLLDGKPVAPCALRGRKIA------------------ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 350 pvrwnTVMFNQPSWWQQGKREAAVVERYHRALGIKLADG-----------DQPVRTL-------SGGNQQKVLLARCLEA 411
Cdd:PRK10418 83 -----TIMQNPRSAFNPLHTMHTHARETCLALGKPADDAtltaaleavglENAARVLklypfemSGGMLQRMMIALALLC 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2095916338 412 NPLLLIVDEPTRGVDVSARADIYQLLKS-VAAQNVAVLMISSDVEEFVGLADRVLVMHQGR 471
Cdd:PRK10418 158 EAPFIIADEPTTDLDVVAQARILDLLESiVQKRALGMLLVTHDMGVVARLADDVAVMSHGR 218
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
274-471 |
2.06e-10 |
|
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: 60.59 E-value: 2.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 274 DLSLEIRAGEIVGLAGLVGSGRTEFAETLYGLRPPRAGRIWLENREISQESTRaRLASGLVYLPEDRQvsgLFlDAPVRW 353
Cdd:cd03244 22 NISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLH-DLRSRISIIPQDPV---LF-SGTIRS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 354 NTVMFNQPS---WWQQGKREA--AVVERYHRALGIKLADGDqpvRTLSGGNQQKVLLARCLEANPLLLIVDEPTRGVDVS 428
Cdd:cd03244 97 NLDPFGEYSdeeLWQALERVGlkEFVESLPGGLDTVVEEGG---ENLSVGQRQLLCLARALLRKSKILVLDEATASVDPE 173
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2095916338 429 ARADIYQLLKSVAAqNVAVLMISSDVEEFVGlADRVLVMHQGR 471
Cdd:cd03244 174 TDALIQKTIREAFK-DCTVLTIAHRLDTIID-SDRILVLDKGR 214
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
274-470 |
2.18e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 61.22 E-value: 2.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 274 DLSLEIRAGEIVGLAGLVGSGRTEFAETL------YGLRPPRAGRIWLENREISQ-ESTRARLASGLVYlpedrQVSGLF 346
Cdd:PRK14246 28 DITIKIPNNSIFGIMGPSGSGKSTLLKVLnrlieiYDSKIKVDGKVLYFGKDIFQiDAIKLRKEVGMVF-----QQPNPF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 347 LDAPVrWNTVMFNQPSWWQQGKRE-AAVVERYHRALGIKLADGDQ---PVRTLSGGNQQKVLLARCLEANPLLLIVDEPT 422
Cdd:PRK14246 103 PHLSI-YDNIAYPLKSHGIKEKREiKKIVEECLRKVGLWKEVYDRlnsPASQLSGGQQQRLTIARALALKPKVLLMDEPT 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2095916338 423 RGVDVSARADIYQLLKSVAAQnVAVLMISSDVEEFVGLADRVLVMHQG 470
Cdd:PRK14246 182 SMIDIVNSQAIEKLITELKNE-IAIVIVSHNPQQVARVADYVAFLYNG 228
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
274-471 |
2.38e-10 |
|
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: 60.18 E-value: 2.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 274 DLSLEIRAGEIVGLAGLVGSGRTEFAETLYGlrppragriwlenrEISQESTRARLASGLVYLPedrQVSGLfLDAPVRW 353
Cdd:cd03250 23 DINLEVPKGELVAIVGPVGSGKSSLLSALLG--------------ELEKLSGSVSVPGSIAYVS---QEPWI-QNGTIRE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 354 NtVMFNQPswWQQgkreaavvERYHRAL-------GIK-LADGDQPV-----RTLSGGNQQKVLLARCLEANPLLLIVDE 420
Cdd:cd03250 85 N-ILFGKP--FDE--------ERYEKVIkacalepDLEiLPDGDLTEigekgINLSGGQKQRISLARAVYSDADIYLLDD 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2095916338 421 PTRGVDVSARADIYQ-LLKSVAAQNVAVLMISSDVeEFVGLADRVLVMHQGR 471
Cdd:cd03250 154 PLSAVDAHVGRHIFEnCILGLLLNNKTRILVTHQL-QLLPHADQIVVLDNGR 204
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
4-251 |
2.60e-10 |
|
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: 63.11 E-value: 2.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 4 LLEARQIRKQFSGVAVlKGIDfTLCAG----QVHALMGGNGAGKSTLMKIIAGVETPDSGELTIGERAFARlNPALAHQL 79
Cdd:TIGR01257 1937 ILRLNELTKVYSGTSS-PAVD-RLCVGvrpgECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT-NISDVHQN 2013
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 80 GIYlVPQEPMLFPNLSVRENILFRLPKRADTTARLQE----KLQQLNCQINLDASASTLEVADQQMVEILRGLMREARIL 155
Cdd:TIGR01257 2014 MGY-CPQFDAIDDLLTGREHLYLYARLRGVPAEEIEKvanwSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLV 2092
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 156 ILDEPTASLTPGETERLFSQIRALQALDVGIVFISHKLPEIRQLASHVSVMRDGAVVLSGE----TAGYGDQQLISAMTP 231
Cdd:TIGR01257 2093 LLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGTiqhlKSKFGDGYIVTMKIK 2172
|
250 260
....*....|....*....|
gi 2095916338 232 ASRDHALSDTQKLWLALPGN 251
Cdd:TIGR01257 2173 SPKDDLLPDLNPVEQFFQGN 2192
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
254-453 |
2.70e-10 |
|
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: 62.38 E-value: 2.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 254 TQAQDFPVLRVEDLT------GEGFIDLSLEIRAGEIVGLAGLVGSGRTEFAETLYGLRPPRAGRIWLENREISQESTRA 327
Cdd:TIGR02868 327 AVGLGKPTLELRDLSagypgaPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDE 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 328 rLASGLVYLPEDRQVsglfLDAPVRWNtVMFNQPS------WWQQgkrEAAVVERYHRALgiklADGDQPV-----RTLS 396
Cdd:TIGR02868 407 -VRRRVSVCAQDAHL----FDTTVREN-LRLARPDatdeelWAAL---ERVGLADWLRAL----PDGLDTVlgeggARLS 473
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2095916338 397 GGNQQKVLLARCLEANPLLLIVDEPTRGVDVSARADIYQLLKSvAAQNVAVLMISSD 453
Cdd:TIGR02868 474 GGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLA-ALSGRTVVLITHH 529
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
275-470 |
2.83e-10 |
|
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: 63.11 E-value: 2.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 275 LSLEIRAGEIVGLAGLVGSGRTEFAETLYGLRPPRAGRIWLENREISQESTRARLASGlvYLPE----DRQVSG---LFL 347
Cdd:TIGR01257 1958 LCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISDVHQNMG--YCPQfdaiDDLLTGrehLYL 2035
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 348 DAPVRwntvmfNQPSwwqqgkREAAVVERYH-RALGIKLAdGDQPVRTLSGGNQQKVLLARCLEANPLLLIVDEPTRGVD 426
Cdd:TIGR01257 2036 YARLR------GVPA------EEIEKVANWSiQSLGLSLY-ADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMD 2102
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2095916338 427 VSARADIYQLLKSVAAQNVAVLMISSDVEEFVGLADRVLVMHQG 470
Cdd:TIGR01257 2103 PQARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKG 2146
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
274-471 |
3.50e-10 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 61.63 E-value: 3.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 274 DLSLEIRAGEIVGLAGLVGSGRTEFAETLYGLRPPRAGRIWLENREISQESTRAR--------------------LASGL 333
Cdd:COG3839 21 DIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKDRniamvfqsyalyphmtvyenIAFPL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 334 ----VYLPE-DRQVsglfldapvrwntvmfnqpswwqqgkREAAvveryhRALGI-KLADgdQPVRTLSGGNQQKVLLAR 407
Cdd:COG3839 101 klrkVPKAEiDRRV--------------------------REAA------ELLGLeDLLD--RKPKQLSGGQRQRVALGR 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2095916338 408 CLEANPLLLIVDEPTRGVD----VSARADIYQLLKSVaaqNVAVLMISSDVEEFVGLADRVLVMHQGR 471
Cdd:COG3839 147 ALVREPKVFLLDEPLSNLDaklrVEMRAEIKRLHRRL---GTTTIYVTHDQVEAMTLADRIAVMNDGR 211
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
388-471 |
3.69e-10 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 59.58 E-value: 3.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 388 GDQPVRTLSGGNQQKVLLARCLEANPLLLIVDEPTRGVDVSARADIYQLLKSVAAQNVAVLMIS----SDveEFVGLADR 463
Cdd:cd03233 112 GNEFVRGISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTALEILKCIRTMADVLKTTTFVSlyqaSD--EIYDLFDK 189
|
....*...
gi 2095916338 464 VLVMHQGR 471
Cdd:cd03233 190 VLVLYEGR 197
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
2-164 |
3.72e-10 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 62.11 E-value: 3.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 2 KPLLEARQIRKQFSGvavlkgidFTLCA--GQVH-----ALMGGNGAGKSTLMKIIAGVETPDSGELTIGERafarlnpa 74
Cdd:COG1245 339 ETLVEYPDLTKSYGG--------FSLEVegGEIRegevlGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLK-------- 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 75 LAH--QlgiYLVPQEPMlfpnlSVRENILFRLPKRADTTARLQEKLQQLNCQINLDASASTLEVADQQMVEILRGLMREA 152
Cdd:COG1245 403 ISYkpQ---YISPDYDG-----TVEEFLRSANTDDFGSSYYKTEIIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDA 474
|
170
....*....|..
gi 2095916338 153 RILILDEPTASL 164
Cdd:COG1245 475 DLYLLDEPSAHL 486
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
274-471 |
3.80e-10 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 60.11 E-value: 3.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 274 DLSLEIRAGEIVGLAGLVGSGRTEFAETLYGLRPPRAGRIWLEN----------REISQEStrarlasGLVYlpedrQVS 343
Cdd:PRK09493 19 NIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGlkvndpkvdeRLIRQEA-------GMVF-----QQF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 344 GLFLDAPVRWNtVMFNQPSWWQQGKREAavvERYHRALGIK--LAD-GDQPVRTLSGGNQQKVLLARCLEANPLLLIVDE 420
Cdd:PRK09493 87 YLFPHLTALEN-VMFGPLRVRGASKEEA---EKQARELLAKvgLAErAHHYPSELSGGQQQRVAIARALAVKPKLMLFDE 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2095916338 421 PTRGVDVSARADIYQLLKSVAAQNVAVLMISSDVEEFVGLADRVLVMHQGR 471
Cdd:PRK09493 163 PTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGR 213
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
274-471 |
3.99e-10 |
|
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: 59.35 E-value: 3.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 274 DLSLEIRAGEIVGLAGLVGSGRTEFAETLYGLRPPRAGRIWLENREISQESTRaRLASGLVYLPEDRqvsgLFLDAPVRW 353
Cdd:cd03369 26 NVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLE-DLRSSLTIIPQDP----TLFSGTIRS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 354 NTVMFNQPSwwqqgkreaavVERYHRALGIKlADGDQpvrtLSGGNQQKVLLARCLEANPLLLIVDEPTRGVDVSARADI 433
Cdd:cd03369 101 NLDPFDEYS-----------DEEIYGALRVS-EGGLN----LSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDALI 164
|
170 180 190
....*....|....*....|....*....|....*...
gi 2095916338 434 YQLLKSvAAQNVAVLMISSDVEEFVGLaDRVLVMHQGR 471
Cdd:cd03369 165 QKTIRE-EFTNSTILTIAHRLRTIIDY-DKILVMDAGE 200
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
261-449 |
4.07e-10 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 59.43 E-value: 4.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 261 VLRVEDLT---GEG--FIDLSLEIRAGEIVGLAGLVGSGRTEFAETLYGLRPPRAGRIWLENREISQEstRARLASGLVY 335
Cdd:PRK13538 1 MLEARNLAcerDERilFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQ--RDEYHQDLLY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 336 L-------PEdrqvsglfLDApvrWNTVMFNQPSwWQQGKREAAvveryHRALG-IKLAD-GDQPVRTLSGGNQQKVLLA 406
Cdd:PRK13538 79 LghqpgikTE--------LTA---LENLRFYQRL-HGPGDDEAL-----WEALAqVGLAGfEDVPVRQLSAGQQRRVALA 141
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2095916338 407 RCLEANPLLLIVDEPTRGVDVSARADIYQLLKSVAAQNVAVLM 449
Cdd:PRK13538 142 RLWLTRAPLWILDEPFTAIDKQGVARLEALLAQHAEQGGMVIL 184
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
274-471 |
4.08e-10 |
|
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: 59.94 E-value: 4.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 274 DLSLEIRAGEIVGLAGLVGSGRTefaeTLYGLRP----PRAGRIWLEN---REISQESTRARLasGLVylpedRQVSGLF 346
Cdd:cd03251 20 DISLDIPAGETVALVGPSGSGKS----TLVNLIPrfydVDSGRILIDGhdvRDYTLASLRRQI--GLV-----SQDVFLF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 347 LDApVRWNtVMFNQPSWWQQGKREAAVVERYHRALgIKLADG-DQPV----RTLSGGNQQKVLLARCLEANPLLLIVDEP 421
Cdd:cd03251 89 NDT-VAEN-IAYGRPGATREEVEEAARAANAHEFI-MELPEGyDTVIgergVKLSGGQRQRIAIARALLKDPPILILDEA 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2095916338 422 TRGVDVSARADIYQLLKSvAAQNVAVLMIS---SDVEEfvglADRVLVMHQGR 471
Cdd:cd03251 166 TSALDTESERLVQAALER-LMKNRTTFVIAhrlSTIEN----ADRIVVLEDGK 213
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
269-471 |
4.22e-10 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 61.04 E-value: 4.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 269 GEGFIDLSLEIRAGEIVGLAGLVGSGRTEFAETLYGLRPPRAGRIWLENREISQESTRARLAsglvylPEDRQVSGLFLD 348
Cdd:PRK11144 11 GDLCLTVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEKGICLP------PEKRRIGYVFQD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 349 A---P---VRWN---------TVMFNQpswwqqgkreaaVVEryhrALGIKLADGDQPvRTLSGGNQQKVLLARCLEANP 413
Cdd:PRK11144 85 ArlfPhykVRGNlrygmaksmVAQFDK------------IVA----LLGIEPLLDRYP-GSLSGGEKQRVAIGRALLTAP 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2095916338 414 LLLIVDEPTRGVDVSARADIYQLLKSVAAQ-NVAVLMISSDVEEFVGLADRVLVMHQGR 471
Cdd:PRK11144 148 ELLLMDEPLASLDLPRKRELLPYLERLAREiNIPILYVSHSLDEILRLADRVVVLEQGK 206
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
275-471 |
5.53e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 60.09 E-value: 5.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 275 LSLEIRAGEIVGLAGLVGSGRTEFAETLYGLRPPRAGRIWLENREISQEST---RARLASGLVYLPEDRQvsgLFldAPV 351
Cdd:PRK13639 21 INFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKsllEVRKTVGIVFQNPDDQ---LF--APT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 352 RWNTVMFNQpswWQQGKREAAVVERYHRALGIKLADG--DQPVRTLSGGNQQKVLLARCLEANPLLLIVDEPTRGVDVSA 429
Cdd:PRK13639 96 VEEDVAFGP---LNLGLSKEEVEKRVKEALKAVGMEGfeNKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMG 172
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2095916338 430 RADIYQLLKSVAAQNVAVLMISSDVEEFVGLADRVLVMHQGR 471
Cdd:PRK13639 173 ASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGK 214
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
19-215 |
6.77e-10 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 61.37 E-value: 6.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 19 VLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDSGELTIGERAFARLNPA-LAHQLGIylVPQEPMLFpNLSVR 97
Cdd:COG5265 373 ILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQAsLRAAIGI--VPQDTVLF-NDTIA 449
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 98 ENILF------------------------RLPKRADTtaRLQE---KLqqlncqinldasaSTLEvadQQMVEILRGLMR 150
Cdd:COG5265 450 YNIAYgrpdaseeeveaaaraaqihdfieSLPDGYDT--RVGErglKL-------------SGGE---KQRVAIARTLLK 511
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2095916338 151 EARILILDEPTASLTpGETERlfsQI-RALQALDVG---IVfISHKLPEIRQlASHVSVMRDGAVVLSG 215
Cdd:COG5265 512 NPPILIFDEATSALD-SRTER---AIqAALREVARGrttLV-IAHRLSTIVD-ADEILVLEAGRIVERG 574
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
20-211 |
7.10e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 59.75 E-value: 7.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 20 LKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDSGELTI-GERAFARLNPALAHQLGiyLVPQEP-MLFPNLSVR 97
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIdGDLLTEENVWDIRHKIG--MVFQNPdNQFVGATVE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 98 ENILFRLPKRA----DTTARLQEKLQQLNCQINLDASASTLEVADQQMVEILRGLMREARILILDEPTASLTPGETERLF 173
Cdd:PRK13650 101 DDVAFGLENKGipheEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELI 180
|
170 180 190
....*....|....*....|....*....|....*....
gi 2095916338 174 SQIRAL-QALDVGIVFISHKLPEIrQLASHVSVMRDGAV 211
Cdd:PRK13650 181 KTIKGIrDDYQMTVISITHDLDEV-ALSDRVLVMKNGQV 218
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
278-466 |
7.31e-10 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 59.34 E-value: 7.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 278 EIRAGEIVGLAGLVGSGRTEFAETLYGLRPPRAGRIWLENREISQESTrarlasglvYLPEDRQVSglfLDAPVRWNTVM 357
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSYKPQ---------YIKADYEGT---VRDLLSSITKD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 358 FNQPSWWQQGKREAAVVERYHralgikladgDQPVRTLSGGNQQKVLLARCLEANPLLLIVDEPTRGVDVSARADIYQLL 437
Cdd:cd03237 89 FYTHPYFKTEIAKPLQIEQIL----------DREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVI 158
|
170 180 190
....*....|....*....|....*....|
gi 2095916338 438 KSVAAQNVAVLM-ISSDVEEFVGLADRVLV 466
Cdd:cd03237 159 RRFAENNEKTAFvVEHDIIMIDYLADRLIV 188
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
19-211 |
8.29e-10 |
|
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: 61.50 E-value: 8.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 19 VLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDSGELTIGERAFARLNpalAHQL--GIYLVPQEPMLFPNlSV 96
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIG---LHDLrfKITIIPQDPVLFSG-SL 1376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 97 RENiLFRLPKRADTT-------ARLQEKLQQLNCQINLDAS--ASTLEVADQQMVEILRGLMREARILILDEPTASLTPg 167
Cdd:TIGR00957 1377 RMN-LDPFSQYSDEEvwwalelAHLKTFVSALPDKLDHECAegGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDL- 1454
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2095916338 168 ETERLF-SQIRAlQALDVGIVFISHKLPEIRQLaSHVSVMRDGAV 211
Cdd:TIGR00957 1455 ETDNLIqSTIRT-QFEDCTVLTIAHRLNTIMDY-TRVIVLDKGEV 1497
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
275-471 |
8.60e-10 |
|
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: 61.57 E-value: 8.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 275 LSLEIRAGEIVGLAGLVGSGRTEFAETLYGLRPPRAGRIWLENREISQESTRARLASGLVylpedRQVSGLFLDAPVRWN 354
Cdd:TIGR01257 949 LNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDAVRQSLGMC-----PQHNILFHHLTVAEH 1023
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 355 TVMFNQ---PSWWQQGKREAAVVER---YHRAlgikladgDQPVRTLSGGNQQKVLLARCLEANPLLLIVDEPTRGVDVS 428
Cdd:TIGR01257 1024 ILFYAQlkgRSWEEAQLEMEAMLEDtglHHKR--------NEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPY 1095
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2095916338 429 ARADIYQLLKSVAAQNvAVLMISSDVEEFVGLADRVLVMHQGR 471
Cdd:TIGR01257 1096 SRRSIWDLLLKYRSGR-TIIMSTHHMDEADLLGDRIAIISQGR 1137
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
12-215 |
9.37e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 59.86 E-value: 9.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 12 KQFSGVAVLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDSGELTIGEraFARLNPALAHQLGIYLVPQEPMLF 91
Cdd:PRK13631 34 KQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGD--IYIGDKKNNHELITNPYSKKIKNF 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 92 PNLSVRENILFRLP----------------------KRADTTARLQEKLQQLNCQIN-LDASASTLEVADQQMVEILRGL 148
Cdd:PRK13631 112 KELRRRVSMVFQFPeyqlfkdtiekdimfgpvalgvKKSEAKKLAKFYLNKMGLDDSyLERSPFGLSGGQKRRVAIAGIL 191
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2095916338 149 MREARILILDEPTASLTP-GETErLFSQIRALQALDVGIVFISHKLPEIRQLASHVSVMRDGAVVLSG 215
Cdd:PRK13631 192 AIQPEILIFDEPTAGLDPkGEHE-MMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTG 258
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
271-470 |
1.00e-09 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 60.43 E-value: 1.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 271 GFIDLSLEIRAGEIVGLAGLVGSGRTEFAETLYGLRPPRAGRIWLENREISQ-------ESTRARLAsgLVYlpedrQVS 343
Cdd:PRK10070 43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKisdaelrEVRRKKIA--MVF-----QSF 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 344 GLFLDAPVRWNTVMFNQPSWWQQGKREAAVVERYhRALGIKLADGDQPvRTLSGGNQQKVLLARCLEANPLLLIVDEPTR 423
Cdd:PRK10070 116 ALMPHMTVLDNTAFGMELAGINAEERREKALDAL-RQVGLENYAHSYP-DELSGGMRQRVGLARALAINPDILLMDEAFS 193
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2095916338 424 GVDVSARADIY-QLLKSVAAQNVAVLMISSDVEEFVGLADRVLVMHQG 470
Cdd:PRK10070 194 ALDPLIRTEMQdELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNG 241
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
83-198 |
1.06e-09 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 61.20 E-value: 1.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 83 LVPQEPMLFpNLSVRENILFRLP-------KRADTTARLQEKLQQLNCQ--INLDASASTLEVADQQMVEILRGLMREAR 153
Cdd:PTZ00265 1300 IVSQEPMLF-NMSIYENIKFGKEdatredvKRACKFAAIDEFIESLPNKydTNVGPYGKSLSGGQKQRIAIARALLREPK 1378
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 2095916338 154 ILILDEPTASLTpGETERLFSQ--IRALQALDVGIVFISHKLPEIRQ 198
Cdd:PTZ00265 1379 ILLLDEATSSLD-SNSEKLIEKtiVDIKDKADKTIITIAHRIASIKR 1424
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
276-471 |
1.15e-09 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 58.44 E-value: 1.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 276 SLEIRAGEIVGLAGLVGSGRTEFAETLYGLRPPRAGRIWLENreisQESTRARlasglvylPEDRQVSGLFLDapvrwNT 355
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNG----QDHTTTP--------PSRRPVSMLFQE-----NN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 356 vMFNQPSWWQQ-------GKREAAVVERYHRALGIKLADGDQPVR---TLSGGNQQKVLLARCL-EANPLLLIvDEPTRG 424
Cdd:PRK10771 82 -LFSHLTVAQNiglglnpGLKLNAAQREKLHAIARQMGIEDLLARlpgQLSGGQRQRVALARCLvREQPILLL-DEPFSA 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2095916338 425 VDVSARADIYQLLKSVAAQ-NVAVLMISSDVEEFVGLADRVLVMHQGR 471
Cdd:PRK10771 160 LDPALRQEMLTLVSQVCQErQLTLLMVSHSLEDAARIAPRSLVVADGR 207
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
3-229 |
1.26e-09 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 59.82 E-value: 1.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 3 PLLEARQIRKQF----SGVAVLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVeTPDSGELTIGERAF-----ARLNP 73
Cdd:PRK15093 2 PLLDIRNLTIEFktsdGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGV-TKDNWRVTADRMRFddidlLRLSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 74 ALAHQL---GIYLVPQEPM--LFPNLSVRENILFRLP---------------KRadttaRLQEKLQQLNCQINLDASAS- 132
Cdd:PRK15093 81 RERRKLvghNVSMIFQEPQscLDPSERVGRQLMQNIPgwtykgrwwqrfgwrKR-----RAIELLHRVGIKDHKDAMRSf 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 133 --TLEVADQQMVEILRGLMREARILILDEPTASLTPGETERLFSQIRAL-QALDVGIVFISHKLPEIRQLASHVSVMRDG 209
Cdd:PRK15093 156 pyELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLnQNNNTTILLISHDLQMLSQWADKINVLYCG 235
|
250 260 270
....*....|....*....|....*....|
gi 2095916338 210 AVVlsgETAGYGD----------QQLISAM 229
Cdd:PRK15093 236 QTV---ETAPSKElvttphhpytQALIRAI 262
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
17-197 |
1.32e-09 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 60.81 E-value: 1.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 17 VAVLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDSGELTIGErafarlnpalAHQL----------GIYLVPQ 86
Cdd:PTZ00265 398 VEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIIND----------SHNLkdinlkwwrsKIGVVSQ 467
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 87 EPMLFPNlSVRENILFRLPKRADTTArLQEKLQQ----------------------LNCQIN------------------ 126
Cdd:PTZ00265 468 DPLLFSN-SIKNNIKYSLYSLKDLEA-LSNYYNEdgndsqenknkrnscrakcagdLNDMSNttdsneliemrknyqtik 545
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 127 ---------------------------LDASASTLEVADQQMVEILRGLMREARILILDEPTASLTpGETERLFSQ-IRA 178
Cdd:PTZ00265 546 dsevvdvskkvlihdfvsalpdkyetlVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLD-NKSEYLVQKtINN 624
|
250 260
....*....|....*....|
gi 2095916338 179 LQALDVGI-VFISHKLPEIR 197
Cdd:PTZ00265 625 LKGNENRItIIIAHRLSTIR 644
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
12-214 |
1.33e-09 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 60.66 E-value: 1.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 12 KQFSGVAVLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDS--GELTIGERAFARlnPALAHqlgIYLVPQEPM 89
Cdd:PLN03211 76 RQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRKPTK--QILKR---TGFVTQDDI 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 90 LFPNLSVRENILF----RLPKradtTARLQEKL---QQLNCQINLDASAST---------LEVADQQMVEILRGLMREAR 153
Cdd:PLN03211 151 LYPHLTVRETLVFcsllRLPK----SLTKQEKIlvaESVISELGLTKCENTiignsfirgISGGERKRVSIAHEMLINPS 226
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2095916338 154 ILILDEPTASLTPGETERLFSQIRALQALDVGIVFISHklpeirQLASHVSVMRDGAVVLS 214
Cdd:PLN03211 227 LLILDEPTSGLDATAAYRLVLTLGSLAQKGKTIVTSMH------QPSSRVYQMFDSVLVLS 281
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
20-164 |
1.61e-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: 57.25 E-value: 1.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 20 LKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPD--SGELTIGERafaRLNPALAHQLGiYlVPQEPMLFPNLSVR 97
Cdd:cd03232 23 LNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAGviTGEILINGR---PLDKNFQRSTG-Y-VEQQDVHSPNLTVR 97
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2095916338 98 ENILFrlpkradtTARLQEklqqlncqinldasastLEVADQQMVEILRGLMREARILILDEPTASL 164
Cdd:cd03232 98 EALRF--------SALLRG-----------------LSVEQRKRLTIGVELAAKPSILFLDEPTSGL 139
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
395-471 |
1.65e-09 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 59.37 E-value: 1.65e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2095916338 395 LSGGNQQKVLLARCLEANPLLLIVDEPTRGVDVSARADIYQLLKSVAAQ-NVAVLMISSDVEEFVGLADRVLVMHQGR 471
Cdd:PRK11022 154 LSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKeNMALVLITHDLALVAEAAHKIIVMYAGQ 231
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
274-476 |
1.88e-09 |
|
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: 56.95 E-value: 1.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 274 DLSLEIRAGEIVGLAGLVGSGRTEFA-ETLYglrppragriwlenreisqESTRARLASglvylpedrqvsglFLDAPVR 352
Cdd:cd03238 13 NLDVSIPLNVLVVVTGVSGSGKSTLVnEGLY-------------------ASGKARLIS--------------FLPKFSR 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 353 WNTVMFNQPSwwqqgkreaAVVEryhraLGIKLADGDQPVRTLSGGNQQKVLLARCLEANP--LLLIVDEPTRGVDVSar 430
Cdd:cd03238 60 NKLIFIDQLQ---------FLID-----VGLGYLTLGQKLSTLSGGELQRVKLASELFSEPpgTLFILDEPSTGLHQQ-- 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2095916338 431 aDIYQLL---KSVAAQNVAVLMISSDvEEFVGLADRVLVM--HQGRHSGEL 476
Cdd:cd03238 124 -DINQLLeviKGLIDLGNTVILIEHN-LDVLSSADWIIDFgpGSGKSGGKV 172
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-235 |
1.97e-09 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 58.25 E-value: 1.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 1 MKPLLEARQIRKQFSGVAVLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGV-----ETPDSGELTI-GERAFARLNPA 74
Cdd:PRK14239 2 TEPILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndlnpEVTITGSIVYnGHNIYSPRTDT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 75 LAHQLGIYLVPQEPMLFPnLSVRENILFRL-----PKRADTTARLQEKLQQLN----CQINLDASASTLEVADQQMVEIL 145
Cdd:PRK14239 82 VDLRKEIGMVFQQPNPFP-MSIYENVVYGLrlkgiKDKQVLDEAVEKSLKGASiwdeVKDRLHDSALGLSGGQQQRVCIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 146 RGLMREARILILDEPTASLTPGETERLFSQIRALQAlDVGIVFISHKLpeirQLASHVSvmRDGAVVLSGETAGYGDQQL 225
Cdd:PRK14239 161 RVLATSPKIILLDEPTSALDPISAGKIEETLLGLKD-DYTMLLVTRSM----QQASRIS--DRTGFFLDGDLIEYNDTKQ 233
|
250
....*....|
gi 2095916338 226 IsAMTPASRD 235
Cdd:PRK14239 234 M-FMNPKHKE 242
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
274-471 |
2.09e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 58.56 E-value: 2.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 274 DLSLEIRAGEIVGLAGLVGSGRTEFAETLYGLRPPRAGRI-WLENREISQESTRAR---LASGLVYLPEDRQVSglFLDA 349
Cdd:PRK13651 25 NVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIeWIFKDEKNKKKTKEKekvLEKLVIQKTRFKKIK--KIKE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 350 PVRWNTVMFnQPSWWQQ-----------GKREAAVV--ERYHRALG-IKLADGDQ------PVrTLSGGNQQKVLLARCL 409
Cdd:PRK13651 103 IRRRVGVVF-QFAEYQLfeqtiekdiifGPVSMGVSkeEAKKRAAKyIELVGLDEsylqrsPF-ELSGGQKRRVALAGIL 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2095916338 410 EANPLLLIVDEPTRGVDVSARADIYQLLKSVAAQNVAVLMISSDVEEFVGLADRVLVMHQGR 471
Cdd:PRK13651 181 AMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTKRTIFFKDGK 242
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
17-217 |
2.09e-09 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 58.76 E-value: 2.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 17 VAVLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVeTPDSGELT-----IGERAFARLNPALAHQL---GIYLVPQEP 88
Cdd:COG4170 20 VKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGI-TKDNWHVTadrfrWNGIDLLKLSPRERRKIigrEIAMIFQEP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 89 M--LFPNLSVRENILFRLPKRADTT---ARLQEKLQQL----------NCQINLDASASTLEVADQQMVEILRGLMREAR 153
Cdd:COG4170 99 SscLDPSAKIGDQLIEAIPSWTFKGkwwQRFKWRKKRAiellhrvgikDHKDIMNSYPHELTEGECQKVMIAMAIANQPR 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2095916338 154 ILILDEPTASL---TPGETERLFSQIRALQalDVGIVFISHKLPEIRQLASHVSVMRDGAVVLSGET 217
Cdd:COG4170 179 LLIADEPTNAMestTQAQIFRLLARLNQLQ--GTSILLISHDLESISQWADTITVLYCGQTVESGPT 243
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
3-200 |
2.17e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 58.12 E-value: 2.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 3 PLLEARQIRKQFSGVAVLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDSGELTIGERAF-------ARLN-PA 74
Cdd:PRK14258 6 PAIKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESEVRVEGRVEFfnqniyeRRVNlNR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 75 LAHQlgIYLVPQEPMLFPnLSVRENILFRL------PK--------RADTTARLQEKLQQlncqiNLDASASTLEVADQQ 140
Cdd:PRK14258 86 LRRQ--VSMVHPKPNLFP-MSVYDNVAYGVkivgwrPKleiddiveSALKDADLWDEIKH-----KIHKSALDLSGGQQQ 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2095916338 141 MVEILRGLMREARILILDEPTASLTPGETERLFSQIRALQAL-DVGIVFISHKLPEIRQLA 200
Cdd:PRK14258 158 RLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRsELTMVIVSHNLHQVSRLS 218
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
23-215 |
2.80e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 58.21 E-value: 2.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 23 IDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDSGELTIGERAFARLNPA-----LAHQLGIYLVPQEPMLFPNlSVR 97
Cdd:PRK13643 25 IDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQkeikpVRKKVGVVFQFPESQLFEE-TVL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 98 ENILFRlPKRADTTARLQEKLQQLNCQ-INLDAS---ASTLEVADQQM--VEILRGLMREARILILDEPTASLTPGETER 171
Cdd:PRK13643 104 KDVAFG-PQNFGIPKEKAEKIAAEKLEmVGLADEfweKSPFELSGGQMrrVAIAGILAMEPEVLVLDEPTAGLDPKARIE 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2095916338 172 LFSQIRALQALDVGIVFISHKLPEIRQLASHVSVMRDGAVVLSG 215
Cdd:PRK13643 183 MMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCG 226
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
396-471 |
2.96e-09 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 58.44 E-value: 2.96e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2095916338 396 SGGNQQKVLLARCLEANPLLLIVDEPTRGVDVSARADIYQLLKSVAAQ-NVAVLMISSD--VEEFVglADRVLVMHQGR 471
Cdd:PRK11308 156 SGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQElGLSYVFISHDlsVVEHI--ADEVMVMYLGR 232
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
389-471 |
7.85e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 56.64 E-value: 7.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 389 DQPVRtLSGGNQQKVLLARCLEANPLLLIVDEPTRGVDVSARADIYQLLKSVaAQNVAVLMISSDVEEFVGLADRVLVMH 468
Cdd:PRK14271 159 DSPFR-LSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSL-ADRLTVIIVTHNLAQAARISDRAALFF 236
|
...
gi 2095916338 469 QGR 471
Cdd:PRK14271 237 DGR 239
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
274-471 |
7.91e-09 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 57.91 E-value: 7.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 274 DLSLEIRAGEIVGLAGLVGSGRTefaeTLYGL----RPPRAGRIWLENREISQ--EST-RARLA--SGLVYLpedrqvsg 344
Cdd:PRK11160 358 GLSLQIKAGEKVALLGRTGCGKS----TLLQLltraWDPQQGEILLNGQPIADysEAAlRQAISvvSQRVHL-------- 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 345 lfLDAPVRWNTVMFNqpswwqqgkrEAAVVERYHRAL---GI-KLADGDQPV--------RTLSGGNQQKVLLARCLEAN 412
Cdd:PRK11160 426 --FSATLRDNLLLAA----------PNASDEALIEVLqqvGLeKLLEDDKGLnawlgeggRQLSGGEQRRLGIARALLHD 493
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2095916338 413 PLLLIVDEPTRGVDVSARADIYQLLKSVaAQNVAVLMISsdvEEFVGLA--DRVLVMHQGR 471
Cdd:PRK11160 494 APLLLLDEPTEGLDAETERQILELLAEH-AQNKTVLMIT---HRLTGLEqfDRICVMDNGQ 550
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
275-471 |
8.06e-09 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 56.72 E-value: 8.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 275 LSLEIRAGEIVGLAGLVGSGRTEFAETLYGLRPPRAGRIWLENREISQESTRArLASGLVYLPED-RQVSGLfldapvrw 353
Cdd:PRK10575 30 LSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKA-FARKVAYLPQQlPAAEGM-------- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 354 nTVmfnqpswwqqgkREAAVVERY--HRALG-------------IKLAdGDQP-----VRTLSGGNQQKVLLARCLEANP 413
Cdd:PRK10575 101 -TV------------RELVAIGRYpwHGALGrfgaadrekveeaISLV-GLKPlahrlVDSLSGGERQRAWIAMLVAQDS 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2095916338 414 LLLIVDEPTRGVDVSARADIYQLLKSVAAQN-VAVLMISSDVEEFVGLADRVLVMHQGR 471
Cdd:PRK10575 167 RCLLLDEPTSALDIAHQVDVLALVHRLSQERgLTVIAVLHDINMAARYCDYLVALRGGE 225
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
19-164 |
1.00e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 58.06 E-value: 1.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 19 VLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDSGELTIGERAFARLN-PALAHQLGIylVPQEPMLFPNlSVR 97
Cdd:PLN03232 1251 VLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGlTDLRRVLSI--IPQSPVLFSG-TVR 1327
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2095916338 98 ENILfrlPKRADTTARLQEKLQQL-------NCQINLDASAS----TLEVADQQMVEILRGLMREARILILDEPTASL 164
Cdd:PLN03232 1328 FNID---PFSEHNDADLWEALERAhikdvidRNPFGLDAEVSeggeNFSVGQRQLLSLARALLRRSKILVLDEATASV 1402
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
274-471 |
1.10e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 56.35 E-value: 1.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 274 DLSLEIRAGEIVGLAGLVGSGRTEFAETLYGLRPPRA---GRIWLENREISQEST-RARLASGLVYLPEDRQvsglFLDA 349
Cdd:PRK13640 25 DISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDnpnSKITVDGITLTAKTVwDIREKVGIVFQNPDNQ----FVGA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 350 PVRwNTVMFNQPSwwQQGKREAaVVERYHRALG-IKLAD-GDQPVRTLSGGNQQKVLLARCLEANPLLLIVDEPTRGVDV 427
Cdd:PRK13640 101 TVG-DDVAFGLEN--RAVPRPE-MIKIVRDVLAdVGMLDyIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDP 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2095916338 428 SARADIYQLLKSVAAQN-VAVLMISSDVEEFVGlADRVLVMHQGR 471
Cdd:PRK13640 177 AGKEQILKLIRKLKKKNnLTVISITHDIDEANM-ADQVLVLDDGK 220
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
260-449 |
1.11e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 55.27 E-value: 1.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 260 PVLRVEDLTG-----EGFIDLSLEIRAGEIVGLAGLVGSGRTEFAETLYGLRPPRAGRIWLENREISQESTRARLAsglv 334
Cdd:PRK13539 1 MMLEGEDLACvrggrVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACH---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 335 YLPEdrqvsglfLDAPVRWNTVMFNQpSWWQQ--GKREAAVveryHRAL-GIKLAD-GDQPVRTLSGGNQQKVLLARCLE 410
Cdd:PRK13539 77 YLGH--------RNAMKPALTVAENL-EFWAAflGGEELDI----AAALeAVGLAPlAHLPFGYLSAGQKRRVALARLLV 143
|
170 180 190
....*....|....*....|....*....|....*....
gi 2095916338 411 ANPLLLIVDEPTRGVDVSARADIYQLLKSVAAQNVAVLM 449
Cdd:PRK13539 144 SNRPIWILDEPTAALDAAAVALFAELIRAHLAQGGIVIA 182
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
274-471 |
1.36e-08 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 55.41 E-value: 1.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 274 DLSLEIRAGEIVGLAGLVGSGRTEFAETLYGLRPPRAGRIWLENREISQESTrarlasglvylPEDRQVSGLfldapvRW 353
Cdd:PRK11124 20 DITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFDFSKT-----------PSDKAIREL------RR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 354 NTVM-FNQPSWW-----QQGKREAAV-------VERYHRALGI----KLAD-GDQPVRTLSGGNQQKVLLARCLEANPLL 415
Cdd:PRK11124 83 NVGMvFQQYNLWphltvQQNLIEAPCrvlglskDQALARAEKLlerlRLKPyADRFPLHLSGGQQQRVAIARALMMEPQV 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2095916338 416 LIVDEPTRGVDVSARADIYQLLKSVAAQNVAVLMISSDVEEFVGLADRVLVMHQGR 471
Cdd:PRK11124 163 LLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTHEVEVARKTASRVVYMENGH 218
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
5-216 |
1.38e-08 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 56.67 E-value: 1.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 5 LEARQIRKQFSGVAVLKGIDFTLCAGQVHALMGGNGAGKSTlMKIIAGVETPDSGELTIGERAFARLNPALAHQLGIYLv 84
Cdd:NF000106 14 VEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**R-GALPAHV*GPDAGRRPWRF*TWCANRRALRRTIG*HR- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 85 PQEPMLFPNLSVRENiLFRLPK-----RADTTARLQEKLQQLNCQINLDASASTLEVADQQMVEILRGLMREARILILDE 159
Cdd:NF000106 92 PVR*GRRESFSGREN-LYMIGR*ldlsRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDE 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2095916338 160 PTASLTPGETERLFSQIRALQALDVGIVFISHKLPEIRQLASHVSVMRDGAVVLSGE 216
Cdd:NF000106 171 PTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGK 227
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
274-471 |
1.74e-08 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 56.24 E-value: 1.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 274 DLSLEIRAGEIVGLAGLVGSGRTEFAETLYGLRPPRAGRIWLENREISQESTR----ARLASGLVYlpedrQVSGLFLDA 349
Cdd:COG1135 23 DVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERelraARRKIGMIF-----QHFNLLSSR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 350 PVRWNtVMFnqP---SWWQQGKREAAVVEryhraL----GikLAD-GDQPVRTLSGGNQQKVLLARCLEANPLLLIVDEP 421
Cdd:COG1135 98 TVAEN-VAL--PleiAGVPKAEIRKRVAE-----LlelvG--LSDkADAYPSQLSGGQKQRVGIARALANNPKVLLCDEA 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2095916338 422 TRGVDVSARADIYQLLKSVAAQ-NVAVLMISSD---VEEfvgLADRVLVMHQGR 471
Cdd:COG1135 168 TSALDPETTRSILDLLKDINRElGLTIVLITHEmdvVRR---ICDRVAVLENGR 218
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
19-163 |
1.96e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 57.06 E-value: 1.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 19 VLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDSGELTIGERAFARLNPA-LAHQLGIylVPQEPMLFPNlSVR 97
Cdd:PLN03130 1254 VLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMdLRKVLGI--IPQAPVLFSG-TVR 1330
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2095916338 98 ENILfrlPKRADTTARLQEKLQQLNCQ-------INLDASAS----TLEVADQQMVEILRGLMREARILILDEPTAS 163
Cdd:PLN03130 1331 FNLD---PFNEHNDADLWESLERAHLKdvirrnsLGLDAEVSeageNFSVGQRQLLSLARALLRRSKILVLDEATAA 1404
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
3-166 |
2.09e-08 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 54.47 E-value: 2.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 3 PLLEARQIRKQFSGVAVLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDSGELTI-------GERafARLNPAL 75
Cdd:PRK13543 10 PLLAAHALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIdgktatrGDR--SRFMAYL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 76 AHQlgiylvpqePMLFPNLSVRENILF------RLPKRADTTArlqekLQQLNCQINLDASASTLEVADQQMVEILRGLM 149
Cdd:PRK13543 88 GHL---------PGLKADLSTLENLHFlcglhgRRAKQMPGSA-----LAIVGLAGYEDTLVRQLSAGQKKRLALARLWL 153
|
170
....*....|....*..
gi 2095916338 150 REARILILDEPTASLTP 166
Cdd:PRK13543 154 SPAPLWLLDEPYANLDL 170
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
19-194 |
2.13e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 54.11 E-value: 2.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 19 VLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDSGELTIGERAFARLNPA----LAHQLGIYLvpqepmlfpNL 94
Cdd:PRK13541 15 NLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKPyctyIGHNLGLKL---------EM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 95 SVRENILFrLPKRADTTARLQEKLQQLNCQINLDASASTLEVADQQMVEILRGLMREARILILDEPTASLTPgETERLFS 174
Cdd:PRK13541 86 TVFENLKF-WSEIYNSAETLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSK-ENRDLLN 163
|
170 180
....*....|....*....|
gi 2095916338 175 QIRALQALDVGIVFISHKLP 194
Cdd:PRK13541 164 NLIVMKANSGGIVLLSSHLE 183
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
30-221 |
2.51e-08 |
|
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: 55.07 E-value: 2.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 30 GQVHALMGGNGAGKSTLMKIIAGVETPDSG------------------ELtigERAFARLnpaLAHQLGIYLVPQEPMLF 91
Cdd:cd03236 26 GQVLGLVGPNGIGKSTALKILAGKLKPNLGkfddppdwdeildefrgsEL---QNYFTKL---LEGDVKVIVKPQYVDLI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 92 PNlSVRENILfRLPKRADTTARLQEKLQQLNCQINLDASASTLEVADQQMVEILRGLMREARILILDEPTASLTPGETER 171
Cdd:cd03236 100 PK-AVKGKVG-ELLKKKDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRLN 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2095916338 172 LFSQIRALQALDVGIVFISHKLPEIRQLASHVSvmrdgavVLSGETAGYG 221
Cdd:cd03236 178 AARLIRELAEDDNYVLVVEHDLAVLDYLSDYIH-------CLYGEPGAYG 220
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
20-229 |
2.90e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 55.01 E-value: 2.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 20 LKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDSGELTIGERAFarlnPA----------LAHQLGIYLVPQEPM 89
Cdd:PRK13645 27 LNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAI----PAnlkkikevkrLRKEIGLVFQFPEYQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 90 LFPNlSVRENILFRLPKRADTTARLQEKLQQLNCQINLD---ASASTLEVADQQMVEI-LRGLM-REARILILDEPTASL 164
Cdd:PRK13645 103 LFQE-TIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLPedyVKRSPFELSGGQKRRVaLAGIIaMDGNTLVLDEPTGGL 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2095916338 165 TP-GETERLFSQIRALQALDVGIVFISHKLPEIRQLASHVSVMRDGAVVLSGETAG-YGDQQLISAM 229
Cdd:PRK13645 182 DPkGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEiFSNQELLTKI 248
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
274-471 |
3.11e-08 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 54.63 E-value: 3.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 274 DLSLEIRAGEIVGLAGLVGSGRTEFAETLYGLRPPRAGRIWLEN------REISQESTRA-RLASGLVY----LPEDRQV 342
Cdd:COG4161 20 DINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGhqfdfsQKPSEKAIRLlRQKVGMVFqqynLWPHLTV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 343 SGLFLDAPVRwntVMfnqpswwQQGKREAavVERYHRALG-IKLADGDQ--PVRtLSGGNQQKVLLARCLEANPLLLIVD 419
Cdd:COG4161 100 MENLIEAPCK---VL-------GLSKEQA--REKAMKLLArLRLTDKADrfPLH-LSGGQQQRVAIARALMMEPQVLLFD 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2095916338 420 EPTRGVDVSARADIYQLLKSVAAQNVAVLMISSDVEEFVGLADRVLVMHQGR 471
Cdd:COG4161 167 EPTAALDPEITAQVVEIIRELSQTGITQVIVTHEVEFARKVASQVVYMEKGR 218
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
273-471 |
3.60e-08 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 55.82 E-value: 3.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 273 IDLSLEIRAGEIVGLAGLVGSGRTEFAETLYGLRPP---RAGRIWLENREISQESTRARLAsglvYLPEDRqvsgLFLDA 349
Cdd:TIGR00955 42 KNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKgvkGSGSVLLNGMPIDAKEMRAISA----YVQQDD----LFIPT 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 350 PVRWNTVMFN-----QPSWWQQGKREAavVERYHRALGI-KLAD---GDQ-PVRTLSGGNQQKVLLARCLEANPLLLIVD 419
Cdd:TIGR00955 114 LTVREHLMFQahlrmPRRVTKKEKRER--VDEVLQALGLrKCANtriGVPgRVKGLSGGERKRLAFASELLTDPPLLFCD 191
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2095916338 420 EPTRGVDVSARADIYQLLKSVAAQNVAVLMI----SSDVEEfvgLADRVLVMHQGR 471
Cdd:TIGR00955 192 EPTSGLDSFMAYSVVQVLKGLAQKGKTIICTihqpSSELFE---LFDKIILMAEGR 244
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
262-465 |
4.10e-08 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 55.67 E-value: 4.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 262 LRVEDLT-----GEGFIDLSLEIRAGEIVGLAGLVGSGRTEFAETLYGLRPPRAGRI-WLENREISqestrarlasglvY 335
Cdd:PRK15064 320 LEVENLTkgfdnGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVkWSENANIG-------------Y 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 336 LPEDrqVSGLFLDapvrwNTVMFNQPSWWQQGKREAAVVeryhRA-LGIKLADGD---QPVRTLSGGNQQKVLLARCLEA 411
Cdd:PRK15064 387 YAQD--HAYDFEN-----DLTLFDWMSQWRQEGDDEQAV----RGtLGRLLFSQDdikKSVKVLSGGEKGRMLFGKLMMQ 455
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2095916338 412 NPLLLIVDEPTRGVDvsaradiyqlLKSVAAQNVA-------VLMISSDvEEFV-GLADRVL 465
Cdd:PRK15064 456 KPNVLVMDEPTNHMD----------MESIESLNMAlekyegtLIFVSHD-REFVsSLATRII 506
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1-212 |
4.37e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 54.33 E-value: 4.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 1 MKPLLEARQIRKQF---SGVAVLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDSGELTI-GERAFARLNPALA 76
Cdd:PRK13642 1 MNKILEVENLVFKYekeSDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIdGELLTAENVWNLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 77 HQLGiyLVPQEP-MLFPNLSVRENILFRLPK----RADTTARLQEKLQQLNCQINLDASASTLEVADQQMVEILRGLMRE 151
Cdd:PRK13642 81 RKIG--MVFQNPdNQFVGATVEDDVAFGMENqgipREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2095916338 152 ARILILDEPTASLTP---GETERLFSQIRALQALDVgiVFISHKLPEIRQlASHVSVMRDGAVV 212
Cdd:PRK13642 159 PEIIILDESTSMLDPtgrQEIMRVIHEIKEKYQLTV--LSITHDLDEAAS-SDRILVMKAGEII 219
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
276-471 |
4.65e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 54.63 E-value: 4.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 276 SLEIRAGEIVGLAGLVGSGRTEFAETLYGLRPPRAGRIWLENREIS------QESTRARLASGLVYLPEDRQVSGLFLDA 349
Cdd:PRK13645 31 SLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPanlkkiKEVKRLRKEIGLVFQFPEYQLFQETIEK 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 350 PVRWNTVMFnqpswwqqGKREAAVVERYHRALGIKLADGDQPVRT---LSGGNQQKVLLARCLEANPLLLIVDEPTRGVD 426
Cdd:PRK13645 111 DIAFGPVNL--------GENKQEAYKKVPELLKLVQLPEDYVKRSpfeLSGGQKRRVALAGIIAMDGNTLVLDEPTGGLD 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2095916338 427 VSARADIYQLLKSV-AAQNVAVLMISSDVEEFVGLADRVLVMHQGR 471
Cdd:PRK13645 183 PKGEEDFINLFERLnKEYKKRIIMVTHNMDQVLRIADEVIVMHEGK 228
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
20-215 |
5.99e-08 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 55.02 E-value: 5.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 20 LKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDSGELT-----IGERAFARLNPALAhqlgiyLVPQEPMLFpNL 94
Cdd:PRK11176 359 LRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILldghdLRDYTLASLRNQVA------LVSQNVHLF-ND 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 95 SVRENILFrlpKRADTTARLQ--------------EKLQQ-LNCQINldASASTLEVADQQMVEILRGLMREARILILDE 159
Cdd:PRK11176 432 TIANNIAY---ARTEQYSREQieeaarmayamdfiNKMDNgLDTVIG--ENGVLLSGGQRQRIAIARALLRDSPILILDE 506
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2095916338 160 PTASLTPgETER-LFSQIRALQAlDVGIVFISHKLPEIRQlASHVSVMRDGAVVLSG 215
Cdd:PRK11176 507 ATSALDT-ESERaIQAALDELQK-NRTSLVIAHRLSTIEK-ADEILVVEDGEIVERG 560
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
266-471 |
6.11e-08 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 54.97 E-value: 6.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 266 DLTGEGFIDLSLEIRAGEIVGLAGLVGSGRTEFAETLYGLRPPRAGRIWLEN---REISQESTRARLasGLVYlpedrQV 342
Cdd:PRK13657 345 DNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGtdiRTVTRASLRRNI--AVVF-----QD 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 343 SGLFlDAPVRWNTvmfnqpswwqQGKREAAVVERYHRALGIKLA--------DGDQPV-----RTLSGGNQQKVLLARCL 409
Cdd:PRK13657 418 AGLF-NRSIEDNI----------RVGRPDATDEEMRAAAERAQAhdfierkpDGYDTVvgergRQLSGGERQRLAIARAL 486
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2095916338 410 EANPLLLIVDEPTRGVDVSARADIYQLLKSVaAQNVAVLMIS---SDVEEfvglADRVLVMHQGR 471
Cdd:PRK13657 487 LKDPPILILDEATSALDVETEAKVKAALDEL-MKGRTTFIIAhrlSTVRN----ADRILVFDNGR 546
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
274-471 |
6.85e-08 |
|
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: 52.32 E-value: 6.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 274 DLSLEIRAGEIVGLAGLVGSGRTEFAETLYGLRPPRAGRIWLENREISqeSTRARLASGLVYLPedrQVSGLFlDAPVRW 353
Cdd:cd03247 20 NLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVS--DLEKALSSLISVLN---QRPYLF-DTTLRN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 354 NtvmfnqpswwqqgkreaavveryhraLGikladgdqpvRTLSGGNQQKVLLARCLEANPLLLIVDEPTRGVDVSARADI 433
Cdd:cd03247 94 N--------------------------LG----------RRFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQL 137
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2095916338 434 YQLLKSVaAQNVAVLMIS---SDVEEFvglaDRVLVMHQGR 471
Cdd:cd03247 138 LSLIFEV-LKDKTLIWIThhlTGIEHM----DKILFLENGK 173
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
274-489 |
8.88e-08 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 53.17 E-value: 8.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 274 DLSLEIRAGEIVGLAGLVGSGRTEFAETLYGLRPPRAGRIWLENREISQEST--RARLasglvylpedrqVSGLFLD--- 348
Cdd:COG1101 24 GLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEykRAKY------------IGRVFQDpmm 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 349 --AP---VRWNTVM------FNQPSWWQQGKREAAVVERYhRALGIKLADG-DQPVRTLSGGNQQKVLLARCLEANPLLL 416
Cdd:COG1101 92 gtAPsmtIEENLALayrrgkRRGLRRGLTKKRRELFRELL-ATLGLGLENRlDTKVGLLSGGQRQALSLLMATLTKPKLL 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2095916338 417 IVDEPTRGVDVSARADIYQLLKS-VAAQNVAVLMISSDVEEFVGLADRVLVMHQGR----HSGElARQAVTVDRMMTL 489
Cdd:COG1101 171 LLDEHTAALDPKTAALVLELTEKiVEENNLTTLMVTHNMEQALDYGNRLIMMHEGRiildVSGE-EKKKLTVEDLLEL 247
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
19-212 |
9.96e-08 |
|
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: 52.99 E-value: 9.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 19 VLKGIDFTLCAGQVHALMGGNGAGKSTL-MKIIAGVETPDsGELTIGERAFARLN-PALAHQLGIYLvpQEPMLFPNlSV 96
Cdd:cd03288 36 VLKHVKAYIKPGQKVGICGRTGSGKSSLsLAFFRMVDIFD-GKIVIDGIDISKLPlHTLRSRLSIIL--QDPILFSG-SI 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 97 RENILfrlPKRADTTARLQEKLQ--QLNCQIN-----LDA----SASTLEVADQQMVEILRGLMREARILILDEPTASLT 165
Cdd:cd03288 112 RFNLD---PECKCTDDRLWEALEiaQLKNMVKslpggLDAvvteGGENFSVGQRQLFCLARAFVRKSSILIMDEATASID 188
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2095916338 166 PGeTERLFSQIRALQALDVGIVFISHKLPEIRQlASHVSVMRDGAVV 212
Cdd:cd03288 189 MA-TENILQKVVMTAFADRTVVTIAHRVSTILD-ADLVLVLSRGILV 233
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
292-475 |
1.19e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 53.27 E-value: 1.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 292 GSGRTEFAETLYGLRPPRAGRIWLENREISQESTR-ARLASGLVYLPEDRQVSGLFLDAPVRWNTVmfnqpswwQQGKRE 370
Cdd:PRK13652 40 GAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIReVRKFVGLVFQNPDDQIFSPTVEQDIAFGPI--------NLGLDE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 371 AAVVERYHRAL---GIKLADGDQPvRTLSGGNQQKVLLARCLEANPLLLIVDEPTRGVDVSARADIYQLLKSVAAQ-NVA 446
Cdd:PRK13652 112 ETVAHRVSSALhmlGLEELRDRVP-HHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETyGMT 190
|
170 180
....*....|....*....|....*....
gi 2095916338 447 VLMISSDVEEFVGLADRVLVMHQGRHSGE 475
Cdd:PRK13652 191 VIFSTHQLDLVPEMADYIYVMDKGRIVAY 219
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
15-217 |
1.42e-07 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 52.96 E-value: 1.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 15 SGVAVLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDSGELTIGERAfarLNPALAHQLGIYlVPQEPML---F 91
Cdd:PRK15056 18 NGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQP---TRQALQKNLVAY-VPQSEEVdwsF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 92 PNLsVRENIL---------FRLPKRADtTARLQEKLQQLNCQINLDASASTLEVADQQMVEILRGLMREARILILDEPTA 162
Cdd:PRK15056 94 PVL-VEDVVMmgryghmgwLRRAKKRD-RQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFT 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2095916338 163 SLTPGETERLFSQIRALQALDVGIVFISHKLPEIRQLASHvSVMRDGAVVLSGET 217
Cdd:PRK15056 172 GVDVKTEARIISLLRELRDEGKTMLVSTHNLGSVTEFCDY-TVMVKGTVLASGPT 225
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
5-215 |
1.52e-07 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 52.68 E-value: 1.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 5 LEARQIRKQFSGVAVLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDSGELTI-GERAFARLNPALAHQLGiyL 83
Cdd:PRK10253 8 LRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLdGEHIQHYASKEVARRIG--L 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 84 VPQEPMLFPNLSVRENI---------LFRLPKRADTTArLQEKLQQLNCQINLDASASTLEVADQQMVEILRGLMREARI 154
Cdd:PRK10253 86 LAQNATTPGDITVQELVargryphqpLFTRWRKEDEEA-VTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAI 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2095916338 155 LILDEPTASLTPG---ETERLFSQIRALQALDVGIVFisHKLPEIRQLASHVSVMRDGAVVLSG 215
Cdd:PRK10253 165 MLLDEPTTWLDIShqiDLLELLSELNREKGYTLAAVL--HDLNQACRYASHLIALREGKIVAQG 226
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
15-210 |
1.53e-07 |
|
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: 51.95 E-value: 1.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 15 SGVAVLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDSGELTIGERAFARLNPALAHQLGIYLVP---QEPMLF 91
Cdd:cd03290 12 SGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRNRYSVAyaaQKPWLL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 92 pNLSVRENILFRLP------KRADTTARLQEKLQQL--NCQINLDASASTLEVADQQMVEILRGLMREARILILDEPTAS 163
Cdd:cd03290 92 -NATVEENITFGSPfnkqryKAVTDACSLQPDIDLLpfGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSA 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2095916338 164 LTPGETERLFSQ--IRALQALDVGIVFISHKLPEIRQlASHVSVMRDGA 210
Cdd:cd03290 171 LDIHLSDHLMQEgiLKFLQDDKRTLVLVTHKLQYLPH-ADWIIAMKDGS 218
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
274-449 |
1.60e-07 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 52.58 E-value: 1.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 274 DLSLEIRAGEIVGLAGLVGSGRTEFAETLYGLRPPRAGRIwlenrEISQESTRARLASGLV-YLPEDRQVSGLFldaPVR 352
Cdd:PRK15056 25 DASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKI-----SILGQPTRQALQKNLVaYVPQSEEVDWSF---PVL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 353 WNTVM----FNQPSWWQQGKRE-----------AAVVERYHRALGikladgdqpvrTLSGGNQQKVLLARCLEANPLLLI 417
Cdd:PRK15056 97 VEDVVmmgrYGHMGWLRRAKKRdrqivtaalarVDMVEFRHRQIG-----------ELSGGQKKRVFLARAIAQQGQVIL 165
|
170 180 190
....*....|....*....|....*....|..
gi 2095916338 418 VDEPTRGVDVSARADIYQLLKSVAAQNVAVLM 449
Cdd:PRK15056 166 LDEPFTGVDVKTEARIISLLRELRDEGKTMLV 197
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
274-471 |
2.07e-07 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 53.57 E-value: 2.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 274 DLSLEIRAGEIVGLAGLVGSGRTEFAETLYGLRPPRAGRIWLENREISQESTRarlasglvYLpeDRQVsGLFLDAPVRW 353
Cdd:TIGR00958 499 GLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHH--------YL--HRQV-ALVGQEPVLF 567
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 354 N-TVMFNQPSWWQQGKRE----AAVVERYHRALGIKLADGDQPV----RTLSGGNQQKVLLARCLEANPLLLIVDEPTRG 424
Cdd:TIGR00958 568 SgSVRENIAYGLTDTPDEeimaAAKAANAHDFIMEFPNGYDTEVgekgSQLSGGQKQRIAIARALVRKPRVLILDEATSA 647
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2095916338 425 VDVSARADIYQLLKSvaaQNVAVLMIS---SDVEEfvglADRVLVMHQGR 471
Cdd:TIGR00958 648 LDAECEQLLQESRSR---ASRTVLLIAhrlSTVER----ADQILVLKKGS 690
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
260-467 |
2.21e-07 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 51.64 E-value: 2.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 260 PVLRVEDL---TGEGFI--DLSLEIRAGEIVGLAGLVGSGRTEFAETLYGLRPPRAGRIWLENREISQEStrarlasglv 334
Cdd:PRK10247 6 PLLQLQNVgylAGDAKIlnNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLK---------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 335 ylPED--RQVSGLFLDAPVRWNTVMFNQPSWWQ------QGKREAAVVERYHRALGIKladgDQPVRTLSGGNQQKVLLA 406
Cdd:PRK10247 76 --PEIyrQQVSYCAQTPTLFGDTVYDNLIFPWQirnqqpDPAIFLDDLERFALPDTIL----TKNIAELSGGEKQRISLI 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2095916338 407 RCLEANPLLLIVDEPTRGVDVSARADIYQLL-KSVAAQNVAVLMISSDVEEfVGLADRVLVM 467
Cdd:PRK10247 150 RNLQFMPKVLLLDEITSALDESNKHNVNEIIhRYVREQNIAVLWVTHDKDE-INHADKVITL 210
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
255-471 |
2.85e-07 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 52.92 E-value: 2.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 255 QAQDFPVLRVED--LTGEgfidLSLEIRAGEIVGLAGLVGSGRTEFAETLYGLRPPRaGRIW---LENREISQESTRARL 329
Cdd:PRK11174 351 EAEDLEILSPDGktLAGP----LNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPYQ-GSLKingIELRELDPESWRKHL 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 330 AsglvYLPEDRQVsglfLDAPVRWNTVMFNQ---PSWWQQGKREAAVVERYHR-ALGIKLADGDQPVRtLSGGNQQKVLL 405
Cdd:PRK11174 426 S----WVGQNPQL----PHGTLRDNVLLGNPdasDEQLQQALENAWVSEFLPLlPQGLDTPIGDQAAG-LSVGQAQRLAL 496
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2095916338 406 ARCLEANPLLLIVDEPTRGVDVSARADIYQLLKSvAAQNVAVLMISSDVEEFVGLaDRVLVMHQGR 471
Cdd:PRK11174 497 ARALLQPCQLLLLDEPTASLDAHSEQLVMQALNA-ASRRQTTLMVTHQLEDLAQW-DQIWVMQDGQ 560
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
24-164 |
2.89e-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: 51.64 E-value: 2.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 24 DFTLCA-------GQVHALMGGNGAGKSTLMKIIAGVETPDSGELTIgerafarLNPALAHQLGiYLVPQEPMlfpnlSV 96
Cdd:cd03237 12 EFTLEVeggsiseSEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEI-------ELDTVSYKPQ-YIKADYEG-----TV 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2095916338 97 REnILFRLPKRADTTARLQ-EKLQQLNCQINLDASASTLEVADQQMVEILRGLMREARILILDEPTASL 164
Cdd:cd03237 79 RD-LLSSITKDFYTHPYFKtEIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYL 146
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
19-215 |
2.89e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 52.01 E-value: 2.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 19 VLKGIDFTLCAGQVHALMGGNGAGKSTLMK-------------IIAGVETPDSGEL-TIGERA---FArlNPAlaHQLGI 81
Cdd:PRK13633 25 ALDDVNLEVKKGEFLVILGRNGSGKSTIAKhmnallipsegkvYVDGLDTSDEENLwDIRNKAgmvFQ--NPD--NQIVA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 82 YLVPQEPMLFP-NLSVrenilfrLPKraDTTARLQEKLQQLNCQINLDASASTLEVADQQMVEILRGLMREARILILDEP 160
Cdd:PRK13633 101 TIVEEDVAFGPeNLGI-------PPE--EIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEP 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2095916338 161 TASLTPGETERLFSQIRALQALD-VGIVFISHKLPEIRQlASHVSVMRDGAVVLSG 215
Cdd:PRK13633 172 TAMLDPSGRREVVNTIKELNKKYgITIILITHYMEEAVE-ADRIIVMDSGKVVMEG 226
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
260-470 |
3.07e-07 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 51.78 E-value: 3.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 260 PVLRvedltgegfiDLSLEIRAGEIVGLAGLVGSGRTEFAETLYGLRPPRAGRIWLENReISQESTRARLASGLVylpED 339
Cdd:cd03291 51 PVLK----------NINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR-ISFSSQFSWIMPGTI---KE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 340 RQVSGLFLDApVRWNTVMfnqpswwQQGKREAAVVeryhralgiKLADGDQPVR-----TLSGGNQQKVLLARCLEANPL 414
Cdd:cd03291 117 NIIFGVSYDE-YRYKSVV-------KACQLEEDIT---------KFPEKDNTVLgeggiTLSGGQRARISLARAVYKDAD 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2095916338 415 LLIVDEPTRGVDVSARADIYQLLKSVAAQNVAVLMISSDVEEfVGLADRVLVMHQG 470
Cdd:cd03291 180 LYLLDSPFGYLDVFTEKEIFESCVCKLMANKTRILVTSKMEH-LKKADKILILHEG 234
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
395-471 |
4.54e-07 |
|
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: 49.37 E-value: 4.54e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2095916338 395 LSGGNQQKVLLARCLEANPLLLIVDEPTRGVDVSARADIYQLLKSvaaQNVAVLMISSDvEEFV-GLADRVLVMHQGR 471
Cdd:cd03221 71 LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEEALKE---YPGTVILVSHD-RYFLdQVATKIIELEDGK 144
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
275-471 |
4.84e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 52.82 E-value: 4.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 275 LSLEIRAGEIVGLAGLVGSGRTEFAETLYGLRPPRAGRIWLENREISQestrarlaSGLVYLpedRQVSGLFLDAPV--- 351
Cdd:PLN03130 1258 LSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISK--------FGLMDL---RKVLGIIPQAPVlfs 1326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 352 ---RWNTVMFNQPS---WWQQGKRE--AAVVERYHRALGIKLADGDQpvrTLSGGNQQKVLLARCLEANPLLLIVDEPTR 423
Cdd:PLN03130 1327 gtvRFNLDPFNEHNdadLWESLERAhlKDVIRRNSLGLDAEVSEAGE---NFSVGQRQLLSLARALLRRSKILVLDEATA 1403
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2095916338 424 GVDVSARADIYQLLKSvAAQNVAVLMISSDVEEFVGlADRVLVMHQGR 471
Cdd:PLN03130 1404 AVDVRTDALIQKTIRE-EFKSCTMLIIAHRLNTIID-CDRILVLDAGR 1449
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
8-215 |
5.64e-07 |
|
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: 49.95 E-value: 5.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 8 RQIRKQFSGVAVLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPD---SGELTIGERAFARLNPALAHQLgIYlV 84
Cdd:cd03233 11 FTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKEFAEKYPGEI-IY-V 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 85 PQEPMLFPNLSVRENILFRlpkradttarlqeklqqLNCQINldASASTLEVADQQMVEILRGLMREARILILDEPTASL 164
Cdd:cd03233 89 SEEDVHFPTLTVRETLDFA-----------------LRCKGN--EFVRGISGGERKRVSIAEALVSRASVLCWDNSTRGL 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2095916338 165 TPGETERLFSQIRAL-QALD-VGIVFISHKLPEIRQLASHVSVMRDGAVVLSG 215
Cdd:cd03233 150 DSSTALEILKCIRTMaDVLKtTTFVSLYQASDEIYDLFDKVLVLYEGRQIYYG 202
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
5-67 |
5.70e-07 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 51.82 E-value: 5.70e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2095916338 5 LEARQIRKQFSGVAVLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDSGELTIGERA 67
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSENA 382
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
16-164 |
8.30e-07 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 51.83 E-value: 8.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 16 GVAVLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDSGELTigerafarlnpalaHQLGIYLVPQEPMLFPNlS 95
Cdd:TIGR01271 438 VTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIK--------------HSGRISFSPQTSWIMPG-T 502
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2095916338 96 VRENILFRLP------KRADTTARLQEKLQQL--NCQINLDASASTLEVADQQMVEILRGLMREARILILDEPTASL 164
Cdd:TIGR01271 503 IKDNIIFGLSydeyryTSVIKACQLEEDIALFpeKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHL 579
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
239-471 |
8.49e-07 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 50.08 E-value: 8.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 239 SDTQKLWLALPGNRRTQAQDFPVLRvedltgegfiDLSLEIRAGEIVGLAGLVGSGRTefaeTLygLR------PPRAGR 312
Cdd:COG1134 19 EPSRSLKELLLRRRRTRREEFWALK----------DVSFEVERGESVGIIGRNGAGKS----TL--LKliagilEPTSGR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 313 IWlenreisqesTRARLAS------GL---------VYLpedrqvSGLFLDAPVRwntvmfnqpswwQQGKREAAVVEry 377
Cdd:COG1134 83 VE----------VNGRVSAllelgaGFhpeltgrenIYL------NGRLLGLSRK------------EIDEKFDEIVE-- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 378 hralgikLAD-G---DQPVRTLSGGNQQKVLLARCLEANPLLLIVDEPTRGVDVSARADIYQLLKSVAAQNVAVLMISSD 453
Cdd:COG1134 133 -------FAElGdfiDQPVKTYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRESGRTVIFVSHS 205
|
250
....*....|....*...
gi 2095916338 454 VEEFVGLADRVLVMHQGR 471
Cdd:COG1134 206 MGAVRRLCDRAIWLEKGR 223
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
393-470 |
1.13e-06 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 49.16 E-value: 1.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 393 RTLSGGNQQKVLLARCLEANPLLLIVDEPTRGVDVSARADIYQLLKSVAAQNVAVLMI----SSDV-EEFvglaDRVLVM 467
Cdd:cd03232 107 RGLSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFLKKLADSGQAILCTihqpSASIfEKF----DRLLLL 182
|
...
gi 2095916338 468 HQG 470
Cdd:cd03232 183 KRG 185
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
16-166 |
1.71e-06 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 51.06 E-value: 1.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 16 GVAVLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDsGELTIGERAFARLN-PALAHQLGIylVPQEPMLFPNl 94
Cdd:TIGR01271 1231 GRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTE-GEIQIDGVSWNSVTlQTWRKAFGV--IPQKVFIFSG- 1306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 95 SVRENI----------LFRLPKRADTTARLQEKLQQLNCQinLDASASTLEVADQQMVEILRGLMREARILILDEPTASL 164
Cdd:TIGR01271 1307 TFRKNLdpyeqwsdeeIWKVAEEVGLKSVIEQFPDKLDFV--LVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHL 1384
|
..
gi 2095916338 165 TP 166
Cdd:TIGR01271 1385 DP 1386
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
1-218 |
2.09e-06 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 48.93 E-value: 2.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 1 MKPLLEARQIRKQFSGVAVlKGIDFTLCAGQVHALMGGNGAGKS-----TLMKIIAGVeTPDSGELTIGERAFArlnPAL 75
Cdd:PRK10418 1 MPQQIELRNIALQAAQPLV-HGVSLTLQRGRVLALVGGSGSGKSltcaaALGILPAGV-RQTAGRVLLDGKPVA---PCA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 76 AHQLGIYLVPQEPMLFPN------LSVRENILFRlpKRADTTARLQEKLQQlncqINLDASASTLEVADQQM-------V 142
Cdd:PRK10418 76 LRGRKIATIMQNPRSAFNplhtmhTHARETCLAL--GKPADDATLTAALEA----VGLENAARVLKLYPFEMsggmlqrM 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 143 EILRGLMREARILILDEPTASLTpgeterLFSQIRALQAL-------DVGIVFISHKLPEIRQLASHVSVMRDGAVVLSG 215
Cdd:PRK10418 150 MIALALLCEAPFIIADEPTTDLD------VVAQARILDLLesivqkrALGMLLVTHDMGVVARLADDVAVMSHGRIVEQG 223
|
...
gi 2095916338 216 ETA 218
Cdd:PRK10418 224 DVE 226
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
16-164 |
2.21e-06 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 49.02 E-value: 2.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 16 GVAVLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDSGELTIGERAFARLNP-ALAHQLGiYLvPQEPMLFPNL 94
Cdd:PRK10575 23 GRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSkAFARKVA-YL-PQQLPAAEGM 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 95 SVRENI-LFRLP--------KRADttarlQEKLQQLNCQINLDASAS----TLEVADQQMVEILRGLMREARILILDEPT 161
Cdd:PRK10575 101 TVRELVaIGRYPwhgalgrfGAAD-----REKVEEAISLVGLKPLAHrlvdSLSGGERQRAWIAMLVAQDSRCLLLDEPT 175
|
...
gi 2095916338 162 ASL 164
Cdd:PRK10575 176 SAL 178
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
274-471 |
3.17e-06 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 49.03 E-value: 3.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 274 DLSLEIRAGEIVGLAGLVGSGRTEFAETLYGLRPPRAGRIWLENREISQ----ESTRARLASGLV----YLPEDRQVSG- 344
Cdd:PRK11153 23 NVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTAlsekELRKARRQIGMIfqhfNLLSSRTVFDn 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 345 --LFLDApvrwntvmfnqpswwqQGKREAAVVERYHRALGI-KLAD-GDQPVRTLSGGNQQKVLLARCLEANPLLLIVDE 420
Cdd:PRK11153 103 vaLPLEL----------------AGTPKAEIKARVTELLELvGLSDkADRYPAQLSGGQKQRVAIARALASNPKVLLCDE 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2095916338 421 PTRGVDVSARADIYQLLKSVAAQ-NVAVLMISSDVEEFVGLADRVLVMHQGR 471
Cdd:PRK11153 167 ATSALDPATTRSILELLKDINRElGLTIVLITHEMDVVKRICDRVAVIDAGR 218
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
23-67 |
3.23e-06 |
|
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: 49.41 E-value: 3.23e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 2095916338 23 IDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDSGELTIGERA 67
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQP 395
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
19-229 |
3.54e-06 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 49.33 E-value: 3.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 19 VLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDSGELTIGERAFARLN-PALAHQLGIylVPQEPMLFPNlSVR 97
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQlDSWRSRLAV--VSQTPFLFSD-TVA 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 98 ENILFRLPkraDTTARLQEKLQQLNC------------QINLDASASTLEVADQQMVEILRGLMREARILILDEpTASLT 165
Cdd:PRK10789 407 NNIALGRP---DATQQEIEHVARLASvhddilrlpqgyDTEVGERGVMLSGGQKQRISIARALLLNAEILILDD-ALSAV 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 166 PGETE-------RLFSQIRAlqaldvgiVFIS-HKLPEIRQlASHVSVMRDGAVV-------LSGETAGYGD----QQLI 226
Cdd:PRK10789 483 DGRTEhqilhnlRQWGEGRT--------VIISaHRLSALTE-ASEILVMQHGHIAqrgnhdqLAQQSGWYRDmyryQQLE 553
|
...
gi 2095916338 227 SAM 229
Cdd:PRK10789 554 AAL 556
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
274-487 |
3.63e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 49.97 E-value: 3.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 274 DLSLEIRAGEIVGLAGLVGSGRTEFAETLYGLRPPragriwlenreisQESTRARLASGLVYLPedrQVSGLFlDAPVRW 353
Cdd:PLN03232 635 DINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSH-------------AETSSVVIRGSVAYVP---QVSWIF-NATVRE 697
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 354 NtVMFNQpswwqqgKREAavvERYHRALGIKLADGDQ---PVRTL----------SGGNQQKVLLARCLEANPLLLIVDE 420
Cdd:PLN03232 698 N-ILFGS-------DFES---ERYWRAIDVTALQHDLdllPGRDLteigergvniSGGQKQRVSMARAVYSNSDIYIFDD 766
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2095916338 421 PTRGVDVSARADIYQLLKSVAAQNVAVLMISSDVeEFVGLADRVLVMHQG--RHSG---ELARQAVTVDRMM 487
Cdd:PLN03232 767 PLSALDAHVAHQVFDSCMKDELKGKTRVLVTNQL-HFLPLMDRIILVSEGmiKEEGtfaELSKSGSLFKKLM 837
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
274-470 |
4.76e-06 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 49.56 E-value: 4.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 274 DLSLEIRAGEIVGLAGLVGSGRTEFAETLYGLRPPRAGRIWLENREISQESTRaRLASGLVYLPEDRqvsgLFLDAPVRW 353
Cdd:TIGR00957 1304 HINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLH-DLRFKITIIPQDP----VLFSGSLRM 1378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 354 NTVMFNQPS----WWQQgkrEAAVVERYHRALGIKL----ADGDQpvrTLSGGNQQKVLLARCLEANPLLLIVDEPTRGV 425
Cdd:TIGR00957 1379 NLDPFSQYSdeevWWAL---ELAHLKTFVSALPDKLdhecAEGGE---NLSVGQRQLVCLARALLRKTKILVLDEATAAV 1452
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2095916338 426 DVSARaDIYQLLKSVAAQNVAVLMISSDVEEFVGLAdRVLVMHQG 470
Cdd:TIGR00957 1453 DLETD-NLIQSTIRTQFEDCTVLTIAHRLNTIMDYT-RVIVLDKG 1495
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
261-470 |
5.37e-06 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 48.09 E-value: 5.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 261 VLRVEDLT-----GEGFIDLSLEIRAGEIVGLAGLVGSGRTEFAETLYGL----RPPRAgRIWLENREISQESTRAR--- 328
Cdd:PRK09984 4 IIRVEKLAktfnqHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgdKSAGS-HIELLGRTVQREGRLARdir 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 329 --------------LASGLVYLpeDRQVSGLFLDAPVrWNTVMfnqpSWWQQGKREAAVveryhRALG-IKLAD-GDQPV 392
Cdd:PRK09984 83 ksrantgyifqqfnLVNRLSVL--ENVLIGALGSTPF-WRTCF----SWFTREQKQRAL-----QALTrVGMVHfAHQRV 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2095916338 393 RTLSGGNQQKVLLARCLEANPLLLIVDEPTRGVDVSARADIYQLLKSVAAQN-VAVLMISSDVEEFVGLADRVLVMHQG 470
Cdd:PRK09984 151 STLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDgITVVVTLHQVDYALRYCERIVALRQG 229
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
16-173 |
6.16e-06 |
|
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: 47.93 E-value: 6.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 16 GVAVLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDSGELTigerafarlnpalaHQLGIYLVPQEPMLFPNlS 95
Cdd:cd03291 49 GAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIK--------------HSGRISFSSQFSWIMPG-T 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 96 VRENILFRLP------KRADTTARLQEKLQQLNCQIN--LDASASTLEVADQQMVEILRGLMREARILILDEPTASLTPG 167
Cdd:cd03291 114 IKENIIFGVSydeyryKSVVKACQLEEDITKFPEKDNtvLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVF 193
|
....*.
gi 2095916338 168 ETERLF 173
Cdd:cd03291 194 TEKEIF 199
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
19-235 |
6.43e-06 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 49.01 E-value: 6.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 19 VLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDSGELtIGERAFArlnpalahqlgiyLVPQEPMLFpNLSVRE 98
Cdd:PTZ00243 675 LLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV-WAERSIA-------------YVPQQAWIM-NATVRG 739
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 99 NILFRLPKRAdttARLQE--KLQQLNCQINLDASASTLEVADQQM---------VEILRGLMREARILILDEPTASLTPG 167
Cdd:PTZ00243 740 NILFFDEEDA---ARLADavRVSQLEADLAQLGGGLETEIGEKGVnlsggqkarVSLARAVYANRDVYLLDDPLSALDAH 816
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2095916338 168 ETERLFSQIrALQALDVGI-VFISHKLpEIRQLASHVSVMRDGAVVLSGETAGYGDQQLISAMTPASRD 235
Cdd:PTZ00243 817 VGERVVEEC-FLGALAGKTrVLATHQV-HVVPRADYVVALGDGRVEFSGSSADFMRTSLYATLAAELKE 883
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
274-470 |
6.92e-06 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 48.75 E-value: 6.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 274 DLSLEIRAGEIVGLAGLVGSGRTEFAETLYGLRPPRAGRIWLENReISQESTRARLASGLVylpEDRQVSGLFLDApVRW 353
Cdd:TIGR01271 444 NISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR-ISFSPQTSWIMPGTI---KDNIIFGLSYDE-YRY 518
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 354 NTVMfnqpSWWQQGKREAAVVERYHRALGiklaDGDQpvrTLSGGNQQKVLLARCLEANPLLLIVDEPTRGVDVSARADI 433
Cdd:TIGR01271 519 TSVI----KACQLEEDIALFPEKDKTVLG----EGGI---TLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEI 587
|
170 180 190
....*....|....*....|....*....|....*..
gi 2095916338 434 YQLLKSVAAQNVAVLMISSDVEEfVGLADRVLVMHQG 470
Cdd:TIGR01271 588 FESCLCKLMSNKTRILVTSKLEH-LKKADKILLLHEG 623
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
388-471 |
7.57e-06 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 48.72 E-value: 7.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 388 GDQPVRTLSGGNQQKVLLARCLEANPLLLIVDEPTRGVDVSARADIYQLLKSVAAQNVAVLMI----SSDVEEfvgLADR 463
Cdd:PLN03211 200 GNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLTLGSLAQKGKTIVTSmhqpSSRVYQ---MFDS 276
|
....*...
gi 2095916338 464 VLVMHQGR 471
Cdd:PLN03211 277 VLVLSEGR 284
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
389-468 |
8.21e-06 |
|
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: 48.24 E-value: 8.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 389 DQPVRTLSGGNQQKVLLARCL--EANplLLIVDEPTRGVDVSARADIYQLLKSVAAQNVAVLMISSDVEEFVGLADRVLV 466
Cdd:COG1245 207 DRDISELSGGELQRVAIAAALlrDAD--FYFFDEPSSYLDIYQRLNVARLIRELAEEGKYVLVVEHDLAILDYLADYVHI 284
|
..
gi 2095916338 467 MH 468
Cdd:COG1245 285 LY 286
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
395-468 |
8.40e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 47.34 E-value: 8.40e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2095916338 395 LSGGNQQKVLLARCLEANPLLLIVDEPTRGVDVSARADIYQLLKSVAAQN-VAVLMISSDVEEFVGLADRVLVMH 468
Cdd:PRK14258 151 LSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSeLTMVIVSHNLHQVSRLSDFTAFFK 225
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
396-471 |
8.65e-06 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 47.81 E-value: 8.65e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2095916338 396 SGGNQQKVLLARCLEANPLLLIVDEPTRGVDVSARADIYQLLKSVAAQNVAVLMISSDVEEFVGLADRVLVMHQGR 471
Cdd:NF000106 146 SGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGR 221
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
275-484 |
8.86e-06 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 48.04 E-value: 8.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 275 LSLEIRAGEIVGLAGLVGSGRTEFAETLYGLRPPRAGRIWLENREISQESTRA--RLASGL---VYL------PEDRQVS 343
Cdd:PRK10522 342 INLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDyrKLFSAVftdFHLfdqllgPEGKPAN 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 344 GLFLDapvrwntvmfnqpSWWQQGKREAAVVERYHRALGIKLADGdqpvrtlsggnQQK--VLLARCLEANPLLLIvDEP 421
Cdd:PRK10522 422 PALVE-------------KWLERLKMAHKLELEDGRISNLKLSKG-----------QKKrlALLLALAEERDILLL-DEW 476
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2095916338 422 TRGVDVSARADIYQ-LLKSVAAQNVAVLMISSDVEEFVGlADRVLVMHQGRHSgEL---ARQAVTVD 484
Cdd:PRK10522 477 AADQDPHFRREFYQvLLPLLQEMGKTIFAISHDDHYFIH-ADRLLEMRNGQLS-ELtgeERDAASRD 541
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
69-303 |
1.16e-05 |
|
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: 48.09 E-value: 1.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 69 ARLNP-ALAHQLGIYLVPQepmlFPNLSVRENILF----RLPKRADTTAR--LQEKLQQLNCQIN-------LDASASTL 134
Cdd:TIGR00630 414 TRLKPeALAVTVGGKSIAD----VSELSIREAHEFfnqlTLTPEEKKIAEevLKEIRERLGFLIDvgldylsLSRAAGTL 489
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 135 EVADQQMVEI-------LRGLMreariLILDEPTASLTPGETERLFSQIRALQALDVGIVFISHKLPEIRqLASHVSVMR 207
Cdd:TIGR00630 490 SGGEAQRIRLatqigsgLTGVL-----YVLDEPSIGLHQRDNRRLINTLKRLRDLGNTLIVVEHDEDTIR-AADYVIDIG 563
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 208 DGAVVLSGETAGYGDQQLISAMTPASRDHALSDTQKlwLALPGNRRTQAQDFpvLRVEDLTGEGFIDLSLEIRAGEIVGL 287
Cdd:TIGR00630 564 PGAGEHGGEVVASGTPEEILANPDSLTGQYLSGRKK--IEVPAERRPGNGKF--LTLKGARENNLKNITVSIPLGLFTCI 639
|
250
....*....|....*..
gi 2095916338 288 AGLVGSGR-TEFAETLY 303
Cdd:TIGR00630 640 TGVSGSGKsTLINDTLY 656
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
389-471 |
1.28e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 46.83 E-value: 1.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 389 DQPVRTLSGGNQQKVLLARCLEANPLLLIVDEPTRGVDVSARADIYQLLKSVaAQNVAVLMISSDVEEFVGLADRVLVMH 468
Cdd:PRK14247 141 DAPAGKLSGGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLEL-KKDMTIVLVTHFPQQAARISDYVAFLY 219
|
...
gi 2095916338 469 QGR 471
Cdd:PRK14247 220 KGQ 222
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
275-471 |
1.64e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 47.66 E-value: 1.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 275 LSLEIRAGEIVGLAGLVGSGRTEFAETLYGLRPPRAGRIWLENREISQES-TRARLAsgLVYLPEdrqvSGLFLDAPVRW 353
Cdd:PLN03232 1255 LSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGlTDLRRV--LSIIPQ----SPVLFSGTVRF 1328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 354 NTVMF---NQPSWWQQGKRE--AAVVERYHRALGIKLADGDQpvrTLSGGNQQKVLLARCLEANPLLLIVDEPTRGVDVS 428
Cdd:PLN03232 1329 NIDPFsehNDADLWEALERAhiKDVIDRNPFGLDAEVSEGGE---NFSVGQRQLLSLARALLRRSKILVLDEATASVDVR 1405
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2095916338 429 ARADIYQLLKSvAAQNVAVLMISSDVEEFVGlADRVLVMHQGR 471
Cdd:PLN03232 1406 TDSLIQRTIRE-EFKSCTMLVIAHRLNTIID-CDKILVLSSGQ 1446
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
393-476 |
1.71e-05 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 47.49 E-value: 1.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 393 RTLSGGNQQKVLLARCLEANPLLLIVDEPTRGVDVSARADIYQLLKSvAAQNVAVLMIS--SDVEEFvglADRVLVMhQG 470
Cdd:COG4178 484 QVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLRE-ELPGTTVISVGhrSTLAAF---HDRVLEL-TG 558
|
....*.
gi 2095916338 471 RHSGEL 476
Cdd:COG4178 559 DGSWQL 564
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
254-324 |
1.71e-05 |
|
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: 47.10 E-value: 1.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 254 TQAQDFPVLRVEDLT--------GEGF----IDLSleIRAGEIVGLAGLVGSGRTEFAETLYGLRPPRAGRIWLENREIS 321
Cdd:COG4615 320 PAPADFQTLELRGVTyrypgedgDEGFtlgpIDLT--IRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVT 397
|
...
gi 2095916338 322 QES 324
Cdd:COG4615 398 ADN 400
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
19-164 |
2.02e-05 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 47.41 E-value: 2.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 19 VLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETpdSGELTIGER--AFARLNPALAHQLGiYlVPQEPMLFPNLSV 96
Cdd:TIGR00956 778 ILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVT--TGVITGGDRlvNGRPLDSSFQRSIG-Y-VQQQDLHLPTSTV 853
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 97 RENILF----RLPKRADttarLQEKLQQLNCQINL-------DA----SASTLEVADQQMVEILRGLM-REARILILDEP 160
Cdd:TIGR00956 854 RESLRFsaylRQPKSVS----KSEKMEYVEEVIKLlemesyaDAvvgvPGEGLNVEQRKRLTIGVELVaKPKLLLFLDEP 929
|
....
gi 2095916338 161 TASL 164
Cdd:TIGR00956 930 TSGL 933
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
20-164 |
2.20e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 47.28 E-value: 2.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 20 LKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAgvetpdsGELTIGERAFARLNPALAHqlgiylVPQEPMLFpNLSVREN 99
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISAML-------GELSHAETSSVVIRGSVAY------VPQVSWIF-NATVREN 698
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2095916338 100 ILF-------RLPKRADTTArLQEKLQQLNCQ--INLDASASTLEVADQQMVEILRGLMREARILILDEPTASL 164
Cdd:PLN03232 699 ILFgsdfeseRYWRAIDVTA-LQHDLDLLPGRdlTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSAL 771
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
274-471 |
2.32e-05 |
|
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: 45.61 E-value: 2.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 274 DLSLEIRAGEIVGLAGLVGSGRTEFAETLYGLRPPRAGRIWLENREISQESTRARLAS-GLVylpedRQVSGLFlDAPVR 352
Cdd:cd03249 21 GLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQiGLV-----SQEPVLF-DGTIA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 353 WNTVMfnqpswwqqGKREAAV--VERYHRALGI-----KLADG-DQPV----RTLSGGNQQKVLLARCLEANPLLLIVDE 420
Cdd:cd03249 95 ENIRY---------GKPDATDeeVEEAAKKANIhdfimSLPDGyDTLVgergSQLSGGQKQRIAIARALLRNPKILLLDE 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2095916338 421 PTRGVDVSARADIYQLLKSvAAQNVAVLMIS---SDVEEfvglADRVLVMHQGR 471
Cdd:cd03249 166 ATSALDAESEKLVQEALDR-AMKGRTTIVIAhrlSTIRN----ADLIAVLQNGQ 214
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
274-470 |
2.55e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 47.04 E-value: 2.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 274 DLSLEIRAGEIVGLAGLVGSGRTEFAETLYGLRPPRAGRIWLenreisqesTRARLAsglvYLPedrQVSGLFlDAPVRW 353
Cdd:PLN03130 635 NINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDASVV---------IRGTVA----YVP---QVSWIF-NATVRD 697
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 354 NtVMFNQPswWQQGKREAAV-VERYHRALGIkLADGDQPV-----RTLSGGNQQKVLLARCLEANPLLLIVDEPTRGVDV 427
Cdd:PLN03130 698 N-ILFGSP--FDPERYERAIdVTALQHDLDL-LPGGDLTEigergVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDA 773
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2095916338 428 S-ARADIYQLLKSVAAQNVAVLMisSDVEEFVGLADRVLVMHQG 470
Cdd:PLN03130 774 HvGRQVFDKCIKDELRGKTRVLV--TNQLHFLSQVDRIILVHEG 815
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
261-471 |
3.58e-05 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 45.16 E-value: 3.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 261 VLRVEDLT---GEGFIDLS------LEIRAGEIVGLAGLVGSGRTEFAETLYGLRPPRAGRIWLENREISQ--ESTRARL 329
Cdd:PRK10584 6 IVEVHHLKksvGQGEHELSiltgveLVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQmdEEARAKL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 330 AS---GLVY-----LPEDRQVSGLFLDAPVRWNTvmfnqpswwQQGKREAAVVERYHRALGIKLadgDQPVRTLSGGNQQ 401
Cdd:PRK10584 86 RAkhvGFVFqsfmlIPTLNALENVELPALLRGES---------SRQSRNGAKALLEQLGLGKRL---DHLPAQLSGGEQQ 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 402 KVLLARCLEANPLLLIVDEPTRGVDVSARADIYQLLKSVAAQNVAVLMISSDVEEFVGLADRVLVMHQGR 471
Cdd:PRK10584 154 RVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLAARCDRRLRLVNGQ 223
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
390-471 |
4.04e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 46.39 E-value: 4.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 390 QPVRTLSGGNQQKVLLARCLEANPLLLIVDEPTRGVDVSAradIYQLLKSVAAQNVAVLMISSDVEEFVGLADRVLVMHQ 469
Cdd:PLN03073 623 QPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDA---VEALIQGLVLFQGGVLMVSHDEHLISGSVDELWVVSE 699
|
..
gi 2095916338 470 GR 471
Cdd:PLN03073 700 GK 701
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
19-164 |
4.26e-05 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 46.38 E-value: 4.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 19 VLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDSGELTIGERAFARLNPALAHQLGiyLVPQEPMLFPNLSVRE 98
Cdd:PLN03140 895 LLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTGGYIEGDIRISGFPKKQETFARISG--YCEQNDIHSPQVTVRE 972
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2095916338 99 NILF----RLPKR---------ADTTARLQEkLQQLNCQINLDASASTLEVADQQMVEILRGLMREARILILDEPTASL 164
Cdd:PLN03140 973 SLIYsaflRLPKEvskeekmmfVDEVMELVE-LDNLKDAIVGLPGVTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGL 1050
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
393-465 |
4.44e-05 |
|
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: 44.07 E-value: 4.44e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2095916338 393 RTLSGGNQQKVLLARCLEANPLLLIVDEPTRGVDVSARADIYQLLKSVAAqnvAVLMISSDvEEFVGLADRVL 465
Cdd:cd03223 90 DVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLKELGI---TVISVGHR-PSLWKFHDRVL 158
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
383-447 |
5.18e-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: 45.70 E-value: 5.18e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2095916338 383 IKLADGDQPVRTLSGGNQQKVLLARCLEANPLLLIVDEPTRGVDVSARADIYQLLKSVAAQNVAV 447
Cdd:TIGR03719 150 LRCPPWDADVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPGTVVAV 214
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
20-216 |
5.51e-05 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 44.81 E-value: 5.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 20 LKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDSGELT-IGERAFARLNPALAHQL-GIylvpqepmlfpnlsvr 97
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDrNGEVSVIAISAGLSGQLtGI---------------- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 98 ENILFRLPKRADTtarlQEKLQQLNCQInldASASTLEVADQQMVEILRGLMR-----------EARILILDEptaSLTP 166
Cdd:PRK13546 104 ENIEFKMLCMGFK----RKEIKAMTPKI---IEFSELGEFIYQPVKKYSSGMRaklgfsinitvNPDILVIDE---ALSV 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2095916338 167 GE---TERLFSQIRALQALDVGIVFISHKLPEIRQLASHVSVMRDGAVVLSGE 216
Cdd:PRK13546 174 GDqtfAQKCLDKIYEFKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGE 226
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
279-471 |
6.44e-05 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 45.87 E-value: 6.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 279 IRAGEIVGLAGLVGSGRTEF----AETLYGLRPPRAGRIWLENreISQESTRARLASGLVYLPE-DRQVSGL----FLDA 349
Cdd:TIGR00956 84 IKPGELTVVLGRPGSGCSTLlktiASNTDGFHIGVEGVITYDG--ITPEEIKKHYRGDVVYNAEtDVHFPHLtvgeTLDF 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 350 PVRWNTVMfNQPSWWQQGKREAAVVERYHRALGIKLAD----GDQPVRTLSGGNQQKVLLARCLEANPLLLIVDEPTRGV 425
Cdd:TIGR00956 162 AARCKTPQ-NRPDGVSREEYAKHIADVYMATYGLSHTRntkvGNDFVRGVSGGERKRVSIAEASLGGAKIQCWDNATRGL 240
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2095916338 426 DVSARADIYQLLKSVA--AQNVAVLMISSDVEEFVGLADRVLVMHQGR 471
Cdd:TIGR00956 241 DSATALEFIRALKTSAniLDTTPLVAIYQCSQDAYELFDKVIVLYEGY 288
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
3-79 |
6.94e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 45.55 E-value: 6.94e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2095916338 3 PLLEARQIRKQFSGVAVLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDSGEltIGERAFARLNPALAHQL 79
Cdd:PRK10636 311 PLLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGE--IGLAKGIKLGYFAQHQL 385
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
5-217 |
9.48e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 44.31 E-value: 9.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 5 LEARQIRKQF-----SGVAVLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDSG-------------------- 59
Cdd:PRK13651 3 IKVKNIVKIFnkklpTELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGtiewifkdeknkkktkekek 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 60 ---ELTIGERAFARLNPA--LAHQLGIYLVPQEPMLFPNlSVRENILF------RLPKRADTTARLQEKLQQLNcQINLD 128
Cdd:PRK13651 83 vleKLVIQKTRFKKIKKIkeIRRRVGVVFQFAEYQLFEQ-TIEKDIIFgpvsmgVSKEEAKKRAAKYIELVGLD-ESYLQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 129 ASASTLEVADQQMVEILRGLMREARILILDEPTASLTPGETERLFSQIRALQALDVGIVFISHKLPEIRQLASHVSVMRD 208
Cdd:PRK13651 161 RSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTKRTIFFKD 240
|
....*....
gi 2095916338 209 GAVVLSGET 217
Cdd:PRK13651 241 GKIIKDGDT 249
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1-222 |
1.14e-04 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 44.33 E-value: 1.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 1 MKPLLEARQIRKQFSG----VAVLKGIDFTLCAGQVHALMGGNGAGKS----TLM------KIIAGVETPDSGE-LTIGE 65
Cdd:PRK09473 9 ADALLDVKDLRVTFSTpdgdVTAVNDLNFSLRAGETLGIVGESGSGKSqtafALMgllaanGRIGGSATFNGREiLNLPE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 66 RAfarLNPALAHQlgIYLVPQEPM--LFPNLSVRENIL--FRLPKRADTTARLQEKLQQLNcqinldasASTLEVADQQM 141
Cdd:PRK09473 89 KE---LNKLRAEQ--ISMIFQDPMtsLNPYMRVGEQLMevLMLHKGMSKAEAFEESVRMLD--------AVKMPEARKRM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 142 --------------VEILRGLMREARILILDEPTASLTPgeteRLFSQIRAL-----QALDVGIVFISHKLPEIRQLASH 202
Cdd:PRK09473 156 kmyphefsggmrqrVMIAMALLCRPKLLIADEPTTALDV----TVQAQIMTLlnelkREFNTAIIMITHDLGVVAGICDK 231
|
250 260
....*....|....*....|
gi 2095916338 203 VSVMrdgavvLSGETAGYGD 222
Cdd:PRK09473 232 VLVM------YAGRTMEYGN 245
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
20-79 |
1.17e-04 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 44.50 E-value: 1.17e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2095916338 20 LKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDSGELTI-GERAFARLNPALAHQL 79
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIkGSAALIAISSGLNGQL 100
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
395-430 |
1.20e-04 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 43.61 E-value: 1.20e-04
10 20 30
....*....|....*....|....*....|....*..
gi 2095916338 395 LSGGNQQKVLLARCLEANPLLLIVDEPTRGVD-VSAR 430
Cdd:PRK14239 149 LSGGQQQRVCIARVLATSPKIILLDEPTSALDpISAG 185
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
274-470 |
1.96e-04 |
|
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: 42.70 E-value: 1.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 274 DLSLEIRAGEIVGLAGLVGSGRTEFAETLYGLRPPRAGRIWLENREISQESTRARLASGLVYLPEDRQVSGLfLDAPVRW 353
Cdd:cd03290 19 NINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRNRYSVAYAAQKPWL-LNATVEE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 354 NtVMFNQPSwwqQGKREAAVVERYHRALGIK-LADGDQPVR-----TLSGGNQQKVLLARCLEANPLLLIVDEPTRGVDV 427
Cdd:cd03290 98 N-ITFGSPF---NKQRYKAVTDACSLQPDIDlLPFGDQTEIgergiNLSGGQRQRICVARALYQNTNIVFLDDPFSALDI 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2095916338 428 SARADIYQ--LLKSVAAQNVAVLMISSDVeEFVGLADRVLVMHQG 470
Cdd:cd03290 174 HLSDHLMQegILKFLQDDKRTLVLVTHKL-QYLPHADWIIAMKDG 217
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
19-70 |
2.24e-04 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 42.64 E-value: 2.24e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 2095916338 19 VLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAG--VETPDSGELTIGERAFAR 70
Cdd:COG2401 45 VLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGalKGTPVAGCVDVPDNQFGR 98
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
274-471 |
2.85e-04 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 42.89 E-value: 2.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 274 DLSLEIRAGEIVGLAGLVGSGRTEFAETLYGLRP----PRA----GRIWLENREISQESTRaRLASGLVYLPEDRQVSGL 345
Cdd:PRK13547 19 DLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTgggaPRGarvtGDVTLNGEPLAAIDAP-RLARLRAVLPQAAQPAFA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 346 FldaPVRWNTVMFNQPSWWQQGKREAAVVERYHRALgiKLADGD----QPVRTLSGGNQQKVLLARCL---------EAN 412
Cdd:PRK13547 98 F---SAREIVLLGRYPHARRAGALTHRDGEIAWQAL--ALAGATalvgRDVTTLSGGELARVQFARVLaqlwpphdaAQP 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 413 PLLLIVDEPTRGVDVSARADIYQLLKSVAAQ-NVAVLMISSDVEEFVGLADRVLVMHQGR 471
Cdd:PRK13547 173 PRYLLLDEPTAALDLAHQHRLLDTVRRLARDwNLGVLAIVHDPNLAARHADRIAMLADGA 232
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
20-191 |
3.18e-04 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 43.42 E-value: 3.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 20 LKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDSGELTIGERAFARLNPALAHQLgIYLVPQEPMLFPNLSVREN 99
Cdd:PRK10522 339 VGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKL-FSAVFTDFHLFDQLLGPEG 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 100 ilfrlpKRADtTARLQEKLQQLNCQINL---DASASTLEVADQQM--VEILRGLMREARILILDEPTASLTPgETERLFS 174
Cdd:PRK10522 418 ------KPAN-PALVEKWLERLKMAHKLeleDGRISNLKLSKGQKkrLALLLALAEERDILLLDEWAADQDP-HFRREFY 489
|
170
....*....|....*....
gi 2095916338 175 Q--IRALQALDVGIVFISH 191
Cdd:PRK10522 490 QvlLPLLQEMGKTIFAISH 508
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
381-465 |
3.70e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 43.28 E-value: 3.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 381 LGIKLADGDQPVRTLSGGNQQKVLLARCL--EANPLLLIVDEPTRGVDVSARADIYQLLKSVAAQNVAVLMISSDvEEFV 458
Cdd:PRK00635 463 LGLPYLTPERALATLSGGEQERTALAKHLgaELIGITYILDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEHD-EQMI 541
|
....*..
gi 2095916338 459 GLADRVL 465
Cdd:PRK00635 542 SLADRII 548
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
395-452 |
4.35e-04 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 42.14 E-value: 4.35e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 2095916338 395 LSGGNQQKVLLARCLEANPLLLIVDEPTRGVDVSARADIYQLLKSVAAQNVAVLMISS 452
Cdd:PRK14267 150 LSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHS 207
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
23-218 |
4.36e-04 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 42.42 E-value: 4.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 23 IDFTLCAGQVHALMGGNGAGKSTLMKIIAG-VETPD---SGELTIGERAFARLNPALAHQL---GIYLVPQEPM--LFPN 93
Cdd:PRK11022 26 ISYSVKQGEVVGIVGESGSGKSVSSLAIMGlIDYPGrvmAEKLEFNGQDLQRISEKERRNLvgaEVAMIFQDPMtsLNPC 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 94 LSVRENIL--FRLPKRADTTARLQEKLQQLNcQINLDASASTLEVADQQM-------VEILRGLMREARILILDEPTASL 164
Cdd:PRK11022 106 YTVGFQIMeaIKVHQGGNKKTRRQRAIDLLN-QVGIPDPASRLDVYPHQLsggmsqrVMIAMAIACRPKLLIADEPTTAL 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2095916338 165 TPGETERLFSQIRALQAL-DVGIVFISHKLPEIRQLASHVSVMRDGAVVLSGETA 218
Cdd:PRK11022 185 DVTIQAQIIELLLELQQKeNMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAH 239
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
274-471 |
5.03e-04 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 42.79 E-value: 5.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 274 DLSLEIRAGEIVGLAGLVGSGRTEFAETLYGLRPPRAGRIWLENREISQESTRA-----RLASGLVYlpedrQVSGLFLD 348
Cdd:PRK10535 26 GISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADAlaqlrREHFGFIF-----QRYHLLSH 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 349 APVRWNTVMfnqPSWWQqGKREAAVVERyHRALGIKLADGD----QPVRtLSGGNQQKVLLARCLEANPLLLIVDEPTRG 424
Cdd:PRK10535 101 LTAAQNVEV---PAVYA-GLERKQRLLR-AQELLQRLGLEDrveyQPSQ-LSGGQQQRVSIARALMNGGQVILADEPTGA 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2095916338 425 VDVSARADIYQLLKSVAAQNVAVLMISSDvEEFVGLADRVLVMHQGR 471
Cdd:PRK10535 175 LDSHSGEEVMAILHQLRDRGHTVIIVTHD-PQVAAQAERVIEIRDGE 220
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
242-455 |
5.34e-04 |
|
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: 42.98 E-value: 5.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 242 QKLWlalPGNRRTQAQDFPVLRVEDltGEGFI-DLSLEIRAGEIVGLAGLVGSGRTEFAETLYGLRPPRaGRIWLENreI 320
Cdd:TIGR01271 1209 QKCW---PSGGQMDVQGLTAKYTEA--GRAVLqDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTE-GEIQIDG--V 1280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 321 SQEST---RARLASGLVylPEDRQV-SGLF---LDAPVRWNtvmfNQPSWW---QQGKReaAVVERYHRALGIKLADGDQ 390
Cdd:TIGR01271 1281 SWNSVtlqTWRKAFGVI--PQKVFIfSGTFrknLDPYEQWS----DEEIWKvaeEVGLK--SVIEQFPDKLDFVLVDGGY 1352
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2095916338 391 pvrTLSGGNQQKVLLARCLEANPLLLIVDEPTRGVDVSARADIYQLLKSvAAQNVAVLMISSDVE 455
Cdd:TIGR01271 1353 ---VLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQ-SFSNCTVILSEHRVE 1413
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
20-216 |
8.81e-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: 40.70 E-value: 8.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 20 LKGIDFTLCAGQVHALMGGNGAGKSTLM--KIIAGvetpdsgeltiGERAFAR-LNPALAHQLGIYLVPQEPM---LFPN 93
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSSLAfdTIYAE-----------GQRRYVEsLSAYARQFLGQMDKPDVDSiegLSPA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 94 LSVRENILFRLPKRADTT------------AR--LQEKLQQLN----CQINLDASASTLEVADQQMV----EILRGLMre 151
Cdd:cd03270 80 IAIDQKTTSRNPRSTVGTvteiydylrllfARvgIRERLGFLVdvglGYLTLSRSAPTLSGGEAQRIrlatQIGSGLT-- 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2095916338 152 ARILILDEPTASLTPGETERLFSQIRALQALDVGIVFISHKlPEIRQLASHVSVMRDGAVVLSGE 216
Cdd:cd03270 158 GVLYVLDEPSIGLHPRDNDRLIETLKRLRDLGNTVLVVEHD-EDTIRAADHVIDIGPGAGVHGGE 221
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
274-481 |
1.06e-03 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 41.54 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 274 DLSLEIRAGEIVGLAGLVGSGRTEFAETLYGLRPPRAGRIWLEN---REISQESTRARLA--SGLVYLpedrqvsglfld 348
Cdd:PRK11176 361 NINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGhdlRDYTLASLRNQVAlvSQNVHL------------ 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 349 apvrWNTVMFNQPSWWQQGKREAAVVERYHR---ALG--IKLADGDQPV-----RTLSGGNQQKVLLARCLEANPLLLIV 418
Cdd:PRK11176 429 ----FNDTIANNIAYARTEQYSREQIEEAARmayAMDfiNKMDNGLDTVigengVLLSGGQRQRIAIARALLRDSPILIL 504
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2095916338 419 DEPTRGVDV-SARAdIYQLLKSVaAQNVAVLMIS---SDVEEfvglADRVLVMHQGR------HSGELARQAV 481
Cdd:PRK11176 505 DEATSALDTeSERA-IQAALDEL-QKNRTSLVIAhrlSTIEK----ADEILVVEDGEivergtHAELLAQNGV 571
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
385-422 |
1.15e-03 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 41.64 E-value: 1.15e-03
10 20 30
....*....|....*....|....*....|....*...
gi 2095916338 385 LADGDQPVRTLSGGNQQKVLLARCLEANPLLLIVDEPT 422
Cdd:PRK11819 154 CPPWDAKVTKLSGGERRRVALCRLLLEKPDMLLLDEPT 191
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
114-465 |
1.22e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 41.74 E-value: 1.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 114 LQEKLQQLNCQ----INL-------DASASTLEVADQQMVEILRGLMRE--ARILILDEPTASLTPGETERLFSQIRALQ 180
Cdd:PRK00635 446 IEEVLQGLKSRlsilIDLglpyltpERALATLSGGEQERTALAKHLGAEliGITYILDEPSIGLHPQDTHKLINVIKKLR 525
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 181 ALDVGIVFISHKLPEIrQLASHVSVMRDGAVVLSGE-----------------TAGYGDQQLISAMtPASRDHALSdtqk 243
Cdd:PRK00635 526 DQGNTVLLVEHDEQMI-SLADRIIDIGPGAGIFGGEvlfngspreflaksdslTAKYLRQELTIPI-PEKRTNSLG---- 599
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 244 lWLALpgnrrTQAqdfpvlrvedlTGEGFIDLSLEIRAGEIVGLAGLVGSGRTEF---------AETLYGLRPP------ 308
Cdd:PRK00635 600 -TLTL-----SKA-----------TKHNLKDLTISLPLGRLTVVTGVSGSGKSSLindtlvpavEEFIEQGFCSnlsiqw 662
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 309 -RAGRIWLENREISQESTRArlaSGLVYLPEDRQVSGLFLDAP-----------VRWN---------------TVMFNQ- 360
Cdd:PRK00635 663 gAISRLVHITRDLPGRSQRS---IPLTYIKAFDDLRELFAEQPrskrlgltkshFSFNtplgacaecqglgsiTTTDNRt 739
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 361 --PSWWQQGKR-EAAVVE-RYHR--------------------------------ALGIKLADGDQPVRTLSGGNQQKVL 404
Cdd:PRK00635 740 siPCPSCLGKRfLPQVLEvRYKGkniadilemtayeaekffldepsihekihalcSLGLDYLPLGRPLSSLSGGEIQRLK 819
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2095916338 405 LARCLEA---NPLLLIVDEPTRGVDVSaraDIYQL---LKSVAAQNVAVLMISSDVeEFVGLADRVL 465
Cdd:PRK00635 820 LAYELLApskKPTLYVLDEPTTGLHTH---DIKALiyvLQSLTHQGHTVVIIEHNM-HVVKVADYVL 882
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
395-468 |
1.28e-03 |
|
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: 39.86 E-value: 1.28e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2095916338 395 LSGGNQQKVLLARCLEANPLLLIVDEPTRGVDVSARADIYQLLKSVAAQNV-AVLMISSDVEEFVGLADRVLVMH 468
Cdd:cd03222 72 LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKkTALVVEHDLAVLDYLSDRIHVFE 146
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
20-272 |
1.42e-03 |
|
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: 41.47 E-value: 1.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 20 LKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDSGELTI-GERAFarlnpalahqlgiylVPQEPMLfPNLSVRE 98
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMkGSVAY---------------VPQQAWI-QNDSLRE 717
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 99 NILFRL---PKRADTTARLQEKLQQLNC-----QINLDASASTLEVADQQMVEILRGLMREARILILDEPTASLTPGETE 170
Cdd:TIGR00957 718 NILFGKalnEKYYQQVLEACALLPDLEIlpsgdRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGK 797
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 171 RLFSQIRALQALDVGI--VFISHKLPEIRQLaSHVSVMRDGAVVLSGETAGYGDQ-----QLISAMTPASRDHALSDTQK 243
Cdd:TIGR00957 798 HIFEHVIGPEGVLKNKtrILVTHGISYLPQV-DVIIVMSGGKISEMGSYQELLQRdgafaEFLRTYAPDEQQGHLEDSWT 876
|
250 260
....*....|....*....|....*....
gi 2095916338 244 LWLALPGNRRTQAQDfpVLRVEDLTGEGF 272
Cdd:TIGR00957 877 ALVSGEGKEAKLIEN--GMLVTDVVGKQL 903
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
2-164 |
1.55e-03 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 41.09 E-value: 1.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 2 KPLLEARQIRKQFSGVAVLKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDSGELTIG---ERAF-----ARLNP 73
Cdd:PRK11147 317 KIVFEMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGtklEVAYfdqhrAELDP 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 74 A------LA-------------HQLGiYLvpQEpMLFPnlsvrenilfrlPKRADTTARlqeklqqlncqinldasasTL 134
Cdd:PRK11147 397 EktvmdnLAegkqevmvngrprHVLG-YL--QD-FLFH------------PKRAMTPVK-------------------AL 441
|
170 180 190
....*....|....*....|....*....|
gi 2095916338 135 EVADQQMVEILRGLMREARILILDEPTASL 164
Cdd:PRK11147 442 SGGERNRLLLARLFLKPSNLLILDEPTNDL 471
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
390-465 |
2.49e-03 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 39.13 E-value: 2.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 390 QPVRTLSGGnqQKVL--------LARCLEANPLLLIVDEPTRGVDVSARAD-IYQLLKSVAAQNVAVLMISSDVEEFVGL 460
Cdd:cd03240 111 DMRGRCSGG--EKVLasliirlaLAETFGSNCGILALDEPTTNLDEENIEEsLAEIIEERKSQKNFQLIVITHDEELVDA 188
|
....*
gi 2095916338 461 ADRVL 465
Cdd:cd03240 189 ADHIY 193
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
125-198 |
2.68e-03 |
|
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: 38.84 E-value: 2.68e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2095916338 125 INLDASASTLEVADQQMVEILRGLMREAR--ILILDEPTASLTPGETERLFSQIRALQALDVGIVFISHKLPEIRQ 198
Cdd:cd03238 79 LTLGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGLIDLGNTVILIEHNLDVLSS 154
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
389-468 |
3.35e-03 |
|
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: 39.27 E-value: 3.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 389 DQPVRTLSGGNQQKVLLARCLEANPLLLIVDEPTRGVDVSARADIYQLLKSVAAQNVAVLMISSDVEEFVGLADRVLVMH 468
Cdd:cd03236 134 DRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRLNAARLIRELAEDDNYVLVVEHDLAVLDYLSDYIHCLY 213
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
20-164 |
4.50e-03 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 39.72 E-value: 4.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 20 LKGIDFTLCAGQVHALMGGNGAGKSTLMKIIAGVETPDS-GELTI-GERAFarlnpalahqlgiylVPQEPMLFpNLSVR 97
Cdd:PLN03130 633 LSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSdASVVIrGTVAY---------------VPQVSWIF-NATVR 696
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2095916338 98 ENILFRLP------KRADTTARLQEKLQQL--NCQINLDASASTLEVADQQMVEILRGLMREARILILDEPTASL 164
Cdd:PLN03130 697 DNILFGSPfdperyERAIDVTALQHDLDLLpgGDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSAL 771
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
389-471 |
5.49e-03 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 38.48 E-value: 5.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 389 DQPVRTLSGGNQQKVLLARCLEANP--LLLivDEPTRGVDVSARADIYQLLKSVaAQNVAVLMISSDVEEFVGLADRVLV 466
Cdd:COG1117 149 KKSALGLSGGQQQRLCIARALAVEPevLLM--DEPTSALDPISTAKIEELILEL-KKDYTIVIVTHNMQQAARVSDYTAF 225
|
....*
gi 2095916338 467 MHQGR 471
Cdd:COG1117 226 FYLGE 230
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
409-470 |
6.14e-03 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 39.32 E-value: 6.14e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2095916338 409 LEANP-LLLIVDEPTRGVDVSARADIYQLLKSVAAQNVAVLMI----SSDV-EEFvglaDRVLVMHQG 470
Cdd:TIGR00956 916 LVAKPkLLLFLDEPTSGLDSQTAWSICKLMRKLADHGQAILCTihqpSAILfEEF----DRLLLLQKG 979
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
390-471 |
6.36e-03 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 38.86 E-value: 6.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 390 QPvRTLSGGNQQKVLLARCLEANPLLLIVDEPTRGVD----VSARADIYQLLKSVaaqNVAVLMISSDVEEFVGLADRVL 465
Cdd:PRK11000 130 KP-KALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDaalrVQMRIEISRLHKRL---GRTMIYVTHDQVEAMTLADKIV 205
|
....*.
gi 2095916338 466 VMHQGR 471
Cdd:PRK11000 206 VLDAGR 211
|
|
| ATPase_flagellum-secretory_path_III |
cd01136 |
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ... |
3-51 |
8.93e-03 |
|
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; Flagellum-specific ATPase/type III secretory pathway virulence-related protein. This group of ATPases are responsible for the export of flagellum and virulence-related proteins. The bacterial flagellar motor is similar to the F0F1-ATPase, in that they both are proton-driven rotary molecular devices. However, the main function of the bacterial flagellar motor is to rotate the flagellar filament for cell motility. Intracellular pathogens such as Salmonella and Chlamydia also have proteins which are similar to the flagellar-specific ATPase, but function in the secretion of virulence-related proteins via the type III secretory pathway.
Pssm-ID: 410880 [Multi-domain] Cd Length: 265 Bit Score: 37.92 E-value: 8.93e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 2095916338 3 PLLEARQIRKQFS-GVAVLKGIdFTLCAGQVHALMGGNGAGKSTLMKIIA 51
Cdd:cd01136 40 NPLKRAPIEQPLPtGVRAIDGL-LTCGEGQRIGIFAGSGVGKSTLLGMIA 88
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
393-471 |
9.96e-03 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 38.29 E-value: 9.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095916338 393 RTLSGGNQQKVLLARCLEANPLLLIVDEPTRGVD----VSARADIYQLLKSVAAQNVAVlmiSSDVEEFVGLADRVLVMH 468
Cdd:PRK11650 133 RELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDaklrVQMRLEIQRLHRRLKTTSLYV---THDQVEAMTLADRVVVMN 209
|
...
gi 2095916338 469 QGR 471
Cdd:PRK11650 210 GGV 212
|
|
| |
